TargetID	Target_Name	Uniprot_ID	Uniprot_ID_HUMAN	BioChemical_Class	Synonyms	Gene_Name	Function	EC_Number	PDB_Structure	Sequence	Target_type	Reference	Highest_status new	BC Class ID	Family	Sequence similarities	EC	EC Name	PFAM name	PFAM id	PFAM	TCDB	TCDB Name	KEGG_pathway	Reactome	BioCyc	Structure_3d
TTD16BI	HUMAN pH-dependent viral fusion/replication (pH-DVF/R)	Pathway/Process	.	.	.	pH-DVF/R	.	.	.	.	.	Remdesivir and chloroquine effectively inhibit the recently emerged novel coronavirus (2019-nCoV) in vitro. Cell Res. 2020 Mar;30(3):269-271.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZGK1R	HUMAN glycosylation of host receptor (GHR)	Pathway/Process	.	.	.	GHR	.	.	.	.	.	Remdesivir and chloroquine effectively inhibit the recently emerged novel coronavirus (2019-nCoV) in vitro. Cell Res. 2020 Mar;30(3):269-271.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXQ1JS	HUAMN eIF4E-eIF4G interaction (eIF4E-eIF4G)	Pathway/Process	.	.	.	eIF4E-eIF4G	.	.	.	.	.	Blocking eIF4E-eIF4G interaction as a strategy to impair coronavirus replication. J Virol. 2011 Jul;85(13):6381-9.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTAIY2U	HUMAN clathrin-mediated endocytosis (RME)	Pathway/Process	.	.	.	RME	.	.	.	.	.	Targeting the Endocytic Pathway and Autophagy Process as a Novel Therapeutic Strategy in COVID-19. Int J Biol Sci. 2020 Mar 15;16(10):1724-1731.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTDJB68	HUMAN MYD88NF-kappa-B proinflammatory pathway (MYD88-NFKB pathway)	Pathway/Process	.	.	.	MYD88-NFKB pathway	.	.	.	.	.	Statin therapy in COVID-19 infection. Eur Heart J Cardiovasc Pharmacother. 2020 Apr 29. pii: pvaa042.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3A1EZ	HUMAN toll-like receptor 7/9 signalling pathway (TLR7/9 pathway)	Pathway/Process	.	.	.	TLR7/9 pathway	.	.	.	.	.	Mechanisms of action of hydroxychloroquine and chloroquine: implications for rheumatology. Nat Rev Rheumatol. 2020 Mar;16(3):155-166.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTDT8RP	HUMAN casein kinase II (CSK2)	P68400; P19784; Q8NEV1; P67870	CSK21_HUMAN; CSK22_HUMAN; CSK23_HUMAN; CSK2B_HUMAN	Kinase	Protein kinase CK2; Casein kinase II; CK2; CK II	CSK2	"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."	EC 2.7.11.1	6Q4Q; 6Q38; 6HME; 6HBN; 6GMD	MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMGSSSMPGGSTPVSSANMMSGISSVPTPSPLGPLAGSPVIAAANPLGMPVPAAAGAQQ	.	"News report, company report or official report of Senhwa Biosciences, Inc. Senhwa Biosciences Silmitasertib Named as Potential COVID-19 Therapy. 2020 March 31."	.	.	.	.	.	.	.	.	.	.	.	hsa03008: Ribosome biogenesis in eukaryotes; hsa04064: NF-kappa B signaling pathway; hsa04137: Mitophagy - animal; hsa04310: Wnt signaling pathway; hsa04520: Adherens junction; hsa05010: Alzheimer disease; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05162: Measles; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer	R-HSA-1483191: Synthesis of PC; R-HSA-201688: WNT mediated activation of DVL; R-HSA-2514853: Condensation of Prometaphase Chromosomes; R-HSA-445144: Signal transduction by L1; R-HSA-6804756: Regulation of TP53 Activity through Phosphorylation; R-HSA-6814122: Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding; R-HSA-8934903: Receptor Mediated Mitophagy; R-HSA-8939243: RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known; R-HSA-8948751: Regulation of PTEN stability and activity; R-HSA-9755511: KEAP1-NFE2L2 pathway	.	P68400
TTO361H	HUMAN calpain-2/calpain small subunit 1 heterodimer (CAPN2/CAPNS1)	P17655/P04632	CAN2_HUMAN/CPNS1_HUMAN	Peptidase C2 family	Calpain-2 large subunit/calpain small subunit 1 dimer	CAPN2/CAPNS1	"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."	.	.	MAGIAAKLAKDREAAEGLGSHDRAIKYLNQDYEALRNECLEAGTLFQDPSFPAIPSALGFKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPLNQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELKKPPPNLFKIIQKALQKGSLLGCSIDITSAADSEAITFQKLVKGHAYSVTGAEEVESNGSLQKLIRIRNPWGEVEWTGRWNDNCPSWNTIDPEERERLTRRHEDGEFWMSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDEEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELSGQTNIHLSKNFFLTNRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDFCIRVFSEKKADYQAVDDEIEANLEEFDISEDDIDDGFRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDSDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKMPCQLHQVIVARFADDQLIIDFDNFVRCLVRLETLFKIFKQLDPENTGTIELDLISWLCFSVL	.	ClinicalTrials.gov (NCT04334460) Safety and Antiviral Activity of BLD-2660 in COVID-19 Hospitalized Subjects. U.S. National Institutes of Health.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P17655
TT140V6	HUMAN vascular endothelial growth factor (VEGF)	P15692; P49765; P49767; O43915	VEGFA_HUMAN; VEGFB_HUMAN; VEGFC_HUMAN; VEGFD_HUMAN	Growth factor	Vascular endothelial cell growth factor	VEGF	"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."	.	.	MNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPHPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR	.	ClinicalTrials.gov (NCT04275414) Bevacizumab in Severe or Critical Patients With COVID-19 Pneumonia (BEST-CP)	.	.	.	.	.	.	.	.	.	.	.	hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa04010: MAPK signaling pathway; hsa04014: Ras signaling pathway; hsa04015: Rap1 signaling pathway; hsa04020: Calcium signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04370: VEGF signaling pathway; hsa04510: Focal adhesion; hsa04926: Relaxin signaling pathway; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa05163: Human cytomegalovirus infection; hsa05165: Human papillomavirus infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05206: MicroRNAs in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05211: Renal cell carcinoma; hsa05212: Pancreatic cancer; hsa05219: Bladder cancer; hsa05323: Rheumatoid arthritis; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-114608: Platelet degranulation; R-HSA-1234158: Regulation of gene expression by Hypoxia-inducible Factor; R-HSA-194138: Signaling by VEGF; R-HSA-194313: VEGF ligand-receptor interactions; R-HSA-195399: VEGF binds to VEGFR leading to receptor dimerization; R-HSA-4420097: VEGFA-VEGFR2 Pathway; R-HSA-5218921: VEGFR2 mediated cell proliferation; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-8866910: TFAP2 (AP-2) family regulates transcription of growth factors and their receptors; R-HSA-9679191: Potential therapeutics for SARS	.	P15692
TT45V0U	HUMAN calpain-1/calpain small subunit 1 heterodimer (CAPN1/CAPNS1)	P07384/P04632	CAN1_HUMAN/CPNS1_HUMAN	Peptidase C2 family	Calpain-1 large subunit/calpain small subunit 1 dimer	CAPN1/CAPNS1	Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.	.	.	MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLGQDYEQLRVRCLQSGTLFRDEAFPPVPQSLGYKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQVVSLIRMRNPWGEVEWTGAWSDSSSEWNNVDPYERDQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKSRTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPAVHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTVELDDQIQANLPDEQVLSEEEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA	.	ClinicalTrials.gov (NCT04334460) Safety and Antiviral Activity of BLD-2660 in COVID-19 Hospitalized Subjects. U.S. National Institutes of Health.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P07384
TTGL3J0	COVID-19 ribonucleic acid (RNA)	Other molecule	.	.	.	RNA	.	.	.	.	.	Biomarkers heavily used as diagnostic tools in COVID-19 trials. News Report.14 Apr 2020	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTV50LE	HUMAN serum direct bilirubin (DBIL)	Other molecule	.	.	.	DBIL	.	.	.	.	.	Hematological Findings and Complications of COVID-19. Am J Hematol. 2020 Apr 13. doi: 10.1002/ajh.25829.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJQV83	HUMAN creatinine (CREA)	Other molecule	.	.	.	CREA	.	.	.	.	.	Hematological Findings and Complications of COVID-19. Am J Hematol. 2020 Apr 13. doi: 10.1002/ajh.25829.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTEKDU8	HUMAN serum urea (SeU)	Other molecule	.	.	.	SeU	.	.	.	.	.	Hematological Findings and Complications of COVID-19. Am J Hematol. 2020 Apr 13. doi: 10.1002/ajh.25829.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTM6Z3L	HUMAN cystatin C (CysC)	Other molecule	.	.	.	CysC	.	.	.	.	.	Hematological Findings and Complications of COVID-19. Am J Hematol. 2020 Apr 13. doi: 10.1002/ajh.25829.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTP85OW	Glioblastoma A-172 cells	.	.	Cell Line	Human glioblastoma A-172 cells; A172; A 172; A-172 MG; A-172MG	A-172 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5E7Y4	Ovarian cancer A2780 cells	.	.	Cell Line	Human ovarian carcinoma A2780 cells; A-2780; A2780S	A2780 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMFLY2	Lung cancer A-427 cells	.	.	Cell Line	Human lung adenocarcinoma A-427 cells; A427; A427N	A-427 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTPJ4SN	Lung cancer A-549 cells	.	.	Cell Line	Human lung adenocarcinoma A-549 cells; A 549; A549; NCI-A549; A549/ATCC; A549 ATCC; A549ATCC; hA549	A-549 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT6JDG8	Fibroblast BJ cells	.	.	Cell Line	Human fibroblast BJ cells; FF-WT-BJ; BJ1	BJ cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTCYA0I	Microglial BV-2 cells	.	.	Cell Line	Mouse microglial BV-2 cells; BV2	BV-2 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTFRYVC	Colon cancer Caco-2 cells	.	.	Cell Line	Human colon adenocarcinoma Caco-2 cells; CaCo-2; CACO-2; Caco 2; CACO 2; CACO2; CaCo2; CaCO2; Caco2; Caco-2/ATCC; Caco-II	Caco-2 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT1CVAY	Leukemia CCRF-CEM cells	.	.	Cell Line	Human lymphoblastic leukemia CCRF-CEM cells; CCRF/CEM; CCRFCEM; CCRF.CEM; CCRF CEM; CCRF; CEM; CEM-CCRF; CEM-CCRF (CAMR); CCRF/CEM/0; CEM/0; CEM-0; CCRF-CEM/S; GM03671; GM03671C	CCRF-CEM cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTY26AJ	Ductal cancer CFPAC-1 cells	.	.	Cell Line	Human ductal adenocarcinoma CFPAC-1 cells; CFPac-1; CF PAC-1; CF-PAC1; CF-Pac1; CF Pac1; CFPAC1; CFPac1; CFPAC	CFPAC-1 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJI4K5	Colon cancer COLO 205 cells	.	.	Cell Line	Human colon adenocarcinoma COLO 205 cells; Colo 205; CoLo 205; COLO-205; Colo-205; COLO.205; Colo205; COLO205; Co 205; Colorado 205	COLO 205 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTGJ8YB	Breast cancer DOD-1 cells	.	.	Cell Line	Human breast carcinoma DOD-1 cells; Du4475; DU4475; DU-4475; Du-4475; DU 4475; Du 4475; Duke University 4475	DOD-1 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTWPU2O	Bladder cancer EJ-1 cells	.	.	Cell Line	Human bladder carcinoma EJ-1 cells; EJ1	EJ-1 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHW1MN	Breast cancer FM3A cells	.	.	Cell Line	Mouse breast cancer FM3A cells; FM3A clone 28; FM3A cl28	FM3A cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2RS1V	Lung cancer H322 cells	.	.	Cell Line	Human lung adenocarcinoma H322 cells; H-322; H322T; NCI-H322; NCI-H322T; NCI-322; NCIH322	H322 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTKOTX1	Colon cancer HCT-116 cells	.	.	Cell Line	Human colon carcinoma HCT-116 cells; HCT-116; HCT.116; HCT_116; HCT116; CoCL2	HCT-116 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3TBWL	Colon cancer HCT-15 cells	.	.	Cell Line	Human colon adenocarcinoma HCT-15 cells; HCT-15; HCT.15; HCT15	HCT-15 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTBJP8M	Kidney HEK293 cells	.	.	Cell Line	Human embryonic kidney HEK293 cells; Hek293; HEK-293; HEK/293; HEK 293; HEK;293; 293; 293 HEK; 293 Ad5; Human Embryonic Kidney 293	HEK293 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTEIHSY	Cervical cancer HeLa cells	.	.	Cell Line	Human endocervical cancer HeLa cells; HELA; Hela; He La; He-La; Henrietta Lacks cells; Helacyton gartleri	HeLa cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHE03Y	Hepatoblastoma HepG2 cells	.	.	Cell Line	Human hepatoblastoma HepG2 cells; HEP-G2; Hep G2; HEP G2; HepG2; HEPG2	HepG2 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTW8HEX	Foreskin HFF fibroblasts	.	.	Cell Line	Human foreskin HFF fibroblasts	HFF fibroblasts	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOQI30	Leukemia HL-60 cells	.	.	Cell Line	Human acute myeloid leukemia HL-60 cells; HL 60; HL.60 HL60	HL-60 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3K9CA	Colon cancer HT-29 cells	.	.	Cell Line	Human colon adenocarcinoma HT-29 cells; HT 29; HT29	HT-29 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTRKYBO	Fungoides HuT78 cells	.	.	Cell Line	Human mycosis fungoides HuT78 cells; Hut 78; HUT 78; HuT-78; HUT-78; HuT 78; Hut78; HUT78; NCI-H78	HuT78 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5XPTY	Duodenal cancer HuTu80 cells	.	.	Cell Line	Human duodenal adenocarcinoma HuTu80 cells; HUTU 80; Hutu 80; HuTu-80; HUTU-80; Hutu-80; HUTU80; HuTu 80; Hutu80	HuTu80 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTE59V4	Umbilical vein endothelial cells	.	.	Cell Line	Human umbilical vein endothelial cells; HUVEC; HUV-EC-C; HUVEC; HUVEC-C	vein endothelial cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3DGQ4	Leukemia K562 cells	.	.	Cell Line	Human chronic myeloid leukemia K562 cells; K-562; K.562; K 562; KO; GM05372; GM05372E	K562 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTF4IO1	Cervical cancer KB cells	.	.	Cell Line	Human endocervical adenocarcinoma KB cells; Strain KB	KB cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT9MR3L	Cervical cancer KB-3-1 cells	.	.	Cell Line	Human endocervical adenocarcinoma KB-3-1 cells; KB 3-1; KB3-1; KB31	KB-3-1 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTKEURC	Leukemia L1210 cells	.	.	Cell Line	Mouse leukemia L1210 cells; L 1210; L-1210; Leukemic 1210; Leukemia 1210; Leukemia L1210	L1210 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQWR94	Myoblast L6 cells	.	.	Cell Line	Rat myoblast L6 cells; L-6; L-6 myoblast	L6 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTH65VJ	Leukemia AML cells	.	.	Cell Line	Primary acute myeloid leukemia cells; Primary AML cells; AML-193; AML193	AML cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT7V1B4	Lung cancer LLC1 cells	.	.	Cell Line	Mouse lung adenocarcinoma LLC1 cells; LL/2 (LLc1); LL/2(LLc1); LL/2; LL2; LLC1; LLC; Lewis lung carcinoma line 1; Lewis lung carcinoma; Lewis Lung Cancer; Lewis-Lung; Lewis Lung	LLC1 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTCLT56	Prostate cancer LNCaP cells	.	.	Cell Line	Human prostate carcinoma LNCaP cells; LNCAP; LNCap; Ln-Cap; Lymph Node Carcinoma of the prostate	LNCaP cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTX1SVA	Breast cancer MCF7 cells	.	.	Cell Line	Human breast carcinoma MCF7 cells; MCF 7; MCF.7; MCF-7; Michigan Cancer Foundation-7; ssMCF-7; ssMCF7; MCF7/WT; MCF7-CTRL; IBMF-7	MCF7 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8UCAX	Carcinoma MDA-MB-231 cells	.	.	Cell Line	Human breast adenocarcinoma MDA-MB-231 cells; MDA_MB_231; MDA-MB 231; MDA.MB.231; MDA MB 231; MDA MB231; MDA Mb231; MDA-MB231; MDAMB-231; MDAMB231; MDA-231; MDA231; MDA231-BRE; MB231; MD Anderson-Metastatic Breast-231	MDA-MB-231 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTAGU2J	Melanoma MDA-MB-435 cells	.	.	Cell Line	Human amelanotic melanoma MDA-MB-435 cells; MDA-MB435; MDAMB435; MDA.MB.435; MDA-435; MDA 435; MDA435; MD Anderson-Metastatic Breast-435	MDA-MB-435 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTPN23T	Immortalized MDCK cells	.	.	Cell Line	Dog kidney immortalized MDCK cells; MDCK (NBL-2); NBL-2; Madin-Darby Canine Kidney; Madin Darby Canine Kidney	MDCK cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXQYOZ	Ductal cancer PaCa-2 cells	.	.	Cell Line	Human ductal adenocarcinoma MIA PaCa-2 cells; MIA-PaCa-2; MIA-PACA-2; MIA-Pa-Ca-2; MIA Paca2; MIA PaCa2; MiaPaCa-2; MIAPACA-2; MiaPaca.2; MiaPaCa2; Miapaca2; MIAPaCa2; MIAPACA2; Mia PACA 2; MIAPaCa-2; PaCa2	PaCa-2 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTY0N32	Leukemia MOLT-4 cells	.	.	Cell Line	Human acute lymphoblastic leukemia MOLT-4 cells; Molt-4; MOLT 4; Molt 4; MOLT.4; MOLT4; Molt4; GM02219; GM02219C; GM2219C; GM02219D	MOLT-4 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMCDFL	Fetal lung MRC5 cells	.	.	Cell Line	Human fetal lung MRC5 cells; MRC-5; MRC 5; MRCV; MRC-V; Medical Research Council cell strain-5	lung MRC5 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTI7TXU	Leukemia MT4 cells	.	.	Cell Line	Human acute lymphoblastic leukemia MT4 cells; MT-4	MT4 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2N4ZR	Ovarian cancer ADR-RES cells	.	.	Cell Line	Human ovarian adenocarcinoma NCI/ADR-RES cells; NCI-ADR-RES; NCI.ADR.RES; NCIADR.RES; NCI/ADRRES; NCIADRRES; ADR-RES; MCF-7/ADR; MCF-7/ADR-RES; MCF-7/AdrR; MCF-7/Adr; MCF-7/adr; MCF-7ADR; MCF7-ADR; MCF7ADR; OVCAR-8/ADR; OVCAR8/ADR	ADR-RES cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT0YBT8	Lung cancer NCI-H358 cells	.	.	Cell Line	Human lung adenocarcinoma NCI-H358 cells; H358; H-358; NCIH358	NCI-H358 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTV7NMF	Lung cancer NCI-H460 cells	.	.	Cell Line	Human lung carcinoma NCI-H460 cells; NCI.H460; H460; H-460; NCIH460; NCI-HUT-460; NCI-460	NCI-H460 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTP8T7A	Immortalized NIH3T3 cells	.	.	Cell Line	Mouse embryo immortalized NIH3T3 cells; NIH/3T3; NIH-3T3; NIH 3T3; 3T3; 3T3NIH; 3T3-Swiss; Swiss-3T3; Swiss/3T3; Swiss 3T3; Swiss3T3	NIH3T3 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTLSI8H	Ovarian cancer OVCAR-3 cells	.	.	Cell Line	Human ovarian adenocarcinoma OVCAR-3 cells; Ovcar-3; OVCAR 3; OVCAR.3; NIH:OVCAR-3; NIH:Ovcar-3; NIH:OVCAR3; NIH-OVCAR-3; NIHOVCAR3; OVCAR3; Ovcar3	OVCAR-3 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT9UCBP	Lymphoma P388/ADR cells	.	.	Cell Line	Mouse lymphoma P388/ADR cells	P388/ADR cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT0BKWT	Prostate cancer PC-3 cells	.	.	Cell Line	Human prostate carcinoma PC-3 cells; PC3; PC.3	PC-3 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQKMWE	Leukemia RAW264.7 cells	.	.	Cell Line	Mouse leukemia RAW264.7 cells; RAW264; RAW2647; RAW264.7; RAW-264.7; Raw 264.7; Raw264.7	RAW264.7 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNIWBA	Melanoma RPMI-7951 cells	.	.	Cell Line	Human melanoma RPMI-7951 cells; RPMI 7951; RPMI7951; Roswell Park Memorial Institute 7951	RPMI-7951 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTVADBW	Lymphoma S49 cells	.	.	Cell Line	Mouse lymphoma S49 cells; S49 Kin; Kin-S49; Kin; kin	S49 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTH4NGE	Cervical cancer SGC-7901 cells	.	.	Cell Line	Human endocervical adenocarcinoma SGC-7901 cells; SGC 7901; SGC7901	SGC-7901 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHXW3C	Neuroblastoma SH-SY5Y cells	.	.	Cell Line	Human neuroblastoma SH-SY5Y cells; SH-Sy5y; SHSY5Y; SHSY-5Y; SK-SH-SY5Y; SY5Y; SH-SY5Y Parental	SH-SY5Y cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2CFJE	Melanoma SK-MEL-5 cells	.	.	Cell Line	Human cutaneous melanoma SK-MEL-5 cells; SK-Mel-5; SK MEL 5; SK.MEL.5; SK-MEL5; SKMel-5; SKMEL-5; SKMEL5; SKMel5; SKmel5; AA-Mel	SK-MEL-5 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTP2LDO	Ovarian cancer SK-OV-3 cells	.	.	Cell Line	Human ovarian adenocarcinoma SK-OV-3 cells; SKOV-3; SK-OV3; SK.OV.3; SKOV3; Skov3; SKO3	SK-OV-3 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT87MKN	Colon cancer SW480 cells	.	.	Cell Line	Human colon adenocarcinoma SW480 cells; SW-480; SW 480; SW480E	SW480 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTF52YP	Colon cancer SW620 cells	.	.	Cell Line	Human colon adenocarcinoma SW620 cells; SW-620; SW 620; SW.620	SW620 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNP30R	Astrocytoma U251 cells	.	.	Cell Line	Human astrocytoma U251 cells; U-251MG; U-251 MG; U-251-MG; U-251_MG; U251-MG; U251MG; U-251; U251n; U251N; 251 MG; 251MG	U251 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJ0BUR	Leukemia U937 cells	.	.	Cell Line	Human acute monocytic leukemia U937 cells; U-937; U 937	U937 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTVTFOP	Fibrosarcoma WEHI-164 cells	.	.	Cell Line	Mouse fibrosarcoma WEHI-164 cells; WEHI 164; WEHI164; WEHI 164 TC	WEHI-164 cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTBIHJG	Colon cancer WiDr cells	.	.	Cell Line	Human colon adenocarcinoma WiDr cells; WiDR; WIDR; WiDr/S; WiDr-TC; WiDrTC; LED-WiDr; Led-WiDr	WiDr cells	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT6SR2J	ABHD5-Perilipin complex	.	ABHD5_HUMAN-PLIN1_HUMAN	Protein Complex	Abhydrolase domain-containing protein 5 complexed with Lipid droplet-associated protein; Abhydrolase domain-containing protein 5 complexed with Perilipin-1; 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 complexed with Lipid droplet-associated protein; 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 complexed with Perilipin-1; Lipid droplet-binding protein CGI-58 complexed with Perilipin-1; Lipid droplet-binding protein CGI-58 complexed with Lipid droplet-associated protein	ABHD5-Perilipin complex	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q8WTS1
TTZUNRB	Proconvertin-TF complex	.	FA7_HUMAN-TF_HUMAN	Protein Complex	Coagulation factor VII complexed with CD142; Eptacog alfa complexed with Coagulation factor III; Proconvertin complexed with TF; SPCA complexed with Thromboplastin; Serum prothrombin conversion accelerator complexed with Tissue factor	Proconvertin-TF complex	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P08709
TTKO9JN	CDK1-CCNB1 complex	.	CDK1_HUMAN-CCNB1_HUMAN	Protein Complex	CDK1 complexed with G2/mitotic-specific cyclin-B1; Cell division control protein 2 homolog complexed with G2/mitotic-specific cyclin-B1; Cell division protein kinase 1 complexed with G2/mitotic-specific cyclin-B1; Cyclin-dependent kinase 1 complexed with G2/mitotic-specific cyclin-B1; p34 protein kinase complexed with G2/mitotic-specific cyclin-B1	CDK1-CCNB1 complex	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P06493
TTSXQ9A	CDK2-CCNA2 complex	.	CDK2_HUMAN-CCNA2_HUMAN	Protein Complex	Cell division protein kinase 2 complexed with Cyclin-A2; Cyclin-dependent kinase 2 complexed with Cyclin-A2; p33 protein kinase complexed with Cyclin-A2	CDK2-CCNA2 complex	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P24941
TT5BJ3D	GluA1-GluA2 complex	.	GRIA1_HUMAN-GRIA2_HUMAN	Protein Complex	"AMPA-selective glutamate receptor 1 complexed with AMPA-selective glutamate receptor 2; GluA1 complexed with GluA2; GluR-1 complexed with GluR-2; GluR-A complexed with GluR-B; GluR-K1 complexed with GluR-K2; Glutamate receptor 1 complexed with Glutamate receptor 2; Glutamate receptor ionotropic, AMPA 1 complexed with Glutamate receptor ionotropic, AMPA 2"	GluA1-GluA2 complex	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P42261
TTAQR9C	GluA2-GluA3 complex	.	GRIA2_HUMAN-GRIA3_HUMAN	Protein Complex	"AMPA-selective glutamate receptor 2 complexed with AMPA-selective glutamate receptor 3; GluA2 complexed with GluA3; GluR-2 complexed with GluR-3; GluR-A complexed with GluR-B; GluR-K2 complexed with GluR-K3; Glutamate receptor 2 complexed with Glutamate receptor 3; Glutamate receptor ionotropic, AMPA 2 complexed with Glutamate receptor ionotropic, AMPA 3"	GluA2-GluA3 complex	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P42262
TT9WR4E	NMDAR2B-NMDAR1 complex	.	NMDE2_HUMAN-NMDZ1_HUMAN	Protein Complex	"GluN2B complexed with GluN1; Glutamate [NMDA] receptor subunit epsilon-1 complexed with Glutamate [NMDA] receptor subunit zeta-1; Glutamate receptor ionotropic, NMDA 2B complexed with Glutamate receptor ionotropic, NMDA 1; N-methyl D-aspartate receptor subtype 2B complexed with N-methyl-D-aspartate receptor subunit NR1; NMDAR2B complexed with NMD-R1; NR2B complexed with GluN1; hNR2B complexed with GluN1"	NMDAR2B-NMDAR1 complex	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q13224
TT9VOT3	Hsp60-Hsp10 complex	.	CH60_HUMAN-CH10_HUMAN	Protein Complex	"Heat shock protein 60 complexed with Early-pregnancy factor; Hsp60 complexed with Hsp10; HuCHA60 complexed with Hsp10; 60 kDa chaperonin complexed with 10 kDa chaperonin; 60 kDa heat shock protein, mitochondrial complexed with 10 kDa heat shock protein, mitochondrial; CPN60 complexed with CPN10; Chaperonin 60 complexed with Chaperonin 10; HSP-60 complexed with EPF; Mitochondrial matrix protein P1 complexed with Hsp10; P60 lymphocyte protein complexed with Hsp10"	Hsp60-Hsp10 complex	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P10809
TTWDQKY	NMDAR2A-NMDAR1 complex	.	NMDE1_HUMAN-NMDZ1_HUMAN	Protein Complex	"GluN2A complexed with GluN1; Glutamate [NMDA] receptor subunit epsilon-1 complexed with Glutamate [NMDA] receptor subunit zeta-1; Glutamate receptor ionotropic, NMDA 2A complexed with Glutamate receptor ionotropic, NMDA 1; N-methyl D-aspartate receptor subtype 2A complexed with N-methyl-D-aspartate receptor subunit NR1; NMDAR2A complexed with NMD-R1; NR2A complexed with GluN1; hNR2A complexed with GluN1"	NMDAR2A-NMDAR1 complex	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q12879
TTCE6QO	NMDAR2C-NMDAR1 complex	.	NMDE3_HUMAN-NMDZ1_HUMAN	Protein Complex	"GluN2C complexed with GluN1; Glutamate [NMDA] receptor subunit epsilon-1 complexed with Glutamate [NMDA] receptor subunit zeta-1; Glutamate receptor ionotropic, NMDA 2C complexed with Glutamate receptor ionotropic, NMDA 1; N-methyl D-aspartate receptor subtype 2C complexed with N-methyl-D-aspartate receptor subunit NR1; NMDAR2C complexed with NMD-R1; NR2C complexed with GluN1; hNR2C complexed with GluN1"	NMDAR2C-NMDAR1 complex	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q14957
TTM897O	NMDAR2D-NMDAR1 complex	.	NMDE4_HUMAN-NMDZ1_HUMAN	Protein Complex	"GluN2D complexed with GluN1; Glutamate [NMDA] receptor subunit epsilon-1 complexed with Glutamate [NMDA] receptor subunit zeta-1; Glutamate receptor ionotropic, NMDA 2D complexed with Glutamate receptor ionotropic, NMDA 1; N-methyl D-aspartate receptor subtype 2D complexed with N-methyl-D-aspartate receptor subunit NR1; NMDAR2D complexed with NMD-R1; NR2D complexed with GluN1; hNR2D complexed with GluN1"	NMDAR2D-NMDAR1 complex	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	O15399
TTBMU54	Adenosine receptor A2	.	AA2AR_HUMAN; AA2BR_HUMAN	Protein Family	.	Adenosine receptor A2	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P29274
TT5XDGA	Carbonic anhydrase V	.	CAH5A_HUMAN; CAH5B_HUMAN	Protein Family	.	Carbonic anhydrase V	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P35218
TTODU18	Glutamate receptor NMDA	.	NMDZ1_HUMAN; NMDE1_HUMAN; NMDE2_HUMAN; NMDE3_HUMAN; NMDE4_HUMAN; NMD3A_HUMAN; NMD3B_HUMAN	Protein Family	.	Glutamate receptor NMDA	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q05586
TTQ3PN1	Glutamate receptor	.	GRIA1_HUMAN; GRIA2_HUMAN; GRIA3_HUMAN; GRIA4_HUMAN	Protein Family	.	Glutamate receptor	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P42261
TTJ60V4	Nuclear factor-kappa B	.	NFKB1_HUMAN; NFKB2_HUMAN; TF65_HUMAN	Protein Family	.	Nuclear factor-kappa B	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P19838
TT6EMVP	CD85k-Fibronectin interaction (LILRB4-FN1 PPI)	Q8NHJ6-P02751	LIRB4_HUMAN-FINC_HUMAN	.	.	LILRB4-FN1 PPI	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of NGM Biopharma"	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZPFCG	CD47-SHPS1 interaction (CD47-SHPS1 PPI)	Q08722-P78324 	CD47_HUMAN-SHPS1_HUMAN	.	.	CD47-SHPS1 PPI	.	.	.	.	Clinical trial	"ClinicalTrials.gov (NCT05626322) A PHASE 1b/2 STUDY OF PF-07901801, A CD47 BLOCKING AGENT, WITH TAFASITAMAB AND LENALIDOMIDE FOR PARTICIPANTS WITH RELAPSED/REFRACTORY DIFFUSE LARGE B CELL LYMPHOMA NOT ELIGIBLE FOR STEM CELL TRANSPLANTATION. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHWZMR	Integrin alpha-5/beta-1 (ITGA5/B1)	P06756-P05556	ITAV_HUMAN-ITB1_HUMAN	.	.	ITGA5/B1	.	.	.	.	Clinical trial	Dual inhibition of alpha(v)beta(6) and alpha(v)beta(1) reduces fibrogenesis in lung tissue explants from patients with IPF. Respir Res. 2021 Oct 19;22(1):265.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTT3IXG	Kynurenine oxoglutarate transaminase II (AADAT)	Q8N5Z0	AADAT_HUMAN	Transaminase	"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"	AADAT	"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)."	EC 2.6.1.39	6D0A; 5TF5; 5EUN; 5EFS; 4GEB	MNYARFITAASAARNPSPIRTMTDILSRGPKSMISLAGGLPNPNMFPFKTAVITVENGKTIQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQGLCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKPEDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNKFRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQLMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKVKGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQLIKESL	Preclinical	Improvement of kynurenine aminotransferase-II inhibitors guided by mimicking sulfate esters. PLoS One. 2018 Apr 24;13(4):e0196404.	.	.	.	.	.	.	.	.	.	.	.	hsa00310: Lysine degradation; hsa00380: Tryptophan metabolism; hsa01100: Metabolic pathways; hsa01210: 2-Oxocarboxylic acid metabolism	R-HSA-71064: Lysine catabolism; R-HSA-71240: Tryptophan catabolism	MetaCyc:HS03239-MON	Q8N5Z0
TT0Z32T	Adaptor-associated kinase 1 (AAK1)	Q2M2I8	AAK1_HUMAN	Kinase	Adaptor-associated kinase 1	AAK1	"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."	EC 2.7.11.1	5TE0; 5L4Q; 4WSQ	MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPAKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPPPQAAGSSNQPGLLASVPQPKPQAPPSQPLPQTQAKQPQAPPTPQQTPSTQAQGLPAQAQATPQHQQQLFLKQQQQQQQPPPAQQQPAGTFYQQQQAQTQQFQAVHPATQKPAIAQFPVVSQGGSQQQLMQNFYQQQQQQQQQQQQQQLATALHQQQLMTQQAALQQKPTMAAGQQPQPQPAAAPQPAPAQEPAIQAPVRQQPKVQTTPPPAVQGQKVGSLTPPSSPKTQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRTSQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKHPEKLGGSAESLIPGFQSTQGDAFATTSFSAGTAEKRKGGQTVDSGLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVTSNRTDSLTGEDSLLDCSLLSNPTTDLLEEFAPTAISAPVHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	.	R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis	.	Q2M2I8
TTN9A16	HUMAN adaptor-associated kinase 1 (AAK1)	Q2M2I8	AAK1_HUMAN	Kinase	Adaptor-associated kinase 1	AAK1	"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."	EC 2.7.11.1	5TE0; 5L4Q; 4WSQ	MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPAKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPPPQAAGSSNQPGLLASVPQPKPQAPPSQPLPQTQAKQPQAPPTPQQTPSTQAQGLPAQAQATPQHQQQLFLKQQQQQQQPPPAQQQPAGTFYQQQQAQTQQFQAVHPATQKPAIAQFPVVSQGGSQQQLMQNFYQQQQQQQQQQQQQQLATALHQQQLMTQQAALQQKPTMAAGQQPQPQPAAAPQPAPAQEPAIQAPVRQQPKVQTTPPPAVQGQKVGSLTPPSSPKTQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRTSQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKHPEKLGGSAESLIPGFQSTQGDAFATTSFSAGTAEKRKGGQTVDSGLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVTSNRTDSLTGEDSLLDCSLLSNPTTDLLEEFAPTAISAPVHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL	.	Baricitinib for COVID-19: a suitable treatment Lancet Infect Dis. 2020 Apr 3. pii: S1473-3099(20)30262-0.	17	.	.	.	.	.	.	.	.	.	.	.	R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis	.	Q2M2I8
TT19ATJ	Abeta-binding alcohol dehydrogenase (ABAD)	Q2L8D9	Q2L8D9_HUMAN	.	Amyloid beta-binding alcohol dehydrogenase	ABAD	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. 	.	.	MAAACRSVK	Literature-reported	ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science. 2004 Apr 16;304(5669):448-52.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTT2LD9	GABA transaminase (ABAT)	P80404	GABT_HUMAN	Transaminase	L-AIBAT; Gamma-amino-N-butyrate transaminase; GABA-T; GABA-AT; GABA aminotransferase; ABAT; (S)-3-amino-2-methylpropionate transaminase	ABAT	"Catalyzes the conversion of gamma-aminobutyrate and L- beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate andbeta-alanine."	EC 2.6.1.19	.	MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMKQLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQNASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYRSKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPSFDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGGDNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMMTGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLLDLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVFRDHHAHLFLNIFSDILADFK	Successful	"DrugBank: a knowledgebase for drugs, drug actions and drug targets. Nucleic Acids Res. 2008 Jan;36(Database issue):D901-6."	34	.	.	.	.	.	.	.	.	.	.	"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"	R-HSA-916853: Degradation of GABA	MetaCyc:HS02477-MON	P80404
TTJW1GN	ATP-binding cassette transporter A1 (ABCA1)	O95477	ABCA1_HUMAN	ABC transporter	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	ABCA1	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.	EC 7.6.2.1	5XJY	MACWPQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDTSMKDMRKVLRTLQQIKKSSSNLKLQDFLVDNETFSGFLYHNLSLPKSTVDKMLRADVILHKVFLQGYQLHLTSLCNGSKSEEMIQLGDQEVSELCGLPREKLAAAERVLRSNMDILKPILRTLNSTSPFPSKELAEATKTLLHSLGTLAQELFSMRSWSDMRQEVMFLTNVNSSSSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAETFYDNSTTPYCNDLMKNLESSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDLEGMWEELSPKIWTFMENSQEMDLVRMLLDSRDNDHFWEQQLDGLDWTAQDIVAFLAKHPEDVQSSNGSVYTWREAFNETNQAIRTISRFMECVNLNKLEPIATEVWLINKSMELLDERKFWAGIVFTGITPGSIELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGTEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFVFLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFTLKIFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTSVSMMLFDTFLYGVMTWYIEAVFPGQYGIPRPWYFPCTKSYWFGEESDEKSHPGSNQKRISEICMEEEPTHLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLSSCRNSSSTVSYLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGTLPARRNRRAFGDKQSCLRPFTEDDAADPNDSDIDPESRETDLLSGMDGKGSYQVKGWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQPWMYNEQYTFVSNDAPEDTGTLELLNALTKDPGFGTRCMEGNPIPDTPCQAGEEEWTTAPVPQTIMDLFQNGNWTMQNPSPACQCSSDKIKKMLPVCPPGAGGLPPPQRKQNTADILQDLTGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGVSNTQALPPSQEVNDAIKQMKKHLKLAKDSSADRFLNSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSHYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTDNKLNNINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEGVVFFLITVLIQYRFFIRPRPVNAKLSPLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQDFFGLAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNFAKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	TC=3.A.1	ABC transporter	ABC transporter superfamily. ABCA family.	.	.	ABC transporter	PF00005	PF00005; ABC_tran	3.A.1.211.14	The ATP-binding Cassette (ABC) Superfamily	hsa02010:ABC transporters; hsa04975:Fat digestion and absorption	R-HSA-194223:HDL-mediated lipid transport; R-HSA-1989781:PPARA activates gene expression	.	O95477
TTLB52K	ATP-binding cassette transporter A4 (ABCA4)	P78363	ABCA4_HUMAN	ABC transporter	Stargardt disease protein; RmP; Retinal-specific ATP-binding cassette transporter; RIM protein; RIM ABC transporter; ATP-binding cassette sub-family A member 4; ABCA4	ABCA4	"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."	EC 7.6.2.1	.	MGFVRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSHHECHFPNKAMPSAGMLPWLQGIFCNVNNPCFQSPTPGESPGIVSNYNNSILARVYRDFQELLMNAPESQHLGRIWTELHILSQFMDTLRTHPERIAGRGIRIRDILKDEETLTLFLIKNIGLSDSVVYLLINSQVRPEQFAHGVPDLALKDIACSEALLERFIIFSQRRGAKTVRYALCSLSQGTLQWIEDTLYANVDFFKLFRVLPTLLDSRSQGINLRSWGGILSDMSPRIQEFIHRPSMQDLLWVTRPLMQNGGPETFTKLMGILSDLLCGYPEGGGSRVLSFNWYEDNNYKAFLGIDSTRKDPIYSYDRRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKILYTPDSPAARRILKNANSTFEELEHVRKLVKAWEEVGPQIWYFFDNSTQMNMIRDTLGNPTVKDFLNRQLGEEGITAEAILNFLYKGPRESQADDMANFDWRDIFNITDRTLRLVNQYLECLVLDKFESYNDETQLTQRALSLLEENMFWAGVVFPDMYPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGITRSQVQAEAPVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMLCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTAELKKAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPTEGDEFSFLLSMQMMLLDAAVYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPLTEETEDPEHPEGIHDSFFEREHPGWVPGVCVKNLVKIFEPCGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGRDIETSLDAVRQSLGMCPQHNILFHHLTVAEHMLFYAQLKGKSQEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVILDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIAQGRLYCSGTPLFLKNCFGTGLYLTLVRKMKNIQSQRKGSEGTCSCSSKGFSTTCPAHVDDLTPEQVLDGDVNELMDVVLHHVPEAKLVECIGQELIFLLPNKNFKHRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDSDSGPLFAGGAQQKRENVNPRHPCLGPREKAGQTPQDSNVCSPGAPAAHPEGQPPPEPECPGPQLNTGTQLVLQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIVIPPFGEYPALTLHPWIYGQQYTFFSMDEPGSEQFTVLADVLLNKPGFGNRCLKEGWLPEYPCGNSTPWKTPSVSPNITQLFQKQKWTQVNPSPSCRCSTREKLTMLPECPEGAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGGKLPVVPITGEALVGFLSDLGRIMNVSGGPITREASKEIPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKDRSPEEYGITVISQPLNLTKEQLSEITVLTTSVDAVVAICVIFSMSFVPASFVLYLIQERVNKSKHLQFISGVSPTTYWVTNFLWDIMNYSVSAGLVVGIFIGFQKKAYTSPENLPALVALLLLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFILELFENNRTLLRFNAVLRKLLIVFPHFCLGRGLIDLALSQAVTDVYARFGEEHSANPFHWDLIGKNLFAMVVEGVVYFLLTLLVQRHFFLSQWIAEPTKEPIVDEDDDVAEERQRIITGGNKTDILRLHELTKIYPGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISEVHQNMGYCPQFDAIDELLTGREHLYLYARLRGVPAEEIEKVANWSIKSLGLTVYADCLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNVIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFRCMGTIQHLKSKFGDGYIVTMKIKSPKDDLLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSSLARIFQLLLSHKDSLLIEEYSVTQTTLDQVFVNFAKQQTESHDLPLHPRAAGASRQAQD	Clinical trial	"Clinical pipeline report, company report or official report of Oxford BioMedica."	19	.	.	.	.	.	.	.	.	.	.	hsa02010:ABC transporters	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	.	P78363
TT3OT40	Multidrug resistance protein 1 (ABCB1)	P08183	MDR1_HUMAN	ABC transporter	PGY1; P-glycoprotein 1; MDR1; CD243 antigen; CD243; ATP-binding cassette sub-family B member 1	ABCB1	Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.	EC 7.6.2.2	6QEX; 6FN4; 6FN1; 6C0V	MDLEGDRNGGAKKKNFFKLNNKSEKDKKEKKPTVSVFSMFRYSNWLDKLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMSNITNRSDINDTGFFMNLEEDMTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVELENAADESKSEIDALEMSSNDSRSSLIRKRSTRRSVRGSQAQDRKLSTKEALDESIPPVSFWRIMKLNLTEWPYFVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDSYSTEGLMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAGTKRQ	Successful	"VX-710 (biricodar) increases drug retention and enhances chemosensitivity in resistant cells overexpressing P-glycoprotein, multidrug resistance protein, and breast cancer resistance protein. Clin Cancer Res. 2004 Mar 1;10(5):1826-34."	34	TC=3.A.1	Acid anhydrides hydrolase	ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily. 	7.6.2.2	Catalysing the translocation of other compounds	ABC transporter transmembrane region; ABC transporter	PF00664; PF00005	PF00664; ABC_membrane; PF00005; ABC_tran	3.A.1.201.1	ATP-binding cassette	hsa02010:ABC transporters; hsa04976:Bile secretion; hsa05206:MicroRNAs in cancer	R-HSA-382556:ABC-family proteins mediated transport	MetaCyc:HS01500-MON	P08183
TTUXCAF	ATP-binding cassette transporter B11 (ABCB11)	O95342	ABCBB_HUMAN	ABC transporter	"BSEP; ATP-binding cassette, sub-family B, member 11; ATP-binding cassette sub-family B member 11"	ABCB11	Involved in the ATP-dependent secretion of bile salts into the canaliculus of hepatocytes.	.	.	MSDSVILRSIKKFGEENDGFESDKSYNNDKKSRLQDEKKGDGVRVGFFQLFRFSSSTDIWLMFVGSLCAFLHGIAQPGVLLIFGTMTDVFIDYDVELQELQIPGKACVNNTIVWTNSSLNQNMTNGTRCGLLNIESEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDEGEYTPGTLVQIFLSVIVGALNLGNASPCLEAFATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIKGEIEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQGNQALNEEDIKDATEDDMLARTFSRGSYQDSLRASIRQRSKSQLSYLVHEPPLAVVDHKSTYEEDRKDKDIPVQEEVEPAPVRRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDLRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQPPISVYNTAGEKWDNFQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVTTGSPIS	Literature-reported	NCBI GEO: archive for functional genomics data sets--update. Nucleic Acids Res. 2013 Jan;41(Database issue):D991-5.	.	TC=3.A.1	ABC transporter	ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily. 	.	.	ABC transporter transmembrane region; ABC transporter	PF00664; PF00005	PF00664; ABC_membrane; PF00005; ABC_tran	3.A.1.201.2	The ATP-binding Cassette (ABC) Superfamily	hsa02010:ABC transporters; hsa04976:Bile secretion	R-HSA-159418:Recycling of bile acids and salts	.	O95342
TTJUXV6	Multidrug resistance protein 3 (ABCB4)	P21439	MDR3_HUMAN	Acid anhydrides hydrolase	PGY3; P-gp; MDR3; ATP-binding cassette sub-family B member 4; ABCB4	ABCB4	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.	EC 7.6.2.1	.	MDLEAAKNGTAWRPTSAEGDFELGISSKQKRKKTKTVKMIGVLTLFRYSDWQDKLFMSLGTIMAIAHGSGLPLMMIVFGEMTDKFVDTAGNFSFPVNFSLSLLNPGKILEEEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDSIKGNLEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQTSGSQIQSEEFELNDEKAATRMAPNGWKSRLFRHSTQKNLKNSQMCQKSLDVETDGLEANVPPVSFLKVLKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVKQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHMRFRDVILVFSAIVFGAVALGHASSFAPDYAKAKLSAAHLFMLFERQPLIDSYSEEGLKPDKFEGNITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFGFQLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAGTQNL	Clinical trial	"Reversal of multidrug resistance by a novel quinoline derivative, MS-209. Cancer Chemother Pharmacol. 1995;35(4):271-7."	9	.	.	.	.	.	.	.	.	.	.	hsa02010:ABC transporters; hsa04976:Bile secretion	R-HSA-1989781:PPARA activates gene expression; R-HSA-382556:ABC-family proteins mediated transport	.	P21439
TTOI92F	Multidrug resistance-associated protein 1 (ABCC1)	P33527	MRP1_HUMAN	ABC transporter	MRP1; MRP; Leukotriene C(4) transporter; LTC4 transporter; ATP-binding cassette sub-family C member 1	ABCC1	"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."	EC 7.6.2.2	4C3Z; 2CBZ	MALRGFCSADGSDPLWDWNVTWNTSNPDFTKCFQNTVLVWVPCFYLWACFPFYFLYLSRHDRGYIQMTPLNKTKTALGFLLWIVCWADLFYSFWERSRGIFLAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKIMTALKEDAQVDLFRDITFYVYFSLLLIQLVLSCFSDRSPLFSETIHDPNPCPESSASFLSRITFWWITGLIVRGYRQPLEGSDLWSLNKEDTSEQVVPVLVKNWKKECAKTRKQPVKVVYSSKDPAQPKESSKVDANEEVEALIVKSPQKEWNPSLFKVLYKTFGPYFLMSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFAVYVTIDENNILDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRPVKDGGGTNSITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQNDSLRENILFGCQLEEPYYRSVIQACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQDAEENGVTGVSGPGKEAKQMENGMLVTDSAGKQLQRQLSSSSSYSGDISRHHNSTAELQKAEAKKEETWKLMEADKAQTGQVKLSVYWDYMKAIGLFISFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSSWPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSMAKDAGLV	Successful	Transport of diclofenac by breast cancer resistance protein (ABCG2) and stimulation of multidrug resistance protein 2 (ABCC2)-mediated drug transpo... Drug Metab Dispos. 2009 Jan;37(1):129-36.	34	TC=3.A.1	ABC transporter	ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. 	.	.	ABC transporter transmembrane region; ABC transporter	PF00664; PF00005	PF00664; ABC_membrane; PF00005; ABC_tran	3.A.1.208.8	The ATP-binding Cassette (ABC) Superfamily	hsa02010:ABC transporters; hsa04071:Sphingolipid signaling pathway; hsa04977:Vitamin digestion and absorption; hsa05206:MicroRNAs in cancer	"R-HSA-196741:Cobalamin (Cbl, vitamin B12) transport and metabolism; R-HSA-382556:ABC-family proteins mediated transport"	MetaCyc:ENSG00000103222-MON	P33527
TTQ79SU	HUMAN multidrug resistance-associated protein 1 (ABCC1)	P33527	MRP1_HUMAN	ABC transporter	MRP1; MRP; Leukotriene C(4) transporter; LTC4 transporter; ATP-binding cassette sub-family C member 1	ABCC1	"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."	EC 7.6.2.2	4C3Z; 2CBZ	MALRGFCSADGSDPLWDWNVTWNTSNPDFTKCFQNTVLVWVPCFYLWACFPFYFLYLSRHDRGYIQMTPLNKTKTALGFLLWIVCWADLFYSFWERSRGIFLAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKIMTALKEDAQVDLFRDITFYVYFSLLLIQLVLSCFSDRSPLFSETIHDPNPCPESSASFLSRITFWWITGLIVRGYRQPLEGSDLWSLNKEDTSEQVVPVLVKNWKKECAKTRKQPVKVVYSSKDPAQPKESSKVDANEEVEALIVKSPQKEWNPSLFKVLYKTFGPYFLMSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFAVYVTIDENNILDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRPVKDGGGTNSITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQNDSLRENILFGCQLEEPYYRSVIQACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQDAEENGVTGVSGPGKEAKQMENGMLVTDSAGKQLQRQLSSSSSYSGDISRHHNSTAELQKAEAKKEETWKLMEADKAQTGQVKLSVYWDYMKAIGLFISFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSSWPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSMAKDAGLV	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa01523: Antifolate resistance; hsa02010: ABC transporters; hsa04071: Sphingolipid signaling pathway; hsa04977: Vitamin digestion and absorption; hsa05206: MicroRNAs in cancer	R-HSA-189483: Heme degradation; R-HSA-2142691: Synthesis of Leukotrienes (LT) and Eoxins (EX); R-HSA-382556: ABC-family proteins mediated transport; R-HSA-9707564: Cytoprotection by HMOX1; R-HSA-9753281: Paracetamol ADME; R-HSA-9758890: Transport of RCbl within the body	MetaCyc:ENSG00000103222-MON	P33527
TTFLHJV	Multidrug resistance-associated protein 2 (ABCC2)	Q92887	MRP2_HUMAN	ABC transporter	"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"	ABCC2	May function as a cellular cisplatin transporter. Mediates hepatobiliary excretion of numerous organic anions.	EC 7.6.2.2	.	MLEKFCNSTFWNSSFLDSPEADLPLCFEQTVLVWIPLGYLWLLAPWQLLHVYKSRTKRSSTTKLYLAKQVFVGFLLILAAIELALVLTEDSGQATVPAVRYTNPSLYLGTWLLVLLIQYSRQWCVQKNSWFLSLFWILSILCGTFQFQTLIRTLLQGDNSNLAYSCLFFISYGFQILILIFSAFSENNESSNNPSSIASFLSSITYSWYDSIILKGYKRPLTLEDVWEVDEEMKTKTLVSKFETHMKRELQKARRALQRRQEKSSQQNSGARLPGLNKNQSQSQDALVLEDVEKKKKKSGTKKDVPKSWLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVYVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDDLDTSAIRHDCNFDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKNLKTFLRHTGPEEEATVHDGSEEEDDDYGLISSVEEIPEDAASITMRRENSFRRTLSRSSRSNGRHLKSLRNSLKTRNVNSLKEDEELVKGQKLIKKEFIETGKVKFSIYLEYLQAIGLFSIFFIILAFVMNSVAFIGSNLWLSAWTSDSKIFNSTDYPASQRDMRVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFMAKEAGIENVNSTKF	Literature-reported	Targeting an extracellular epitope of the human multidrug resistance protein 1 (MRP1) in malignant cells with a novel recombinant single chain Fv a... Int J Cancer. 2004 Jul 20;110(6):882-90.	.	TC=3.A.1	ABC transporter	ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. 	.	.	ABC transporter transmembrane region; ABC transporter	PF00664; PF00005	PF00664; ABC_membrane; PF00005; ABC_tran	3.A.1.208.2	The ATP-binding Cassette (ABC) Superfamily	hsa02010:ABC transporters; hsa04976:Bile secretion	R-HSA-382556:ABC-family proteins mediated transport	.	Q92887
TTVLG21	Multidrug resistance protein 3	.	MRP3_HUMAN	Single Protein	ATP-binding cassette sub-family C member 3; Canalicular multispecific organic anion transporter 2; MOAT-D; Multi-specific organic anion transporter D; Multidrug resistance-associated protein 3	ABCC3	"ATP-dependent transporter of the ATP-binding cassette (ABC) family that bind and hydrolyze ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes. Transports glucuronide conjugates such as bilirubin diglucuronide, estradiol-17-beta-o-glucuronide and GSH conjugates such as leukotriene C4 (LTC4). Transports also various bile salts (taurocholate, glycocholate, taurochenodeoxycholate-3-sulfate, taurolithocholate- 3-sulfate)."	.	.	MDALCGSGELGSKFWDSNLSVHTENPDLTPCFQNSLLAWVPCIYLWVALPCYLLYLRHHCRGYIILSHLSKLKMVLGVLLWCVSWADLFYSFHGLVHGRAPAPVFFVTPLVVGVTMLLATLLIQYERLQGVQSSGVLIIFWFLCVVCAIVPFRSKILLAKAEGEISDPFRFTTFYIHFALVLSALILACFREKPPFFSAKNVDPNPYPETSAGFLSRLFFWWFTKMAIYGYRHPLEEKDLWSLKEEDRSQMVVQQLLEAWRKQEKQTARHKASAAPGKNASGEDEVLLGARPRPRKPSFLKALLATFGSSFLISACFKLIQDLLSFINPQLLSILIRFISNPMAPSWWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVIYRKALVITNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSVLAGVAFMVLLIPLNGAVAVKMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSFLKQVEGIRQGELQLLRTAAYLHTTTTFTWMCSPFLVTLITLWVYVYVDPNNVLDAEKAFVSVSLFNILRLPLNMLPQLISNLTQASVSLKRIQQFLSQEELDPQSVERKTISPGYAITIHSGTFTWAQDLPPTLHSLDIQVPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGKVHMKGSVAYVPQQAWIQNCTLQENVLFGKALNPKRYQQTLEACALLADLEMLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDADIFLLDDPLSAVDSHVAKHIFDHVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQVSEMGPYPALLQRNGSFANFLCNYAPDEDQGHLEDSWTALEGAEDKEALLIEDTLSNHTDLTDNDPVTYVVQKQFMRQLSALSSDGEGQGRPVPRRHLGPSEKVQVTEAKADGALTQEEKAAIGTVELSVFWDYAKAVGLCTTLAICLLYVGQSAAAIGANVWLSAWTNDAMADSRQNNTSLRLGVYAALGILQGFLVMLAAMAMAAGGIQAARVLHQALLHNKIRSPQSFFDTTPSGRILNCFSKDIYVVDEVLAPVILMLLNSFFNAISTLVVIMASTPLFTVVILPLAVLYTLVQRFYAATSRQLKRLESVSRSPIYSHFSETVTGASVIRAYNRSRDFEIISDTKVDANQRSCYPYIISNRWLSIGVEFVGNCVVLFAALFAVIGRSSLNPGLVGLSVSYSLQVTFALNWMIRMMSDLESNIVAVERVKEYSKTETEAPWVVEGSRPPEGWPPRGEVEFRNYSVRYRPGLDLVLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEGGENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIAHRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGMARDAGLA	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	O15438
TTUEAFL	Multidrug resistance protein 4 (ABCC4)	O15439	MRP4_HUMAN	ABC transporter	Multispecific organic anion transporter B; Multidrug resistanceassociated protein 4; MRP/cMOATrelated ABC transporter; MOATB; ATPbinding cassette subfamily C member 4; ABCC4	ABCC4	May be an organic anion pump relevant to cellular detoxification.	.	.	MLPVYQEVKPNPLQDANLCSRVFFWWLNPLFKIGHKRRLEEDDMYSVLPEDRSQHLGEELQGFWDKEVLRAENDAQKPSLTRAIIKCYWKSYLVLGIFTLIEESAKVIQPIFLGKIINYFENYDPMDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLGSVITASRVFVAVTLYGAVRLTVTLFFPSAIERVSEAIVSIRRIQTFLLLDEISQRNRQLPSDGKKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLKKDNEESEQPPVPGTPTLRNRTFSESSVWSQQSSRPSLKDGALESQDTENVPVTLSEENRSEGKVGFQAYKNYFRAGAHWIVFIFLILLNTAAQVAYVLQDWWLSYWANKQSMLNVTVNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVPLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAMFVIIVAFGSLILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYTDLEKEAPWEYQKRPPPAWPHEGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNKESLFYKMVQQLGKAEAAALTETAKQVYFKRNYPHIGHTDHMVTNTSNGQPSTLTIFETAL	Literature-reported	High-throughput screening identifies Ceefourin 1 and Ceefourin 2 as highly selective inhibitors of multidrug resistance protein 4 (MRP4). Biochem Pharmacol. 2014 Sep 1;91(1):97-108.	.	.	.	.	.	.	.	.	.	.	.	hsa01523: Antifolate resistance; hsa02010: ABC transporters; hsa04024: cAMP signaling pathway; hsa04976: Bile secretion	R-HSA-114608: Platelet degranulation; R-HSA-382556: ABC-family proteins mediated transport; R-HSA-9748787: Azathioprine ADME; R-HSA-9753281: Paracetamol ADME	.	O15439
TTP835K	ATP-binding cassette transporter C8 (ABCC8)	Q09428	ABCC8_HUMAN	ABC transporter	Sulfonylurea receptor 1; SUR1-type K(ATP) channel; SUR1; Kir6.2/SUR1; ATPbinding cassette subfamily C member 8; ABCC8	ABCC8	Putative subunit of the beta-cell ATP-sensitive potassium channel (KATP). Regulator of ATP-sensitive K(+) channels and insulin release.	.	6C3P; 6C3O	MPLAFCGSENHSAAYRVDQGVLNNGCFVDALNVVPHVFLLFITFPILFIGWGSQSSKVHIHHSTWLHFPGHNLRWILTFMLLFVLVCEIAEGILSDGVTESHHLHLYMPAGMAFMAAVTSVVYYHNIETSNFPKLLIALLVYWTLAFITKTIKFVKFLDHAIGFSQLRFCLTGLLVILYGMLLLVEVNVIRVRRYIFFKTPREVKPPEDLQDLGVRFLQPFVNLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCEAFDAQVRKDIQGTQGARAIWQALSHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLGKENDVFQPKTQFLGVYFVSSQEFLANAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSEFLSSAEIREEQCAPHEPTPQGPASKYQAVPLRVVNRKRPAREDCRGLTGPLQSLVPSADGDADNCCVQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDPSPERETATDLDIRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLFEHWKTLMNRQDQELEKETVTERKATEPPQGLSRAMSSRDGLLQDEEEEEEEAAESEEDDNLSSMLHQRAEIPWRACAKYLSSAGILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAESYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRADK	Successful	Mechanism of disopyramide-induced hypoglycaemia in a patient with Type 2 diabetes. Diabet Med. 2009 Jan;26(1):76-8.	34	TC=3.A.1	.	.	.	.	.	.	.	.	.	hsa02010:ABC transporters; hsa04911:Insulin secretion; hsa04930:Type II diabetes mellitus	R-HSA-382556:ABC-family proteins mediated transport; R-HSA-422356:Regulation of insulin secretion	.	Q09428
TTEF5MJ	ATP-binding cassette transporter C9 (ABCC9)	O60706	ABCC9_HUMAN	ABC transporter	Sulfonylurea receptor 2; SUR2; ATP-binding cassette sub-family C member 9	ABCC9	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.	.	.	MSLSFCGNNISSYNINDGVLQNSCFVDALNLVPHVFLLFITFPILFIGWGSQSSKVQIHHNTWLHFPGHNLRWILTFALLFVHVCEIAEGIVSDSRRESRHLHLFMPAVMGFVATTTSIVYYHNIETSNFPKLLLALFLYWVMAFITKTIKLVKYCQSGLDISNLRFCITGMMVILNGLLMAVEINVIRVRRYVFFMNPQKVKPPEDLQDLGVRFLQPFVNLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKVADHPNRTPSIWLAMYRAFGRPILLSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISETLSSKEFLENAYVLAVLLFLALILQRTFLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEIGDDSWRTGESSLPFESCKKHTGVQPKTINRKQPGRYHLDSYEQSTRRLRPAETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNRQDQELEKDMEADQTTLERKTLRRAMYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMPWKTCWRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENYEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSSIMDAGLVLVFSEGILVECDTVPNLLAHKNGLFSTLVMTNK	Successful	Mechanism of disopyramide-induced hypoglycaemia in a patient with Type 2 diabetes. Diabet Med. 2009 Jan;26(1):76-8.	34	.	.	.	.	.	.	.	.	.	.	hsa02010: ABC transporters	"R-HSA-1296025: ATP sensitive Potassium channels; R-HSA-382556: ABC-family proteins mediated transport; R-HSA-5578775: Ion homeostasis; R-HSA-5678420: Defective ABCC9 causes CMD10, ATFB12 and Cantu syndrome"	.	O60706
TTMWDGU	ATP-binding cassette transporter G1 (ABCG1)	P45844	ABCG1_HUMAN	ABC transporter	White protein homolog; WHT1; ATP-binding cassette transporter 8; ATP-binding cassette sub-family G member 1; ABC8	ABCG1	"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."	.	.	MACLMAAFSVGTAMNASSYSAEMTEPKSVCVSVDEVVSSNMEATETDLLNGHLKKVDNNLTEAQRFSSLPRRAAVNIEFRDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEVASGEYGDQNSRLVRAVREGMCDSDHKRDLGGDAEVNPFLWHRPSEEVKQTKRLKGLRKDSSSMEGCHSFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMGVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGLDREDLHCDIDETCHFQKSEAILRELDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRAER	Literature-reported	ABCG1 as a potential oncogene in lung cancer. Exp Ther Med. 2017 Jun;13(6):3189-3194.	.	.	.	.	.	.	.	.	.	.	.	hsa02010: ABC transporters; hsa05417: Lipid and atherosclerosis	R-HSA-1369062: ABC transporters in lipid homeostasis; R-HSA-8964058: HDL remodeling; R-HSA-9029569: NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux	.	P45844
TTIMJ02	ATP-binding cassette transporter G2 (ABCG2)	Q9UNQ0	ABCG2_HUMAN	ABC transporter	Urate exporter; Placenta-specific ATP-binding cassette transporter; Mitoxantrone resistance-associated protein; MXR; CDw338; CD338; Breast cancer resistance protein; BCRP1; BCRP; ABCP	ABCG2	"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."	.	6HZM; 6HIJ; 6HCO; 6HBU; 6FFC	MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS	Successful	The anti-inflammatory mechanism of sulfasalazine is related to adenosine release at inflamed sites. J Immunol. 1996 Mar 1;156(5):1937-41.	34	TC=3.A.1	ABC transporter	ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. 	.	.	ABC-2 type transporter; ABC transporter	PF01061; PF00005	PF01061; ABC2_membrane; PF00005; ABC_tran	3.A.1.204.2	The ATP-binding Cassette (ABC) Superfamily	hsa01523: Antifolate resistance; hsa02010: ABC transporters; hsa04976: Bile secretion	R-HSA-189451: Heme biosynthesis; R-HSA-189483: Heme degradation; R-HSA-2161517: Abacavir transmembrane transport; R-HSA-917937: Iron uptake and transport; R-HSA-9753281: Paracetamol ADME	.	Q9UNQ0
TTKZ7WY	ATP-binding cassette transporter G5 (ABCG5)	Q9H222	ABCG5_HUMAN	ABC transporter	Sterolin1; ATPbinding cassette subfamily G member 5; ABCG5	ABCG5	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.	.	5DO7	MGDLSSLTPGGSMGLQVNRGSQSSLEGAPATAPEPHSLGILHASYSVSHRVRPWWDITSCRQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPKVMLFDEPTTGLDCMTANQIVVLLVELARRNRIVVLTIHQPRSELFQLFDKIAILSFGELIFCGTPAEMLDFFNDCGYPCPEHSNPFDFYMDLTSVDTQSKEREIETSKRVQMIESAYKKSAICHKTLKNIERMKHLKTLPMVPFKTKDSPGVFSKLGVLLRRVTRNLVRNKLAVITRLLQNLIMGLFLLFFVLRVRSNVLKGAIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAVSDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNSVVALLSIAGVLVGSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVNEFYGLNFTCGSSNVSVTTNPMCAFTQGIQFIEKTCPGATSRFTMNFLILYSFIPALVILGIVVFKIRDHLISR	Literature-reported	ABCG5/ABCG8 in cholesterol excretion and atherosclerosis. Clin Chim Acta. 2014 Jan 20;428:82-8.	.	.	.	.	.	.	.	.	.	.	.	hsa02010: ABC transporters; hsa04975: Fat digestion and absorption; hsa04976: Bile secretion; hsa04979: Cholesterol metabolism	R-HSA-1369062: ABC transporters in lipid homeostasis; R-HSA-5679090: Defective ABCG8 causes GBD4 and sitosterolemia; R-HSA-5679096: Defective ABCG5 causes sitosterolemia; R-HSA-9029569: NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux	.	Q9H222
TTSINOV	Monoacylglycerol lipase ABHD6 (ABHD6)	Q9BV23	ABHD6_HUMAN	Carboxylic ester hydrolase	Abhydrolase domain-containing protein 6; 2-arachidonoylglycerol hydrolase	ABHD6	"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."	EC 3.1.1.23	.	MDLDVVNMFVIAGGTLAIPILAFVASFLLWPSALIRIYYWYWRRTLGMQVRYVHHEDYQFCYSFRGRPGHKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGSAAVEKIPLIPSTPEEMSEMLQLCSYVRFKVPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVELLENCGHSVVMERPRKTAKLIIDFLASVHNTDNNKKLD	Patented-recorded	A patent review of Monoacylglycerol Lipase (MAGL) inhibitors (2013-2017).Expert Opin Ther Pat. 2017 Dec;27(12):1341-1351.	15.5	EC:3.1.1	AB hydrolase superfamily	AB hydrolase superfamily.	3.1.1.23 	Acting on ester bonds	alpha/beta hydrolase fold	PF00561	PF00561; Abhydrolase_1	.	.	hsa04723:Retrograde endocannabinoid signaling	R-HSA-426048: Arachidonate production from DAG	.	Q9BV23
TT6B75U	ABL messenger RNA (ABL mRNA)	P00519	ABL1_HUMAN	mRNA target	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)	ABL1	"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."	EC 2.7.10.2	6NPV; 6NPU; 6NPE; 6BL8; 6AMW	MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR	Discontinued	"Pharmaceutical Design And Development: A Molecular Biology Approach, T V Ramabhadran, 2005. Page(219)."	5	mRNA	mRNA target	.	.	.	F-actin binding; Protein tyrosine kinase; SH2 domain; SH3 domain	PF08919; PF07714; PF00017; PF00018	PF08919; F_actin_bind; PF07714; Pkinase_Tyr; PF00017; SH2; PF00018; SH3_1	.	.	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	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	.	P00519
TT3PJMV	Tyrosine-protein kinase ABL1 (ABL)	P00519	ABL1_HUMAN	Kinase	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	ABL1	"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."	EC 2.7.10.2	6NPV; 6NPU; 6NPE; 6BL8; 6AMW	MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR	Successful	Targeted chronic myeloid leukemia therapy: Seeking a cure. Am J Health Syst Pharm. 2007 Dec 15;64(24 Suppl 15):S9-15.	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. ABL subfamily.	2.7.10.2 	Transferring phosphorus-containing groups	F-actin binding; Protein tyrosine kinase; SH2 domain; SH3 domain	PF08919; PF07714; PF00017; PF00018	PF08919; F_actin_bind; PF07714; Pkinase_Tyr; PF00017; SH2; PF00018; SH3_1	.	.	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	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	.	P00519
TTZJTWA	ABL T315I mutant (ABL T315I)	P00519	ABL1_HUMAN	Kinase	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	ABL1	"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."	EC 2.7.10.2	6NPV; 6NPU; 6NPE; 6BL8; 6AMW	MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR	Patented-recorded	Bcr-Abl tyrosine kinase inhibitors: a patent review.Expert Opin Ther Pat. 2015 Apr;25(4):397-412.	15.5	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. ABL subfamily.	2.7.10.2 	Transferring phosphorus-containing groups	F-actin binding; Protein tyrosine kinase; SH2 domain; SH3 domain	PF08919; PF07714; PF00017; PF00018	PF08919; F_actin_bind; PF07714; Pkinase_Tyr; PF00017; SH2; PF00018; SH3_1	.	.	hsa04012: ErbB signaling pathway; hsa04014: Ras signaling pathway; hsa04110: Cell cycle; hsa04360: Axon guidance; hsa04722: Neurotrophin signaling pathway; hsa05130: Pathogenic Escherichia coli infection; hsa05200: Pathways in cancer; hsa05206: MicroRNAs in cancer; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05220: Chronic myeloid leukemia; hsa05416: Viral myocarditis	R-HSA-2029482: Regulation of actin dynamics for phagocytic cup formation; R-HSA-428890: Role of ABL in ROBO-SLIT signaling; R-HSA-525793: 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-69231: Cyclin D associated events in G1; R-HSA-8939236: RUNX1 regulates transcription of genes involved in differentiation of HSCs; R-HSA-8940973: RUNX2 regulates osteoblast differentiation; R-HSA-9664422: FCGR3A-mediated phagocytosis; R-HSA-983231: Factors involved in megakaryocyte development and platelet production	.	P00519
TT1A6HL	Tyrosine-protein kinase ABL2 (ABL2)	P42684	ABL2_HUMAN	Kinase	Tyrosine-protein kinase ARG; Abelson-related gene protein; Abelson tyrosine-protein kinase 2; Abelson murine leukemia viral oncogene homolog 2; ARG; ABLL	ABL2	"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."	EC 2.7.10.2	5NP5; 5NP3; 4EIH; 3ULR; 3HMI	MGQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRTTETGFNIFTQHDHFASCVEDGFEGDKTGGSSPEALHRPYGCDVEPQALNEAIRWSSKENLLGATESDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNQNGEWSEVRSKNGQGWVPSNYITPVNSLEKHSWYHGPVSRSAAEYLLSSLINGSFLVRESESSPGQLSISLRYEGRVYHYRINTTADGKVYVTAESRFSTLAELVHHHSTVADGLVTTLHYPAPKCNKPTVYGVSPIHDKWEMERTDITMKHKLGGGQYGEVYVGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTLEPPFYIVTEYMPYGNLLDYLRECNREEVTAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHVVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNTFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYDLLEKGYRMEQPEGCPPKVYELMRACWKWSPADRPSFAETHQAFETMFHDSSISEEVAEELGRAASSSSVVPYLPRLPILPSKTRTLKKQVENKENIEGAQDATENSASSLAPGFIRGAQASSGSPALPRKQRDKSPSSLLEDAKETCFTRDRKGGFFSSFMKKRNAPTPPKRSSSFREMENQPHKKYELTGNFSSVASLQHADGFSFTPAQQEANLVPPKCYGGSFAQRNLCNDDGGGGGGSGTAGGGWSGITGFFTPRLIKKTLGLRAGKPTASDDTSKPFPRSNSTSSMSSGLPEQDRMAMTLPRNCQRSKLQLERTVSTSSQPEENVDRANDMLPKKSEESAAPSRERPKAKLLPRGATALPLRTPSGDLAITEKDPPGVGVAGVAAAPKGKEKNGGARLGMAGVPEDGEQPGWPSPAKAAPVLPTTHNHKVPVLISPTLKHTPADVQLIGTDSQGNKFKLLSEHQVTSSGDKDRPRRVKPKCAPPPPPVMRLLQHPSICSDPTEEPTALTAGQSTSETQEGGKKAALGAVPISGKAGRPVMPPPQVPLPTSSISPAKMANGTAGTKVALRKTKQAAEKISADKISKEALLECADLLSSALTEPVPNSQLVDTGHQLLDYCSGYVDCIPQTRNKFAFREAVSKLELSLQELQVSSAAAGVPGTNPVLNNLLSCVQEISDVVQR	Literature-reported	Rapid discovery of a novel series of Abl kinase inhibitors by application of an integrated microfluidic synthesis and screening platform. J Med Chem. 2013 Apr 11;56(7):3033-47.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. ABL subfamily.	2.7.10.2	Transferring phosphorus-containing groups	F-actin binding; Protein tyrosine kinase; SH2 domain; SH3 domain	PF08919; PF07714; PF00017; PF00018	PF08919; F_actin_bind; PF07714; Pkinase_Tyr; PF00017; SH2; PF00018; SH3_1	.	.	hsa04012: ErbB signaling pathway; hsa04014: Ras signaling pathway; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05416: Viral myocarditis	R-HSA-428890: Role of ABL in ROBO-SLIT signaling; R-HSA-9013149: RAC1 GTPase cycle; R-HSA-9013423: RAC3 GTPase cycle; R-HSA-9706369: Negative regulation of FLT3	.	P42684
TTM3F49	"3-ketoacyl-CoA thiolase, mitochondrial (ACAA2)"	P42765	THIM_HUMAN	.	"Acetyl-CoA acetyltransferase; Acetyl-CoA acyltransferase; Acyl-CoA hydrolase, mitochondrial; Beta-ketothiolase; Mitochondrial 3-oxoacyl-CoA thiolase; T1"	ACAA2	"In the production of energy from fats, this is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA (Probable). Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain unbranched 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms (Probable). Also catalyzes the condensation of two acetyl-CoA molecules into acetoacetyl-CoA and could be involved in the production of ketone bodies (Probable). Also displays hydrolase activity on various fatty acyl-CoAs (PubMed:25478839). Thereby, could be responsible for the production of acetate in a side reaction to beta-oxidation (Probable). Abolishes BNIP3-mediated apoptosis and mitochondrial damage (PubMed:18371312). {ECO:0000269|PubMed:18371312, ECO:0000269|PubMed:25478839, ECO:0000305|PubMed:25478839}."	EC 2.3.1.16; EC 2.3.1.9; EC 3.1.2.-; EC 3.1.2.1; EC 3.1.2.2	4C2J;4C2K	MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA	Clinical trial	"Clinical pipeline report, company report or official report of Imbria Pharmaceuticals"	.	.	.	.	.	.	.	.	.	.	.	hsa:10449	R-HSA-77289;	MetaCyc:HS09539-MONOMER;	P42765;
TTY84UG	Acetyl-CoA carboxylase 2 (ACACB)	O00763	ACACB_HUMAN	Carbon-carbon ligase	Acetyl-Coenzyme A carboxylase beta; Acetyl CoA carboxylase beta; ACCbeta; ACC2; ACC-beta; ACACB	ACACB	"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."	EC 6.4.1.2	5KKN; 4HQ6; 3TDC; 3JRX; 3JRW	MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQRNGEGHTLPKTPSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGTGTQGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSVAGSSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGKRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPISFETPSNPPLARGHVIAARITSENPDEGFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDIMLGVVCGALNVADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIMNGCHIEIDAHRLNDGGLLLSYNGNSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRPGAVLEAGCVVARLELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLPEPVFSIKLKEWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKSVRRVMAQYASNITSVLCQFPSQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSGIRGYMKTVVLDLLRRYLRVEHHFQQAHYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGPDPSLSDELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCVVEFQFMLPSSHPNRMTVPISITNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEDFTRNFDEVISCFANVPKDTPLFSEARTSLYSEDDCKSLREEPIHILNVSIQCADHLEDEALVPILRTFVQSKKNILVDYGLRRITFLIAQEKEFPKFFTFRARDEFAEDRIYRHLEPALAFQLELNRMRNFDLTAVPCANHKMHLYLGAAKVKEGVEVTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGSRLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSFGNKQGPQHGMLINTPYVTKDLLQAKRFQAQTLGTTYIYDFPEMFRQALFKLWGSPDKYPKDILTYTELVLDSQGQLVEMNRLPGGNEVGMVAFKMRFKTQEYPEGRDVIVIGNDITFRIGSFGPGEDLLYLRASEMARAEGIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGFKYLYLTPQDYTRISSLNSVHCKHIEEGGESRYMITDIIGKDDGLGVENLRGSGMIAGESSLAYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVENSHIILTGASALNKVLGREVYTSNNQLGGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDPIDREIEFLPSRAPYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVETRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQAVKDFNREKLPLMIFANWRGFSGGMKDMYDQVLKFGAYIVDGLRQYKQPILIYIPPYAELRGGSWVVIDATINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLIKSMRRIDPAYKKLMEQLGEPDLSDKDRKDLEGRLKAREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARTFLYWRLRRLLLEDQVKQEILQASGELSHVHIQSMLRRWFVETEGAVKAYLWDNNQVVVQWLEQHWQAGDGPRSTIRENITYLKHDSVLKTIRGLVEENPEVAVDCVIYLSQHISPAERAQVVHLLSTMDSPAST	Successful	AMP-activated protein kinase-dependent and -independent mechanisms underlying in vitro antiglioma action of compound C. Biochem Pharmacol. 2009 Jun 1;77(11):1684-93.	34	.	.	.	.	.	.	.	.	.	.	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	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)	MetaCyc:HS01211-MON	O00763
TTK3C21	Acetoacetyl-CoA thiolase (ACAT1)	P24752	THIL_HUMAN	Acyltransferase	"T2; MAT; Acetyl-CoA acetyltransferase, mitochondrial"	ACAT1	Plays a major role in ketone body metabolism.	EC 2.3.1.9	2IBY; 2IBW; 2IBU; 2IB9; 2IB8	MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	EC:2.3	Acyltransferase	thiolase-like superfamily. Thiolase family.	2.3.1.9	Acyltransferases	"Thiolase, C-terminal domain; Thiolase, N-terminal domain"	PF02803; PF00108	PF02803; Thiolase_C; PF00108; Thiolase_N	.	.	"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"	R-HSA-70895: Branched-chain amino acid catabolism; R-HSA-77108: Utilization of Ketone Bodies; R-HSA-77111: Synthesis of Ketone Bodies	MetaCyc:HS01167-MON	P24752
TTUI5H7	Angiotensin-converting enzyme 2 (ACE2)	Q9BYF1	ACE2_HUMAN	Peptidase	Processed angiotensinconverting enzyme 2; Metalloprotease MPROT15; Angiotensinconverting enzyme homolog; Angiotensinconverting enzyme 2; ACErelated carboxypeptidase; ACEH; ACE2	ACE2	"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."	EC 3.4.17.23	6CS2; 6ACK; 6ACJ; 6ACG; 3SCL	MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENPYASIDISKGENNPGFQNTDDVQTSF	Clinical trial	New Developments in the Pharmacological Treatment of Hypertension: Dead-End or a Glimmer at the Horizon . Curr Hypertens Rep. 2015; 17(6): 42.	21	.	.	.	.	.	.	.	.	.	.	hsa04614:Renin-angiotensin system; hsa04974:Protein digestion and absorption	R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins	.	Q9BYF1
TTYRG7F	HUMAN angiotensin-converting enzyme 2 (ACE2)	Q9BYF1	ACE2_HUMAN	Peptidase	Processed angiotensinconverting enzyme 2; Metalloprotease MPROT15; Angiotensinconverting enzyme homolog; Angiotensinconverting enzyme 2; ACErelated carboxypeptidase; ACEH; ACE2	ACE2	"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."	EC 3.4.17.23	6CS2; 6ACK; 6ACJ; 6ACG; 3SCL	MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENPYASIDISKGENNPGFQNTDDVQTSF	.	Coronaviruses - drug discovery and therapeutic options. Nat Rev Drug Discov. 2016 May;15(5):327-47.	21	.	.	.	.	.	.	.	.	.	.	hsa04614: Renin-angiotensin system; hsa04974: Protein digestion and absorption; hsa05171: Coronavirus disease - COVID-19	R-HSA-2022377: Metabolism of Angiotensinogen to Angiotensins; R-HSA-9678110: Attachment and Entry; R-HSA-9679191: Potential therapeutics for SARS; R-HSA-9694614: Attachment and Entry	.	Q9BYF1
TT1RS9F	Acetylcholinesterase (AChE)	P22303	ACES_HUMAN	Carboxylic ester hydrolase	YT; N-ACHE; ARACHE	ACHE	Role in neuronal apoptosis. Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.	EC 3.1.1.7	6O69; 6F25; 6CQZ; 6CQY; 6CQX	MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL	Successful	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2465).	34	EC:3.1.1	Carboxylic ester hydrolase	type-B carboxylesterase/lipase family.	3.1.1.7	Acting on ester bonds	Acetylcholinesterase tetramerisation domain; Carboxylesterase family	PF08674; PF00135	PF08674; AChE_tetra; PF00135; COesterase	.	.	hsa00564:Glycerophospholipid metabolism; hsa04725:Cholinergic synapse	"R-HSA-112311: Neurotransmitter clearance; R-HSA-1483191: Synthesis of PC; R-HSA-422085: Synthesis, secretion, and deacylation of Ghrelin"	.	P22303
TTKY2NS	Duffy antigen chemokine receptor (ACKR1)	Q16570	ACKR1_HUMAN	GPCR duffy	Plasmodium vivax receptor; GpFy; Glycoprotein D; Fy glycoprotein; Duffy antigen/chemokine receptor; DARC; CD234; ACKR1	ACKR1	"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."	.	4NUV; 4NUU	MGNCLHRAELSPSTENSSQLDFEDVWNSSYGVNDSFPDGDYGANLEAAAPCHSCNLLDDSALPFFILTSVLGILASSTVLFMLFRPLFRWQLCPGWPVLAQLAVGSALFSIVVPVLAPGLGSTRSSALCSLGYCVWYGSAFAQALLLGCHASLGHRLGAGQVPGLTLGLTVGIWGVAALLTLPVTLASGASGGLCTLIYSTELKALQATHTVACLAIFVLLPLGLFGAKGLKKALGMGPGPWMNILWAWFIFWWPHGVVLGLDFLVRSKLLLLSTCLAQQALDLLLNLAEALAILHCVATPLLLALFCHQATRTLLPSLPLPEGWSSHLDTLGSKS	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	hsa05144: Malaria	R-HSA-375276: Peptide ligand-binding receptors	.	Q16570
TTRQJTC	C-X-C chemokine receptor type 7 (ACKR3)	P25106	ACKR3_HUMAN	GPCR rhodopsin	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	ACKR3	"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."	.	.	MDLHLFDYSEPGNFSDISWPCNSSDCIVVDTVMCPNMPNKSVLLYTLSFIYIFIFVIGMIANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVLTIPVWVVSLVQHNQWPMGELTCKVTHLIFSINLFGSIFFLTCMSVDRYLSITYFTNTPSSRKKMVRRVVCILVWLLAFCVSLPDTYYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVVLGFAVPFSIIAVFYFLLARAISASSDQEKHSSRKIIFSYVVVFLVCWLPYHVAVLLDIFSILHYIPFTCRLEHALFTALHVTQCLSLVHCCVNPVLYSFINRNYRYELMKAFIFKYSAKTGLTKLIDASRVSETEYSALEQSTK	Preclinical	"Safety and efficacy of an oral CCR3 antagonist in patients with asthma and eosinophilic bronchitis: a randomized, placebo-controlled clinical trial. Clin Exp Allergy. 2014 Apr;44(4):508-16."	5	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family. Atypical chemokine receptor subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060:Cytokine-cytokine receptor interaction	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P25106
TT0Z6Y2	ATP-citrate synthase (ACLY)	P53396	ACLY_HUMAN	Acyltransferase	Citrate cleavage enzyme; ATP-citrate (pro-S-)-lyase; ACL	ACLY	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.	EC 2.3.3.8	6QFB; 6O0H; 6HXM; 6HXL; 6HXK	MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALGHRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVPSPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHMSM	Successful	The biology and chemistry of hyperlipidemia. Bioorg Med Chem. 2007 Jul 15;15(14):4674-99.	0	EC:2.3	Acyltransferase	.	2.3.3.8	Acyltransferases	"ATP citrate lyase citrate-binding; Citrate synthase, C-terminal domain; CoA binding domain; CoA-ligase"	PF16114; PF00285; PF02629; PF00549	PF16114; Citrate_bind; PF00285; Citrate_synt; PF02629; CoA_binding; PF00549; Ligase_CoA	.	.	hsa00020:Citrate cycle (TCA cycle); hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics	R-HSA-163765:ChREBP activates metabolic gene expression; R-HSA-75105:Fatty Acyl-CoA Biosynthesis	MetaCyc:HS05535-MON	P53396
TTMTF2P	Citrate hydro-lyase (ACO2)	Q99798	ACON_HUMAN	Alpha-carbonic anhydrase	Aconitase; ACO2	ACO2	Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.	EC 4.2.1.3	.	MAPYSLLVTRLQKALGVRQYHVASVLCQRAKVAMSHFEPNEYIHYDLLEKNINIVRKRLNRPLTLSEKIVYGHLDDPASQEIERGKSYLRLRPDRVAMQDATAQMAMLQFISSGLSKVAVPSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGREDIANLADEFKDHLVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGKVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFNPETDYLTGTDGKKFRLEAPDADELPKGEFDPGQDTYQHPPKDSSGQHVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFTPGKPLKCIIKHPNGTQETILLNHTFNETQIEWFRAGSALNRMKELQQ	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	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	R-HSA-1268020:Mitochondrial protein import	MetaCyc:HS02077-MON	Q99798
TTBRZQS	Prostatic acid phosphatase (ACPP)	P15309	PPAP_HUMAN	.	Thiamine monophosphatase; TMPase; PAP	ACPP	"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."	EC 3.1.3.2	3PPD; 2MG0; 2L79; 2L77; 2L3H	MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKRLHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELVGPVIPQDWSTECMTTNSHQGTEDSTD	Clinical trial	Company report (Madisonvaccine)	21	.	.	.	.	.	.	.	.	.	.	.	R-HSA-6798695: Neutrophil degranulation	.	P15309
TTAHE2N	Acrosin (ACR)	P10323	ACRO_HUMAN	.	ACRS	ACR	"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."	EC 3.4.21.10	.	MVEMLPTAILLVLAVSVVAKDNATCDGPCGLRFRQNPQGGVRIVGGKAAQHGAWPWMVSLQIFTYNSHRYHTCGGSLLNSRWVLTAAHCFVGKNNVHDWRLVFGAKEITYGNNKPVKAPLQERYVEKIIIHEKYNSATEGNDIALVEITPPISCGRFIGPGCLPHFKAGLPRGSQSCWVAGWGYIEEKAPRPSSILMEARVDLIDLDLCNSTQWYNGRVQPTNVCAGYPVGKIDTCQGDSGGPLMCKDSKESAYVVVGITSWGVGCARAKRPGIYTATWPYLNWIASKIGSNALRMIQSATPPPPTTRPPPIRPPFSHPISAHLPWYFQPPPRPLPPRPPAAQPRPPPSPPPPPPPPASPLPPPPPPPPPTPSSTTKLPQGLSFAKRLQQLIEVLKGKTYSDGKNHYDMETTELPELTSTS	Literature-reported	Synthesis and inhibition of human acrosin and trypsin and acute toxicity of aryl 4-guanidinobenzoates. J Med Chem. 1986 Apr;29(4):514-9.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1300645: Acrosome Reaction and Sperm:Oocyte Membrane Binding	.	P10323
TTGAZF9	Gamma-actin (ACTG)	P63261	ACTG_HUMAN	.	"Actin, cytoplasmic 2; ACTG"	ACTG1	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.	.	6G2T; 6CXJ; 6CXI; 5JLH	MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF	Literature-reported	Cross-reacting material 197 (CRM197) affects actin cytoskeleton of endothelial cells. Gen Physiol Biophys. 2017 Oct;36(4):383-389.	.	.	.	.	.	.	.	.	.	.	.	hsa04015: Rap1 signaling pathway; hsa04145: Phagosome; hsa04210: Apoptosis; hsa04390: Hippo signaling pathway; hsa04510: Focal adhesion; hsa04520: Adherens junction; hsa04530: Tight junction; hsa04611: Platelet activation; hsa04613: Neutrophil extracellular trap formation; hsa04670: Leukocyte transendothelial migration; hsa04714: Thermogenesis; hsa04810: Regulation of actin cytoskeleton; hsa04919: Thyroid hormone signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04971: Gastric acid secretion; hsa05014: Amyotrophic lateral sclerosis; hsa05100: Bacterial invasion of epithelial cells; hsa05110: Vibrio cholerae infection; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05135: Yersinia infection; hsa05164: Influenza A; hsa05205: Proteoglycans in cancer; hsa05225: Hepatocellular carcinoma; hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy; hsa05416: Viral myocarditis; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-1445148: Translocation of SLC2A4 (GLUT4) to the plasma membrane; R-HSA-190873: Gap junction degradation; R-HSA-196025: Formation of annular gap junctions; R-HSA-2029482: Regulation of actin dynamics for phagocytic cup formation; R-HSA-3928662: EPHB-mediated forward signaling; R-HSA-3928665: EPH-ephrin mediated repulsion of cells; R-HSA-418990: Adherens junctions interactions; R-HSA-437239: Recycling pathway of L1; R-HSA-4420097: VEGFA-VEGFR2 Pathway; R-HSA-445095: Interaction between L1 and Ankyrins; R-HSA-446353: Cell-extracellular matrix interactions; R-HSA-5626467: RHO GTPases activate IQGAPs; R-HSA-5663213: RHO GTPases Activate WASPs and WAVEs; R-HSA-5663220: RHO GTPases Activate Formins; R-HSA-5674135: MAP2K and MAPK activation; R-HSA-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-8856828: Clathrin-mediated endocytosis; R-HSA-9013418: RHOBTB2 GTPase cycle; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants; R-HSA-9662360: Sensory processing of sound by inner hair cells of the cochlea; R-HSA-9662361: Sensory processing of sound by outer hair cells of the cochlea; R-HSA-9664422: FCGR3A-mediated phagocytosis	.	P63261
TTJNBQA	Activin receptor-like kinase 2 (ALK-2)	Q04771	ACVR1_HUMAN	Kinase	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	ACVR1	"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."	EC 2.7.11.30	6GIP; 6GIN; 6GI6; 6EIX; 6ACR	MVDGVMILPVLIMIALPSPSMEDEKPKVNPKLYMCVCEGLSCGNEDHCEGQQCFSSLSINDGFHVYQKGCFQVYEQGKMTCKTPPSPGQAVECCQGDWCNRNITAQLPTKGKSFPGTQNFHLEVGLIILSVVFAVCLLACLLGVALRKFKRRNQERLNPRDVEYGTIEGLITTNVGDSTLADLLDHSCTSGSGSGLPFLVQRTVARQITLLECVGKGRYGEVWRGSWQGENVAVKIFSSRDEKSWFRETELYNTVMLRHENILGFIASDMTSRHSSTQLWLITHYHEMGSLYDYLQLTTLDTVSCLRIVLSIASGLAHLHIEIFGTQGKPAIAHRDLKSKNILVKKNGQCCIADLGLAVMHSQSTNQLDVGNNPRVGTKRYMAPEVLDETIQVDCFDSYKRVDIWAFGLVLWEVARRMVSNGIVEDYKPPFYDVVPNDPSFEDMRKVVCVDQQRPNIPNRWFSDPTLTSLAKLMKECWYQNPSARLTALRIKKTLTKIDNSLDKLKTDC	Clinical trial	"Inhibitors of JAK-family kinases: an update on the patent literature 2013-2015, part 2.Expert Opin Ther Pat. 2017 Feb;27(2):145-161."	15.5	EC:2.7	.	protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.	2.7.11.30	Transferring phosphorus-containing groups	Activin types I and II receptor domain; Protein tyrosine kinase; Transforming growth factor beta type I GS-motif	PF01064; PF07714; PF08515	PF01064; Activin_recp; PF07714; Pkinase_Tyr; PF08515; TGF_beta_GS	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04350: TGF-beta signaling pathway; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa05418: Fluid shear stress and atherosclerosis	.	.	Q04771
TTPKHTZ	Activin receptor type IB (ACVR1B)	P36896	ACV1B_HUMAN	Kinase	Serine/threonine-protein kinase receptor R2; SKR2; Activin receptor-like kinase 4; Activin receptor type-1B; ALK4; ALK-4; ACVRLK4; ACTR-IB	ACVR1B	"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)."	EC 2.7.11.30	.	MAESAGASSFFPLVVLLLAGSGGSGPRGVQALLCACTSCLQANYTCETDGACMVSIFNLDGMEHHVRTCIPKVELVPAGKPFYCLSSEDLRNTHCCYTDYCNRIDLRVPSGHLKEPEHPSMWGPVELVGIIAGPVFLLFLIIIIVFLVINYHQRVYHNRQRLDMEDPSCEMCLSKDKTLQDLVYDLSTSGSGSGLPLFVQRTVARTIVLQEIIGKGRFGEVWRGRWRGGDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTIEGMIKLALSAASGLAHLHMEIVGTQGKPGIAHRDLKSKNILVKKNGMCAIADLGLAVRHDAVTDTIDIAPNQRVGTKRYMAPEVLDETINMKHFDSFKCADIYALGLVYWEIARRCNSGGVHEEYQLPYYDLVPSDPSIEEMRKVVCDQKLRPNIPNWWQSYEALRVMGKMMRECWYANGAARLTALRIKKTLSQLSVQEDVKI	Patented-recorded	Synthesis and structure-activity relationships of a novel and selective bone morphogenetic protein receptor (BMP) inhibitor derived from the pyrazolo[1.5-a]pyrimidine scaffold of dorsomorphin: the discovery of ML347 as an ALK2 versus ALK3 selective MLPCN probe. Bioorg Med Chem Lett. 2013 Jun 1;23(11):3248-52.	0	EC:2.7	.	protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.	2.7.11.30	Transferring phosphorus-containing groups	Activin types I and II receptor domain; Protein kinase domain; Transforming growth factor beta type I GS-motif	PF01064; PF00069; PF08515	PF01064; Activin_recp; PF00069; Pkinase; PF08515; TGF_beta_GS	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04350: TGF-beta signaling pathway; hsa04550: Signaling pathways regulating pluripotency of stem cells	R-HSA-1181150: Signaling by NODAL; R-HSA-1433617: Regulation of signaling by NODAL; R-HSA-1502540: Signaling by Activin	.	P36896
TTX2DRI	Activin receptor type IIA (ACVR2A)	P27037	AVR2A_HUMAN	Kinase	Activin receptor type2A; Activin receptor type-2A; ACVR2; ACTRIIA; ACTR-IIA	ACVR2A	"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."	EC 2.7.11.30	5NH3; 4ASX; 3SOC; 3Q4T	MGAAAKLAFAVFLISCSSGAILGRSETQECLFFNANWEKDRTNQTGVEPCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCVEKKDSPEVYFCCCEGNMCNEKFSYFPEMEVTQPTSNPVTPKPPYYNILLYSLVPLMLIAGIVICAFWVYRHHKMAYPPVLVPTQDPGPPPPSPLLGLKPLQLLEVKARGRFGCVWKAQLLNEYVAVKIFPIQDKQSWQNEYEVYSLPGMKHENILQFIGAEKRGTSVDVDLWLITAFHEKGSLSDFLKANVVSWNELCHIAETMARGLAYLHEDIPGLKDGHKPAISHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELASRCTAADGPVDEYMLPFEEEIGQHPSLEDMQEVVVHKKKRPVLRDYWQKHAGMAMLCETIEECWDHDAEARLSAGCVGERITQMQRLTNIITTEDIVTVVTMVTNVDFPPKESSL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	EC:2.7	Kinase	protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.	2.7.11.30	Transferring phosphorus-containing groups	Activin types I and II receptor domain; Protein kinase domain	PF01064; PF00069	PF01064; Activin_recp; PF00069; Pkinase	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04350: TGF-beta signaling pathway; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-1181150: Signaling by NODAL; R-HSA-1433617: Regulation of signaling by NODAL; R-HSA-1502540: Signaling by Activin; R-HSA-201451: Signaling by BMP	.	P27037
TTLFRKS	Activin receptor type IIB (ACVR2B)	Q13705	AVR2B_HUMAN	Kinase	Activin receptor type2B; Activin receptor type-2B; ACTRIIB; ACTR-IIB	ACVR2B	"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)."	EC 2.7.11.30	5NHR; 5NGV; 4FAO; 2QLU; 2H62	MTAPWVALALLWGSLCAGSGRGEAETRECIYYNANWELERTNQSGLERCEGEQDKRLHCYASWRNSSGTIELVKKGCWLDDFNCYDRQECVATEENPQVYFCCCEGNFCNERFTHLPEAGGPEVTYEPPPTAPTLLTVLAYSLLPIGGLSLIVLLAFWMYRHRKPPYGHVDIHEDPGPPPPSPLVGLKPLQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSYLHEDVPWCRGEGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEELQEVVVHKKMRPTIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERVSLIRRSVNGTTSDCLVSLVTSVTNVDLPPKESSI	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1792).	0	EC:2.7	Kinase	protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.	2.7.11.30	Transferring phosphorus-containing groups	Activin types I and II receptor domain; Protein kinase domain	PF01064; PF00069	PF01064; Activin_recp; PF00069; Pkinase	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04350:TGF-beta signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells	R-HSA-1433617:Regulation of signaling by NODAL	.	Q13705
TTGYPTC	Activin receptor-like kinase-1 (ACVRL1)	P37023	ACVL1_HUMAN	Kinase	Serine/threonine-protein kinase receptor R3; SKR3; Activin receptor-like kinase 1; ALK-1; ACVRLK1; ACVRL1	ACVRL1	"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."	EC 2.7.11.30	4FAO; 3MY0; 2LCR	MTLGSPRKGLLMLLMALVTQGDPVKPSRGPLVTCTCESPHCKGPTCRGAWCTVVLVREEGRHPQEHRGCGNLHRELCRGRPTEFVNHYCCDSHLCNHNVSLVLEATQPPSEQPGTDGQLALILGPVLALLALVALGVLGLWHVRRRQEKQRGLHSELGESSLILKASEQGDSMLGDLLDSDCTTGSGSGLPFLVQRTVARQVALVECVGKGRYGEVWRGLWHGESVAVKIFSSRDEQSWFRETEIYNTVLLRHDNILGFIASDMTSRNSSTQLWLITHYHEHGSLYDFLQRQTLEPHLALRLAVSAACGLAHLHVEIFGTQGKPAIAHRDFKSRNVLVKSNLQCCIADLGLAVMHSQGSDYLDIGNNPRVGTKRYMAPEVLDEQIRTDCFESYKWTDIWAFGLVLWEIARRTIVNGIVEDYRPPFYDVVPNDPSFEDMKKVVCVDQQTPTIPNRLAADPVLSGLAQMMRECWYPNPSARLTALRIKKTLQKISNSPEKPKVIQ	Clinical trial	ALK1 as an emerging target for antiangiogenic therapy of cancer. Blood. 2011 June 30; 117(26): 6999-7006.	21	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction	R-HSA-201451: Signaling by BMP	.	P37023
TTLP57V	Adenosine deaminase (ADA)	P00813	ADA_HUMAN	Carbon-nitrogen hydrolase	Adenosine aminohydrolase; ADA1	ADA	"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."	EC 3.5.4.4	3IAR; 1M7M	MAQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPDFLAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAIDLAGDETIPGSSLLPGHVQAYQEAVKSGIHRTVHAGEVGSAEVVKEAVDILKTERLGHGYHTLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIFKSTLDTDYQMTKRDMGFTEEEFKRLNINAAKSSFLPEDEKRELLDLLYKAYGMPPSASAGQNL	Successful	Cladribine: from the bench to the bedside--focus on hairy cell leukemia. Expert Rev Anticancer Ther. 2004 Oct;4(5):745-57.	34	EC:3.5	Carbon-nitrogen hydrolase	metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family.	3.5.4.4 	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Adenosine/AMP deaminase	PF00962	PF00962; A_deaminase	.	.	hsa00230:Purine metabolism; hsa01100:Metabolic pathways; hsa05340:Primary immunodeficiency	R-HSA-74217:Purine salvage	MetaCyc:HS02191-MON	P00813
TTVXEGU	ADAM10 messenger RNA (ADAM10 mRNA)	O14672	ADA10_HUMAN	mRNA target	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)	ADAM10	"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."	EC 3.4.24.81	6BE6; 6BDZ; 1M1I	MVLLRVLILLLSWAAGMGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHEDQFLRLDFHAHGRHFNLRMKRDTSLFSDEFKVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVIDGRFEGFIQTRGGTFYVEPAERYIKDRTLPFHSVIYHEDDINYPHKYGPQGGCADHSVFERMRKYQMTGVEEVTQIPQEEHAANGPELLRKKRTTSAEKNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTADEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDECCFDANQPEGRKCKLKPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAREGICNGFTALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYGLEECTCASSDGKDDKELCHVCCMKKMDPSTCASTGSVQWSRHFSGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPELYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQQPQRQRPRESYQMGHMRR	Literature-reported	Conversion of an MMP-potent scaffold to an MMP-selective HER-2 sheddase inhibitor via scaffold hybridization and subtle P1' permutations. Bioorg Med Chem Lett. 2008 Jan 15;18(2):560-4.	0	mRNA	mRNA target	.	.	.	Disintegrin; Reprolysin family propeptide	PF00200; PF01562	PF00200; Disintegrin; PF01562; Pep_M12B_propep	.	.	hsa05010:Alzheimer's disease; hsa05120:Epithelial cell signaling in Helicobacter pylori infection	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	MetaCyc:ENSG00000137845-MON	O14672
TTOMWSY	Mammalian disintegrin-metalloprotease (ADAM10)	O14672	ADA10_HUMAN	Peptidase	Mammalian disintegrinmetalloprotease; MADM; Kuzbanian protein homolog; KUZ; Disintegrin and metalloproteinase domaincontaining protein 10; Disintegrin and metalloproteinase domain-containing protein 10; CDw156; CD156c; ADAM 10	ADAM10	"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."	EC 3.4.24.81	6BE6; 6BDZ; 1M1I	MVLLRVLILLLSWAAGMGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHEDQFLRLDFHAHGRHFNLRMKRDTSLFSDEFKVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVIDGRFEGFIQTRGGTFYVEPAERYIKDRTLPFHSVIYHEDDINYPHKYGPQGGCADHSVFERMRKYQMTGVEEVTQIPQEEHAANGPELLRKKRTTSAEKNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTADEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDECCFDANQPEGRKCKLKPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAREGICNGFTALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYGLEECTCASSDGKDDKELCHVCCMKKMDPSTCASTGSVQWSRHFSGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPELYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQQPQRQRPRESYQMGHMRR	Clinical trial	Company report (Incyte)	19	EC:3.4	Peptidase	.	3.4.24.81 	Acting on peptide bonds (peptidases)	Disintegrin; Reprolysin family propeptide	PF00200; PF01562	PF00200; Disintegrin; PF01562; Pep_M12B_propep	8.A.77.1.4	The Sheddase (Sheddase) Family	hsa05010:Alzheimer's disease; hsa05120:Epithelial cell signaling in Helicobacter pylori infection	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	MetaCyc:ENSG00000137845-MON	O14672
TT6AZXG	TNF alpha converting enzyme (ADAM17)	P78536	ADA17_HUMAN	Peptidase	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	ADAM17	"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."	EC 3.4.24.86	3O64; 3LGP; 3LEA; 3LE9; 3L0V	MRQSLLFLTSVVPFVLAPRPPDDPGFGPHQRLEKLDSLLSDYDILSLSNIQQHSVRKRDLQTSTHVETLLTFSALKRHFKLYLTSSTERFSQNFKVVVVDGKNESEYTVKWQDFFTGHVVGEPDSRVLAHIRDDDVIIRINTDGAEYNIEPLWRFVNDTKDKRMLVYKSEDIKNVSRLQSPKVCGYLKVDNEELLPKGLVDREPPEELVHRVKRRADPDPMKNTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNMAKSYPNEEKDAWDVKMLLEQFSFDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGLAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTIESKAQECFQERSNKVCGNSRVDEGEECDPGIMYLNNDTCCNSDCTLKEGVQCSDRNSPCCKNCQFETAQKKCQEAINATCKGVSYCTGNSSECPPPGNAEDDTVCLDLGKCKDGKCIPFCEREQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCEKRVQDVIERFWDFIDQLSINTFGKFLADNIVGSVLVFSLIFWIPFSILVHCVDKKLDKQYESLSLFHPSNVEMLSSMDSASVRIIKPFPAPQTPGRLQPAPVIPSAPAAPKLDHQRMDTIQEDPSTDSHMDEDGFEKDPFPNSSTAAKSFEDLTDHPVTRSEKAASFKLQRQNRVDSKETEC	Clinical trial	Acetylenic TACE inhibitors. Part 3: Thiomorpholine sulfonamide hydroxamates. Bioorg Med Chem Lett. 2006 Mar 15;16(6):1605-9.	21	EC:3.4	Peptidase	.	3.4.24.86 	Acting on peptide bonds (peptidases)	"Membrane-proximal domain, switch, for ADAM17; Disintegrin; Reprolysin family propeptide"	PF16698; PF00200; PF01562	PF16698; ADAM17_MPD; PF00200; Disintegrin; PF01562; Pep_M12B_propep	8.A.77.1.2	The Sheddase (Sheddase) Family	hsa04330:Notch signaling pathway; hsa05010:Alzheimer's disease; hsa05120:Epithelial cell signaling in Helicobacter pylori infection	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	.	P78536
TT4OLB0	A disintegrin and metalloproteinase (ADAM)	Q99965; Q9H2U9	ADAM2_HUMAN; ADAM7_HUMAN	Peptidase	Disintegrin and metalloproteinase domain-containing protein; ADAM	ADAM2	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. 	.	.	MWRVLFLLSGLGGLRMDSNFDSLPVQITVPEKIRSIIKEGIESQASYKIVIEGKPYTVNLMQKNFLPHNFRVYSYSGTGIMKPLDQDFQNFCHYQGYIEGYPKSVVMVSTCTGLRGVLQFENVSYGIEPLESSVGFEHVIYQVKHKKADVSLYNEKDIESRDLSFKLQSVEPQQDFAKYIEMHVIVEKQLYNHMGSDTTVVAQKVFQLIGLTNAIFVSFNITIILSSLELWIDENKIATTGEANELLHTFLRWKTSYLVLRPHDVAFLLVYREKSNYVGATFQGKMCDANYAGGVVLHPRTISLESLAVILAQLLSLSMGITYDDINKCQCSGAVCIMNPEAIHFSGVKIFSNCSFEDFAHFISKQKSQCLHNQPRLDPFFKQQAVCGNAKLEAGEECDCGTEQDCALIGETCCDIATCRFKAGSNCAEGPCCENCLFMSKERMCRPSFEECDLPEYCNGSSASCPENHYVQTGHPCGLNQWICIDGVCMSGDKQCTDTFGKEVEFGPSECYSHLNSKTDVSGNCGISDSGYTQCEADNLQCGKLICKYVGKFLLQIPRATIIYANISGHLCIAVEFASDHADSQKMWIKDGTSCGSNKVCRNQRCVSSSYLGYDCTTDKCNDRGVCNNKKHCHCSASYLPPDCSVQSDLWPGGSIDSGNFPPVAIPARLPERRYIENIYHSKPMRWPFFLFIPFFIIFCVLIAIMVKVNFQRKKWRTEDYSSDEQPESESEPKG	Literature-reported	A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions. Toxins (Basel). 2016 Apr 23;8(4):122.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2534343: Interaction With Cumulus Cells And The Zona Pellucida	.	Q99965
TTAJDQY	ADAM metallopeptidase 30 (ADAM30)	Q9UKF2	ADA30_HUMAN	Peptidase	Disintegrin and metalloproteinase domaincontaining protein 30; ADAM30	ADAM30	May be involved in spermatogenesis and fertilization.	EC 3.4.24.-	.	MRSVQIFLSQCRLLLLLVPTMLLKSLGEDVIFHPEGEFDSYEVTIPEKLSFRGEVQGVVSPVSYLLQLKGKKHVLHLWPKRLLLPRHLRVFSFTEHGELLEDHPYIPKDCNYMGSVKESLDSKATISTCMGGLRGVFNIDAKHYQIEPLKASPSFEHVVYLLKKEQFGNQVCGLSDDEIEWQMAPYENKARLRDFPGSYKHPKYLELILLFDQSRYRFVNNNLSQVIHDAILLTGIMDTYFQDVRMRIHLKALEVWTDFNKIRVGYPELAEVLGRFVIYKKSVLNARLSSDWAHLYLQRKYNDALAWSFGKVCSLEYAGSVSTLLDTNILAPATWSAHELGHAVGMSHDEQYCQCRGRLNCIMGSGRTGFSNCSYISFFKHISSGATCLNNIPGLGYVLKRCGNKIVEDNEECDCGSTEECQKDRCCQSNCKLQPGANCSIGLCCHDCRFRPSGYVCRQEGNECDLAEYCDGNSSSCPNDVYKQDGTPCKYEGRCFRKGCRSRYMQCQSIFGPDAMEAPSECYDAVNLIGDQFGNCEITGIRNFKKCESANSICGRLQCINVETIPDLPEHTTIISTHLQAENLMCWGTGYHLSMKPMGIPDLGMINDGTSCGEGRVCFKKNCVNSSVLQFDCLPEKCNTRGVCNNRKNCHCMYGWAPPFCEEVGYGGSIDSGPPGLLRGAIPSSIWVVSIIMFRLILLILSVVFVFFRQVIGNHLKPKQEKMPLSKAKTEQEESKTKTVQEESKTKTGQEESEAKTGQEESKAKTGQEESKANIESKRPKAKSVKKQKK	Literature-reported	ADAM30 Downregulates APP-Linked Defects Through Cathepsin D Activation in Alzheimer's Disease. EBioMedicine. 2016 Jul;9:278-292.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2534343: Interaction With Cumulus Cells And The Zona Pellucida	.	Q9UKF2
TTQICM2	ADAM metallopeptidase 33 (ADAM33)	Q9BZ11	ADA33_HUMAN	Peptidase	UNQ873/PRO1891; Disintegrin and metalloproteinase domain-containing protein 33; C20orf153; ADAM 33	ADAM33	"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."	EC 3.4.24.-	1R55; 1R54	MGWRPRRARGTPLLLLLLLLLLWPVPGAGVLQGHIPGQPVTPHWVLDGQPWRTVSLEEPVSKPDMGLVALEAEGQELLLELEKNHRLLAPGYIETHYGPDGQPVVLAPNHTDHCHYQGRVRGFPDSWVVLCTCSGMSGLITLSRNASYYLRPWPPRGSKDFSTHEIFRMEQLLTWKGTCGHRDPGNKAGMTSLPGGPQSRGRREARRTRKYLELYIVADHTLFLTRHRNLNHTKQRLLEVANYVDQLLRTLDIQVALTGLEVWTERDRSRVTQDANATLWAFLQWRRGLWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPDGCCVEAAAESGGCVMAAATGHPFPRVFSACSRRQLRAFFRKGGGACLSNAPDPGLPVPPALCGNGFVEAGEECDCGPGQECRDLCCFAHNCSLRPGAQCAHGDCCVRCLLKPAGALCRQAMGDCDLPEFCTGTSSHCPPDVYLLDGSPCARGSGYCWDGACPTLEQQCQQLWGPGSHPAPEACFQVVNSAGDAHGNCGQDSEGHFLPCAGRDALCGKLQCQGGKPSLLAPHMVPVDSTVHLDGQEVTCRGALALPSAQLDLLGLGLVEPGTQCGPRMVCQSRRCRKNAFQELQRCLTACHSHGVCNSNHNCHCAPGWAPPFCDKPGFGGSMDSGPVQAENHDTFLLAMLLSVLLPLLPGAGLAWCCYRLPGAHLQRCSWGCRRDPACSGPKDGPHRDHPLGGVHPMELGPTATGQPWPLDPENSHEPSSHPEKPLPAVSPDPQADQVQMPRSCLW	Patented-recorded	Specific targeting of metzincin family members with small-molecule inhibitors: progress toward a multifarious challenge. Bioorg Med Chem. 2008 Oct 1;16(19):8781-94.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9BZ11
TTQWYMD	Cell surface antigen MS2 (ADAM8)	P78325	ADAM8_HUMAN	Peptidase	CD156a antigen; CD156; ADAM8; A disintegrin and metalloproteinase domain 8	ADAM8	Possible involvement in extravasation of leukocytes.	EC 3.4.24.-	4DD8	MRGLGLWLLGAMMLPAIAPSRPWALMEQYEVVLPWRLPGPRVRRALPSHLGLHPERVSYVLGATGHNFTLHLRKNRDLLGSGYTETYTAANGSEVTEQPRGQDHCFYQGHVEGYPDSAASLSTCAGLRGFFQVGSDLHLIEPLDEGGEGGRHAVYQAEHLLQTAGTCGVSDDSLGSLLGPRTAAVFRPRPGDSLPSRETRYVELYVVVDNAEFQMLGSEAAVRHRVLEVVNHVDKLYQKLNFRVVLVGLEIWNSQDRFHVSPDPSVTLENLLTWQARQRTRRHLHDNVQLITGVDFTGTTVGFARVSAMCSHSSGAVNQDHSKNPVGVACTMAHEMGHNLGMDHDENVQGCRCQERFEAGRCIMAGSIGSSFPRMFSDCSQAYLESFLERPQSVCLANAPDLSHLVGGPVCGNLFVERGEQCDCGPPEDCRNRCCNSTTCQLAEGAQCAHGTCCQECKVKPAGELCRPKKDMCDLEEFCDGRHPECPEDAFQENGTPCSGGYCYNGACPTLAQQCQAFWGPGGQAAEESCFSYDILPGCKASRYRADMCGVLQCKGGQQPLGRAICIVDVCHALTTEDGTAYEPVPEGTRCGPEKVCWKGRCQDLHVYRSSNCSAQCHNHGVCNHKQECHCHAGWAPPHCAKLLTEVHAASGSLPVFVVVVLVLLAVVLVTLAGIIVYRKARSRILSRNVAPKTTMGRSNPLFHQAASRVPAKGGAPAPSRGPQELVPTTHPGQPARHPASSVALKRPPPAPPVTVSSPPFPVPVYTRQAPKQVIKPTFAPPVPPVKPGAGAANPGPAEGAVGPKVALKPPIQRKQGAGAPTAP	Literature-reported	"Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23. J Biol Chem. 2003 Aug 15;278(33):30469-77."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1474228: Degradation of the extracellular matrix; R-HSA-6798695: Neutrophil degranulation	.	P78325
TTTYQNS	Cellular disintegrin-related protein (ADAM9)	Q13443	ADAM9_HUMAN	.	ADAM 9; Cellular disintegrin-related protein; Meltrin-gamma; Metalloprotease/disintegrin/cysteine-rich protein 9; Myeloma cell metalloproteinase	ADAM9	"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."	EC 3.4.24.-	.	MGSGARFPSGTLRVRWLLLLGLVGPVLGAARPGFQQTSHLSSYEIITPWRLTRERREAPRPYSKQVSYVIQAEGKEHIIHLERNKDLLPEDFVVYTYNKEGTLITDHPNIQNHCHYRGYVEGVHNSSIALSDCFGLRGLLHLENASYGIEPLQNSSHFEHIIYRMDDVYKEPLKCGVSNKDIEKETAKDEEEEPPSMTQLLRRRRAVLPQTRYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMYIMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWREKFLITRRRHDSAQLVLKKGFGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRDCSCGAKSCIMNSGASGSRNFSSCSAEDFEKLTLNKGGNCLLNIPKPDEAYSAPSCGNKLVDAGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCRFLPGGTLCRGKTSECDVPEYCNGSSQFCQPDVFIQNGYPCQNNKAYCYNGMCQYYDAQCQVIFGSKAKAAPKDCFIEVNSKGDRFGNCGFSGNEYKKCATGNALCGKLQCENVQEIPVFGIVPAIIQTPSRGTKCWGVDFQLGSDVPDPGMVNEGTKCGAGKICRNFQCVDASVLNYDCDVQKKCHGHGVCNSNKNCHCENGWAPPNCETKGYGGSVDSGPTYNEMNTALRDGLLVFFFLIVPLIVCAIFIFIKRDQLWRSYFRKKRSQTYESDGKNQANPSRQPGSVPRHVSPVTPPREVPIYANRFAVPTYAAKQPQQFPSRPPPPQPKVSSQGNLIPARPAPAPPLYSSLT	Clinical trial	"Clinical pipeline report, company report or official report of ImmunoGen."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1442490: Collagen degradation	.	Q13443
TTS2TEI	ADAM metallopeptidase with thrombospondin 1 (ADAMTS1)	Q9UHI8	ATS1_HUMAN	Peptidase	METH1; METH-1; KIAA1346; ADAMTS-1; ADAM-TS1; ADAM-TS 1	ADAMTS1	"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."	EC 3.4.24.-	3Q2H; 3Q2G; 2V4B; 2JIH	MQRAVPEGFGRRKLGSDMGNAERAPGSRSFGPVPTLLLLAAALLAVSDALGRPSEEDEELVVPELERAPGHGTTRLRLHAFDQQLDLELRPDSSFLAPGFTLQNVGRKSGSETPLPETDLAHCFYSGTVNGDPSSAAALSLCEGVRGAFYLLGEAYFIQPLPAASERLATAAPGEKPPAPLQFHLLRRNRQGDVGGTCGVVDDEPRPTGKAETEDEDEGTEGEDEGAQWSPQDPALQGVGQPTGTGSIRKKRFVSSHRYVETMLVADQSMAEFHGSGLKHYLLTLFSVAARLYKHPSIRNSVSLVVVKILVIHDEQKGPEVTSNAALTLRNFCNWQKQHNPPSDRDAEHYDTAILFTRQDLCGSQTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKQCASLNGVNQDSHMMASMLSNLDHSQPWSPCSAYMITSFLDNGHGECLMDKPQNPIQLPGDLPGTSYDANRQCQFTFGEDSKHCPDAASTCSTLWCTGTSGGVLVCQTKHFPWADGTSCGEGKWCINGKCVNKTDRKHFDTPFHGSWGMWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNLEDCPDNNGKTFREEQCEAHNEFSKASFGSGPAVEWIPKYAGVSPKDRCKLICQAKGIGYFFVLQPKVVDGTPCSPDSTSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTCKKISGSVTSAKPGYHDIITIPTGATNIEVKQRNQRGSRNNGSFLAIKAADGTYILNGDYTLSTLEQDIMYKGVVLRYSGSSAALERIRSFSPLKEPLTIQVLTVGNALRPKIKYTYFVKKKKESFNAIPTFSAWVIEEWGECSKSCELGWQRRLVECRDINGQPASECAKEVKPASTRPCADHPCPQWQLGEWSSCSKTCGKGYKKRSLKCLSHDGGVLSHESCDPLKKPKHFIDFCTMAECS	Literature-reported	"Synthesis and structure-activity relationship of a novel, achiral series of TNF-alpha converting enzyme inhibitors. Bioorg Med Chem Lett. 2006 May 15;16(10):2699-704."	0	EC:3.4	.	.	3.4.24.-	Acting on peptide bonds (peptidases)	ADAM cysteine-rich domain; ADAM-TS Spacer 1; Reprolysin family propeptide; Reprolysin (M12B) family zinc metalloprotease ; Thrombospondin type 1 domain	PF17771; PF05986; PF01562; PF01421; PF00090	PF17771; ADAM_CR_2; PF05986; ADAM_spacer1; PF01562; Pep_M12B_propep; PF01421; Reprolysin; PF00090; TSP_1	8.A.77.1.6	The Sheddase (Sheddase) Family	.	R-HSA-1474228: Degradation of the extracellular matrix; R-HSA-5083635: Defective B3GALTL causes PpS; R-HSA-5173214: O-glycosylation of TSR domain-containing proteins	.	Q9UHI8
TTUREBK	A disintegrin and metalloproteinase with thrombospondin motifs 13 (ADAMTS13)	Q76LX8	ATS13_HUMAN	.	ADAM-TS 13; ADAM-TS13; ADAMTS-13; von Willebrand factor-cleaving protease; vWF-CP; vWF-cleaving protease	ADAMTS13	Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation. {ECO:0000269|PubMed:19880749}.	EC 3.4.24.87	3GHM;3GHN;3VN4;6QIG;7B01	MHQRHPRARCPPLCVAGILACGFLLGCWGPSHFQQSCLQALEPQAVSSYLSPGAPLKGRPPSPGFQRQRQRQRRAAGGILHLELLVAVGPDVFQAHQEDTERYVLTNLNIGAELLRDPSLGAQFRVHLVKMVILTEPEGAPNITANLTSSLLSVCGWSQTINPEDDTDPGHADLVLYITRFDLELPDGNRQVRGVTQLGGACSPTWSCLITEDTGFDLGVTIAHEIGHSFGLEHDGAPGSGCGPSGHVMASDGAAPRAGLAWSPCSRRQLLSLLSAGRARCVWDPPRPQPGSAGHPPDAQPGLYYSANEQCRVAFGPKAVACTFAREHLDMCQALSCHTDPLDQSSCSRLLVPLLDGTECGVEKWCSKGRCRSLVELTPIAAVHGRWSSWGPRSPCSRSCGGGVVTRRRQCNNPRPAFGGRACVGADLQAEMCNTQACEKTQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLSLCVSGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTCSPRKGSFTAGRAREYVTFLTVTPNLTSVYIANHRPLFTHLAVRIGGRYVVAGKMSISPNTTYPSLLEDGRVEYRVALTEDRLPRLEEIRIWGPLQEDADIQVYRRYGEEYGNLTRPDITFTYFQPKPRQAWVWAAVRGPCSVSCGAGLRWVNYSCLDQARKELVETVQCQGSQQPPAWPEACVLEPCPPYWAVGDFGPCSASCGGGLRERPVRCVEAQGSLLKTLPPARCRAGAQQPAVALETCNPQPCPARWEVSEPSSCTSAGGAGLALENETCVPGADGLEAPVTEGPGSVDEKLPAPEPCVGMSCPPGWGHLDATSAGEKAPSPWGSIRTGAQAAHVWTPAAGSCSVSCGRGLMELRFLCMDSALRVPVQEELCGLASKPGSRREVCQAVPCPARWQYKLAACSVSCGRGVVRRILYCARAHGEDDGEEILLDTQCQGLPRPEPQEACSLEPCPPRWKVMSLGPCSASCGLGTARRSVACVQLDQGQDVEVDEAACAALVRPEASVPCLIADCTYRWHVGTWMECSVSCGDGIQRRRDTCLGPQAQAPVPADFCQHLPKPVTVRGCWAGPCVGQGTPSLVPHEEAAAPGRTTATPAGASLEWSQARGLLFSPAPQPRRLLPGPQENSVQSSACGRQHLEPTGTIDMRGPGQADCAVAIGRPLGEVVTLRVLESSLNCSAGDMLLLWGRLTWRKMCRKLLDMTFSSKTNTLVVRQRCGRPGGGVLLRYGSQLAPETFYRECDMQLFGPWGEIVSPSLSPATSNAGGCRLFINVAPHARIAIHALATNMGAGTEGANASYILIRDTHSLRTTAFHGQQVLYWESESSQAEMEFSEGFLKAQASLRGQYWTLQSWVPEMQDPQSWKGKEGT	Clinical trial	Evidence of protective effects of recombinant ADAMTS13 in a humanized model of sickle cell disease. Haematologica. 2022 Nov 1;107(11):2650-2660.	.	.	.	.	.	.	.	.	.	.	.	hsa:11093	R-HSA-5083635;R-HSA-5173214;	.	Q76LX8;
TTYG6BU	Aggrecanase-1 (ADAMTS4)	O75173	ATS4_HUMAN	Peptidase	Aggrecanase 1; ADMP-1; ADAMTS4; ADAM-TS4; ADAM-TS 4; A disintegrin and metalloproteinase with thrombospondin motifs 4	ADAMTS4	"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."	EC 3.4.24.82	4WKI; 4WKE; 4WK7; 3B2Z; 2RJP	MSQTGSHPGRGLAGRWLWGAQPCLLLPIVPLSWLVWLLLLLLASLLPSARLASPLPREEEIVFPEKLNGSVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGTYLTGTINGDPESVASLHWDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPGAHILRRKSPASGQGPMCNVKAPLGSPSPRPRRAKRFASLSRFVETLVVADDKMAAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQRGLNTPEDSDPDHFDTAILFTRQDLCGVSTCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNSKPCISLNGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLLDKPEAPLHLPVTFPGKDYDADRQCQLTFGPDSRHCPQLPPPCAALWCSGHLNGHAMCQTKHSPWADGTPCGPAQACMGGRCLHMDQLQDFNIPQAGGWGPWGPWGDCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCPTGSALTFREEQCAAYNHRTDLFKSFPGPMDWVPRYTGVAPQDQCKLTCQAQALGYYYVLEPRVVDGTPCSPDSSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGCSKQSGSFRKFRYGYNNVVTIPAGATHILVRQQGNPGHRSIYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVSLRYSGATAASETLSGHGPLAQPLTLQVLVAGNPQDTRLRYSFFVPRPTPSTPRPTPQDWLHRRAQILEILRRRPWAGRK	Patented-recorded	"Design and synthesis of a series of (2R)-N(4)-hydroxy-2-(3-hydroxybenzyl)-N(1)- [(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide derivati... J Med Chem. 2001 Oct 11;44(21):3347-50."	2	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-5173214:O-glycosylation of TSR domain-containing proteins	MetaCyc:ENSG00000158859-MON	O75173
TTXSU2Y	Aggrecanase (ADAMTS5)	Q9UNA0	ATS5_HUMAN	Peptidase	Aggrecanase-2; ADMP-2; ADAMTS5; ADAMTS-5; ADAM-TS5; ADAM-TS 5; ADAM-TS 11; A disintegrin and metalloproteinase with thrombospondinmotifs 5	ADAMTS5	"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."	EC 3.4.24.-	3LJT; 3HYG; 3HY9; 3HY7; 3B8Z	MLLGWASLLLCAFRLPLAAVGPAATPAQDKAGQPPTAAAAAQPRRRQGEEVQERAEPPGHPHPLAQRRRSKGLVQNIDQLYSGGGKVGYLVYAGGRRFLLDLERDGSVGIAGFVPAGGGTSAPWRHRSHCFYRGTVDGSPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGPWAEEEKGRVYGDGSARILHVYTREGFSFEALPPRASCETPASTPEAHEHAPAHSNPSGRAALASQLLDQSALSPAGGSGPQTWWRRRRRSISRARQVELLLVADASMARLYGRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQHNQLGDDHEEHYDAAILFTREDLCGHHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDSKFCEETFGSTEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLLDLPRKQILGPEELPGQTYDATQQCNLTFGPEYSVCPGMDVCARLWCAVVRQGQMVCLTKKLPAVEGTPCGKGRICLQGKCVDKTKKKYYSTSSHGNWGSWGSWGQCSRSCGGGVQFAYRHCNNPAPRNNGRYCTGKRAIYRSCSLMPCPPNGKSFRHEQCEAKNGYQSDAKGVKTFVEWVPKYAGVLPADVCKLTCRAKGTGYYVVFSPKVTDGTECRLYSNSVCVRGKCVRTGCDGIIGSKLQYDKCGVCGGDNSSCTKIVGTFNKKSKGYTDVVRIPEGATHIKVRQFKAKDQTRFTAYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGWSHRDDFLHGMGYSATKEILIVQILATDPTKPLDVRYSFFVPKKSTPKVNSVTSHGSNKVGSHTSQPQWVTGPWLACSRTCDTGWHTRTVQCQDGNRKLAKGCPLSQRPSAFKQCLLKKC	Clinical trial	Elevated aggrecanase activity in a rat model of joint injury is attenuated by an aggrecanase specific inhibitor. Osteoarthritis Cartilage. 2011 Mar;19(3):315-23.	17	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-5173214:O-glycosylation of TSR domain-containing proteins	.	Q9UNA0
TTV1ZSQ	Adenylate cyclase type 1 (ADCY1)	Q08828	ADCY1_HUMAN	Phosphorus-oxygen lyase	Ca(2+)/calmodulin-activated adenylyl cyclase; Adenylyl cyclase 1; Adenylate cyclase type I; ATP pyrophosphate-lyase 1	ADCY1	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.	EC 4.6.1.1	.	MAGAPRGGGGGGGGAGEPGGAERAAGTSRRRGLRACDEEFACPELEALFRGYTLRLEQAATLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCVLFLALLVVTNVRSLQVPQLQQVGQLALLFSLTFALLCCPFALGGPARGSAGAAGGPATAEQGVWQLLLVTFVSYALLPVRSLLAIGFGLVVAASHLLVTATLVPAKRPRLWRTLGANALLFVGVNMYGVFVRILTERSQRKAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHDNVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWSNDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGYGHERNSFLKTHNIETFFIVPSHRRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALRTASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQKYHQLQDEYFTSAVVLTLILAALFGLVYLLIFPQSVVVLLLLVFCICFLVACVLYLHITRVQCFPGCLTIQIRTVLCIFIVVLIYSVAQGCVVGCLPWAWSSKPNSSLVVLSSGGQRTALPTLPCESTHHALLCCLVGTLPLAIFFRVSSLPKMILLSGLTTSYILVLELSGYTRTGGGAVSGRSYEPIVAILLFSCALALHARQVDIRLRLDYLWAAQAEEEREDMEKVKLDNRRILFNLLPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEIIADFDELMEKDFYKDIEKIKTIGSTYMAAVGLAPTSGTKAKKSISSHLSTLADFAIEMFDVLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQVTEEVHRLLRRCPYHFVCRGKVSVKGKGEMLTYFLEGRTDGNGSQIRSLGLDRKMCPFGRAGLQGRRPPVCPMPGVSVRAGLPPHSPGQYLPSAAAGKEA	Successful	Ecto- and cytosolic 5'-nucleotidases in normal and AMP deaminase-deficient human skeletal muscle. Biol Chem. 2006 Jan;387(1):53-8.	34	EC:4.6	Phosphorus-oxygen lyases	adenylyl cyclase class-4/guanylyl cyclase family.	4.6.1.1 	Phosphorus-oxygen lyases	Adenylyl cyclase N-terminal extracellular and transmembrane region; Adenylate and Guanylate cyclase catalytic domain	PF16214; PF00211	PF16214; AC_N; PF00211; Guanylate_cyc	.	.	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	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	.	Q08828
TTBQ9IM	Adenylate cyclase type 2 (ADCY2)	Q08462	ADCY2_HUMAN	Phosphorus-oxygen lyase	ADCY2	ADCY2	"This is a membrane-bound, calmodulin-insensitive adenylyl cyclase."	EC 4.6.1.1	.	MWQEAMRRRRYLRDRSEEAAGGGDGLPRSRDWLYESYYCMSQQHPLIVFLLLIVMGSCLALLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRLFSLVIWICLVAMGYLFMCFGGTVSPWDQVSFFLFIIFVVYTMLPFNMRDAIIASVLTSSSHTIVLSVCLSATPGGKEHLVWQILANVIIFICGNLAGAYHKHLMELALQQTYQDTCNCIKSRIKLEFEKRQQERLLLSLLPAHIAMEMKAEIIQRLQGPKAGQMENTNNFHNLYVKRHTNVSILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVKMGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLNGAYKVEEGDGDIRDPYLKQHLVKTYFVINPKGERRSPQHLFRPRHTLDGAKMRASVRMTRYLESWGAAKPFAHLHHRDSMTTENGKISTTDVPMGQHNFQNRTLRTKSQKKRFEEELNERMIQAIDGINAQKQWLKSEDIQRISLLFYNKVLEKEYRATALPAFKYYVTCACLIFFCIFIVQILVLPKTSVLGISFGAAFLLLAFILFVCFAGQLLQCSKKASPLLMWLLKSSGIIANRPWPRISLTIITTAIILMMAVFNMFFLSDSEETIPPTANTTNTSFSASNNQVAILRAQNLFFLPYFIYSCILGLISCSVFLRVNYELKMLIMMVALVGYNTILLHTHAHVLGDYSQVLFERPGIWKDLKTMGSVSLSIFFITLLVLGRQNEYYCRLDFLWKNKFKKEREEIETMENLNRVLLENVLPAHVAEHFLARSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAVPSQEHSQEPERQYMHIGTMVEFAFALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLVLQTLGYTCTCRGIINVKGKGDLKTYFVNTEMSRSLSQSNVAS	Literature-reported	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	2	.	.	.	.	.	.	.	.	.	.	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	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	.	Q08462
TTN64VU	Adenylate cyclase type 5 (AC5)	O95622	ADCY5_HUMAN	Phosphorus-oxygen lyase	Adenylyl cyclase 5; Adenylate cyclase type V; ATP pyrophosphate-lyase 5; AC5	ADCY5	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.	EC 4.6.1.1	.	MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGAVTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRRGAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEGGEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQITIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVFTITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSPWPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADLLVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS	Literature-reported	Alternating Hemiplegia of Childhood as a New Presentation of Adenylate Cyclase 5-Mutation-Associated Disease: A Report of Two Cases. J Pediatr. 2017 Feb;181:306-308.e1.	.	.	.	.	.	.	.	.	.	.	.	"hsa00230: Purine metabolism; hsa01100: Metabolic pathways; hsa01522: Endocrine resistance; hsa04015: Rap1 signaling pathway; hsa04022: cGMP-PKG signaling pathway; hsa04024: cAMP signaling pathway; hsa04062: Chemokine signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04114: Oocyte meiosis; hsa04211: Longevity regulating pathway; hsa04213: Longevity regulating pathway - multiple species; hsa04261: Adrenergic signaling in cardiomyocytes; hsa04270: Vascular smooth muscle contraction; hsa04371: Apelin signaling pathway; hsa04540: Gap junction; hsa04611: Platelet activation; hsa04713: Circadian entrainment; hsa04714: Thermogenesis; hsa04723: Retrograde endocannabinoid signaling; hsa04724: Glutamatergic synapse; hsa04725: Cholinergic synapse; hsa04726: Serotonergic synapse; hsa04727: GABAergic synapse; hsa04728: Dopaminergic 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; hsa04924: Renin secretion; hsa04925: Aldosterone synthesis and secretion; hsa04926: Relaxin signaling pathway; hsa04927: Cortisol synthesis and secretion; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04934: Cushing syndrome; hsa04935: Growth hormone synthesis, secretion and action; hsa04970: Salivary secretion; hsa04971: Gastric acid secretion; hsa04972: Pancreatic secretion; hsa04976: Bile secretion; hsa05012: Parkinson disease; hsa05030: Cocaine addiction; hsa05031: Amphetamine addiction; hsa05032: Morphine addiction; hsa05034: Alcoholism; hsa05163: Human cytomegalovirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05200: Pathways in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05414: Dilated cardiomyopathy"	"R-HSA-163359: Glucagon signaling in metabolic regulation; R-HSA-163615: PKA activation; R-HSA-164378: PKA activation in glucagon signalling; R-HSA-170660: Adenylate cyclase activating pathway; R-HSA-170670: Adenylate cyclase inhibitory pathway; R-HSA-381676: Glucagon-like Peptide-1 (GLP1) regulates insulin secretion; R-HSA-400042: Adrenaline,noradrenaline inhibits insulin secretion; 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; R-HSA-9634597: GPER1 signaling; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production; R-HSA-9664323: FCGR3A-mediated IL10 synthesis"	.	O95622
TTW4LYC	Pituitary adenylate cyclase-activating 38 (PACAP-38)	P18509 (132-169)	PACA_HUMAN	Glucagon	Pituitary adenylate cyclase-activating polypeptide; PACAP38; PACAP27; PACAP-38; PACAP-27; PACAP; ADCYAP1	ADCYAP1	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.	.	2JOD; 2D2P; 1GEA	HSDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRVKNK	Clinical trial	"Pituitary adenylate cyclase-activating polypeptides, PACAP-38 and PACAP-27, regulation of sympathetic neuron catecholamine, and neuropeptide Y expr... Ann N Y Acad Sci. 1996 Dec 26;805:204-16; discussion 217-8."	17	.	.	.	.	.	.	.	.	.	.	hsa04911:Insulin secretion	R-HSA-187024:NGF-independant TRKA activation; R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors	.	P18509
TT5OREU	PACAP type I receptor (PAC1R)	P41586	PACR_HUMAN	.	Pituitary adenylate cyclase-activating polypeptide type I receptor; PACAP-R1; PACAP-R-1	ADCYAP1R1	"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."	.	3N94; 2JOD	MAGVVHVSLAALLLLPMAPAMHSDCIFKKEQAMCLEKIQRANELMGFNDSSPGCPGMWDNITCWKPAHVGEMVLVSCPELFRIFNPDQVWETETIGESDFGDSNSLDLSDMGVVSRNCTEDGWSEPFPHYFDACGFDEYESETGDQDYYYLSVKALYTVGYSTSLVTLTTAMVILCRFRKLHCTRNFIHMNLFVSFMLRAISVFIKDWILYAEQDSNHCFISTVECKAVMVFFHYCVVSNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTVCVTVWATLRLYFDDTGCWDMNDSTALWWVIKGPVVGSIMVNFVLFIGIIVILVQKLQSPDMGGNESSIYLRLARSTLLLIPLFGIHYTVFAFSPENVSKRERLVFELGLGSFQGFVVAVLYCFLNGEVQAEIKRKWRSWKVNRYFAVDFKHRHPSLASSGVNGGTQLSILSKSSSQIRMSGLPADNLAT	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	hsa04024: cAMP signaling pathway; hsa04080: Neuroactive ligand-receptor interaction; hsa04713: Circadian entrainment; hsa04911: Insulin secretion; hsa04924: Renin secretion	R-HSA-187024: NGF-independant TRKA activation; R-HSA-418555: G alpha (s) signalling events; R-HSA-420092: Glucagon-type ligand receptors; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production	.	P41586
TTM5OJN	CIRL-1 messenger RNA (CIRL-1 mRNA)	O94910	AGRL1_HUMAN	mRNA target	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)	ADGRL1	"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."	.	.	MARLAAVLWNLCVTAVLVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYKVEQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYVDDDSEAAGNRVDYAFNTNANREEPVSLTFPNPYQFISSVDYNPRDNQLYVWNNYFVVRYSLEFGPPDPSAGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPVPSTRRPPAPNLHVSPELFCEPREVRRVQWPATQQGMLVERPCPKGTRGIASFQCLPALGLWNPRGPDLSNCTSPWVNQVAQKIKSGENAANIASELARHTRGSIYAGDVSSSVKLMEQLLDILDAQLQALRPIERESAGKNYNKMHKRERTCKDYIKAVVETVDNLLRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKENVVLEVTVLNTEGQVQELVFPQEEYPRKNSIQLSAKTIKQNSRNGVVKVVFILYNNLGLFLSTENATVKLAGEAGPGGPGGASLVVNSQVIAASINKESSRVFLMDPVIFTVAHLEDKNHFNANCSFWNYSERSMLGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREIYQGRINELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEIACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRHSYCCIRSPPGGTHGSLKTSAMRSNTRYYTGTQSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQPRGGTSPYNTLIAESVGFNPSSPPVFNSPGSYREPKHPLGGREACGMDTLPLNGNFNNSYSLRSGDFPPGDGGPEPPRGRNLADAAAFEKMIISELVHNNLRGSSSAAKGPPPPEPPVPPVPGGGGEEEAGGPGGADRAEIELLYKALEEPLLLPRAQSVLYQSDLDESESCTAEDGATSRPLSSPPGRDSLYASGANLRDSPSYPDSSPEGPSEALPPPPPAPPGPPEIYYTSRPPALVARNPLQGYYQVRRPSHEGYLAAPGLEGPGPDGDGQMQLVTSL	Literature-reported	Involvement of the calcium-independent receptor for alpha-latrotoxin in brain ischemia. Brain Res Mol Brain Res. 2002 Aug 15;104(2):246-9.	.	mRNA	mRNA target	.	.	.	"7 transmembrane receptor (Secretin family); GPCR-Autoproteolysis INducing (GAIN) domain; Galactose binding lectin domain; GPCR proteolysis site, GPS, motif ; Hormone receptor domain; Latrophilin Cytoplasmic C-terminal region; Olfactomedin-like domain"	PF00002; PF16489; PF02140; PF01825; PF02793; PF02354; PF02191	PF00002; 7tm_2; PF16489; GAIN; PF02140; Gal_Lectin; PF01825; GPS; PF02793; HRM; PF02354; Latrophilin; PF02191; OLF	.	.	.	.	.	O94910
TTQST3U	CIRL-3 messenger RNA (CIRL-3 mRNA)	Q9HAR2	AGRL3_HUMAN	mRNA target	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)	ADGRL3	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.	.	5CMN	MWPSQLLIFMMLLAPIIHAFSRAPIPMAVVRRELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCPGTYKYLEVQYECVPYKVEQKVFLCPGLLKGVYQSEHLFESDHQSGAWCKDPLQASDKIYYMPWTPYRTDTLTEYSSKDDFIAGRPTTTYKLPHRVDGTGFVVYDGALFFNKERTRNIVKFDLRTRIKSGEAIIANANYHDTSPYRWGGKSDIDLAVDENGLWVIYATEQNNGKIVISQLNPYTLRIEGTWDTAYDKRSASNAFMICGILYVVKSVYEDDDNEATGNKIDYIYNTDQSKDSLVDVPFPNSYQYIAAVDYNPRDNLLYVWNNYHVVKYSLDFGPLDSRSGQAHHGQVSYISPPIHLDSELERPSVKDISTTGPLGMGSTTTSTTLRTTTLSPGRSTTPSVSGRRNRSTSTPSPAVEVLDDMTTHLPSASSQIPALEESCEAVEAREIMWFKTRQGQIAKQPCPAGTIGVSTYLCLAPDGIWDPQGPDLSNCSSPWVNHITQKLKSGETAANIARELAEQTRNHLNAGDITYSVRAMDQLVGLLDVQLRNLTPGGKDSAARSLNKAMVETVNNLLQPQALNAWRDLTTSDQLRAATMLLHTVEESAFVLADNLLKTDIVRENTDNIKLEVARLSTEGNLEDLKFPENMGHGSTIQLSANTLKQNGRNGEIRVAFVLYNNLGPYLSTENASMKLGTEALSTNHSVIVNSPVITAAINKEFSNKVYLADPVVFTVKHIKQSEENFNPNCSFWSYSKRTMTGYWSTQGCRLLTTNKTHTTCSCNHLTNFAVLMAHVEVKHSDAVHDLLLDVITWVGILLSLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLAAFTWMFLEGVQLYIMLVEVFESEHSRRKYFYLVGYGMPALIVAVSAAVDYRSYGTDKVCWLRLDTYFIWSFIGPATLIIMLNVIFLGIALYKMFHHTAILKPESGCLDNIKSWVIGAIALLCLLGLTWAFGLMYINESTVIMAYLFTIFNSLQGMFIFIFHCVLQKKVRKEYGKCLRTHCCSGKSTESSIGSGKTSGSRTPGRYSTGSQSRIRRMWNDTVRKQSESSFITGDINSSASLNREGLLNNARDTSVMDTLPLNGNHGNSYSIASGEYLSNCVQIIDRGYNHNETALEKKILKELTSNYIPSYLNNHERSSEQNRNLMNKLVNNLGSGREDDAIVLDDATSFNHEESLGLELIHEESDAPLLPPRVYSTENHQPHHYTRRRIPQDHSESFFPLLTNEHTEDLQSPHRDSLYTSMPTLAGVAATESVTTSTQTEPPPAKCGDAEDVYYKSMPNLGSRNHVHQLHTYYQLGRGSSDGFIVPPNKDGTPPEGSSKGPAHLVTSL	Literature-reported	Involvement of the calcium-independent receptor for alpha-latrotoxin in brain ischemia. Brain Res Mol Brain Res. 2002 Aug 15;104(2):246-9.	.	mRNA	mRNA target	.	.	.	"7 transmembrane receptor (Secretin family); GPCR-Autoproteolysis INducing (GAIN) domain; Galactose binding lectin domain; GPCR proteolysis site, GPS, motif ; Hormone receptor domain; Latrophilin Cytoplasmic C-terminal region; Olfactomedin-like domain"	PF00002; PF16489; PF02140; PF01825; PF02793; PF02354; PF02191	PF00002; 7tm_2; PF16489; GAIN; PF02140; Gal_Lectin; PF01825; GPS; PF02793; HRM; PF02354; Latrophilin; PF02191; OLF	.	.	.	.	.	Q9HAR2
TT5AHZ0	Alcohol dehydrogenase 1A (ADH1A)	P07327	ADH1A_HUMAN	.	Alcohol dehydrogenase subunit alpha; ADH1	ADH1A	Facilitates the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+) to NADH.	EC 1.1.1.1	1U3T; 1HSO	MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNPQGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQNLSMNPMLLLTGRTWKGAILGGFKSKECVPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTILMF	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	hsa00010: Glycolysis / Gluconeogenesis; hsa00071: Fatty acid degradation; hsa00350: Tyrosine metabolism; hsa00620: Pyruvate metabolism; hsa00830: Retinol metabolism; hsa00980: Metabolism of xenobiotics by cytochrome P450; hsa00982: Drug metabolism - cytochrome P450; hsa01100: Metabolic pathways; hsa04936: Alcoholic liver disease	R-HSA-2161541: Abacavir metabolism; R-HSA-5365859: RA biosynthesis pathway; R-HSA-71384: Ethanol oxidation	.	P07327
TT3LE7P	Gastric alcohol dehydrogenase (ADH7)	P40394	ADH7_HUMAN	Short-chain dehydrogenases reductase	Alcohol dehydrogenase class IV mu/sigma chain; Alcohol dehydrogenase class 4 mu/sigma chain; ADH7	ADH7	"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."	EC 1.1.1.1	1D1T; 1D1S; 1AGN	MFAEIQIQDKDRMGTAGKVIKCKAAVLWEQKQPFSIEEIEVAPPKTKEVRIKILATGICRTDDHVIKGTMVSKFPVIVGHEATGIVESIGEGVTTVKPGDKVIPLFLPQCRECNACRNPDGNLCIRSDITGRGVLADGTTRFTCKGKPVHHFMNTSTFTEYTVVDESSVAKIDDAAPPEKVCLIGCGFSTGYGAAVKTGKVKPGSTCVVFGLGGVGLSVIMGCKSAGASRIIGIDLNKDKFEKAMAVGATECISPKDSTKPISEVLSEMTGNNVGYTFEVIGHLETMIDALASCHMNYGTSVVVGVPPSAKMLTYDPMLLFTGRTWKGCVFGGLKSRDDVPKLVTEFLAKKFDLDQLITHVLPFKKISEGFELLNSGQSIRTVLTF	Literature-reported	Retinol dehydrogenase 13 deficiency diminishes carbon tetrachloride-induced liver fibrosis in mice. Toxicol Lett. 2017 Jan 4;265:17-22.	.	.	.	.	.	.	.	.	.	.	.	hsa00010: Glycolysis / Gluconeogenesis; hsa00071: Fatty acid degradation; hsa00350: Tyrosine metabolism; hsa00620: Pyruvate metabolism; hsa00830: Retinol metabolism; hsa00980: Metabolism of xenobiotics by cytochrome P450; hsa00982: Drug metabolism - cytochrome P450; hsa01100: Metabolic pathways; hsa04936: Alcoholic liver disease	R-HSA-71384: Ethanol oxidation	.	P40394
TTXKA7D	Adiponectin (ADIPOQ)	Q15848	ADIPO_HUMAN	Adiponectin protein	"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"	ADIPOQ	"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."	.	4DOU	MLLLGAVLLLLALPGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGEKGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSVGLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKDVKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGERNGLYADNDNDSTFTGFLLYHDTN	Literature-reported	"Biomarkers of diabetic nephropathy, the present and the future. Curr Diabetes Rev. 2012 Sep;8(5):317-28."	.	TC=8.A.94	.	.	.	.	C1q domain; Collagen triple helix repeat (20 copies)	PF00386; PF01391	PF00386; C1q; PF01391; Collagen	8.A.94.1.1	The Adiponectin (Adiponectin) Family	hsa03320: PPAR signaling pathway; hsa04152: AMPK signaling pathway; hsa04211: Longevity regulating pathway; hsa04920: Adipocytokine signaling pathway; hsa04930: Type II diabetes mellitus; hsa04932: Non-alcoholic fatty liver disease; hsa04936: Alcoholic liver disease	R-HSA-163680: AMPK inhibits chREBP transcriptional activation activity; R-HSA-381340: Transcriptional regulation of white adipocyte differentiation	.	Q15848
TTHGD1B	Adiponectin receptor (ADIPOR)	Q96A54; Q86V24	PAQR1_HUMAN; PAQR2_HUMAN	.	Progestin and adipoQ receptor family member; PAQR; Adiponectin receptor protein	ADIPOR1	"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."	.	.	MSSHKGSVVAQGNGAPASNREADTVELAELGPLLEEKGKRVIANPPKAEEEQTCPVPQEEEEEVRVLTLPLQAHHAMEKMEEFVYKVWEGRWRVIPYDVLPDWLKDNDYLLHGHRPPMPSFRACFKSIFRIHTETGNIWTHLLGFVLFLFLGILTMLRPNMYFMAPLQEKVVFGMFFLGAVLCLSFSWLFHTVYCHSEKVSRTFSKLDYSGIALLIMGSFVPWLYYSFYCSPQPRLIYLSIVCVLGISAIIVAQWDRFATPKHRQTRAGVFLGLGLSGVVPTMHFTIAEGFVKATTVGQMGWFFLMAVMYITGAGLYAARIPERFFPGKFDIWFQSHQIFHVLVVAAAFVHFYGVSNLQEFRYGLEGGCTDDTLL	Literature-reported	"Adiporon, an adiponectin receptor agonist acts as an antidepressant and metabolic regulator in a mouse model of depression. Transl Psychiatry. 2018 Aug 16;8(1):159."	.	.	.	.	.	.	.	.	.	.	.	hsa04152: AMPK signaling pathway; hsa04211: Longevity regulating pathway; hsa04920: Adipocytokine signaling pathway; hsa04932: Non-alcoholic fatty liver disease; hsa04936: Alcoholic liver disease	R-HSA-163680: AMPK inhibits chREBP transcriptional activation activity	.	Q96A54
TTL732K	Adenosine kinase (ADK)	P55263	ADK_HUMAN	Kinase	Adenosine 5'-phosphotransferase; AK	ADK	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.	EC 2.7.1.20	4O1L; 2I6B; 2I6A; 1BX4	MAAAEEEPKPKKLKVEAPQALRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKARVCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTFPEKPDFH	Clinical trial	"Adenosine kinase inhibitors. 6. Synthesis, water solubility, and antinociceptive activity of 5-phenyl-7-(5-deoxy-beta-D-ribofuranosyl)pyrrolo[2,3-d]pyrimidines substituted at C4 with glycinamides andrelated compounds. J Med Chem. 2005 Dec 1;48(24):7808-20."	17	EC:2.7	.	carbohydrate kinase PfkB family.	2.7.1.20	Transferring phosphorus-containing groups	pfkB family carbohydrate kinase	PF00294	PF00294; PfkB	.	.	hsa00230:Purine metabolism; hsa01100:Metabolic pathways	R-HSA-74217:Purine salvage	MetaCyc:HS08097-MON	P55263
TTV14YH	Adrenomedullin (ADM)	P35318	ADML_HUMAN	Adrenomedullin	AM; ADM	ADM	"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."	.	5V6Y; 4RWF; 2L7S; 2FLY	MKLVSVALMYLGSLAFLGADTARLDVASEFRKKWNKWALSRGKRELRMSSSYPTGLADVKAGPAQTLIRPQDMKGASRSPEDSSPDAARIRVKRYRQSMNNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGYGRRRRRSLPEAGPGRTLVSSKPQAHGAPAPPSGSAPHFL	Literature-reported	Expression of the hypoxically regulated angiogenic factor adrenomedullin correlates with uterine leiomyoma vascular density. Clin Cancer Res. 2000 Jul;6(7):2808-14.	.	.	.	adrenomedullin family.	.	.	Calcitonin / CGRP / IAPP family	PF00214	PF00214; Calc_CGRP_IAPP	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04270: Vascular smooth muscle contraction	R-HSA-418555: G alpha (s) signalling events; R-HSA-419812: Calcitonin-like ligand receptors; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production	.	P35318
TTM642F	Adrenomedullin 2 (ADM2)	Q7Z4H4	ADM2_HUMAN	Adrenomedullin	Intermedin; ADM2	ADM2	"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."	.	6D1U	MARIPTAALGCISLLCLQLPGSLSRSLGGDPRPVKPREPPARSPSSSLQPRHPAPRPVVWKLHRALQAQRGAGLAPVMGQPLRDGGRQHSGPRRHSGPRRTQAQLLRVGCVLGTCQVQNLSHRLWQLMGPAGRQDSAPVDPSSPHSYG	Literature-reported	Adrenomedullin2 (ADM2)/Intermedin (IMD): A Potential Role in the Pathophysiology of Preeclampsia. J Clin Endocrinol Metab. 2016 Nov;101(11):4478-4488.	.	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04270: Vascular smooth muscle contraction	R-HSA-418555: G alpha (s) signalling events; R-HSA-419812: Calcitonin-like ligand receptors; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production	.	Q7Z4H4
TTK25J1	Adenosine A1 receptor (ADORA1)	P30542	AA1R_HUMAN	GPCR rhodopsin	Adenosine receptor A1; A(1) adenosine receptor	ADORA1	The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Receptor for adenosine.	.	6D9H; 5UEN; 5N2S	MPPSISAFQAAYIGIEVLIALVSVPGNVLVIWAVKVNQALRDATFCFIVSLAVADVAVGALVIPLAILINIGPQTYFHTCLMVACPVLILTQSSILALLAIAVDRYLRVKIPLRYKMVVTPRRAAVAIAGCWILSFVVGLTPMFGWNNLSAVERAWAANGSMGEPVIKCEFEKVISMEYMVYFNFFVWVLPPLLLMVLIYLEVFYLIRKQLNKKVSASSGDPQKYYGKELKIAKSLALILFLFALSWLPLHILNCITLFCPSCHKPSILTYIAIFLTHGNSAMNPIVYAFRIQKFRVTFLKIWNDHFRCQPAPPIDEDLPEERPDD	Successful	Caffeine as a psychomotor stimulant: mechanism of action. Cell Mol Life Sci. 2004 Apr;61(7-8):857-72.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.3.4	The G-protein-coupled receptor (GPCR) Family	hsa04022:cGMP-PKG signaling pathway; hsa04024:cAMP signaling pathway; hsa04071:Sphingolipid signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa05032:Morphine addiction	R-HSA-417973:Adenosine P1 receptors; R-HSA-418594:G alpha (i) signalling events	.	P30542
TT92EIB	ADORA1 messenger RNA (ADORA1 mRNA)	P30542	AA1R_HUMAN	mRNA target	Adenosine receptor A1 (mRNA); A(1) adenosine receptor (mRNA)	ADORA1	The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Receptor for adenosine.	.	6D9H; 5UEN; 5N2S	MPPSISAFQAAYIGIEVLIALVSVPGNVLVIWAVKVNQALRDATFCFIVSLAVADVAVGALVIPLAILINIGPQTYFHTCLMVACPVLILTQSSILALLAIAVDRYLRVKIPLRYKMVVTPRRAAVAIAGCWILSFVVGLTPMFGWNNLSAVERAWAANGSMGEPVIKCEFEKVISMEYMVYFNFFVWVLPPLLLMVLIYLEVFYLIRKQLNKKVSASSGDPQKYYGKELKIAKSLALILFLFALSWLPLHILNCITLFCPSCHKPSILTYIAIFLTHGNSAMNPIVYAFRIQKFRVTFLKIWNDHFRCQPAPPIDEDLPEERPDD	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	mRNA	mRNA target	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04022: cGMP-PKG signaling pathway; hsa04024: cAMP signaling pathway; hsa04071: Sphingolipid signaling pathway; hsa04080: Neuroactive ligand-receptor interaction; hsa04923: Regulation of lipolysis in adipocytes; hsa04924: Renin secretion; hsa05032: Morphine addiction	R-HSA-417973:Adenosine P1 receptors; R-HSA-418594:G alpha (i) signalling events	.	P30542
TTM2AOE	Adenosine A2a receptor (ADORA2A)	P29274	AA2AR_HUMAN	GPCR rhodopsin	Adenosine receptor A2a; ADORA2; A2a Adenosine receptor; A(2A) adenosine receptor	ADORA2A	The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Receptor for adenosine.	.	6MH8; 6GDG; 6AQF; 5WF6; 5WF5	MPIMGSSVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADIAVGVLAIPFAITISTGFCAACHGCLFIACFVLVLTQSSIFSLLAIAIDRYIAIRIPLRYNGLVTGTRAKGIIAICWVLSFAIGLTPMLGWNNCGQPKEGKNHSQGCGEGQVACLFEDVVPMNYMVYFNFFACVLVPLLLMLGVYLRIFLAARRQLKQMESQPLPGERARSTLQKEVHAAKSLAIIVGLFALCWLPLHIINCFTFFCPDCSHAPLWLMYLAIVLSHTNSVVNPFIYAYRIREFRQTFRKIIRSHVLRQQEPFKAAGTSARVLAAHGSDGEQVSLRLNGHPPGVWANGSAPHPERRPNGYALGLVSGGSAQESQGNTGLPDVELLSHELKGVCPEPPGLDDPLAQDGAGVS	Successful	Caffeine as a psychomotor stimulant: mechanism of action. Cell Mol Life Sci. 2004 Apr;61(7-8):857-72.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.3.8	The G-protein-coupled receptor (GPCR) Family	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	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	.	P29274
TTNE7KG	Adenosine A2b receptor (ADORA2B)	P29275	AA2BR_HUMAN	GPCR rhodopsin	Adenosine receptor A2b; A2b Adenosine receptor	ADORA2B	The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Receptor for adenosine.	.	.	MLLETQDALYVALELVIAALSVAGNVLVCAAVGTANTLQTPTNYFLVSLAAADVAVGLFAIPFAITISLGFCTDFYGCLFLACFVLVLTQSSIFSLLAVAVDRYLAICVPLRYKSLVTGTRARGVIAVLWVLAFGIGLTPFLGWNSKDSATNNCTEPWDGTTNESCCLVKCLFENVVPMSYMVYFNFFGCVLPPLLIMLVIYIKIFLVACRQLQRTELMDHSRTTLQREIHAAKSLAMIVGIFALCWLPVHAVNCVTLFQPAQGKNKPKWAMNMAILLSHANSVVNPIVYAYRNRDFRYTFHKIISRYLLCQADVKSGNGQAGVQPALGVGL	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04015:Rap1 signaling pathway; hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04270:Vascular smooth muscle contraction; hsa05034:Alcoholism	R-HSA-417973:Adenosine P1 receptors; R-HSA-418555:G alpha (s) signalling events; R-HSA-5683826:Surfactant metabolism	.	P29275
TTJFY5U	Adenosine A3 receptor (ADORA3)	P0DMS8	AA3R_HUMAN	GPCR rhodopsin	Adenosine receptor A3A; Adenosine receptor A3; Adenosine 3 receptor; A3AR; A3 Adenosine receptor	ADORA3	The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. Isoform 2: Receptor for adenosine.	.	1R7N; 1OEA	MPNNSTALSLANVTYITMEIFIGLCAIVGNVLVICVVKLNPSLQTTTFYFIVSLALADIAVGVLVMPLAIVVSLGITIHFYSCLFMTCLLLIFTHASIMSLLAIAVDRYLRVKLTVRYKRVTTHRRIWLALGLCWLVSFLVGLTPMFGWNMKLTSEYHRNVTFLSCQFVSVMRMDYMVYFSFLTWIFIPLVVMCAIYLDIFYIIRNKLSLNLSNSKETGAFYGREFKTAKSLFLVLFLFALSWLPLSIINCIIYFNGEVPQLVLYMGILLSHANSMMNPIVYAYKIKKFKETYLLILKACVVCHPSDSLDTSIEKNSE	Clinical trial	A role for central A3-adenosine receptors. Mediation of behavioral depressant effects. FEBS Lett. 1993 Dec 20;336(1):57-60.	25	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04022: cGMP-PKG signaling pathway; hsa04071: Sphingolipid signaling pathway; hsa04080: Neuroactive ligand-receptor interaction	R-HSA-417973:Adenosine P1 receptors; R-HSA-418594:G alpha (i) signalling events	.	P0DMS8
TTNGILX	Adrenergic receptor alpha-1A (ADRA1A)	P35348	ADA1A_HUMAN	GPCR rhodopsin	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	ADRA1A	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.	.	.	MVFLSGNASDSSNCTQPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEVLGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGLMALLCVWALSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYLPLAIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGMASAKTKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV	Successful	Pharma & Vaccines. Product Development Pipeline. April 29 2009.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA1A sub-subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	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	R-HSA-390696:Adrenoceptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-416482:G alpha (12/13) signalling events	.	P35348
TTDBOI7	HUAMN alpha-1 adrenergic receptor (ADRA1)	P35348; P35368; P25100	ADA1A_HUMAN; ADA1B_HUMAN; ADA1D_HUMAN	Adrenergic receptor subfamily	Alpha-1 adrenoreceptor	ADRA1A	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.	.	.	MVFLSGNASDSSNCTQPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEVLGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGLMALLCVWALSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYLPLAIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGMASAKTKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARVRSKSFLQVCCCVGPSTPSLDKNHQVPTIKVHTISLSENGEEV	.	Carvedilol increases the production of interleukin-12 and interferon-gamma and improves the survival of mice infected with the encephalomyocarditis virus. J Am Coll Cardiol. 2003 Jan 15;41(2):340-5.	.	.	.	.	.	.	.	.	.	.	.	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	R-HSA-390696: Adrenoceptors; R-HSA-416476: G alpha (q) signalling events; R-HSA-416482: G alpha (12/13) signalling events	.	P35348
TTBRKXS	Adrenergic receptor alpha-1B (ADRA1B)	P35368	ADA1B_HUMAN	GPCR rhodopsin	Alpha-1B adrenoreceptor; Alpha-1B adrenoceptor; Alpha-1B adrenergic receptor; Alpha 1B-adrenoreceptor; Alpha 1B-adrenoceptor	ADRA1B	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.	.	.	MNPDLDTGHNTSAPAHWGELKNANFTGPNQTSSNSTLPQLDITRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPTNYFIVNLAMADLLLSFTVLPFSAALEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRKAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLFSTLKPPDAVFKVVFWLGYFNSCLNPIIYPCSSKEFKRAFVRILGCQCRGRGRRRRRRRRRLGGCAYTYRPWTRGGSLERSQSRKDSLDDSGSCLSGSQRTLPSASPSPGYLGRGAPPPVELCAFPEWKAPGALLSLPAPEPPGRRGRHDSGPLFTFKLLTEPESPGTDGGASNGGCEAAADVANGQPGFKSNMPLAPGQF	Successful	Interaction of neuroleptics and antidepressants with rat brain alpha 2-receptors: a possible relationship between alpha 2-receptor antagonism and antidepressant action. Biol Psychiatry. 1984 Sep;19(9):1283-91.	34	PF00001	.	G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA1B sub-subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	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	R-HSA-390696:Adrenoceptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-416482:G alpha (12/13) signalling events	.	P35368
TT34BHT	Adrenergic receptor alpha-1D (ADRA1D)	P25100	ADA1D_HUMAN	GPCR rhodopsin	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	ADRA1D	This alpha-adrenergic receptor mediates its effect through the influx of extracellular calcium.	.	.	MTFRDLLSVSFEGPRPDSSAGGSSAGGGGGSAGGAAPSEGPAVGGVPGGAGGGGGVVGAGSGEDNRSSAGEPGSAGAGGDVNGTAAVGGLVVSAQGVGVGVFLAAFILMAVAGNLLVILSVACNRHLQTVTNYFIVNLAVADLLLSATVLPFSATMEVLGFWAFGRAFCDVWAAVDVLCCTASILSLCTISVDRYVGVRHSLKYPAIMTERKAAAILALLWVVALVVSVGPLLGWKEPVPPDERFCGITEEAGYAVFSSVCSFYLPMAVIVVMYCRVYVVARSTTRSLEAGVKRERGKASEVVLRIHCRGAATGADGAHGMRSAKGHTFRSSLSVRLLKFSREKKAAKTLAIVVGVFVLCWFPFFFVLPLGSLFPQLKPSEGVFKVIFWLGYFNSCVNPLIYPCSSREFKRAFLRLLRCQCRRRRRRRPLWRVYGHHWRASTSGLRQDCAPSSGDAPPGAPLALTALPDPDPEPPGTPEMQAPVASRRKPPSAFREWRLLGPFRRPTTQLRAKVSSLSHKIRAGGAQRAEAACAQRSEVEAVSLGVPHEVAEGATCQAYELADYSNLRETDI	Successful	Alfuzosin: a review of the therapeutic use of the prolonged-release formulation given once daily in the management of benign prostatic hyperplasia. Drugs. 2002;62(4):633-53.	34	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	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	R-HSA-390696:Adrenoceptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-416482:G alpha (12/13) signalling events	.	P25100
TTWG9A4	Adrenergic receptor alpha-2A (ADRA2A)	P08913	ADA2A_HUMAN	GPCR rhodopsin	Alpha-2AAR; Alpha-2A adrenoreceptor; Alpha-2A adrenoceptor; Alpha-2A adrenergic receptor; Alpha-2 adrenergic receptor subtype C10; ADRAR; ADRA2R	ADRA2A	"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."	.	1HOF; 1HOD; 1HO9; 1HLL	MFRQEQPLAEGSFAPMGSLQPDAGNASWNGTEAPGGGARATPYSLQVTLTLVCLAGLLMLLTVFGNVLVIIAVFTSRALKAPQNLFLVSLASADILVATLVIPFSLANEVMGYWYFGKAWCEIYLALDVLFCTSSIVHLCAISLDRYWSITQAIEYNLKRTPRRIKAIIITVWVISAVISFPPLISIEKKGGGGGPQPAEPRCEINDQKWYVISSCIGSFFAPCLIMILVYVRIYQIAKRRTRVPPSRRGPDAVAAPPGGTERRPNGLGPERSAGPGGAEAEPLPTQLNGAPGEPAPAGPRDTDALDLEESSSSDHAERPPGPRRPERGPRGKGKARASQVKPGDSLPRRGPGATGIGTPAAGPGEERVGAAKASRWRGRQNREKRFTFVLAVVIGVFVVCWFPFFFTYTLTAVGCSVPRTLFKFFFWFGYCNSSLNPVIYTIFNHDFRRAFKKILCRGDRKRIV	Successful	alpha2A-adrenergic receptors heterosynaptically regulate glutamatergic transmission in the bed nucleus of the stria terminalis. Neuroscience. 2009 Sep 29;163(1):339-51.	34	PF00001	.	G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA2A sub-subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction	"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"	.	P08913
TTWM4TY	Adrenergic receptor alpha-2B (ADRA2B)	P18089	ADA2B_HUMAN	GPCR rhodopsin	Subtype C2; Alpha-2BAR; Alpha-2B adrenoreceptor; Alpha-2B adrenoceptor; Alpha-2B adrenergic receptor; Alpha-2 adrenergic receptor subtype C2; ADRA2RL1; ADRA2L1	ADRA2B	"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."	.	2CVA	MDHQDPYSVQATAAIAAAITFLILFTIFGNALVILAVLTSRSLRAPQNLFLVSLAAADILVATLIIPFSLANELLGYWYFRRTWCEVYLALDVLFCTSSIVHLCAISLDRYWAVSRALEYNSKRTPRRIKCIILTVWLIAAVISLPPLIYKGDQGPQPRGRPQCKLNQEAWYILASSIGSFFAPCLIMILVYLRIYLIAKRSNRRGPRAKGGPGQGESKQPRPDHGGALASAKLPALASVASAREVNGHSKSTGEKEEGETPEDTGTRALPPSWAALPNSGQGQKEGVCGASPEDEAEEEEEEEEEEEECEPQAVPVSPASACSPPLQQPQGSRVLATLRGQVLLGRGVGAIGGQWWRRRAQLTREKRFTFVLAVVIGVFVLCWFPFFFSYSLGAICPKHCKVPHGLFQFFFWIGYCNSSLNPVIYTIFNQDFRRAFRRILCRPWTQTAW	Successful	Synthesis and pharmacologic evaluation of 2-endo-amino-3-exo-isopropylbicyclo[2.2.1]heptane: a potent imidazoline1 receptor specific agent. J Med Chem. 1996 Mar 15;39(6):1193-5.	34	PF00001	.	G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA2B sub-subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction	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	.	P18089
TT2NUT5	Adrenergic receptor alpha-2C (ADRA2C)	P18825	ADA2C_HUMAN	GPCR rhodopsin	Subtype C4; Alpha-2CAR; Alpha-2C adrenoreceptor; Alpha-2C adrenoceptor; Alpha-2C adrenergic receptor; Alpha-2 adrenergic receptor subtype C4; ADRA2RL2; ADRA2L2	ADRA2C	Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins.	.	.	MASPALAAALAVAAAAGPNASGAGERGSGGVANASGASWGPPRGQYSAGAVAGLAAVVGFLIVFTVVGNVLVVIAVLTSRALRAPQNLFLVSLASADILVATLVMPFSLANELMAYWYFGQVWCGVYLALDVLFCTSSIVHLCAISLDRYWSVTQAVEYNLKRTPRRVKATIVAVWLISAVISFPPLVSLYRQPDGAAYPQCGLNDETWYILSSCIGSFFAPCLIMGLVYARIYRVAKLRTRTLSEKRAPVGPDGASPTTENGLGAAAGAGENGHCAPPPADVEPDESSAAAERRRRRGALRRGGRRRAGAEGGAGGADGQGAGPGAAESGALTASRSPGPGGRLSRASSRSVEFFLSRRRRARSSVCRRKVAQAREKRFTFVLAVVMGVFVLCWFPFFFSYSLYGICREACQVPGPLFKFFFWIGYCNSSLNPVIYTVFNQDFRRSFKHILFRRRRRGFRQ	Successful	"Effects of amosulalol, a combined alpha 1- and beta-adrenoceptor-blocking agent, on ischemic myocardial energy metabolism in dogs. J Pharm Sci. 1993 Mar;82(3):291-5."	34	PF00001	.	G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA2C sub-subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction	"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"	.	P18825
TTR6W5O	Adrenergic receptor beta-1 (ADRB1)	P08588	ADRB1_HUMAN	GPCR rhodopsin	Beta-1 adrenoreceptor; Beta-1 adrenoceptor; Beta-1 adrenergic receptor; B1AR; ADRB1R	ADRB1	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.	.	2LSQ	MGAGVLVLGASEPGNLSSAAPLPDGAATAARLLVPASPPASLLPPASESPEPLSQQWTAGMGLLMALIVLLIVAGNVLVIVAIAKTPRLQTLTNLFIMSLASADLVMGLLVVPFGATIVVWGRWEYGSFFCELWTSVDVLCVTASIETLCVIALDRYLAITSPFRYQSLLTRARARGLVCTVWAISALVSFLPILMHWWRAESDEARRCYNDPKCCDFVTNRAYAIASSVVSFYVPLCIMAFVYLRVFREAQKQVKKIDSCERRFLGGPARPPSPSPSPVPAPAPPPGPPRPAAAAATAPLANGRAGKRRPSRLVALREQKALKTLGIIMGVFTLCWLPFFLANVVKAFHRELVPDRLFVFFNWLGYANSAFNPIIYCRSPDFRKAFQRLLCCARRAARRRHATHGDRPRASGCLARPGPPPSPGAASDDDDDDVVGATPPARLLEPWAGCNGGAAADSDSSLDEPCRPGFASESKV	Successful	Binding of beta-adrenoceptor antagonists to rat and rabbit lung: special reference to levobunolol. Arzneimittelforschung. 1984;34(5):579-84.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB1 sub-subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.3.11	The G-protein-coupled receptor (GPCR) Family	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	R-HSA-390696:Adrenoceptors; R-HSA-418555:G alpha (s) signalling events	.	P08588
TTJB8UY	HUMAN beta adrenergic receptor (BAR)	P08588; P07550; P13945	ADRB1_HUMAN; ADRB2_HUMAN; ADRB3_HUMAN	G-protein coupled receptor 1 family	Beta adrenoreceptor	ADRB1	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.	.	.	MGAGVLVLGASEPGNLSSAAPLPDGAATAARLLVPASPPASLLPPASESPEPLSQQWTAGMGLLMALIVLLIVAGNVLVIVAIAKTPRLQTLTNLFIMSLASADLVMGLLVVPFGATIVVWGRWEYGSFFCELWTSVDVLCVTASIETLCVIALDRYLAITSPFRYQSLLTRARARGLVCTVWAISALVSFLPILMHWWRAESDEARRCYNDPKCCDFVTNRAYAIASSVVSFYVPLCIMAFVYLRVFREAQKQVKKIDSCERRFLGGPARPPSPSPSPVPAPAPPPGPPRPAAAAATAPLANGRAGKRRPSRLVALREQKALKTLGIIMGVFTLCWLPFFLANVVKAFHRELVPDRLFVFFNWLGYANSAFNPIIYCRSPDFRKAFQRLLCCARRAARRRHATHGDRPRASGCLARPGPPPSPGAASDDDDDDVVGATPPARLLEPWAGCNGGAAADSDSSLDEPCRPGFASESKV	.	Can beta-adrenergic blockers be used in the treatment of COVID-19 Med Hypotheses. 2020 May 5;142:109809.	.	.	.	.	.	.	.	.	.	.	.	hsa04020: Calcium signaling pathway; hsa04022: cGMP-PKG signaling pathway; hsa04024: cAMP signaling pathway; hsa04080: Neuroactive ligand-receptor interaction; hsa04261: Adrenergic signaling in cardiomyocytes; hsa04540: Gap junction; hsa04923: Regulation of lipolysis in adipocytes; hsa04924: Renin secretion; hsa04970: Salivary secretion; hsa05207: Chemical carcinogenesis - receptor activation; hsa05414: Dilated cardiomyopathy	R-HSA-390696: Adrenoceptors; R-HSA-418555: G alpha (s) signalling events; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production	.	P08588
TTG8ZWP	ADRB2 messenger RNA (ADRB2 mRNA)	P07550	ADRB2_HUMAN	mRNA target	Beta-2 adrenoreceptor (mRNA); Beta-2 adrenoceptor (mRNA); Beta-2 adrenergic receptor (mRNA); B2AR (mRNA); ADRB2R (mRNA)	ADRB2	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.	.	6MXT; 5X7D; 5JQH; 5D6L; 5D5B	MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSGYHVEQEKENKLLCEDLPGTEDFVGHQGTVPSDNIDSQGRNCSTNDSLL	Clinical trial	"In vitro and in vivo efficacy of SYL040012, a novel siRNA compound for treatment of glaucoma. Mol Ther. 2014 Jan;22(1):81-91."	21	mRNA	mRNA target	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	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	R-HSA-390696:Adrenoceptors; R-HSA-418555:G alpha (s) signalling events	.	P07550
TT2CJVK	Adrenergic receptor beta-2 (ADRB2)	P07550	ADRB2_HUMAN	GPCR rhodopsin	Beta-2 adrenoreceptor; Beta-2 adrenoceptor; Beta-2 adrenergic receptor; B2AR; ADRB2R	ADRB2	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.	.	6MXT; 5X7D; 5JQH; 5D6L; 5D5B	MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSGYHVEQEKENKLLCEDLPGTEDFVGHQGTVPSDNIDSQGRNCSTNDSLL	Successful	"Evaluation of a new oral beta2-adrenoceptor stimulant bronchodilator, terbutaline. Pharmacology. 1975;13(3):201-11."	34	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.3.5	The G-protein-coupled receptor (GPCR) Family	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	R-HSA-390696:Adrenoceptors; R-HSA-418555:G alpha (s) signalling events	.	P07550
TTMXGCW	Adrenergic receptor beta-3 (ADRB3)	P13945	ADRB3_HUMAN	GPCR rhodopsin	Beta3AR; Beta3-AR; Beta-3 adrenoreceptor; Beta-3 adrenoceptor; Beta-3 adrenergic receptor; B3AR; ADRB3R	ADRB3	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.	.	2CDW	MAPWPHENSSLAPWPDLPTLAPNTANTSGLPGVPWEAALAGALLALAVLATVGGNLLVIVAIAWTPRLQTMTNVFVTSLAAADLVMGLLVVPPAATLALTGHWPLGATGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGALVTKRCARTAVVLVWVVSAAVSFAPIMSQWWRVGADAEAQRCHSNPRCCAFASNMPYVLLSSSVSFYLPLLVMLFVYARVFVVATRQLRLLRGELGRFPPEESPPAPSRSLAPAPVGTCAPPEGVPACGRRPARLLPLREHRALCTLGLIMGTFTLCWLPFFLANVLRALGGPSLVPGPAFLALNWLGYANSAFNPLIYCRSPDFRSAFRRLLCRCGRRLPPEPCAAARPALFPSGVPAARSSPAQPRLCQRLDGASWGVS	Successful	"Comparison of the beta2-adrenoceptor selectivity of rimiterol, salbutamol and isoprenaline by the intravenous route in man. Br J Clin Pharmacol. 1975 Feb;2(1):41-8."	34	PF00001	.	G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB3 sub-subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04144:Endocytosis; hsa04970:Salivary secretion	R-HSA-390696:Adrenoceptors; R-HSA-418555:G alpha (s) signalling events	.	P13945
TTCFEA1	Alpha-fetoprotein (AFP)	P02771	FETA_HUMAN	Serum albumin family	Alpha-fetoglobulin; Alpha-1-fetoprotein; AFP	AFP	"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."	.	3MRK	MKWVESIFLIFLLNFTESRTLHRNEYGIASILDSYQCTAEISLADLATIFFAQFVQEATYKEVSKMVKDALTAIEKPTGDEQSSGCLENQLPAFLEELCHEKEILEKYGHSDCCSQSEEGRHNCFLAHKKPTPASIPLFQVPEPVTSCEAYEEDRETFMNKFIYEIARRHPFLYAPTILLWAARYDKIIPSCCKAENAVECFQTKAATVTKELRESSLLNQHACAVMKNFGTRTFQAITVTKLSQKFTKVNFTEIQKLVLDVAHVHEHCCRGDVLDCLQDGEKIMSYICSQQDTLSNKITECCKLTTLERGQCIIHAENDEKPEGLSPNLNRFLGDRDFNQFSSGEKNIFLASFVHEYSRRHPQLAVSVILRVAKGYQELLEKCFQTENPLECQDKGEEELQKYIQESQALAKRSCGLFQKLGEYYLQNAFLVAYTKKAPQLTSSELMAITRKMAATAATCCQLSEDKLLACGEGAADIIIGHLCIRHEMTPVNPGVGQCCTSSYANRRPCFSSLVVDETYVPPAFSDDKFIFHKDLCQAQGVALQTMKQEFLINLVKQKPQITEEQLEAVIADFSGLLEKCCQGQEQEVCFAEEGQKLISKTRAALGV	Clinical trial	"MM-093, a recombinant human alpha-fetoprotein for the potential treatment of rheumatoid arthritis and other autoimmune diseases. Curr Opin Mol Ther. 2007 Dec;9(6):603-10."	21	.	.	.	.	.	.	.	.	.	.	hsa04390:Hippo signaling pathway	R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation	.	P02771
TTMO9HF	Advanced glycosylation end product receptor (AGER)	Q15109	RAGE_HUMAN	Immunoglobulin	Receptor foradvanced glycosylation end products; RAGESEC; RAGE; AGER	AGER	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.	.	5D7F; 4YBH; 4XYN; 4P2Y; 4OI8	MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEEERAELNQSEEPEAGESSTGGP	Clinical trial	Receptor for advanced glycation endproduct modulators: a new therapeutic target in Alzheimer's disease. Expert Opin Investig Drugs. 2015 Mar;24(3):393-9.	25	.	.	.	.	.	.	.	.	.	.	hsa04613: Neutrophil extracellular trap formation; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05415: Diabetic cardiomyopathy; hsa05417: Lipid and atherosclerosis	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	.	Q15109
TTDUDE4	Advanced glycosylation end product-specific receptor messenger RNA (AGER mRNA)	Q15109	RAGE_HUMAN	mRNA target	Receptor for advanced glycosylation end products (mRNA)	AGER	"Cell surface pattern recognition receptor that senses endogenous stress signals with a broad ligand repertoire including advanced glycation end products, S100 proteins, high-mobility group box 1 protein/HMGB1, amyloid beta/APP oligomers, nucleic acids, phospholipids and glycosaminoglycans (PubMed:27572515, PubMed:28515150, PubMed:34743181). Advanced glycosylation end products are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes (PubMed:21565706). These ligands accumulate at inflammatory sites during the pathogenesis of various diseases, including diabetes, vascular complications, neurodegenerative disorders, and cancers and RAGE transduces their binding into pro-inflammatory responses. Upon ligand binding, uses TIRAP and MYD88 as adapters to transduce the signal ultimately leading to the induction or inflammatory cytokines IL6, IL8 and TNFalpha through activation of NF-kappa-B (PubMed:21829704). Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key pro-inflammatory mediators (PubMed:19386136). Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons (PubMed:19906677). ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase (MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. Participates in endothelial albumin transcytosis together with HMGB1 through the RAGE/SRC/Caveolin-1 pathway, leading to endothelial hyperpermeability (PubMed:27572515). Mediates the loading of HMGB1 in extracellular vesicles (EVs) that shuttle HMGB1 to hepatocytes by transferrin-mediated endocytosis and subsequently promote hepatocyte pyroptosis by activating the NLRP3 inflammasome (PubMed:34743181). Promotes also extracellular hypomethylated DNA (CpG DNA) uptake by cells via the endosomal route to activate inflammatory responses (PubMed:24081950, PubMed:28515150). {ECO:0000250|UniProtKB:Q62151, ECO:0000269|PubMed:19906677, ECO:0000269|PubMed:20943659, ECO:0000269|PubMed:21559403, ECO:0000269|PubMed:21565706, ECO:0000269|PubMed:21829704, ECO:0000269|PubMed:24081950, ECO:0000269|PubMed:27572515, ECO:0000269|PubMed:28515150, ECO:0000269|PubMed:34743181}."	.	2E5E;2ENS;2L7U;2LE9;2LMB;2M1K;2MJW;2MOV;3CJJ;3O3U;4LP4;4LP5;4OF5;4OFV;4OI7;4OI8;4P2Y;4XYN;4YBH;5D7F;6VXG;6XQ1;6XQ3;6XQ5;6XQ6;6XQ7;6XQ8;6XQ9;7LML;7LMW	MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEEERAELNQSEEPEAGESSTGGP	Clinical trial	"Clinical pipeline report, company report or official report of Arrowhead Pharmaceuticals"	.	.	.	.	.	.	.	.	.	.	.	hsa:177	R-HSA-445989;R-HSA-879415;R-HSA-933542;	.	Q15109;
TTJETQC	Acylglycerol kinase (AGK)	Q53H12	AGK_HUMAN	Kinase	"hAGK; Multisubstrate lipid kinase; Multiple substrate lipid kinase; MuLK; HsMuLK; Acylglycerol kinase, mitochondrial; AGK"	AGK	"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."	EC 2.7.1.107	.	MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQVKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHVEGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPTQ	Literature-reported	Acylglycerol Kinase Mutated in Sengers Syndrome Is a Subunit of the TIM22 Protein Translocase in Mitochondria. Mol Cell. 2017 Aug 3;67(3):471-483.e7.	.	EC:2.7	.	.	.	.	.	.	.	.	.	hsa00561: Glycerolipid metabolism; hsa01100: Metabolic pathways	R-HSA-1483206: Glycerophospholipid biosynthesis; R-HSA-6802952: Signaling by BRAF and RAF1 fusions	.	Q53H12
TTPL1TK	Lysophosphatidic acid transferase (AGPAT1)	Q99943	PLCA_HUMAN	Acyltransferase	Protein G15; AGPAT1; 1acylsnglycerol3phosphate acyltransferase alpha; 1acylglycerol3phosphate Oacyltransferase 1; 1AGPAT 1; 1AGP acyltransferase 1	AGPAT1	Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.	EC 2.3.1.51	.	MDLWPGAWMLLLLLFLLLLFLLPTLWFCSPSAKYFFKMAFYNGWILFLAVLAIPVCAVRGRNVENMKILRLMLLHIKYLYGIRVEVRGAHHFPPSQPYVVVSNHQSSLDLLGMMEVLPGRCVPIAKRELLWAGSAGLACWLAGVIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGTRNHNGSMLPFKRGAFHLAVQAQVPIVPIVMSSYQDFYCKKERRFTSGQCQVRVLPPVPTEGLTPDDVPALADRVRHSMLTVFREISTDGRGGGDYLKKPGGGG	Literature-reported	Lysophosphatidic acid acyltransferase beta regulates mTOR signaling. PLoS One. 2013 Oct 31;8(10):e78632.	.	.	.	.	.	.	.	.	.	.	.	hsa00561: Glycerolipid metabolism; hsa00564: Glycerophospholipid metabolism; hsa01100: Metabolic pathways; hsa04072: Phospholipase D signaling pathway; hsa04975: Fat digestion and absorption	R-HSA-1483166: Synthesis of PA; R-HSA-163765: ChREBP activates metabolic gene expression	MetaCyc:HS09762-MON	Q99943
TT9AYVR	Lysophosphatidic acid acyltransferase beta (LPAATB)	O15120	PLCB_HUMAN	Acyltransferase	Lysophosphatidic acid acyltransferase-beta; LPAAT-beta; AGPAT2; 1-acylglycerol-3-phosphate O-acyltransferase 2; 1-AGPAT 2; 1-AGP acyltransferase 2	AGPAT2	Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.	EC 2.3.1.51	.	MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENMSIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAKRELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGDLLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAADVPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ	Literature-reported	Lysophosphatidic acid acyltransferase-beta: a novel target for induction of tumour cell apoptosis. Expert Opin Ther Targets. 2003 Oct;7(5):643-61.	.	.	.	.	.	.	.	.	.	.	.	hsa00561: Glycerolipid metabolism; hsa00564: Glycerophospholipid metabolism; hsa01100: Metabolic pathways; hsa04072: Phospholipase D signaling pathway; hsa04975: Fat digestion and absorption	R-HSA-1483166: Synthesis of PA; R-HSA-6798695: Neutrophil degranulation	MetaCyc:HS09990-MON	O15120
TT9K86S	Anterior gradient protein 2 (AG-2)	O95994	AGR2_HUMAN	.	hAG2; Secreted cement gland protein XAG2 homolog; AGR2; AG2	AGR2	"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."	.	2LNT; 2LNS	MEKIPVSAFLLLVALSYTLARDTTVKPGAKKDTKDSRPKLPQTLSRGWGDQLIWTQTYEEALYKSKTSNKPLMIIHHLDECPHSQALKKVFAENKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIMFVDPSLTVRADITGRYSNRLYAYEPADTALLLDNMKKALKLLKTEL	Literature-reported	"Identification, characterization and application of a new peptide against anterior gradient homolog 2 (AGR2). Oncotarget. 2018 Jun 8;9(44):27363-27379."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	O95994
TT4DE1O	Agouti-related protein (AGRP)	O00253	AGRP_HUMAN	Agouti protein	Agouti-related peptide; Agouti related protein; AGRP	AGRP	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.	.	2IQV; 1MR0; 1HYK	MLTAAVLSCALLLALPATRGAQMGLAPMEGIRRPDQALLPELPGLGLRAPLKKTTAEQAEEDLLQEAQALAEVLDLQDREPRSSRRCVRLHESCLGQQVPCCDPCATCYCRFFNAFCYCRKLGTAMNPCSRT	Clinical trial	"Clinical pipeline report, company report or official report of TransTech Pharma (2011)."	21	.	.	.	.	.	.	.	.	.	.	hsa04920:Adipocytokine signaling pathway	"R-HSA-9615017: FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes"	.	O00253
TT5C0UB	Angiotensinogen (AGT)	P01019	ANGT_HUMAN	Serpin protein	Serpin A8; SERPINA8	AGT	"Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis."	.	6I3I; 6I3F; 5XJM; 5M3Y; 5M3X	MRKRAPQSEMAPAGVSLRATILCLLAWAGLAAGDRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQVPFTESACLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLEVTLNRPFLFAVYDQSATALHFLGRVANPLSTA	Literature-reported	Genetic Association Between Angiotensinogen Polymorphisms and Lung Cancer Risk. Medicine (Baltimore). 2015 Sep;94(37):e1250.	.	Serpin	Serpin family	serpin family.	.	.	Serpin (serine protease inhibitor)	PF00079	PF00079; Serpin	.	.	.	R-HSA-1989781: PPARA activates gene expression; R-HSA-2022377: Metabolism of Angiotensinogen to Angiotensins; R-HSA-375276: Peptide ligand-binding receptors; R-HSA-416476: G alpha (q) signalling events; R-HSA-418594: G alpha (i) signalling events	.	P01019
TT866WZ	Angiotensinogen messenger RNA (AGT mRNA)	P01019	ANGT_HUMAN	mRNA target	Serpin A8 (mRNA)	AGT	"Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis. {ECO:0000269|PubMed:10619573, ECO:0000269|PubMed:1132082, ECO:0000269|PubMed:17138938}.; [Angiotensin-2]: Acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate through its action on the sympathetic nervous system, and alters renal sodium and water absorption through its ability to stimulate the zona glomerulosa cells of the adrenal cortex to synthesize and secrete aldosterone (PubMed:10619573, PubMed:17138938). Acts by binding to angiotensin receptors AGTR1 and AGTR2 (PubMed:1567413). Also binds the DEAR/FBXW7-AS1 receptor (By similarity). {ECO:0000250|UniProtKB:P01015, ECO:0000269|PubMed:10619573, ECO:0000269|PubMed:1567413, ECO:0000269|PubMed:17138938}.; [Angiotensin-3]: Stimulates aldosterone release. {ECO:0000269|PubMed:1132082}.; [Angiotensin 1-7]: Is a ligand for the G-protein coupled receptor MAS1 (By similarity). Has vasodilator and antidiuretic effects. Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets (By similarity). {ECO:0000250|UniProtKB:P11859}."	.	1N9U;1N9V;2JP8;2WXW;2X0B;3CK0;3WOO;3WOR;4AA1;4APH;4FYS;5E2Q;5M3X;5M3Y;5XJM;6I3F;6I3I;6JOD;6OS0;7C6A	MRKRAPQSEMAPAGVSLRATILCLLAWAGLAAGDRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQVPFTESACLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLEVTLNRPFLFAVYDQSATALHFLGRVANPLSTA	Clinical trial	"ClinicalTrials.gov (NCT05103332) A Randomized, Double-blind, Placebo-controlled, Multicenter Study to Evaluate the Efficacy and Safety of Zilebesiran Used as Add-on Therapy in Patients With Hypertension Not Adequately Controlled by a Standard of Care Antihypertensive Medication. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1989781;R-HSA-2022377;R-HSA-375276;R-HSA-416476;R-HSA-418594;	.	P01019;
TT8DBY3	Angiotensin II receptor type-1 (AGTR1)	P30556	AGTR1_HUMAN	GPCR rhodopsin	Type-1 angiotensin II receptor; Angiotensin II type-1 receptor; Angiotensin II receptor 1; Angiotensin 1 receptor; AT2R1B; AT2R1; AT1BR; AT1AR; AT1; AGTR1B; AGTR1A	AGTR1	Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Receptor for angiotensin II.	.	6DO1; 4ZUD; 4YAY; 1ZV0	MILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIENTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYEIQKNKPRNDDIFKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKRYFLQLLKYIPPKAKSHSNLSTKMSTLSYRPSDNVSSSTKKPAPCFEVE	Successful	Radioligand binding assays: application of [(125)I]angiotensin II receptor binding. Methods Mol Biol. 2009;552:131-41.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.13.1	The G-protein-coupled receptor (GPCR) Family	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	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events	.	P30556
TTPKMXQ	HUMAN type-1 angiotensin II receptor (AGTR1)	P30556	AGTR1_HUMAN	GPCR rhodopsin	Type-1 angiotensin II receptor; Angiotensin II type-1 receptor; Angiotensin II receptor 1; Angiotensin 1 receptor; AT2R1B; AT2R1; AT1BR; AT1AR; AT1; AGTR1B; AGTR1A	AGTR1	Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Receptor for angiotensin II.	.	6DO1; 4ZUD; 4YAY; 1ZV0	MILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIENTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYEIQKNKPRNDDIFKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKRYFLQLLKYIPPKAKSHSNLSTKMSTLSYRPSDNVSSSTKKPAPCFEVE	.	Coronavirus Disease 2019 (COVID-19) and Cardiovascular Disease: A Viewpoint on the Potential Influence of Angiotensin-Converting Enzyme Inhibitors/Angiotensin Receptor Blockers on Onset and Severity of Severe Acute Respiratory Syndrome Coronavirus 2 Infection. J Am Heart Assoc. 2020 Apr 7;9(7):e016219.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.13.1	The G-protein-coupled receptor (GPCR) Family	hsa04020: Calcium signaling pathway; hsa04022: cGMP-PKG signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04080: Neuroactive ligand-receptor interaction; hsa04261: Adrenergic signaling in cardiomyocytes; hsa04270: Vascular smooth muscle contraction; hsa04371: Apelin signaling pathway; hsa04614: Renin-angiotensin system; hsa04924: Renin secretion; hsa04925: Aldosterone synthesis and secretion; hsa04927: Cortisol synthesis and secretion; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04934: Cushing syndrome; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05415: Diabetic cardiomyopathy	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-416476: G alpha (q) signalling events; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis	.	P30556
TTQVOEI	Angiotensin II receptor type-2 (AGTR2)	P50052	AGTR2_HUMAN	GPCR rhodopsin	Type-2 angiotensin II receptor; Angiotensin II type-2 receptor; Angiotensin II receptor 2; AT2	AGTR2	Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation. Receptor for angiotensin II.	.	5UNH; 5UNG; 5UNF	MKGNSTLATTSKNITSGLHFGLVNISGNNESTLNCSQKPSDKHLDAIPILYYIIFVIGFLVNIVVVTLFCCQKGPKKVSSIYIFNLAVADLLLLATLPLWATYYSYRYDWLFGPVMCKVFGSFLTLNMFASIFFITCMSVDRYQSVIYPFLSQRRNPWQASYIVPLVWCMACLSSLPTFYFRDVRTIEYLGVNACIMAFPPEKYAQWSAGIALMKNILGFIIPLIFIATCYFGIRKHLLKTNSYGKNRITRDQVLKMAAAVVLAFIICWLPFHVLTFLDALAWMGVINSCEVIAVIDLALPFAILLGFTNSCVNPFLYCFVGNRFQQKLRSVFRVPITWLQGKRESMSCRKSSSLREMETFVS	Successful	"The preparation of (perfluoroalkyl)imidazoles as nonpeptide angiotensin II receptor antagonists, Bioorg. Med. Chem. Lett. 3(5):895-898 (1993)."	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04261:Adrenergic signaling in cardiomyocytes; hsa04614:Renin-angiotensin system	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events	.	P50052
TTF5NVW	Alanine glyoxylate aminotransferase (AGXT)	P21549	SPYA_HUMAN	Transaminase	Serine--pyruvate aminotransferase; SPAT; Alanine--glyoxylate aminotransferase; AGT1; AGT	AGXT	"Catalyzes  L-alanine and glyoxylate to  pyruvate and glycine. Participates in alanine and aspartate metabolism and glycine, serine and threonine metabolism."	EC 2.6.1.51	5OG0; 5OFY; 5LUC; 5HHY; 5F9S	MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSFYLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLRIGLLGCNATRENVDRVTEALRAALQHCPKKKL	Literature-reported	Adenovirus-associated virus vector-mediated gene transfer in hemophilia B. N Engl J Med. 2011 Dec 22;365(25):2357-65.	2	.	.	.	.	.	.	.	.	.	.	"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"	R-HSA-389661: Glyoxylate metabolism and glycine degradation; R-HSA-9033241: Peroxisomal protein import	MetaCyc:HS10525-MON	P21549
TTE2KUJ	Adenosylhomocysteinase (AHCY)	P23526	SAHH_HUMAN	Ether bond hydrolase	SAHH; SAH hydrolase; S-adenosyl-L-homocysteine hydrolase	AHCY	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.	EC 3.3.1.1	5W4B; 5W49; 4YVF; 4PGF; 4PFJ	MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYFKDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMSCDGPFKPDHYRY	Literature-reported	Molecular approaches for the treatment of hemorrhagic fever virus infections. Antiviral Res. 1993 Sep;22(1):45-75.	2	EC:3.3	Ether hydrolase	adenosylhomocysteinase family.	3.3.1.1	Acting on ether bonds	"S-adenosyl-L-homocysteine hydrolase; S-adenosyl-L-homocysteine hydrolase, NAD binding domain"	PF05221; PF00670	PF05221; AdoHcyase; PF00670; AdoHcyase_NAD	.	.	hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways	"R-HSA-156581: Methylation; R-HSA-1614635: Sulfur amino acid metabolism; R-HSA-2408508: Metabolism of ingested SeMet, Sec, MeSec into H2Se; R-HSA-5578997: Defective AHCY causes HMAHCHD"	MetaCyc:HS02273-MON	P23526
TT037IE	Aryl hydrocarbon receptor (AHR)	P35869	AHR_HUMAN	.	bHLHe76; Class E basic helixloophelix protein 76; Class E basic helix-loop-helix protein 76; AhR; Ah receptor	AHR	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.	.	5NJ8	MNSSSANITYASRKRRKPVQKTVKPIPAEGIKSNPSKRHRDRLNTELDRLASLLPFPQDVINKLDKLSVLRLSVSYLRAKSFFDVALKSSPTERNGGQDNCRAANFREGLNLQEGEFLLQALNGFVLVVTTDALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALNPSQCTESGQGIEEATGLPQTVVCYNPDQIPPENSPLMERCFICRLRCLLDNSSGFLAMNFQGKLKYLHGQKKKGKDGSILPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPIGCDAKGRIVLGYTEAELCTRGSGYQFIHAADMLYCAESHIRMIKTGESGMIVFRLLTKNNRWTWVQSNARLLYKNGRPDYIIVTQRPLTDEEGTEHLRKRNTKLPFMFTTGEAVLYEATNPFPAIMDPLPLRTKNGTSGKDSATTSTLSKDSLNPSSLLAAMMQQDESIYLYPASSTSSTAPFENNFFNESMNECRNWQDNTAPMGNDTILKHEQIDQPQDVNSFAGGHPGLFQDSKNSDLYSIMKNLGIDFEDIRHMQNEKFFRNDFSGEVDFRDIDLTDEILTYVQDSLSKSPFIPSDYQQQQSLALNSSCMVQEHLHLEQQQQHHQKQVVVEPQQQLCQKMKHMQVNGMFENWNSNQFVPFNCPQQDPQQYNVFTDLHGISQEFPYKSEMDSMPYTQNFISCNQPVLPQHSKCTELDYPMGSFEPSPYPTTSSLEDFVTCLQLPENQKHGLNPQSAIITPQTCYAGAVSMYQCQPEPQHTHVGQMQYNPVLPGQQAFLNKFQNGVLNETYPAELNNINNTQTTTHLQPLHHPSEARPFPDLTSSGFL	Successful	"A Phase I study of the angiogenesis inhibitor SU5416 (semaxanib) in solid tumours, incorporating dynamic contrast MR pharmacodynamic end points. Br J Cancer. 2005 Oct 17;93(8):876-83."	34	.	.	.	.	.	Helix-loop-helix DNA-binding domain; PAS fold; PAS fold	PF00010; PF00989; PF08447	PF00010; HLH; PF00989; PAS; PF08447; PAS_3	.	.	hsa04659: Th17 cell differentiation; hsa04934: Cushing syndrome; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species	R-HSA-1989781: PPARA activates gene expression; R-HSA-211945: Phase I - Functionalization of compounds; R-HSA-211976: Endogenous sterols; R-HSA-211981: Xenobiotics; R-HSA-8937144: Aryl hydrocarbon receptor signalling	.	P35869
TTKF4WV	Connecting peptide (C-peptide)	P02765 (301-340)	FETUA_HUMAN	Fetuin family	Fetuin-A; Alpha-2-Z-globulin; Alpha-2-HS-glycoprotein chainB; Alpha-2-HS-glycoprotein (301-340); AHSG	AHSG	"Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions."	.	.	LAAPPGHQLHRAHYDLRHTFMGVVSLGSPSGEVSHPRKTR	Clinical trial	ClinicalTrials.gov (NCT01681290) Safety and Efficacy of CBX129801 in Patients With Type 1 Diabetes. U.S. National Institutes of Health.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	P02765
TT43L8U	Alpha-2-HS-glycoprotein (AHSG)	P02765	FETUA_HUMAN	Fetuin family	PRO2743; Ba-alpha-2-glycoprotein; Alpha2-HS glycoprotein	AHSG	"Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions."	.	.	MKSLVLLLCLAQLWGCHSAPHGPGLIYRQPNCDDPETEEAALVAIDYINQNLPWGYKHTLNQIDEVKVWPQQPSGELFEIEIDTLETTCHVLDPTPVARCSVRQLKEHAVEGDCDFQLLKLDGKFSVVYAKCDSSPDSAEDVRKVCQDCPLLAPLNDTRVVHAAKAALAAFNAQNNGSNFQLEEISRAQLVPLPPSTYVEFTVSGTDCVAKEATEAAKCNLLAEKQYGFCKATLSEKLGGAEVAVTCMVFQTQPVSSQPQPEGANEAVPTPVVDPDAPPSPPLGAPGLPPAGSPPDSHVLLAAPPGHQLHRAHYDLRHTFMGVVSLGSPSGEVSHPRKTRTVVQPSVGAAAGPVVPPCPGRIRHFKV	Literature-reported	The use of biomarkers for assessing HAART-associated renal toxicity in HIV-infected patients. Curr HIV Res. 2012 Sep;10(6):521-31.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-114608: Platelet degranulation; R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-6798695: Neutrophil degranulation; R-HSA-8957275: Post-translational protein phosphorylation	.	P02765
TTKRTP6	Cytosine deaminase (AICDA)	Q9GZX7	AICDA_HUMAN	Carbon-nitrogen hydrolase	Activationinduced cytidine deaminase; AICDA	AICDA	"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."	EC 3.5.4.38	5W1C; 5W0Z; 5W0U; 5W0R; 5JJ4	MDSLLMNRRKFLYQFKNVRWAKGRRETYLCYVVKRRDSATSFSLDFGYLRNKNGCHVELLFLRYISDWDLDPGRCYRVTWFTSWSPCYDCARHVADFLRGNPNLSLRIFTARLYFCEDRKAEPEGLRRLHRAGVQIAIMTFKDYFYCWNTFVENHERTFKAWEGLHENSVRLSRQLRRILLPLYEVDDLRDAFRTLGL	Clinical trial	Micromanaging oncolytic viruses. SciBX 1(42); doi:10.1038/scibx.2008.1014. Nov. 20 2008	17	.	.	.	.	.	.	.	.	.	.	hsa04672:Intestinal immune network for IgA production; hsa05340:Primary immunodeficiency	.	.	Q9GZX7
TT12MEP	Allograft inflammatory factor-1 (AIF1)	P55008	AIF1_HUMAN	.	Protein G1; Ionized calciumbinding adapter molecule 1; Allograft inflammatory factor 1; AIF1	AIF1	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.	.	2G2B; 2D58	MSQTRDLQGGKAFGLLKAQQEERLDEINKQFLDDPKYSSDEDLPSKLEGFKEKYMEFDLNGNGDIDIMSLKRMLEKLGVPKTHLELKKLIGEVSSGSGETFSYPDFLRMMLGKRSAILKMILMYEEKAREKEKPTGPPAKKAISELP	Literature-reported	"Allograft Inflammatory Factor-1 Links T-Cell Activation, Interferon Response, and Macrophage Activation in Chronic Kawasaki Disease Arteritis. J Pediatric Infect Dis Soc. 2017 Sep 1;6(3):e94-e102."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P55008
TTXWHGF	AIMP multisynthetase complex protein 2 (AIMP2)	Q13155	AIMP2_HUMAN	.	Protein JTV-1; PRO0992; Multisynthase complex auxiliary component p38; JTV1; Aminoacyl tRNA synthase complex-interacting multifunctional protein 2	AIMP2	"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."	.	6ILD; 5Y6L; 5A5H; 5A34; 5A1N	MPMYQVKPYHGGGAPLRVELPTCMYRLPNVHGRSYGPAPGAGHVQEESNLSLQALESRQDDILKRLYELKAAVDGLSKMIQTPDADLDVTNIIQADEPTTLTTNALDLNSVLGKDYGALKDIVINANPASPPLSLLVLHRLLCEHFRVLSTVHTHSSVKSVPENLLKCFGEQNKKQPRQDYQLGFTLIWKNVPKTQMKFSIQTMCPIEGEGNIARFLFSLFGQKHNAVNATLIDSWVDIAIFQLKEGSSKEKAAVFRSMNSALGKSPWLAGNELTVADVVLWSVLQQIGGCSVTVPANVQRWMRSCENLAPFNTALKLLK	Literature-reported	Oncogenic Mutation of AIMP2/p38 Inhibits Its Tumor-Suppressive Interaction with Smurf2. Cancer Res. 2016 Jun 1;76(11):3422-36.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2408522: Selenoamino acid metabolism; R-HSA-379716: Cytosolic tRNA aminoacylation	.	Q13155
TTFBNVI	Aldose reductase (AKR1B1)	P15121	ALDR_HUMAN	Short-chain dehydrogenases reductase	Aldehyde reductase; AKR1B1	AKR1B1	Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.	EC 1.1.1.300	6F8O; 6F84; 6F82; 6F81; 6F7R	MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALLSCTSHKDYPFHEEF	Successful	"Inhibition of human lens aldose reductase by flavonoids, sulindac and indomethacin. Biochem Pharmacol. 1983 Jul 1;32(13):1995-8."	34	.	.	.	.	.	.	.	.	.	.	hsa00040:Pentose and glucuronate interconversions; hsa00051:Fructose and mannose metabolism; hsa00052:Galactose metabolism; hsa00561:Glycerolipid metabolism; hsa01100:Metabolic pathways	R-HSA-196108: Pregnenolone biosynthesis; R-HSA-5652227: Fructose biosynthesis	MetaCyc:HS01502-MON	P15121
TT5ZWB6	Dihydrodiol dehydrogenase type I (AKR1C3)	P42330	AK1C3_HUMAN	Short-chain dehydrogenases reductase	"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"	AKR1C3	"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."	EC 1.-.-.-	6GXK; 6F78; 6F2U; 5JM5; 5HNU	MDSKHQCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYFNSDSFASHPNYPYSDEY	Successful	"Ouellet M, Percival MD: Effect of inhibitor time-dependency on selectivity towards cyclooxygenase isoforms. Biochem J. 1995 Feb 15;306 ( Pt 1):247-51."	34	.	CH CH donor oxidoreductase	aldo/keto reductase family.	1.-.-.-	Oxidoreductases	Aldo/keto reductase family	PF00248	PF00248; Aldo_ket_red	.	.	hsa00140:Steroid hormone biosynthesis; hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways; hsa04913:Ovarian steroidogenesis	R-HSA-975634:Retinoid metabolism and transport	MetaCyc:HS03054-MON	P42330
TTWTSCV	RAC-alpha serine/threonine-protein kinase (AKT1)	P31749	AKT1_HUMAN	Kinase	RAC-PK-alpha; RAC; Proto-oncogene c-Akt; Protein kinase B alpha; PKB alpha	AKT1	"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."	EC 2.7.11.1	6NPZ; 6HHJ; 6HHI; 6HHH; 6HHG	MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA	Clinical trial	"Clinical pipeline report, company report or official report of Genentech (2011)."	25	EC:2.7	Kinase	protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.	2.7.11.1	Transferring phosphorus-containing groups	PH domain; Protein kinase domain; Protein kinase C terminal domain	PF00169; PF00069; PF00433	PF00169; PH; PF00069; Pkinase; PF00433; Pkinase_C	.	.	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	"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"	.	P31749
TTOQGR3	AKT1 messenger RNA (AKT1 mRNA)	P31749	AKT1_HUMAN	mRNA target	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)	AKT1	"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."	EC 2.7.11.1	6NPZ; 6HHJ; 6HHI; 6HHH; 6HHG	MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA	Literature-reported	AKT1 and AKT2 isoforms play distinct roles during breast cancer progression through the regulation of specific downstream proteins. Sci Rep. 2017 Mar 13;7:44244.	.	mRNA	mRNA target	.	.	.	PH domain; Protein kinase domain; Protein kinase C terminal domain	PF00169; PF00069; PF00433	PF00169; PH; PF00069; Pkinase; PF00433; Pkinase_C	.	.	"hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa01522: Endocrine resistance; hsa01524: Platinum drug resistance; 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; hsa04072: Phospholipase D signaling pathway; hsa04140: Autophagy - animal; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04152: AMPK signaling pathway; hsa04210: Apoptosis; hsa04211: Longevity regulating pathway; hsa04213: Longevity regulating pathway - multiple species; hsa04218: Cellular senescence; hsa04261: Adrenergic signaling in cardiomyocytes; hsa04370: VEGF signaling pathway; hsa04371: Apelin signaling pathway; hsa04380: Osteoclast differentiation; hsa04510: Focal adhesion; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04611: Platelet activation; hsa04613: Neutrophil extracellular trap formation; hsa04620: Toll-like receptor signaling pathway; hsa04625: C-type lectin 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; hsa04926: Relaxin signaling pathway; hsa04929: GnRH secretion; hsa04931: Insulin resistance; hsa04932: Non-alcoholic fatty liver disease; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04935: Growth hormone synthesis, secretion and action; hsa04936: Alcoholic liver disease; hsa04973: Carbohydrate digestion and absorption; hsa05010: Alzheimer disease; hsa05017: Spinocerebellar ataxia; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05135: Yersinia infection; hsa05142: Chagas disease; hsa05145: Toxoplasmosis; hsa05152: Tuberculosis; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05162: Measles; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; hsa05165: Human papillomavirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; 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; 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; hsa05415: Diabetic cardiomyopathy; hsa05417: Lipid and atherosclerosis; hsa05418: Fluid shear stress and atherosclerosis"	"R-HSA-111447: Activation of BAD and translocation to mitochondria; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1358803: Downregulation of ERBB2:ERBB3 signaling; R-HSA-1445148: Translocation of SLC2A4 (GLUT4) to the plasma membrane; R-HSA-1474151: Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation; R-HSA-165159: MTOR signalling; 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 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-450385: Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA; 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; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6804757: Regulation of TP53 Degradation; R-HSA-6804758: Regulation of TP53 Activity through Acetylation; R-HSA-6804759: Regulation of TP53 Activity through Association with Co-factors; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-69202: Cyclin E associated events during G1/S transition; R-HSA-69656: Cyclin A:Cdk2-associated events at S phase entry; R-HSA-8849469: PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1; R-HSA-8876198: RAB GEFs exchange GTP for GDP on RABs; R-HSA-8941332: RUNX2 regulates genes involved in cell migration; R-HSA-8948751: Regulation of PTEN stability and activity; R-HSA-9009391: Extra-nuclear estrogen signaling; R-HSA-9604323: Negative regulation of NOTCH4 signaling; R-HSA-9607240: FLT3 Signaling; R-HSA-9614399: Regulation of localization of FOXO transcription factors; R-HSA-9634638: Estrogen-dependent nuclear events downstream of ESR-membrane signaling; R-HSA-9755511: KEAP1-NFE2L2 pathway; R-HSA-9755779: SARS-CoV-2 targets host intracellular signalling and regulatory pathways"	.	P31749
TT2MN5K	Phosphorylated protein kinase B (pAKT)	P31749; P31751; Q9Y243	AKT1_HUMAN; AKT2_HUMAN; AKT3_HUMAN	Kinase	RAC-serine/threonine-protein kinase; RAC-PK; Protein kinase B; Protein kinase Akt; PKB	AKT1	"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."	.	.	MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA	Clinical trial	"Clinical pipeline report, company report or official report of MetronomX."	21	.	.	.	.	.	.	.	.	.	.	"hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa01522: Endocrine resistance; hsa01524: Platinum drug resistance; 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; hsa04072: Phospholipase D signaling pathway; hsa04140: Autophagy - animal; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04152: AMPK signaling pathway; hsa04210: Apoptosis; hsa04211: Longevity regulating pathway; hsa04213: Longevity regulating pathway - multiple species; hsa04218: Cellular senescence; hsa04261: Adrenergic signaling in cardiomyocytes; hsa04370: VEGF signaling pathway; hsa04371: Apelin signaling pathway; hsa04380: Osteoclast differentiation; hsa04510: Focal adhesion; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04611: Platelet activation; hsa04613: Neutrophil extracellular trap formation; hsa04620: Toll-like receptor signaling pathway; hsa04625: C-type lectin 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; hsa04926: Relaxin signaling pathway; hsa04929: GnRH secretion; hsa04931: Insulin resistance; hsa04932: Non-alcoholic fatty liver disease; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04935: Growth hormone synthesis, secretion and action; hsa04936: Alcoholic liver disease; hsa04973: Carbohydrate digestion and absorption; hsa05010: Alzheimer disease; hsa05017: Spinocerebellar ataxia; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05135: Yersinia infection; hsa05142: Chagas disease; hsa05145: Toxoplasmosis; hsa05152: Tuberculosis; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05162: Measles; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; hsa05165: Human papillomavirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; 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; 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; hsa05415: Diabetic cardiomyopathy; hsa05417: Lipid and atherosclerosis; hsa05418: Fluid shear stress and atherosclerosis"	"R-HSA-111447: Activation of BAD and translocation to mitochondria; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1358803: Downregulation of ERBB2:ERBB3 signaling; R-HSA-1445148: Translocation of SLC2A4 (GLUT4) to the plasma membrane; R-HSA-1474151: Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation; R-HSA-165159: MTOR signalling; 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 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-450385: Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA; 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; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6804757: Regulation of TP53 Degradation; R-HSA-6804758: Regulation of TP53 Activity through Acetylation; R-HSA-6804759: Regulation of TP53 Activity through Association with Co-factors; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-69202: Cyclin E associated events during G1/S transition; R-HSA-69656: Cyclin A:Cdk2-associated events at S phase entry; R-HSA-8849469: PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1; R-HSA-8876198: RAB GEFs exchange GTP for GDP on RABs; R-HSA-8941332: RUNX2 regulates genes involved in cell migration; R-HSA-8948751: Regulation of PTEN stability and activity; R-HSA-9009391: Extra-nuclear estrogen signaling; R-HSA-9604323: Negative regulation of NOTCH4 signaling; R-HSA-9607240: FLT3 Signaling; R-HSA-9614399: Regulation of localization of FOXO transcription factors; R-HSA-9634638: Estrogen-dependent nuclear events downstream of ESR-membrane signaling; R-HSA-9755511: KEAP1-NFE2L2 pathway; R-HSA-9755779: SARS-CoV-2 targets host intracellular signalling and regulatory pathways"	.	P31749
TTH24WI	RAC-beta serine/threonine-protein kinase (AKT2)	P31751	AKT2_HUMAN	Kinase	RAC-PK-beta; Protein kinase B beta; Protein kinase Akt-2; PKB beta	AKT2	"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."	EC 2.7.11.1	3E8D; 3D0E; 3.00E+88; 3.00E+87; 2XH5	MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPMDYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGLLELDQRTHFPQFSYSASIRE	Literature-reported	"Molecular pharmacology and antitumor activity of PHT-427, a novel Akt/phosphatidylinositide-dependent protein kinase 1 pleckstrin homology domain inhibitor. Mol Cancer Ther. 2010 Mar;9(3):706-17."	0	EC:2.7	Kinase	protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.	2.7.11.1	Transferring phosphorus-containing groups	PH domain; Protein kinase domain; Protein kinase C terminal domain	PF00169; PF00069; PF00433	PF00169; PH; PF00069; Pkinase; PF00433; Pkinase_C	.	.	"hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa01522: Endocrine resistance; hsa01524: Platinum drug resistance; 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; hsa04072: Phospholipase D signaling pathway; hsa04140: Autophagy - animal; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04152: AMPK signaling pathway; hsa04210: Apoptosis; hsa04211: Longevity regulating pathway; hsa04213: Longevity regulating pathway - multiple species; hsa04218: Cellular senescence; hsa04261: Adrenergic signaling in cardiomyocytes; hsa04370: VEGF signaling pathway; hsa04371: Apelin signaling pathway; hsa04380: Osteoclast differentiation; hsa04510: Focal adhesion; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04611: Platelet activation; hsa04613: Neutrophil extracellular trap formation; hsa04620: Toll-like receptor signaling pathway; hsa04625: C-type lectin 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; hsa04926: Relaxin signaling pathway; hsa04929: GnRH secretion; hsa04931: Insulin resistance; hsa04932: Non-alcoholic fatty liver disease; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04935: Growth hormone synthesis, secretion and action; hsa04936: Alcoholic liver disease; hsa04973: Carbohydrate digestion and absorption; hsa05010: Alzheimer disease; hsa05017: Spinocerebellar ataxia; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05135: Yersinia infection; hsa05142: Chagas disease; hsa05145: Toxoplasmosis; hsa05152: Tuberculosis; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05162: Measles; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; hsa05165: Human papillomavirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; 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; 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; hsa05415: Diabetic cardiomyopathy; hsa05417: Lipid and atherosclerosis; hsa05418: Fluid shear stress and atherosclerosis"	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	.	P31751
TTO6SGY	AKT3 messenger RNA (AKT3 mRNA)	Q9Y243	AKT3_HUMAN	mRNA target	STK-2 (mRNA); RAC-PK-gamma (mRNA); Protein kinase B gamma (mRNA); Protein kinase Akt-3 (mRNA); PKBG (mRNA); PKB gamma (mRNA)	AKT3	"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."	EC 2.7.11.1	2X18	MSDVTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVADRLQRQEEERMNCSPTSQIDNIGEEEMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE	Literature-reported	"US patent application no. 6,187,586, Antisense modulation of AKT-3 expression."	0	mRNA	mRNA target	.	.	.	PH domain; Protein kinase domain; Protein kinase C terminal domain	PF00169; PF00069; PF00433	PF00169; PH; PF00069; Pkinase; PF00433; Pkinase_C	.	.	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	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	.	Q9Y243
TTAZ05C	RAC-gamma serine/threonine-protein kinase (AKT3)	Q9Y243	AKT3_HUMAN	Kinase	STK-2; RAC-PK-gamma; Protein kinase B gamma; Protein kinase Akt-3; PKBG; PKB gamma	AKT3	"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."	EC 2.7.11.1	2X18	MSDVTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVADRLQRQEEERMNCSPTSQIDNIGEEEMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE	Clinical trial	Inhibiting the akt pathway in cancer treatment: three leading candidates. P T. 2011 Apr;36(4):225-7.	21	EC:2.7	Kinase	protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.	2.7.11.1	Transferring phosphorus-containing groups	PH domain; Protein kinase domain; Protein kinase C terminal domain	PF00169; PF00069; PF00433	PF00169; PH; PF00069; Pkinase; PF00433; Pkinase_C	.	.	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	R-HSA-111447: Activation of BAD and translocation to mitochondria; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1358803: Downregulation of ERBB2:ERBB3 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; R-HSA-6804757: Regulation of TP53 Degradation; R-HSA-6804758: Regulation of TP53 Activity through Acetylation; R-HSA-6804759: Regulation of TP53 Activity through Association with Co-factors; R-HSA-69202: Cyclin E associated events during G1/S transition; R-HSA-69656: Cyclin A:Cdk2-associated events at S phase entry; R-HSA-8876198: RAB GEFs exchange GTP for GDP on RABs; R-HSA-8941332: RUNX2 regulates genes involved in cell migration; R-HSA-8948751: Regulation of PTEN stability and activity; R-HSA-9607240: FLT3 Signaling; R-HSA-9614399: Regulation of localization of FOXO transcription factors; R-HSA-9634638: Estrogen-dependent nuclear events downstream of ESR-membrane signaling; R-HSA-9755511: KEAP1-NFE2L2 pathway; R-HSA-9755779: SARS-CoV-2 targets host intracellular signalling and regulatory pathways	.	Q9Y243
TTJHKYD	Delta-aminolevulinic acid dehydratase (ALAD)	P13716	HEM2_HUMAN	Alpha-carbonic anhydrase	Porphobilinogen synthase; Delta-aminolevulinate dehydratase; ALADH; ALAD	ALAD	"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."	EC 4.2.1.24	5HNR; 5HMS; 1PV8; 1.00E+51	MQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPITSLPGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVKPGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEAMTAFRRAGADIIITYYTPQLLQWLKEE	Successful	Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9.	34	.	.	.	.	.	.	.	.	.	.	hsa00860:Porphyrin and chlorophyll metabolism; hsa01100:Metabolic pathways	R-HSA-189451: Heme biosynthesis; R-HSA-6798695: Neutrophil degranulation	MetaCyc:HS07501-MON	P13716
TTG1FXO	ALAS1 messenger RNA (ALAS1 mRNA)	P13196	HEM1_HUMAN	.	ALAS-H; 5-aminolevulinic acid synthase 1; Delta-ALA synthase 1; Delta-aminolevulinate synthase 1	ALAS1	.	EC 2.3.1.37	.	MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKETPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGSSVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPERVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLITKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLELKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health  Human Services. 2019	.	.	.	.	.	.	.	.	.	.	.	"hsa00260: Glycine, serine and threonine metabolism; hsa00860: Porphyrin metabolism; hsa01100: Metabolic pathways; hsa01240: Biosynthesis of cofactors"	R-HSA-189451: Heme biosynthesis; R-HSA-1989781: PPARA activates gene expression; R-HSA-2151201: Transcriptional activation of mitochondrial biogenesis	MetaCyc:HS00424-MON	P13196
TTFNGC9	Serum albumin (ALB)	P02768	ALBU_HUMAN	.	Serum albumin	ALB	"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."	.	6JE7; 6EZQ; 6A7P; 5Z0B; 5YOQ	MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL	Successful	Protocol design for high relaxivity contrast agents in MR imaging of the CNS. Eur Radiol. 2006 Nov;16 Suppl 7:M3-7.	34	.	Serum albumin	ALB/AFP/VDB family.	.	.	Serum albumin family	PF00273	PF00273; Serum_albumin	.	.	hsa04918: Thyroid hormone synthesis	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	.	P02768
TT2AFT6	Activated leukocyte cell adhesionmolecule (ALCAM)	Q13740	CD166_HUMAN	Basigin protein	MEMD; CD166 antigen; CD166; Activated leukocyte cell adhesion molecule	ALCAM	"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."	.	5A2F; 1KJC	MESKGASSCRLLFCLLISATVFRPGLGWYTVNSAYGDTIIIPCRLDVPQNLMFGKWKYEKPDGSPVFIAFRSSTKKSVQYDDVPEYKDRLNLSENYTLSISNARISDEKRFVCMLVTEDNVFEAPTIVKVFKQPSKPEIVSKALFLETEQLKKLGDCISEDSYPDGNITWYRNGKVLHPLEGAVVIIFKKEMDPVTQLYTMTSTLEYKTTKADIQMPFTCSVTYYGPSGQKTIHSEQAVFDIYYPTEQVTIQVLPPKNAIKEGDNITLKCLGNGNPPPEEFLFYLPGQPEGIRSSNTYTLTDVRRNATGDYKCSLIDKKSMIASTAITVHYLDLSLNPSGEVTRQIGDALPVSCTISASRNATVVWMKDNIRLRSSPSFSSLHYQDAGNYVCETALQEVEGLKKRESLTLIVEGKPQIKMTKKTDPSGLSKTIICHVEGFPKPAIQWTITGSGSVINQTEESPYINGRYYSKIIISPEENVTLTCTAENQLERTVNSLNVSAISIPEHDEADEISDENREKVNDQAKLIVGIVVGLLLAALVAGVVYWLYMKKSKTASKHVNKDLGNMEENKKLEENNHKTEA	Clinical trial	MiR-148a and miR-152 reduce tamoxifen resistance in ER+ breast cancer via downregulating ALCAM. Biochem Biophys Res Commun. 2017 Feb 5;483(2):840-846.	.	TC=8.A.23	.	.	.	.	CD80-like C2-set immunoglobulin domain 	PF08205	PF08205; C2-set_2	8.A.23.1.10	The Basigin (Basigin) Family	hsa04514: Cell adhesion molecules	R-HSA-373760: L1CAM interactions	.	Q13740
TTCTAOJ	Acetaldehyde dehydrogenase (ALDH)	P00352; P05091; P30837	AL1A1_HUMAN; ALDH2_HUMAN; AL1B1_HUMAN	Aldehyde/oxo donor oxidoreductase	Aldehyde dehydrogenase; ALDH	ALDH1A1	"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."	.	.	MSSSGTPDLPVLLTDLKIQYTKIFINNEWHDSVSGKKFPVFNPATEEELCQVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGRLLYKLADLIERDRLLLATMESMNGGKLYSNAYLNDLAGCIKTLRYCAGWADKIQGRTIPIDGNFFTYTRHEPIGVCGQIIPWNFPLVMLIWKIGPALSCGNTVVVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVLADADLDNAVEFAHHGVFYHQGQCCIAASRIFVEESIYDEFVRRSVERAKKYILGNPLTPGVTQGPQIDKEQYDKILDLIESGKKEGAKLECGGGPWGNKGYFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTFYGLSAGVFTKDIDKAITISSALQAGTVWVNCYGVVSAQCPFGGFKMSGNGRELGEYGFHEYTEVKTVTVKISQKNS	Successful	"Disulfiram and calcium carbimide. Mode of action, adverse effects and clinical use. Tidsskr Nor Laegeforen. 1990 Apr 10;110(10):1224-8."	34	.	.	.	.	.	.	.	.	.	.	hsa00830: Retinol metabolism; hsa01100: Metabolic pathways	R-HSA-5365859: RA biosynthesis pathway; R-HSA-70350: Fructose catabolism; R-HSA-71384: Ethanol oxidation	MetaCyc:HS09183-MON	P00352
TTFLN4T	Mitochondrial aldehyde dehydrogenase (ALDH2)	P05091	ALDH2_HUMAN	Aldehyde/oxo donor oxidoreductase	"Aldehyde dehydrogenase, mitochondrial; ALDM; ALDHI; ALDH-E2; ALDH class 2"	ALDH2	"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."	EC 1.2.1.3	5L13; 4KWG; 4KWF; 4FR8; 4FQF	MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS	Clinical trial	A novel aldehyde dehydrogenase-3 activator leads to adult salivary stem cell enrichment in vivo. Clin Cancer Res. 2011 Dec 1;17(23):7265-72.	21	.	.	.	.	.	.	.	.	.	.	"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"	R-HSA-380612: Metabolism of serotonin; R-HSA-71384: Ethanol oxidation	MetaCyc:MON66-302	P05091
TTB6UM0	Fatty aldehyde dehydrogenase (ALDH3A2)	P51648	AL3A2_HUMAN	Aldehyde/oxo donor oxidoreductase	Microsomal aldehyde dehydrogenase; Aldehyde dehydrogenase family 3 member A2; Aldehyde dehydrogenase 10; ALDH10	ALDH3A2	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.	EC 1.2.1.3	4QGK	MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQEVITVLGEIDFMLENLPEWVTAKPVKKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELLKQRFDHIFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQTCIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLALYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRPCLLKSLKREGANKLRYPPNSQSKVDWGKFFLLKRFNKEKLGLLLLTFLGIVAAVLVKAEYY	Successful	Pharmacological treatment of alcohol dependence: target symptoms and target mechanisms. Pharmacol Ther. 2006 Sep;111(3):855-76.	34	.	.	.	.	.	.	.	.	.	.	"hsa00010: Glycolysis / Gluconeogenesis; 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; hsa00770: Pantothenate and CoA biosynthesis; hsa01100: Metabolic pathways; hsa01240: Biosynthesis of cofactors; hsa04936: Alcoholic liver disease"	R-HSA-1660661: Sphingolipid de novo biosynthesis; R-HSA-389599: Alpha-oxidation of phytanate; R-HSA-9603798: Class I peroxisomal membrane protein import; R-HSA-9609523: Insertion of tail-anchored proteins into the endoplasmic reticulum membrane; R-HSA-9696270: RND2 GTPase cycle; R-HSA-9696273: RND1 GTPase cycle	MetaCyc:HS01061-MON	P51648
TTJUWVB	Succinate-semialdehyde dehydrogenase (ALDH5A1)	P51649	SSDH_HUMAN	Aldehyde/oxo donor oxidoreductase	"Succinic dehydrogenase; Succinate-semialdehyde dehydrogenase, mitochondrial; SSADH; NAD(+)-dependent succinic semialdehyde dehydrogenase; Aldehyde dehydrogenase family 5 member A1"	ALDH5A1	Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA).	EC 1.2.1.24	2W8R; 2W8Q; 2W8P; 2W8O; 2W8N	MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGRLAGLSAALLRTDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL	Successful	Redox-switch modulation of human SSADH by dynamic catalytic loop. EMBO J. 2009 Apr 8;28(7):959-68.	34	EC:1.2	Oxidoreductases acting on aldehyde or oxo group of donors	aldehyde dehydrogenase family.	1.2.1.24	Acting on the aldehyde or oxo group of donors	Aldehyde dehydrogenase family	PF00171	PF00171; Aldedh	.	.	"hsa00250:Alanine, aspartate and glutamate metabolism; hsa00650:Butanoate metabolism; hsa01100:Metabolic pathways"	R-HSA-916853: Degradation of GABA	MetaCyc:HS03550-MON	P51649
TTPMQSO	ALK tyrosine kinase receptor (ALK)	Q9UM73	ALK_HUMAN	Kinase	CD246; Anaplastic lymphoma kinase	ALK	"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."	EC 2.7.10.1	6MX8; 6EDL; 6EBW; 6E0R; 6CDT	MGAIGLLWLLPLLLSTAAVGSGMGTGQRAGSPAAGPPLQPREPLSYSRLQRKSLAVDFVVPSLFRVYARDLLLPPSSSELKAGRPEARGSLALDCAPLLRLLGPAPGVSWTAGSPAPAEARTLSRVLKGGSVRKLRRAKQLVLELGEEAILEGCVGPPGEAAVGLLQFNLSELFSWWIRQGEGRLRIRLMPEKKASEVGREGRLSAAIRASQPRLLFQIFGTGHSSLESPTNMPSPSPDYFTWNLTWIMKDSFPFLSHRSRYGLECSFDFPCELEYSPPLHDLRNQSWSWRRIPSEEASQMDLLDGPGAERSKEMPRGSFLLLNTSADSKHTILSPWMRSSSEHCTLAVSVHRHLQPSGRYIAQLLPHNEAAREILLMPTPGKHGWTVLQGRIGRPDNPFRVALEYISSGNRSLSAVDFFALKNCSEGTSPGSKMALQSSFTCWNGTVLQLGQACDFHQDCAQGEDESQMCRKLPVGFYCNFEDGFCGWTQGTLSPHTPQWQVRTLKDARFQDHQDHALLLSTTDVPASESATVTSATFPAPIKSSPCELRMSWLIRGVLRGNVSLVLVENKTGKEQGRMVWHVAAYEGLSLWQWMVLPLLDVSDRFWLQMVAWWGQGSRAIVAFDNISISLDCYLTISGEDKILQNTAPKSRNLFERNPNKELKPGENSPRQTPIFDPTVHWLFTTCGASGPHGPTQAQCNNAYQNSNLSVEVGSEGPLKGIQIWKVPATDTYSISGYGAAGGKGGKNTMMRSHGVSVLGIFNLEKDDMLYILVGQQGEDACPSTNQLIQKVCIGENNVIEEEIRVNRSVHEWAGGGGGGGGATYVFKMKDGVPVPLIIAAGGGGRAYGAKTDTFHPERLENNSSVLGLNGNSGAAGGGGGWNDNTSLLWAGKSLQEGATGGHSCPQAMKKWGWETRGGFGGGGGGCSSGGGGGGYIGGNAASNNDPEMDGEDGVSFISPLGILYTPALKVMEGHGEVNIKHYLNCSHCEVDECHMDPESHKVICFCDHGTVLAEDGVSCIVSPTPEPHLPLSLILSVVTSALVAALVLAFSGIMIVYRRKHQELQAMQMELQSPEYKLSKLRTSTIMTDYNPNYCFAGKTSSISDLKEVPRKNITLIRGLGHGAFGEVYEGQVSGMPNDPSPLQVAVKTLPEVCSEQDELDFLMEALIISKFNHQNIVRCIGVSLQSLPRFILLELMAGGDLKSFLRETRPRPSQPSSLAMLDLLHVARDIACGCQYLEENHFIHRDIAARNCLLTCPGPGRVAKIGDFGMARDIYRASYYRKGGCAMLPVKWMPPEAFMEGIFTSKTDTWSFGVLLWEIFSLGYMPYPSKSNQEVLEFVTSGGRMDPPKNCPGPVYRIMTQCWQHQPEDRPNFAIILERIEYCTQDPDVINTALPIEYGPLVEEEEKVPVRPKDPEGVPPLLVSQQAKREEERSPAAPPPLPTTSSGKAAKKPTAAEISVRVPRGPAVEGGHVNMAFSQSNPPSELHKVHGSRNKPTSLWNPTYGSWFTEKPTKKNNPIAKKEPHDRGNLGLEGSCTVPPNVATGRLPGASLLLEPSSLTANMKEVPLFRLRHFPCGNVNYGYQQQGLPLEAATAPGAGHYEDTILKSKNSMNQPGP	Successful	"CH5424802, a selective ALK inhibitor capable of blocking the resistant gatekeeper mutant. Cancer Cell. 2011 May 17;19(5):679-90."	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	"MAM domain, meprin/A5/mu; Protein tyrosine kinase"	PF00629; PF07714	PF00629; MAM; PF07714; Pkinase_Tyr	.	.	hsa05223:Non-small cell lung cancer	R-HSA-201556: Signaling by ALK; R-HSA-9700645: ALK mutants bind TKIs; R-HSA-9717264: ASP-3026-resistant ALK mutants; R-HSA-9717301: NVP-TAE684-resistant ALK mutants; R-HSA-9717316: alectinib-resistant ALK mutants; R-HSA-9717319: brigatinib-resistant ALK mutants; R-HSA-9717323: ceritinib-resistant ALK mutants; R-HSA-9717326: crizotinib-resistant ALK mutants; R-HSA-9717329: lorlatinib-resistant ALK mutants; R-HSA-9725370: Signaling by ALK fusions and activated point mutants; R-HSA-9725371: Nuclear events stimulated by ALK signaling in cancer	.	Q9UM73
TTOHB1M	RNA demethylase ALKBH5	.	ALKB5_HUMAN	Single Protein	Alkylated DNA repair protein alkB homolog 5; Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5	ALKBH5	"Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro). Requires molecular oxygen, alpha-ketoglutarate and iron. Demethylation of m6A mRNA affects mRNA processing and export."	.	.	MAAASGYTDLREKLKSMTSRDNYKAGSREAAAAAAAAVAAAAAAAAAAEPYPVSGAKRKYQEDSDPERSDYEEQQLQKEEEARKVKSGIRQMRLFSQDECAKIEARIDEVVSRAEKGLYNEHTVDRAPLRNKYFFGEGYTYGAQLQKRGPGQERLYPPGDVDEIPEWVHQLVIQKLVEHRVIPEGFVNSAVINDYQPGGCIVSHVDPIHIFERPIVSVSFFSDSALCFGCKFQFKPIRVSEPVLSLPVRRGSVTVLSGYAADEITHCIRPQDIKERRAVIILRKTRLDAPRLETKSLSSSVLPPSYASDRLSGNNRDPALKPKRSHRKADPDAAHRPRILEMDKEENRRSVLLPTHRRRGSFSSENYWRKSYESSEDCSEAAGSPARKVKMRRH	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q6P6C2
TT12ABZ	Arachidonate 12-lipoxygenase (12-LOX)	P18054	LOX12_HUMAN	Oxygenase	"Platelet-type lipoxygenase 12; Lipoxin synthase 12-LO; LOG12; Arachidonate 12-lipoxygenase, 12S-type; 12S-lipoxygenase; 12S-LOX; 12LO; 12-lipoxygenase"	ALOX12	"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."	EC 1.13.11.31	3D3L; 2ABU	MGRYRIRVATGAWLFSGSYNRVQLWLVGTRGEAELELQLRPARGEEEEFDHDVAEDLGLLQFVRLRKHHWLVDDAWFCDRITVQGPGACAEVAFPCYRWVQGEDILSLPEGTARLPGDNALDMFQKHREKELKDRQQIYCWATWKEGLPLTIAADRKDDLPPNMRFHEEKRLDFEWTLKAGALEMALKRVYTLLSSWNCLEDFDQIFWGQKSALAEKVRQCWQDDELFSYQFLNGANPMLLRRSTSLPSRLVLPSGMEELQAQLEKELQNGSLFEADFILLDGIPANVIRGEKQYLAAPLVMLKMEPNGKLQPMVIQIQPPNPSSPTPTLFLPSDPPLAWLLAKSWVRNSDFQLHEIQYHLLNTHLVAEVIAVATMRCLPGLHPIFKFLIPHIRYTMEINTRARTQLISDGGIFDKAVSTGGGGHVQLLRRAAAQLTYCSLCPPDDLADRGLLGLPGALYAHDALRLWEIIARYVEGIVHLFYQRDDIVKGDPELQAWCREITEVGLCQAQDRGFPVSFQSQSQLCHFLTMCVFTCTAQHAAINQGQLDWYAWVPNAPCTMRMPPPTTKEDVTMATVMGSLPDVRQACLQMAISWHLSRRQPDMVPLGHHKEKYFSGPKPKAVLNQFRTDLEKLEKEITARNEQLDWPYEYLKPSCIENSVTI	Literature-reported	Discovery of platelet-type 12-human lipoxygenase selective inhibitors by high-throughput screening of structurally diverse libraries. Bioorg Med Chem. 2007 Nov 15;15(22):6900-8.	2	EC:1.13	Oxidoreductases acting on single donors	lipoxygenase family.	1.13.11.31	Acting on single donors with incorporation of molecular oxygen (oxygenases)	Lipoxygenase; PLAT/LH2 domain	PF00305; PF01477	PF00305; Lipoxygenase; PF01477; PLAT	.	.	hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways; hsa04726:Serotonergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels	R-HSA-2142696: Synthesis of Hepoxilins (HX) and Trioxilins (TrX); R-HSA-2142700: Synthesis of Lipoxins (LX); R-HSA-2142712: Synthesis of 12-eicosatetraenoic acid derivatives; R-HSA-9018677: Biosynthesis of DHA-derived SPMs; R-HSA-9025106: Biosynthesis of DPAn-6 SPMs; R-HSA-9026290: Biosynthesis of DPAn-3-derived maresins	MetaCyc:HS03167-MON	P18054
TTQ4QQH	"Arachidonate 12-lipoxygenase, 12R-type (ALOX12B)"	O75342	LX12B_HUMAN	.	12R-LOX; 12R-lipoxygenase; Epidermis-type lipoxygenase 12	ALOX12B	"Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:9837935, PubMed:9618483, PubMed:21558561). In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins (PubMed:21558561). Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss (PubMed:21558561). May also play a role in the regulation of the expression of airway mucins (PubMed:22441738). {ECO:0000269|PubMed:21558561, ECO:0000269|PubMed:22441738, ECO:0000269|PubMed:9618483, ECO:0000269|PubMed:9837935}."	EC 1.13.11.-	.	MATYKVRVATGTDLLSGTRDSISLTIVGTQGESHKQLLNHFGRDFATGAVGQYTVQCPQDLGELIIIRLHKERYAFFPKDPWYCNYVQICAPNGRIYHFPAYQWMDGYETLALREATGKTTADDSLPVLLEHRKEEIRAKQDFYHWRVFLPGLPSYVHIPSYRPPVRRHRNPNRPEWNGYIPGFPILINFKATKFLNLNLRYSFLKTASFFVRLGPMALAFKVRGLLDCKHSWKRLKDIRKIFPGKKSVVSEYVAEHWAEDTFFGYQYLNGVNPGLIRRCTRIPDKFPVTDDMVAPFLGEGTCLQAELEKGNIYLADYRIMEGIPTVELSGRKQHHCAPLCLLHFGPEGKMMPIAIQLSQTPGPDCPIFLPSDSEWDWLLAKTWVRYAEFYSHEAIAHLLETHLIAEAFCLALLRNLPMCHPLYKLLIPHTRYTVQINSIGRAVLLNEGGLSAKGMSLGVEGFAGVMVRALSELTYDSLYLPNDFVERGVQDLPGYYYRDDSLAVWNALEKYVTEIITYYYPSDAAVEGDPELQSWVQEIFKECLLGRESSGFPRCLRTVPELIRYVTIVIYTCSAKHAAVNTGQMEFTAWMPNFPASMRNPPIQTKGLTTLETFMDTLPDVKTTCITLLVLWTLSREPDDRRPLGHFPDIHFVEEAPRRSIEAFRQRLNQISHDIRQRNKCLPIPYYYLDPVLIENSISI	Clinical trial	"Clinical pipeline report, company report or official report of Veralox Therapeutics"	.	.	.	.	.	.	.	.	.	.	.	hsa:242	R-HSA-2142712;	MetaCyc:ENSG00000179477-MONOMER;	O75342;
TTN9T81	Arachidonate 15-lipoxygenase (15-LOX)	P16050	LOX15_HUMAN	Oxygenase	"LOG15; Arachidonate omega-6 lipoxygenase; Arachidonate 12-lipoxygenase, leukocyte-type; 15-Lipoxygenase; 15-LOX-1; 12/15-lipoxygenase; 12-LOX"	ALOX15	"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."	EC 1.13.11.33	2ABT	MGLYRIRVSTGASLYAGSNNQVQLWLVGQHGEAALGKRLWPARGKETELKVEVPEYLGPLLFVKLRKRHLLKDDAWFCNWISVQGPGAGDEVRFPCYRWVEGNGVLSLPEGTGRTVGEDPQGLFQKHREEELEERRKLYRWGNWKDGLILNMAGAKLYDLPVDERFLEDKRVDFEVSLAKGLADLAIKDSLNVLTCWKDLDDFNRIFWCGQSKLAERVRDSWKEDALFGYQFLNGANPVVLRRSAHLPARLVFPPGMEELQAQLEKELEGGTLFEADFSLLDGIKANVILCSQQHLAAPLVMLKLQPDGKLLPMVIQLQLPRTGSPPPPLFLPTDPPMAWLLAKCWVRSSDFQLHELQSHLLRGHLMAEVIVVATMRCLPSIHPIFKLIIPHLRYTLEINVRARTGLVSDMGIFDQIMSTGGGGHVQLLKQAGAFLTYSSFCPPDDLADRGLLGVKSSFYAQDALRLWEIIYRYVEGIVSLHYKTDVAVKDDPELQTWCREITEIGLQGAQDRGFPVSLQARDQVCHFVTMCIFTCTGQHASVHLGQLDWYSWVPNAPCTMRLPPPTTKDATLETVMATLPNFHQASLQMSITWQLGRRQPVMVAVGQHEEEYFSGPEPKAVLKKFREELAALDKEIEIRNAKLDMPYEYLRPSVVENSVAI	Patented-recorded	15-Lipoxygenase inhibitors: a patent review.Expert Opin Ther Pat. 2016;26(1):65-88.	15.5	EC:1.13	Oxidoreductases acting on single donors	lipoxygenase family.	1.13.11.33 	Acting on single donors with incorporation of molecular oxygen (oxygenases)	Lipoxygenase; PLAT/LH2 domain	PF00305; PF01477	PF00305; Lipoxygenase; PF01477; PLAT	.	.	hsa00590:Arachidonic acid metabolism; hsa00591:Linoleic acid metabolism; hsa01100:Metabolic pathways; hsa04726:Serotonergic synapse	R-HSA-2142691: Synthesis of Leukotrienes (LT) and Eoxins (EX); R-HSA-2142712: Synthesis of 12-eicosatetraenoic acid derivatives; R-HSA-2142770: Synthesis of 15-eicosatetraenoic acid derivatives; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9018677: Biosynthesis of DHA-derived SPMs; R-HSA-9018681: Biosynthesis of protectins; R-HSA-9018896: Biosynthesis of E-series 18(S)-resolvins; R-HSA-9023661: Biosynthesis of E-series 18(R)-resolvins; R-HSA-9025106: Biosynthesis of DPAn-6 SPMs; R-HSA-9026286: Biosynthesis of DPAn-3-derived protectins and resolvins	MetaCyc:HS08621-MON	P16050
TTSJ6Q4	LOX-5 messenger RNA (ALOX5 mRNA)	P09917	LOX5_HUMAN	mRNA target	LOG5 (mRNA); 5-lipoxygenase (mRNA); 5-LO (mRNA)	ALOX5	"Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes."	EC 1.13.11.34	3V99; 3V98; 3V92; 3O8Y; 2ABV	MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNGCNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDPCTLQFLAAPICLLYKNLANKIVPIAIQLNQIPGDENPIFLPSDAKYDWLLAKIWVRSSDFHVHQTITHLLRTHLVSEVFGIAMYRQLPAVHPIFKLLVAHVRFTIAINTKAREQLICECGLFDKANATGGGGHVQMVQRAMKDLTYASLCFPEAIKARGMESKEDIPYYFYRDDGLLVWEAIRTFTAEVVDIYYEGDQVVEEDPELQDFVNDVYVYGMRGRKSSGFPKSVKSREQLSEYLTVVIFTASAQHAAVNFGQYDWCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCWHLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMARFRKNLEAIVSVIAERNKKKQLPYYYLSPDRIPNSVAI	Discontinued	Designed multiple ligands. An emerging drug discovery paradigm. J Med Chem. 2005 Oct 20;48(21):6523-43.	5	mRNA	mRNA target	.	.	.	Lipoxygenase; PLAT/LH2 domain	PF00305; PF01477	PF00305; Lipoxygenase; PF01477; PLAT	.	.	hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways; hsa04726:Serotonergic synapse; hsa04913:Ovarian steroidogenesis; hsa05145:Toxoplasmosis	R-HSA-2142688: Synthesis of 5-eicosatetraenoic acids; R-HSA-2142691: Synthesis of Leukotrienes (LT) and Eoxins (EX); R-HSA-2142700: Synthesis of Lipoxins (LX); R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6798695: Neutrophil degranulation; R-HSA-9012546: Interleukin-18 signaling; R-HSA-9018676: Biosynthesis of D-series resolvins; R-HSA-9018682: Biosynthesis of maresins; R-HSA-9018896: Biosynthesis of E-series 18(S)-resolvins; R-HSA-9020265: Biosynthesis of aspirin-triggered D-series resolvins; R-HSA-9023661: Biosynthesis of E-series 18(R)-resolvins; R-HSA-9026286: Biosynthesis of DPAn-3-derived protectins and resolvins; R-HSA-9026290: Biosynthesis of DPAn-3-derived maresins; R-HSA-9026403: Biosynthesis of DPAn-3-derived 13-series resolvins; R-HSA-9027604: Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives	MetaCyc:HS00336-MON	P09917
TT2J34L	Arachidonate 5-lipoxygenase (5-LOX)	P09917	LOX5_HUMAN	Oxygenase	LOG5; 5-lipoxygenase; 5-LO	ALOX5	"Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes."	EC 1.13.11.34	3V99; 3V98; 3V92; 3O8Y; 2ABV	MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNGCNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDPCTLQFLAAPICLLYKNLANKIVPIAIQLNQIPGDENPIFLPSDAKYDWLLAKIWVRSSDFHVHQTITHLLRTHLVSEVFGIAMYRQLPAVHPIFKLLVAHVRFTIAINTKAREQLICECGLFDKANATGGGGHVQMVQRAMKDLTYASLCFPEAIKARGMESKEDIPYYFYRDDGLLVWEAIRTFTAEVVDIYYEGDQVVEEDPELQDFVNDVYVYGMRGRKSSGFPKSVKSREQLSEYLTVVIFTASAQHAAVNFGQYDWCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCWHLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMARFRKNLEAIVSVIAERNKKKQLPYYYLSPDRIPNSVAI	Successful	Inhibition of leukotriene formation by diethylcarbamazine modifies the acid-base balance in the rabbits with blast injuries of the lungs. Vojnosanit Pregl. 1999 May-Jun;56(3):243-7.	34	EC:1.13	Single donor oxidoreductase	lipoxygenase family.	1.13.11.34	Acting on single donors with incorporation of molecular oxygen (oxygenases)	Lipoxygenase; PLAT/LH2 domain	PF00305; PF01477	PF00305; Lipoxygenase; PF01477; PLAT	.	.	hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways; hsa04726:Serotonergic synapse; hsa04913:Ovarian steroidogenesis; hsa05145:Toxoplasmosis	R-HSA-2142688: Synthesis of 5-eicosatetraenoic acids; R-HSA-2142691: Synthesis of Leukotrienes (LT) and Eoxins (EX); R-HSA-2142700: Synthesis of Lipoxins (LX); R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6798695: Neutrophil degranulation; R-HSA-9012546: Interleukin-18 signaling; R-HSA-9018676: Biosynthesis of D-series resolvins; R-HSA-9018682: Biosynthesis of maresins; R-HSA-9018896: Biosynthesis of E-series 18(S)-resolvins; R-HSA-9020265: Biosynthesis of aspirin-triggered D-series resolvins; R-HSA-9023661: Biosynthesis of E-series 18(R)-resolvins; R-HSA-9026286: Biosynthesis of DPAn-3-derived protectins and resolvins; R-HSA-9026290: Biosynthesis of DPAn-3-derived maresins; R-HSA-9026403: Biosynthesis of DPAn-3-derived 13-series resolvins; R-HSA-9027604: Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives	MetaCyc:HS00336-MON	P09917
TTDMBF5	Arachidonate 5-lipoxygenase activating protein (FLAP)	P20292	AL5AP_HUMAN	.	MK-886-binding protein; FLAP; ALOX5AP	ALOX5AP	"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."	.	2Q7R; 2Q7M	MDQETVGNVVLLAIVTLISVVQNGFFAHKVEHESRTQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWSAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSVAGIFNYYLIFFFGSDFENYIKTISTTISPLLLIP	Discontinued	BAY x 1005 attenuates atherosclerosis in apoE/LDLR - double knockout mice. J Physiol Pharmacol. 2007 Sep;58(3):583-8.	9	.	.	.	.	.	.	.	.	.	.	hsa04664: Fc epsilon RI signaling pathway	R-HSA-2142688: Synthesis of 5-eicosatetraenoic acids; R-HSA-2142691: Synthesis of Leukotrienes (LT) and Eoxins (EX); R-HSA-2142700: Synthesis of Lipoxins (LX)	MetaCyc:ENSG00000132965-MON	P20292
TTHYMUV	Intestinal alkaline phosphatase	.	PPBI_HUMAN	Single Protein	Intestinal-type alkaline phosphatase; ALPI	ALPI	"Extracellular region, plasma membrane, alkaline phosphatase activity, magnesium ion binding, protease binding, zinc ion binding, dephosphorylation, digestion, phosphatidic acid biosynthetic process"	.	.	MQGPWVLLLLGLRLQLSLGVIPAEEENPAFWNRQAAEALDAAKKLQPIQKVAKNLILFLGDGLGVPTVTATRILKGQKNGKLGPETPLAMDRFPYLALSKTYNVDRQVPDSAATATAYLCGVKANFQTIGLSAAARFNQCNTTRGNEVISVMNRAKQAGKSVGVVTTTRVQHASPAGTYAHTVNRNWYSDADMPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPADASQNGIRLDGKNLVQEWLAKHQGAWYVWNRTELMQASLDQSVTHLMGLFEPGDTKYEIHRDPTLDPSLMEMTEAALRLLSRNPRGFYLFVEGGRIDHGHHEGVAYQALTEAVMFDDAIERAGQLTSEEDTLTLVTADHSHVFSFGGYTLRGSSIFGLAPSKAQDSKAYTSILYGNGPGYVFNSGVRPDVNESESGSPDYQQQAAVPLSSETHGGEDVAVFARGPQAHLVHGVQEQSFVAHVMAFAACLEPYTACDLAPPACTTDAAHPVAASLPLLAGTLLLLGASAAP	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P09923
TTMR5UV	Alkaline phosphatase tissue-nonspecific (ALPL)	P05186	PPBT_HUMAN	Phosphoric monoester hydrolase	"TNSALP; Liver/bone/kidney isozyme; Alkaline phosphatase, tissue-nonspecific isozyme; Alkaline phosphatase liver/bone/kidney isozyme; AP-TNAP"	ALPL	This isozyme plays a key role in skeletal mineralization by regulating levels of diphosphate (PPi).	EC 3.1.3.1	.	MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF	Successful	Enzyme-replacement therapy in life-threatening hypophosphatasia. N Engl J Med. 2012 Mar 8;366(10):904-13.	34	EC:3.1.3	Phosphoric monoester hydrolases	alkaline phosphatase family.	3.1.3.1 	Acting on ester bonds	Alkaline phosphatase	PF00245	PF00245; Alk_phosphatase	.	.	hsa00790:Folate biosynthesis; hsa01100:Metabolic pathways	R-HSA-163125: Post-translational modification: synthesis of GPI-anchored proteins	.	P05186
TTPQNAZ	Alkaline phosphatase (ALPPL2)	P10696	PPBN_HUMAN	Phosphoric monoester hydrolase	"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"	ALPPL2	"extracellular region, plasma membrane, alkaline phosphatase activity."	EC 3.1.3.1	.	MQGPWVLLLLGLRLQLSLGIIPVEEENPDFWNRQAAEALGAAKKLQPAQTAAKNLIIFLGDGMGVSTVTAARILKGQKKDKLGPETFLAMDRFPYVALSKTYSVDKHVPDSGATATAYLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGAYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPDDYSQGGTRLDGKNLVQEWLAKHQGARYVWNRTELLQASLDPSVTHLMGLFEPGDMKYEIHRDSTLDPSLMEMTEAALLLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVLKDGARPDVTESESGSPEYRQQSAVPLDGETHAGEDVAVFARGPQAHLVHGVQEQTFIAHVMAFAACLEPYTACDLAPRAGTTDAAHPGPSVVPALLPLLAGTLLLLGTATAP	Literature-reported	Alkaline phosphatase ALPPL-2 is a novel pancreatic carcinoma-associated protein. Cancer Res. 2013 Mar 15;73(6):1934-45.	.	EC:3.1.3	Phosphoric monoester hydrolases	alkaline phosphatase family.	3.1.3.1 	Acting on ester bonds	Alkaline phosphatase	PF00245	PF00245; Alk_phosphatase	.	.	hsa00730: Thiamine metabolism; hsa00790: Folate biosynthesis; hsa01100: Metabolic pathways; hsa01240: Biosynthesis of cofactors	R-HSA-163125: Post-translational modification: synthesis of GPI-anchored proteins	.	P10696
TTLN1AP	Alpha-methylacyl-CoA racemase (AMACR)	Q9UHK6	AMACR_HUMAN	CaiB/BaiF CoA-transferase family	IBLi; 2-methylacyl-CoA racemase	AMACR	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.	EC 5.1.99.4	.	MALQGISVVELSGLAPGPFCAMVLADFGARVVRVDRPGSRYDVSRLGRGKRSLVLDLKQPRGAAVLRRLCKRSDVLLEPFRRGVMEKLQLGPEILQRENPRLIYARLSGFGQSGSFCRLAGHDINYLALSGVLSKIGRSGENPYAPLNLLADFAGGGLMCALGIIMALFDRTRTGKGQVIDANMVEGTAYLSSFLWKTQKLSLWEAPRGQNMLDGGAPFYTTYRTADGEFMAVGAIEPQFYELLIKGLGLKSDELPNQMSMDDWPEMKKKFADVFAEKTKAEWCQIFDGTDACVTPVLTFEEVVHHDHNKERGSFITSEEQDVSPRPAPLLLNTPAIPSFKRDPFIGEHTEEILEEFGFSREEIYQLNSDKIIESNKVKASL	Literature-reported	[The value of alpha-methylacyl-CoA racemase expression in the progression of colonic carcinoma]. Rev Esp Patol. 2017 Jan - Mar;50(1):15-21.	.	.	.	.	.	.	.	.	.	.	.	hsa00120: Primary bile acid biosynthesis; hsa01100: Metabolic pathways; hsa04146: Peroxisome	R-HSA-193368: Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol; R-HSA-193775: Synthesis of bile acids and bile salts via 24-hydroxycholesterol; R-HSA-389887: Beta-oxidation of pristanoyl-CoA; R-HSA-9033241: Peroxisomal protein import	MetaCyc:HS01416-MON	Q9UHK6
TTBFROQ	S-adenosylmethionine decarboxylase proenzyme (AMD1)	P17707	DCAM_HUMAN	Carbon-carbon lyase	SamDC; S-adenosylmethioninedecarboxylase; AdoMetDC; AMD	AMD1	"Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels. Essential for biosynthesis of the polyamines spermidine and spermine."	EC 4.1.1.50	3H0W; 3H0V; 3EPB; 3EPA; 3EP9	MEAAHFFEGTEKLLEVWFSRQQPDANQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATMFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLASPQKIEGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS	Successful	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	34	EC:4.1	Carbon carbon lyase	eukaryotic AdoMetDC family.	4.1.1.50 	Carbon-carbon lyases	Adenosylmethionine decarboxylase	PF01536	PF01536; SAM_decarbox	.	.	hsa00270:Cysteine and methionine metabolism; hsa00330:Arginine and proline metabolism; hsa01100:Metabolic pathways	R-HSA-351202: Metabolism of polyamines	.	P17707
TTZDCPK	Anti-mullerian hormone II receptor (AMHR2)	Q16671	AMHR2_HUMAN	.	MRII; MISRII; MISR2; MIS type II receptor; Anti-Muellerian hormone type-2 receptor; Anti-Muellerian hormone type II receptor; AMHR; AMH type II receptor	AMHR2	"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."	EC 2.7.11.30	.	MLGSLGLWALLPTAVEAPPNRRTCVFFEAPGVRGSTKTLGELLDTGTELPRAIRCLYSRCCFGIWNLTQDRAQVEMQGCRDSDEPGCESLHCDPSPRAHPSPGSTLFTCSCGTDFCNANYSHLPPPGSPGTPGSQGPQAAPGESIWMALVLLGLFLLLLLLLGSIILALLQRKNYRVRGEPVPEPRPDSGRDWSVELQELPELCFSQVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLLSGPLLVLELHPKGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNGQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPPAWTPTQPQGPAAIMEAGTQRYMAPELLDKTLDLQDWGMALRRADIYSLALLLWEILSRCPDLRPDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWRCFATDPDGLRELLEDCWDADPEARLTAECVQQRLAALAHPQESHPFPESCPRGCPPLCPEDCTSIPAPTILPCRPQRSACHFSVQQGPCSRNPQPACTLSPV	Literature-reported	The anti-Mullerian hormone type II receptor: insights into the binding domains recognized by a monoclonal antibody and the natural ligand. Biochem J. 2004 May 1;379(Pt 3):785-93.	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04350: TGF-beta signaling pathway	R-HSA-201451: Signaling by BMP	.	Q16671
TTI48OS	Angiomotin (AMOT)	Q4VCS5	AMOT_HUMAN	.	KIAA1071	AMOT	"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."	.	.	MRNSEEQPSGGTTVLQRLLQEQLRYGNPSENRSLLAIHQQATGNGPPFPSGSGNPGPQSDVLSPQDHHQQLVAHAARQEPQGQEIQSENLIMEKQLSPRMQNNEELPTYEEAKVQSQYFRGQQHASVGAAFYVTGVTNQKMRTEGRPSVQRLNPGKMHQDEGLRDLKQGHVRSLSERLMQMSLATSGVKAHPPVTSAPLSPPQPNDLYKNPTSSSEFYKAQGPLPNQHSLKGMEHRGPPPEYPFKGMPPQSVVCKPQEPGHFYSEHRLNQPGRTEGQLMRYQHPPEYGAARPAQDISLPLSARNSQPHSPTSSLTSGGSLPLLQSPPSTRLSPARHPLVPNQGDHSAHLPRPQQHFLPNQAHQGDHYRLSQPGLSQQQQQQQQQHHHHHHHQQQQQQQPQQQPGEAYSAMPRAQPSSASYQPVPADPFAIVSRAQQMVEILSDENRNLRQELEGCYEKVARLQKVETEIQRVSEAYENLVKSSSKREALEKAMRNKLEGEIRRMHDFNRDLRERLETANKQLAEKEYEGSEDTRKTISQLFAKNKESQREKEKLEAELATARSTNEDQRRHIEIRDQALSNAQAKVVKLEEELKKKQVYVDKVEKMQQALVQLQAACEKREQLEHRLRTRLERELESLRIQQRQGNCQPTNVSEYNAAALMELLREKEERILALEADMTKWEQKYLEENVMRHFALDAAATVAAQRDTTVISHSPNTSYDTALEARIQKEEEEILMANKRCLDMEGRIKTLHAQIIEKDAMIKVLQQRSRKEPSKTEQLSCMRPAKSLMSISNAGSGLLSHSSTLTGSPIMEEKRDDKSWKGSLGILLGGDYRAEYVPSTPSPVPPSTPLLSAHSKTGSRDCSTQTERGTESNKTAAVAPISVPAPVAAAATAAAITATAATITTTMVAAAPVAVAAAAAPAAAAAPSPATAAATAAAVSPAAAGQIPAAASVASAAAVAPSAAAAAAVQVAPAAPAPVPAPALVPVPAPAAAQASAPAQTQAPTSAPAVAPTPAPTPTPAVAQAEVPASPATGPGPHRLSIPSLTCNPDKTDGPVFHSNTLERKTPIQILGQEPDAEMVEYLI	Literature-reported	Early prediction of revascularisation by angiomotin-targeting positron emission tomography. Theranostics. 2018 Oct 5;8(18):4985-4994.	.	.	.	angiomotin family.	.	.	Angiomotin C terminal	PF12240	PF12240; Angiomotin_C	.	.	hsa04390: Hippo signaling pathway; hsa04530: Tight junction	R-HSA-2028269: Signaling by Hippo	.	Q4VCS5
TTKZ09F	Adenosine monophosphate deaminase (AMPD)	P23109; Q01433; Q01432	AMPD1_HUMAN; AMPD2_HUMAN; AMPD3_HUMAN	Carbon-nitrogen hydrolase	AMP deaminase	AMPD1	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.	.	.	MNVRIFYSVSQSPHSLLSLLFYCAILESRISATMPLFKLPAEEKQIDDAMRNFAEKVFASEVKDEGGRQEISPFDVDEICPISHHEMQAHIFHLETLSTSTEARRKKRFQGRKTVNLSIPLSETSSTKLSHIDEYISSSPTYQTVPDFQRVQITGDYASGVTVEDFEIVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEAWVANESFYPVFTPPVKKGEDPFRTDNLPENLGYHLKMKDGVVYVYPNEAAVSKDEPKPLPYPNLDTFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKHITGFDSVDDESKHSGHMFSSKSPKPQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNVAQIRMAYRYETWCYELNLIAEGLKSTE	Literature-reported	Mechanisms of cell death induced by 2-chloroadenosine in leukemic B-cells. Biochem Pharmacol. 2008 Apr 1;75(7):1451-60.	0	.	.	.	.	.	.	.	.	.	.	hsa00230: Purine metabolism; hsa01100: Metabolic pathways; hsa01232: Nucleotide metabolism	R-HSA-74217: Purine salvage	.	P23109
TTCGSZ4	Pancreatic alpha-amylase (AMY2A)	P04746	AMYP_HUMAN	Glycosylase	"PA; 1,4-alpha-D-glucan glucanohydrolase"	AMY2A	"Hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose."	EC 3.2.1.1	5VA9; 5U3A; 5TD4; 5KEZ; 5EMY	MKFFLLLFTIGFCWAQYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIYNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLTGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPAGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFVPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRQFQNGNDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVIFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWSFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL	Clinical trial	"Clinical pipeline report, company report or official report of Digestive Care."	29	.	.	.	.	.	.	.	.	.	.	hsa00500: Starch and sucrose metabolism; hsa01100: Metabolic pathways; hsa04970: Salivary secretion; hsa04972: Pancreatic secretion; hsa04973: Carbohydrate digestion and absorption	R-HSA-189085: Digestion of dietary carbohydrate	.	P04746
TTURHFP	Angiogenin (ANG)	P03950	ANGI_HUMAN	Endoribonucleases	Ribonuclease 5; RNase 5; RNASE5	ANG	"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."	EC 3.1.27.-	5M9V; 5M9T; 5M9S; 5M9R; 5M9Q	MVMGLGVLLLVFVLGLGLTPPTLAQDNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFRRP	Literature-reported	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	0	EC:3.1.26	Endoribonucleases	pancreatic ribonuclease family.	3.1.27.-	Acting on ester bonds	Pancreatic ribonuclease	PF00074	PF00074; RnaseA	.	.	hsa05014: Amyotrophic lateral sclerosis	R-HSA-418990:Adherens junctions interactions	.	P03950
TTWNQ1T	Angiopoietin-1 (ANGPT1)	Q15389	ANGP1_HUMAN	Fibrinogen protein	Angiopoietin1; ANGPT1; ANG1; ANG-1	ANGPT1	"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."	.	4K0V; 4JYO; 4EPU	MTVFLSFAFLAAILTHIGCSNQRRSPENSGRRYNRIQHGQCAYTFILPEHDGNCRESTTDQYNTNALQRDAPHVEPDFSSQKLQHLEHVMENYTQWLQKLENYIVENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVTRQTYIIQELEKQLNRATTNNSVLQKQQLELMDTVHNLVNLCTKEGVLLKGGKREEEKPFRDCADVYQAGFNKSGIYTIYINNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	25	.	.	.	.	.	.	.	.	.	.	hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa05323:Rheumatoid arthritis	R-HSA-210993:Tie2 Signaling; R-HSA-5673001:RAF/MAP kinase cascade	.	Q15389
TTKLQTJ	Angiopoietin-2 (ANGPT2)	O15123	ANGP2_HUMAN	Fibrinogen protein	ANG-2	ANGPT2	"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."	.	4ZFG; 4JZC; 2GY7; 1Z3U; 1Z3S	MWQIVFFTLSCDLVLAAAYNNFRKSMDSIGKKQYQVQHGSCSYTFLLPEMDNCRSSSSPYVSNAVQRDAPLEYDDSVQRLQVLENIMENNTQWLMKLENYIQDNMKKEMVEIQQNAVQNQTAVMIEIGTNLLNQTAEQTRKLTDVEAQVLNQTTRLELQLLEHSLSTNKLEKQILDQTSEINKLQDKNSFLEKKVLAMEDKHIIQLQSIKEEKDQLQVLVSKQNSIIEELEKKIVTATVNNSVLQKQQHDLMETVNNLLTMMSTSNSAKDPTVAKEEQISFRDCAEVFKSGHTTNGIYTLTFPNSTEEIKAYCDMEAGGGGWTIIQRREDGSVDFQRTWKEYKVGFGNPSGEYWLGNEFVSQLTNQQRYVLKIHLKDWEGNEAYSLYEHFYLSSEELNYRIHLKGLTGTAGKISSISQPGNDFSTKDGDNDKCICKCSQMLTGGWWFDACGPSNLNGMYYPQRQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	25	Fibrinogen	Fibrinogen	.	.	.	"Fibrinogen beta and gamma chains, C-terminal globular domain"	PF00147	PF00147; Fibrinogen_C	.	.	hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04151:PI3K-Akt signaling pathway	R-HSA-210993:Tie2 Signaling	.	O15123
TT0APVH	HUMAN angiopoietin-2 (ANG-2)	O15123	ANGP2_HUMAN	Fibrinogen protein	ANG-2	ANGPT2	"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."	.	4ZFG; 4JZC; 2GY7; 1Z3U; 1Z3S	MWQIVFFTLSCDLVLAAAYNNFRKSMDSIGKKQYQVQHGSCSYTFLLPEMDNCRSSSSPYVSNAVQRDAPLEYDDSVQRLQVLENIMENNTQWLMKLENYIQDNMKKEMVEIQQNAVQNQTAVMIEIGTNLLNQTAEQTRKLTDVEAQVLNQTTRLELQLLEHSLSTNKLEKQILDQTSEINKLQDKNSFLEKKVLAMEDKHIIQLQSIKEEKDQLQVLVSKQNSIIEELEKKIVTATVNNSVLQKQQHDLMETVNNLLTMMSTSNSAKDPTVAKEEQISFRDCAEVFKSGHTTNGIYTLTFPNSTEEIKAYCDMEAGGGGWTIIQRREDGSVDFQRTWKEYKVGFGNPSGEYWLGNEFVSQLTNQQRYVLKIHLKDWEGNEAYSLYEHFYLSSEELNYRIHLKGLTGTAGKISSISQPGNDFSTKDGDNDKCICKCSQMLTGGWWFDACGPSNLNGMYYPQRQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF	.	Updates: Lilly's Global COVID-19 Response	.	.	.	.	.	.	.	.	.	.	.	hsa04010: MAPK signaling pathway; hsa04014: Ras signaling pathway; hsa04015: Rap1 signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa05167: Kaposi sarcoma-associated herpesvirus infection	R-HSA-210993: Tie2 Signaling	.	O15123
TT59GO7	ANGPTL3 messenger RNA (ANGPTL3 mRNA)	Q9Y5C1	ANGL3_HUMAN	mRNA target	UNQ153/PRO179 (mRNA); Angiopoietin-related protein 3 (mRNA); Angiopoietin-like protein 3 (mRNA); Angiopoietin-5 (mRNA); ANGPT5 (mRNA); ANG-5 (mRNA)	ANGPTL3	"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."	.	6EUA	MFTIKLLLFIVPLVISSRIDQDNSSFDSLSPEPKSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKELRRTTYKLQVKNEEVKNMSLELNSKLESLLEEKILLQQKVKYLEEQLTNLIQNQPETPEHPEVTSLKTFVEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRRTSIQEPTEISLSSKPRAPRTTPFLQLNEIRNVKHDGIPAECTTIYNRGEHTSGMYAIRPSNSQVFHVYCDVISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLDGEFWLGLEKIYSIVKQSNYVLRIELEDWKDNKHYIEYSFYLGNHETNYTLHLVAITGNVPNAIPENKDLVFSTWDHKAKGHFNCPEGYSGGWWWHDECGENNLNGKYNKPRAKSKPERRRGLSWKSQNGRLYSIKSTKMLIHPTDSESFE	Clinical trial	"Clinical pipeline report, company report or official report of ISIS Pharmaceuticals."	17	mRNA	mRNA target	.	.	.	"Fibrinogen beta and gamma chains, C-terminal globular domain"	PF00147	PF00147; Fibrinogen_C	.	.	hsa04979: Cholesterol metabolism	R-HSA-8963889: Assembly of active LPL and LIPC lipase complexes; R-HSA-9029558: NR1H2 & NR1H3 regulate gene expression linked to lipogenesis	.	Q9Y5C1
TTUO98L	Angiopoietin-related protein 3 (ANGPTL3)	Q9Y5C1	ANGL3_HUMAN	Fibrinogen protein	UNQ153/PRO179; Angiopoietin-like protein 3; Angiopoietin-5; ANGPT5; ANG-5	ANGPTL3	"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)."	.	6EUA	MFTIKLLLFIVPLVISSRIDQDNSSFDSLSPEPKSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKELRRTTYKLQVKNEEVKNMSLELNSKLESLLEEKILLQQKVKYLEEQLTNLIQNQPETPEHPEVTSLKTFVEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRRTSIQEPTEISLSSKPRAPRTTPFLQLNEIRNVKHDGIPAECTTIYNRGEHTSGMYAIRPSNSQVFHVYCDVISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLDGEFWLGLEKIYSIVKQSNYVLRIELEDWKDNKHYIEYSFYLGNHETNYTLHLVAITGNVPNAIPENKDLVFSTWDHKAKGHFNCPEGYSGGWWWHDECGENNLNGKYNKPRAKSKPERRRGLSWKSQNGRLYSIKSTKMLIHPTDSESFE	Successful	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	hsa04979: Cholesterol metabolism	R-HSA-8963889: Assembly of active LPL and LIPC lipase complexes; R-HSA-9029558: NR1H2 & NR1H3 regulate gene expression linked to lipogenesis	.	Q9Y5C1
TTWALY5	Angiopoietin-related protein 4 (ANGPTL4)	Q9BY76	ANGL4_HUMAN	Fibrinogen protein	UNQ171/PRO197; PSEC0166; PP1158; PGAR; Hepatic fibrinogen/angiopoietin-related protein; HFARP; Angiopoietin-like protein PP1158; Angiopoietin-like protein 4; Angiopoietin-like 4; ARP4	ANGPTL4	"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."	.	6EUB	MSGAPTAGAALMLCAATAVLLSAQGGPVQSKSPRFASWDEMNVLAHGLLQLGQGLREHAERTRSQLSALERRLSACGSACQGTEGSTDLPLAPESRVDPEVLHSLQTQLKAQNSRIQQLFHKVAQQQRHLEKQHLRIQHLQSQFGLLDHKHLDHEVAKPARRKRLPEMAQPVDPAHNVSRLHRLPRDCQELFQVGERQSGLFEIQPQGSPPFLVNCKMTSDGGWTVIQRRHDGSVDFNRPWEAYKAGFGDPHGEFWLGLEKVHSITGDRNSRLAVQLRDWDGNAELLQFSVHLGGEDTAYSLQLTAPVAGQLGATTVPPSGLSVPFSTWDQDHDLRRDKNCAKSLSGGWWFGTCSHSNLNGQYFRSIPQQRQKLKKGIFWKTWRGRYYPLQATTMLIQPMAAEAAS	Literature-reported	Potential Role of ANGPTL4 in the Cross Talk between Metabolism and Cancer through PPAR Signaling Pathway. PPAR Res. 2017;2017:8187235.	.	Fibrinogen	Fibrinogen	.	.	.	"Fibrinogen beta and gamma chains, C-terminal globular domain"	PF00147	PF00147; Fibrinogen_C	.	.	hsa03320: PPAR signaling pathway; hsa04979: Cholesterol metabolism	R-HSA-1989781: PPARA activates gene expression; R-HSA-381340: Transcriptional regulation of white adipocyte differentiation; R-HSA-8963889: Assembly of active LPL and LIPC lipase complexes	.	Q9BY76
TTKFPMH	Ankyrin (ANK)	P16157	ANK1_HUMAN	.	Erythrocyte ankyrin; Ankyrin-R; Ankyrin-1; ANK-1; ANK	ANK1	"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."	.	3UD2; 3UD1; 3KBU; 3KBT; 3F59	MPYSVGFREADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETKTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYDAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHVRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKVNAKAKDDQTPLHCAARIGHTNMVKLLLENNANPNLATTAGHTPLHIAAREGHVETVLALLEKEASQACMTKKGFTPLHVAAKYGKVRVAELLLERDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQVEVARSLLQYGGSANAESVQGVTPLHLAAQEGHAEMVALLLSKQANGNLGNKSGLTPLHLVAQEGHVPVADVLIKHGVMVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSDGTTPLAIAKRLGYISVTDVLKVVTDETSFVLVSDKHRMSFPETVDEILDVSEDEGEELISFKAERRDSRDVDEEKELLDFVPKLDQVVESPAIPRIPCAMPETVVIRSEEQEQASKEYDEDSLIPSSPATETSDNISPVASPVHTGFLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLSTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHRSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSRLCQDYDTIGPEGGSLKSKLVPLVQATFPENAVTKRVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLVYANECANFTTNVSARFWLSDCPRTAEAVNFATLLYKELTAVPYMAKFVIFAKMNDPREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMSLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAMPVKVRDSSREPGGSLSFLRKAMKYEDTQHILCHLNITMPPCAKGSGAEDRRRTPTPLALRYSILSESTPGSLSGTEQAEMKMAVISEHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSVALLNLWVIREGQNANMENLYTALQSIDRGEIVNMLEGSGRQSRNLKPDRRHTDRDYSLSPSQMNGYSSLQDELLSPASLGCALSSPLRADQYWNEVAVLDAIPLAATEHDTMLEMSDMQVWSAGLTPSLVTAEDSSLECSKAEDSDATGHEWKLEGALSEEPRGPELGSLELVEDDTVDSDATNGLIDLLEQEEGQRSEEKLPGSKRQDDATGAGQDSENEVSLVSGHQRGQARITHSPTVSQVTERSQDRLQDWDADGSIVSYLQDAAQGSWQEEVTQGPHSFQGTSTMTEGLEPGGSQEYEKVLVSVSEHTWTEQPEAESSQADRDRRQQGQEEQVQEAKNTFTQVVQGNEFQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQIDLSSADAAQEHEEVTVEGPLEDPSELEVDIDYFMKHSKDHTSTPNP	Literature-reported	Autoinhibition of ankyrin-B/G membrane target bindings by intrinsically disordered segments from the tail regions. Elife. 2017 Aug 25;6. pii: e29150.	.	.	.	.	.	.	.	.	.	.	.	hsa05205: Proteoglycans in cancer	R-HSA-445095: Interaction between L1 and Ankyrins; R-HSA-447038: NrCAM interactions; R-HSA-447041: CHL1 interactions; R-HSA-447043: Neurofascin interactions; R-HSA-6807878: COPI-mediated anterograde transport	.	P16157
TTOJI4S	Calcium-dependent chloride channel anoctamin (ANO)	Q5XXA6	ANO1_HUMAN	.	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	ANO1	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.	.	.	MRVNEKYSTLPAEDRSVHIINICAIEDIGYLPSEGTLLNSLSVDPDAECKYGLYFRDGRRKVDYILVYHHKRPSGNRTLVRRVQHSDTPSGARSVKQDHPLPGKGASLDAGSGEPPMDYHEDDKRFRREEYEGNLLEAGLELERDEDTKIHGVGFVKIHAPWNVLCREAEFLKLKMPTKKMYHINETRGLLKKINSVLQKITDPIQPKVAEHRPQTMKRLSYPFSREKQHLFDLSDKDSFFDSKTRSTIVYEILKRTTCTKAKYSMGITSLLANGVYAAAYPLHDGDYNGENVEFNDRKLLYEEWARYGVFYKYQPIDLVRKYFGEKIGLYFAWLGVYTQMLIPASIVGIIVFLYGCATMDENIPSMEMCDQRHNITMCPLCDKTCSYWKMSSACATARASHLFDNPATVFFSVFMALWAATFMEHWKRKQMRLNYRWDLTGFEEEEEAVKDHPRAEYEARVLEKSLKKESRNKEKRRHIPEESTNKWKQRVKTAMAGVKLTDKVKLTWRDRFPAYLTNLVSIIFMIAVTFAIVLGVIIYRISMAAALAMNSSPSVRSNIRVTVTATAVIINLVVIILLDEVYGCIARWLTKIEVPKTEKSFEERLIFKAFLLKFVNSYTPIFYVAFFKGRFVGRPGDYVYIFRSFRMEECAPGGCLMELCIQLSIIMLGKQLIQNNLFEIGIPKMKKLIRYLKLKQQSPPDHEECVKRKQRYEVDYNLEPFAGLTPEYMEMIIQFGFVTLFVASFPLAPLFALLNNIIEIRLDAKKFVTELRRPVAVRAKDIGIWYNILRGIGKLAVIINAFVISFTSDFIPRLVYLYMYSKNGTMHGFVNHTLSSFNVSDFQNGTAPNDPLDLGYEVQICRYKDYREPPWSENKYDISKDFWAVLAARLAFVIVFQNLVMFMSDFVDWVIPDIPKDISQQIHKEKVLMVELFMREEQDKQQLLETWMEKERQKDEPPCNHHNTKACPDSLGSPAPSHAYHGGVL	Successful	Nat Rev Drug Discov. 2013 Feb;12(2):87-90.	34	.	Calcium-dependent chloride channel	anoctamin family.	.	.	"Dimerisation domain of Ca+-activated chloride-channel, anoctamin; Calcium-activated chloride channel"	PF16178; PF04547	PF16178; Anoct_dimer; PF04547; Anoctamin	1.A.17.1.1	The Calcium-Dependent Chloride Channel (Ca-ClC) Family	.	R-HSA-2672351:Stimuli-sensing channels	.	Q5XXA6
TT2X79I	Prostate cancer-associated protein 5 (NGEP)	Q6IWH7	ANO7_HUMAN	.	Transmembrane protein 16G; TMEM16G; PCANAP5; New gene expressed in prostate; NGEP; IPCA-5; Dresden transmembrane protein of the prostate; D-TMPP; Anoctamin-7	ANO7	"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."	.	.	MRMAATAWAGLQGPPLPTLCPAVRTGLYCRDQAHAERWAMTSETSSGSHCARSRMLRRRAQEEDSTVLIDVSPPEAEKRGSYGSTAHASEPGGQQAAACRAGSPAKPRIADFVLVWEEDLKLDRQQDSAARDRTDMHRTWRETFLDNLRAAGLCVDQQDVQDGNTTVHYALLSASWAVLCYYAEDLRLKLPLQELPNQASNWSAGLLAWLGIPNVLLEVVPDVPPEYYSCRFRVNKLPRFLGSDNQDTFFTSTKRHQILFEILAKTPYGHEKKNLLGIHQLLAEGVLSAAFPLHDGPFKTPPEGPQAPRLNQRQVLFQHWARWGKWNKYQPLDHVRRYFGEKVALYFAWLGFYTGWLLPAAVVGTLVFLVGCFLVFSDIPTQELCGSKDSFEMCPLCLDCPFWLLSSACALAQAGRLFDHGGTVFFSLFMALWAVLLLEYWKRKSATLAYRWDCSDYEDTEERPRPQFAASAPMTAPNPITGEDEPYFPERSRARRMLAGSVVIVVMVAVVVMCLVSIILYRAIMAIVVSRSGNTLLAAWASRIASLTGSVVNLVFILILSKIYVSLAHVLTRWEMHRTQTKFEDAFTLKVFIFQFVNFYSSPVYIAFFKGRFVGYPGNYHTLFGVRNEECAAGGCLIELAQELLVIMVGKQVINNMQEVLIPKLKGWWQKFRLRSKKRKAGASAGASQGPWEDDYELVPCEGLFDEYLEMVLQFGFVTIFVAACPLAPLFALLNNWVEIRLDARKFVCEYRRPVAERAQDIGIWFHILAGLTHLAVISNAFLLAFSSDFLPRAYYRWTRAHDLRGFLNFTLARAPSSFAAAHNRTCRYRAFRDDDGHYSQTYWNLLAIRLAFVIVFEHVVFSVGRLLDLLVPDIPESVEIKVKREYYLAKQALAENEVLFGTNGTKDEQPEGSELSSHWTPFTVPKASQLQQ	Literature-reported	"NGEP, a gene encoding a membrane protein detected only in prostate cancer and normal prostate. Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):3059-64."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2672351: Stimuli-sensing channels	.	Q6IWH7
TTPHMWB	Aminopeptidase N (ANPEP)	P15144	AMPN_HUMAN	Peptidase	Myeloid plasma membrane glycoprotein CD13; Microsomal aminopeptidase; HAPN; Gp150; Aminopeptidase M; Alanyl aminopeptidase; ANPEP	ANPEP	"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."	EC 3.4.11.2	6ATK; 5LHD; 4FYT; 4FYS; 4FYR	MAKGFYISKSLGILGILLGVAAVCTIIALSVVYSQEKNKNANSSPVASTTPSASATTNPASATTLDQSKAWNRYRLPNTLKPDSYRVTLRPYLTPNDRGLYVFKGSSTVRFTCKEATDVIIIHSKKLNYTLSQGHRVVLRGVGGSQPPDIDKTELVEPTEYLVVHLKGSLVKDSQYEMDSEFEGELADDLAGFYRSEYMEGNVRKVVATTQMQAADARKSFPCFDEPAMKAEFNITLIHPKDLTALSNMLPKGPSTPLPEDPNWNVTEFHTTPKMSTYLLAFIVSEFDYVEKQASNGVLIRIWARPSAIAAGHGDYALNVTGPILNFFAGHYDTPYPLPKSDQIGLPDFNAGAMENWGLVTYRENSLLFDPLSSSSSNKERVVTVIAHELAHQWFGNLVTIEWWNDLWLNEGFASYVEYLGADYAEPTWNLKDLMVLNDVYRVMAVDALASSHPLSTPASEINTPAQISELFDAISYSKGASVLRMLSSFLSEDVFKQGLASYLHTFAYQNTIYLNLWDHLQEAVNNRSIQLPTTVRDIMNRWTLQMGFPVITVDTSTGTLSQEHFLLDPDSNVTRPSEFNYVWIVPITSIRDGRQQQDYWLIDVRAQNDLFSTSGNEWVLLNLNVTGYYRVNYDEENWRKIQTQLQRDHSAIPVINRAQIINDAFNLASAHKVPVTLALNNTLFLIEERQYMPWEAALSSLSYFKLMFDRSEVYGPMKNYLKKQVTPLFIHFRNNTNNWREIPENLMDQYSEVNAISTACSNGVPECEEMVSGLFKQWMENPNNNPIHPNLRSTVYCNAIAQGGEEEWDFAWEQFRNATLVNEADKLRAALACSKELWILNRYLSYTLNPDLIRKQDATSTIISITNNVIGQGLVWDFVQSNWKKLFNDYGGGSFSFSNLIQAVTRRFSTEYELQQLEQFKKDNEETGFGSGTRALEQALEKTKANIKWVKENKEVVLQWFTENSK	Clinical trial	Recent insights into the role of dipeptidyl aminopeptidase IV (DPIV) and aminopeptidase N (APN) families in immune functions. Clin Chem Lab Med. 2009;47(3):253-61.	21	.	.	.	.	.	.	.	.	.	.	hsa00480:Glutathione metabolism; hsa01100:Metabolic pathways; hsa04614:Renin-angiotensin system; hsa04640:Hematopoietic cell lineage	R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins	.	P15144
TTRLPUB	Bacillus anthracis Protective antigen (Anthrax PA)	P13423	PAG_BACAN	.	Protective antigen; Anthrax toxins translocating protein; Anthrax PA83; Anthrax PA-83; Anthrax PA	Anthrax PA	"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."	.	5FR3; 4NAM; 4H2A; 4EE2; 3TEZ	MKKRKVLIPLMALSTILVSSTGNLEVIQAEVKQENRLLNESESSSQGLLGYYFSDLNFQAPMVVTSSTTGDLSIPSSELENIPSENQYFQSAIWSGFIKVKKSDEYTFATSADNHVTMWVDDQEVINKASNSNKIRLEKGRLYQIKIQYQRENPTEKGLDFKLYWTDSQNKKEVISSDNLQLPELKQKSSNSRKKRSTSAGPTVPDRDNDGIPDSLEVEGYTVDVKNKRTFLSPWISNIHEKKGLTKYKSSPEKWSTASDPYSDFEKVTGRIDKNVSPEARHPLVAAYPIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEVHGNAEVHASFFDIGGSVSAGFSNSNSSTVAIDHSLSLAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTSLVLGKNQTLATIKAKENQLSQILAPNNYYPSKNLAPIALNAQDDFSSTPITMNYNQFLELEKTKQLRLDTDQVYGNIATYNFENGRVRVDTGSNWSEVLPQIQETTARIIFNGKDLNLVERRIAAVNPSDPLETTKPDMTLKEALKIAFGFNEPNGNLQYQGKDITEFDFNFDQQTSQNIKNQLAELNATNIYTVLDKIKLNAKMNILIRDKRFHYDRNNIAVGADESVVKEAHREVINSSTEGLLLNIDKDIRKILSGYIVEIEDTEGLKEVINDRYDMLNISSLRQDGKTFIDFKKYNDKLPLYISNPNYKVNVYAVTKENTIINPSENGDTSTNGIKKILIFSKKGYEIG	Successful	Efficacy of ETI-204 monoclonal antibody as an adjunct therapy in a New Zealand white rabbit partial survival model for inhalational anthrax. Antimicrob Agents Chemother. 2015 Apr;59(4):2206-14.	34	.	.	.	.	.	.	.	.	.	.	bar04621: NOD-like receptor signaling pathway	R-HSA-5210891: Uptake and function of anthrax toxins	.	P13423
TTOD34I	Anthrax toxin receptor 2	.	ANTR2_HUMAN	Single Protein	Capillary morphogenesis gene 2 protein; CMG-2	ANTXR2	Necessary for cellular interactions with laminin and the extracellular matrix.	.	.	MVAERSPARSPGSWLFPGLWLLVLSGPGGLLRAQEQPSCRRAFDLYFVLDKSGSVANNWIEIYNFVQQLAERFVSPEMRLSFIVFSSQATIILPLTGDRGKISKGLEDLKRVSPVGETYIHEGLKLANEQIQKAGGLKTSSIIIALTDGKLDGLVPSYAEKEAKISRSLGASVYCVGVLDFEQAQLERIADSKEQVFPVKGGFQALKGIINSILAQSCTEILELQPSSVCVGEEFQIVLSGRGFMLGSRNGSVLCTYTVNETYTTSVKPVSVQLNSMLCPAPILNKAGETLDVSVSFNGGKSVISGSLIVTATECSNGIAAIIVILVLLLLLGIGLMWWFWPLCCKVVIKDPPPPPAPAPKEEEEEPLPTKKWPTVDASYYGGRGVGGIKRMEVRWGDKGSTEEGARLEKAKNAVVKIPEETEEPIRPRPPRPKPTHQPPQTKWYTPIKGRLDALWALLRRQYDRVSLMRPQEGDEVCIWECIEKELTA	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P58335
TTUCK4B	Phospholipase A2 inhibitory protein (PA2IP)	P04083	ANXA1_HUMAN	.	p35; Lipocortin I; LPC1; Chromobindin-9; Calpactin-2; Calpactin II; Annexin-1; Annexin I; Annexin A1; ANX1	ANXA1	"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)."	.	5VFW; 1QLS; 1BO9; 1AIN	MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN	Successful	2008 FDA drug approvals. Nat Rev Drug Discov. 2009 Feb;8(2):93-6.	34	.	.	.	.	.	.	.	.	.	.	.	R-HSA-416476: G alpha (q) signalling events; R-HSA-418594: G alpha (i) signalling events; R-HSA-444473: Formyl peptide receptors bind formyl peptides and many other ligands; R-HSA-445355: Smooth Muscle Contraction; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling	.	P04083
TT0NL6U	Annexin A10 (ANXA10)	Q9UJ72	ANX10_HUMAN	Annexin protein	Annexin-14; Annexin-10; ANX14	ANXA10	"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."	.	.	MFCGDYVQGTIFPAPNFNPIMDAQMLGGALQGFDCDKDMLINILTQRCNAQRMMIAEAYQSMYGRDLIGDMREQLSDHFKDVMAGLMYPPPLYDAHELWHAMKGVGTDENCLIEILASRTNGEIFQMREAYCLQYSNNLQEDIYSETSGHFRDTLMNLVQGTREEGYTDPAMAAQDAMVLWEACQQKTGEHKTMLQMILCNKSYQQLRLVFQEFQNISGQDMVDAINECYDGYFQELLVAIVLCVRDKPAYFAYRLYSAIHDFGFHNKTVIRILIARSEIDLLTIRKRYKERYGKSLFHDIRNFASGHYKKALLAICAGDAEDY	Literature-reported	"Down-regulation of annexin A10 in hepatocellular carcinoma is associated with vascular invasion, early recurrence, and poor prognosis in synergy wi... Am J Pathol. 2002 May;160(5):1831-7."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9UJ72
TT4YANI	Annexin A2 (ANXA2)	P07355	ANXA2_HUMAN	Annexin protein	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	ANXA2	"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."	.	5N7G; 5N7F; 5N7D; 5LQ2; 5LQ0	MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNAQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD	Literature-reported	Annexin A2 inhibition suppresses ovarian cancer progression via regulating -catenin/EMT. Oncol Rep. 2017 Jun;37(6):3643-3650.	.	TC=1.A.31	Annexin family	annexin family.	.	.	Annexin	PF00191	PF00191; Annexin	1.A.31.1.4	The Annexin (Annexin) Family	hsa05132: Salmonella infection	R-HSA-445355: Smooth Muscle Contraction; R-HSA-6798695: Neutrophil degranulation; R-HSA-75205: Dissolution of Fibrin Clot; R-HSA-8950505: Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation	.	P07355
TTM7D9O	Annexin II receptor (ANXA2R)	Q3ZCQ2	AX2R_HUMAN	.	Annexin2 receptor; AXIIR; ANXA2R	ANXA2R	May act as a receptor for annexin II on marrow stromal cells to induce osteoclast formation.	.	.	MEQHFLGCVKRAWDSAEVAPEPQPPPIVSSEDRGPWPLPLYPVLGEYSLDSCDLGLLSSPCWRLPGVYWQNGLSPGVQSTLEPSTAKPTEFSWPGTQKQQEAPVEEVGQAEEPDRLRLQQLPWSSPLHPWDRQQDTEVCDSGCLLERRHPPALQPWRHLPGFSDCLEWILRVGFAAFSVLWACCSRICGAKQP	Literature-reported	SiRNA directed against annexin II receptor inhibits angiogenesis via suppressing MMP2 and MMP9 expression. Cell Physiol Biochem. 2015;35(3):875-84.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q3ZCQ2
TT2Z83I	Annexin A5 (ANXA5)	P08758	ANXA5_HUMAN	Annexin protein	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	ANXA5	"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."	.	2XO3; 2XO2; 1SAV; 1HVG; 1HVF	MAQVLRGTVTDFPGFDERADAETLRKAMKGLGTDEESILTLLTSRSNAQRQEISAAFKTLFGRDLLDDLKSELTGKFEKLIVALMKPSRLYDAYELKHALKGAGTNEKVLTEIIASRTPEELRAIKQVYEEEYGSSLEDDVVGDTSGYYQRMLVVLLQANRDPDAGIDEAQVEQDAQALFQAGELKWGTDEEKFITIFGTRSVSHLRKVFDKYMTISGFQIEETIDRETSGNLEQLLLAVVKSIRSIPAYLAETLYYAMKGAGTDDHTLIRVMVSRSEIDLFNIRKEFRKNFATSLYSMIKGDTSGDYKKALLLLCGEDD	Clinical trial	Expression and purification of recombinant human annexin V in Escherichia coli. Prep Biochem Biotechnol. 2000 Nov;30(4):305-12.	21	TC=1.A.31	Annexin family	annexin family.	.	.	Annexin	PF00191	PF00191; Annexin	1.A.31.1.7	The Annexin (Annexin) Family	.	R-HSA-114608: Platelet degranulation	.	P08758
TTSW16P	Annexin A8 (ANXA8)	P13928	ANXA8_HUMAN	Annexin protein	Vascular anticoagulant-beta; VAC-beta; Annexin-8; Annexin VIII; ANX8	ANXA8	"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."	.	1W45; 1W3W	MAWWKSWIEQEGVTVKSSSHFNPDPDAETLYKAMKGIGTNEQAIIDVLTKRSNTQRQQIAKSFKAQFGKDLTETLKSELSGKFERLIVALMYPPYRYEAKELHDAMKGLGTKEGVIIEILASRTKNQLREIMKAYEEDYGSSLEEDIQADTSGYLERILVCLLQGSRDDVSSFVDPGLALQDAQDLYAAGEKIRGTDEMKFITILCTRSATHLLRVFEEYEKIANKSIEDSIKSETHGSLEEAMLTVVKCTQNLHSYFAERLYYAMKGAGTRDGTLIRNIVSRSEIDLNLIKCHFKKMYGKTLSSMIMEDTSGDYKNALLSLVGSDP	Literature-reported	Annexin A8 Is a Prognostic Marker and Potential Therapeutic Target for Pancreatic Cancer. Pancreas. 2015 Jan;44(1):122-7.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P13928
TT2EJXQ	Acyloxyacyl hydrolase (neutrophil)	P28039	AOAH_HUMAN	.	Acyloxyacyl hydrolase	AOAH	"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)."	EC 3.1.1.77	5W7C; 5W78	MQSPWKILTVAPLFLLLSLQSSASPANDDQSRPSLSNGHTCVGCVLVVSVIEQLAQVHNSTVQASMERLCSYLPEKLFLKTTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFCKQNTGQPLCHLYPLPKETWKFTLQKARQIVKKSPILKYSRSGSDICSLPVLAKICQKIKLAMEQSVPFKDVDSDKYSVFPTLRGYHWRGRDCNDSDESVYPGRRPNNWDVHQDSNCNGIWGVDPKDGVPYEKKFCEGSQPRGIILLGDSAGAHFHISPEWITASQMSLNSFINLPTALTNELDWPQLSGATGFLDSTVGIKEKSIYLRLWKRNHCNHRDYQNISRNGASSRNLKKFIESLSRNKVLDYPAIVIYAMIGNDVCSGKSDPVPAMTTPEKLYSNVMQTLKHLNSHLPNGSHVILYGLPDGTFLWDNLHNRYHPLGQLNKDMTYAQLYSFLNCLQVSPCHGWMSSNKTLRTLTSERAEQLSNTLKKIAASEKFTNFNLFYMDFAFHEIIQEWQKRGGQPWQLIEPVDGFHPNEVALLLLADHFWKKVQLQWPQILGKENPFNPQIKQVFGDQGGH	Literature-reported	"A high-throughput, multiplexed assay for superfamily-wide profiling of enzyme activity. Nat Chem Biol. 2014 Aug;10(8):656-63."	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P28039
TTM3B5R	Diamine oxidase (AOC1)	P19801	AOC1_HUMAN	CH-NH(2) donor oxidoreductase	Kidney amine oxidase; KAO; Histaminase; Amiloride-binding protein; AOC1; ABP	AOC1	"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."	EC 1.4.3.22	3MPH; 3K5T; 3HII; 3HIG; 3HI7	MPALGWAVAAILMLQTAMAEPSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSSTTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAVIFFGDQEHPNVTEFAVGPLPGPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDRCLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNGKFYGSPEELARKYADGEVDVVVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGPRLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVHFGGERIAYEVSVQEAVALYGGHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFEMPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMHATGYVHATFYTPEGLRHGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENITNPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFTSPQENPWGHKRTYRLQIHSMADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWHPPVVFEQFLHNNENIENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRDNGPNYVQRWIPEDRDCSMPPPFSYNGTYRPV	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	hsa00330:Arginine and proline metabolism; hsa00340:Histidine metabolism; hsa00380:Tryptophan metabolism	R-HSA-211945: Phase I - Functionalization of compounds; R-HSA-6798695: Neutrophil degranulation	MetaCyc:HS00083-MON	P19801
TT7HC21	Membrane copper amine oxidase (AOC3)	Q16853	AOC3_HUMAN	CH-NH(2) donor oxidoreductase	Vascular adhesion protein-1; Vascular adhesion protein 1; VAP1; VAP-1; Semicarbazide-sensitive amine oxidase; SSAO; Membrane primary amine oxidase; HPAO; Copper amine oxidase	AOC3	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.	EC 1.4.3.21	4BTY; 4BTX; 4BTW; 3ALA; 2Y74	MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLFADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPPAREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDIDQMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFLHHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSWSLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLVYEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQAPKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFHPSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVWAEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHPRGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDFSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSADSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN	Successful	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	34	EC:1.4	.	copper/topaquinone oxidase family.	1.4.3.21 	Acting on the CH-NH2 group of donors	"Copper amine oxidase, enzyme domain; Copper amine oxidase, N2 domain; Copper amine oxidase, N3 domain"	PF01179; PF02727; PF02728	PF01179; Cu_amine_oxid; PF02727; Cu_amine_oxidN2; PF02728; Cu_amine_oxidN3	.	.	"hsa00260:Glycine, serine and threonine metabolism; hsa00350:Tyrosine metabolism; hsa00360:Phenylalanine metabolism; hsa00410:beta-Alanine metabolism; hsa01100:Metabolic pathways"	R-HSA-211945: Phase I - Functionalization of compounds	.	Q16853
TT3MOS2	Aldehyde oxidase (AOX1)	Q06278	AOXA_HUMAN	Aldehyde/oxo donor oxidoreductase	AOX1	AOX1	"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."	EC 1.2.3.1	6Q6Q; 5EPG; 4UHX; 4UHW	MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPGMVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCCLDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTRVFGSERMMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHAYNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHIISRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSRKWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKLIGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPVHYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYCDDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAEKFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPERKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKYIQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGEDMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKFPNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPEKVRIINMYKEIDQTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLGSRAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETVPNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVGYFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAIDIGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSNTLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFTKMIPRDEPGSYVPWNVPI	Successful	Inhibition by SKF-525A of the aldehyde oxidase-mediated metabolism of the experimental antitumour agent acridine carboxamide. Biochem Pharmacol. 1993 May 25;45(10):2159-62.	34	.	.	.	.	.	.	.	.	.	.	"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"	R-HSA-964975: Vitamins B6 activation to pyridoxal phosphate	MetaCyc:ENSG00000138356-MON	Q06278
TTSMK36	Adenomatous polyposis coli 2 (APC2)	O95996	APCL_HUMAN	.	Adenomatous polyposis coli proteinlike; Adenomatous polyposis coli protein-like; Adenomatous polyposis coli protein 2; APClike; APCL; APC-like	APC2	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.	.	.	MASSVAPYEQLVRQVEALKAENSHLRQELRDNSSHLSKLETETSGMKEVLKHLQGKLEQEARVLVSSGQTEVLEQLKALQMDITSLYNLKFQPPTLGPEPAARTPEGSPVHGSGPSKDSFGELSRATIRLLEELDRERCFLLNEIEKEEKEKLWYYSQLQGLSKRLDELPHVETQFSMQMDLIRQQLEFEAQHIRSLMEERFGTSDEMVQRAQIRASRLEQIDKELLEAQDRVQQTEPQALLAVKSVPVDEDPETEVPTHPEDGTPQPGNSKVEVVFWLLSMLATRDQEDTARTLLAMSSSPESCVAMRRSGCLPLLLQILHGTEAAAGGRAGAPGAPGAKDARMRANAALHNIVFSQPDQGLARKEMRVLHVLEQIRAYCETCWDWLQARDGGPEGGGAGSAPIPIEPQICQATCAVMKLSFDEEYRRAMNELGGLQAVAELLQVDYEMHKMTRDPLNLALRRYAGMTLTNLTFGDVANKATLCARRGCMEAIVAQLASDSEELHQVVSSILRNLSWRADINSKKVLREAGSVTALVQCVLRATKESTLKSVLSALWNLSAHSTENKAAICQVDGALGFLVSTLTYKCQSNSLAIIESGGGILRNVSSLVATREDYRQVLRDHNCLQTLLQHLTSHSLTIVSNACGTLWNLSARSARDQELLWDLGAVGMLRNLVHSKHKMIAMGSAAALRNLLAHRPAKHQAAATAVSPGSCVPSLYVRKQRALEAELDARHLAQALEHLEKQGPPAAEAATKKPLPPLRHLDGLAQDYASDSGCFDDDDAPSSLAAAAATGEPASPAALSLFLGSPFLQGQALARTPPTRRGGKEAEKDTSGEAAVAAKAKAKLALAVARIDQLVEDISALHTSSDDSFSLSSGDPGQEAPREGRAQSCSPCRGPEGGRREAGSRAHPLLRLKAAHASLSNDSLNSGSASDGYCPREHMLPCPLAALASRREDPRCGQPRPSRLDLDLPGCQAEPPAREATSADARVRTIKLSPTYQHVPLLEGASRAGAEPLAGPGISPGARKQAWLPADHLSKVPEKLAAAPLSVASKALQKLAAQEGPLSLSRCSSLSSLSSAGRPGPSEGGDLDDSDSSLEGLEEAGPSEAELDSTWRAPGATSLPVAIPAPRRNRGRGLGVEDATPSSSSENYVQETPLVLSRCSSVSSLGSFESPSIASSIPSEPCSGQGSGTISPSELPDSPGQTMPPSRSKTPPLAPAPQGPPEATQFSLQWESYVKRFLDIADCRERCRLPSELDAGSVRFTVEKPDENFSCASSLSALALHEHYVQQDVELRLLPSACPERGGGAGGAGLHFAGHRRREEGPAPTGSRPRGAADQELELLRECLGAAVPARLRKVASALVPGRRALPVPVYMLVPAPAPAQEDDSCTDSAEGTPVNFSSAASLSDETLQGPPRDQPGGPAGRQRPTGRPTSARQAMGHRHKAGGAGRSAEQSRGAGKNRAGLELPLGRPPSAPADKDGSKPGRTRGDGALQSLCLTTPTEEAVYCFYGNDSDEEPPAAAPTPTHRRTSAIPRAFTRERPQGRKEAPAPSKAAPAAPPPARTQPSLIADETPPCYSLSSSASSLSEPEPSEPPAVHPRGREPAVTKDPGPGGGRDSSPSPRAAEELLQRCISSALPRRRPPVSGLRRRKPRATRLDERPAEGSRERGEEAAGSDRASDLDSVEWRAIQEGANSIVTWLHQAAAATREASSESDSILSFVSGLSVGSTLQPPKHRKGRQAEGEMGSARRPEKRGAASVKTSGSPRSPAGPEKPRGTQKTTPGVPAVLRGRTVIYVPSPAPRAQPKGTPGPRATPRKVAPPCLAQPAAPAKVPSPGQQRSRSLHRPAKTSELATLSQPPRSATPPARLAKTPSSSSSQTSPASQPLPRKRPPVTQAAGALPGPGASPVPKTPARTLLAKQHKTQRSPVRIPFMQRPARRGPPPLARAVPEPGPRGRAGTEAGPGARGGRLGLVRVASALSSGSESSDRSGFRRQLTFIKESPGLRRRRSELSSAESAASAPQGASPRRGRPALPAVFLCSSRCEELRAAPRQGPAPARQRPPAARPSPGERPARRTTSESPSRLPVRAPAARPETVKRYASLPHISVARRPDGAVPAAPASADAARRSSDGEPRPLPRVAAPGTTWRRIRDEDVPHILRSTLPATALPLRGSTPEDAPAGPPPRKTSDAVVQTEEVAAPKTNSSTSPSLETREPPGAPAGGQLSLLGSDVDGPSLAKAPISAPFVHEGLGVAVGGFPASRHGSPSRSARVPPFNYVPSPMVVAATTDSAAEKAPATASATLLE	Literature-reported	Destruction complex function in the Wnt signaling pathway of Drosophila requires multiple interactions between Adenomatous polyposis coli 2 and Arm... Genetics. 2012 Mar;190(3):1059-75.	.	.	.	adenomatous polyposis coli (APC) family.	.	.	"APC basic domain; Coiled-coil N-terminus of APC, dimerisation domain; APC repeat; Adenomatous polyposis coli (APC) repeat; Armadillo/beta-catenin-like repeat; SAMP Motif"	PF05956; PF16689; PF05923; PF18797; PF00514; PF05924	PF05956; APC_basic; PF16689; APC_N_CC; PF05923; APC_r; PF18797; APC_rep; PF00514; Arm; PF05924; SAMP	.	.	hsa04310: Wnt signaling pathway; hsa04390: Hippo signaling pathway; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04810: Regulation of actin cytoskeleton; hsa04934: Cushing syndrome; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05165: Human papillomavirus infection; hsa05200: Pathways in cancer; hsa05206: MicroRNAs in cancer; hsa05210: Colorectal cancer; hsa05213: Endometrial cancer; hsa05217: Basal cell carcinoma; hsa05224: Breast cancer; hsa05225: Hepatocellular carcinoma; hsa05226: Gastric cancer	.	.	O95996
TTB7VAT	Serum amyloid P-component (APCS)	P02743	SAMP_HUMAN	Pentraxin family	SAP; APCS; 9.5S alpha-1-glycoprotein	APCS	Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin.	.	4AYU; 4AVV; 4AVT; 4AVS; 3KQR	MNKPLLWISVLTSLLEAFAHTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV	Clinical trial	Interaction of serum amyloid P component with hexanoyl bis(D-proline) (CPHPC).Acta Crystallogr D Biol Crystallogr.2014 Aug;70(Pt 8):2232-40.	19	.	.	.	.	.	.	.	.	.	.	.	R-HSA-977225:Amyloid formation	.	P02743
TTYWEDQ	Acylamino-acid-releasing enzyme (APEH)	P13798	ACPH_HUMAN	Peptidase	Oxidized protein hydrolase; OPH; DNF15S2 protein; Acylpeptide hydrolase; Acylaminoacyl-peptidase; Acyl-peptide hydrolase; APH; APEH; AARE	APEH	"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."	EC 3.4.19.1	.	MERQVLLSEPEEAAALYRGLSRQPALSAACLGPEVTTQYGGQYRTVHTEWTQRDLERMENIRFCRQYLVFHDGDSVVFAGPAGNSVETRGELLSRESPSGTMKAVLRKAGGTGPGEEKQFLEVWEKNRKLKSFNLSALEKHGPVYEDDCFGCLSWSHSETHLLYVAEKKRPKAESFFQTKALDVSASDDEIARLKKPDQAIKGDQFVFYEDWGENMVSKSIPVLCVLDVESGNISVLEGVPENVSPGQAFWAPGDAGVVFVGWWHEPFRLGIRFCTNRRSALYYVDLIGGKCELLSDDSLAVSSPRLSPDQCRIVYLQYPSLIPHHQCSQLCLYDWYTKVTSVVVDVVPRQLGENFSGIYCSLLPLGCWSADSQRVVFDSAQRSRQDLFAVDTQVGTVTSLTAGGSGGSWKLLTIDQDLMVAQFSTPSLPPTLKVGFLPSAGKEQSVLWVSLEEAEPIPDIHWGIRVLQPPPEQENVQYAGLDFEAILLQPGSPPDKTQVPMVVMPHGGPHSSFVTAWMLFPAMLCKMGFAVLLVNYRGSTGFGQDSILSLPGNVGHQDVKDVQFAVEQVLQEEHFDASHVALMGGSHGGFISCHLIGQYPETYRACVARNPVINIASMLGSTDIPDWCVVEAGFPFSSDCLPDLSVWAEMLDKSPIRYIPQVKTPLLLMLGQEDRRVPFKQGMEYYRALKTRNVPVRLLLYPKSTHALSEVEVESDSFMNAVLWLRTHLGS	Literature-reported	"A high-throughput, multiplexed assay for superfamily-wide profiling of enzyme activity. Nat Chem Biol. 2014 Aug;10(8):656-63."	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-6798695: Neutrophil degranulation; R-HSA-72764: Eukaryotic Translation Termination	MetaCyc:HS08997-MON	P13798
TTHGL48	AP endonuclease 1 (APEX1)	P27695	APEX1_HUMAN	Alpha-carbonic anhydrase	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	APEX1	"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."	EC 3.1.-.-	6MKO; 6MKM; 6MKK; 6MK3; 6BOW	MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL	Clinical trial	Inhibition of APE1/Ref-1 redox activity with APX3330 blocks retinal angiogenesis in vitro and in vivo. Vision Res. 2011 Jan;51(1):93-100.	17	.	.	.	.	.	.	.	.	.	.	hsa03410:Base excision repair	R-HSA-110357: Displacement of DNA glycosylase by APEX1; R-HSA-110362: POLB-Dependent Long Patch Base Excision Repair; R-HSA-110373: Resolution of AP sites via the multiple-nucleotide patch replacement pathway; R-HSA-5651801: PCNA-Dependent Long Patch Base Excision Repair; R-HSA-73930: Abasic sugar-phosphate removal via the single-nucleotide replacement pathway; R-HSA-73933: Resolution of Abasic Sites (AP sites)	.	P27695
TT9W8GU	Gamma-secretase (GS)	Q96BI3; Q8WW43; Q9NZ42; Q92542; P49768	APH1A_HUMAN; APH1B_HUMAN; PEN2_HUMAN; NICA_HUMAN; PSN1_HUMAN	.	Presenilin-stabilization factor-like; PSFL; Aph-1beta	APH1A	"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."	.	.	MGAAVFFGCTFVAFGPAFALFLITVAGDPLRVIILVAGAFFWLVSLLLASVVWFILVHVTDRSDARLQYGLLIFGAAVSVLLQEVFRFAYYKLLKKADEGLASLSEDGRSPISIRQMAYVSGLSFGIISGVFSVINILADALGPGVVGIHGDSPYYFLTSAFLTAAIILLHTFWGVVFFDACERRRYWALGLVVGSHLLTSGLTFLNPWYEASLLPIYAVTVSMGLWAFITAGGSLRSIQRSLLCRRQEDSRVMVYSALRIPPED	Clinical trial	A phase 3 trial of semagacestat for treatment of Alzheimer's disease. N Engl J Med. 2013 Jul 25;369(4):341-50.	25	.	.	.	.	.	.	.	.	.	.	hsa04330:Notch signaling pathway; hsa05010:Alzheimer's disease	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	.	Q96BI3
TTZS04O	Gamma-secretase subunit APH-1A/1B (APH-1)	Q96BI3-Q8WW43	APH1A_HUMAN-APH1B_HUMAN	.	Anterior pharynx-defective 1	APH1A-APH1B	"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."	.	.	MTAAVFFGCAFIAFGPALALYVFTIATEPLRIIFLIAGAFFWLVSLLISSLVWFMARVIIDNKDGPTQKYLLIFGAFVSVYIQEMFRFAYYKLLKKASEGLKSINPGETAPSMRLLAYVSGLGFGIMSGVFSFVNTLSDSLGPGTVGIHGDSPQFFLYSAFMTLVIILLHVFWGIVFFDGCEKKKWGILLIVLLTHLLVSAQTFISSYYGINLASAFIILVLMGTWAFLAAGGSCRSLKLCLLCQDKNFLLYNQRSRMGAAVFFGCTFVAFGPAFALFLITVAGDPLRVIILVAGAFFWLVSLLLASVVWFILVHVTDRSDARLQYGLLIFGAAVSVLLQEVFRFAYYKLLKKADEGLASLSEDGRSPISIRQMAYVSGLSFGIISGVFSVINILADALGPGVVGIHGDSPYYFLTSAFLTAAIILLHTFWGVVFFDACERRRYWALGLVVGSHLLTSGLTFLNPWYEASLLPIYAVTVSMGLWAFITAGGSLRSIQRSLLCRRQEDSRVMVYSALRIPPED	Patented-recorded	Gamma secretase inhibitors: a patent review (2013 - 2015).Expert Opin Ther Pat. 2017 Jul;27(7):851-866.	15.5	.	APH-1 family	.	.	.	.	.	.	.	.	.	.	.	Q96BI3
TT87D3J	APJ endogenous ligand (Apelin)	Q9ULZ1	APEL_HUMAN	.	Apelin13; APEL	APLN	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).	.	.	MNLRLCVQALLLLWLSLTAVCGGSLMPLPDGNGLEDGNVRHLVQPRGSRNGPGPWQGGRRKFRRQRPRLSHKGPMPF	Literature-reported	Apelin/APJ system: A novel potential therapy target for kidney disease. J Cell Physiol. 2018 May;233(5):3892-3900.	.	.	Apelin family	apelin family.	.	.	APJ endogenous ligand	PF15360	PF15360; Apelin	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04371: Apelin signaling pathway	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-418594: G alpha (i) signalling events	.	Q9ULZ1
TTJ8E43	Apelin receptor (APLNR)	P35414	APJ_HUMAN	.	G-protein coupled receptor HG11; G-protein coupled receptor APJ; Angiotensin receptor-like 1; APJ; AGTRL1	APLNR	"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."	.	5VBL; 2LOW; 2LOV; 2LOU; 2LOT	MEEGGDFDNYYGADNQSECEYTDWKSSGALIPAIYMLVFLLGTTGNGLVLWTVFRSSREKRRSADIFIASLAVADLTFVVTLPLWATYTYRDYDWPFGTFFCKLSSYLIFVNMYASVFCLTGLSFDRYLAIVRPVANARLRLRVSGAVATAVLWVLAALLAMPVMVLRTTGDLENTTKVQCYMDYSMVATVSSEWAWEVGLGVSSTTVGFVVPFTIMLTCYFFIAQTIAGHFRKERIEGLRKRRRLLSIIVVLVVTFALCWMPYHLVKTLYMLGSLLHWPCDFDLFLMNIFPYCTCISYVNSCLNPFLYAFFDPRFRQACTSMLCCGQSRCAGTSHSSSGEKSASYSSGHSQGPGPNMGKGGEQMHEKSIPYSQETLVVD	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04371: Apelin signaling pathway	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-418594: G alpha (i) signalling events	.	P35414
TT5S8DR	APOA1 messenger RNA (APOA1 mRNA)	P02647	APOA1_HUMAN	mRNA target	Truncated apolipoprotein AI (mRNA); Apolipoprotein A1 (mRNA); Apolipoprotein A-I (mRNA); ApoAI (mRNA); ApoA-I (mRNA); Apo-AI (mRNA)	APOA1	"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)."	.	6CM1; 6CLZ; 6CCX; 6CCH; 6CC9	MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ	Literature-reported	"US patent application no. 7,259,150, Modulation of apolipoprotein (a) expression."	0	mRNA	mRNA target	.	.	.	Apolipoprotein A1/A4/E domain	PF01442	PF01442; Apolipoprotein	.	.	hsa03320:PPAR signaling pathway; hsa04975:Fat digestion and absorption; hsa04977:Vitamin digestion and absorption; hsa05143:African trypanosomiasis	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	.	P02647
TT7GN3U	Apolipoprotein A-I (APOA1)	P02647	APOA1_HUMAN	Apolipoprotein	Truncated apolipoprotein AI; Apolipoprotein A1; ApoAI; ApoA-I; Apo-AI	APOA1	"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)."	.	6CM1; 6CLZ; 6CCX; 6CCH; 6CC9	MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ	Clinical trial	"CER-001, a HDL-mimetic, stimulates the reverse lipid transport and atherosclerosis regression in high cholesterol diet-fed LDL-receptor deficient mice. Atherosclerosis. 2014 Jan;232(1):110-8."	21	Apolipoprotein	Apolipoprotein	apolipoprotein A1/A4/E family.	.	.	Apolipoprotein A1/A4/E domain	PF01442	PF01442; Apolipoprotein	.	.	hsa03320:PPAR signaling pathway; hsa04975:Fat digestion and absorption; hsa04977:Vitamin digestion and absorption; hsa05143:African trypanosomiasis	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	.	P02647
TTGQA9W	Apolipoprotein A-II (APOA2)	P02652	APOA2_HUMAN	Apolipoprotein	Apolipoprotein A2; ApoA-II; Apo-AII	APOA2	"May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism."	.	.	MKLLAATVLLLTICSLEGALVRRQAKEPCVESLVSQYFQTVTDYGKDLMEKVKSPELQAEAKSYFEKSKEQLTPLIKKAGTELVNFLSYFVELGTQPATQ	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	Apolipoprotein	Apolipoprotein	apolipoprotein A2 family.	.	.	Apolipoprotein A-II (ApoA-II)	PF04711	PF04711; ApoA-II	.	.	hsa03320:PPAR signaling pathway	R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-1989781:PPARA activates gene expression; R-HSA-975634:Retinoid metabolism and transport	.	P02652
TTNC3WS	Apolipoprotein A-IV (APOA4)	P06727	APOA4_HUMAN	Apolipoprotein	Apolipoprotein A4; ApoAIV; APOA4	APOA4	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.	.	3S84	MFLKAVVLTLALVAVAGARAEVSADQVATVMWDYFSQLSNNAKEAVEHLQKSELTQQLNALFQDKLGEVNTYAGDLQKKLVPFATELHERLAKDSEKLKEEIGKELEELRARLLPHANEVSQKIGDNLRELQQRLEPYADQLRTQVSTQAEQLRRQLTPYAQRMERVLRENADSLQASLRPHADELKAKIDQNVEELKGRLTPYADEFKVKIDQTVEELRRSLAPYAQDTQEKLNHQLEGLTFQMKKNAEELKARISASAEELRQRLAPLAEDVRGNLRGNTEGLQKSLAELGGHLDQQVEEFRRRVEPYGENFNKALVQQMEQLRQKLGPHAGDVEGHLSFLEKDLRDKVNSFFSTFKEKESQDKTLSLPELEQQQEQQQEQQQEQVQMLAPLES	Literature-reported	Apolipoprotein L1 and apolipoprotein A-IV and their association with kidney function. Curr Opin Lipidol. 2017 Feb;28(1):39-45.	.	.	.	.	.	.	.	.	.	.	.	hsa04975: Fat digestion and absorption; hsa04977: Vitamin digestion and absorption; hsa04979: Cholesterol metabolism; hsa05417: Lipid and atherosclerosis	R-HSA-8963888: Chylomicron assembly; R-HSA-8963889: Assembly of active LPL and LIPC lipase complexes; R-HSA-8963901: Chylomicron remodeling; R-HSA-975634: Retinoid metabolism and transport; R-HSA-977225: Amyloid fiber formation	.	P06727
TTN1IE2	APOB messenger RNA (APOB mRNA)	P04114	APOB_HUMAN	mRNA target	Apolipoprotein B48 (mRNA); Apolipoprotein B-100 (mRNA); Apo B48 (mRNA); Apo B100 (mRNA); Apo B-100 (mRNA)	APOB	"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)."	.	.	MDPPRPALLALLALPALLLLLLAGARAEEEMLENVSLVCPKDATRFKHLRKYTYNYEAESSSGVPGTADSRSATRINCKVELEVPQLCSFILKTSQCTLKEVYGFNPEGKALLKKTKNSEEFAAAMSRYELKLAIPEGKQVFLYPEKDEPTYILNIKRGIISALLVPPETEEAKQVLFLDTVYGNCSTHFTVKTRKGNVATEISTERDLGQCDRFKPIRTGISPLALIKGMTRPLSTLISSSQSCQYTLDAKRKHVAEAICKEQHLFLPFSYKNKYGMVAQVTQTLKLEDTPKINSRFFGEGTKKMGLAFESTKSTSPPKQAEAVLKTLQELKKLTISEQNIQRANLFNKLVTELRGLSDEAVTSLLPQLIEVSSPITLQALVQCGQPQCSTHILQWLKRVHANPLLIDVVTYLVALIPEPSAQQLREIFNMARDQRSRATLYALSHAVNNYHKTNPTGTQELLDIANYLMEQIQDDCTGDEDYTYLILRVIGNMGQTMEQLTPELKSSILKCVQSTKPSLMIQKAAIQALRKMEPKDKDQEVLLQTFLDDASPGDKRLAAYLMLMRSPSQADINKIVQILPWEQNEQVKNFVASHIANILNSEELDIQDLKKLVKEALKESQLPTVMDFRKFSRNYQLYKSVSLPSLDPASAKIEGNLIFDPNNYLPKESMLKTTLTAFGFASADLIEIGLEGKGFEPTLEALFGKQGFFPDSVNKALYWVNGQVPDGVSKVLVDHFGYTKDDKHEQDMVNGIMLSVEKLIKDLKSKEVPEARAYLRILGEELGFASLHDLQLLGKLLLMGARTLQGIPQMIGEVIRKGSKNDFFLHYIFMENAFELPTGAGLQLQISSSGVIAPGAKAGVKLEVANMQAELVAKPSVSVEFVTNMGIIIPDFARSGVQMNTNFFHESGLEAHVALKAGKLKFIIPSPKRPVKLLSGGNTLHLVSTTKTEVIPPLIENRQSWSVCKQVFPGLNYCTSGAYSNASSTDSASYYPLTGDTRLELELRPTGEIEQYSVSATYELQREDRALVDTLKFVTQAEGAKQTEATMTFKYNRQSMTLSSEVQIPDFDVDLGTILRVNDESTEGKTSYRLTLDIQNKKITEVALMGHLSCDTKEERKIKGVISIPRLQAEARSEILAHWSPAKLLLQMDSSATAYGSTVSKRVAWHYDEEKIEFEWNTGTNVDTKKMTSNFPVDLSDYPKSLHMYANRLLDHRVPQTDMTFRHVGSKLIVAMSSWLQKASGSLPYTQTLQDHLNSLKEFNLQNMGLPDFHIPENLFLKSDGRVKYTLNKNSLKIEIPLPFGGKSSRDLKMLETVRTPALHFKSVGFHLPSREFQVPTFTIPKLYQLQVPLLGVLDLSTNVYSNLYNWSASYSGGNTSTDHFSLRARYHMKADSVVDLLSYNVQGSGETTYDHKNTFTLSYDGSLRHKFLDSNIKFSHVEKLGNNPVSKGLLIFDASSSWGPQMSASVHLDSKKKQHLFVKEVKIDGQFRVSSFYAKGTYGLSCQRDPNTGRLNGESNLRFNSSYLQGTNQITGRYEDGTLSLTSTSDLQSGIIKNTASLKYENYELTLKSDTNGKYKNFATSNKMDMTFSKQNALLRSEYQADYESLRFFSLLSGSLNSHGLELNADILGTDKINSGAHKATLRIGQDGISTSATTNLKCSLLVLENELNAELGLSGASMKLTTNGRFREHNAKFSLDGKAALTELSLGSAYQAMILGVDSKNIFNFKVSQEGLKLSNDMMGSYAEMKFDHTNSLNIAGLSLDFSSKLDNIYSSDKFYKQTVNLQLQPYSLVTTLNSDLKYNALDLTNNGKLRLEPLKLHVAGNLKGAYQNNEIKHIYAISSAALSASYKADTVAKVQGVEFSHRLNTDIAGLASAIDMSTNYNSDSLHFSNVFRSVMAPFTMTIDAHTNGNGKLALWGEHTGQLYSKFLLKAEPLAFTFSHDYKGSTSHHLVSRKSISAALEHKVSALLTPAEQTGTWKLKTQFNNNEYSQDLDAYNTKDKIGVELTGRTLADLTLLDSPIKVPLLLSEPINIIDALEMRDAVEKPQEFTIVAFVKYDKNQDVHSINLPFFETLQEYFERNRQTIIVVLENVQRNLKHINIDQFVRKYRAALGKLPQQANDYLNSFNWERQVSHAKEKLTALTKKYRITENDIQIALDDAKINFNEKLSQLQTYMIQFDQYIKDSYDLHDLKIAIANIIDEIIEKLKSLDEHYHIRVNLVKTIHDLHLFIENIDFNKSGSSTASWIQNVDTKYQIRIQIQEKLQQLKRHIQNIDIQHLAGKLKQHIEAIDVRVLLDQLGTTISFERINDILEHVKHFVINLIGDFEVAEKINAFRAKVHELIERYEVDQQIQVLMDKLVELAHQYKLKETIQKLSNVLQQVKIKDYFEKLVGFIDDAVKKLNELSFKTFIEDVNKFLDMLIKKLKSFDYHQFVDETNDKIREVTQRLNGEIQALELPQKAEALKLFLEETKATVAVYLESLQDTKITLIINWLQEALSSASLAHMKAKFRETLEDTRDRMYQMDIQQELQRYLSLVGQVYSTLVTYISDWWTLAAKNLTDFAEQYSIQDWAKRMKALVEQGFTVPEIKTILGTMPAFEVSLQALQKATFQTPDFIVPLTDLRIPSVQINFKDLKNIKIPSRFSTPEFTILNTFHIPSFTIDFVEMKVKIIRTIDQMLNSELQWPVPDIYLRDLKVEDIPLARITLPDFRLPEIAIPEFIIPTLNLNDFQVPDLHIPEFQLPHISHTIEVPTFGKLYSILKIQSPLFTLDANADIGNGTTSANEAGIAASITAKGESKLEVLNFDFQANAQLSNPKINPLALKESVKFSSKYLRTEHGSEMLFFGNAIEGKSNTVASLHTEKNTLELSNGVIVKINNQLTLDSNTKYFHKLNIPKLDFSSQADLRNEIKTLLKAGHIAWTSSGKGSWKWACPRFSDEGTHESQISFTIEGPLTSFGLSNKINSKHLRVNQNLVYESGSLNFSKLEIQSQVDSQHVGHSVLTAKGMALFGEGKAEFTGRHDAHLNGKVIGTLKNSLFFSAQPFEITASTNNEGNLKVRFPLRLTGKIDFLNNYALFLSPSAQQASWQVSARFNQYKYNQNFSAGNNENIMEAHVGINGEANLDFLNIPLTIPEMRLPYTIITTPPLKDFSLWEKTGLKEFLKTTKQSFDLSVKAQYKKNKHRHSITNPLAVLCEFISQSIKSFDRHFEKNRNNALDFVTKSYNETKIKFDKYKAEKSHDELPRTFQIPGYTVPVVNVEVSPFTIEMSAFGYVFPKAVSMPSFSILGSDVRVPSYTLILPSLELPVLHVPRNLKLSLPDFKELCTISHIFIPAMGNITYDFSFKSSVITLNTNAELFNQSDIVAHLLSSSSSVIDALQYKLEGTTRLTRKRGLKLATALSLSNKFVEGSHNSTVSLTTKNMEVSVATTTKAQIPILRMNFKQELNGNTKSKPTVSSSMEFKYDFNSSMLYSTAKGAVDHKLSLESLTSYFSIESSTKGDVKGSVLSREYSGTIASEANTYLNSKSTRSSVKLQGTSKIDDIWNLEVKENFAGEATLQRIYSLWEHSTKNHLQLEGLFFTNGEHTSKATLELSPWQMSALVQVHASQPSSFHDFPDLGQEVALNANTKNQKIRWKNEVRIHSGSFQSQVELSNDQEKAHLDIAGSLEGHLRFLKNIILPVYDKSLWDFLKLDVTTSIGRRQHLRVSTAFVYTKNPNGYSFSIPVKVLADKFIIPGLKLNDLNSVLVMPTFHVPFTDLQVPSCKLDFREIQIYKKLRTSSFALNLPTLPEVKFPEVDVLTKYSQPEDSLIPFFEITVPESQLTVSQFTLPKSVSDGIAALDLNAVANKIADFELPTIIVPEQTIEIPSIKFSVPAGIVIPSFQALTARFEVDSPVYNATWSASLKNKADYVETVLDSTCSSTVQFLEYELNVLGTHKIEDGTLASKTKGTFAHRDFSAEYEEDGKYEGLQEWEGKAHLNIKSPAFTDLHLRYQKDKKGISTSAASPAVGTVGMDMDEDDDFSKWNFYYSPQSSPDKKLTIFKTELRVRESDEETQIKVNWEEEAASGLLTSLKDNVPKATGVLYDYVNKYHWEHTGLTLREVSSKLRRNLQNNAEWVYQGAIRQIDDIDVRFQKAASGTTGTYQEWKDKAQNLYQELLTQEGQASFQGLKDNVFDGLVRVTQEFHMKVKHLIDSLIDFLNFPRFQFPGKPGIYTREELCTMFIREVGTVLSQVYSKVHNGSEILFSYFQDLVITLPFELRKHKLIDVISMYRELLKDLSKEAQEVFKAIQSLKTTEVLRNLQDLLQFIFQLIEDNIKQLKEMKFTYLINYIQDEINTIFSDYIPYVFKLLKENLCLNLHKFNEFIQNELQEASQELQQIHQYIMALREEYFDPSIVGWTVKYYELEEKIVSLIKNLLVALKDFHSEYIVSASNFTSQLSSQVEQFLHRNIQEYLSILTDPDGKGKEKIAELSATAQEIIKSQAIATKKIISDYHQQFRYKLQDFSDQLSDYYEKFIAESKRLIDLSIQNYHTFLIYITELLKKLQSTTVMNPYMKLAPGELTIIL	Successful	Design and development of antisense drugs. Expert Opin. Drug Discov. 2008 3(10):1189-1207.	34	mRNA	mRNA target	.	.	.	Apolipoprotein B100 C terminal; Domain of Unknown Function (DUF1081); Domain of unknown function (DUF1943); Lipoprotein amino terminal region	PF12491; PF06448; PF09172; PF01347	PF12491; ApoB100_C; PF06448; DUF1081; PF09172; DUF1943; PF01347; Vitellogenin_N	.	.	hsa04975:Fat digestion and absorption; hsa04977:Vitamin digestion and absorption	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	.	.
TT2718H	Apolipoprotein B-100 (APOB)	P04114	APOB_HUMAN	Apolipoprotein	Apolipoprotein B48; Apo B48; Apo B100; Apo B-100	APOB	"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)."	.	.	MDPPRPALLALLALPALLLLLLAGARAEEEMLENVSLVCPKDATRFKHLRKYTYNYEAESSSGVPGTADSRSATRINCKVELEVPQLCSFILKTSQCTLKEVYGFNPEGKALLKKTKNSEEFAAAMSRYELKLAIPEGKQVFLYPEKDEPTYILNIKRGIISALLVPPETEEAKQVLFLDTVYGNCSTHFTVKTRKGNVATEISTERDLGQCDRFKPIRTGISPLALIKGMTRPLSTLISSSQSCQYTLDAKRKHVAEAICKEQHLFLPFSYKNKYGMVAQVTQTLKLEDTPKINSRFFGEGTKKMGLAFESTKSTSPPKQAEAVLKTLQELKKLTISEQNIQRANLFNKLVTELRGLSDEAVTSLLPQLIEVSSPITLQALVQCGQPQCSTHILQWLKRVHANPLLIDVVTYLVALIPEPSAQQLREIFNMARDQRSRATLYALSHAVNNYHKTNPTGTQELLDIANYLMEQIQDDCTGDEDYTYLILRVIGNMGQTMEQLTPELKSSILKCVQSTKPSLMIQKAAIQALRKMEPKDKDQEVLLQTFLDDASPGDKRLAAYLMLMRSPSQADINKIVQILPWEQNEQVKNFVASHIANILNSEELDIQDLKKLVKEALKESQLPTVMDFRKFSRNYQLYKSVSLPSLDPASAKIEGNLIFDPNNYLPKESMLKTTLTAFGFASADLIEIGLEGKGFEPTLEALFGKQGFFPDSVNKALYWVNGQVPDGVSKVLVDHFGYTKDDKHEQDMVNGIMLSVEKLIKDLKSKEVPEARAYLRILGEELGFASLHDLQLLGKLLLMGARTLQGIPQMIGEVIRKGSKNDFFLHYIFMENAFELPTGAGLQLQISSSGVIAPGAKAGVKLEVANMQAELVAKPSVSVEFVTNMGIIIPDFARSGVQMNTNFFHESGLEAHVALKAGKLKFIIPSPKRPVKLLSGGNTLHLVSTTKTEVIPPLIENRQSWSVCKQVFPGLNYCTSGAYSNASSTDSASYYPLTGDTRLELELRPTGEIEQYSVSATYELQREDRALVDTLKFVTQAEGAKQTEATMTFKYNRQSMTLSSEVQIPDFDVDLGTILRVNDESTEGKTSYRLTLDIQNKKITEVALMGHLSCDTKEERKIKGVISIPRLQAEARSEILAHWSPAKLLLQMDSSATAYGSTVSKRVAWHYDEEKIEFEWNTGTNVDTKKMTSNFPVDLSDYPKSLHMYANRLLDHRVPQTDMTFRHVGSKLIVAMSSWLQKASGSLPYTQTLQDHLNSLKEFNLQNMGLPDFHIPENLFLKSDGRVKYTLNKNSLKIEIPLPFGGKSSRDLKMLETVRTPALHFKSVGFHLPSREFQVPTFTIPKLYQLQVPLLGVLDLSTNVYSNLYNWSASYSGGNTSTDHFSLRARYHMKADSVVDLLSYNVQGSGETTYDHKNTFTLSYDGSLRHKFLDSNIKFSHVEKLGNNPVSKGLLIFDASSSWGPQMSASVHLDSKKKQHLFVKEVKIDGQFRVSSFYAKGTYGLSCQRDPNTGRLNGESNLRFNSSYLQGTNQITGRYEDGTLSLTSTSDLQSGIIKNTASLKYENYELTLKSDTNGKYKNFATSNKMDMTFSKQNALLRSEYQADYESLRFFSLLSGSLNSHGLELNADILGTDKINSGAHKATLRIGQDGISTSATTNLKCSLLVLENELNAELGLSGASMKLTTNGRFREHNAKFSLDGKAALTELSLGSAYQAMILGVDSKNIFNFKVSQEGLKLSNDMMGSYAEMKFDHTNSLNIAGLSLDFSSKLDNIYSSDKFYKQTVNLQLQPYSLVTTLNSDLKYNALDLTNNGKLRLEPLKLHVAGNLKGAYQNNEIKHIYAISSAALSASYKADTVAKVQGVEFSHRLNTDIAGLASAIDMSTNYNSDSLHFSNVFRSVMAPFTMTIDAHTNGNGKLALWGEHTGQLYSKFLLKAEPLAFTFSHDYKGSTSHHLVSRKSISAALEHKVSALLTPAEQTGTWKLKTQFNNNEYSQDLDAYNTKDKIGVELTGRTLADLTLLDSPIKVPLLLSEPINIIDALEMRDAVEKPQEFTIVAFVKYDKNQDVHSINLPFFETLQEYFERNRQTIIVVLENVQRNLKHINIDQFVRKYRAALGKLPQQANDYLNSFNWERQVSHAKEKLTALTKKYRITENDIQIALDDAKINFNEKLSQLQTYMIQFDQYIKDSYDLHDLKIAIANIIDEIIEKLKSLDEHYHIRVNLVKTIHDLHLFIENIDFNKSGSSTASWIQNVDTKYQIRIQIQEKLQQLKRHIQNIDIQHLAGKLKQHIEAIDVRVLLDQLGTTISFERINDILEHVKHFVINLIGDFEVAEKINAFRAKVHELIERYEVDQQIQVLMDKLVELAHQYKLKETIQKLSNVLQQVKIKDYFEKLVGFIDDAVKKLNELSFKTFIEDVNKFLDMLIKKLKSFDYHQFVDETNDKIREVTQRLNGEIQALELPQKAEALKLFLEETKATVAVYLESLQDTKITLIINWLQEALSSASLAHMKAKFRETLEDTRDRMYQMDIQQELQRYLSLVGQVYSTLVTYISDWWTLAAKNLTDFAEQYSIQDWAKRMKALVEQGFTVPEIKTILGTMPAFEVSLQALQKATFQTPDFIVPLTDLRIPSVQINFKDLKNIKIPSRFSTPEFTILNTFHIPSFTIDFVEMKVKIIRTIDQMLNSELQWPVPDIYLRDLKVEDIPLARITLPDFRLPEIAIPEFIIPTLNLNDFQVPDLHIPEFQLPHISHTIEVPTFGKLYSILKIQSPLFTLDANADIGNGTTSANEAGIAASITAKGESKLEVLNFDFQANAQLSNPKINPLALKESVKFSSKYLRTEHGSEMLFFGNAIEGKSNTVASLHTEKNTLELSNGVIVKINNQLTLDSNTKYFHKLNIPKLDFSSQADLRNEIKTLLKAGHIAWTSSGKGSWKWACPRFSDEGTHESQISFTIEGPLTSFGLSNKINSKHLRVNQNLVYESGSLNFSKLEIQSQVDSQHVGHSVLTAKGMALFGEGKAEFTGRHDAHLNGKVIGTLKNSLFFSAQPFEITASTNNEGNLKVRFPLRLTGKIDFLNNYALFLSPSAQQASWQVSARFNQYKYNQNFSAGNNENIMEAHVGINGEANLDFLNIPLTIPEMRLPYTIITTPPLKDFSLWEKTGLKEFLKTTKQSFDLSVKAQYKKNKHRHSITNPLAVLCEFISQSIKSFDRHFEKNRNNALDFVTKSYNETKIKFDKYKAEKSHDELPRTFQIPGYTVPVVNVEVSPFTIEMSAFGYVFPKAVSMPSFSILGSDVRVPSYTLILPSLELPVLHVPRNLKLSLPDFKELCTISHIFIPAMGNITYDFSFKSSVITLNTNAELFNQSDIVAHLLSSSSSVIDALQYKLEGTTRLTRKRGLKLATALSLSNKFVEGSHNSTVSLTTKNMEVSVATTTKAQIPILRMNFKQELNGNTKSKPTVSSSMEFKYDFNSSMLYSTAKGAVDHKLSLESLTSYFSIESSTKGDVKGSVLSREYSGTIASEANTYLNSKSTRSSVKLQGTSKIDDIWNLEVKENFAGEATLQRIYSLWEHSTKNHLQLEGLFFTNGEHTSKATLELSPWQMSALVQVHASQPSSFHDFPDLGQEVALNANTKNQKIRWKNEVRIHSGSFQSQVELSNDQEKAHLDIAGSLEGHLRFLKNIILPVYDKSLWDFLKLDVTTSIGRRQHLRVSTAFVYTKNPNGYSFSIPVKVLADKFIIPGLKLNDLNSVLVMPTFHVPFTDLQVPSCKLDFREIQIYKKLRTSSFALNLPTLPEVKFPEVDVLTKYSQPEDSLIPFFEITVPESQLTVSQFTLPKSVSDGIAALDLNAVANKIADFELPTIIVPEQTIEIPSIKFSVPAGIVIPSFQALTARFEVDSPVYNATWSASLKNKADYVETVLDSTCSSTVQFLEYELNVLGTHKIEDGTLASKTKGTFAHRDFSAEYEEDGKYEGLQEWEGKAHLNIKSPAFTDLHLRYQKDKKGISTSAASPAVGTVGMDMDEDDDFSKWNFYYSPQSSPDKKLTIFKTELRVRESDEETQIKVNWEEEAASGLLTSLKDNVPKATGVLYDYVNKYHWEHTGLTLREVSSKLRRNLQNNAEWVYQGAIRQIDDIDVRFQKAASGTTGTYQEWKDKAQNLYQELLTQEGQASFQGLKDNVFDGLVRVTQEFHMKVKHLIDSLIDFLNFPRFQFPGKPGIYTREELCTMFIREVGTVLSQVYSKVHNGSEILFSYFQDLVITLPFELRKHKLIDVISMYRELLKDLSKEAQEVFKAIQSLKTTEVLRNLQDLLQFIFQLIEDNIKQLKEMKFTYLINYIQDEINTIFSDYIPYVFKLLKENLCLNLHKFNEFIQNELQEASQELQQIHQYIMALREEYFDPSIVGWTVKYYELEEKIVSLIKNLLVALKDFHSEYIVSASNFTSQLSSQVEQFLHRNIQEYLSILTDPDGKGKEKIAELSATAQEIIKSQAIATKKIISDYHQQFRYKLQDFSDQLSDYYEKFIAESKRLIDLSIQNYHTFLIYITELLKKLQSTTVMNPYMKLAPGELTIIL	Clinical trial	2011 Pipeline of Santaris Pharma.	17	Apolipoprotein	Apolipoprotein	.	.	.	Apolipoprotein B100 C terminal; Domain of Unknown Function (DUF1081); Domain of unknown function (DUF1943); Lipoprotein amino terminal region	PF12491; PF06448; PF09172; PF01347	PF12491; ApoB100_C; PF06448; DUF1081; PF09172; DUF1943; PF01347; Vitellogenin_N	.	.	hsa04975:Fat digestion and absorption; hsa04977:Vitamin digestion and absorption	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	.	.
TTP96KH	Deoxycytidine deaminase	.	ABC3G_HUMAN	Single Protein	APOBEC-related cytidine deaminase; APOBEC-related protein; ARCD; APOBEC-related protein 9; ARP-9; CEM-15; CEM15; Deoxycytidine deaminase; A3G	APOBEC3G	"DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits potent antiviral activity against Vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA."	.	.	MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSELKYHPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGRCQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLDEHSQDLSGRLRAILQNQEN	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9HC16
TTXOZQ1	ApoC-III messenger RNA (APOC3 mRNA)	P02656	APOC3_HUMAN	mRNA target	Apolipoprotein CIII (mRNA); Apolipoprotein C3 (mRNA); Apolipoprotein C-III (mRNA); ApoC-III (mRNA); Apo-CIII (mRNA)	APOC3	"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."	.	2JQ3	MQPRVLLVVALLALLASARASEAEDASLLSFMQGYMKHATKTAKDALSSVQESQVAQQARGWVTDGFSSLKDYWSTVKDKFSEFWDLDPEVRPTSAVAA	Successful	"Clinical pipeline report, company report or official report of ISIS Pharmaceuticals (2011)."	17	mRNA	mRNA target	.	.	.	Apolipoprotein CIII (Apo-CIII)	PF05778	PF05778; Apo-CIII	.	.	hsa03320:PPAR signaling pathway	R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-194223:HDL-mediated lipid transport; R-HSA-975634:Retinoid metabolism and transport	.	P02656
TT4L35O	Apolipoprotein C-III (ApoCIII)	P02656	APOC3_HUMAN	Apolipoprotein	Apolipoprotein CIII; Apolipoprotein C3; ApoC-III; Apo-CIII	APOC3	"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."	.	2JQ3	MQPRVLLVVALLALLASARASEAEDASLLSFMQGYMKHATKTAKDALSSVQESQVAQQARGWVTDGFSSLKDYWSTVKDKFSEFWDLDPEVRPTSAVAA	Clinical trial	"Clinical pipeline report, company report or official report of ISIS Pharmaceuticals."	25	Apolipoprotein	Apolipoprotein	apolipoprotein C3 family.	.	.	Apolipoprotein CIII (Apo-CIII)	PF05778	PF05778; Apo-CIII	.	.	hsa03320:PPAR signaling pathway	R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-194223:HDL-mediated lipid transport; R-HSA-975634:Retinoid metabolism and transport	.	P02656
TTKS9CB	Apolipoprotein E (APOE)	P02649	APOE_HUMAN	Apolipoprotein	ApoE; Apo-E	APOE	"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."	.	6NCO; 6NCN; 2L7B; 2KNY; 2KC3	MKVLWAALLVTFLAGCQAKVEQAVETEPEPELRQQTEWQSGQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELRALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVCGRLVQYRGEVQAMLGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGLSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQIRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGTSAAPVPSDNH	Clinical trial	"Clinical pipeline report, company report or official report of LipimetiX."	21	Apolipoprotein	Apolipoprotein	apolipoprotein A1/A4/E family.	.	.	Apolipoprotein A1/A4/E domain	PF01442	PF01442; Apolipoprotein	.	.	hsa05010:Alzheimer's disease	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	.	P02649
TT2OUI9	Beta-2-glycoprotein 1 (APOH)	P02749	APOH_HUMAN	.	Beta-2-glycoprotein I; Beta(2)GPI; B2GPI; Apolipoprotein H; Apo-H; Anticardiolipin cofactor; Activated protein C-binding protein; APOH; APC inhibitor	APOH	"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."	.	4JHS; 3OP8; 2KRI; 1QUB; 1G4G	MISPVLILFSSFLCHVAIAGRTCPKPDDLPFSTVVPLKTFYEPGEEITYSCKPGYVSRGGMRKFICPLTGLWPINTLKCTPRVCPFAGILENGAVRYTTFEYPNTISFSCNTGFYLNGADSAKCTEEGKWSPELPVCAPIICPPPSIPTFATLRVYKPSAGNNSLYRDTAVFECLPQHAMFGNDTITCTTHGNWTKLPECREVKCPFPSRPDNGFVNYPAKPTLYYKDKATFGCHDGYSLDGPEEIECTKLGNWSAMPSCKASCKVPVKKATVVYQGERVKIQEKFKNGMLHGDKVSFFCKNKEKKCSYTEDAQCIDGTIEVPKCFKEHSSLAFWKTDASDVKPC	Discontinued	Emergence of targeted immune therapies for systemic lupus. Expert Opin Emerg Drugs. 2005 Feb;10(1):53-65.	3	.	.	.	.	.	.	.	.	.	.	hsa04979: Cholesterol metabolism	R-HSA-114608: Platelet degranulation	.	P02749
TTDB8PW	Apolipoprotein L1 messenger RNA (APOL1 mRNA)	O14791	APOL1_HUMAN	mRNA target	Apolipoprotein L (mRNA); Apo-L (mRNA); ApoL (mRNA); Apolipoprotein L-I (mRNA); ApoL-I (mRNA)	APOL1	May play a role in lipid exchange and transport throughout the body. May participate in reverse cholesterol transport from peripheral cells to the liver.	.	7L6K;7LF7;7LFA;7LFB;7LFD	MEGAALLRVSVLCIWMSALFLGVGVRAEEAGARVQQNVPSGTDTGDPQSKPLGDWAAGTMDPESSIFIEDAIKYFKEKVSTQNLLLLLTDNEAWNGFVAAAELPRNEADELRKALDNLARQMIMKDKNWHDKGQQYRNWFLKEFPRLKSELEDNIRRLRALADGVQKVHKGTTIANVVSGSLSISSGILTLVGMGLAPFTEGGSLVLLEPGMELGITAALTGITSSTMDYGKKWWTQAQAHDLVIKSLDKLKEVREFLGENISNFLSLAGNTYQLTRGIGKDIRALRRARANLQSVPHASASRPRVTEPISAESGEQVERVNEPSILEMSRGVKLTDVAPVSFFLVLDVVYLVYESKHLHEGAKSETAEELKKVAQELEEKLNILNNNYKILQADQEL	Clinical trial	"Clinical pipeline report, company report or official report of Ionis"	.	.	.	.	.	.	.	.	.	.	.	hsa:8542	R-HSA-2168880;R-HSA-381426;R-HSA-8957275;	.	O14791;
TTE4KHA	Amyloid beta A4 protein (APP)	P05067	A4_HUMAN	Amyloid beta-protein peptide	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	APP	"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."	.	6IYC; 6GFI; 6CO3; 5W3P; 5VZY	MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. 2015	34	TC=1.C.50	Peptidase	APP family.	.	.	"Beta-amyloid precursor protein C-terminus; Copper-binding of amyloid precursor, CuBD; E2 domain of amyloid precursor protein; Amyloid A4 N-terminal heparin-binding; Beta-amyloid peptide (beta-APP); Kunitz/Bovine pancreatic trypsin inhibitor domain"	PF10515; PF12924; PF12925; PF02177; PF03494; PF00014	PF10515; APP_amyloid; PF12924; APP_Cu_bd; PF12925; APP_E2; PF02177; APP_N; PF03494; Beta-APP; PF00014; Kunitz_BPTI	1.C.50.1.2	The Amyloid -Protein Peptide (APP) Family	hsa04330:Notch signaling pathway; hsa05010:Alzheimer's disease	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	MetaCyc:ENSG00000142192-MON	P05067
TTG51ON	APP messenger RNA (APP mRNA)	P05067	A4_HUMAN	mRNA target	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)	APP	"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."	.	6IYC; 6GFI; 6CO3; 5W3P; 5VZY	MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN	Literature-reported	Expression of BC1 Impairs Spatial Learning and Memory in Alzheimer's Disease Via APP Translation. Mol Neurobiol. 2018 Jul;55(7):6007-6020.	.	mRNA	mRNA target	.	.	.	"Beta-amyloid precursor protein C-terminus; Copper-binding of amyloid precursor, CuBD; E2 domain of amyloid precursor protein; Amyloid A4 N-terminal heparin-binding; Beta-amyloid peptide (beta-APP); Kunitz/Bovine pancreatic trypsin inhibitor domain"	PF10515; PF12924; PF12925; PF02177; PF03494; PF00014	PF10515; APP_amyloid; PF12924; APP_Cu_bd; PF12925; APP_E2; PF02177; APP_N; PF03494; Beta-APP; PF00014; Kunitz_BPTI	.	.	hsa04726: Serotonergic synapse; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases	R-HSA-114608: Platelet degranulation; R-HSA-3000178: ECM proteoglycans; 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-418594: G alpha (i) signalling events; R-HSA-432720: Lysosome Vesicle Biogenesis; R-HSA-444473: Formyl peptide receptors bind formyl peptides and many other ligands; R-HSA-445989: TAK1-dependent IKK and NF-kappa-B activation; R-HSA-844456: The NLRP3 inflammasome; R-HSA-879415: Advanced glycosylation endproduct receptor signaling; R-HSA-8862803: Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models; R-HSA-8957275: Post-translational protein phosphorylation; R-HSA-933542: TRAF6 mediated NF-kB activation; R-HSA-9609523: Insertion of tail-anchored proteins into the endoplasmic reticulum membrane; R-HSA-9660826: Purinergic signaling in leishmaniasis infection; R-HSA-977225: Amyloid fiber formation	MetaCyc:ENSG00000142192-MON	P05067
TTSF1KH	Aquaporin-1 (AQP1)	P29972	AQP1_HUMAN	Major intrinsic protein	Water channel protein for red blood cells and kidney proximal tubule; Urine water channel; CHIP28; Aquaporin-CHIP; AQP-1	AQP1	"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."	.	4CSK; 1IH5; 1H6I; 1FQY	MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNVKVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAILSGITSSLTGNSLGRNDLADGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGHLLAIDYTGCGINPARSFGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDADDINSRVEMKPK	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 688).	0	TC=1.A.8	.	.	.	.	.	.	.	.	.	hsa04924: Renin secretion; hsa04964: Proximal tubule bicarbonate reclamation; hsa04976: Bile secretion	R-HSA-1237044: Erythrocytes take up carbon dioxide and release oxygen; R-HSA-1247673: Erythrocytes take up oxygen and release carbon dioxide; R-HSA-432040: Vasopressin regulates renal water homeostasis via Aquaporins; R-HSA-432047: Passive transport by Aquaporins	.	P29972
TTLDNMQ	Aquaporin 3 (AQP3)	Q92482	AQP3_HUMAN	.	Aquaporin-3; Aquaglyceroporin-3; AQP-3	AQP3	"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)."	.	.	MGRQKELVSRCGEMLHIRYRLLRQALAECLGTLILVMFGCGSVAQVVLSRGTHGGFLTINLAFGFAVTLGILIAGQVSGAHLNPAVTFAMCFLAREPWIKLPIYTLAQTLGAFLGAGIVFGLYYDAIWHFADNQLFVSGPNGTAGIFATYPSGHLDMINGFFDQFIGTASLIVCVLAIVDPYNNPVPRGLEAFTVGLVVLVIGTSMGFNSGYAVNPARDFGPRLFTALAGWGSAVFTTGQHWWWVPIVSPLLGSIAGVFVYQLMIGCHLEQPPPSNEEENVKLAHVKHKEQI	Literature-reported	Critical role of aquaporin 3 on growth of human esophageal and oral squamous cell carcinoma. Cancer Sci. 2011 Jun;102(6):1128-36.	.	.	.	.	.	.	.	.	.	.	.	hsa04962: Vasopressin-regulated water reabsorption	R-HSA-432040: Vasopressin regulates renal water homeostasis via Aquaporins; R-HSA-432047: Passive transport by Aquaporins	.	Q92482
TTNGCRK	Aquaporin-7 (AQP7)	O14520	AQP7_HUMAN	Major intrinsic protein	Aquaporin-7-like; Aquaporin adipose; Aquaglyceroporin-7; AQPap; AQP7L; AQP-7	AQP7	Forms a channel for water and glycerol.	.	.	MVQASGHRRSTRGSKMVSWSVIAKIQEILQRKMVREFLAEFMSTYVMMVFGLGSVAHMVLNKKYGSYLGVNLGFGFGVTMGVHVAGRISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYSLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNPALPGTEALVIGILVVIIGVSLGMNTGYAINPSRDLPPRIFTFIAGWGKQVFSNGENWWWVPVVAPLLGAYLGGIIYLVFIGSTIPREPLKLEDSVAYEDHGITVLPKMGSHEPTISPLTPVSVSPANRSSVHPAPPLHESMALEHF	Literature-reported	Pancreatic Aquaporin-7: A Novel Target for Anti-diabetic Drugs Front Chem. 2018 Apr 5;6:99.	.	TC=1.A.8	.	.	.	.	.	.	.	.	.	hsa03320:PPAR signaling pathway; hsa04923:Regulation of lipolysis in adipocytes	R-HSA-432030: Transport of glycerol from adipocytes to the liver by Aquaporins; R-HSA-432047: Passive transport by Aquaporins	MetaCyc:ENSG00000165269-MON	O14520
TTQEI32	Aquaporin-9 (AQP9)	O43315	AQP9_HUMAN	Major intrinsic protein	Small solute channel 1; SSC1; Aquaglyceroporin-9; AQP-9	AQP9	"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."	.	.	MQPEGAEKGKSFKQRLVLKSSLAKETLSEFLGTFILIVLGCGCVAQAILSRGRFGGVITINVGFSMAVAMAIYVAGGVSGGHINPAVSLAMCLFGRMKWFKLPFYVGAQFLGAFVGAATVFGIYYDGLMSFAGGKLLIVGENATAHIFATYPAPYLSLANAFADQVVATMILLIIVFAIFDSRNLGAPRGLEPIAIGLLIIVIASSLGLNSGCAMNPARDLSPRLFTALAGWGFEVFRAGNNFWWIPVVGPLVGAVIGGLIYVLVIEIHHPEPDSVFKTEQSEDKPEKYELSVIM	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 696).	0	TC=1.A.8	.	.	.	.	.	.	.	.	.	hsa04613: Neutrophil extracellular trap formation; hsa04976: Bile secretion	R-HSA-432030: Transport of glycerol from adipocytes to the liver by Aquaporins; R-HSA-432047: Passive transport by Aquaporins	MetaCyc:ENSG00000103569-MON	O43315
TTKPW01	Androgen receptor messenger RNA (AR mRNA)	P10275	ANDR_HUMAN	mRNA target	Testosterone receptor (mRNA); Nuclear receptor subfamily 3 group C member 4 (mRNA); NR3C4 (mRNA); Dihydrotestosterone receptor (mRNA); DHTR (mRNA); Androgen receptor (mRNA)	AR	"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."	.	5VO4; 5V8Q; 5T8J; 5T8E; 5JJM	MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLLQQQQQQQQQQQQQQQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSALECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDNAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGGGGGGGGGGGEAGAVAPYGYTRPPQGLAGQESDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETTQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 628).	31	mRNA	mRNA target	.	.	.	"Androgen receptor; Ligand-binding domain of nuclear hormone receptor; Zinc finger, C4 type (two domains)"	PF02166; PF00104; PF00105	PF02166; Androgen_recep; PF00104; Hormone_recep; PF00105; zf-C4	.	.	hsa04114:Oocyte meiosis; hsa05200:Pathways in cancer; hsa05215:Prostate cancer	R-HSA-383280:Nuclear Receptor transcription pathway; R-HSA-5625886:Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3	.	P10275
TTS64P2	Androgen receptor (AR)	P10275	ANDR_HUMAN	Nuclear hormone receptor	Testosterone receptor; Nuclear receptor subfamily 3 group C member 4; NR3C4; Dihydrotestosterone receptor; DHTR	AR	"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."	.	5VO4; 5V8Q; 5T8J; 5T8E; 5JJM	MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLLQQQQQQQQQQQQQQQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSALECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDNAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGGGGGGGGGGGEAGAVAPYGYTRPPQGLAGQESDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETTQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ	Successful	Androgen receptor as a target in androgen-independent prostate cancer. Urology. 2002 Sep;60(3 Suppl 1):132-8; discussion 138-9.	34	Nuclear hormone receptor	Zinc finger	nuclear hormone receptor family. NR3 subfamily.	.	.	"Androgen receptor; Ligand-binding domain of nuclear hormone receptor; Zinc finger, C4 type (two domains)"	PF02166; PF00104; PF00105	PF02166; Androgen_recep; PF00104; Hormone_recep; PF00105; zf-C4	.	.	hsa04114:Oocyte meiosis; hsa05200:Pathways in cancer; hsa05215:Prostate cancer	R-HSA-383280:Nuclear Receptor transcription pathway; R-HSA-5625886:Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3	.	P10275
TT5TURO	A-Raf messenger RNA (ARAF mRNA)	P10398	ARAF_HUMAN	mRNA target	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)	ARAF	May also regulate the TOR signaling cascade. Involved in the transduction of mitogenic signals from the cell membrane to the nucleus.	EC 2.7.11.1	2MSE; 1WXM	MEPPRGPPANGAEPSRAVGTVKVYLPNKQRTVVTVRDGMSVYDSLDKALKVRGLNQDCCVVYRLIKGRKTVTAWDTAIAPLDGEELIVEVLEDVPLTMHNFVRKTFFSLAFCDFCLKFLFHGFRCQTCGYKFHQHCSSKVPTVCVDMSTNRQQFYHSVQDLSGGSRQHEAPSNRPLNELLTPQGPSPRTQHCDPEHFPFPAPANAPLQRIRSTSTPNVHMVSTTAPMDSNLIQLTGQSFSTDAAGSRGGSDGTPRGSPSPASVSSGRKSPHSKSPAEQRERKSLADDKKKVKNLGYRDSGYYWEVPPSEVQLLKRIGTGSFGTVFRGRWHGDVAVKVLKVSQPTAEQAQAFKNEMQVLRKTRHVNILLFMGFMTRPGFAIITQWCEGSSLYHHLHVADTRFDMVQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGAQPLEQPSGSVLWMAAEVIRMQDPNPYSFQSDVYAYGVVLYELMTGSLPYSHIGCRDQIIFMVGRGYLSPDLSKISSNCPKAMRRLLSDCLKFQREERPLFPQILATIELLQRSLPKIERSASEPSLHRTQADELPACLLSAARLVP	Clinical trial	"Clinical pipeline report, company report or official report of Roche."	17	mRNA	mRNA target	.	.	.	Phorbol esters/diacylglycerol binding domain (C1 domain); Protein tyrosine kinase; Raf-like Ras-binding domain	PF00130; PF07714; PF02196	PF00130; C1_1; PF07714; Pkinase_Tyr; PF02196; RBD	.	.	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	R-HSA-5673000:RAF activation; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5675221:Negative regulation of MAPK pathway	.	P10398
TTQ9K3Y	Serine/threonine-protein kinase Raf (RAF)	P10398; P15056; P04049	ARAF_HUMAN; BRAF_HUMAN; RAF1_HUMAN	.	Proto-oncogene Raf	ARAF	"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."	.	.	MEPPRGPPANGAEPSRAVGTVKVYLPNKQRTVVTVRDGMSVYDSLDKALKVRGLNQDCCVVYRLIKGRKTVTAWDTAIAPLDGEELIVEVLEDVPLTMHNFVRKTFFSLAFCDFCLKFLFHGFRCQTCGYKFHQHCSSKVPTVCVDMSTNRQQFYHSVQDLSGGSRQHEAPSNRPLNELLTPQGPSPRTQHCDPEHFPFPAPANAPLQRIRSTSTPNVHMVSTTAPMDSNLIQLTGQSFSTDAAGSRGGSDGTPRGSPSPASVSSGRKSPHSKSPAEQRERKSLADDKKKVKNLGYRDSGYYWEVPPSEVQLLKRIGTGSFGTVFRGRWHGDVAVKVLKVSQPTAEQAQAFKNEMQVLRKTRHVNILLFMGFMTRPGFAIITQWCEGSSLYHHLHVADTRFDMVQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGAQPLEQPSGSVLWMAAEVIRMQDPNPYSFQSDVYAYGVVLYELMTGSLPYSHIGCRDQIIFMVGRGYLSPDLSKISSNCPKAMRRLLSDCLKFQREERPLFPQILATIELLQRSLPKIERSASEPSLHRTQADELPACLLSAARLVP	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	"hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa01522: Endocrine resistance; hsa04010: MAPK signaling pathway; 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; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05034: Alcoholism; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05208: Chemical carcinogenesis - reactive oxygen species; 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; hsa05224: Breast cancer; hsa05225: Hepatocellular carcinoma; hsa05226: Gastric cancer"	R-HSA-5673000: RAF activation; R-HSA-5674135: MAP2K and MAPK activation; R-HSA-5675221: Negative regulation of MAPK pathway; R-HSA-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants; R-HSA-9726840: SHOC2 M1731 mutant abolishes MRAS complex function; R-HSA-9726842: Gain-of-function MRAS complexes activate RAF signaling	.	P10398
TT76B3W	Amphiregulin (AREG)	P15514	AREG_HUMAN	.	SDGF; Colorectum cellderived growth factor; Colorectum cell-derived growth factor; CRDGF; AREGB; AR	AREG	"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."	.	2RNL	MRAPLLPPAPVVLSLLILGSGHYAAGLDLNDTYSGKREPFSGDHSADGFEVTSRSEMSSGSEISPVSEMPSSSEPSSGADYDYSEEYDNEPQIPGYIVDDSVRVEQVVKPPQNKTESENTSDKPKRKKKGGKNGKNRRNRKKKNPCNAEFQNFCIHGECKYIEHLEAVTCKCQQEYFGERCGEKSMKTHSMIDSSLSKIALAAIAAFMSAVILTAVAVITVQLRRQYVRKYEGEAEERKKLRQENGNVHAIA	Literature-reported	Amphiregulin as a novel target for breast cancer therapy. J Mammary Gland Biol Neoplasia. 2008 Jun;13(2):171-9.	.	.	.	amphiregulin family.	.	.	.	.	.	.	.	hsa04010: MAPK signaling pathway; hsa04012: ErbB signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04390: Hippo signaling pathway; hsa05210: Colorectal cancer	"R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-177929: Signaling by EGFR; 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-204005: COPII-mediated vesicle transport; R-HSA-212718: EGFR interacts with phospholipase C-gamma; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5638303: Inhibition of Signaling by Overexpressed EGFR; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-5694530: Cargo concentration in the ER; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis; R-HSA-9009391: Extra-nuclear estrogen signaling; R-HSA-9634638: Estrogen-dependent nuclear events downstream of ESR-membrane signaling"	.	P15514
TT70KXY	ADP-ribosylation factor 1 (ARF1)	P84077	ARF1_HUMAN	Small GTPase	PVNH8	ARF1	"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."	.	6FAE; 6DFF; 6D84; 6D83; 6CRI	MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK	Literature-reported	Suppression of breast cancer metastasis through the inactivation of ADP-ribosylation factor 1. Oncotarget. 2016 Sep 6;7(36):58111-58120.	.	Small GTPase	Small GTPase superfamily	small GTPase superfamily. Arf family.	.	.	ADP-ribosylation factor family	PF00025	PF00025; Arf	.	.	hsa04072: Phospholipase D signaling pathway; hsa04144: Endocytosis; hsa05110: Vibrio cholerae infection; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05134: Legionellosis	R-HSA-1660499: Synthesis of PIPs at the plasma membrane; R-HSA-1660514: Synthesis of PIPs at the Golgi membrane; R-HSA-167590: Nef Mediated CD4 Down-regulation; R-HSA-199992: trans-Golgi Network Vesicle Budding; R-HSA-2132295: MHC class II antigen presentation; R-HSA-432720: Lysosome Vesicle Biogenesis; R-HSA-432722: Golgi Associated Vesicle Biogenesis; R-HSA-6807878: COPI-mediated anterograde transport; R-HSA-6811434: COPI-dependent Golgi-to-ER retrograde traffic; R-HSA-6811438: Intra-Golgi traffic; R-HSA-8950505: Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation	.	P84077
TT7ZQEV	Arginase-1 (ARG1)	P05089	ARGI1_HUMAN	.	Liver-type arginase; Type I arginase	ARG1	"Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys. {ECO:0000305}.; Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion (PubMed:15546957, PubMed:16709924, PubMed:19380772). In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival (By similarity). In humans, the immunological role in the monocytic/macrophage/dendritic cell (DC) lineage is unsure. {ECO:0000250|UniProtKB:Q61176, ECO:0000269|PubMed:15546957, ECO:0000269|PubMed:16709924, ECO:0000269|PubMed:19380772}."	EC 3.5.3.1	1WVA;1WVB;2AEB;2PHA;2PHO;2PLL;2ZAV;3DJ8;3E6K;3E6V;3F80;3GMZ;3GN0;3KV2;3LP4;3LP7;3MFV;3MFW;3MJL;3SJT;3SKK;3TF3;3TH7;3THE;3THH;3THJ;4FCI;4FCK;4GSM;4GSV;4GSZ;4GWC;4GWD;4HWW;4HXQ;4IE1;6Q92;6Q9P;6QAF;6V7C;6V7D;6V7E;6V7F;7K4G;7K4H;7K4I;7K4J;7K4K;7KLK;7KLL;7KLM;7LEX;7LEY;7LEZ;7LF0;7LF1;7LF2;8AUP;8E5M;8E5N	MSAKSRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLACFGLAREGNHKPIDYLNPPK	Clinical trial	"Preclinical safety and antitumor activity of the arginine-degrading therapeutic enzyme pegzilarginase, a PEGylated, cobalt-substituted recombinant human arginase 1. Transl Res. 2020 Mar;217:11-22."	.	.	.	.	.	.	.	.	.	.	.	hsa:383	R-HSA-6798695;R-HSA-70635;	MetaCyc:HS04231-MONOMER;	P05089;
TTSANDR	Arginase (ARG)	P05089; P78540	ARGI1_HUMAN; ARGI2_HUMAN	.	L-arginase; Canavanase; Arginine transamidinase; Arginine amidinase	ARG1	"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."	.	.	MSAKSRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLACFGLAREGNHKPIDYLNPPK	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	19	.	.	.	.	.	.	.	.	.	.	hsa00220: Arginine biosynthesis; hsa00330: Arginine and proline metabolism; hsa01100: Metabolic pathways; hsa01230: Biosynthesis of amino acids; hsa05146: Amoebiasis	R-HSA-6798695: Neutrophil degranulation; R-HSA-70635: Urea cycle	MetaCyc:HS04231-MON	P05089
TTV1AG6	Kidney-type arginase (ARG2)	P78540	ARGI2_HUMAN	Carbon-nitrogen hydrolase	Non-hepatic arginase; Human penile arginase; Arginase II; ARG2	ARG2	"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."	EC 3.5.3.1	4IXV; 4IXU; 4IE3; 4IE2; 4I06	MSLRGSLSRLLQTRVHSILKKSVHSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSSLGCHLKDFGDLSFTPVPKDDLYNNLIVNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDHSLAIGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSFLLRELQDKVPQLPGFSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDIDRLGIQKVMERTFDLLIGKRQRPIHLSFDIDAFDPTLAPATGTPVVGGLTYREGMYIAEEIHNTGLLSALDLVEVNPQLATSEEEAKTTANLAVDVIASSFGQTREGGHIVYDQLPTPSSPDESENQARVRI	Clinical trial	Arginase reciprocally regulates nitric oxide synthase activity and contributes to endothelial dysfunction in aging blood vessels. Circulation. 2003 Oct 21;108(16):2000-6.	21	.	.	.	.	.	.	.	.	.	.	hsa00330:Arginine and proline metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01230:Biosynthesis of amino acids; hsa05146:Amoebiasis	R-HSA-70635: Urea cycle	MetaCyc:HS01388-MON	P78540
TT1R5DZ	Rho guanine nucleotide exchange factor 3 (ARHGEF3)	Q9NR81	ARHG3_HUMAN	.	XPLN; Exchange factor found in platelets and leukemic and neuronal tissues	ARHGEF3	Acts as guanine nucleotide exchange factor (GEF) for RhoA and RhoB GTPases.	.	.	MVAKDYPFYLTVKRANCSLELPPASGPAKDAEEPSNKRVKPLSRVTSLANLIPPVKATPLKRFSQTLQRSISFRSESRPDILAPRPWSRNAAPSSTKRRDSKLWSETFDVCVNQMLTSKEIKRQEAIFELSQGEEDLIEDLKLAKKAYHDPMLKLSIMTEQELNQIFGTLDSLIPLHEELLSQLRDVRKPDGSTEHVGPILVGWLPCLSSYDSYCSNQVAAKALLDHKKQDHRVQDFLQRCLESPFSRKLDLWNFLDIPRSRLVKYPLLLREILRHTPNDNPDQQHLEEAINIIQGIVAEINTKTGESECRYYKERLLYLEEGQKDSLIDSSRVLCCHGELKNNRGVKLHVFLFQEVLVITRAVTHNEQLCYQLYRQPIPVKDLLLEDLQDGEVRLGGSLRGAFSNNERIKNFFRVSFKNGSQSQTHSLQANDTFNKQQWLNCIRQAKETVLCAAGQAGVLDSEGSFLNPTTGSRELQGETKLEQMDQSDSESDCSMDTSEVSLDCERMEQTDSSCGNSRHGESNV	Literature-reported	XPLN is modulated by HDAC inhibitors and negatively regulates SPARC expression by targeting mTORC2 in human lung fibroblasts. Pulm Pharmacol Ther. 2017 Jun;44:61-69.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-193648: NRAGE signals death through JNK; R-HSA-416482: G alpha (12/13) signalling events; R-HSA-8980692: RHOA GTPase cycle; R-HSA-9013026: RHOB GTPase cycle	.	Q9NR81
TTIDSFT	ADP-ribosylation factor-like protein 2 (ARL2)	P36404	ARL2_HUMAN	Small GTPase	ARFL2	ARL2	"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)."	.	3DOF; 3DOE	MGLLTILKKMKQKERELRLLMLGLDNAGKTTILKKFNGEDIDTISPTLGFNIKTLEHRGFKLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQSLLVEERLAGATLLIFANKQDLPGALSSNAIREVLELDSIRSHHWCIQGCSAVTGENLLPGIDWLLDDISSRIFTAD	Literature-reported	MicroRNA-497-5p Suppresses Tumor Cell Growth of Osteosarcoma by Targeting ADP Ribosylation Factor-Like Protein 2. Cancer Biother Radiopharm. 2017 Dec;32(10):371-378.	.	Small GTPase	Small GTPase superfamily	small GTPase superfamily. Arf family.	.	.	ADP-ribosylation factor family	PF00025	PF00025; Arf	.	.	.	R-HSA-389977: Post-chaperonin tubulin folding pathway; R-HSA-83936: Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane; R-HSA-9648002: RAS processing	.	P36404
TTMVD4A	Beta-arrestin-1 (ARRB1)	P49407	ARRB1_HUMAN	Arrestin protein	Non-visual arrestin-2; Betaarrestin1; Arrestin beta1; Arrestin beta-1; ARR1	ARRB1	"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."	.	2IV8	MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVDPVDGVVLVDPEYLKERRVYVTLTCAFRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIPPNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGPQPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYADICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNLASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEPPHREVPENETPVDTNLIELDTNDDDIVFEDFARQRLKGMKDDKEEEEDGTGSPQLNNR	Literature-reported	Beta-Arrestin1 Levels in Mononuclear Leukocytes Support Depression Scores for Women with Premenstrual Dysphoric Disorder. Int J Environ Res Public Health. 2015 Dec 22;13(1):ijerph13010043.	.	Arrestin	.	arrestin family.	.	.	"Arrestin (or S-antigen), C-terminal domain; Arrestin (or S-antigen), N-terminal domain"	PF02752; PF00339	PF02752; Arrestin_C; PF00339; Arrestin_N	.	.	"hsa04010: MAPK signaling pathway; hsa04062: Chemokine signaling pathway; hsa04144: Endocytosis; hsa04340: Hedgehog signaling pathway; hsa04728: Dopaminergic synapse; hsa04740: Olfactory transduction; hsa04926: Relaxin signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04929: GnRH secretion; hsa05032: Morphine addiction; hsa05207: Chemical carcinogenesis - receptor activation"	R-HSA-2122948: Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-418555: G alpha (s) signalling events; R-HSA-432720: Lysosome Vesicle Biogenesis; R-HSA-432722: Golgi Associated Vesicle Biogenesis; R-HSA-456926: Thrombin signalling through proteinase activated receptors (PARs); R-HSA-5635838: Activation of SMO; R-HSA-5674135: MAP2K and MAPK activation; R-HSA-5689880: Ub-specific processing proteases; R-HSA-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants	.	P49407
TTPDCTM	Beta-arrestin messenger RNA (ARRB mRNA)	P49407; P32121	ARRB1_HUMAN; ARRB2_HUMAN	mRNA target	Non-visual arrestin; Beta-arrestin; Arrestin beta; ARR	ARRB1	"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)."	.	.	MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVDPVDGVVLVDPEYLKERRVYVTLTCAFRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIPPNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGPQPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYADICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNLASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEPPHREVPENETPVDTNLIELDTNDDDIVFEDFARQRLKGMKDDKEEEEDGTGSPQLNNR	Literature-reported	Penehyclidine Hydrochloride Decreases Pulmonary Microvascular Endothelial Inflammatory Injury Through a Beta-Arrestin-1-Dependent Mechanism. Inflammation. 2018 Oct;41(5):1610-1620.	.	mRNA	mRNA target	.	.	.	.	.	.	.	.	"hsa04010: MAPK signaling pathway; hsa04062: Chemokine signaling pathway; hsa04144: Endocytosis; hsa04340: Hedgehog signaling pathway; hsa04728: Dopaminergic synapse; hsa04740: Olfactory transduction; hsa04926: Relaxin signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04929: GnRH secretion; hsa05032: Morphine addiction; hsa05207: Chemical carcinogenesis - receptor activation"	R-HSA-2122948: Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-418555: G alpha (s) signalling events; R-HSA-432720: Lysosome Vesicle Biogenesis; R-HSA-432722: Golgi Associated Vesicle Biogenesis; R-HSA-456926: Thrombin signalling through proteinase activated receptors (PARs); R-HSA-5635838: Activation of SMO; R-HSA-5674135: MAP2K and MAPK activation; R-HSA-5689880: Ub-specific processing proteases; R-HSA-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants	.	P49407
TT8SO2I	Beta-arrestin-2 (ARRB2)	P32121	ARRB2_HUMAN	Arrestin protein	Non-visual arrestin-3; Betaarrestin2; Arrestin beta2; Arrestin beta-2; ARR2; ARB2	ARRB2	"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."	.	.	MGEKPGTRVFKKSSPNCKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTCAFRYGREDLDVLGLSFRKDLFIATYQAFPPVPNPPRPPTRLQDRLLRKLGQHAHPFFFTIPQNLPCSVTLQPGPEDTGKACGVDFEIRAFCAKSLEEKSHKRNSVRLVIRKVQFAPEKPGPQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYADICLFSTAQYKCPVAQLEQDDQVSPSSTFCKVYTITPLLSDNREKRGLALDGKLKHEDTNLASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIPLPRPQSAAPETDVPVDTNLIEFDTNYATDDDIVFEDFARLRLKGMKDDDYDDQLC	Literature-reported	An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior. Cell. 2005 Jul 29;122(2):261-73.	.	Arrestin	.	arrestin family.	.	.	"Arrestin (or S-antigen), C-terminal domain; Arrestin (or S-antigen), N-terminal domain"	PF02752; PF00339	PF02752; Arrestin_C; PF00339; Arrestin_N	.	.	"hsa04010: MAPK signaling pathway; hsa04062: Chemokine signaling pathway; hsa04144: Endocytosis; hsa04340: Hedgehog signaling pathway; hsa04728: Dopaminergic synapse; hsa04740: Olfactory transduction; hsa04926: Relaxin signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04929: GnRH secretion; hsa05032: Morphine addiction; hsa05207: Chemical carcinogenesis - receptor activation"	R-HSA-2122948: Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-418555: G alpha (s) signalling events; R-HSA-456926: Thrombin signalling through proteinase activated receptors (PARs); R-HSA-5099900: WNT5A-dependent internalization of FZD4; R-HSA-5635838: Activation of SMO; R-HSA-5674135: MAP2K and MAPK activation; R-HSA-5689880: Ub-specific processing proteases; R-HSA-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants	.	P32121
TTYQANR	Cerebroside-sulfatase (ARSA)	P15289	ARSA_HUMAN	Sulfuric ester hydrolase	Cerebrosidesulfatase; Arylsulfatase A component C; ASA; ARSA	ARSA	Hydrolyzes cerebroside sulfate.	EC 3.1.6.8	2HI8; 2AIK; 2AIJ; 1N2L; 1N2K	MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSSLTAHEPPLLYDLSKDPGENYNLLGGVAGATPEVLQALKQLQLLKAQLDAAVTFGPSQVARGEDPALQICCHPGCTPRPACCHCPDPHA	Successful	ClinicalTrials.gov (NCT00681811) Open-Label Extension Study of Recombinant Human Arylsulfatase A (HGT-1111) in Late Infantile MLD. U.S. National Institutes of Health.	21	.	.	.	.	.	.	.	.	.	.	hsa00600:Sphingolipid metabolism; hsa04142:Lysosome	R-HSA-1660662:Glycosphingolipid metabolism	MetaCyc:HS02032-MON	P15289
TTESQTG	N-acetylgalactosamine-4-sulfatase (G4S)	P15848	ARSB_HUMAN	Sulfuric ester hydrolase	Nacetylgalactosamine4sulfatase; G4S; ASB; ARSB	ARSB	"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."	EC 3.1.6.12	1FSU	MGPRGAASLPRGPGPRRLLLPVVLPLLLLLLLAPPGSGAGASRPPHLVFLLADDLGWNDVGFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHERCTLIDALNVTRCALDFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKLARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNIDPNFVDSSPCPRNSMAPAKDDSSLPEYSAFNTSVHAAIRHGNWKLLTGYPGCGYWFPPPSQYNVSEIPSSDPPTKTLWLFDIDRDPEERHDLSREYPHIVTKLLSRLQFYHKHSVPVYFPAQDPRCDPKATGVWGPWM	Successful	Enzyme replacement therapy for mucopolysaccharidosis VI: long-term cardiac effects of galsulfase (Naglazyme ) therapy. J Inherit Metab Dis. 2013 Mar;36(2):385-94.	34	.	.	.	.	.	.	.	.	.	.	hsa00531: Glycosaminoglycan degradation; hsa01100: Metabolic pathways; hsa04142: Lysosome	R-HSA-1660662: Glycosphingolipid metabolism; R-HSA-1663150: The activation of arylsulfatases; R-HSA-2024101: CS/DS degradation; R-HSA-2206285: MPS VI - Maroteaux-Lamy syndrome; R-HSA-6798695: Neutrophil degranulation	MetaCyc:HS03665-MON	P15848
TTB4ZEN	Development and differentiation-enhancing factor-like 1 (DDEFL1)	Q8TDY4	ASAP3_HUMAN	.	"UPLC1; Protein up-regulated in liver cancer 1; DDEFL1; Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3"	ASAP3	Promotes cell proliferation.	.	3LVR; 3LVQ; 2B0O	MPEQFSVAEFLAVTAEDLSSPAGAAAFAAKMPRYRGAALAREEILEGDQAILQRIKKAVRAIHSSGLGHVENEEQYREAVESLGNSHLSQNSHELSTGFLNLAVFTREVAALFKNLIQNLNNIVSFPLDSLMKGQLRDGRQDSKKQLEKAWKDYEAKMAKLEKERDRARVTGGIPGEVAQDMQRERRIFQLHMCEYLLKAGESQMKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLFPFIEKLAASVHALHQAQEDELQKLTQLRDSLRGTLQLESREEHLSRKNSGCGYSIHQHQGNKQFGTEKVGFLYKKSDGIRRVWQKRKCGVKYGCLTISHSTINRPPVKLTLLTCQVRPNPEEKKCFDLVTHNRTYHFQAEDEHECEAWVSVLQNSKDEALSSAFLGEPSAGPGSWGSAGHDGEPHDLTKLLIAEVKSRPGNSQCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGVRFSRMQSLTLDLLGPSELLLALNMGNTSFNEVMEAQLPSHGGPKPSAESDMGTRRDYIMAKYVEHRFARRCTPEPQRLWTAICNRDLLSVLEAFANGQDFGQPLPGPDAQAPEELVLHLAVKVANQASLPLVDFIIQNGGHLDAKAADGNTALHYAALYNQPDCLKLLLKGRALVGTVNEAGETALDIARKKHHKECEELLEQAQAGTFAFPLHVDYSWVISTEPGSDSEEDEEEKRCLLKLPAQAHWASGRLDISNKTYETVASLGAATPQGESEDCPPPLPVKNSSRTLVQGCARHASGDRSEVSSLSSEAPETPESLGSPASSSSLMSPLEPGDPSQAPPNSEEGLREPPGTSRPSLTSGTTPSEMYLPVRFSSESTRSYRRGARSPEDGPSARQPLPRRNVPVGITEGDGSRTGSLPASSVQLLQD	Literature-reported	Isolation of development and differentiation enhancing factor-like 1 (DDEFL1) as a drug target for hepatocellular carcinomas. Int J Oncol. 2004 Jan;24(1):43-8.	.	.	.	.	.	.	.	.	.	.	.	hsa04144: Endocytosis; hsa04666: Fc gamma R-mediated phagocytosis	.	.	Q8TDY4
TTYM94H	Asialoglycoprotein receptor 1 (ASGR1)	P07306	ASGR1_HUMAN	.	Hepatic lectin H1; HL-1; C-type lectin domain family 4 member H1	ASGR1	"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."	.	5JQ1; 5JPV; 1DV8	MTKEYQDLQHLDNEESDHHQLRKGPPPPQPLLQRLCSGPRLLLLSLGLSLLLLVVVCVIGSQNSQLQEELRGLRETFSNFTASTEAQVKGLSTQGGNVGRKMKSLESQLEKQQKDLSEDHSSLLLHVKQFVSDLRSLSCQMAALQGNGSERTCCPVNWVEHERSCYWFSRSGKAWADADNYCRLEDAHLVVVTSWEEQKFVQHHIGPVNTWMGLHDQNGPWKWVDGTDYETGFKNWRPEQPDDWYGHGLGGGEDCAHFTDDGRWNDDVCQRPYRWVCETELDKASQEPPLL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	hsa04918:Thyroid hormone synthesis	R-HSA-446203: Asparagine N-linked glycosylation	.	P07306
TTRJYB6	Acid-sensing ion channel 1 (ASIC1)	P78348	ASIC1_HUMAN	Amiloride-sensitive sodium channel	"Brain sodium channel 2; BNaC2; Amiloride-sensitive cation channel 2, neuronal; ASIC1; ACCN2"	ASIC1	Isoform 1 does not display proton-gated cation channel activity.	.	.	MELKAEEEEVGGVQPVSIQAFASSSTLHGLAHIFSYERLSLKRALWALCFLGSLAVLLCVCTERVQYYFHYHHVTKLDEVAASQLTFPAVTLCNLNEFRFSQVSKNDLYHAGELLALLNNRYEIPDTQMADEKQLEILQDKANFRSFKPKPFNMREFYDRAGHDIRDMLLSCHFRGEVCSAEDFKVVFTRYGKCYTFNSGRDGRPRLKTMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQDEPPFIDQLGFGVAPGFQTFVACQEQRLIYLPPPWGTCKAVTMDSDLDFFDSYSITACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDQEYCVCEMPCNLTRYGKELSMVKIPSKASAKYLAKKFNKSEQYIGENILVLDIFFEVLNYETIEQKKAYEIAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHKLCRRGKCQKEAKRSSADKGVALSLDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFTC	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	hsa04750:Inflammatory mediator regulation of TRP channels	R-HSA-2672351:Stimuli-sensing channels	.	P78348
TTVMWLP	Acid-sensing ion channel 2 (ASIC2)	Q16515	ASIC2_HUMAN	Amiloride-sensitive sodium channel	"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"	ASIC2	"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."	.	.	MDLKESPSEGSLQPSSIQIFANTSTLHGIRHIFVYGPLTIRRVLWAVAFVGSLGLLLVESSERVSYYFSYQHVTKVDEVVAQSLVFPAVTLCNLNGFRFSRLTTNDLYHAGELLALLDVNLQIPDPHLADPSVLEALRQKANFKHYKPKQFSMLEFLHRVGHDLKDMMLYCKFKGQECGHQDFTTVFTKYGKCYMFNSGEDGKPLLTTVKGGTGNGLEIMLDIQQDEYLPIWGETEETTFEAGVKVQIHSQSEPPFIQELGFGVAPGFQTFVATQEQRLTYLPPPWGECRSSEMGLDFFPVYSITACRIDCETRYIVENCNCRMVHMPGDAPFCTPEQHKECAEPALGLLAEKDSNYCLCRTPCNLTRYNKELSMVKIPSKTSAKYLEKKFNKSEKYISENILVLDIFFEALNYETIEQKKAYEVAALLGDIGGQMGLFIGASILTILELFDYIYELIKEKLLDLLGKEEDEGSHDENVSTCDTMPNHSETISHTVNVPLQTTLGTLEEIAC	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 685).	0	.	.	.	.	.	.	.	.	.	.	hsa04742:Taste transduction; hsa04750:Inflammatory mediator regulation of TRP channels	R-HSA-2672351:Stimuli-sensing channels	.	Q16515
TTLGDIS	Acid-sensing ion channel 3 (ASIC3)	Q9UHC3	ASIC3_HUMAN	Amiloride-sensitive sodium channel	hTNaC1; hASIC3; Testis sodium channel 1; TNAC1; SLNAC1; Neuronal amiloride-sensitive cation channel 3; Amiloride-sensitive cation channel 3; ASIC3; ACCN3	ASIC3	"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."	.	.	MKPTSGPEEARRPASDIRVFASNCSMHGLGHVFGPGSLSLRRGMWAAAVVLSVATFLYQVAERVRYYREFHHQTALDERESHRLIFPAVTLCNINPLRRSRLTPNDLHWAGSALLGLDPAEHAAFLRALGRPPAPPGFMPSPTFDMAQLYARAGHSLDDMLLDCRFRGQPCGPENFTTIFTRMGKCYTFNSGADGAELLTTTRGGMGNGLDIMLDVQQEEYLPVWRDNEETPFEVGIRVQIHSQEEPPIIDQLGLGVSPGYQTFVSCQQQQLSFLPPPWGDCSSASLNPNYEPEPSDPLGSPSPSPSPPYTLMGCRLACETRYVARKCGCRMVYMPGDVPVCSPQQYKNCAHPAIDAMLRKDSCACPNPCASTRYAKELSMVRIPSRAAARFLARKLNRSEAYIAENVLALDIFFEALNYETVEQKKAYEMSELLGDIGGQMGLFIGASLLTILEILDYLCEVFRDKVLGYFWNRQHSQRHSSTNLLQEGLGSHRTQVPHLSLGPRPPTPPCAVTKTLSASHRTCYLVTQL	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 686).	0	.	.	.	.	.	.	.	.	.	.	hsa04750:Inflammatory mediator regulation of TRP channels	R-HSA-2672351:Stimuli-sensing channels	.	Q9UHC3
TT6TLZP	Aspartoacylase (ASPA)	P45381	ACY2_HUMAN	.	Aminoacylase-2; ACY-2	ASPA	Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it acts as a scavenger of NAA from body fluids.	EC 3.5.1.15	2I3C;2O4H;2O53;2Q51;4MRI;4MXU;4NFR;4TNU	MTSCHIAEEHIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVKPFITNPRAVKKCTRYIDCDLNRIFDLENLGKKMSEDLPYEVRRAQEINHLFGPKDSEDSYDIIFDLHNTTSNMGCTLILEDSRNNFLIQMFHYIKTSLAPLPCYVYLIEHPSLKYATTRSIAKYPVGIEVGPQPQGVLRADILDQMRKMIKHALDFIHHFNEGKEFPPCAIEVYKIIEKVDYPRDENGEIAAIIHPNLQDQDWKPLHPGDPMFLTLDGKTIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTKLTLNAKSIRCCLH	Clinical trial	"Clinical pipeline report, company report or official report of Adrenas Therapeutics"	.	.	.	.	.	.	.	.	.	.	.	hsa:443	R-HSA-8963693;	MetaCyc:HS03094-MONOMER;	P45381;
TTTX5M8	Aspergillus Mannitol 2-dehydrogenase (Asperg M2DH)	Q4WQY4	M2DH_ASPFU	Short-chain dehydrogenases reductase	MDH; M2DH	Asperg M2DH	Catalyzes the NAD(H)-dependent interconversion of D- fructose and D-mannitol in the mannitol metabolic pathway. Has a preference for NADH over NADPH.	.	.	MAPLKLNSRNLSQIAAAGGALVKIPTYQRGRAVKEGIVHIGVGGFHRAHLAVYIDQLMQKHGVNDYAICGVGLQPFDSAMRDALASQDHLYTLIERSAKGSFAHVIGSINSYLFAPDNREAVIAKMAHPDTKIVSLTITESGYYYNENTHELQSEHPDIQFDLDPANEKAPRTTFGFLYAGLTRRYQQGLKPFTVMSCDNMQKNGSITRHMLESFARLRNPEVAEWIAEEGAFPNAMVDRITPQTSETDKTALAEKFGIVDSWPVVTEPFTQWVIEDQFSDGRPPFEKVGVQVVKDVHAVEQFEKHKLRLLNGSHSALGYPGQLAGFQYVHEVMANPLFRKFVWQMMQEEVKPLLPEIPGVDIDEYCNTLIERFTNPTIMDQLPRICLNASGKIPQFIMPSIAEAIWETGPFRRLCFVAAAWFHYIKGVDDRGKPFEVVDPMREELQAKARAGGNDPSELLSIKSLFGDDLRNDERFLREITTAMNDIARDGIMKTLPKYIN	Successful	Polyol-specific long-chain dehydrogenases/reductases of mannitol metabolism in Aspergillus fumigatus: biochemical characterization and pH studies o... Chem Biol Interact. 2009 Mar 16;178(1-3):274-82.	34	.	.	.	.	.	.	.	.	.	.	afm00051: Fructose and mannose metabolism; afm01100: Metabolic pathways	.	.	Q4WQY4
TTV0PE2	Aspergillus Mannitol-1-phosphate 5-dehydrogenase (Asperg mpdA)	Q4X1A4	MTLD_ASPFU	Short-chain dehydrogenases reductase	mpdA; MPDH; MPD; M1PDH	Asperg mpdA	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.	EC 1.1.1.17	.	MGKKAIQFGGGNIGRGFVAEFLHEAGYEVVFIDVVDKIIDALKSTPSYEVTEVSEEGEKTKTITNYRAINSKTNEEDVVKEIGTADVVTCAVGPNVLKFIAPVIAKGIDARTASKPVAVIACENAIGATDTLRGFIEQNTDKDRLSSMSERARFANSAIDRIVPNQPPNAGLNVRIEKFYEWTVEQTPFGEFGHPDIPAIHWVDDLKPYIERKLFTVNTGHATTAYYGHMRGKKMIADALADAEIRQIVHKVLEQTAKLITTKHEITEQEQNEYVDTIVKRMSNPFLEDNVERVGRAPLRKLSRNERFIGPASQLAEKGLPFDALLGSIEMALRFQNVPGDEESAELAKILKEMSAEEATGKLTGLEKHHPLYEPVQNVIAKVQKDSK	Successful	Polyol-specific long-chain dehydrogenases/reductases of mannitol metabolism in Aspergillus fumigatus: biochemical characterization and pH studies o... Chem Biol Interact. 2009 Mar 16;178(1-3):274-82.	34	.	.	.	.	.	.	.	.	.	.	afm00051: Fructose and mannose metabolism; afm01100: Metabolic pathways	.	.	Q4X1A4
TT2KHP7	Aspartate beta-hydroxylase (ASPH)	Q12797	ASPH_HUMAN	Paired donor oxygen oxidoreductase	Peptideaspartate betadioxygenase; Aspartyl/asparaginyl betahydroxylase; ASPH; ASP betahydroxylase	ASPH	"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}."	EC 1.14.11.16	6RK9; 5JZU; 5JZA; 5JZ8; 5JZ6	MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARRETKHGGHKNGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHVEGEDLQQEDGPTGEPQQEDDEFLMATDVDDRFETLEPEVSHEETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQEVPPETNRKTDDPEQKAKVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPKETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHPELTPQQRRSLPAI	Literature-reported	Aspartate beta-hydroxylase promotes cholangiocarcinoma progression by modulating RB1 phosphorylation. Cancer Lett. 2018 Aug 10;429:1-10.	.	.	.	.	.	.	.	.	.	.	.	hsa04020: Calcium signaling pathway; hsa04260: Cardiac muscle contraction	R-HSA-2672351: Stimuli-sensing channels; R-HSA-5578775: Ion homeostasis	.	Q12797
TT4WT91	Asparaginase (ASRGL1)	Q7L266	ASGL1_HUMAN	Peptidase	Lasparagine amidohydrolase; Isoaspartyl peptidase/Lasparaginase beta chain; Isoaspartyl peptidase/Lasparaginase; Isoaspartyl dipeptidase; Betaaspartylpeptidase; Asparaginaselike protein 1; ASRGL1	ASRGL1	"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."	EC 3.4.19.5	4ZM9; 4PVS; 4PVR; 4PVQ; 4PVP	MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTTITDLP	Successful	Pharmacokinetic and pharmacodynamic properties of calaspargase pegol Escherichia coli L-asparaginase in the treatment of patients with acute lymphoblastic leukemia: results from Children's Oncology Group Study AALL07P4. J Clin Oncol. 2014 Dec 1;32(34):3874-82.	34	.	.	.	.	.	.	.	.	.	.	"hsa00250: Alanine, aspartate and glutamate metabolism; hsa01100: Metabolic pathways"	R-HSA-8964208: Phenylalanine metabolism	MetaCyc:HS08648-MON	Q7L266
TT9A0HI	ATPase family AAA domain containing 2 (ATAD2)	Q6PL18	ATAD2_HUMAN	Acid anhydride hydrolase	PRO2000; L16; ATPase family AAA domain-containing protein 2; ANCCA; AAA nuclear coregulator cancer-associated protein	ATAD2	"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."	EC 3.6.1.3	6HIE; 6HID; 6HIC; 6HIB; 6HIA	MVVLRSSLELHNHSAASATGSLDLSSDFLSLEHIGRRRLRSAGAAQKKPAATTAKAGDGSSVKEVETYHRTRALRSLRKDAQNSSDSSFEKNVEITEQLANGRHFTRQLARQQADKKKEEHREDKVIPVTRSLRARNIVQSTEHLHEDNGDVEVRRSCRIRSRYSGVNQSMLFDKLITNTAEAVLQKMDDMKKMRRQRMRELEDLGVFNETEESNLNMYTRGKQKDIQRTDEETTDNQEGSVESSEEGEDQEHEDDGEDEDDEDDDDDDDDDDDDDDEDDEDEEDGEEENQKRYYLRQRKATVYYQAPLEKPRHQRKPNIFYSGPASPARPRYRLSSAGPRSPYCKRMNRRRHAIHSSDSTSSSSSEDEQHFERRRKRSRNRAINRCLPLNFRKDELKGIYKDRMKIGASLADVDPMQLDSSVRFDSVGGLSNHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSQGDKRVAFFMRKGADCLSKWVGESERQLRLLFDQAYQMRPSIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKEARKEILKIHTRDWNPKPLDTFLEELAENCVGYCGADIKSICAEAALCALRRRYPQIYTTSEKLQLDLSSINISAKDFEVAMQKMIPASQRAVTSPGQALSTVVKPLLQNTVDKILEALQRVFPHAEFRTNKTLDSDISCPLLESDLAYSDDDVPSVYENGLSQKSSHKAKDNFNFLHLNRNACYQPMSFRPRILIVGEPGFGQGSHLAPAVIHALEKFTVYTLDIPVLFGVSTTSPEETCAQVIREAKRTAPSIVYVPHIHVWWEIVGPTLKATFTTLLQNIPSFAPVLLLATSDKPHSALPEEVQELFIRDYGEIFNVQLPDKEERTKFFEDLILKQAAKPPISKKKAVLQALEVLPVAPPPEPRSLTAEEVKRLEEQEEDTFRELRIFLRNVTHRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLRDIDLICSNALEYNPDRDPGDRLIRHRACALRDTAYAIIKEELDEDFEQLCEEIQESRKKRGCSSSKYAPSYYHVMPKQNSTLVGDKRSDPEQNEKLKTPSTPVACSTPAQLKRKIRKKSNWYLGTIKKRRKISQAKDDSQNAIDHKIESDTEETQDTSVDHNETGNTGESSVEENEKQQNASESKLELRNNSNTCNIENELEDSRKTTACTELRDKIACNGDASSSQIIHISDENEGKEMCVLRMTRARRSQVEQQQLITVEKALAILSQPTPSLVVDHERLKNLLKTVVKKSQNYNIFQLENLYAVISQCIYRHRKDHDKTSLIQKMEQEVENFSCSR	Literature-reported	Fragment-Based Discovery of Low-Micromolar ATAD2 Bromodomain Inhibitors. J Med Chem. 2015 Jul 23;58(14):5649-73.	0	EC:3.6	.	AAA ATPase family.	3.6.1.3	Acting on acid anhydrides	ATPase family associated with various cellular activities (AAA); AAA+ lid domain; Bromodomain	PF00004; PF17862; PF00439	PF00004; AAA; PF17862; AAA_lid_3; PF00439; Bromodomain	.	.	.	R-HSA-8866910: TFAP2 (AP-2) family regulates transcription of growth factors and their receptors	.	Q6PL18
TTWUHQ1	Alpha-tubulin N-acetyltransferase 1 (ATAT1)	Q5SQI0	ATAT_HUMAN	Acetyltransferase ATAT1 family	MEC17; C6orf134; Alpha-TAT; Acetyltransferase mec-17 homolog	ATAT1	"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."	EC 2.3.1.108	4U9Z; 4U9Y; 4PK3; 4PK2; 4IF5	MEFPFDVDALFPERITVLDQHLRPPARRPGTTTPARVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARPAGKGAIIGFIKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVNNFVIFEGFFAHQHRPPAPSLRATRHSRAAAVDPTPAAPARKLPPKRAEGDIKPYSSSDREFLKVAVEPPWPLNRAPRRATPPAHPPPRSSSLGNSPERGPLRPFVPEQELLRSLRLCPPHPTARLLLAADPGGSPAQRRRTRGTPPGLVAQSCCYSRHGGVNSSSPNTGNQDSKQGEQETKNRSASEEQALSQDGSGEKPMHTAPPQAPAPPAQSWTVGGDILNARFIRNLQERRSTRPW	Literature-reported	Alpha-tubulin acetyltransferase/MEC-17 regulates cancer cell migration and invasion through epithelial-mesenchymal transition suppression and cell ... Sci Rep. 2018 Nov 30;8(1):17477.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-5617833: Cilium Assembly	MetaCyc:ENSG00000137343-MON	Q5SQI0
TTCE793	Cyclic-AMP-dependent transcription factor ATF-3 (ATF3)	P18847	ATF3_HUMAN	Basic leucine zipper bZIP	cAMP-dependent transcription factor ATF-3; Cyclic AMP-dependent transcription factor ATF-3; Activating transcription factor 3	ATF3	"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."	.	.	MMLQHPGQVSASEVSASAIVPCLSPPGSLVFEDFANLTPFVKEELRFAIQNKHLCHRMSSALESVTVSDRPLGVSITKAEVAPEEDERKKRRRERNKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLIYMLNLHRPTCIVRAQNGRTPEDERNLFIQQIKEGTLQS	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	bZIP	.	bZIP family. ATF subfamily.	.	.	bZIP transcription factor	PF00170	PF00170; bZIP_1	.	.	.	R-HSA-380994: ATF4 activates genes in response to endoplasmic reticulum stress; R-HSA-9633012: Response of EIF2AK4 (GCN2) to amino acid deficiency; R-HSA-9648895: Response of EIF2AK1 (HRI) to heme deficiency	.	P18847
TTQCKWT	Activating transcription factor 4 (ATF-4)	P18848	ATF4_HUMAN	Basic leucine zipper bZIP	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	ATF4	"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."	.	1CI6	MTEMSFLSSEVLVGDLMSPFDQSGLGAEESLGLLDDYLEVAKHFKPHGFSSDKAKAGSSEWLAVDGLVSPSNNSKEDAFSGTDWMLEKMDLKEFDLDALLGIDDLETMPDDLLTTLDDTCDLFAPLVQETNKQPPQTVNPIGHLPESLTKPDQVAPFTFLQPLPLSPGVLSSTPDHSFSLELGSEVDITEGDRKPDYTAYVAMIPQCIKEEDTPSDNDSGICMSPESYLGSPQHSPSTRGSPNRSLPSPGVLCGSARPKPYDPPGEKMVAAKVKGEKLDKKLKKMEQNKTAATRYRQKKRAEQEALTGECKELEKKNEALKERADSLAKEIQYLKDLIEEVRKARGKKRVP	Literature-reported	Role of ATF4 in skeletal muscle atrophy. Curr Opin Clin Nutr Metab Care. 2017 May;20(3):164-168.	.	bZIP	.	bZIP family.	.	.	bZIP transcription factor	PF00170	PF00170; bZIP_1	.	.	"hsa04010: MAPK signaling pathway; hsa04022: cGMP-PKG signaling pathway; hsa04137: Mitophagy - animal; hsa04141: Protein processing in endoplasmic reticulum; hsa04151: PI3K-Akt signaling pathway; hsa04210: Apoptosis; hsa04211: Longevity regulating pathway; hsa04261: Adrenergic signaling in cardiomyocytes; hsa04668: TNF signaling pathway; hsa04720: Long-term potentiation; hsa04722: Neurotrophin signaling pathway; hsa04725: Cholinergic synapse; hsa04728: Dopaminergic synapse; hsa04911: Insulin secretion; hsa04912: GnRH signaling pathway; hsa04915: Estrogen signaling pathway; hsa04918: Thyroid hormone synthesis; hsa04922: Glucagon signaling pathway; hsa04925: Aldosterone synthesis and secretion; hsa04926: Relaxin signaling pathway; hsa04927: Cortisol synthesis and secretion; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04932: Non-alcoholic fatty liver disease; hsa04934: Cushing syndrome; hsa04935: Growth hormone synthesis, secretion and action; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05014: Amyotrophic lateral sclerosis; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05030: Cocaine addiction; hsa05031: Amphetamine addiction; hsa05034: Alcoholism; hsa05161: Hepatitis B; hsa05163: Human cytomegalovirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05203: Viral carcinogenesis; hsa05207: Chemical carcinogenesis - receptor activation; hsa05215: Prostate cancer; hsa05417: Lipid and atherosclerosis"	R-HSA-380994: ATF4 activates genes in response to endoplasmic reticulum stress; R-HSA-381042: PERK regulates gene expression; R-HSA-381183: ATF6 (ATF6-alpha) activates chaperone genes; R-HSA-9633012: Response of EIF2AK4 (GCN2) to amino acid deficiency; R-HSA-9648895: Response of EIF2AK1 (HRI) to heme deficiency; R-HSA-9759194: Nuclear events mediated by NFE2L2	.	P18848
TTG6KCU	Autophagy-related 2B (ATG2B)	Q96BY7	ATG2B_HUMAN	Autophagy phagophore-formation transporter	C14orf103; Autophagyrelated protein 2 homolog B; Autophagy-related protein 2 homolog B	ATG2B	Required for both autophagosome formation and regulation of lipid droplet morphology and dispersion.	.	.	MPWPFSESIKKRACRYLLQRYLGHFLQEKLSLEQLSLDLYQGTGSLAQVPLDKWCLNEILESADAPLEVTEGFIQSISLSVPWGSLLQDNCALEVRGLEMVFRPRPRPATGSEPMYWSSFMTSSMQLAKECLSQKLTDEQGEGSQPFEGLEKFAETIETVLRRVKVTFIDTVLRIEHVPENSKTGTALEIRIERTVYCDETADESSGINVHQPTAFAHKLLQLSGVSLFWDEFSASAKSSPVCSTAPVETEPKLSPSWNPKIIYEPHPQLTRNLPEIAPSDPVQIGRLIGRLELSLTLKQNEVLPGAKLDVDGQIDSIHLLLSPRQVHLLLDMLAAIAGPENSSKIGLANKDRKNRPMQQEDEYRIQMELNRYYLRKDSLSVGVSSEQSFYETETARTPSSREEEVFFSMADMDMSHSLSSLPPLGDPPNMDLELSLTSTYTNTPAGSPLSATVLQPTWGEFLDHHKEQPVRGSTFPSNLVHPTPLQKTSLPSRSVSVDESRPELIFRLAVGTFSISVLHIDPLSPPETSQNLNPLTPMAVAFFTCIEKIDPARFSTEDFKSFRAVFAEACSHDHLRFIGTGIKVSYEQRQRSASRYFSTDMSIGQMEFLECLFPTDFHSVPPHYTELLTFHSKEETGSHSPVCLQLHYKHSENRGPQGNQARLSSVPHKAELQIKLNPVCCELDISIVDRLNSLLQPQKLATVEMMASHMYTSYNKHISLHKAFTEVFLDDSHSPANCRISVQVATPALNLSVRFPIPDLRSDQERGPWFKKSLQKEILYLAFTDLEFKTEFIGGSTPEQIKLELTFRELIGSFQEEKGDPSIKFFHVSSGVDGDTTSSDDFDWPRIVLKINPPAMHSILERIAAEEEEENDGHYQEEEEGGAHSLKDVCDLRRPAPSPFSSRRVMFENEQMVMPGDPVEMTEFQDKAISNSHYVLELTLPNIYVTLPNKSFYEKLYNRIFNDLLLWEPTAPSPVETFENISYGIGLSVASQLINTFNKDSFSAFKSAVHYDEESGSEEETLQYFSTVDPNYRSRRKKKLDSQNKNSQSFLSVLLNINHGLIAVFTDVKQDNGDLLENKHGEFWLEFNSGSLFCVTKYEGFDDKHYICLHSSSFSLYHKGIVNGVILPTETRLPSSTRPHWLEPTIYSSEEDGLSKTSSDGVGGDSLNMLSVAVKILSDKSESNTKEFLIAVGLKGATLQHRMLPSGLSWHEQILYFLNIADEPVLGYNPPTSFTTFHVHLWSCALDYRPLYLPIRSLLTVETFSVSSSVALDKSSSTLRIILDEAALHLSDKCNTVTINLSRDYVRVMDMGLLELTITAVKSDSDGEQTEPRFELHCSSDVVHIRTCSDSCAALMNLIQYIASYGDLQTPNKADMKPGAFQRRSKVDSSGRSSSRGPVLPEADQQMLRDLMSDAMEEIDMQQGTSSVKPQANGVLDEKSQIQEPCCSDLFLFPDESGNVSQESGPTYASFSHHFISDAMTGVPTENDDFCILFAPKAAMQEKEEEPVIKIMVDDAIVIRDNYFSLPVNKTDTSKAPLHFPIPVIRYVVKEVSLVWHLYGGKDFGIVPPTSPAKSYISPHSSPSHTPTRHGRNTVCGGKGRNHDFLMEIQLSKVKFQHEVYPPCKPDCDSSLSEHPVSRQVFIVQDLEIRDRLATSQMNKFLYLYCSKEMPRKAHSNMLTVKALHVCPESGRSPQECCLRVSLMPLRLNIDQDALFFLKDFFTSLSAEVELQMTPDPEVKKSPGADVTCSLPRHLSTSKEPNLVISFSGPKQPSQNDSANSVEVVNGMEEKNFSAEEASFRDQPVFFREFRFTSEVPIRLDYHGKHVSMDQGTLAGILIGLAQLNCSELKLKRLSYRHGLLGVDKLFSYAITEWLNDIKKNQLPGILGGVGPMHSLVQLVQGLKDLVWLPIEQYRKDGRIVRGFQRGAASFGTSTAMAALELTNRMVQTIQAAAETAYDMVSPGTLSIEPKKTKRFPHHRLAHQPVDLREGVAKAYSVVKEGITDTAQTIYETAAREHESRGVTGAVGEVLRQIPPAVVKPLIVATEATSNVLGGMRNQIRPDVRQDESQKWRHGDD	Literature-reported	miR-143 inhibits cell proliferation by targeting autophagy-related 2B in non-small cell lung cancer H1299 cells. Mol Med Rep. 2015 Jan;11(1):571-6.	.	TC=9.A.15	.	ATG2 family.	.	.	Autophagy-related protein C terminal domain; N-terminal region of Chorein or VPS13	PF09333; PF12624	PF09333; ATG_C; PF12624; Chorein_N	9.A.15.2.1	The Autophagy-related Phagophore-formation Transporter (APT) Family	hsa04136: Autophagy - other; hsa04140: Autophagy - animal; hsa05010: Alzheimer disease; hsa05014: Amyotrophic lateral sclerosis; hsa05016: Huntington disease; hsa05017: Spinocerebellar ataxia; hsa05022: Pathways of neurodegeneration - multiple diseases	.	.	Q96BY7
TTLVB9Z	Autophagy-related protein 7 (ATG7)	O95352	ATG7_HUMAN	Autophagy phagophore-formation transporter	hAGP7; Ubiquitin-like modifier-activating enzyme ATG7; Ubiquitin-activating enzyme E1-like protein; ATG12-activating enzyme E1 ATG7; APG7L; APG7-like	ATG7	"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."	.	.	MAAATGDPGLSKLQFAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTLEFSAFDMSAPTPARCCPAIGTLYNTNTLESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFADLKKYHFYYWFCYPALCLPESLPLIQGPVGLDQRFSLKQIEALECAYDNLCQTEGVTALPYFLIKYDENMVLVSLLKHYSDFFQGQRTKITIGVYDPCNLAQYPGWPLRNFLVLAAHRWSSSFQSVEVVCFRDRTMQGARDVAHSIIFEVKLPEMAFSPDCPKAVGWEKNQKGGMGPRMVNLSECMDPKRLAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDCLGGGKPKALAAADRLQKIFPGVNARGFNMSIPMPGHPVNFSSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRKLVINAALGFDTFVVMRHGLKKPKQQGAGDLCPNHPVASADLLGSSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSSKVLDQYEREGFNFLAKVFNSSHSFLEDLTGLTLLHQETQAAEIWDMSDDETI	Literature-reported	Autophagy gene ATG7 regulates ultraviolet radiation-induced inflammation and skin tumorigenesis. Autophagy. 2017;13(12):2086-2103.	.	TC=9.A.15	.	ATG7 family.	.	.	Ubiquitin-like modifier-activating enzyme ATG7 N-terminus; ThiF family	PF16420; PF00899	PF16420; ATG7_N; PF00899; ThiF	9.A.15.2.1	The Autophagy-related Phagophore-formation Transporter (APT) Family	hsa04136: Autophagy - other; hsa04140: Autophagy - animal; hsa04216: Ferroptosis; hsa04613: Neutrophil extracellular trap formation	R-HSA-1632852: Macroautophagy; R-HSA-6798695: Neutrophil degranulation; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	O95352
TT9NVXQ	Phosphoribosylaminoimidazolecarboxamide formyltransferase (ATIC)	P31939	PUR9_HUMAN	Methyltransferase	PURH; OK/SW-cl.86; Bifunctional purine biosynthesis protein PURH	ATIC	Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis.	.	5UZ0; 5UY8; 1PL0; 1PKX; 1P4R	MAPGQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNLYPFVKTVASPGVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVVSTEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVSQMPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKELKEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAAYARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTILSKKKNGNYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNVVTKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHCTRLAGDKANYWWLRHHPQVLSMKFKTGVKRAEISNAIDQYVTGTIGEDEDLIKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDAFFPFRDNVDRAKRSGVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH	Literature-reported	Virtual screening of human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase against the NCI diversity set by use of AutoDock to identif... J Med Chem. 2004 Dec 30;47(27):6681-90.	0	.	.	.	.	.	.	.	.	.	.	hsa00230: Purine metabolism; hsa00670: One carbon pool by folate; hsa01100: Metabolic pathways; hsa01523: Antifolate resistance	R-HSA-73817: Purine ribonucleoside monophosphate biosynthesis; R-HSA-9725370: Signaling by ALK fusions and activated point mutants	MetaCyc:HS06490-MON	P31939
TTKBM7V	ATM serine/threonine kinase (ATM)	Q13315	ATM_HUMAN	Kinase	Serine-protein kinase ATM; Ataxia telangiectasia mutated; A-T mutated	ATM	"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."	EC 2.7.11.1	6HKA; 5NP1; 5NP0	MSLVLNDLLICCRQLEHDRATERKKEVEKFKRLIRDPETIKHLDRHSDSKQGKYLNWDAVFRFLQKYIQKETECLRIAKPNVSASTQASRQKKMQEISSLVKYFIKCANRRAPRLKCQELLNYIMDTVKDSSNGAIYGADCSNILLKDILSVRKYWCEISQQQWLELFSVYFRLYLKPSQDVHRVLVARIIHAVTKGCCSQTDGLNSKFLDFFSKAIQCARQEKSSSGLNHILAALTIFLKTLAVNFRIRVCELGDEILPTLLYIWTQHRLNDSLKEVIIELFQLQIYIHHPKGAKTQEKGAYESTKWRSILYNLYDLLVNEISHIGSRGKYSSGFRNIAVKENLIELMADICHQVFNEDTRSLEISQSYTTTQRESSDYSVPCKRKKIELGWEVIKDHLQKSQNDFDLVPWLQIATQLISKYPASLPNCELSPLLMILSQLLPQQRHGERTPYVLRCLTEVALCQDKRSNLESSQKSDLLKLWNKIWCITFRGISSEQIQAENFGLLGAIIQGSLVEVDREFWKLFTGSACRPSCPAVCCLTLALTTSIVPGTVKMGIEQNMCEVNRSFSLKESIMKWLLFYQLEGDLENSTEVPPILHSNFPHLVLEKILVSLTMKNCKAAMNFFQSVPECEHHQKDKEELSFSEVEELFLQTTFDKMDFLTIVRECGIEKHQSSIGFSVHQNLKESLDRCLLGLSEQLLNNYSSEITNSETLVRCSRLLVGVLGCYCYMGVIAEEEAYKSELFQKAKSLMQCAGESITLFKNKTNEEFRIGSLRNMMQLCTRCLSNCTKKSPNKIASGFFLRLLTSKLMNDIADICKSLASFIKKPFDRGEVESMEDDTNGNLMEVEDQSSMNLFNDYPDSSVSDANEPGESQSTIGAINPLAEEYLSKQDLLFLDMLKFLCLCVTTAQTNTVSFRAADIRRKLLMLIDSSTLEPTKSLHLHMYLMLLKELPGEEYPLPMEDVLELLKPLSNVCSLYRRDQDVCKTILNHVLHVVKNLGQSNMDSENTRDAQGQFLTVIGAFWHLTKERKYIFSVRMALVNCLKTLLEADPYSKWAILNVMGKDFPVNEVFTQFLADNHHQVRMLAAESINRLFQDTKGDSSRLLKALPLKLQQTAFENAYLKAQEGMREMSHSAENPETLDEIYNRKSVLLTLIAVVLSCSPICEKQALFALCKSVKENGLEPHLVKKVLEKVSETFGYRRLEDFMASHLDYLVLEWLNLQDTEYNLSSFPFILLNYTNIEDFYRSCYKVLIPHLVIRSHFDEVKSIANQIQEDWKSLLTDCFPKILVNILPYFAYEGTRDSGMAQQRETATKVYDMLKSENLLGKQIDHLFISNLPEIVVELLMTLHEPANSSASQSTDLCDFSGDLDPAPNPPHFPSHVIKATFAYISNCHKTKLKSILEILSKSPDSYQKILLAICEQAAETNNVYKKHRILKIYHLFVSLLLKDIKSGLGGAWAFVLRDVIYTLIHYINQRPSCIMDVSLRSFSLCCDLLSQVCQTAVTYCKDALENHLHVIVGTLIPLVYEQVEVQKQVLDLLKYLVIDNKDNENLYITIKLLDPFPDHVVFKDLRITQQKIKYSRGPFSLLEEINHFLSVSVYDALPLTRLEGLKDLRRQLELHKDQMVDIMRASQDNPQDGIMVKLVVNLLQLSKMAINHTGEKEVLEAVGSCLGEVGPIDFSTIAIQHSKDASYTKALKLFEDKELQWTFIMLTYLNNTLVEDCVKVRSAAVTCLKNILATKTGHSFWEIYKMTTDPMLAYLQPFRTSRKKFLEVPRFDKENPFEGLDDINLWIPLSENHDIWIKTLTCAFLDSGGTKCEILQLLKPMCEVKTDFCQTVLPYLIHDILLQDTNESWRNLLSTHVQGFFTSCLRHFSQTSRSTTPANLDSESEHFFRCCLDKKSQRTMLAVVDYMRRQKRPSSGTIFNDAFWLDLNYLEVAKVAQSCAAHFTALLYAEIYADKKSMDDQEKRSLAFEEGSQSTTISSLSEKSKEETGISLQDLLLEIYRSIGEPDSLYGCGGGKMLQPITRLRTYEHEAMWGKALVTYDLETAIPSSTRQAGIIQALQNLGLCHILSVYLKGLDYENKDWCPELEELHYQAAWRNMQWDHCTSVSKEVEGTSYHESLYNALQSLRDREFSTFYESLKYARVKEVEEMCKRSLESVYSLYPTLSRLQAIGELESIGELFSRSVTHRQLSEVYIKWQKHSQLLKDSDFSFQEPIMALRTVILEILMEKEMDNSQRECIKDILTKHLVELSILARTFKNTQLPERAIFQIKQYNSVSCGVSEWQLEEAQVFWAKKEQSLALSILKQMIKKLDASCAANNPSLKLTYTECLRVCGNWLAETCLENPAVIMQTYLEKAVEVAGNYDGESSDELRNGKMKAFLSLARFSDTQYQRIENYMKSSEFENKQALLKRAKEEVGLLREHKIQTNRYTVKVQRELELDELALRALKEDRKRFLCKAVENYINCLLSGEEHDMWVFRLCSLWLENSGVSEVNGMMKRDGMKIPTYKFLPLMYQLAARMGTKMMGGLGFHEVLNNLISRISMDHPHHTLFIILALANANRDEFLTKPEVARRSRITKNVPKQSSQLDEDRTEAANRIICTIRSRRPQMVRSVEALCDAYIILANLDATQWKTQRKGINIPADQPITKLKNLEDVVVPTMEIKVDHTGEYGNLVTIQSFKAEFRLAGGVNLPKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGEFLVNNEDGAHKRYRPNDFSAFQCQKKMMEVQKKSFEEKYEVFMDVCQNFQPVFRYFCMEKFLDPAIWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGITGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLLYDPLFDWTMNPLKALYLQQRPEDETELHPTLNADDQECKRNLSDIDQSFNKVAERVLMRLQEKLKGVEEGTVLSVGGQVNLLIQQAIDPKNLSRLFPGWKAWV	Clinical trial	Targeting ATR in vivo using the novel inhibitor VE-822 results in selective sensitization of pancreatic tumors to radiation. Cell Death Dis. 2012 Dec 6;3:e441.	17	EC:2.7	.	PI3/PI4-kinase family. ATM subfamily.	2.7.11.1 	Transferring phosphorus-containing groups	FAT domain; FATC domain; Phosphatidylinositol 3- and 4-kinase; Telomere-length maintenance and DNA damage repair	PF02259; PF02260; PF00454; PF11640	PF02259; FAT; PF02260; FATC; PF00454; PI3_PI4_kinase; PF11640; TAN	.	.	hsa01524: Platinum drug resistance; hsa03440: Homologous recombination; hsa04064: NF-kappa B signaling pathway; hsa04068: FoxO signaling pathway; hsa04110: Cell cycle; hsa04115: p53 signaling pathway; hsa04210: Apoptosis; hsa04218: Cellular senescence; hsa05131: Shigellosis; hsa05165: Human papillomavirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05202: Transcriptional misregulation in cancer; hsa05206: MicroRNAs in cancer	R-HSA-2559586: DNA Damage/Telomere Stress Induced Senescence; R-HSA-3371453: Regulation of HSF1-mediated heat shock response; R-HSA-349425: Autodegradation of the E3 ubiquitin ligase COP1; R-HSA-5685938: HDR through Single Strand Annealing (SSA); R-HSA-5685942: HDR through Homologous Recombination (HRR); R-HSA-5693548: Sensing of DNA Double Strand Breaks; R-HSA-5693554: Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA); R-HSA-5693565: Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks; R-HSA-5693568: Resolution of D-loop Structures through Holliday Junction Intermediates; R-HSA-5693571: Nonhomologous End-Joining (NHEJ); R-HSA-5693579: Homologous DNA Pairing and Strand Exchange; R-HSA-5693607: Processing of DNA double-strand break ends; R-HSA-5693616: Presynaptic phase of homologous DNA pairing and strand exchange; R-HSA-6796648: TP53 Regulates Transcription of DNA Repair Genes; R-HSA-6803204: TP53 Regulates Transcription of Genes Involved in Cytochrome C Release; R-HSA-6803207: TP53 Regulates Transcription of Caspase Activators and Caspases; R-HSA-6804756: Regulation of TP53 Activity through Phosphorylation; R-HSA-6804757: Regulation of TP53 Degradation; R-HSA-6804760: Regulation of TP53 Activity through Methylation; R-HSA-69473: G2/M DNA damage checkpoint; R-HSA-69541: Stabilization of p53; R-HSA-912446: Meiotic recombination; R-HSA-9664873: Pexophagy; R-HSA-9701192: Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function; R-HSA-9704331: Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function; R-HSA-9704646: Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function; R-HSA-9709570: Impaired BRCA2 binding to RAD51; R-HSA-9709603: Impaired BRCA2 binding to PALB2	.	.
TTWK8D0	Sodium pump subunit alpha-1 (ATP1A1)	P05023	AT1A1_HUMAN	Acid anhydrides hydrolase	Sodium/potassium-transporting ATPase alpha1; Sodium pump 1; Na+/K+ ATPase 1; ATP1A1	ATP1A1	"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."	EC 7.2.2.13	.	MGKGVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYAKIVEIPFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPIDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVDWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY	Successful	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	34	.	.	.	.	.	.	.	.	.	.	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	R-HSA-936837:Ion transport by P-type ATPases	.	P05023
TTWNK8B	HUMAN sodium pump subunit alpha-1 (ATP1A1)	P05023	AT1A1_HUMAN	Acid anhydrides hydrolase	Sodium/potassium-transporting ATPase alpha1; Sodium pump 1; Na+/K+ ATPase 1; ATP1A1	ATP1A1	"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."	EC 7.2.2.13	.	MGKGVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYAKIVEIPFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPIDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVDWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY	.	"The 14-3-3 Protein Translates the NA+,K+-ATPase {alpha}1-subunit Phosphorylation Signal Into Binding and Activation of Phosphoinositide 3-kinase During Endocytosis J Biol Chem. 2005 Apr 22;280(16):16272-7."	34	.	.	.	.	.	.	.	.	.	.	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; hsa04925: Aldosterone synthesis and secretion; 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	R-HSA-5578775: Ion homeostasis; R-HSA-936837: Ion transport by P-type ATPases; R-HSA-9679191: Potential therapeutics for SARS	.	P05023
TTQ38E9	Sodium/potassium-transporting ATPase (SPT ATPase)	P05023; P50993; P13637; P05026; P14415; P54709	AT1A1_HUMAN; AT1A2_HUMAN; AT1A3_HUMAN; AT1B1_HUMAN; AT1B2_HUMAN; AT1B3_HUMAN	Acid anhydrides hydrolase	Na(+)/K(+) ATPase	ATP1A1	"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. "	.	.	MGKGVGRDKYEPAAVSEQGDKKGKKGKKDRDMDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFGGFSMLLWIGAILCFLAYSIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTENQSGVSFDKTSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYAKIVEIPFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRCSSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPIDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPIHLLGLRVDWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY	Successful	Treatment of congestive heart failure--current status of use of digitoxin. Eur J Clin Invest. 2001;31 Suppl 2:10-7.	34	.	.	.	.	.	.	.	.	.	.	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	R-HSA-5578775: Ion homeostasis; R-HSA-936837: Ion transport by P-type ATPases; R-HSA-9679191: Potential therapeutics for SARS	.	P05023
TT5B6HJ	Sodium pump alpha-2 (ATP1A2)	P50993	AT1A2_HUMAN	Cation transporting ATPase	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	ATP1A2	"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."	EC 7.2.2.13	.	MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDVLARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPMSQVNPREAKACVVHGSDLKDMTSEQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTMNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY	Literature-reported	Sodium pump isoform expression in heart failure: implication for treatment. Basic Res Cardiol. 2002;97 Suppl 1:I25-30.	.	TC=3.A.3	Acid anhydrides hydrolase	cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. 	7.2.2.13	Catalysing the translocation of inorganic cations	"Cation transporting ATPase, C-terminus; Cation transporter/ATPase, N-terminus"	PF00689; PF00690	PF00689; Cation_ATPase_C; PF00690; Cation_ATPase_N	3.A.3.1.1	The P-type ATPase (P-ATPase) Superfamily	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; hsa04925: Aldosterone synthesis and secretion; 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	R-HSA-5578775: Ion homeostasis; R-HSA-936837: Ion transport by P-type ATPases; R-HSA-9679191: Potential therapeutics for SARS	.	P50993
TTE6THL	Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (ATP2A2)	P16615	AT2A2_HUMAN	Cation transporting ATPase	"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"	ATP2A2	"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."	EC 7.2.2.10	6JJU; 5ZTF	MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDRVEGDTCSLNEFTITGSTYAPIGEVHKDDKPVNCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTSGVKQKIMSVIREWGSGSDTLRCLALATHDNPLRREEMHLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELNPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFEGVDCAIFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNVTQWLMVLKISLPVILMDETLKFVARNYLEPGKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS	Clinical trial	Interaction of D-600 with the transmembrane domain of the sarcoplasmic reticulum Ca(2+)-ATPase. Am J Physiol Cell Physiol. 2000 Jul;279(1):C166-72.	21	TC=3.A.3	Acid anhydrides hydrolase	cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily. 	7.2.2.10	Catalysing the translocation of inorganic cations	"Cation transporting ATPase, C-terminus; Cation transporter/ATPase, N-terminus"	PF00689; PF00690	PF00689; Cation_ATPase_C; PF00690; Cation_ATPase_N	3.A.3.2.7	The P-type ATPase (P-ATPase) Superfamily	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	R-HSA-1912420:Pre-NOTCH Processing in Golgi; R-HSA-936837:Ion transport by P-type ATPases	.	P16615
TTF1QVM	Gastric H(+)/K(+) ATPase alpha (ATP4A)	P20648	ATP4A_HUMAN	Acid anhydrides hydrolase	Gastric H+/K+ ATPase alpha subunit; Gastric H(+)/K(+)-ATPase; ATP4A	ATP4A	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.	EC 7.2.2.19	.	MGKAENYELYSVELGPGPGGDMAAKMSKKKKAGGGGGKRKEKLENMKKEMEINDHQLSVAELEQKYQTSATKGLSASLAAELLLRDGPNALRPPRGTPEYVKFARQLAGGLQCLMWVAAAICLIAFAIQASEGDLTTDDNLYLAIALIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQATVIRDGDKFQINADQLVVGDLVEMKGGDRVPADIRILAAQGCKVDNSSLTGESEPQTRSPECTHESPLETRNIAFFSTMCLEGTVQGLVVNTGDRTIIGRIASLASGVENEKTPIAIEIEHFVDIIAGLAILFGATFFIVAMCIGYTFLRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRLASKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHTADTTEDQSGQTFDQSSETWRALCRVLTLCNRAAFKSGQDAVPVPKRIVIGDASETALLKFSELTLGNAMGYRDRFPKVCEIPFNSTNKFQLSIHTLEDPRDPRHLLVMKGAPERVLERCSSILIKGQELPLDEQWREAFQTAYLSLGGLGERVLGFCQLYLNEKDYPPGYAFDVEAMNFPSSGLCFAGLVSMIDPPRATVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRVPVDQVNRKDARACVINGMQLKDMDPSELVEALRTHPEMVFARTSPQQKLVIVESCQRLGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFDNLKKSIAYTLTKNIPELTPYLIYITVSVPLPLGCITILFIELCTDIFPSVSLAYEKAESDIMHLRPRNPKRDRLVNEPLAAYSYFQIGAIQSFAGFTDYFTAMAQEGWFPLLCVGLRAQWEDHHLQDLQDSYGQEWTFGQRLYQQYTCYTVFFISIEVCQIADVLIRKTRRLSAFQQGFFRNKILVIAIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPLPYGILIFVYDEIRKLGVRCCPGSWWDQELYY	Successful	Review article: rabeprazole's tolerability profile in clinical trials. Aliment Pharmacol Ther. 1999 Oct;13 Suppl 5:17-23.	34	.	.	.	.	.	.	.	.	.	.	hsa00190:Oxidative phosphorylation; hsa04966:Collecting duct acid secretion; hsa04971:Gastric acid secretion	R-HSA-936837:Ion transport by P-type ATPases	MetaCyc:HS02790-MON	P20648
TTLOKXP	Gastric H(+)/K(+) ATPase (Proton pump)	P20648; P51164	ATP4A_HUMAN; ATP4B_HUMAN	.	Proton pump; Potassium-transporting ATPase	ATP4A	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.	.	.	MGKAENYELYSVELGPGPGGDMAAKMSKKKKAGGGGGKRKEKLENMKKEMEINDHQLSVAELEQKYQTSATKGLSASLAAELLLRDGPNALRPPRGTPEYVKFARQLAGGLQCLMWVAAAICLIAFAIQASEGDLTTDDNLYLAIALIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQATVIRDGDKFQINADQLVVGDLVEMKGGDRVPADIRILAAQGCKVDNSSLTGESEPQTRSPECTHESPLETRNIAFFSTMCLEGTVQGLVVNTGDRTIIGRIASLASGVENEKTPIAIEIEHFVDIIAGLAILFGATFFIVAMCIGYTFLRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRLASKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHTADTTEDQSGQTFDQSSETWRALCRVLTLCNRAAFKSGQDAVPVPKRIVIGDASETALLKFSELTLGNAMGYRDRFPKVCEIPFNSTNKFQLSIHTLEDPRDPRHLLVMKGAPERVLERCSSILIKGQELPLDEQWREAFQTAYLSLGGLGERVLGFCQLYLNEKDYPPGYAFDVEAMNFPSSGLCFAGLVSMIDPPRATVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRVPVDQVNRKDARACVINGMQLKDMDPSELVEALRTHPEMVFARTSPQQKLVIVESCQRLGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFDNLKKSIAYTLTKNIPELTPYLIYITVSVPLPLGCITILFIELCTDIFPSVSLAYEKAESDIMHLRPRNPKRDRLVNEPLAAYSYFQIGAIQSFAGFTDYFTAMAQEGWFPLLCVGLRAQWEDHHLQDLQDSYGQEWTFGQRLYQQYTCYTVFFISIEVCQIADVLIRKTRRLSAFQQGFFRNKILVIAIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPLPYGILIFVYDEIRKLGVRCCPGSWWDQELYY	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	hsa00190: Oxidative phosphorylation; hsa01100: Metabolic pathways; hsa04966: Collecting duct acid secretion; hsa04971: Gastric acid secretion	R-HSA-936837: Ion transport by P-type ATPases	MetaCyc:HS02790-MON	P20648
TTWDM4U	HUMAN ATPase H+ transporting accessory protein 1 (ATP6AP1)	Q15904	VAS1_HUMAN	Vacuolar ATPase subunit S1 family	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	ATP6AP1	"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."	.	.	MMAAMATARVRMGPRCAQALWRMPWLPVFLSLAAAAAAAAAEQQVPLVLWSSDRDLWAPAADTHEGHITSDLQLSTYLDPALELGPRNVLLFLQDKLSIEDFTAYGGVFGNKQDSAFSNLENALDLAPSSLVLPAVDWYAVSTLTTYLQEKLGASPLHVDLATLRELKLNASLPALLLIRLPYTASSGLMAPREVLTGNDEVIGQVLSTLKSEDVPYTAALTAVRPSRVARDVAVVAGGLGRQLLQKQPVSPVIHPPVSYNDTAPRILFWAQNFSVAYKDQWEDLTPLTFGVQELNLTGSFWNDSFARLSLTYERLFGTTVTFKFILANRLYPVSARHWFTMERLEVHSNGSVAYFNASQVTGPSIYSFHCEYVSSLSKKGSLLVARTQPSPWQMMLQDFQIQAFNVMGEQFSYASDCASFFSPGIWMGLLTSLFMLFIFTYGLHMILSLKTMDRFDDHKGPTISLTQIV	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa00190: Oxidative phosphorylation; hsa01100: Metabolic pathways; hsa04142: Lysosome; hsa04145: Phagosome; hsa05110: Vibrio cholerae infection; hsa05120: Epithelial cell signaling in Helicobacter pylori infection; hsa05152: Tuberculosis; hsa05161: Hepatitis B; hsa05165: Human papillomavirus infection; hsa05323: Rheumatoid arthritis	R-HSA-77387: Insulin receptor recycling; R-HSA-8980692: RHOA GTPase cycle; R-HSA-917977: Transferrin endocytosis and recycling; R-HSA-983712: Ion channel transport	MetaCyc:HS01034-MON	Q15904
TTL2PXZ	Vacuolar-type proton ATPase catalytic A (v-ATPase-A)	P38606	VATA_HUMAN	Acid anhydrides hydrolase	Vacuolar proton pump subunit alpha; Vacuolar ATPase isoform VA68; VPP2; V-ATPase subunit A; V-ATPase 69 kDa subunit; ATP6V1A1; ATP6V1A; ATP6A1	ATP6V1A	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.	EC 7.1.2.2	.	MDFSKLPKILDEDKESTFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQTQSIYIPRGVNVSALSRDIKWDFTPCKNLRVGSHITGGDIYGIVSENSLIKHKIMLPPRNRGTVTYIAPPGNYDTSDVVLELEFEGVKEKFTMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAQSDNKITWSIIREHMGDILYKLSSMKFKDPLKDGEAKIKSDYAQLLEDMQNAFRSLED	Literature-reported	"Novel antifungal agents, targets or therapeutic strategies for the treatment of invasive fungal diseases: a review of the literature (2005-2009). Rev Iberoam Micol. 2009 Mar 31;26(1):15-22."	2.1	.	.	.	.	.	.	.	.	.	.	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	R-HSA-1222556:ROS production in response to bacteria; R-HSA-77387:Insulin receptor recycling; R-HSA-917977:Transferrin endocytosis and recycling	MetaCyc:HS03781-MON	P38606
TT2Q719	HUMAN vacuolar-type proton ATPase catalytic A (v-ATPase-A)	P38606	VATA_HUMAN	Acid anhydrides hydrolase	Vacuolar proton pump subunit alpha; Vacuolar ATPase isoform VA68; VPP2; V-ATPase subunit A; V-ATPase 69 kDa subunit; ATP6V1A1; ATP6V1A; ATP6A1	ATP6V1A	"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."	EC 7.1.2.2	.	MDFSKLPKILDEDKESTFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQTQSIYIPRGVNVSALSRDIKWDFTPCKNLRVGSHITGGDIYGIVSENSLIKHKIMLPPRNRGTVTYIAPPGNYDTSDVVLELEFEGVKEKFTMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAQSDNKITWSIIREHMGDILYKLSSMKFKDPLKDGEAKIKSDYAQLLEDMQNAFRSLED	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa00190: Oxidative phosphorylation; hsa01100: Metabolic pathways; hsa04145: Phagosome; hsa04150: mTOR signaling pathway; hsa04721: Synaptic vesicle cycle; hsa04966: Collecting duct acid secretion; hsa05110: Vibrio cholerae infection; hsa05120: Epithelial cell signaling in Helicobacter pylori infection; hsa05165: Human papillomavirus infection; hsa05323: Rheumatoid arthritis	R-HSA-1222556: ROS and RNS production in phagocytes; R-HSA-77387: Insulin receptor recycling; R-HSA-917977: Transferrin endocytosis and recycling; R-HSA-9639288: Amino acids regulate mTORC1; R-HSA-983712: Ion channel transport	MetaCyc:HS03781-MON	P38606
TTOPO51	Copper-transporting ATPase 2 (ATP7B)	P35670	ATP7B_HUMAN	.	Copper pump 2; Wilson disease-associated protein	ATP7B	"Copper ion transmembrane transporter involved in the export of copper out of the cells. It is involved in copper homeostasis in the liver, where it ensures the efflux of copper from hepatocytes into the bile in response to copper overload. {ECO:0000269|PubMed:18203200, ECO:0000269|PubMed:22240481, ECO:0000269|PubMed:24706876, ECO:0000269|PubMed:26004889}."	EC 7.2.2.8	2ARF;2EW9;2KOY;2LQB;2N7Y;2ROP;6A71;6A72;7XUK;7XUM;7XUN;7XUO;8IOY	MPEQERQITAREGASRKILSKLSLPTRAWEPAMKKSFAFDNVGYEGGLDGLGPSSQVATSTVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSVVCLQQVCHQIGDMGFEASIAEGKAASWPSRSLPAQEAVVKLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAAIKSKVAPLSLGPIDIERLQSTNPKRPLSSANQNFNNSETLGHQGSHVVTLQLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTSPVALQRAIEALPPGNFKVSLPDGAEGSGTDHRSSSSHSPGSPPRNQVQGTCSTTLIAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVSESCSTNPLGNHSAGNSMVQTTDGTPTSVQEVAPHTGRLPANHAPDILAKSPQSTRAVAPQKCFLQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAAVMEDYAGSDGNIELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHASLAQRNPNAHHLDHKMEIKQWKKSFLCSLVFGIPVMALMIYMLIPSNEPHQSMVLDHNIIPGLSILNLIFFILCTFVQLLGGWYFYVQAYKSLRHRSANMDVLIVLATSIAYVYSLVILVVAVAEKAERSPVTFFDTPPMLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEDNLIIREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGFIDFGVVQRYFPNPNKHISQTEVIIRFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATLPLRKVLAVVGTAEASSEHPLGVAVTKYCKEELGTETLGYCTDFQAVPGCGIGCKVSNVEGILAHSERPLSAPASHLNEAGSLPAEKDAVPQTFSVLIGNREWLRRNGLTISSDVSDAMTDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPIGIVLQPWMGSAAMAASSVSVVLSSLQLKCYKKPDLERYEAQAHGHMKPLTASQVSVHIGMDDRWRDSPRATPWDQVSYVSQVSLSSLTSDKPSRHSAAADDDGDKWSLLLNGRDEEQYI	Clinical trial	"ClinicalTrials.gov (NCT04537377) A Phase I/II, Multicenter, Non-randomized, Open Label, Adaptive Design, 5-year Follow-up, Single Dose-escalation Study of VTX-801 in Adult Patients With Wilson's Disease. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	hsa:540	R-HSA-936837;	.	P35670;
TT8ZYBQ	Serine/threonine-protein kinase ATR (FRP1)	Q13535	ATR_HUMAN	Kinase	FRAP-related protein 1; Ataxia telangiectasia and Rad3-related protein	ATR	"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."	EC 2.7.11.1	5YZ0	MGEHGLELASMIPALRELGSATPEEYNTVVQKPRQILCQFIDRILTDVNVVAVELVKKTDSQPTSVMLLDFIQHIMKSSPLMFVNVSGSHEAKGSCIEFSNWIITRLLRIAATPSCHLLHKKICEVICSLLFLFKSKSPAIFGVLTKELLQLFEDLVYLHRRNVMGHAVEWPVVMSRFLSQLDEHMGYLQSAPLQLMSMQNLEFIEVTLLMVLTRIIAIVFFRRQELLLWQIGCVLLEYGSPKIKSLAISFLTELFQLGGLPAQPASTFFSSFLELLKHLVEMDTDQLKLYEEPLSKLIKTLFPFEAEAYRNIEPVYLNMLLEKLCVMFEDGVLMRLKSDLLKAALCHLLQYFLKFVPAGYESALQVRKVYVRNICKALLDVLGIEVDAEYLLGPLYAALKMESMEIIEEIQCQTQQENLSSNSDGISPKRRRLSSSLNPSKRAPKQTEEIKHVDMNQKSILWSALKQKAESLQISLEYSGLKNPVIEMLEGIAVVLQLTALCTVHCSHQNMNCRTFKDCQHKSKKKPSVVITWMSLDFYTKVLKSCRSLLESVQKLDLEATIDKVVKIYDALIYMQVNSSFEDHILEDLCGMLSLPWIYSHSDDGCLKLTTFAANLLTLSCRISDSYSPQAQSRCVFLLTLFPRRIFLEWRTAVYNWALQSSHEVIRASCVSGFFILLQQQNSCNRVPKILIDKVKDDSDIVKKEFASILGQLVCTLHGMFYLTSSLTEPFSEHGHVDLFCRNLKATSQHECSSSQLKASVCKPFLFLLKKKIPSPVKLAFIDNLHHLCKHLDFREDETDVKAVLGTLLNLMEDPDKDVRVAFSGNIKHILESLDSEDGFIKELFVLRMKEAYTHAQISRNNELKDTLILTTGDIGRAAKGDLVPFALLHLLHCLLSKSASVSGAAYTEIRALVAAKSVKLQSFFSQYKKPICQFLVESLHSSQMTALPNTPCQNADVRKQDVAHQREMALNTLSEIANVFDFPDLNRFLTRTLQVLLPDLAAKASPAASALIRTLGKQLNVNRREILINNFKYIFSHLVCSCSKDELERALHYLKNETEIELGSLLRQDFQGLHNELLLRIGEHYQQVFNGLSILASFASSDDPYQGPRDIISPELMADYLQPKLLGILAFFNMQLLSSSVGIEDKKMALNSLMSLMKLMGPKHVSSVRVKMMTTLRTGLRFKDDFPELCCRAWDCFVRCLDHACLGSLLSHVIVALLPLIHIQPKETAAIFHYLIIENRDAVQDFLHEIYFLPDHPELKKIKAVLQEYRKETSESTDLQTTLQLSMKAIQHENVDVRIHALTSLKETLYKNQEKLIKYATDSETVEPIISQLVTVLLKGCQDANSQARLLCGECLGELGAIDPGRLDFSTTETQGKDFTFVTGVEDSSFAYGLLMELTRAYLAYADNSRAQDSAAYAIQELLSIYDCREMETNGPGHQLWRRFPEHVREILEPHLNTRYKSSQKSTDWSGVKKPIYLSKLGSNFAEWSASWAGYLITKVRHDLASKIFTCCSIMMKHDFKVTIYLLPHILVYVLLGCNQEDQQEVYAEIMAVLKHDDQHTINTQDIASDLCQLSTQTVFSMLDHLTQWARHKFQALKAEKCPHSKSNRNKVDSMVSTVDYEDYQSVTRFLDLIPQDTLAVASFRSKAYTRAVMHFESFITEKKQNIQEHLGFLQKLYAAMHEPDGVAGVSAIRKAEPSLKEQILEHESLGLLRDATACYDRAIQLEPDQIIHYHGVVKSMLGLGQLSTVITQVNGVHANRSEWTDELNTYRVEAAWKLSQWDLVENYLAADGKSTTWSVRLGQLLLSAKKRDITAFYDSLKLVRAEQIVPLSAASFERGSYQRGYEYIVRLHMLCELEHSIKPLFQHSPGDSSQEDSLNWVARLEMTQNSYRAKEPILALRRALLSLNKRPDYNEMVGECWLQSARVARKAGHHQTAYNALLNAGESRLAELYVERAKWLWSKGDVHQALIVLQKGVELCFPENETPPEGKNMLIHGRAMLLVGRFMEETANFESNAIMKKYKDVTACLPEWEDGHFYLAKYYDKLMPMVTDNKMEKQGDLIRYIVLHFGRSLQYGNQFIYQSMPRMLTLWLDYGTKAYEWEKAGRSDRVQMRNDLGKINKVITEHTNYLAPYQFLTAFSQLISRICHSHDEVFVVLMEIIAKVFLAYPQQAMWMMTAVSKSSYPMRVNRCKEILNKAIHMKKSLEKFVGDATRLTDKLLELCNKPVDGSSSTLSMSTHFKMLKKLVEEATFSEILIPLQSVMIPTLPSILGTHANHASHEPFPGHWAYIAGFDDMVEILASLQKPKKISLKGSDGKFYIMMCKPKDDLRKDCRLMEFNSLINKCLRKDAESRRRELHIRTYAVIPLNDECGIIEWVNNTAGLRPILTKLYKEKGVYMTGKELRQCMLPKSAALSEKLKVFREFLLPRHPPIFHEWFLRTFPDPTSWYSSRSAYCRSTAVMSMVGYILGLGDRHGENILFDSLTGECVHVDFNCLFNKGETFEVPEIVPFRLTHNMVNGMGPMGTEGLFRRACEVTMRLMRDQREPLMSVLKTFLHDPLVEWSKPVKGHSKAPLNETGEVVNEKAKTHVLDIEQRLQGVIKTRNRVTGLPLSIEGHVHYLIQEATDENLLCQMYLGWTPYM	Clinical trial	ATR inhibitors VE-821 and VX-970 sensitize cancer cells to topoisomerase i inhibitors by disabling DNA replication initiation and fork elongation responses. Cancer Res. 2014 Dec 1;74(23):6968-79.	17	EC:2.7	Kinase	PI3/PI4-kinase family. ATM subfamily.	2.7.11.1	Transferring phosphorus-containing groups	FAT domain; FATC domain; Phosphatidylinositol 3- and 4-kinase; UME (NUC010) domain	PF02259; PF02260; PF00454; PF08064	PF02259; FAT; PF02260; FATC; PF00454; PI3_PI4_kinase; PF08064; UME	.	.	hsa03460:Fanconi anemia pathway; hsa04110:Cell cycle; hsa04115:p53 signaling pathway; hsa05166:HTLV-I infection	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	.	Q13535
TTFLIKM	Apoptosis-related protein 3 (ATRAID)	Q6UW56	ARAID_HUMAN	.	p18; C2orf28	ATRAID	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.	.	.	MAPHDPGSLTTLVPWAAALLLALGVERALALPEICTQCPGSVQNLSKVAFYCKTTRELMLHARCCLNQKGTILGLDLQNCSLEDPGPNFHQAHTTVIIDLQANPLKGDLANTFRGFTQLQTLILPQHVNCPGGINAWNTITSYIDNQICQGQKNLCNNTGDPEMCPENGSCVPDGPGLLQCVCADGFHGYKCMRQGSFSLLMFFGILGATTLSVSILLWATQRRKAKTS	Literature-reported	Apoptosis related protein 3 is a lysosomal membrane protein. Biochem Biophys Res Commun. 2015 May 15;460(4):915-22.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q6UW56
TTPQJ7P	Ataxin-2 messenger RNA (ATXN2 mRNA)	Q99700	ATX2_HUMAN	mRNA target	Spinocerebellar ataxia type 2 protein (mRNA); Trinucleotide repeat-containing gene 13 protein (mRNA)	ATXN2	"Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane. {ECO:0000269|PubMed:18602463}."	.	3KTR	MRSAAAAPRSPAVATESRRFAAARWPGWRSLQRPARRSGRGGGGAAPGPYPSAAPPPPGPGPPPSRQSSPPSASDCFGSNGNGGGAFRPGSRRLLGLGGPPRPFVVLLLPLASPGAPPAAPTRASPLGARASPPRSGVSLARPAPGCPRPACEPVYGPLTMSLKPQQQQQQQQQQQQQQQQQQQQQQQPPPAAANVRKPGGSGLLASPAAAPSPSSSSVSSSSATAPSSVVAATSGGGRPGLGRGRNSNKGLPQSTISFDGIYANMRMVHILTSVVGSKCEVQVKNGGIYEGVFKTYSPKCDLVLDAAHEKSTESSSGPKREEIMESILFKCSDFVVVQFKDMDSSYAKRDAFTDSAISAKVNGEHKEKDLEPWDAGELTANEELEALENDVSNGWDPNDMFRYNEENYGVVSTYDSSLSSYTVPLERDNSEEFLKREARANQLAEEIESSAQYKARVALENDDRSEEEKYTAVQRNSSEREGHSINTRENKYIPPGQRNREVISWGSGRQNSPRMGQPGSGSMPSRSTSHTSDFNPNSGSDQRVVNGGVPWPSPCPSPSSRPPSRYQSGPNSLPPRAATPTRPPSRPPSRPSRPPSHPSAHGSPAPVSTMPKRMSSEGPPRMSPKAQRHPRNHRVSAGRGSISSGLEFVSHNPPSEAATPPVARTSPSGGTWSSVVSGVPRLSPKTHRPRSPRQNSIGNTPSGPVLASPQAGIIPTEAVAMPIPAASPTPASPASNRAVTPSSEAKDSRLQDQRQNSPAGNKENIKPNETSPSFSKAENKGISPVVSEHRKQIDDLKKFKNDFRLQPSSTSESMDQLLNKNREGEKSRDLIKDKIEPSAKDSFIENSSSNCTSGSSKPNSPSISPSILSNTEHKRGPEVTSQGVQTSSPACKQEKDDKEEKKDAAEQVRKSTLNPNAKEFNPRSFSQPKPSTTPTSPRPQAQPSPSMVGHQQPTPVYTQPVCFAPNMMYPVPVSPGVQPLYPIPMTPMPVNQAKTYRAVPNMPQQRQDQHHQSAMMHPASAAGPPIAATPPAYSTQYVAYSPQQFPNQPLVQHVPHYQSQHPHVYSPVIQGNARMMAPPTHAQPGLVSSSATQYGAHEQTHAMYACPKLPYNKETSPSFYFAISTGSLAQQYAHPNATLHPHTPHPQPSATPTGQQQSQHGGSHPAPSPVQHHQHQAAQALHLASPQQQSAIYHAGLAPTPPSMTPASNTQSPQNSFPAAQQTVFTIHPSHVQPAYTNPPHMAHVPQAHVQSGMVPSHPTAHAPMMLMTTQPPGGPQAALAQSALQPIPVSTTAHFPYMTHPSVQAHHQQQL	Clinical trial	"ClinicalTrials.gov (NCT04494256) A Phase 1/2 Multiple-Ascending-Dose Study With a Long-Term Open-Label Extension to Assess the Safety, Tolerability, Pharmacokinetics, Pharmacodynamics, and Effect on Disease Progression of BIIB105 Administered Intrathecally to Adults With Amyotrophic Lateral Sclerosis With or Without Poly-CAG Expansion in the ATXN2 Gene. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	hsa:6311	.	.	Q99700;
TT6A17J	Ataxin-3 messenger RNA (ATXN3 mRNA)	P54252	ATX3_HUMAN	mRNA target	Machado-Joseph disease protein 1 (mRNA); Spinocerebellar ataxia type 3 protein (mRNA)	ATXN3	"Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates (PubMed:12297501, PubMed:17696782, PubMed:23625928, PubMed:28445460, PubMed:33157014, PubMed:16118278). Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins (PubMed:17696782). Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (By similarity). Interacts with key regulators of transcription and represses transcription: acts as a histone-binding protein that regulates transcription (PubMed:12297501). Acts as a negative regulator of mTORC1 signaling in response to amino acid deprivation by mediating deubiquitination of RHEB, thereby promoting RHEB inactivation by the TSC-TBC complex (PubMed:33157014). Regulates autophagy via the deubiquitination of 'Lys-402' of BECN1 leading to the stabilization of BECN1 (PubMed:28445460). {ECO:0000250|UniProtKB:Q9CVD2, ECO:0000269|PubMed:12297501, ECO:0000269|PubMed:16118278, ECO:0000269|PubMed:17696782, ECO:0000269|PubMed:23625928, ECO:0000269|PubMed:28445460, ECO:0000269|PubMed:33157014}."	EC 3.4.19.12	1YZB;2AGA;2DOS;2JRI;2KLZ;4WTH;4YS9	MESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERMRMAEGGVTSEDYRTFLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICNYKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQMIRVQQMHRPKLIGEELAQLKEQRVHKTDLERVLEANDGSGMLDEDEEDLQRALALSRQEIDMEDEEADLRRAIQLSMQGSSRNISQDMTQTSGTNLTSEELRKRREAYFEKQQQKQQQQQQQQQQGDLSGQSSHPCERPATSSGALGSDLGDAMSEEDMLQAAVTMSLETVRNDLKTEGKK	Clinical trial	"ClinicalTrials.gov (NCT05160558) A Phase 1, Blinded, Randomized, Placebo-controlled Study to Investigate the Safety, Tolerability, and Pharmacokinetics of Multiple Ascending Doses of BIIB132 Administered Intrathecally to Adults With Spinocerebellar Ataxia 3. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	hsa:4287	R-HSA-5689877;R-HSA-9615017;	.	P54252;
TTPS3C0	Aurora kinase A (AURKA)	O14965	AURKA_HUMAN	Kinase	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	AURKA	"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."	EC 2.7.11.1	6R4D; 6R4C; 6R4B; 6R4A; 6R49	MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRVPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS	Clinical trial	"Effect of Aurora A kinase inhibitor MLN8237 combined with rituximab on antitumor activity in preclinical B-cell non-Hodgkin's lymphoma models. Journal of Clinical Oncology, 2009:8553."	25	EC:2.7	Kinase	protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.	2.7.11.1 	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04114:Oocyte meiosis	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	.	O14965
TT9RTBL	Aurora B messenger RNA (AURKB mRNA)	Q96GD4	AURKB_HUMAN	mRNA target	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)	AURKB	"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."	EC 2.7.11.1	4AF3	MAQKENSYPWPYGRQTAPSGLSTLPQRVLRKEPVTPSALVLMSRSNVQPTAAPGQKVMENSSGTPDILTRHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRRVLPPSALQSVA	Clinical trial	Potent and selective Aurora inhibitors identified by the expansion of a novel scaffold for protein kinase inhibition. J Med Chem. 2005 Apr 21;48(8):3080-4.	21	mRNA	mRNA target	.	.	.	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	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	.	Q96GD4
TT5LS6T	Aurora kinase B (AURKB)	Q96GD4	AURKB_HUMAN	Kinase	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	AURKB	"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."	EC 2.7.11.1	4AF3	MAQKENSYPWPYGRQTAPSGLSTLPQRVLRKEPVTPSALVLMSRSNVQPTAAPGQKVMENSSGTPDILTRHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRRVLPPSALQSVA	Clinical trial	A phase I trial of AT9283 (a selective inhibitor of aurora kinases) in children and adolescents with solid tumors: a Cancer Research UK study. Clin Cancer Res. 2015 Jan 15;21(2):267-73.	25	EC:2.7	Kinase	protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	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	.	Q96GD4
TTLYXIT	Aurora kinase C (AURKC)	Q9UQB9	AURKC_HUMAN	Kinase	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	AURKC	"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."	EC 2.7.11.1	6GR9; 6GR8	MSSPRAVVQLGKAQPAGEELATANQTAQQPSSPAMRRLTVDDFEIGRPLGKGKFGNVYLARLKESHFIVALKVLFKSQIEKEGLEHQLRREIEIQAHLQHPNILRLYNYFHDARRVYLILEYAPRGELYKELQKSEKLDEQRTATIIEELADALTYCHDKKVIHRDIKPENLLLGFRGEVKIADFGWSVHTPSLRRKTMCGTLDYLPPEMIEGRTYDEKVDLWCIGVLCYELLVGYPPFESASHSETYRRILKVDVRFPLSMPLGARDLISRLLRYQPLERLPLAQILKHPWVQAHSRRVLPPCAQMAS	Clinical trial	"Preclinical characterization of ABT-348, a kinase inhibitor targeting the aurora, vascular endothelial growth factor receptor/platelet-derived growth factor receptor, and Src kinase families. J Pharmacol Exp Ther. 2012 Dec;343(3):617-27."	21	EC:2.7	.	protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04114:Oocyte meiosis	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	.	Q9UQB9
TTJ8EWH	Arginine vasopressin (AVP)	P01185	NEU2_HUMAN	.	Vasopressin-neurophysin 2-copeptin; VP; Copeptin; AVP-NPII; ARVP	AVP	Neurophysin 2 specifically binds vasopressin.	.	.	MPDTMLPACFLGLLAFSSACYFQNCPRGGKRAMSDLELRQCLPCGPGGKGRCFGPSICCADELGCFVGTAEALRCQEENYLPSPCQSGQKACGSGGRCAAFGVCCNDESCVTEPECREGFHRRARASDRSNATQLDGPAGALLLRLVQLAGAPEPFEPAQPDAY	Literature-reported	Emergent early markers of renal progression in autosomal-dominant polycystic kidney disease patients: implications for prevention and treatment. Am J Nephrol. 2012;36(2):162-7. 	.	.	.	vasopressin/oxytocin family.	.	.	"Neurohypophysial hormones, N-terminal Domain; Neurohypophysial hormones, C-terminal Domain"	PF00220; PF00184	PF00220; Hormone_4; PF00184; Hormone_5	.	.	hsa04962:Vasopressin-regulated water reabsorption	"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"	.	P01185
TT4TFGN	Vasopressin V1a receptor (V1AR)	P37288	V1AR_HUMAN	GPCR rhodopsin	Vascular/hepatic-type arginine vasopressin receptor; V1aR; V1a vasopressin receptor; Antidiuretic hormone receptor 1a; AVPR1; AVPR V1a	AVPR1A	"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."	.	1YTV	MRLSAGPDAGPSGNSSPWWPLATGAGNTSREAEALGEGNGPPRDVRNEELAKLEIAVLAVTFAVAVLGNSSVLLALHRTPRKTSRMHLFIRHLSLADLAVAFFQVLPQMCWDITYRFRGPDWLCRVVKHLQVFGMFASAYMLVVMTADRYIAVCHPLKTLQQPARRSRLMIAAAWVLSFVLSTPQYFVFSMIEVNNVTKARDCWATFIQPWGSRAYVTWMTGGIFVAPVVILGTCYGFICYNIWCNVRGKTASRQSKGAEQAGVAFQKGFLLAPCVSSVKSISRAKIRTVKMTFVIVTAYIVCWAPFFIIQMWSVWDPMSVWTESENPTITITALLGSLNSCCNPWIYMFFSGHLLQDCVQSFPCCQNMKEKFNKEDTDSMSRRQTFYSNNRSPTNSTGMWKDSPKSSKSIKFIPVST	Successful	Investigational vasopressin receptor modulators in the pipeline. Expert Opin Investig Drugs. 2009 Aug;18(8):1119-31.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family. Vasopressin/oxytocin receptor subfamily.	.	.	7 transmembrane receptor (rhodopsin family); Domain of unknown function (DUF1856)	PF00001; PF08983	PF00001; 7tm_1; PF08983; DUF1856	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04270:Vascular smooth muscle contraction	R-HSA-388479:Vasopressin-like receptors; R-HSA-416476:G alpha (q) signalling events	.	P37288
TTL9MHW	Vasopressin V1b receptor (V1BR)	P47901	V1BR_HUMAN	GPCR rhodopsin	Vasopressin V3 receptor; Vasopressin V(1b) Receptor; VPR3; V1bR; Antidiuretic hormone receptor 1b; AVPR3; AVPR V3; AVPR V1b	AVPR1B	The activity of this receptor is mediated by G proteins which activate a phosphatidyl-inositol-calcium second messenger system. Receptor for arginine vasopressin.	.	.	MDSGPLWDANPTPRGTLSAPNATTPWLGRDEELAKVEIGVLATVLVLATGGNLAVLLTLGQLGRKRSRMHLFVLHLALTDLAVALFQVLPQLLWDITYRFQGPDLLCRAVKYLQVLSMFASTYMLLAMTLDRYLAVCHPLRSLQQPGQSTYLLIAAPWLLAAIFSLPQVFIFSLREVIQGSGVLDCWADFGFPWGPRAYLTWTTLAIFVLPVTMLTACYSLICHEICKNLKVKTQAWRVGGGGWRTWDRPSPSTLAATTRGLPSRVSSINTISRAKIRTVKMTFVIVLAYIACWAPFFSVQMWSVWDKNAPDEDSTNVAFTISMLLGNLNSCCNPWIYMGFNSHLLPRPLRHLACCGGPQPRMRRRLSDGSLSSRHTTLLTRSSCPATLSLSLSLTLSGRPRPEESPRDLELADGEGTAETIIF	Successful	Design of potent and selective agonists for the human vasopressin V1b receptor based on modifications of [deamino-cys1]arginine vasopressin at position 4. J Med Chem. 2004 Apr 22;47(9):2375-88.	34	PF00001	.	G-protein coupled receptor 1 family. Vasopressin/oxytocin receptor subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.10.2	The G-protein-coupled receptor (GPCR) Family	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04270:Vascular smooth muscle contraction	R-HSA-388479:Vasopressin-like receptors; R-HSA-416476:G alpha (q) signalling events	.	P47901
TTK8R02	Vasopressin V2 receptor (V2R)	P30518	V2R_HUMAN	GPCR rhodopsin	Renal-type arginine vasopressin receptor; DIR3; DIR; Antidiuretic hormone receptor; AVPR V2; ADHR	AVPR2	The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Involved in renal water reabsorption. Receptor for arginine vasopressin.	.	4JQI	MLMASTTSAVPGHPSLPSLPSNSSQERPLDTRDPLLARAELALLSIVFVAVALSNGLVLAALARRGRRGHWAPIHVFIGHLCLADLAVALFQVLPQLAWKATDRFRGPDALCRAVKYLQMVGMYASSYMILAMTLDRHRAICRPMLAYRHGSGAHWNRPVLVAWAFSLLLSLPQLFIFAQRNVEGGSGVTDCWACFAEPWGRRTYVTWIALMVFVAPTLGIAACQVLIFREIHASLVPGPSERPGGRRRGRRTGSPGEGAHVSAAVAKTVRMTLVIVVVYVLCWAPFFLVQLWAAWDPEAPLEGAPFVLLMLLASLNSCTNPWIYASFSSSVSSELRSLLCCARGRTPPSLGPQDESCTTASSSLAKDTSS	Successful	Vasopressin receptors: structure/function relationships and signal transduction in target cells. J Soc Biol. 2005;199(4):351-9.	34	PF00001	.	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.10.3	The G-protein-coupled receptor (GPCR) Family	hsa04080:Neuroactive ligand-receptor interaction; hsa04962:Vasopressin-regulated water reabsorption	R-HSA-388479:Vasopressin-like receptors; R-HSA-418555:G alpha (s) signalling events; R-HSA-432040:Vasopressin regulates renal water homeostasis via Aquaporins	.	P30518
TTZPY6J	Tyrosine-protein kinase UFO (AXL)	P30530	UFO_HUMAN	Kinase	UFO; Tyrosine-protein kinase receptor UFO; AXL oncogene	AXL	"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."	EC 2.7.10.1	5VXZ; 5U6B; 4RA0; 2C5D	MAWRCPRMGRVPLAWCLALCGWACMAPRGTQAEESPFVGNPGNITGARGLTGTLRCQLQVQGEPPEVHWLRDGQILELADSTQTQVPLGEDEQDDWIVVSQLRITSLQLSDTGQYQCLVFLGHQTFVSQPGYVGLEGLPYFLEEPEDRTVAANTPFNLSCQAQGPPEPVDLLWLQDAVPLATAPGHGPQRSLHVPGLNKTSSFSCEAHNAKGVTTSRTATITVLPQQPRNLHLVSRQPTELEVAWTPGLSGIYPLTHCTLQAVLSDDGMGIQAGEPDPPEEPLTSQASVPPHQLRLGSLHPHTPYHIRVACTSSQGPSSWTHWLPVETPEGVPLGPPENISATRNGSQAFVHWQEPRAPLQGTLLGYRLAYQGQDTPEVLMDIGLRQEVTLELQGDGSVSNLTVCVAAYTAAGDGPWSLPVPLEAWRPGQAQPVHQLVKEPSTPAFSWPWWYVLLGAVVAAACVLILALFLVHRRKKETRYGEVFEPTVERGELVVRYRVRKSYSRRTTEATLNSLGISEELKEKLRDVMVDRHKVALGKTLGEGEFGAVMEGQLNQDDSILKVAVKTMKIAICTRSELEDFLSEAVCMKEFDHPNVMRLIGVCFQGSERESFPAPVVILPFMKHGDLHSFLLYSRLGDQPVYLPTQMLVKFMADIASGMEYLSTKRFIHRDLAARNCMLNENMSVCVADFGLSKKIYNGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQPADCLDGLYALMSRCWELNPQDRPSFTELREDLENTLKALPPAQEPDEILYVNMDEGGGYPEPPGAAGGADPPTQPDPKDSCSCLTAAEVHPAGRYVLCPSTTPSPAQPADRGSPAAPGQEDGA	Successful	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. AXL/UFO subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Fibronectin type III domain; Protein tyrosine kinase	PF00041; PF07714	PF00041; fn3; PF07714; Pkinase_Tyr	.	.	hsa01521: EGFR tyrosine kinase inhibitor resistance	R-HSA-4420097:VEGFA-VEGFR2 Pathway	.	P30530
TTUPYLV	Zinc alpha-2 glycoprotein (AZGP1)	P25311	ZA2G_HUMAN	.	Zn-alpha-2-glycoprotein; Zn-alpha-2-GP; Zinc-alpha-2-glycoprotein; ZNGP1; ZAG	AZGP1	Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids.	.	3ES6; 1ZAG; 1T80; 1T7Z; 1T7Y	MVRMVPVLLSLLLLLGPAVPQENQDGRYSLTYIYTGLSKHVEDVPAFQALGSLNDLQFFRYNSKDRKSQPMGLWRQVEGMEDWKQDSQLQKAREDIFMETLKDIVEYYNDSNGSHVLQGRFGCEIENNRSSGAFWKYYYDGKDYIEFNKEIPAWVPFDPAAQITKQKWEAEPVYVQRAKAYLEEECPATLRKYLKYSKNILDRQDPPSVVVTSHQAPGEKKKLKCLAYDFYPGKIDVHWTRAGEVQEPELRGDVLHNGNGTYQSWVVVAVPPQDTAPYSCHVQHSSLAQPLVVPWEAS	Literature-reported	Modulation by interferon-gamma of zinc-alpha 2-glycoprotein gene expression in human epithelial cell lines. Anticancer Res. 1997 Sep-Oct;17(5A):3387-91.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-5223345: Miscellaneous transport and binding events	.	P25311
TTY7FKA	Beta-2-microglobulin (B2M)	P61769	B2MG_HUMAN	.	Beta-2-microglobulin	B2M	"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."	.	6MTM; 6MTL; 6MT6; 6MT5; 6MT4	MSRSVALAVLALLSLSGLEAIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM	Literature-reported	Identification of beta2-microglobulin as a potential target for ovarian cancer. Cancer Biol Ther. 2009 Dec;8(24):2323-8.	.	.	.	.	.	.	.	.	.	.	.	hsa04612: Antigen processing and presentation; hsa05163: Human cytomegalovirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection	"R-HSA-1236974: ER-Phagosome pathway; R-HSA-1236977: Endosomal/Vacuolar pathway; R-HSA-164940: Nef mediated downregulation of MHC class I complex cell surface expression; R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-2172127: DAP12 interactions; R-HSA-2424491: DAP12 signaling; R-HSA-6798695: Neutrophil degranulation; R-HSA-877300: Interferon gamma signaling; R-HSA-9637628: Modulation by Mtb of host immune system; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses; R-HSA-977225: Amyloid fiber formation; R-HSA-983170: Antigen Presentation: Folding, assembly and peptide loading of class I MHC"	.	P61769
TTJUNZF	Beta-secretase 1 (BACE1)	P56817	BACE1_HUMAN	Peptidase	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	BACE1	"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)."	EC 3.4.23.46	6FGY; 6EQM; 6EJ3; 6EJ2; 6DMI	MAQALPWLLLWMGAGVLPAHGTQHGIRLPLRSGLGGAPLGLRLPRETDEEPEEPGRRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYNIPQTDESTLMTIAYVMAAICALFMLPLCLMVCQWRCLRCLRQQHDDFADDISLLK	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	EC:3.4	Peptidase A1 family	peptidase A1 family.	3.4.23.46 	Acting on peptide bonds (peptidases)	Eukaryotic aspartyl protease	PF00026	PF00026; Asp	8.A.32.1.1	The -Amyloid Cleaving Enzyme (BACE1) Family	hsa05010:Alzheimer disease	R-HSA-977225: Amyloid fiber formation	MetaCyc:ENSG00000160610-MON	P56817
TT69DB8	Beta-site APP-cleaving enzyme 2 (BACE2)	Q9Y5Z0	BACE2_HUMAN	.	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	BACE2	"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."	EC 3.4.23.45	4BFB; 4BEL; 3ZLQ; 3ZL7; 3ZKX	MGALARALLLPLLAQWLLRAAPELAPAPFTLPLRVAAATNRVVAPTPGPGTPAERHADGLALALEPALASPAGAANFLAMVDNLQGDSGRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNTSFLVNIATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIPNVFSMQMCGAGLPVAGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARASLIPEFSDGFWTGSQLACWTNSETPWSYFPKISIYLRDENSSRSFRITILPQLYIQPMMGAGLNYECYRFGISPSTNALVIGATVMEGFYVIFDRAQKRVGFAASPCAEIAGAAVSEISGPFSTEDVASNCVPAQSLSEPILWIVSYALMSVCGAILLVLIVLLLLPFRCQRRPRDPEVVNDESSLVRHRWK	Clinical trial	BACE2 as a new diabetes target: a patent review (2010 - 2012). Expert Opin Ther Pat. 2013 May;23(5):649-63.	16	.	.	.	.	.	.	.	.	.	.	hsa05010: Alzheimer disease	.	MetaCyc:G66-33964-MON	Q9Y5Z0
TTQEAIO	Amyloid precursor protein secretase (Secretase)	Q9Y5Z0; Q9NZ42; Q96BI3; Q8WW43	BACE2_HUMAN; PEN2_HUMAN; APH1A_HUMAN; APH1B_HUMAN	.	Secretase	BACE2	"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."	.	.	MGALARALLLPLLAQWLLRAAPELAPAPFTLPLRVAAATNRVVAPTPGPGTPAERHADGLALALEPALASPAGAANFLAMVDNLQGDSGRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKGFNTSFLVNIATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIPNVFSMQMCGAGLPVAGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARASLIPEFSDGFWTGSQLACWTNSETPWSYFPKISIYLRDENSSRSFRITILPQLYIQPMMGAGLNYECYRFGISPSTNALVIGATVMEGFYVIFDRAQKRVGFAASPCAEIAGAAVSEISGPFSTEDVASNCVPAQSLSEPILWIVSYALMSVCGAILLVLIVLLLLPFRCQRRPRDPEVVNDESSLVRHRWK	Literature-reported	Therapeutic Targeting of Amyloid Precursor Protein and its Processing Enzymes for Breast Cancer Treatment. Curr Protein Pept Sci. 2018;19(9):841-849.	.	.	.	.	.	.	.	.	.	.	.	.	.	MetaCyc:G66-33964-MON	Q9Y5Z0
TT2ME4S	Transcription regulator protein BACH1 (Bach1)	O14867	BACH1_HUMAN	Basic leucine zipper bZIP	HA2303; BTB and CNC homolog 1	BACH1	"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."	.	2IHC	MSLSENSVFAYESSVHSTNVLLSLNDQRKKDVLCDVTIFVEGQRFRAHRSVLAACSSYFHSRIVGQADGELNITLPEEVTVKGFEPLIQFAYTAKLILSKENVDEVCKCVEFLSVHNIEESCFQFLKFKFLDSTADQQECPRKKCFSSHCQKTDLKLSLLDQRDLETDEVEEFLENKNVQTPQCKLRRYQGNAKASPPLQDSASQTYESMCLEKDAALALPSLCPKYRKFQKAFGTDRVRTGESSVKDIHASVQPNERSENECLGGVPECRDLQVMLKCDESKLAMEPEETKKDPASQCPTEKSEVTPFPHNSSIDPHGLYSLSLLHTYDQYGDLNFAGMQNTTVLTEKPLSGTDVQEKTFGESQDLPLKSDLGTREDSSVASSDRSSVEREVAEHLAKGFWSDICSTDTPCQMQLSPAVAKDGSEQISQKRSECPWLGIRISESPEPGQRTFTTLSSVNCPFISTLSTEGCSSNLEIGNDDYVSEPQQEPCPYACVISLGDDSETDTEGDSESCSAREQECEVKLPFNAQRIISLSRNDFQSLLKMHKLTPEQLDCIHDIRRRSKNRIAAQRCRKRKLDCIQNLESEIEKLQSEKESLLKERDHILSTLGETKQNLTGLCQKVCKEAALSQEQIQILAKYSAADCPLSFLISEKDKSTPDGELALPSIFSLSDRPPAVLPPCARGNSEPGYARGQESQQMSTATSEQAGPAEQCRQSGGISDFCQQMTDKCTTDE	Patented-recorded	"BACH1, the master regulator gene: A novel candidate target for cancer therapy. Gene. 2016 Aug 15;588(1):30-7."	.	bZIP	BZIP family	bZIP family. CNC subfamily.	.	.	BTB/POZ domain; bZIP Maf transcription factor	PF00651; PF03131	PF00651; BTB; PF03131; bZIP_Maf	.	.	.	R-HSA-9707587: Regulation of HMOX1 expression and activity; R-HSA-9707616: Heme signaling; R-HSA-9708530: Regulation of BACH1 activity; R-HSA-9759194: Nuclear events mediated by NFE2L2	.	O14867
TT8RHGB	Bacterial Pyruvate decarboxylase (Bact aceE)	P0AFG8	ODP1_ECOLI	Aldehyde/oxo donor oxidoreductase	aceE; Pyruvate decarboxylase E1 component	Bact aceE	"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."	.	2QTC; 2QTA; 2IEA; 2G67; 2G28	MSERFPNDVDPIETRDWLQAIESVIREEGVERAQYLIDQLLAEARKGGVNVAAGTGISNYINTIPVEEQPEYPGNLELERRIRSAIRWNAIMTVLRASKKDLELGGHMASFQSSATIYDVCFNHFFRARNEQDGGDLVYFQGHISPGVYARAFLEGRLTQEQLDNFRQEVHGNGLSSYPHPKLMPEFWQFPTVSMGLGPIGAIYQAKFLKYLEHRGLKDTSKQTVYAFLGDGEMDEPESKGAITIATREKLDNLVFVINCNLQRLDGPVTGNGKIINELEGIFEGAGWNVIKVMWGSRWDELLRKDTSGKLIQLMNETVDGDYQTFKSKDGAYVREHFFGKYPETAALVADWTDEQIWALNRGGHDPKKIYAAFKKAQETKGKATVILAHTIKGYGMGDAAEGKNIAHQVKKMNMDGVRHIRDRFNVPVSDADIEKLPYITFPEGSEEHTYLHAQRQKLHGYLPSRQPNFTEKLELPSLQDFGALLEEQSKEISTTIAFVRALNVMLKNKSIKDRLVPIIADEARTFGMEGLFRQIGIYSPNGQQYTPQDREQVAYYKEDEKGQILQEGINELGAGCSWLAAATSYSTNNLPMIPFYIYYSMFGFQRIGDLCWAAGDQQARGFLIGGTSGRTTLNGEGLQHEDGHSHIQSLTIPNCISYDPAYAYEVAVIMHDGLERMYGEKQENVYYYITTLNENYHMPAMPEGAEEGIRKGIYKLETIEGSKGKVQLLGSGSILRHVREAAEILAKDYGVGSDVYSVTSFTELARDGQDCERWNMLHPLETPRVPYIAQVMNDAPAVASTDYMKLFAEQVRTYVPADDYRVLGTDGFGRSDSRENLRHHFEVDASYVVVAALGELAKRGEIDKKVVADAIAKFNIDADKVNPRLA	Successful	Vitamins and cofactors: highlights of ESBOC 2009. Nat Chem Biol. 2009 Aug;5(8):530-3.	34	.	.	.	.	.	.	.	.	.	.	ecj00010: Glycolysis / Gluconeogenesis; ecj00020: Citrate cycle (TCA cycle); ecj00620: Pyruvate metabolism; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01120: Microbial metabolism in diverse environments; ecj01200: Carbon metabolism	.	EcoCyc:E1P-MON; MetaCyc:E1P-MON	P0AFG8
TTOR5EH	Bacterial Holo-ACP synthase (Bact acpS)	P24224	ACPS_ECOLI	Kinase	acpS; Holo-[acyl-carrier protein] synthase; 4'-phosphopantetheinyl transferase acpS	Bact acpS	Transfers the 4'-phosphopantetheine moiety from coenzyme A to the 'Ser-36' of acyl-carrier-protein.	.	5XUH; 5XU7; 5VCB; 5VBX	MAILGLGTDIVEIARIEAVIARSGDRLARRVLSDNEWAIWKTHHQPVRFLAKRFAVKEAAAKAFGTGIRNGLAFNQFEVFNDELGKPRLRLWGEALKLAEKLGVANMHVTLADERHYACATVIIES	Literature-reported	Lipid biosynthesis as a target for antibacterial agents. Prog Lipid Res. 2001 Nov;40(6):467-97.	.	.	.	.	.	.	.	.	.	.	.	ecj00770: Pantothenate and CoA biosynthesis; ecj01100: Metabolic pathways	.	EcoCyc:HOLO-ACP-SYNTH-MON; MetaCyc:HOLO-ACP-SYNTH-MON	P24224
TTB30PF	Bacterial Phosphoshikimate1-carboxyvinyltransferase (Bact aroA)	P0A6D3	AROA_ECOLI	Alkyl aryl transferase	aroA of Escherichia coli; EPSPS of Escherichia coli; EPSP synthase of Escherichia coli; 5-enolpyruvylshikimate-3-phosphate synthase of Escherichia coli	Bact aroA	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.	EC 2.5.1.19	3FK1; 3FK0; 3FJZ; 3FJX; 2QFU	MESLTLQPIARVDGTINLPGSKSVSNRALLLAALAHGKTVLTNLLDSDDVRHMLNALTALGVSYTLSADRTRCEIIGNGGPLHAEGALELFLGNAGTAMRPLAAALCLGSNDIVLTGEPRMKERPIGHLVDALRLGGAKITYLEQENYPPLRLQGGFTGGNVDVDGSVSSQFLTALLMTAPLAPEDTVIRIKGDLVSKPYIDITLNLMKTFGVEIENQHYQQFVVKGGQSYQSPGTYLVEGDASSASYFLAAAAIKGGTVKVTGIGRNSMQGDIRFADVLEKMGATICWGDDYISCTRGELNAIDMDMNHIPDAAMTIATAALFAKGTTTLRNIYNWRVKETDRLFAMATELRKVGAEVEEGHDYIRITPPEKLNFAEIATYNDHRMAMCFSLVALSDTPVTILDPKCTAKTFPDYFEQLARISQAA	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	"ecj00400: Phenylalanine, tyrosine and tryptophan biosynthesis; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01230: Biosynthesis of amino acids"	.	EcoCyc:AROA-MON; MetaCyc:AROA-MON	P0A6D3
TTPS7KA	Bacterial Dehydroquinate synthase (Bact aroB)	P07639	AROB_ECOLI	Alpha-carbonic anhydrase	DHQS; 3-dehydroquinate synthase	Bact aroB	Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).	.	.	MERIVVTLGERSYPITIASGLFNEPASFLPLKSGEQVMLVTNETLAPLYLDKVRGVLEQAGVNVDSVILPDGEQYKSLAVLDTVFTALLQKPHGRDTTLVALGGGVVGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVVDLDCLKTLPPRELASGLAEVIKYGIILDGAFFNWLEENLDALLRLDGPAMAYCIRRCCELKAEVVAADERETGLRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGMVMAARTSERLGQFSSAETQRIITLLKRAGLPVNGPREMSAQAYLPHMLRDKKVLAGEMRLILPLAIGKSEVRSGVSHELVLNAIADCQSA	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	"ecj00400: Phenylalanine, tyrosine and tryptophan biosynthesis; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01230: Biosynthesis of amino acids"	.	EcoCyc:AROB-MON; MetaCyc:AROB-MON	P07639
TTQAOZR	Bacterial Chorismate synthase (Bact aroC)	P12008	AROC_ECOLI	Alpha-carbonic anhydrase	aroC; Chorismate synthase; CS; 5enolpyruvylshikimate3phosphate phospholyase; 5-enolpyruvylshikimate-3-phosphate phospholyase	Bact aroC	"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."	EC 4.2.3.5	.	MAGNTIGQLFRVTTFGESHGLALGCIVDGVPPGIPLTEADLQHDLDRRRPGTSRYTTQRREPDQVKILSGVFEGVTTGTSIGLLIENTDQRSQDYSAIKDVFRPGHADYTYEQKYGLRDYRGGGRSSARETAMRVAAGAIAKKYLAEKFGIEIRGCLTQMGDIPLDIKDWSQVEQNPFFCPDPDKIDALDELMRALKKEGDSIGAKVTVVASGVPAGLGEPVFDRLDADIAHALMSINAVKGVEIGDGFDVVALRGSQNRDEITKDGFQSNHAGGILGGISSGQQIIAHMALKPTSSITVPGRTINRFGEEVEMITKGRHDPCVGIRAVPIAEAMLAIVLMDHLLRQRAQNADVKTDIPRW	Literature-reported	"US patent application no. 2009,0048,155, Methods for preventing and treating tissue injury and sepsis associated with yersinia pestis infection."	2	.	.	.	.	.	.	.	.	.	.	"ecj00400: Phenylalanine, tyrosine and tryptophan biosynthesis; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01230: Biosynthesis of amino acids"	.	EcoCyc:AROC-MON; MetaCyc:AROC-MON	P12008
TTQWGU9	Bacterial Aspartate-semialdehyde dehydrogenase (Bact asd2)	P23247	DHAS2_VIBCH	Aldehyde/oxo donor oxidoreductase	asd2; L-Aspartate-beta-semialdehyde dehydrogenase; ASADH; ASA dehydrogenase	Bact asd2	Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L- aspartyl-4-phosphate.	.	2R00; 2QZ9	MSQQFNVAIFGATGAVGETMLEVLQEREFPVDELFLLASERSEGKTYRFNGKTVRVQNVEEFDWSQVHIALFSAGGELSAKWAPIAAEAGVVVIDNTSHFRYDYDIPLVVPEVNPEAIAEFRNRNIIANPNCSTIQMLVALKPIYDAVGIERINVTTYQSVSGAGKAGIDELAGQTAKLLNGYPAETNTFSQQIAFNCIPQIDQFMDNGYTKEEMKMVWETQKIFNDPSIMVNPTCVRVPVFYGHAEAVHVETRAPIDAEQVMDMLEQTDGIELFRGADFPTQVRDAGGKDHVLVGRVRNDISHHSGINLWVVADNVRKGAATNAVQIAELLVRDYF	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	"vch00260: Glycine, serine and threonine metabolism; vch00261: Monobactam biosynthesis; vch00270: Cysteine and methionine metabolism; vch00300: Lysine biosynthesis; vch01100: Metabolic pathways; vch01110: Biosynthesis of secondary metabolites; vch01120: Microbial metabolism in diverse environments; vch01210: 2-Oxocarboxylic acid metabolism; vch01230: Biosynthesis of amino acids"	.	.	P23247
TTMEJZ5	Bacterial Bacitracin transport ATP-binding bcrA (Bact bcrA)	P42332	BCRA_BACLI	ABC transporter	BCRA	Bact bcrA	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.	.	.	MSTIIKTTDLTKMYGSQKSVDHLNINVKQGDIYGFLGRNGAGKTTTIRMLLGLIKPTSGQIEIFGENFFKNKKEILRRIGSIVEVPGFYANLTARENLLINAKIIGIHKKNAIDEVLEIVGLQHETKKLVGKFSLGMKQRLGIARALLHYPELLILDEPTNGLDPIGIKEMRRLIHSLAKERNITIFISSHILSEIEQLVDHVGIIHEGKLLEEIPFDHLKKRNRKYLEFQLSDQNKAVVLMEQHFDIHDYEVHQDGIIRVYSHLGQQGKLNKLFVENGIDVLKITMSEDSLEDYFVKLIGGGTIG	Literature-reported	Identification of an immunodominant drug efflux pump in Burkholderia cepacia. J Antimicrob Chemother. 2002 Apr;49(4):619-24.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P42332
TTQ5J3T	Bacterial Betaine aldehyde dehydrogenase (Bact betB)	P17445	BETB_ECOLI	Aldehyde/oxo donor oxidoreductase	betB; BADH	Bact betB	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.	EC 1.2.1.8	.	MSRMAEQQLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWASMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGVGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFDPQTNFGPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKGDGFDNGAWVAPTVFTDCSDDMTIVREEIFGPVMSILTYESEDEVIRRANDTDYGLAAGIVTADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQVEMAKFQSIF	Literature-reported	Inactivation of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves by disulfiram. Chem Biol Interact. 2003 Feb 1;143-144:149-58.	.	.	.	.	.	.	.	.	.	.	.	"ecj00260: Glycine, serine and threonine metabolism; ecj01100: Metabolic pathways"	.	EcoCyc:BADH-MON; MetaCyc:BADH-MON	P17445
TTB52WU	Bacterial Botulinum toxin A (Bact botA)	P10845	BXA1_CLOBO	Peptidase	botA	Bact botA	"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."	.	6MHJ; 6DKK; 5VGX; 5VGV; 5V8U	MPFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLFFSPSEDNFTNDLNKGEEITSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKYELDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVSTTDKIADITIIIPYIGPALNIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRNEKWDEVYKYIVTNWLAKVNTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMININKFLNQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLLSTFTEYIKNIINTSILNLRYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFSTSFWIRIPKYFNSISLNNEYTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNRLNNSKIYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGDYLQYDKPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGTKFIIKKYASGNKDNIVRNNDRVYINVVVKNKEYRLATNASQAGVEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVASNWYNRQIERSSRTLGCSWEFIPVDDGWGERPL	Clinical trial	"Clinical pipeline report, company report or official report of Revance Therapeutics."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	P0DPI0
TTPL9SG	Bacterial Botulinum toxin B (Bact botB)	P10844	BXB_CLOBO	Peptidase	botB; Botulinum neurotoxin type B; Botulinum neurotoxin B heavy chain; BontoxilysinB; BoNT/B	Bact botB	"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."	.	6G5K; 6G5G; 6G5F; 5VMR; 5VID	MPVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITDRIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNTNDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGDRRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIFGPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVSVFNNVQENKGASIFNRRGYFSDPALILMHELIHVLHGLYGIKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIITPSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIYKNKFKDKYKFVEDSEGKYSIDVESFDKLYKSLMFGFTETNIAENYKIKTRASYFSDSLPPVKIKNLLDNEIYTIEEGFNISDKDMEKEYRGQNKAINKQAYEEISKEHLAVYKIQMCKSVKAPGICIDVDNEDLFFIADKNSFSDDLSKNERIEYNTQSNYIENDFPINELILDTDLISKIELPSENTESLTDFNVDVPVYEKQPAIKKIFTDENTIFQYLYSQTFPLDIRDISLTSSFDDALLFSNKVYSFFSMDYIKTANKVVEAGLFAGWVKQIVNDFVIEANKSNTMDKIADISLIVPYIGLALNVGNETAKGNFENAFEIAGASILLEFIPELLIPVVGAFLLESYIDNKNKIIKTIDNALTKRNEKWSDMYGLIVAQWLSTVNTQFYTIKEGMYKALNYQAQALEEIIKYRYNIYSEKEKSNINIDFNDINSKLNEGINQAIDNINNFINGCSVSYLMKKMIPLAVEKLLDFDNTLKKNLLNYIDENKLYLIGSAEYEKSKVNKYLKTIMPFDLSIYTNDTILIEMFNKYNSEILNNIILNLRYKDNNLIDLSGYGAKVEVYDGVELNDKNQFKLTSSANSKIRVTQNQNIIFNSVFLDFSVSFWIRIPKYKNDGIQNYIHNEYTIINCMKNNSGWKISIRGNRIIWTLIDINGKTKSVFFEYNIREDISEYINRWFFVTITNNLNNAKIYINGKLESNTDIKDIREVIANGEIIFKLDGDIDRTQFIWMKYFSIFNTELSQSNIEERYKIQSYSEYLKDFWGNPLMYNKEYYMFNAGNKNSYIKLKKDSPVGEILTRSKYNQNSKYINYRDLYIGEKFIIRRKSNSQSINDDIVRKEDYIYLDFFNLNQEWRVYTYKYFKKEEEKLFLAPISDSDEFYNTIQIKEYDEQPTYSCQLLFKKDEESTDEIGLIGIHRFYESGIVFEEYKDYFCISKWYLKEVKRKPYNLKLGCNWQFIPKDEGWTE	Literature-reported	Botulinum toxin type B for cervical dystonia. Cochrane Database Syst Rev. 2016 May 13;(5):CD004315.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-5250958: Toxicity of botulinum toxin type B (botB)	.	P10844
TT61VIL	Bacterial Cycloinulo-oligosaccharide fructanotransferase (Bact cft)	Q9F0I5	Q9F0I5_PAEMA	.	Cycloinulo-oligosaccharide fructanotransferase	Bact cft	Converts inulin into cyclooligosaccharides (cyclofructans) consisting of 6 to 8 molecules of (21)linked cyclic Dfructofuranose through intramolecular transfructosylation.	.	.	MRKVKRGKCWISGMVIWAMVLQLVVPGISVASENRTVAGETLIPKNDVKSSVTDAIYQIKNIPQNDMGLSVTDSVYQIRNPGFETGDLTGWTVIKGDAFGPNSVTDETTWWAEKIPYNQEGAYHLNGWKYDESATGVLRSSTFELGGSGGISFKLGGAKNPDKVFINIVEVDTGQVIARYGNSAFADVGFPDPAQGMRLANMVQYKADLSTQLGKKLYVEVVDNATSDWGVIFADAFSMYHESEPAEGIVATDIKPDFKRYEIDNPSFETGNLDGWTVEEDAFEVTDEAHASKEGNFYAKSSLQGKGSITSNTFTLQGTGTINFTVLDILKPENAYVALFDANSNTLLMKTGNVSANEKISWKVQEHYNKKLYVKVVDHSNEASIAVDSFQASDRGTIFYLNLDEGAGKKALEKVHNLRHDVNYVFNNARYMASKDPRWTPRGIKGGALLFDGSSNYIEVNANVTVPVSDALTIEAWVAPRSYEWGDGNKLSAIVNQSDQDKAEGFSLGMYRHGTWSMQVGIGGQWIQVWVKDHPLEKYKWNYVAATFSKEDGKIKLYLNGEEVASQATPVNVPITPSTESLIIGKNNKPVELAGVFSFNMFSGLLDEVKLHNKALTNQEILAGYESVKALHGGSIPKIPNADIDEDPSVFDGDQHRPQYHAMPPQNWMNEAHAPIYYNGKYHLFYQHNPQGPFWHQIHWGHWVSDDMVNWENVRPALAPEAGTLDPDGTWSGSAAYDRNGNPVLFYTAGNDSLSPNQRTGLATPADLSDPYLEKWEKYPKPVTEQNGKGIHNEFRDPFVWYDKEVDKWYQLVTSGLPDFSSGTALVYVSDDMYNWKYKGPLYVSDRIRYPELGTVWELPVLLPLGTDSTGKQKYIFMINPHEKPEHVPPANDVQRDVEVFYWIGTWDRDNFKFIPDQEAPSKMDVGDGYLTAESGLVTPDGRTVVFSMVQNVRTPQAEYQSGWAHNLSLPVSLSLDKYDKLHIEPIKELQSLRGEKWVDFSDKNLESANQLIKNVKGDMLEIVMEIDPREAQKFGLKVRRSEKGQEETLIYYDKKNGTFNVDRTKSSIDPDVRVDGIQGGYVDLEGENLKLHIFLDRSVIEAFANYKKKLTTRVYVGRYDSLGLQIWADGDINIKSMQVWDMNALTGKPAAPVYVPDKWDNSVYKDITELPNHDFATGDLTGWMTEGDAFQNVHVTNTQFFWDNIFFNPSHKIPGSYHLWGFNEQAGGDSLTGALRSQNFVLGGNGKINFLISGGRDIDRLYVALVRASDDKELFKETATNYEEYQRKIWDATDYIGEELYIKVVDHSKGGFGHINVDDFNVPVQVKKKTNN	Literature-reported	Identification and characterization of a novel inulin binding module (IBM) from the CFTase of Bacillus macerans CFC1. FEMS Microbiol Lett. 2004 May 1;234(1):105-10.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTTRNH6	Bacterial ATP-dependent Clp proteolytic protease (Bact clpP)	Q5GS83	CLPP_WOLTR	Peptidase	clpP; Bact Endopeptidase Clp	Bact clpP	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.	EC 3.4.21.92	.	MTLIPIVIEQTSRGERAYDIYSRLVKERIIFVTGPVEDNMASVIVAQLLFLESENPDKDIYMYINSPGGVVTAGLSIYDTMQYIKPDVSTLCIGQAASMGSLLLAAGTEGKRYSLPHSRIMIHQPSGGYQGQATDIEIHANEILRVKRKLNQIYEKHTGNSLKKIEGMMERDKFMDPEEARRIGLIDRVIAERKDIKVENIKVEQKVG	Literature-reported	The ATP-Dependent Protease ClpP Inhibits Biofilm Formation by Regulating Agr and Cell Wall Hydrolase Sle1 in Staphylococcus aureus. Front Cell Infect Microbiol. 2017 May 15;7:181.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q5GS83
TTSEOPJ	Bacterial Pantothenate kinase (Bact coaA)	P0A6I3	COAA_ECOLI	Kinase	Rts protein; Pantothenic acid kinase; Pantothenate kinase	Bact coaA	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.	EC 2.7.1.33	1SQ5; 1ESN; 1ESM	MSIKEQTLMTPYLQFDRNQWAALRDSVPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHAVEEVRLRK	Literature-reported	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	0	.	.	.	.	.	.	.	.	.	.	ecj00770: Pantothenate and CoA biosynthesis; ecj01100: Metabolic pathways; ecj01240: Biosynthesis of cofactors	.	EcoCyc:PANTOTHENATE-KIN-MON; MetaCyc:PANTOTHENATE-KIN-MON	P0A6I3
TTBE0LS	Bacterial O-acetylserine sulfhydrylase A (Bact cysK)	P0ABK5	CYSK_ECOLI	Alkyl aryl transferase	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	Bact cysK	"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."	.	5J5V; 5J43	MSKIFEDNSLTIGHTPLVRLNRIGNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLKPGVELVEPTSGNTGIALAYVAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGAKGMKGAIQKAEEIVASNPEKYLLLQQFSNPANPEIHEKTTGPEIWEDTDGQVDVFIAGVGTGGTLTGVSRYIKGTKGKTDLISVAVEPTDSPVIAQALAGEEIKPGPHKIQGIGAGFIPANLDLKLVDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDESFTNKNIVVILPSSGERYLSTALFADLFTEKELQQ	Literature-reported	"Isozyme-specific ligands for O-acetylserine sulfhydrylase, a novel antibiotic target. PLoS One. 2013 Oct 22;8(10):e77558."	.	.	.	.	.	.	.	.	.	.	.	ecj00270: Cysteine and methionine metabolism; ecj00920: Sulfur metabolism; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01120: Microbial metabolism in diverse environments; ecj01200: Carbon metabolism; ecj01230: Biosynthesis of amino acids	.	EcoCyc:ACSERLYA-MON; MetaCyc:ACSERLYA-MON	P0ABK5
TTTP8L7	Bacterial O-acetylserine sulfhydrylase B (Bact cysM)	P16703	CYSM_ECOLI	Alkyl aryl transferase	OAS-TL B; O-acetylserine sulfhydrylase B; O-acetylserine (thiol)-lyase B; Cysteine synthase B; CSase B	Bact cysM	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.	.	2V03; 2BHT; 2BHS	MSTLEQTIGNTPLVKLQRMGPDNGSEVWLKLEGNNPAGSVKDRAALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGYRMKLLMPDNMSQERRAAMRAYGAELILVTKEQGMEGARDLALEMANRGEGKLLDQFNNPDNPYAHYTTTGPEIWQQTGGRITHFVSSMGTTGTITGVSRFMREQSKPVTIVGLQPEEGSSIPGIRRWPTEYLPGIFNASLVDEVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAGALRVAKANPDAVVVAIICDRGDRYLSTGVFGEEHFSQGAGI	Literature-reported	"Isozyme-specific ligands for O-acetylserine sulfhydrylase, a novel antibiotic target. PLoS One. 2013 Oct 22;8(10):e77558."	.	.	.	.	.	.	.	.	.	.	.	ecj00270: Cysteine and methionine metabolism; ecj01100: Metabolic pathways; ecj01230: Biosynthesis of amino acids	.	EcoCyc:ACSERLYB-MON; MetaCyc:ACSERLYB-MON	P16703
TTV8DM2	Bacterial Dihydrofolate reductase (Bact DHFR)	P0ABQ4	DYR_ECOLI	.	Bact Dihydrofolate reductase	Bact DHFR	"Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis."	EC 1.5.1.3	7DFR; 6MTH; 6MT8; 6MR9; 6DFR	MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR	Clinical trial	Iclaprim: a novel dihydrofolate reductase inhibitor for skin and soft tissue infections.Future Microbiol.2009 Mar;4(2):131-44.	25	.	.	.	.	.	.	.	.	.	.	ecj00670: One carbon pool by folate; ecj00790: Folate biosynthesis; ecj01100: Metabolic pathways; ecj01240: Biosynthesis of cofactors	.	EcoCyc:DIHYDROFOLATEREDUCT-MON; MetaCyc:DIHYDROFOLATEREDUCT-MON	P0ABQ4
TTPUDAR	Bacterial Initiator protein DnaA (Bact dnaA)	P03004	DNAA_ECOLI	.	Chromosomal replication initiator protein DnaA	Bact dnaA	"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."	.	2E0G; 1J1V	MSLSLWQQCLARLQDELPATEFSMWIRPLQAELSDNTLALYAPNRFVLDWVRDKYLNNINGLLTSFCGADAPQLRFEVGTKPVTQTPQAAVTSNVAAPAQVAQTQPQRAAPSTRSGWDNVPAPAEPTYRSNVNVKHTFDNFVEGKSNQLARAAARQVADNPGGAYNPLFLYGGTGLGKTHLLHAVGNGIMARKPNAKVVYMHSERFVQDMVKALQNNAIEEFKRYYRSVDALLIDDIQFFANKERSQEEFFHTFNALLEGNQQIILTSDRYPKEINGVEDRLKSRFGWGLTVAIEPPELETRVAILMKKADENDIRLPGEVAFFIAKRLRSNVRELEGALNRVIANANFTGRAITIDFVREALRDLLALQEKLVTIDNIQKTVAEYYKIKVADLLSKRRSRSVARPRQMAMALAKELTNHSLPEIGDAFGGRDHTTVLHACRKIEQLREESHDIKEDFSNLIRTLSS	Literature-reported	Regulatory dynamics in the ternary DnaA complex for initiation of chromosomal replication in Escherichia coli. Nucleic Acids Res. 2017 Dec 1;45(21):12354-12373.	.	.	.	.	.	.	.	.	.	.	.	ecj02020: Two-component system	.	EcoCyc:PD03831	P03004
TTY8KJS	Bacterial Deoxyuridine triphosphate nucleotidohydrolase (Bact dut)	P06968	DUT_ECOLI	Acid anhydrides hydrolase	Deoxyuridine triphosphate nucleotidohydrolase; Deoxyuridine 5'-triphosphate nucleotidohydrolase; DUTPase; DUTP pyrophosphatase of Escherichia coli; Bact dut	Bact dut	"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."	.	2HRM; 2HR6; 1SYL; 1SEH; 1RNJ	MMKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLNDAVELAPGDTTLVPTGLAIHIADPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	ecj00240: Pyrimidine metabolism; ecj01100: Metabolic pathways; ecj01232: Nucleotide metabolism	.	EcoCyc:DUTP-PYROP-MON; MetaCyc:DUTP-PYROP-MON	P06968
TTVL6MZ	Bacterial Elongation factor Tu (Bact EFTu)	P0CE47	EFTU1_ECOLI	GTP-binding elongation factor family	tufA; P43; Elongation factor Tu 1; EFTu 1	Bact EFTu	May play an important regulatory rolein cell growth and in the bacterial response to nutrient deprivation.	.	5UYQ; 5UYP; 5UYN; 5UYM; 5UYL	MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG	Literature-reported	"In vitro and in vivo activities of novel, semisynthetic thiopeptide inhibitors of bacterial elongation factor Tu. Antimicrob Agents Chemother. 2011 Nov;55(11):5277-83."	.	.	.	.	.	.	.	.	.	.	.	.	.	EcoCyc:EG11036-MON	P0CE47
TTLUBN0	Bacterial RNA endonuclease (Bact endA)	P25736	END1_ECOLI	Endodeoxyribonucleases	endA; Endonuclease I; Endo I	Bact endA	Has double-strand break activity.	EC 3.1.21.1	.	MYRYLSIAAVVLSAAFSGPALAEGINSFSQAKAAAVKVHADAPGTFYCGCKINWQGKKGVVDLQSCGYQVRKNENRASRVEWEHVVPAWQFGHQRQCWQDGGRKNCAKDPVYRKMESDMHNLQPSVGEVNGDRGNFMYSQWNGGEGQYGQCAMKVDFKEKAAEPPARARGAIARTYFYMRDQYNLTLSRQQTQLFNAWNKMYPVTDWECERDERIAKVQGNHNPYVQRACQARKS	Literature-reported	Influenza chemotherapy: a review of the present state of art and of new drugs in development. Arch Virol. 2000;145(11):2233-48.	.	.	.	.	.	.	.	.	.	.	.	.	.	EcoCyc:EG11336-MON; MetaCyc:EG11336-MON	P25736
TTO3MV6	Bacterial GTP-binding protein YihA (Bact engB)	P0A6P7	ENGB_ECOLI	.	engB; Probable GTP-binding protein engB	Bact engB	"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."	.	1PUI	MTNLNYQQTHFVMSAPDIRHLPSDTGIEVAFAGRSNAGKSSALNTLTNQKSLARTSKTPGRTQLINLFEVADGKRLVDLPGYGYAEVPEEMKRKWQRALGEYLEKRQSLQGLVVLMDIRHPLKDLDQQMIEWAVDSNIAVLVLLTKADKLASGARKAQLNMVREAVLAFNGDVQVETFSSLKKQGVDKLRQKLDTWFSEMQPVEETQDGE	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	EcoCyc:EG11203-MON	P0A6P7
TT0O4QL	Bacterial Beta-ketoacyl-ACP synthase I (Bact fabB)	P0A954	FABB_ECOL6	Acyltransferase	fabB; KAS I; Condensing enzyme FabB; 3-oxoacyl-[acyl-carrier-protein] synthase I	Bact fabB	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.	EC 2.3.1.41	.	MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKLDTTGLIDRKVVRFMSDASIYAFLSMEQAIADAGLSPEAYQNNPRVGLIAGSGGGSPRFQVFGADAMRGPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEFDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTPIDYLNSHGTSTPVGDVKELAAIREVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINIEELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLVMRKLKD	Literature-reported	Therapeutic target database update 2012: a resource for facilitating target-oriented drug discovery. Nucleic Acids Res. 2012 Jan;40(Database issue):D1128-36.	0	.	.	.	.	.	.	.	.	.	.	ecc00061: Fatty acid biosynthesis; ecc00780: Biotin metabolism; ecc01100: Metabolic pathways; ecc01212: Fatty acid metabolism; ecc01240: Biosynthesis of cofactors	.	ECOL199310:C2869-MON	P0A954
TTRFV0W	Bacterial Oxoacyl-[acyl-carrier-protein] synthase II (Bact fabF)	P0AAI5	FABF_ECOLI	Acyltransferase	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	Bact fabF	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.	EC 2.3.1.179	3I8P; 3HO9; 3HO2; 3HNZ; 3G11	MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNGSLIFKKI	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	ecj00061: Fatty acid biosynthesis; ecj00780: Biotin metabolism; ecj01100: Metabolic pathways; ecj01212: Fatty acid metabolism; ecj01240: Biosynthesis of cofactors	.	EcoCyc:3-OXOACYL-ACP-SYNTHII-MON; MetaCyc:3-OXOACYL-ACP-SYNTHII-MON	P0AAI5
TTRVTMX	Bacterial Beta-ketoacyl-ACP synthase III (Bact fabH)	P0A6R0	FABH_ECOLI	Acyltransferase	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	Bact fabH	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.	EC 2.3.1.180	5BNS; 5BNR; 5BNM; 4Z8D; 3IL9	MYTKIIGTGSYLPEQVRTNADLEKMVDTSDEWIVTRTGIRERHIAAPNETVSTMGFEAATRAIEMAGIEKDQIGLIVVATTSATHAFPSAACQIQSMLGIKGCPAFDVAAACAGFTYALSVADQYVKSGAVKYALVVGSDVLARTCDPTDRGTIIIFGDGAGAAVLAASEEPGIISTHLHADGSYGELLTLPNADRVNPENSIHLTMAGNEVFKVAVTELAHIVDETLAANNLDRSQLDWLVPHQANLRIISATAKKLGMSMDNVVVTLDRHGNTSAASVPCALDEAVRDGRIKPGQLVLLEAFGGGFTWGSALVRF	Literature-reported	The apicoplast as an antimalarial drug target. Drug Resist Updat. 2001 Jun;4(3):145-51.	0	.	.	.	.	.	.	.	.	.	.	ecj00061: Fatty acid biosynthesis; ecj01100: Metabolic pathways; ecj01212: Fatty acid metabolism	.	EcoCyc:FABH-MON; MetaCyc:FABH-MON	P0A6R0
TTFKXOM	Bacterial NADH-dependent enoyl-ACP reductase (Bact fabI)	P0AEK4	FABI_ECOLI	Short-chain dehydrogenases reductase	Enoyl[acylcarrierprotein] reductase [NADH] FabI; ENR of Mycobacterium tuberculosis	Bact fabI	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.	.	5CG2; 5CG1; 5CFZ; 4JX8; 4JQC	MGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMNELELK	Literature-reported	The MUT056399 inhibitor of FabI is a new antistaphylococcal compound. Antimicrob Agents Chemother. 2011 Oct;55(10):4692-7.	2.1	.	.	.	.	.	.	.	.	.	.	ecj00061: Fatty acid biosynthesis; ecj00780: Biotin metabolism; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01212: Fatty acid metabolism; ecj01240: Biosynthesis of cofactors	.	EcoCyc:ENOYL-ACP-REDUCT-NADH-MON; MetaCyc:ENOYL-ACP-REDUCT-NADH-MON	P0AEK4
TTCH81V	Bacterial NADH-dependent enoyl-ACP reductase 1 (Bact fabI1)	P58380	FABI1_RHIME	CH-CH donor oxidoreductase	NADH-dependent enoyl-ACP reductase 1; Enoyl-[acyl-carrier-protein] reductase [NADH] 1	Bact fabI1	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.	.	.	MAQASGLMNGKRGVIMGVANNRSIAWGIAKALAEAGAEIALTWQGDALKKRVEPLAQELGAFMAGHCDVTDLATIDAVFSALEEKWGKIDFVVHAIAFSDKDELTGRYLDTSRDNFARTMDISVYSFTAVAARADRVMNDGGSILTLTYYGAEKVMPHYNVMGVAKAALEASVRYLAVDLGNRGIRVNAISAGPIKTLAASGIGDFRYILKWNEYNAPLKRTVSIEEVGNSALYLLSDLSSGVTGEVHHVDSGYHTVGMKAVDAPDISVLKD	Literature-reported	Lipid biosynthesis as a target for antibacterial agents. Prog Lipid Res. 2001 Nov;40(6):467-97.	0	.	.	.	.	.	.	.	.	.	.	sme00061:Fatty acid biosynthesis; sme00780:Biotin metabolism; sme01100:Metabolic pathways; sme01212:Fatty acid metabolism	.	.	P58380
TT283NK	Bacterial NADH-dependent enoyl-ACP reductase 2 (Bact fabI2)	P58381	FABI2_RHIME	CH-CH donor oxidoreductase	NADH-dependent enoyl-ACP reductase 2; Enoyl-[acyl-carrier-protein] reductase [NADH] 2	Bact fabI2	"Identified as the FabI protein, which is the target of a group of antibacterial compounds, the diazaborines."	.	.	MNGLMNGKRGLIMGVANSHSIAWGIAKSLAAQGAELAFTYQGEALGKRVKPLAAEVNSDFLLPCDVEDIGSVDAVVDAIKERWGKLDFVVHAIGFSDKNELKGLYADTTRDNFSRTMVISCFSFTEIAKRAAELMSEGGTMLTLTYGGSMRVMPNYNVMGVAKAALEASVRYLAADYGSRGIRVNAISAGPIRTLAGAGISDARAMLSWQQKNSPLRRTVTIEDVGSSALYLLSDLSRGVTGEIHYVDSGYNITSMPTLEALRVADAD	Literature-reported	Lipid biosynthesis as a target for antibacterial agents. Prog Lipid Res. 2001 Nov;40(6):467-97.	0	.	.	.	.	.	.	.	.	.	.	sme00061:Fatty acid biosynthesis; sme00780:Biotin metabolism; sme01100:Metabolic pathways; sme01212:Fatty acid metabolism	.	.	P58381
TTTCRU2	Bacterial Fimbrin D-mannose adhesin (Bact FimH)	P08191	FIMH_ECOLI	.	fimH; b4320; Type 1 fimbrin D-mannose specific adhesin; Protein FimH; JW4283	Bact FimH	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).	.	6GTY; 6GTX; 6G2S; 6G2R; 6.00E+15	MKRVITLFAVLLMGWSVNAWSFACKTANGTAIPIGGGSANVYVNLAPVVNVGQNLVVDLSTQIFCHNDYPETITDYVTLQRGSAYGGVLSNFSGTVKYSGSSYPFPTTSETPRVVYNSRTDKPWPVALYLTPVSSAGGVAIKAGSLIAVLILRQTNNYNSDDFQFVWNIYANNDVVVPTGGCDVSARDVTVTLPDYPGSVPIPLTVYCAKSQNLGYYLSGTTADAGNSIFTNTASFSPAQGVGVQLTRNGTIIPANNTVSLGAVGTSAVSLGLTANYARTGGQVTAGNVQSIIGVTFVYQ	Clinical trial	Mannose-derived FimH antagonists: a promising anti-virulence therapeutic strategy for urinary tract infections and Crohn's disease.Expert Opin Ther Pat. 2016;26(2):175-97.	15.5	.	Fimbrial protein family	fimbrial protein family.	.	.	"Fimbrial protein; FimH, mannose binding"	PF00419; PF09160	PF00419; Fimbrial; PF09160; FimH_man-bind	.	.	.	.	EcoCyc:EG10315-MON	P08191
TTG9CFY	Bacterial Dihydroneopterinaldolase (Bact folB)	P0AC16	FOLB_ECOLI	Carbon-carbon lyase	"folB  of Escherichia coli; FOLB of Escherichia coli; DHNA of Escherichia coli; 7,8-Dihydroneopterin aldolase"	Bact folB	"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."	.	2O90	MDIVFIEQLSVITTIGVYDWEQTIEQKLVFDIEMAWDNRKAAKSDDVADCLSYADIAETVVSHVEGARFALVERVAEEVAELLLARFNSPWVRIKLSKPGAVARAANVGVIIERGNNLKENN	Discontinued	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	9	.	.	.	.	.	.	.	.	.	.	ecj00790: Folate biosynthesis; ecj01100: Metabolic pathways; ecj01240: Biosynthesis of cofactors	.	EcoCyc:H2NEOPTERINALDOL-MON; MetaCyc:H2NEOPTERINALDOL-MON	P0AC16
TTGERMY	Bacterial Dihydroneopterin aldolase (Bact folB)	O84620	FOLB_CHLTR	Carbon-carbon lyase	folB of Chlamydia trachomatis; DhnA-type aldolase; DHNA of Chlamydia trachomatis	Bact folB	"Catalyzes the conversion of 7,8-dihydroneopterin to 6- hydroxymethyl-7,8-dihydropterin."	EC 4.1.2.25	.	MLLYRLDIADFRVWVSIGVSEQERHYPQPVLVSLSLFFKEEPKACSTDKVSDSVCYAELVSLIEEVATNNPCALIERLAKVLLEKIEKALAGQVSRIDLRVSKERPPIPDLLSPVSFSISREVP	Literature-reported	Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis. Science. 1998 Oct 23;282(5389):754-9.	.	.	.	.	.	.	.	.	.	.	.	ctr00790: Folate biosynthesis; ctr01100: Metabolic pathways; ctr01240: Biosynthesis of cofactors	.	MetaCyc:MON-18793	O84620
TT38ECI	Bacterial Hydroxymethyl-dihydropterin pyrophosphokinase (Bact folK)	P26281	HPPK_ECOLI	Kinase	"PPPK; HPPK; 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase; 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase"	Bact folK	"2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity, magnesium ion binding"	.	6AN6; 6AN4; 5ETP; 5ETO; 5ETN	MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW	Literature-reported	"Bisubstrate analogue inhibitors of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: synthesis and biochemical and crystallographic studies. J Med Chem. 2001 Apr 26;44(9):1364-71."	2.1	.	.	.	.	.	.	.	.	.	.	ecj00790: Folate biosynthesis; ecj01100: Metabolic pathways; ecj01240: Biosynthesis of cofactors	.	EcoCyc:H2PTERIDINEPYROPHOSPHOKIN-MON; MetaCyc:H2PTERIDINEPYROPHOSPHOKIN-MON	P26281
TT4ILYC	Bacterial Dihydropteroate synthetase (Bact folP)	P0AC13	DHPS_ECOLI	Alkyl aryl transferase	folP; H2Pte synthase; Dihydropteroate synthase; Dihydropteroate pyrophosphorylase; DHPS	Bact folP	Dhps catalyzes the formation of the immediate precursor of folic acid. It is implicated in resistance to sulfonamide.	EC 2.5.1.15	1AJZ; 1AJ2; 1AJ0	MKLFAQGTSLDLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELQRVIPVVEAIAQRFEVWISVDTSKPEVIRESAKVGAHIINDIRSLSEPGALEAAAETGLPVCLMHMQGNPKTMQEAPKYDDVFAEVNRYFIEQIARCEQAGIAKEKLLLDPGFGFGKNLSHNYSLLARLAEFHHFNLPLLVGMSRKSMIGQLLNVGPSERLSGSLACAVIAAMQGAHIIRVHDVKETVEAMRVVEATLSAKENKRYE	Successful	Emerging drugs for bacterial urinary tract infections. Expert Opin Emerg Drugs. 2005 May;10(2):275-98.	34	.	.	.	.	.	.	.	.	.	.	ecj00790: Folate biosynthesis; ecj01100: Metabolic pathways; ecj01240: Biosynthesis of cofactors	.	EcoCyc:H2PTEROATESYNTH-MON; MetaCyc:H2PTEROATESYNTH-MON	P0AC13
TTHDSE2	Bacterial Fumarate reductase flavoprotein (Bact frdA)	O06913	FRDA_HELPY	CH-CH donor oxidoreductase	Fumarate reductase; FRDA	Bact frdA	"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."	EC 1.3.5.4	.	MKITYCDALIIGGGLAGLRASIACKQKGLNTIVLSLVPVRRSHSAAAQGGMQASLANAKKSEGDNEDLHFLDTVKGSDWGCDQQVARMFVTTAPKAIRELASWGVPWTRIKKGDRPAVVNGEHVTITERDDRHGYILSRDFGGTKKWRTCFTADATGHTMLYAVANEALHHKVDIQDRKDMLAFIHHDNKCYGAVVRDLITGEISAYVSKGTLLATGGYGRVYKHTTNAVICDGAGAASALETGVAKLGNMEAVQFHPTALVPSGILMTEGCRGDGGVLRDKFGRRFMPAYEPEKKELASRDVVSRRILEHIQKGYGAKSPYGDHVWLDIAILGRNHVEKNLRDVRDIAMTFAGIDPADSKEQTKDNMQGVPANEPEYGQAMAKQKGWIPIKPMQHYSMGGVRTNPKGETHLKGLFCAGEAACWDLHGFNRLGGNSVSEAVVAGMIIGDYFASHCLEAQIEINTQKVEAFIKESQDYMHFLLHNEGKEDVYEIRERMKEVMDEKVGVFREGKRLEEALKELQELYARSKNICVKNKVLHNNPELEDAYRTKKMLKLALCITQGALLRTESRGAHTRIDYPKRDDEKWLNRTLASWPSAEQDMPTIEYEELDVMKMEISPDFRGYGKKGNFIPHPKKEERDAEILKTILELEKLGKDRIEVQHALMPFELQEKYKARNMRLEDEEVRARGEHLYSFNVHELLDQHNANLKGEHHE	Successful	Fumarate reductase is essential for Helicobacter pylori colonization of the mouse stomach. Microb Pathog. 2000 Nov;29(5):279-87.	34	.	.	.	.	.	.	.	.	.	.	hpy00020: Citrate cycle (TCA cycle); hpy00190: Oxidative phosphorylation; hpy00620: Pyruvate metabolism; hpy00650: Butanoate metabolism	.	MetaCyc:HP0192-MON	O06913
TT4W1VJ	Bacterial Celldivision protein FtsZ (Bact ftsZ)	P45485	FTSZ_WOLSP	Peptidase	FtsZprotein; FtsZ	Bact ftsZ	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.	.	.	MSIDLSLPELPILHPRITVVGVGGAGGNAVNNMIQSNLQGVNFVVANTDAQALEKSLCDKKIQLGINLTKGLGAGALPDVGKGAAEESIDEIMEHIKDSHMLFITAGMGGGTGTGAAPVIAKAAREARAAVKDRAPKEKKILTVGVVTKPFGFEGVRRMPIAELGLEELQKYVDTLIVIPNQNLFRIANEKTTFSDAFKLADNVLHIGIRGVTDLMVMPGLINLDFADIETVMSEMGKAMIGTGEAEGEDRAISAAEAAISNPLLDNVSMKGAQGILINITGGGDMTLFEVDAAANRVREEVDENANIIFGATFDQAMEGRVRVSVLATGIDGRNNKSETSPISQSEDSEKEKFKWPYSQSESTQDKTLETKPAEQVSEGAKWGSNIYDIPAYLRRKK	Clinical trial	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P45485
TT3DQUT	Bacterial Lantibiotic mersacidin (Bact glmM)	P31120	GLMM_ECOLI	.	glmM of Escherichia coli; Protein mrsA; Mersacidin	Bact glmM	"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."	EC 5.4.2.10	.	MSNRKYFGTDGIRGRVGDAPITPDFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTPAVAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEAEMEKEISCVDSAELGKASRIVDAAGRYIEFCKATFPNELSLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNGVNINAEVGATDVRALQARVLAEKADLGIAFDGDGDRVIMVDHEGNKVDGDQIMYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPFARAKVGDRYVLEKMQEKGWRIGAENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLCSGMKMFPQILVNVRYTAGSGDPLEHESVKAVTAEVEAALGNRGRVLLRKSGTEPLIRVMVEGEDEAQVTEFAHRIADAVKAV	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	ecj00520: Amino sugar and nucleotide sugar metabolism; ecj01100: Metabolic pathways; ecj01250: Biosynthesis of nucleotide sugars	.	EcoCyc:PHOSGLUCOSAMINEMUT-MON; MetaCyc:PHOSGLUCOSAMINEMUT-MON	P31120
TTC67I0	Bacterial Glucosamine-6-phosphate synthase (Bact glmS)	P17169	GLMS_ECOLI	Transaminase	glmS; L-glutamine-D-fructose-6-phosphate amidotransferase; Hexosephosphate aminotransferase; Glucosamine--fructose-6-phosphate aminotransferase; GFAT; D-fructose-6-phosphate amidotransferase	Bact glmS	"Catalyzesthe first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source."	EC 2.6.1.16	4AMV; 3OOJ; 2VF5; 2VF4; 2J6H	MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNLQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGYLGSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAKLSRLKGLDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE	Clinical trial	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	17	.	.	.	.	.	.	.	.	.	.	"ecj00250: Alanine, aspartate and glutamate metabolism; ecj00520: Amino sugar and nucleotide sugar metabolism; ecj01100: Metabolic pathways; ecj01250: Biosynthesis of nucleotide sugars"	.	EcoCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MON; MetaCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MON	P17169
TTN6J5F	Bacterial DNA gyrase (Bact gyrase)	P20831; P0A0K8	GYRA_STAAU; GYRB_STAAU	ATP-hydrolyzing DNA topoisomerase	DNA gyrase	Bact gyrA	"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."	.	.	MAELPQSRINERNITSEMRESFLDYAMSVIVARALPDVRDGLKPVHRRILYGLNEQGMTPDKSYKKSARIVGDVMGKYHPHGDSSIYEAMVRMAQDFSYRYPLVDGQGNFGSMDGDGAAAMRYTEARMTKITLELLRDINKDTIDFIDNYDGNEREPSVLPARFPNLLANGASGIAVGMATNIPPHNLTELINGVLSLSKNPDISIAELMEDIEGPDFPTAGLILGKSGIRRAYETGRGSIQMRSRAVIEERGGGRQRIVVTEIPFQVNKARMIEKIAELVRDKKIDGITDLRDETSLRTGVRVVIDVRKDANASVILNNLYKQTPLQTSFGVNMIALVNGRPKLINLKEALVHYLEHQKTVVRRRTQYNLRKAKDRAHILEGLRIALDHIDEIISTIRESDTDKVAMESLQQRFKLSEKQAQAILDMRLRRLTGLERDKIEAEYNELLNYISELEAILADEEVLLQLVRDELTEIRDRFGDDRRTEIQLGGFEDLEDEDLIPEEQIVITLSHNNYIKRLPVSTYRAQNRGGRGVQGMNTLEEDFVSQLVTLSTHDHVLFFTNKGRVYKLKGYEVPELSRQSKGIPVVNAIELENDEVISTMIAVKDLESEDNFLVFATKRGVVKRSALSNFSRINRNGKIAISFREDDELIAVRLTSGQEDILIGTSHASLIRFPESTLRPLGRTATGVKGITLREGDEVVGLDVAHANSVDEVLVVTENGYGKRTPVNDYRLSNRGGKGIKTATITERNGNVVCITTVTGEEDLMIVTNAGVIIRLDVADISQNGRAAQGVRLIRLGDDQFVSTVAKVKEDAEDETNEDEQSTSTVSEDGTEQQREAVVNDETPGNAIHTEVIDSEENDEDGRIEVRQDFMDRVEEDIQQSLDEDEE	Successful	Hughes B: 2009 FDA drug approvals. Nat Rev Drug Discov. 2010 Feb;9(2):89-92.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	P20831
TTS7LWX	Bacterial DNA gyrase B (Bact gyrB)	P0AES6	GYRB_ECOLI	ATP-hydrolyzing DNA topoisomerase	gyrB; DNA gyrase subunit B	Bact gyrB	"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."	EC 5.6.2.3	6ENG; 5Z9Q; 5Z9N; 5Z9M; 5Z9L	MSNSYDSSSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNAIDEALAGHCKEIIVTIHADNSVSVQDDGRGIPTGIHPEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSQKLELVIQREGKIHRQIYEHGVPQAPLAVTGETEKTGTMVRFWPSLETFTNVTEFEYEILAKRLRELSFLNSGVSIRLRDKRDGKEDHFHYEGGIKAFVEYLNKNKTPIHPNIFYFSTEKDGIGVEVALQWNDGFQENIYCFTNNIPQRDGGTHLAGFRAAMTRTLNAYMDKEGYSKKAKVSATGDDAREGLIAVVSVKVPDPKFSSQTKDKLVSSEVKSAVEQQMNELLAEYLLENPTDAKIVVGKIIDAARAREAARRAREMTRRKGALDLAGLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGRDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIVERGHVYIAQPPLYKVKKGKQEQYIKDDEAMDQYQISIALDGATLHTNASAPALAGEALEKLVSEYNATQKMINRMERRYPKAMLKELIYQPTLTEADLSDEQTVTRWVNALVSELNDKEQHGSQWKFDVHTNAEQNLFEPIVRVRTHGVDTDYPLDHEFITGGEYRRICTLGEKLRGLLEEDAFIERGERRQPVASFEQALDWLVKESRRGLSIQRYKGLGEMNPEQLWETTMDPESRRMLRVTVKDAIAADQLFTTLMGDAVEPRRAFIEENALKAANIDI	Clinical trial	Isolation and characterization of an Escherichia coli strain exhibiting partial tolerance to quinolones. Antimicrob Agents Chemother. 1989 May;33(5):705-9.	0	.	.	.	.	.	.	.	.	.	.	.	.	EcoCyc:EG10424-MON; MetaCyc:EG10424-MON	P0AES6
TT6LDTK	Bacterial Glutamate-1-semialdehyde aminomutase (Bact hemL)	P23893	GSA_ECOLI	Intramolecular transferases	"Glutamate-1-semialdehyde aminotransferase; Glutamate-1-semialdehyde 2,1-aminomutase; GSA-AT; GSA"	Bact hemL	Catalyses the formation of this key precursor of tetrapyrroles.	.	.	MSKSENLYSAARELIPGGVNSPVRAFTGVGGTPLFIEKADGAYLYDVDGKAYIDYVGSWGPMVLGHNHPAIRNAVIEAAERGLSFGAPTEMEVKMAQLVTELVPTMDMVRMVNSGTEATMSAIRLARGFTGRDKIIKFEGCYHGHADCLLVKAGSGALTLGQPNSPGVPADFAKYTLTCTYNDLASVRAAFEQYPQEIACIIVEPVAGNMNCVPPLPEFLPGLRALCDEFGALLIIDEVMTGFRVALAGAQDYYGVVPDLTCLGKIIGGGMPVGAFGGRRDVMDALAPTGPVYQAGTLSGNPIAMAAGFACLNEVAQPGVHETLDELTTRLAEGLLEAAEEAGIPLVVNHVGGMFGIFFTDAESVTCYQDVMACDVERFKRFFHMMLDEGVYLAPSAFEAGFMSVAHSMEDINNTIDAARRVFAKL	Literature-reported	"Reactions of glutamate 1-semialdehyde aminomutase with R- and S-enantiomers of a novel, mechanism-based inhibitor, 2,3-diaminopropyl sulfate. Biochemistry. 2000 Mar 21;39(11):3091-6."	0	.	.	.	.	.	.	.	.	.	.	ecj00860: Porphyrin metabolism; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01120: Microbial metabolism in diverse environments; ecj01240: Biosynthesis of cofactors	.	EcoCyc:GSAAMINOTRANS-MON; MetaCyc:GSAAMINOTRANS-MON	P23893
TTNAW8S	Bacterial Flavohemoglobin (Bact hmp)	P24232	HMP_ECOLI	Paired donor oxygen oxidoreductase	Nitric oxide dioxygenase; NOD; NO oxygenase; Hemoglobin-like protein; HMP; Ferrisiderophore reductase B; Dihydropteridine reductase	Bact hmp	"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."	EC 1.14.12.17	1GVH	MLDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEKIAQKHTSFQIKPEQYNIVGEHLLATLDEMFSPGQEVLDAWGKAYGVLANVFINREAEIYNENASKAGGWEGTRDFRIVAKTPRSALITSFELEPVDGGAVAEYRPGQYLGVWLKPEGFPHQEIRQYSLTRKPDGKGYRIAVKREEGGQVSNWLHNHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQSLPRFTAHTWYRQPSEADRAKGQFDSEGLMDLSKLEGAFSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECFGPHKVL	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	EcoCyc:EG10456-MON; MetaCyc:EG10456-MON	P24232
TTDTNEF	Bacterial Homoserine dehydrogenase (Bact hom)	P19582	DHOM_BACSU	Short-chain dehydrogenases reductase	Homoserine dehydrogenase; HDH	Bact hom	"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). "	EC 1.1.1.3	.	MKAIRVGLLGLGTVGSGVVKIIQDHQDKLMHQVGCPVTIKKVLVKDLEKKREVDLPKEVLTTEVYDVIDDPDVDVVIEVIGGVEQTKQYLVDALRSKKHVVTANKDLMAVYGSELLAEAKENGCDIYFEASVAGGIPILRTLEEGLSSDRITKMMGIVNGTTNFILTKMIKEKSPYEEVLKEAQDLGFAEADPTSDVEGLDAARKMAILARLGFSMNVDLEDVKVKGISQITDEDISFSKRLGYTMKLIGIAQRDGSKIEVSVQPTLLPDHHPLSAVHNEFNAVYVYGEAVGETMFYGPGAGSMPTATSVVSDLVAVMKNMRLGVTGNSFVGPQYEKNMKSPSDIYAQQFLRIHVKDEVGSFSKITSVFSERGVSFEKILQLPIKGHDELAEIVIVTHHTSEADFSDILQNLNDLEVVQEVKSTYRVEGNGWS	Literature-reported	Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases. Nat Struct Biol. 2000 Mar;7(3):238-44.	.	.	.	.	.	.	.	.	.	.	.	"bsu00260: Glycine, serine and threonine metabolism; bsu00270: Cysteine and methionine metabolism; bsu00300: Lysine biosynthesis; bsu01100: Metabolic pathways; bsu01110: Biosynthesis of secondary metabolites; bsu01120: Microbial metabolism in diverse environments; bsu01230: Biosynthesis of amino acids"	.	BSUB:BSU32260-MON	P19582
TT6KYJ5	Bacterial Isoleucyl-tRNA synthetase (Bact ileS)	P00956	SYI_ECOLI	Carbon-oxygen ligase	ileS; Isoleucine--tRNA ligase of Escherichia coli; IRS of Escherichia coli	Bact ileS	"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)."	EC 6.1.1.5	.	MSDYKSTLNLPETGFPMRGDLAKREPGMLARWTDDDLYGIIRAAKKGKKTFILHDGPPYANGSIHIGHSVNKILKDIIVKSKGLSGYDSPYVPGWDCHGLPIELKVEQEYGKPGEKFTAAEFRAKCREYAATQVDGQRKDFIRLGVLGDWSHPYLTMDFKTEANIIRALGKIIGNGHLHKGAKPVHWCVDCRSALAEAEVEYYDKTSPSIDVAFQAVDQDALKAKFAVSNVNGPISLVIWTTTPWTLPANRAISIAPDFDYALVQIDGQAVILAKDLVESVMQRIGVTDYTILGTVKGAELELLRFTHPFMGFDVPAILGDHVTLDAGTGAVHTAPGHGPDDYVIGQKYGLETANPVGPDGTYLPGTYPTLDGVNVFKANDIVVALLQEKGALLHVEKMQHSYPCCWRHKTPIIFRATPQWFVSMDQKGLRAQSLKEIKGVQWIPDWGQARIESMVANRPDWCISRQRTWGVPMSLFVHKDTEELHPRTLELMEEVAKRVEVDGIQAWWDLDAKEILGDEADQYVKVPDTLDVWFDSGSTHSSVVDVRPEFAGHAADMYLEGSDQHRGWFMSSLMISTAMKGKAPYRQVLTHGFTVDGQGRKMSKSIGNTVSPQDVMNKLGADILRLWVASTDYTGEMAVSDEILKRAADSYRRIRNTARFLLANLNGFDPAKDMVKPEEMVVLDRWAVGCAKAAQEDILKAYEAYDFHEVVQRLMRFCSVEMGSFYLDIIKDRQYTAKADSVARRSCQTALYHIAEALVRWMAPILSFTADEVWGYLPGEREKYVFTGEWYEGLFGLADSEAMNDAFWDELLKVRGEVNKVIEQARADKKVGGSLEAAVTLYAEPELSAKLTALGDELRFVLLTSGATVADYNDAPADAQQSEVLKGLKVALSKAEGEKCPRCWHYTQDVGKVAEHAEICGRCVSNVAGDGEKRKFA	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	ecj00970: Aminoacyl-tRNA biosynthesis	.	EcoCyc:ILES-MON; MetaCyc:ILES-MON	P00956
TT9BH7S	Bacterial Threonine deaminase (Bact ilvA)	P04968	ILVA_ECOLI	Carbon-nitrogen lyases	ilvA; Putative threonine dehydratase	Bact ilvA	"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."	EC 4.3.1.19	1TDJ	MADSQPLSGAPEGAEYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNIRGERLAHILSGANVNFHGLRYVSERCELGEQREALLAVTIPEEKGSFLKFCQLLGGRSVTEFNYRFADAKNACIFVGVRLSRGLEERKEILQMLNDGGYSVVDLSDDEMAKLHVRYMVGGRPSHPLQERLYSFEFPESPGALLRFLNTLGTYWNISLFHYRSHGTDYGRVLAAFELGDHEPDFETRLNELGYDCHDETNNPAFRFFLAG	Literature-reported	Vitamin B 6 biosynthesis in Bacillus subtilis. Hoppe Seylers Z Physiol Chem. 1978 May;359(5):559-70.	.	.	.	.	.	.	.	.	.	.	.	"ecj00260: Glycine, serine and threonine metabolism; ecj00290: Valine, leucine and isoleucine biosynthesis; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01200: Carbon metabolism; ecj01230: Biosynthesis of amino acids"	.	EcoCyc:THREDEHYDSYN-MON; MetaCyc:THREDEHYDSYN-MON	P04968
TT04KI2	Bacterial Ketol-acid reductoisomerase (Bact ilvC)	P05793	ILVC_ECOLI	Short-chain dehydrogenases reductase	Ketol-acid reductoisomerase type II; Ketol-acid reductoisomerase type 2; Ketol-acid reductoisomerase (NADP(+)); KARI; Alpha-keto-beta-hydroxylacyl reductoisomerase; Acetohydroxy-acid isomeroreductase; AHIR	Bact ilvC	"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."	.	3ULK; 1YRL	MANYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRKATENGFKVGTYEELIPQADLVINLTPDKQHSDVVRTVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVEEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVLMIAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYLFSYACVPLLKPFMAELQPGDLGKAIPEGAVDNGQLRDVNEAIRSHAIEQVGKKLRGYMTDMKRIAVAG	Literature-reported	"Enzymology, structure, and dynamics of acetohydroxy acid isomeroreductase. Acc Chem Res. 2001 May;34(5):399-408."	.	.	.	.	.	.	.	.	.	.	.	"ecj00290: Valine, leucine and isoleucine biosynthesis; ecj00770: Pantothenate and CoA biosynthesis; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01210: 2-Oxocarboxylic acid metabolism; ecj01230: Biosynthesis of amino acids"	.	EcoCyc:KETOLREDUCTOISOM-MON; MetaCyc:KETOLREDUCTOISOM-MON	P05793
TTVTX4N	Bacterial Fatty acid synthetase I (Bact inhA)	P9WGR1	INHA_MYCTU	CH-CH donor oxidoreductase	Enoyl-[acyl-carrier-protein] reductase [NADH]; Bacterial InhA	Bact inhA	Involved in the resistance against the antituberculosis drugs isoniazid and ethionamide.	.	6GHN; 6GH4; 6GH1; 6GGM; 6EP8	MTGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFDRLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAIGAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIHISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMTVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAIVGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTGDIIYADGGAHTQLL	Successful	Diversity in enoyl-acyl carrier protein reductases. Cell Mol Life Sci. 2009 May;66(9):1507-17.	34	EC:1.3	.	.	.	.	.	.	.	.	.	.	.	MetaCyc:G185E-5668-MON	P9WGR1
TT5VER7	Bacterial Undecaprenyl pyrophosphate synthetase (Bact ispU)	P60472	UPPS_ECOLI	Alkyl aryl transferase	ispU; Undecaprenyl diphosphate synthase; Undecaprenyl diphosphate  synthase; UPP synthetase; UPP synthase; UDS; Di-trans-poly-cis-decaprenylcistransferase	Bact ispU	"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."	EC 2.5.1.31	5ZHE; 5CQJ; 5CQB; 4H3C; 4H3A	MMLSATQPLSEKLPAHGCRHVAIIMDGNGRWAKKQGKIRAFGHKAGAKSVRRAVSFAANNGIEALTLYAFSSENWNRPAQEVSALMELFVWALDSEVKSLHRHNVRLRIIGDTSRFNSRLQERIRKSEALTAGNTGLTLNIAANYGGRWDIVQGVRQLAEKVQQGNLQPDQIDEEMLNQHVCMHELAPVDLVIRTGGEHRISNFLLWQIAYAELYFTDVLWPDFDEQDFEGALNAFANRERRFGGTEPGDETA	Literature-reported	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	0	.	.	.	.	.	.	.	.	.	.	ecj00550: Peptidoglycan biosynthesis; ecj00900: Terpenoid backbone biosynthesis; ecj01110: Biosynthesis of secondary metabolites	.	EcoCyc:UPPSYN-MON; MetaCyc:UPPSYN-MON	P60472
TTVNA43	Bacterial Deoxy-D-manno-octulosonate 8-phosphate synthase (Bact kdsA)	P0A715	KDSA_ECOLI	Alkyl aryl transferase	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	Bact kdsA	Synthesis of KDO 8-P which is required for lipid A maturation and cellular growth.	.	1X8F; 1X6U; 1Q3N; 1PL9; 1PHW	MKQKVVSIGDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQTFGVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCDRGANFGYDNLVVDMLGFSIMKKVSGNSPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCDGPSALPLAKLEPFLKQMKAIDDLVKGFEELDTSK	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	ecj00540: Lipopolysaccharide biosynthesis; ecj01100: Metabolic pathways; ecj01250: Biosynthesis of nucleotide sugars	.	EcoCyc:KDO-8PSYNTH-MON; MetaCyc:KDO-8PSYNTH-MON	P0A715
TTQ8J1V	Bacterial Deoxy-manno-octulosonate cytidylyltransferase (Bact kdsB)	P04951	KDSB_ECOLI	Kinase	kdsB; CMP-KDO synthetase; CMP-2-keto-3-deoxyoctulosonic acid synthetase; CKS; 3-deoxy-D-manno-octulosonate cytidylytransferase	Bact kdsB	Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.	EC 2.7.7.38	3K8E; 3K8D; 1VH1	MSFVVIIPARYASTRLPGKPLVDINGKPMIVHVLERARESGAERIIVATDHEDVARAVEAAGGEVCMTRADHQSGTERLAEVVEKCAFSDDTVIVNVQGDEPMIPATIIRQVADNLAQRQVGMATLAVPIHNAEEAFNPNAVKVVLDAEGYALYFSRATIPWDRDRFAEGLETVGDNFLRHLGIYGYRAGFIRRYVNWQPSPLEHIEMLEQLRVLWYGEKIHVAVAQEVPGTGVDTPEDLERVRAEMR	Clinical trial	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	25	.	.	.	.	.	.	.	.	.	.	ecj00540: Lipopolysaccharide biosynthesis; ecj01100: Metabolic pathways; ecj01250: Biosynthesis of nucleotide sugars	.	EcoCyc:CPM-KDOSYNTH-MON; MetaCyc:CPM-KDOSYNTH-MON	P04951
TT13OHY	Bacterial Kgp protease (Bact kgp-381)	P96966	P96966_PORGN	Protease	Cysteine protease	Bact kgp-381	Important for both nutrition and virulence of P. gingivalis	.	.	MRKLLLLIAASLLGVGLYAQSAKIKLDAPTTRTTCTNNSFKQFDASFSFNEVELTKVETKGGTFASVSIPGAFPTGEVGSPEVPAVRKLIAVPVGATPVVRVKSFTEQVYSLNQYGSEKLMPHQPSMSKSDDPEKVPFVYNAAAYARKGFVGQELTQVEMLGTMRGVRIAALTINPVQYDVVANQLKVRNNIEIEVSFQGADEVATQRLYDASFSPYFETAYKQLFNRDVYTDHGDLYNTPVRMLVVAGAKFKEALKPWLTWKAQKGFYLDVHYTDEAEVGTTNASIKAFIHKKYNDGLAASAAPVFLALVGDTDVISGEKGKKTKKVTDLYYSAVDGDYFPEMYTFRMSASSPEELTNIIDKY	Literature-reported	Attenuation of the virulence of Porphyromonas gingivalis by using a specific synthetic Kgp protease inhibitor. Infect Immun. 2002 Dec;70(12):6968-75.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJVCG0	Bacterial Sporulation kinase A (Bact kinA)	P16497	KINA_BACSU	.	Stage II sporulation protein J; Stage II sporulation protein F; Sporulation kinase A	Bact kinA	Phosphorylates the sporulation-regulatory proteins spo0A and spo0F. It also autophosphorylates in the presence of ATP.	EC 2.7.13.3	2VLG	MEQDTQHVKPLQTKTDIHAVLASNGRIIYISANSKLHLGYLQGEMIGSFLKTFLHEEDQFLVESYFYNEHHLMPCTFRFIKKDHTIVWVEAAVEIVTTRAERTEREIILKMKVLEEETGHQSLNCEKHEIEPASPESTTYITDDYERLVENLPSPLCISVKGKIVYVNSAMLSMLGAKSKDAIIGKSSYEFIEEEYHDIVKNRIIRMQKGMEVGMIEQTWKRLDGTPVHLEVKASPTVYKNQQAELLLLIDISSRKKFQTILQKSRERYQLLIQNSIDTIAVIHNGKWVFMNESGISLFEAATYEDLIGKNIYDQLHPCDHEDVKERIQNIAEQKTESEIVKQSWFTFQNRVIYTEMVCIPTTFFGEAAVQVILRDISERKQTEELMLKSEKLSIAGQLAAGIAHEIRNPLTAIKGFLQLMKPTMEGNEHYFDIVFSELSRIELILSELLMLAKPQQNAVKEYLNLKKLIGEVSALLETQANLNGIFIRTSYEKDSIYINGDQNQLKQVFINLIKNAVESMPDGGTVDIIITEDEHSVHVTVKDEGEGIPEKVLNRIGEPFLTTKEKGTGLGLMVTFNIIENHQGVIHVDSHPEKGTAFKISFPKK	Literature-reported	Histidine kinases as targets for new antimicrobial agents. Bioorg Med Chem. 2002 Apr;10(4):855-67.	2	.	.	.	.	.	.	.	.	.	.	bsu02020: Two-component system	.	BSUB:BSU13990-MON	P16497
TTIQSC1	Bacterial Lethal factor (Bact lef)	P15917	LEF_BACAN	Peptidase	lef; Anthrax lethal toxin endopeptidase component; Anthrax lethal factor; ALF	Bact lef	"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."	EC 3.4.24.83	5D1U; 5D1T; 5D1S; 4XM8; 4XM7	MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS	Clinical trial	Anti-toxin antibodies in prophylaxis and treatment of inhalation anthrax.Future Microbiol.2009 Feb;4(1):35-43.	17	.	.	.	.	.	.	.	.	.	.	bar04621: NOD-like receptor signaling pathway	R-HSA-5210891:Uptake and function of anthrax toxins	.	P15917
TTGX0HR	Bacterial DNA ligase (Bact ligA)	P15042	DNLJ_ECOLI	Phosphoric ester ligase	ligA; Polydeoxyribonucleotide synthase [NAD+]; NAD+-dependent DNA ligase	Bact ligA	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.	EC 6.5.1.2	5TT5; 4GLX; 2OWO	MESIEQQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPTQRVGAAPLAAFSQIRHEVPMLSLDNVFDEESFLAFNKRVQDRLKNNEKVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLHGENIPARLEVRGEVFLPQAGFEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGVLEGGELPDTHLGRLLQFKKWGLPVSDRVTLCESAEEVLAFYHKVEEDRPTLGFDIDGVVIKVNSLAQQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLRIGDKVVIRRAGDVIPQVVNVVLSERPEDTREVVFPTHCPVCGSDVERVEGEAVARCTGGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFKLTAGKLTGLERMGPKSAQNVVNALEKAKETTFARFLYALGIREVGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVASHVHNFFAEESNRNVISELLAEGVHWPAPIVINAEEIDSPFAGKTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVIDEAEMLRLLGS	Literature-reported	Identification and validation of human DNA ligase inhibitors using computer-aided drug design. J Med Chem. 2008 Aug 14;51(15):4553-62.	0	.	.	.	.	.	.	.	.	.	.	ecj03030: DNA replication; ecj03410: Base excision repair; ecj03420: Nucleotide excision repair; ecj03430: Mismatch repair	.	EcoCyc:EG10534-MON; MetaCyc:EG10534-MON	P15042
TTIB7O8	Bacterial Integral membrane LmrP (Bact lmrP)	Q9CDQ3	Q9CDQ3_LACLA	.	lmrP; L24511; Integral membrane protein LmrP	Bact lmrP	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.	.	.	MKEFWNLDKNLQLRLGIVFLGAFSYGTVFSSMTIYYNQHLGSAITGILLALSAVATFVAGILSGFFADRNGRKPVMVFGTVIQLLGALLAIDSNLPGHVNPWSTFIAFLLISFGYNLVITAGNAMIIDASNAENRKVVFMLDYWAQNLSVILGAALSAWLFRPAFEALLVILLLTVLVSFFLTTFVMTETFRPIVKAKEEAENIFQAYKTVLQDKTYMIFMGANIATTFIIMQFDNFLPVHLSNSFKTITFFGFEIYGQRMLTIYLILACVLVVLLMTTLNRLTKDWSHQKGFIWGSLFMAIGMIFSFLTTTFTPIFIAGIVYTLGEIVYTPSVQTLGVDLMNPEKIGSYNGVAAIKMPIASILAGLLVSISPMIKATGVSLVLALTEVLAIILVLIAVNRHQKTKIN	Successful	"The lactococcal secondary multidrug transporter LmrP confers resistance to lincosamides, macrolides, streptogramins and tetracyclines. Microbiology. 2001 Oct;147(Pt 10):2873-80."	34	.	.	.	.	.	Major Facilitator Superfamily	PF07690	PF07690; MFS_1	.	.	.	.	.	.
TTSI0C6	Bacterial Class 1 lysyl-tRNA synthetase (Bact lysK)	Q937U6	Q937U6_BORHE	Carbon-oxygen ligase	Class 1 lysyl-tRNA synthetase	Bact lysK	"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."	EC 6.1.1.6	.	DFYAKKIIEEKGEKEQYTVASGITPSGTVHIGNFREVISVDLVARALKDAGRNVRFIYSWDNYDVFRKVPKNMPNQELLTTHLRQAITRVPDTQTNQSSYARANEVEFEKYLPIVGIKPEFIDQSLKYMSSDYSSQIKFALDHKDEIEKVLNKYRTTKLADNWYPISIFCTKCNRDTTTIKNYNHCYSIEYCCECGNKESLDLRKTWAVKLPWRIDWPMRWKYENVDFEPAGKDHHSSGGSFDTSIEIVKIFGGTPPITFQYDFISIKGRGGKISSSSGDVGSLKDVLEIYTPEVTRFLFASTKPNTEFSISFDLDVIKIYEDYDKFERVYYGIDDIKENKKEAFKRIYELSQPKLPDKEIPYQIGFRHLSTICQIFEGDKDKIFKLLNDVKESQKAKLINKIECAINWIKKFAPEDFKFSLRYTFDNIEPLKDNNKQGVTQLLDFLKKDFNNITEKEIQDEIYNIARNNNIEPPLFFKQLYNILINKDKGPKLAGFIKIIGIKKFEEIVKHYI	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJMGDT	Bacterial Lysyl-tRNA synthetase (Bact lysS)	P0A8N3	SYK1_ECOLI	Carbon-oxygen ligase	Lysyl-tRNA synthetase; Lysine--tRNA ligase; LysRS	Bact lysS	"Catalyses the formation of lysyl-transfer RNA, Lys-tRNA(Lys), which then is ready to insert lysine into proteins."	EC 6.1.1.6	1KRT; 1KRS; 1BBW; 1BBU	MSEQHAQGADAVVDLNNELKTRREKLANLREQGIAFPNDFRRDHTSDQLHAEFDGKENEELEALNIEVAVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDDLPEGVYNEQFKKWDLGDILGAKGKLFKTKTGELSIHCTELRLLTKALRPLPDKFHGLQDQEARYRQRYLDLISNDESRNTFKVRSQILSGIRQFMVNRGFMEVETPMMQVIPGGAAARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQDILGKTEVTYGDVTLDFGKPFEKLTMREAIKKYRPETDMADLDNFDSAKAIAESIGIHVEKSWGLGRIVTEIFEEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAQRFLDQVAAKDAGDDEAMFYDEDYVTALEHGLPPTAGLGIGIDRMVMLFTNSHTIRDVILFPAMRPVK	Literature-reported	Rickettsiae and Chlamydiae: evidence of horizontal gene transfer and gene exchange. Trends Genet. 1999 May;15(5):173-5.	.	.	.	.	.	.	.	.	.	.	.	ecj00970: Aminoacyl-tRNA biosynthesis	.	EcoCyc:LYSS-MON; MetaCyc:LYSS-MON	P0A8N3
TTDU0HP	Bacterial Cystathionine gamma-synthase (Bact metB)	P00935	METB_ECOLI	Alkyl aryl transferase	metB; O-succinylhomoserine (Thiol)-lyase; CGS	Bact metB	"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."	EC 2.5.1.48	1CS1	MTRKQATIAVRSGLNDDEQYGCVVPPIHLSSTYNFTGFNEPRAHDYSRRGNPTRDVVQRALAELEGGAGAVLTNTGMSAIHLVTTVFLKPGDLLVAPHDCYGGSYRLFDSLAKRGCYRVLFVDQGDEQALRAALAEKPKLVLVESPSNPLLRVVDIAKICHLAREVGAVSVVDNTFLSPALQNPLALGADLVLHSCTKYLNGHSDVVAGVVIAKDPDVVTELAWWANNIGVTGGAFDSYLLLRGLRTLVPRMELAQRNAQAIVKYLQTQPLVKKLYHPSLPENQGHEIAARQQKGFGAMLSFELDGDEQTLRRFLGGLSLFTLAESLGGVESLISHAATMTHAGMAPEARAAAGISETLLRISTGIEDGEDLIADLENGFRAANKG	Literature-reported	Crystal structures of cystathionine gamma-synthase inhibitor complexes rationalize the increased affinity of a novel inhibitor. J Mol Biol. 2001 Aug 24;311(4):789-801.	2.1	.	.	.	.	.	.	.	.	.	.	ecj00270: Cysteine and methionine metabolism; ecj00450: Selenocompound metabolism; ecj00920: Sulfur metabolism; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01230: Biosynthesis of amino acids	.	EcoCyc:O-SUCCHOMOSERLYASE-MON; MetaCyc:O-SUCCHOMOSERLYASE-MON	P00935
TTZP720	Bacterial Cystathionine beta-lyase (Bact metC)	P06721	METC_ECOLI	Carbon-sulfur lyases	Cysteine-S-conjugate beta-lyase MetC; Cysteine lyase MetC; Cysteine desulfhydrase MetC; Cystathionine beta-lyase MetC; CL; CBL; Beta-cystathionase MetC; Bacterial CD	Bact metC	"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."	EC 4.4.1.13	4ITX; 4ITG; 2GQN; 2FQ6; 1CL2	MADKKLDTQLVNAGRSKKYTLGAVNSVIQRASSLVFDSVEAKKHATRNRANGELFYGRRGTLTHFSLQQAMCELEGGAGCVLFPCGAAAVANSILAFIEQGDHVLMTNTAYEPSQDFCSKILSKLGVTTSWFDPLIGADIVKHLQPNTKIVFLESPGSITMEVHDVPAIVAAVRSVVPDAIIMIDNTWAAGVLFKALDFGIDVSIQAATKYLVGHSDAMIGTAVCNARCWEQLRENAYLMGQMVDADTAYITSRGLRTLGVRLRQHHESSLKVAEWLAEHPQVARVNHPALPGSKGHEFWKRDFTGSSGLFSFVLKKKLNNEELANYLDNFSLFSMAYSWGGYESLILANQPEHIAAIRPQGEIDFSGTLIRLHIGLEDVDDLIADLDAGFARIV	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	.	.	.	.	.	.	.	.	.	.	ecj00270: Cysteine and methionine metabolism; ecj00450: Selenocompound metabolism; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01230: Biosynthesis of amino acids	.	EcoCyc:CYSTATHIONINE-BETA-LYASE-MON; MetaCyc:CYSTATHIONINE-BETA-LYASE-MON	P06721
TTT4DEI	Bacterial Phospho-MurNAc-pentapeptide translocase (Bact MraY)	P0A6W3	MRAY_ECOLI	.	UDP-MurNAc-pentapeptide phosphotransferase; Phospho-N-acetylmuramoyl-pentapeptide-transferase	Bact MraY	First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan.	EC 2.7.8.13	.	MLVWLAEHLVKYYSGFNVFSYLTFRAIVSLLTALFISLWMGPRMIAHLQKLSFGQVVRNDGPESHFSKRGTPTMGGIMILTAIVISVLLWAYPSNPYVWCVLVVLVGYGVIGFVDDYRKVVRKDTKGLIARWKYFWMSVIALGVAFALYLAGKDTPATQLVVPFFKDVMPQLGLFYILLAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAGGFALVAWATGNMNFASYLHIPYLRHAGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVLLRQEFLLVIMGGVFVVETLSVILQVGSFKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISLMLVLIGLATLKVR	Literature-reported	Identification of novel inhibitors of phospho-MurNAc-pentapeptide translocase MraY from library screening: Isoquinoline alkaloid michellamine B and... Bioorg Med Chem. 2014 Sep 1;22(17):4566-71.	.	.	.	.	.	.	.	.	.	.	.	ecj00550: Peptidoglycan biosynthesis; ecj01100: Metabolic pathways; ecj01502: Vancomycin resistance	.	EcoCyc:PHOSNACMURPENTATRANS-MON; MetaCyc:PHOSNACMURPENTATRANS-MON	P0A6W3
TT85JMW	Bacterial Penicillin binding protein 3 (Bact mrcA)	P0AD68	FTSI_ECOLI	Hexosyltransferase	mrcA; Peptidoglycan synthetase ftsI; Peptidoglycan glycosyltransferase 3; Penicillin-binding protein 3; PSPB20; PBP-3; PBP 3	Bact mrcA	Cell wall formation. Essential for the formation of a septum of the murein sacculus. Synthesis of cross-linked peptidoglycan from the lipid intermediates.	EC 3.4.16.4	.	MKAAAKTQKPKRQEEHANFISWRFALLCGCILLALAFLLGRVAWLQVISPDMLVKEGDMRSLRVQQVSTSRGMITDRSGRPLAVSVPVKAIWADPKEVHDAGGISVGDRWKALANALNIPLDQLSARINANPKGRFIYLARQVNPDMADYIKKLKLPGIHLREESRRYYPSGEVTAHLIGFTNVDSQGIEGVEKSFDKWLTGQPGERIVRKDRYGRVIEDISSTDSQAAHNLALSIDERLQALVYRELNNAVAFNKAESGSAVLVDVNTGEVLAMANSPSYNPNNLSGTPKEAMRNRTITDVFEPGSTVKPMVVMTALQRGVVRENSVLNTIPYRINGHEIKDVARYSELTLTGVLQKSSNVGVSKLALAMPSSALVDTYSRFGLGKATNLGLVGERSGLYPQKQRWSDIERATFSFGYGLMVTPLQLARVYATIGSYGIYRPLSITKVDPPVPGERVFPESIVRTVVHMMESVALPGGGGVKAAIKGYRIAIKTGTAKKVGPDGRYINKYIAYTAGVAPASQPRFALVVVINDPQAGKYYGGAVSAPVFGAIMGGVLRTMNIEPDALTTGDKNEFVINQGEGTGGRS	Successful	Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole. Mol Microbiol. 2003 Jan;47(2):539-47.	34	.	.	.	.	.	.	.	.	.	.	ecj00550: Peptidoglycan biosynthesis; ecj01100: Metabolic pathways; ecj01501: beta-Lactam resistance	.	EcoCyc:EG10341-MON; MetaCyc:EG10341-MON	P0AD68
TTTKCMH	Bacterial Penicillin binding protein 1 (Bact pbp)	P02918; P02919; P76577	PBPA_ECOLI; PBPB_ECOLI; PBPC_ECOLI	.	Penicillin-binding protein 1; PBP1; PBP-1; Bact pon	Bact mrcA	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).	.	.	MKFVKYFLILAVCCILLGAGSIYGLYRYIEPQLPDVATLKDVRLQIPMQIYSADGELIAQYGEKRRIPVTLDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKEVFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLNEMAVIAGLPKAPSTFNPLYSMDRAVARRNVVLSRMLDEGYITQQQFDQTRTEAINANYHAPEIAFSAPYLSEMVRQEMYNRYGESAYEDGYRIYTTITRKVQQAAQQAVRNNVLDYDMRHGYRGPANVLWKVGESAWDNNKITDTLKALPTYGPLLPAAVTSANPQQATAMLADGSTVALSMEGVRWARPYRSDTQQGPTPRKVTDVLQTGQQIWVRQVGDAWWLAQVPEVNSALVSINPQNGAVMALVGGFDFNQSKFNRATQALRQVGSNIKPFLYTAAMDKGLTLASMLNDVPISRWDASAGSDWQPKNSPPQYAGPIRLRQGLGQSKNVVMVRAMRAMGVDYAAEYLQRFGFPAQNIVHTESLALGSASFTPMQVARGYAVMANGGFLVDPWFISKIENDQGGVIFEAKPKVACPECDIPVIYGDTQKSNVLENNDVEDVAISREQQNVSVPMPQLEQANQALVAKTGAQEYAPHVINTPLAFLIKSALNTNIFGEPGWQGTGWRAGRDLQRRDIGGKTGTTNSSKDAWFSGYGPGVVTSVWIGFDDHRRNLGHTTASGAIKDQISGYEGGAKSAQPAWDAYMKAVLEGVPEQPLTPPPGIVTVNIDRSTGQLANGGNSREEYFIEGTQPTQQAVHEVGTTIIDNGEAQELF	Clinical trial	"Overexpression, purification and biochemical characterization of a class A high-molecular-mass penicillin-binding protein (PBP), PBP1* and its soluble derivative from Mycobacterium tuberculosis. Biochem J. 2002 Feb 1;361(Pt 3):635-9."	25	.	.	.	.	.	.	.	.	.	.	ecj00550: Peptidoglycan biosynthesis; ecj01100: Metabolic pathways; ecj01501: beta-Lactam resistance	.	EcoCyc:EG10748-MON; MetaCyc:EG10748-MON	P02918
TT329FH	Bacterial Penicillin-binding protein 1B (Bact mrcB)	P02919	PBPB_ECOLI	Acyltransferase	mrcB; PBP1b; PBP-1b; PBP 1b; Murein polymerase	Bact mrcB	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).	.	6G5R; 6FZK; 5HLD; 5HLB; 5HLA	MAGNDREPIGRKGKPTRPVKQKVSRRRYEDDDDYDDYDDYEDEEPMPRKGKGKGKGRKPRGKRGWLWLLLKLAIVFAVLIAIYGVYLDQKIRSRIDGKVWQLPAAVYGRMVNLEPDMTISKNEMVKLLEATQYRQVSKMTRPGEFTVQANSIEMIRRPFDFPDSKEGQVRARLTFDGDHLATIVNMENNRQFGFFRLDPRLITMISSPNGEQRLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGASTLTQQLVKNLFLSSERSYWRKANEAYMALIMDARYSKDRILELYMNEVYLGQSGDNEIRGFPLASLYYFGRPVEELSLDQQALLVGMVKGASIYNPWRNPKLALERRNLVLRLLQQQQIIDQELYDMLSARPLGVQPRGGVISPQPAFMQLVRQELQAKLGDKVKDLSGVKIFTTFDSVAQDAAEKAAVEGIPALKKQRKLSDLETAIVVVDRFSGEVRAMVGGSEPQFAGYNRAMQARRSIGSLAKPATYLTALSQPKIYRLNTWIADAPIALRQPNGQVWSPQNDDRRYSESGRVMLVDALTRSMNVPTVNLGMALGLPAVTETWIKLGVPKDQLHPVPAMLLGALNLTPIEVAQAFQTIASGGNRAPLSALRSVIAEDGKVLYQSFPQAERAVPAQAAYLTLWTMQQVVQRGTGRQLGAKYPNLHLAGKTGTTNNNVDTWFAGIDGSTVTITWVGRDNNQPTKLYGASGAMSIYQRYLANQTPTPLNLVPPEDIADMGVDYDGNFVCSGGMRILPVWTSDPQSLCQQSEMQQQPSGNPFDQSSQPQQQPQQQPAQQEQKDSDGVAGWIKDMFGSN	Literature-reported	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	0	.	.	.	.	.	.	.	.	.	.	ecj00550: Peptidoglycan biosynthesis; ecj01100: Metabolic pathways	.	EcoCyc:EG10605-MON; MetaCyc:EG10605-MON	P02919
TTHWB7G	Bacterial Penicillin binding protein 2 (Bact mrdA)	P0AD65	MRDA_ECOLI	.	PBP-2	Bact mrdA	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.	EC 3.4.16.4	6G9S	MKLQNSFRDYTAESALFVRRALVAFLGILLLTGVLIANLYNLQIVRFTDYQTRSNENRIKLVPIAPSRGIIYDRNGIPLALNRTIYQIEMMPEKVDNVQQTLDALRSVVDLTDDDIAAFRKERARSHRFTSIPVKTNLTEVQVARFAVNQYRFPGVEVKGYKRRYYPYGSALTHVIGYVSKINDKDVERLNNDGKLANYAATHDIGKLGIERYYEDVLHGQTGYEEVEVNNRGRVIRQLKEVPPQAGHDIYLTLDLKLQQYIETLLAGSRAAVVVTDPRTGGVLALVSTPSYDPNLFVDGISSKDYSALLNDPNTPLVNRATQGVYPPASTVKPYVAVSALSAGVITRNTTLFDPGWWQLPGSEKRYRDWKKWGHGRLNVTRSLEESADTFFYQVAYDMGIDRLSEWMGKFGYGHYTGIDLAEERSGNMPTREWKQKRFKKPWYQGDTIPVGIGQGYWTATPIQMSKALMILINDGIVKVPHLLMSTAEDGKQVPWVQPHEPPVGDIHSGYWELAKDGMYGVANRPNGTAHKYFASAPYKIAAKSGTAQVFGLKANETYNAHKIAERLRDHKLMTAFAPYNNPQVAVAMILENGGAGPAVGTLMRQILDHIMLGDNNTDLPAENPAVAAAEDH	Successful	A comparative trial of imipenem versus ceftazidime in the release of endotoxin and cytokine generation in patients with gram-negative urosepsis. Urosepsis Study Group. J Endotoxin Res. 2000;6(1):25-31.	34	.	.	.	.	.	.	.	.	.	.	ecj00550: Peptidoglycan biosynthesis; ecj01100: Metabolic pathways; ecj01501: beta-Lactam resistance	.	EcoCyc:EG10606-MON; MetaCyc:EG10606-MON	P0AD65
TTFSX6G	Bacterial MTA/SAH nucleosidase (Bact mtnN)	P0AF12	MTNN_ECOLI	Glycosylase	mtnN; S-adenosylhomocysteine nucleosidase; P46; 5'-methylthioadenosine nucleosidase; 5'-Methylthioadenosine/S-adenosylhomocysteine (MTA/AdoHcy) nucleosidase	Bact mtnN	"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."	.	4YML; 4WKC; 3O4V; 1Z5P; 1Z5O	MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	ecj00270: Cysteine and methionine metabolism; ecj01100: Metabolic pathways; ecj01230: Biosynthesis of amino acids	.	EcoCyc:EG11090-MON; MetaCyc:EG11090-MON	P0AF12
TTICX3S	Bacterial UDP-N-acetylglucosamine carboxyvinyltransferase (Bact murA)	P0A749	MURA_ECOLI	Alkyl aryl transferase	UDP-N-acetylglucosamine enolpyruvyl transferase; UDP-GlcNAcenolpyruvyl transferase; MurA protein; MurA; Enoylpyruvate transferase; EPT	Bact murA	Cell wall formation. Adds enolpyruvyl to UDP-n- acetylglucosamine. Target for the antibiotic phosphomycin.	.	3SWD; 3KR6; 3KQJ; 3ISS; 2Z2C	MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNGSVHIDARDVNVFCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVMDKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLVAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAEGTGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRALGANIERVKGE	Successful	Evidence that the fosfomycin target Cys115 in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release. J Biol Chem. 2005 Feb 4;280(5):3757-63.	34	.	.	.	.	.	.	.	.	.	.	ecj00520: Amino sugar and nucleotide sugar metabolism; ecj00550: Peptidoglycan biosynthesis; ecj01100: Metabolic pathways; ecj01250: Biosynthesis of nucleotide sugars	.	EcoCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MON; MetaCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MON	P0A749
TTAEOJ4	Bacterial UDP-N-acetylenolpyruvylglucosamine reductase (Bact murB)	P08373	MURB_ECOLI	Short-chain dehydrogenases reductase	UDP-N-acetylmuramate dehydrogenase; MurB	Bact murB	Cell wall formation.	.	2Q85; 2MBR; 1UXY; 1MBT; 1MBB	MNHSLKPWNTFGIDHNAQHIVCAEDEQQLLNAWQYATAEGQPVLILGEGSNVLFLEDYRGTVIINRIKGIEIHDEPDAWYLHVGAGENWHRLVKYTLQEGMPGLENLALIPGCVGSSPIQNIGAYGVELQRVCAYVDSVELATGKQVRLTAKECRFGYRDSIFKHEYQDRFAIVAVGLRLPKEWQPVLTYGDLTRLDPTTVTPQQVFNAVCHMRTTKLPDPKVNGNAGSFFKNPVVSAETAKALLSQFPTAPNYPQADGSVKLAAGWLIDQCQLKGMQIGGAAVHRQQALVLINEDNAKSEDVVQLAHHVRQKVGEKFNVWLEPEVRFIGASGEVSAVETIS	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	ecj00520: Amino sugar and nucleotide sugar metabolism; ecj00550: Peptidoglycan biosynthesis; ecj01100: Metabolic pathways; ecj01250: Biosynthesis of nucleotide sugars	.	EcoCyc:UDPNACETYLMURAMATEDEHYDROG-MON; MetaCyc:UDPNACETYLMURAMATEDEHYDROG-MON	P08373
TTP8UCK	Bacterial Glycosyltransferase MurG (Bact murG)	P17443	MURG_ECOLI	Hexosyltransferase	Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase; MurG	Bact murG	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).	EC 2.4.1.227	1NLM; 1F0K	MSGQGKRLMVMAGGTGGHVFPGLAVAHHLMAQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGIKALIAAPLRIFNAWRQARAIMKAYKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGAFPNAEVVGNPVRTDVLALPLPQQRLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDSVTIWHQSGKGSQQSVEQAYAEAGQPQHKVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHKDRQQYWNALPLEKAGAAKIIEQPQLSVDAVANTLAGWSRETLLTMAERARAASIPDATERVANEVSRVARA	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	ecj00550: Peptidoglycan biosynthesis; ecj01100: Metabolic pathways; ecj01502: Vancomycin resistance	.	EcoCyc:NACGLCTRANS-MON; MetaCyc:NACGLCTRANS-MON	P17443
TT1NFO3	Bacterial Nicotinate-nucleotide adenylyltransferase (Bact nadD)	P0A752	NADD_ECOLI	Kinase	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)	Bact nadD	Catalyzes the reversible adenylation of nicotinate mononucleotide (namn) to nicotinic acid adenine dinucleotide (naad).	EC 2.7.7.18	1K4M; 1K4K	MKSLQALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRPQPEANSVQRKHMLELAIADKPLFTLDERELKRNAPSYTAQTLKEWRQEQGPDVPLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPLEMAQPQYQQWLEDHLTHNPEDLHLQPAGKIYLAETPWFNISATIIRERLQNGESCEDLLPEPVLTYINQQGLYR	Patented-recorded	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	ecj00760: Nicotinate and nicotinamide metabolism; ecj01100: Metabolic pathways; ecj01240: Biosynthesis of cofactors	.	EcoCyc:NICONUCADENYLYLTRAN-MON; MetaCyc:NICONUCADENYLYLTRAN-MON	P0A752
TT8WCXO	Bacterial NH(3)-dependent NAD(+) synthetase (Bact nadE)	P18843	NADE_ECOLI	Carbon-nitrogen ligase	efg; Nitrogen-regulatory protein; Nicotinamide adenine dinucleotide synthetase; NadE; NAD+ synthetase; NAD+ synthase; NAD(+)-synthetase; NAD synthetase; NAD synthase; Diphosphopyridine nucleotide synthetase	Bact nadE	"Catalyzes a keystep in NAD biosynthesis, transforming deamido-NAD into NAD by a two-step reaction."	.	1WXI; 1WXH; 1WXG; 1WXF; 1WXE	MTLQQQIIKALGAKPQINAEEEIRRSVDFLKSYLQTYPFIKSLVLGISGGQDSTLAGKLCQMAINELRLETGNESLQFIAVRLPYGVQADEQDCQDAIAFIQPDRVLTVNIKGAVLASEQALREAGIELSDFVRGNEKARERMKAQYSIAGMTSGVVVGTDHAAEAITGFFTKYGDGGTDINPLYRLNKRQGKQLLAALACPEHLYKKAPTADLEDDRPSLPDEVALGVTYDNIDDYLEGKNVPQQVARTIENWYLKTEHKRRPPITVFDDFWKK	Literature-reported	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	0	.	.	.	.	.	.	.	.	.	.	ecj00760: Nicotinate and nicotinamide metabolism; ecj01100: Metabolic pathways; ecj01240: Biosynthesis of cofactors	.	EcoCyc:NAD-SYNTH-MON; MetaCyc:NAD-SYNTH-MON	P18843
TTCFSA1	Bacterial Trehalose-phosphatase (Bact otsB)	P31678	OTSB_ECOLI	Phosphoric monoester hydrolase	otsB; Trehalose-6-phosphate phosphatase; Trehalose 6-phosphate phosphatase; TPP	Bact otsB	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).	.	.	MTEPLTETPELSAKYAWFFDLDGTLAEIKPHPDQVVVPDNILQGLQLLATASDGALALISGRSMVELDALAKPYRFPLAGVHGAERRDINGKTHIVHLPDAIARDISVQLHTVIAQYPGAELEAKGMAFALHYRQAPQHEDALMTLAQRITQIWPQMALQQGKCVVEIKPRGTSKGEAIAAFMQEAPFIGRTPVFLGDDLTDESGFAVVNRLGGMSVKIGTGATQASWRLAGVPDVWSWLEMITTALQQKRENNRSDDYESFSRSI	Literature-reported	Disruption of the Candida albicans TPS2 gene encoding trehalose-6-phosphate phosphatase decreases infectivity without affecting hypha formation. Infect Immun. 2002 Apr;70(4):1772-82.	.	.	.	.	.	.	.	.	.	.	.	ecj00500: Starch and sucrose metabolism; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites	.	EcoCyc:TREHALOSEPHOSPHASYN-MON; MetaCyc:TREHALOSEPHOSPHASYN-MON	P31678
TT3YGCD	Bacterial Protective antigen (Bact pagA)	P13423	PAG_BACAN	Bacillus anthracis protective antigen	pagA; PA of Bacillus anthracis; Bacterial toxins translocating protein; Bacterial anthracis protective antigen; Bact PA83; Bact PA-83	Bact pagA	"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."	.	5FR3; 4NAM; 4H2A; 4EE2; 3TEZ	MKKRKVLIPLMALSTILVSSTGNLEVIQAEVKQENRLLNESESSSQGLLGYYFSDLNFQAPMVVTSSTTGDLSIPSSELENIPSENQYFQSAIWSGFIKVKKSDEYTFATSADNHVTMWVDDQEVINKASNSNKIRLEKGRLYQIKIQYQRENPTEKGLDFKLYWTDSQNKKEVISSDNLQLPELKQKSSNSRKKRSTSAGPTVPDRDNDGIPDSLEVEGYTVDVKNKRTFLSPWISNIHEKKGLTKYKSSPEKWSTASDPYSDFEKVTGRIDKNVSPEARHPLVAAYPIVHVDMENIILSKNEDQSTQNTDSQTRTISKNTSTSRTHTSEVHGNAEVHASFFDIGGSVSAGFSNSNSSTVAIDHSLSLAGERTWAETMGLNTADTARLNANIRYVNTGTAPIYNVLPTTSLVLGKNQTLATIKAKENQLSQILAPNNYYPSKNLAPIALNAQDDFSSTPITMNYNQFLELEKTKQLRLDTDQVYGNIATYNFENGRVRVDTGSNWSEVLPQIQETTARIIFNGKDLNLVERRIAAVNPSDPLETTKPDMTLKEALKIAFGFNEPNGNLQYQGKDITEFDFNFDQQTSQNIKNQLAELNATNIYTVLDKIKLNAKMNILIRDKRFHYDRNNIAVGADESVVKEAHREVINSSTEGLLLNIDKDIRKILSGYIVEIEDTEGLKEVINDRYDMLNISSLRQDGKTFIDFKKYNDKLPLYISNPNYKVNVYAVTKENTIINPSENGDTSTNGIKKILIFSKKGYEIG	Successful	"Modulation of innate and adaptive immune responses by tofacitinib (CP-690,550). J Immunol. 2011 Apr 1;186(7):4234-43."	34	.	.	.	.	.	.	.	.	.	.	bar04621: NOD-like receptor signaling pathway	R-HSA-5210891:Uptake and function of anthrax toxins	.	P13423
TTFK8YB	Bacterial DNA topoisomerase 4A (Bact parC)	P0AFI2	PARC_ECOLI	Topoisomerase GyrA ParC	parC; Topoisomerase IV subunit A of Escherichia coli	Bact parC	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.	EC 5.6.2.3	4MN4; 1ZVU; 1ZVT	MSDMAERLALHEFTENAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNASAKFKKSARTVGDVLGKYHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKYSELLLSELGQGTADWVPNFDGTLQEPKMLPARLPNILLNGTTGIAVGMATDIPPHNLREVAQAAIALIDQPKTTLDQLLDIVQGPDYPTEAEIITSRAEIRKIYENGRGSVRMRAVWKKEDGAVVISALPHQVSGARVLEQIAAQMRNKKLPMVDDLRDESDHENPTRLVIVPRSNRVDMDQVMNHLFATTDLEKSYRINLNMIGLDGRPAVKNLLEILSEWLVFRRDTVRRRLNYRLEKVLKRLHILEGLLVAFLNIDEVIEIIRNEDEPKPALMSRFGLTETQAEAILELKLRHLAKLEEMKIRGEQSELEKERDQLQGILASERKMNNLLKKELQADAQAYGDDRRSPLQEREEAKAMSEHDMLPSEPVTIVLSQMGWVRSAKGHDIDAPGLNYKAGDSFKAAVKGKSNQPVVFVDSTGRSYAIDPITLPSARGQGEPLTGKLTLPPGATVDHMLMESDDQKLLMASDAGYGFVCTFNDLVARNRAGKALITLPENAHVMPPVVIEDASDMLLAITQAGRMLMFPVSDLPQLSKGKGNKIINIPSAEAARGEDGLAQLYVLPPQSTLTIHVGKRKIKLRPEELQKVTGERGRRGTLMRGLQRIDRVEIDSPRRASSGDSEE	Successful	Isothiazoloquinolones containing functionalized aromatic hydrocarbons at the 7-position: synthesis and in vitro activity of a series of potent anti... Bioorg Med Chem Lett. 2006 Mar 1;16(5):1272-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	EcoCyc:EG10686-MON	P0AFI2
TTHB48R	Bacterial Pyridoxal phosphate biosynthetic pdxJ (Bact pdxJ)	P0A794	PDXJ_ECOLI	.	pdxJ; Pyridoxine 5'-phosphate synthase; PNP synthase	Bact pdxJ	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).	EC 2.6.99.2	1M5W; 1IXQ; 1IXP; 1IXO; 1IXN	MAELLLGVNIDHIATLRNARGTAYPDPVQAAFIAEQAGADGITVHLREDRRHITDRDVRILRQTLDTRMNLEMAVTEEMLAIAVETKPHFCCLVPEKRQEVTTEGGLDVAGQRDKMRDACKRLADAGIQVSLFIDADEEQIKAAAEVGAPFIEIHTGCYADAKTDAEQAQELARIAKAATFAASLGLKVNAGHGLTYHNVKAIAAIPEMHELNIGHAIIGRAVMTGLKDAVAEMKRLMLEARG	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	ecj00750: Vitamin B6 metabolism; ecj01100: Metabolic pathways; ecj01240: Biosynthesis of cofactors	.	EcoCyc:PDXJ-MON; MetaCyc:PDXJ-MON	P0A794
TTM2E7C	Bacterial Plasminogen activator (Bact pla)	P17811	COLY_YERPE	Peptidase	pla; Coagulase/fibrinolysin	Bact pla	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.	EC 3.4.23.48	4DCB; 2X56; 2X55; 2X4M	MKKSSIVATIITILSGSANAASSQLIPNISPDSFTVAASTGMLSGKSHEMLYDAETGRKISQLDWKIKNVAILKGDISWDPYSFLTLNARGWTSLASGSGNMDDYDWMNENQSEWTDHSSHPATNVNHANEYDLNVKGWLLQDENYKAGITAGYQETRFSWTATGGSYSYNNGAYTGNFPKGVRVIGYNQRFSMPYIGLAGQYRINDFELNALFKFSDWVRAHDNDEHYMRDLTFREKTSGSRYYGTVINAGYYVTPNAKVFAEFTYSKYDEGKGGTQTIDKNSGDSVSIGGDAAGISNKNYTVTAGLQYRF	Literature-reported	Plasminogen activator inhibitor-1 in patients with Kawasaki disease: diagnostic value for the prediction of coronary artery lesion and implication ... Pediatr Res. 2003 Jun;53(6):983-8.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P17811
TT6ERZB	Bacterial Phosphatidylcholine-specificphospholipase C (Bact plcN)	Q9RGS8	PHLN_BURPS	Phosphoric diester hydrolase	plcN; Phosphatidylcholine-hydrolyzing phospholipase C; Phosphatidylcholine cholinephosphohydrolase; PLC-N; PC-PLC; Non-hemolytic phospholipase C; Lecithinase	Bact plcN	Hydrolyzes phosphatidylserine as well as phosphatidylcholine.	.	.	MTNQNRRDFLRLAAGTAGAAALQLFPPVIREALAIPANRRTGTIRDVEHIVILMQENRSFDHYFGKLRGVRGFGDPRPLALQNGKSVFHQPVLLGPAELLPFHPDASNLGMQFLQDLPHGWQDMHGAWNKGRYDRWIANKGTTTMAYLERDDIPFHYQLADAFTICDAYHCSIPSSTDPNRYYMWTGYVGNDGAGGGPVLGNEEAGYGWSTYPETLEQAGVSWKIYQDIGTGLDAAGSWGWTQNPYIGNYGDNSLLYFNQYRNAQPGSPLYDKARTGTNVSAGGTLFDVLQQDVKNGTLPQVSWICAPEAYSEHPNWPANYGAWYVEQVLKALTSNPDVWSKTALFITYDENDGFFDHVAPPFAPQSRENGLSTVSTAGEIFAGDATHMAGPYGLGPRVPMLVVSPWTKGGWVCSQTFDHTSLLQFIEARFNDRYSVRAPNVTPWRRAVCGDLTSAFNFSSPDGSWPQLPDTSGYAPPDRNRHPSYVPVPPAAQSMPKQEAGLRAARALPYELFVLGRIDQSTGKFKLTFANTGRAGAAFQVTAGNRLDGPWAYTVEARKRLSDEWSTALTLSIYDLTVYGPNGFLCQFRGSTAAALGLSANPEVIYGYDVANGNITLRLSNRGRAAVRLTVTNAYGNAAPRVYELKPGQRINDYWDLRDSHSWYDLSVSDGAPNGFLRRFAGHVETGRPSTSDPLIATA	Literature-reported	"Function of the p55 tumor necrosis factor receptor ""death domain"" mediated by phosphatidylcholine-specific phospholipase C. J Exp Med. 1996 Aug 1;184(2):725-33."	0	.	.	.	.	.	.	.	.	.	.	bps00562: Inositol phosphate metabolism; bps00564: Glycerophospholipid metabolism; bps01100: Metabolic pathways; bps01110: Biosynthesis of secondary metabolites; bps02024: Quorum sensing	.	.	Q9RGS8
TTO4NP3	Bacterial Serine/threonine protein phosphatase 1 (Bact pphA)	P55798	PRP1_ECOLI	Phosphoric monoester hydrolase	pphA; Nuclear PP1	Bact pphA	"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."	.	.	MKQPAPVYQRIAGHQWRHIWLSGDIHGCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPQSLRCLQLLEQHWVCAVRGNHEQMAMDALASQQMSLWLMNGGDWFIALADNQQKQAKTALEKCQHLPFILEVHSRTGKHVIAHADYPDDVYEWQKDVDLHQVLWSRSRLGERQKGQGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ	Literature-reported	Nuclear protein phosphatase-1 regulates HIV-1 transcription. J Biol Chem. 2003 Aug 22;278(34):32189-94.	.	.	.	.	.	.	.	.	.	.	.	.	.	EcoCyc:G7011-MON; MetaCyc:G7011-MON	P55798
TTA3F9Z	Bacterial Phosphoenolpyruvate synthase (Bact ppsA)	P56070	PPSA_HELPY	Kinase	"ppsA; Pyruvate,water dikinase; Pyruvate, water dikinase; PEP synthase"	Bact ppsA	Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.	.	.	MRYIKFFKELNNKNVNLVGGKNASIGEMFQELVPIGIKVPDGFAITSEAYWYLLEQGGAKQKIIELLENVDATEIDVLKIRSKQIRELIFGTPFPSDLRDEIFQAYEILSQQYHMKEADVAVRSSATAEDLPDASFAGQQDTYLNIKGKTELIHYIKSCLASLFTDRAISYRASRGFDHLKVALSVGVQKMVRADKGSAGVMFSIDTETGFKDAVFITSAWGLGENVVGGTINPDEFYVFKPTLEQNKRPIIKRQLGNKTQKMVYAPRGSEHPTRNIKTTKKEWQSFSLSDEDVLILAKYAIEIEKHYSKEAKQYRPMDIEWAKDGESGEIFIVQARPETVQSQKSKEESQVFEKFKFKNPNEKKEIILQGRAIGSKIGSGKVRIINDLEHMNSFKEGEILVTDNTDPDWEPCMKKASAVITNRGGRTCHAAIVAREIGVPAIVGVSGATDSLYTGMEITVSCAEGEEGYVYAGIYEHEIERVELSNMQETQTKIYINIGNPEKAFGFSQLPNHGVGLARMEMIILNQIKAHPLALVDLHHKKSVKEKNEIENLMAGYANPKDFFVKKIAEGIGMISAAFYPKPVIVRTSDFKSNEYMRMLGGSSYEPNEENPMLGYRGASRYYSESYNEAFSWECEALALVREEMGLTNMKVMIPFLRTIEEGKKVLEILRKNNLESGKNGLEIYIMCELPVNVILADDFLSLFDGFSIGSNDLTQLTLGVDRDSELVSHVFDERNEAMLKMFKKAIEACKRHNKYCGICGQAPSDYPEVTEFLVKEGITSISLNPDSVIPTWNAVAKLEKELKEHGLTEH	Literature-reported	Beyond complete genomes: from sequence to structure and function. Curr Opin Struct Biol. 1998 Jun;8(3):355-63.	.	.	.	.	.	.	.	.	.	.	.	hpy00010: Glycolysis / Gluconeogenesis; hpy00620: Pyruvate metabolism; hpy00680: Methane metabolism; hpy01100: Metabolic pathways; hpy01110: Biosynthesis of secondary metabolites; hpy01120: Microbial metabolism in diverse environments; hpy01200: Carbon metabolism	.	.	P56070
TTJW9OF	Bacterial Protease II (Bact ptrB)	P24555	PTRB_ECOLI	Peptidase	ptrB; Oligopeptidase B	Bact ptrB	Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues.	EC 3.4.21.83	.	MLPKAARIPHAMTLHGDTRIDNYYWLRDDTRSQPEVLDYLQQENSYGHRVMASQQALQDRILKEIIDRIPQREVSAPYIKNGYRYRHIYEPGCEYAIYQRQSAFSEEWDEWETLLDANKRAAHSEFYSMGGMAITPDNTIMALAEDFLSRRQYGIRFRNLETGNWYPELLDNVEPSFVWANDSWIFYYVRKHPVTLLPYQVWRHAIGTPASQDKLIYEEKDDTYYVSLHKTTSKHYVVIHLASATTSEVRLLDAEMADAEPFVFLPRRKDHEYSLDHYQHRFYLRSNRHGKNFGLYRTRMRDEQQWEELIPPRENIMLEGFTLFTDWLVVEERQRGLTSLRQINRKTREVIGIAFDDPAYVTWIAYNPEPETARLRYGYSSMTTPDTLFELDMDTGERRVLKQTEVPGFYAANYRSEHLWIVARDGVEVPVSLVYHRKHFRKGHNPLLVYGYGSYGASIDADFSFSRLSLLDRGFVYAIVHVRGGGELGQQWYEDGKFLKKKNTFNDYLDACDALLKLGYGSPSLCYAMGGSAGGMLMGVAINQRPELFHGVIAQVPFVDVVTTMLDESIPLTTGEFEEWGNPQDPQYYEYMKSYSPYDNVTAQAYPHLLVTTGLHDSQVQYWEPAKWVAKLRELKTDDHLLLLCTDMDSGHGGKSGRFKSYEGVAMEYAFLVALAQGTLPATPAD	Literature-reported	"Role of the oxyanion binding site and subsites S1 and S2 in the catalysis of oligopeptidase B, a novel target for antimicrobial chemotherapy. Biochemistry. 2002 Mar 26;41(12):4096-106."	.	.	.	.	.	.	.	.	.	.	.	.	.	EcoCyc:EG11004-MON; MetaCyc:EG11004-MON	P24555
TTFGVKC	Bacterial Phosphoenolpyruvate transferase (Bact ptsI)	P08839	PT1_ECOLI	Kinase	"ptsI; Phosphotransferase system, enzyme I; Phosphoenolpyruvate-protein phosphotransferase"	Bact ptsI	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).	.	3EZE; 3EZB; 3EZA; 2XDF; 2N5T	MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDDEYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFITDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMRAVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAVAEACGSQAVIVRTMDIGGDKELPYMNFPKEENPFLGWRAIRIAMDRREILRDQLRAILRASAFGKLRIMFPMIISVEEVRALRKEIEIYKQELRDEGKAFDESIEIGVMVETPAAATIARHLAKEVDFFSIGTNDLTQYTLAVDRGNDMISHLYQPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFSMSAISIPRIKKIIRNTNFEDAKVLAEQALAQPTTDELMTLVNKFIEEKTIC	Literature-reported	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	0	.	.	.	.	.	.	.	.	.	.	ecj02060: Phosphotransferase system (PTS)	.	EcoCyc:PTSI-MON; MetaCyc:PTSI-MON	P08839
TTES76Y	Bacterial Sensor protein QseC (Bact QseC)	P40719	QSEC_ECOLI	.	Sensor protein QseC	Bact QseC	Member of a two-component regulatory system QseB/QseC. Activates the flagella regulon by activating transcription of FlhDC. May activate QseB by phosphorylation.	EC 2.7.13.3	3JZ3; 2KSE	MKFTQRLSLRVRLTLIFLILASVTWLLSSFVAWKQTTDNVDELFDTQLMLFAKRLSTLDLNEINAADRMAQTPNRLKHGHVDDDALTFAIFTHDGRMVLNDGDNGEDIPYSYQREGFADGQLVGEDDPWRFVWMTSPDGKYRIVVGQEWEYREDMALAIVAGQLIPWLVALPIMLIIMMVLLGRELAPLNKLALALRMRDPDSEKPLNATGVPSEVRPLVESLNQLFARTHAMMVRERRFTSDAAHELRSPLTALKVQTEVAQLSDDDPQARKKALLQLHSGIDRATRLVDQLLTLSRLDSLDNLQDVAEIPLEDLLQSSVMDIYHTAQQAKIDVRLTLNAHSIKRTGQPLLLSLLVRNLLDNAVRYSPQGSVVDVTLNADNFIVRDNGPGVTPEALARIGERFYRPPGQTATGSGLGLSIVQRIAKLHGMNVEFGNAEQGGFEAKVSW	Literature-reported	The QseC sensor kinase: a bacterial adrenergic receptor. Proc Natl Acad Sci U S A. 2006 Jul 5;103(27):10420-10425.	.	.	.	.	.	.	.	.	.	.	.	ecj02020: Two-component system; ecj02024: Quorum sensing	.	EcoCyc:EG12658-MON	P40719
TTPEFM3	Bacterial Ribosomal ATPase RbbA (Bact rbbA)	P37624	RBBA_ECOLI	.	Ribosome-associated ATPase; Ribosomal bound ATPase	Bact rbbA	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.	.	.	MTHLELVPVPPVAQLAGVSQHYGKTVALNNITLDIPARCMVGLIGPDGVGKSSLLSLISGARVIEQGNVMVLGGDMRDPKHRRDVCPRIAWMPQGLGKNLYHTLSVYENVDFFARLFGHDKAEREVRINELLTSTGLAPFRDRPAGKLSGGMKQKLGLCCALIHDPELLILDEPTTGVDPLSRSQFWDLIDSIRQRQSNMSVLVATAYMEEAERFDWLVAMNAGEVLATGSAEELRQQTQSATLEEAFINLLPQAQRQAHQAVVIPPYQPENAEIAIEARDLTMRFGSFVAVDHVNFRIPRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDPKDIDTRRRVGYMSQAFSLYNELTVRQNLELHARLFHIPEAEIPARVAEMSERFKLNDVEDILPESLPLGIRQRLSLAVAVIHRPEMLILDEPTSGVDPVARDMFWQLMVDLSRQDKVTIFISTHFMNEAERCDRISLMHAGKVLASGTPQELVEKRGAASLEEAFIAYLQEAAGQSNEAEAPPVVHDTTHAPRQGFSLRRLFSYSRREALELRRDPVRSTLALMGTVILMLIMGYGISMDVENLRFAVLDRDQTVSSQAWTLNLSGSRYFIEQPPLTSYDELDRRMRAGDITVAIEIPPNFGRDIARGTPVELGVWIDGAMPSRAETVKGYVQAMHQSWLQDVASRQSTPASQSGLMNIETRYRYNPDVKSLPAIVPAVIPLLLMMIPSMLSALSVVREKELGSIINLYVTPTTRSEFLLGKQLPYIALGMLNFFLLCGLSVFVFGVPHKGSFLTLTLAALLYIIIATGMGLLISTFMKSQIAAIFGTAIITLIPATQFSGMIDPVASLEGPGRWIGEVYPTSHFLTIARGTFSKALDLTDLWQLFIPLLIAIPLVMGLSILLLKKQEG	Literature-reported	A ribosomal ATPase is a target for hygromycin B inhibition on Escherichia coli ribosomes. Antimicrob Agents Chemother. 2001 Oct;45(10):2813-9.	0	.	.	.	.	.	.	.	.	.	.	.	.	EcoCyc:YHIH-MON	P37624
TTTKXDL	Bacterial Dihydroxy-2-butanone-4-phosphate synthase (Bact ribB)	P0A7J0	RIBB_ECOLI	DHBP synthase family	RibB; DHBP synthase	Bact ribB	"Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate."	EC 4.1.99.12	1IEZ; 1G58; 1G57	MNQTLLSSFGTPFERVENALAALREGRGVMVLDDEDRENEGDMIFPAETMTVEQMALTIRHGSGIVCLCITEDRRKQLDLPMMVENNTSAYGTGFTVTIEAAEGVTTGVSAADRITTVRAAIADGAKPSDLNRPGHVFPLRAQAGGVLTRGGHTEATIDLMTLAGFKPAGVLCELTNDDGTMARAPECIEFANKHNMALVTIEDLVAYRQAHERKAS	Literature-reported	"Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase of riboflavin biosynthesis. Structure. 2001 Jan 10;9(1):11-8."	.	.	.	.	.	.	.	.	.	.	.	ecj00740: Riboflavin metabolism; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01240: Biosynthesis of cofactors	.	EcoCyc:DIOHBUTANONEPSYN-MON; MetaCyc:DIOHBUTANONEPSYN-MON	P0A7J0
TTW6MYZ	Bacterial DNA-directed RNA polymerase beta' (Bact rpoC)	Q2G0N5	RPOC_STAA8	Nucleotidyltransferase	rpoC; Transcriptase subunit beta'; RNAP subunit beta'; RNA polymerasesubunit beta'; DNAdirected RNA polymerase subunit beta'	Bact rpoC	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	EC 2.7.7.6	.	MIDVNNFHYMKIGLASPEKIRSWSFGEVKKPETINYRTLKPEKDGLFCERIFGPTKDWECSCGKYKRVRYKGMVCDRCGVEVTKSKVRRERMGHIELAAPVSHIWYFKGIPSRMGLLLDMSPRALEEVIYFASYVVVDPGPTGLEKKTLLSEAEFRDYYDKYPGQFVAKMGAEGIKDLLEEIDLDEELKLLRDELESATGQRLTRAIKRLEVVESFRNSGNKPSWMILDVLPIIPPEIRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLLDLGAPGIIVQNEKRMLQEAVDALIDNGRRGRPVTGPGNRPLKSLSHMLKGKQGRFRQNLLGKRVDYSGRSVIAVGPSLKMYQCGLPKEMALELFKPFVMKELVQREIATNIKNAKSKIERMDDEVWDVLEEVIREHPVLLNRAPTLHRLGIQAFEPTLVEGRAIRLHPLVTTAYNADFDGDQMAVHVPLSKEAQAEARMLMLAAQNILNPKDGKPVVTPSQDMVLGNYYLTLERKDAVNTGAIFNNTNEVLKAYANGFVHLHTRIGVHASSFNNPTFTEEQNKKILATSVGKIIFNEIIPDSFAYINEPTQENLERKTPNRYFIDPTTLGEGGLKEYFENEELIEPFNKKFLGNIIAEVFNRFSITDTSMMLDRMKDLGFKFSSKAGITVGVADIVVLPDKQQILDEHEKLVDRITKQFNRGLITEEERYNAVVEIWTDAKDQIQGELMQSLDKTNPIFMMSDSGARGNASNFTQLAGMRGLMAAPSGKIIELPITSSFREGLTVLEYFISTHGARKGLADTALKTADSGYLTRRLVDVAQDVIVREEDCGTDRGLLVSDIKEGTEMIEPFIERIEGRYSKETIRHPETDEIIIRPDELITPEIAKKITDAGIEQMYIRSAFTCNARHGVCEKCYGKNLATGEKVEVGEAVGTIAAQSIGEPGTQLTMRTFHTGGVAGSDITQGLPRIQEIFEARNPKGQAVITEIEGVVEDIKLAKDRQQEIVVKGANETRSYLASGTSRIIVEIGQPVQRGEVLTEGSIEPKNYLSVAGLNATESYLLKEVQKVYRMQGVEIDDKHVEVMVRQMLRKVRIIEAGDTKLLPGSLVDIHNFTDANREAFKHRKRPATAKPVLLGITKASLETESFLSAASFQETTRVLTDAAIKGKRDDLLGLKENVIIGKLIPAGTGMRRYSDVKYEKTAKPVAEVESQTEVTE	Literature-reported	"Rifampicin resistance in Neisseria meningitidis: evidence from a study of sibling strains, description of new mutations and notes on population gen... J Antimicrob Chemother. 1997 Jun;39(6):747-55."	.	.	.	.	.	.	.	.	.	.	.	sao03020: RNA polymerase	.	.	Q2G0N5
TTR6YA2	Bacterial RNA polymerase sigma factor SigA (Bact sigA)	P0A0J0	SIGA_STAA8	.	RNA polymerase sigma factor SigA	Bact sigA	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.	.	4G94; 4G8X; 4G6D	MSDNTVKIKKQTIDPTLTLEDVKKQLIEKGKKEGHLSHEEIAEKLQNFDIDSDQMDDFFDQLNDNDISLVNEKDSSDTDEKLNPSDLSAPPGVKINDPVRMYLKEIGRVNLLSAQEEIELAKRIEQGDEVAKSRLAEANLRLVVSIAKRYVGRGMLFLDLIQEGNMGLIKAVEKFDFNKGFKFSTYATWWIRQAITRAIADQARTIRIPVHMVETINKLIRVQRQLLQDLGRDPAPEEIGEEMDLPAEKVREILKIAQEPVSLETPIGEEDDSHLGDFIEDQEAQSPSDHAAYELLKEQLEDVLDTLTDREENVLRLRFGLDDGRTRTLEEVGKVFGVTRERIRQIEAKALRKLRHPSRSKRLKDFMD	Successful	NCBI report	34	.	.	.	.	.	.	.	.	.	.	sao02040: Flagellar assembly	.	.	P0A0J0
TTOYRQZ	Bacterial Superoxide dismutase Mn (Bact sodA)	P00448	SODM_ECOLI	Superoxide acceptor oxidoreductase	sodA; MnSOD; Mn-SOD; Manganese superoxide dismutase	Bact sodA	Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.	EC 1.15.1.1	3OT7; 3K9S; 1ZLZ; 1VEW; 1MMM	MSYTLPSLPYAYDALEPHFDKQTMEIHHTKHHQTYVNNANAALESLPEFANLPVEELITKLDQLPADKKTVLRNNAGGHANHSLFWKGLKKGTTLQGDLKAAIERDFGSVDNFKAEFEKAAASRFGSGWAWLVLKGDKLAVVSTANQDSPLMGEAISGASGFPIMGLDVWEHAYYLKFQNRRPDYIKEFWNVVNWDEAAARFAAKK	Literature-reported	"Suppression of manganese superoxide dismutase augments sensitivity to radiation, hyperthermia and doxorubicin in colon cancer cell lines by inducin... Br J Cancer. 2000 Oct;83(7):928-34."	.	.	.	.	.	.	.	.	.	.	.	.	.	EcoCyc:SUPEROX-DISMUTMN-MON; MetaCyc:SUPEROX-DISMUTMN-MON	P00448
TT1HYOF	Bacterial Shiga toxin 2 subunit B (Bact stxII)	Q7DJJ2	Q7DJJ2_ECOLX	.	"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"	Bact stxII	"Shiga toxin, one of the most potent bacterial toxins known. Binds to the cellular receptor, globotriaosylceramide, Gb3, found primarily on endothelial cells."	.	4M1U	MKKMFMAVLFALVSVNAMAADCAKGKIEFSKYNEDDTFTVKVDGKEYWTSRWNLQPLLQSAQLTGMTVTIKSSTCESGSGFAEVQFNND	Clinical trial	Antibacterial antibodies gain traction. Nat Rev Drug Discov. 2015 Nov;14(11):737-8. 	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXHT8A	Bacterial Acid phosphatase surE (Bact surE)	P36664	SURE_ECOLI	Phosphoric monoester hydrolase	Stationary-phase survival protein surE; Phosphomonoesterase; Glycerophosphatase; Acid Phosphomonoesterase; Acid Phosphatase	Bact surE	This protein is essential for the survival of e.coli in stationary phase and for survival of heat and osmotic stresses.	.	.	MRILLSNDDGVHAPGIQTLAKALREFADVQVVAPDRNRSGASNSLTLESSLRTFTFENGDIAVQMGTPTDCVYLGVNALMRPRPDIVVSGINAGPNLGDDVIYSGTVAAAMEGRHLGFPALAVSLDGHKHYDTAAAVTCSILRALCKEPLRTGRILNINVPDLPLDQIKGIRVTRCGTRHPADQVIPQQDPRGNTLYWIGPPGGKCDAGPGTDFAAVDEGYVSITPLHVDLTAHSAQDVVSDWLNSVGVGTQW	Literature-reported	Molecular targets of lithium action. Annu Rev Pharmacol Toxicol. 2001;41:789-813.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P0A840
TTNS6X4	Bacterial Triosephosphate isomerase (Bact TPI)	Q07412	TPIS_PLAFA	Intramolecular oxidoreductase	Triose-phosphate isomerase; TPI; TIM	Bact TPI	"identical protein binding, triose-phosphate isomerase activity."	EC 5.3.1.1	5GZP; 5GV4; 5BRB; 5BNK; 5BMX	MARKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTRKLLQSKFSTGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNVILAYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQANQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESFVDIIKSAM	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	EC:5.3	Intramolecular oxidoreductases	triosephosphate isomerase family.	5.3.1.1	Intramolecular oxidoreductases	Triosephosphate isomerase	PF00121	PF00121; TIM	.	.	.	.	.	Q07412
TTQALFH	Bacterial Beta-glucuronidase (Bact uidA)	P05804	BGLR_ECOLI	.	GUS; Beta-D-glucuronoside glucuronosohydrolase	Bact uidA	"cytosol, protein-containing complex, beta-glucuronidase activity, carbohydrate binding, identical protein binding, glucuronoside catabolic process"	EC 3.2.1.31	.	MLRPVETPTREIKKLDGLWAFSLDRENCGIDQRWWESALQESRAIAVPGSFNDQFADADIRNYAGNVWYQREVFIPKGWAGQRIVLRFDAVTHYGKVWVNNQEVMEHQGGYTPFEADVTPYVIAGKSVRITVCVNNELNWQTIPPGMVITDENGKKKQSYFHDFFNYAGIHRSVMLYTTPNTWVDDITVVTHVAQDCNHASVDWQVVANGDVSVELRDADQQVVATGQGTSGTLQVVNPHLWQPGEGYLYELCVTAKSQTECDIYPLRVGIRSVAVKGEQFLINHKPFYFTGFGRHEDADLRGKGFDNVLMVHDHALMDWIGANSYRTSHYPYAEEMLDWADEHGIVVIDETAAVGFNLSLGIGFEAGNKPKELYSEEAVNGETQQAHLQAIKELIARDKNHPSVVMWSIANEPDTRPQGAREYFAPLAEATRKLDPTRPITCVNVMFCDAHTDTISDLFDVLCLNRYYGWYVQSGDLETAEKVLEKELLAWQEKLHQPIIITEYGVDTLAGLHSMYTDMWSEEYQCAWLDMYHRVFDRVSAVVGEQVWNFADFATSQGILRVGGNKKGIFTRDRKPKSAAFLLQKRWTGMNFGEKPQQGGKQ	Preclinical	Microbiome therapeutics go small molecule. Nat Rev Drug Discov. 2019 Jul;18(8):569-572.	.	.	.	.	.	.	.	.	.	.	.	ecj00040: Pentose and glucuronate interconversions; ecj00053: Ascorbate and aldarate metabolism; ecj00860: Porphyrin metabolism; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01240: Biosynthesis of cofactors	.	EcoCyc:BETA-GLUCURONID-MON; MetaCyc:BETA-GLUCURONID-MON	P05804
TTAS2UO	Bacterial Urease (Bact ureC)	P18314	URE1_KLEAE	Carbon-nitrogen hydrolase	Urease subunit alpha; Urea amidohydrolase subunit alpha	Bact ureC	"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."	.	4EPE; 4EPD; 4EPB; 4EP8; 2KAU	MSNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVIRDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGNPDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQPDALREQVAAGVIGLKIHEDWGATPAAIDCALTVADEMDIQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTLNTIDEHLDMLMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDLGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALAEETGDNDNFRVKRYIAKYTINPALTHGIAHEVGSIEVGKLADLVVWSPAFFGVKPATVIKGGMIAIAPMGDINASIPTPQPVHYRPMFGALGSARHHCRLTFLSQAAAANGVAERLNLRSAIAVVKGCRTVQKADMVHNSLQPNITVDAQTYEVRVDGELITSEPADVLPMAQRYFLF	Successful	"Enzymatic, immunological and phylogenetic characterization of Brucella suis urease. BMC Microbiol. 2008 Jul 19;8:121."	34	.	.	.	.	.	.	.	.	.	.	.	.	.	P18314
TTLP6GN	Bacterial DD-carboxypeptidase (Bact vanYB)	Q47746	VANY_ENTFA	Peptidase	vanYB; DD-peptidase; DD-carboxypeptidase; D-alanyl-D-alanine carboxypeptidase-transpeptidase	Bact vanYB	"Vancomycin-inducible, penicillin-resistant, DD- carboxypeptidase that hydrolyzes depsipeptide- and D-alanyl-D- alanine-containing peptidoglycan precursors. Insensitive to beta- lactams."	EC 3.4.16.4	6A6A; 5ZHW; 5ZHF; 5HNM	MEKSNYHSNVNHHKRHMKQSGEKRAFLWAFIISFTVCTLFLGWRLVSVLEATQLPPIPATHTGSGTGVAENPEENTLATAKEQGDEQEWSLILVNRQNPIPAQYDVELEQLSNGERIDIRISPYLQDLFDAARADGVYPIVASGYRTTEKQQEIMDEKVAEYKAKGYTSAQAKAEAETWVAVPGTSEHQLGLAVDINADGIHSTGNEVYRWLDENSYRFGFIRRYPPDKTEITGVSNEPWHYRYVGIEAATKIYHQGLCLEEYLNTEK	Successful	"Extended-spectrum cephalosporinases: structure, detection and epidemiology. Future Microbiol. 2007 Jun;2:297-307."	34	.	.	.	.	.	.	.	.	.	.	efa00550: Peptidoglycan biosynthesis; efa01100: Metabolic pathways; efa01502: Vancomycin resistance; efa02020: Two-component system	.	.	Q47746
TTTZQOV	Bacterial Purine nucleoside phosphorylase (Bact xapA)	P45563	XAPA_ECOLI	Kinase	Xanthosine phosphorylase; Purine nucleoside phosphorylase II; Purine nucleoside phosphorylase 2; PNP II; Bact Inosine-guanosine phosphorylase	Bact xapA	"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."	EC 2.4.2.1	1YR3; 1YQU; 1YQQ	MSQVQFSHNPLFCIDIIKTYKPDFTPRVAFILGSGLGALADQIENAVAISYEKLPGFPVSTVHGHAGELVLGHLQGVPVVCMKGRGHFYEGRGMTIMTDAIRTFKLLGCELLFCTNAAGSLRPEVGAGSLVALKDHINTMPGTPMVGLNDDRFGERFFSLANAYDAEYRALLQKVAKEEGFPLTEGVFVSYPGPNFETAAEIRMMQIIGGDVVGMSVVPEVISARHCDLKVVAVSAITNMAEGLSDVKLSHAQTLAAAELSKQNFINLICGFLRKIA	Literature-reported	The purine nucleoside phosphorylase from Trichomonas vaginalis is a homologue of the bacterial enzyme. Biochemistry. 2002 Aug 20;41(33):10382-9.	.	.	.	.	.	.	.	.	.	.	.	ecj00230: Purine metabolism; ecj00760: Nicotinate and nicotinamide metabolism; ecj01100: Metabolic pathways; ecj01110: Biosynthesis of secondary metabolites; ecj01232: Nucleotide metabolism	.	EcoCyc:XANTHOSINEPHOSPHORY-MON; MetaCyc:XANTHOSINEPHOSPHORY-MON	P45563
TTC21TJ	Bacterial Endoribonuclease YbeY (Bact YbeY)	P0A898	YBEY_ECOLI	Carboxylic ester hydrolase	ybeY; b0659; JW0656	Bact YbeY	"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."	EC 3.1.-.-	1XM5	MSQVILDLQLACEDNSGLPEESQFQTWLNAVIPQFQEESEVTIRVVDTAESHSLNLTYRGKDKPTNVLSFPFEVPPGMEMSLLGDLVICRQVVEKEAQEQGKPLEAHWAHMVVHGSLHLLGYDHIEDDEAEEMEALETEIMLALGYEDPYIAEKE	Literature-reported	The conserved endoribonuclease YbeY is required for chloroplast ribosomal RNA processing in Arabidopsis. Plant Physiol. 2015 May;168(1):205-21.	.	EC:3.1.1	.	endoribonuclease YbeY family.	3.1.-.- 	Acting on ester bonds	Uncharacterized protein family UPF0054	PF02130	PF02130; UPF0054	.	.	.	.	EcoCyc:G6362-MON	P0A898
TTS5GLJ	B melanoma antigen 1 (BAGE)	Q13072	BAGE1_HUMAN	.	Cancer/testis antigen 2.1; CT2.1; BAGE1; B melanoma antigen; Antigen MZ2BA; Antigen MZ2-BA	BAGE	Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes.	.	.	MAARAVFLALSAQLLQARLMKEESPVVSWRLEPEDGTALCFIF	Literature-reported	"Expression of tumor-specific antigen MAGE, GAGE and BAGE in ovarian cancer tissues and cell lines. BMC Cancer. 2010 Apr 27;10:163."	.	.	.	BAGE family.	.	.	B melanoma antigen family	PF08180	PF08180; BAGE	.	.	.	.	.	Q13072
TT5Z1WV	Adhesion G protein-coupled receptor B1 (BAI1)	O14514	AGRB1_HUMAN	GPCR secretin	Brain-specific angiogenesis inhibitor 1; ADGRB1	BAI1	"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."	.	.	MRGQAAAPGPVWILAPLLLLLLLLGRRARAAAGADAGPGPEPCATLVQGKFFGYFSAAAVFPANASRCSWTLRNPDPRRYTLYMKVAKAPVPCSGPGRVRTYQFDSFLESTRTYLGVESFDEVLRLCDPSAPLAFLQASKQFLQMRRQQPPQHDGLRPRAGPPGPTDDFSVEYLVVGNRNPSRAACQMLCRWLDACLAGSRSSHPCGIMQTPCACLGGEAGGPAAGPLAPRGDVCLRDAVAGGPENCLTSLTQDRGGHGATGGWKLWSLWGECTRDCGGGLQTRTRTCLPAPGVEGGGCEGVLEEGRQCNREACGPAGRTSSRSQSLRSTDARRREELGDELQQFGFPAPQTGDPAAEEWSPWSVCSSTCGEGWQTRTRFCVSSSYSTQCSGPLREQRLCNNSAVCPVHGAWDEWSPWSLCSSTCGRGFRDRTRTCRPPQFGGNPCEGPEKQTKFCNIALCPGRAVDGNWNEWSSWSACSASCSQGRQQRTRECNGPSYGGAECQGHWVETRDCFLQQCPVDGKWQAWASWGSCSVTCGAGSQRRERVCSGPFFGGAACQGPQDEYRQCGTQRCPEPHEICDEDNFGAVIWKETPAGEVAAVRCPRNATGLILRRCELDEEGIAYWEPPTYIRCVSIDYRNIQMMTREHLAKAQRGLPGEGVSEVIQTLVEISQDGTSYSGDLLSTIDVLRNMTEIFRRAYYSPTPGDVQNFVQILSNLLAEENRDKWEEAQLAGPNAKELFRLVEDFVDVIGFRMKDLRDAYQVTDNLVLSIHKLPASGATDISFPMKGWRATGDWAKVPEDRVTVSKSVFSTGLTEADEASVFVVGTVLYRNLGSFLALQRNTTVLNSKVISVTVKPPPRSLRTPLEIEFAHMYNGTTNQTCILWDETDVPSSSAPPQLGPWSWRGCRTVPLDALRTRCLCDRLSTFAILAQLSADANMEKATLPSVTLIVGCGVSSLTLLMLVIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQSYMAVTGHLRNRLIRKRFLCLGWGLPALVVAISVGFTKAKGYSTMNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSKDGITDKKLKERAGASLWSSCVVLPLLALTWMSAVLAVTDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVKCRVVDRQEEGNGDSGGSFQNGHAQLMTDFEKDVDLACRSVLNKDIAACRTATITGTLKRPSLPEEEKLKLAHAKGPPTNFNSLPANVSKLHLHGSPRYPGGPLPDFPNHSLTLKRDKAPKSSFVGDGDIFKKLDSELSRAQEKALDTSYVILPTATATLRPKPKEEPKYSIHIDQMPQTRLIHLSTAPEASLPARSPPSRQPPSGGPPEAPPAQPPPPPPPPPPPPQQPLPPPPNLEPAPPSLGDPGEPAAHPGPSTGPSTKNENVATLSVSSLERRKSRYAELDFEKIMHTRKRHQDMFQDLNRKLQHAAEKDKEVLGPDSKPEKQQTPNKRPWESLRKAHGTPTWVKKELEPLQPSPLELRSVEWERSGATIPLVGQDIIDLQTEV	Literature-reported	BAI1 is an engulfment receptor for apoptotic cells upstream of the ELMO/Dock180/Rac module. Nature. 2007 Nov 15;450(7168):430-4.	0	PF00002	.	G-protein coupled receptor 2 family. LN-TM7 subfamily.	.	.	"7 transmembrane receptor (Secretin family); GPCR-Autoproteolysis INducing (GAIN) domain; GPCR proteolysis site, GPS, motif ; Hormone receptor domain; Thrombospondin type 1 domain"	PF00002; PF16489; PF01825; PF02793; PF00090	PF00002; 7tm_2; PF16489; GAIN; PF01825; GPS; PF02793; HRM; PF00090; TSP_1	.	.	hsa04115: p53 signaling pathway	.	.	O14514
TTFM7V0	Apoptosis regulator BAK (BAK)	Q16611	BAK_HUMAN	B-cell lymphoma Bcl-2	CDN1; Bcl2like protein 7; Bcl2L7; Bcl2-L-7; Bcl2 homologous antagonist/killer; Bcl-2-like protein 7; Bcl-2 homologous antagonist/killer	BAK1	"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."	.	5VX1; 5VX0; 5VWZ; 5VWY; 5VWX	MASGQGPGPPRQECGEPALPSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQLAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGYRLALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNGPILNVLVVLGVVLLGQFVVRRFFKS	Literature-reported	"Novel BCL2 inhibitor, Disarib induces apoptosis by disruption of BCL2-BAK interaction. Biochem Pharmacol. 2017 May 1;131:16-28."	.	TC=1.A.21	Bcl-2 family	Bcl-2 family.	.	.	"Apoptosis regulator proteins, Bcl-2 family"	PF00452	PF00452; Bcl-2	1.A.21.1.3	The Bcl-2 (Bcl-2) Family	hsa01524: Platinum drug resistance; hsa04141: Protein processing in endoplasmic reticulum; hsa04210: Apoptosis; hsa04215: Apoptosis - multiple species; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05130: Pathogenic Escherichia coli infection; hsa05132: Salmonella infection; hsa05160: Hepatitis C; hsa05162: Measles; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; hsa05165: Human papillomavirus infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05200: Pathways in cancer; hsa05202: Transcriptional misregulation in cancer; hsa05203: Viral carcinogenesis; hsa05206: MicroRNAs in cancer; hsa05210: Colorectal cancer; hsa05212: Pancreatic cancer; hsa05213: Endometrial cancer; hsa05214: Glioma; hsa05216: Thyroid cancer; hsa05217: Basal cell carcinoma; hsa05218: Melanoma; hsa05220: Chronic myeloid leukemia; hsa05222: Small cell lung cancer; hsa05223: Non-small cell lung cancer; hsa05224: Breast cancer; hsa05225: Hepatocellular carcinoma; hsa05226: Gastric cancer	R-HSA-111452: Activation and oligomerization of BAK protein; R-HSA-111457: Release of apoptotic factors from the mitochondria; R-HSA-5620971: Pyroptosis	.	Q16611
TT47RXJ	Ubiquitin carboxyl-terminal hydrolase BAP1 (BAP1)	Q92560	BAP1_HUMAN	Peptidase C12 family. BAP1 subfamily	KIAA0272; Cerebral protein 6; BRCA1-associated protein 1	BAP1	"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."	EC 3.4.19.12	.	MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQGPVYGFIFLFKWIEERRSRRKVSTLVDDTSVIDDDIVNNMFFAHQLIPNSCATHALLSVLLNCSSVDLGPTLSRMKDFTKGFSPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGLSAVRTMEAFHFVSYVPITGRLFELDGLKVYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRIKYEARLHVLKVNRQTVLEALQQLIRVTQPELIQTHKSQESQLPEESKSASNKSPLVLEANRAPAASEGNHTDGAEEAAGSCAQAPSHSPPNKPKLVVKPPGSSLNGVHPNPTPIVQRLPAFLDNHNYAKSPMQEEEDLAAGVGRSRVPVRPPQQYSDDEDDYEDDEEDDVQNTNSALRYKGKGTGKPGALSGSADGQLSVLQPNTINVLAEKLKESQKDLSIPLSIKTSSGAGSPAVAVPTHSQPSPTPSNESTDTASEIGSAFNSPLRSPIRSANPTRPSSPVTSHISKVLFGEDDSLLRVDCIRYNRAVRDLGPVISTGLLHLAEDGVLSPLALTEGGKGSSPSIRPIQGSQGSSSPVEKEVVEATDSREKTGMVRPGEPLSGEKYSPKELLALLKCVEAEIANYEACLKEEVEKRKKFKIDDQRRTHNYDEFICTFISMLAQEGMLANLVEQNISVRRRQGVSIGRLHKQRKPDRRKRSRPYKAKRQ	Literature-reported	Ubiquitin carboxyl-terminal hydrolases: involvement in cancer progression and clinical implications. Cancer Metastasis Rev. 2017 Dec;36(4):669-682.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-5689603: UCH proteinases; R-HSA-5693565: Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks	.	Q92560
TTQ57WJ	Apoptosis regulator BAX (BAX)	Q07812	BAX_HUMAN	.	Bcl-2-like protein 4; Bcl2-L-4	BAX	"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."	.	.	MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG	Clinical trial	Apoptosis as a mechanism for the treatment of adult T cell leukemia: promising drugs from benchside to bedside. Drug Discov Today. 2020 Jul;25(7):1189-1197.	.	.	.	.	.	.	.	.	.	.	.	hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa01522: Endocrine resistance; hsa01524: Platinum drug resistance; hsa04071: Sphingolipid signaling pathway; hsa04115: p53 signaling pathway; hsa04141: Protein processing in endoplasmic reticulum; hsa04210: Apoptosis; hsa04211: Longevity regulating pathway; hsa04215: Apoptosis - multiple species; hsa04217: Necroptosis; hsa04722: Neurotrophin signaling pathway; hsa04932: Non-alcoholic fatty liver disease; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa05012: Parkinson disease; hsa05014: Amyotrophic lateral sclerosis; hsa05016: Huntington disease; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05152: Tuberculosis; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05162: Measles; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; hsa05165: Human papillomavirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05200: Pathways in cancer; hsa05202: Transcriptional misregulation in cancer; hsa05203: Viral carcinogenesis; hsa05210: Colorectal cancer; hsa05212: Pancreatic cancer; hsa05213: Endometrial cancer; hsa05214: Glioma; hsa05216: Thyroid cancer; hsa05217: Basal cell carcinoma; hsa05218: Melanoma; hsa05220: Chronic myeloid leukemia; hsa05222: Small cell lung cancer; hsa05223: Non-small cell lung cancer; hsa05224: Breast cancer; hsa05225: Hepatocellular carcinoma; hsa05226: Gastric cancer; hsa05417: Lipid and atherosclerosis	"R-HSA-111457: Release of apoptotic factors from the mitochondria; R-HSA-114294: Activation, translocation and oligomerization of BAX; R-HSA-5620971: Pyroptosis; R-HSA-6803204: TP53 Regulates Transcription of Genes Involved in Cytochrome C Release; R-HSA-6804114: TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest; R-HSA-8878166: Transcriptional regulation by RUNX2; R-HSA-9603505: NTRK3 as a dependence receptor"	.	Q07812
TT2MV0R	Bromodomain adjacent to zinc finger 2A (BAZ2A)	Q9UIF9	BAZ2A_HUMAN	.	hWALp3; Transcription termination factor I-interacting protein 5; Tip5; TTF-I-interacting protein 5; KIAA0314; Bromodomain adjacent to zinc finger domain protein 2A	BAZ2A	"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."	.	6FKP; 6FI0; 6FHU; 6FGW; 6FGV	MEMEANDHFNFTGLPPAPAASGLKPSPSSGEGLYTNGSPMNFPQQGKSLNGDVNVNGLSTVSHTTTSGILNSAPHSSSTSHLHHPSVAYDCLWNYSQYPSANPGSNLKDPPLLSQFSGGQYPLNGILGGSRQPSSPSHNTNLRAGSQEFWANGTQSPMGLNFDSQELYDSFPDQNFEVMPNGPPSFFTSPQTSPMLGSSIQTFAPSQEVGSGIHPDEAAEKEMTSVVAENGTGLVGSLELEEEQPELKMCGYNGSVPSVESLHQEVSVLVPDPTVSCLDDPSHLPDQLEDTPILSEDSLEPFNSLAPEPVSGGLYGIDDTELMGAEDKLPLEDSPVISALDCPSLNNATAFSLLADDSQTSTSIFASPTSPPVLGESVLQDNSFDLNNGSDAEQEEMETQSSDFPPSLTQPAPDQSSTIQLHPATSPAVSPTTSPAVSLVVSPAASPEISPEVCPAASTVVSPAVFSVVSPASSAVLPAVSLEVPLTASVTSPKASPVTSPAAAFPTASPANKDVSSFLETTADVEEITGEGLTASGSGDVMRRRIATPEEVRLPLQHGWRREVRIKKGSHRWQGETWYYGPCGKRMKQFPEVIKYLSRNVVHSVRREHFSFSPRMPVGDFFEERDTPEGLQWVQLSAEEIPSRIQAITGKRGRPRNTEKAKTKEVPKVKRGRGRPPKVKITELLNKTDNRPLKKLEAQETLNEEDKAKIAKSKKKMRQKVQRGECQTTIQGQARNKRKQETKSLKQKEAKKKSKAEKEKGKTKQEKLKEKVKREKKEKVKMKEKEEVTKAKPACKADKTLATQRRLEERQRQQMILEEMKKPTEDMCLTDHQPLPDFSRVPGLTLPSGAFSDCLTIVEFLHSFGKVLGFDPAKDVPSLGVLQEGLLCQGDSLGEVQDLLVRLLKAALHDPGFPSYCQSLKILGEKVSEIPLTRDNVSEILRCFLMAYGVEPALCDRLRTQPFQAQPPQQKAAVLAFLVHELNGSTLIINEIDKTLESMSSYRKNKWIVEGRLRRLKTVLAKRTGRSEVEMEGPEECLGRRRSSRIMEETSGMEEEEEEESIAAVPGRRGRRDGEVDATASSIPELERQIEKLSKRQLFFRKKLLHSSQMLRAVSLGQDRYRRRYWVLPYLAGIFVEGTEGNLVPEEVIKKETDSLKVAAHASLNPALFSMKMELAGSNTTASSPARARGRPRKTKPGSMQPRHLKSPVRGQDSEQPQAQLQPEAQLHAPAQPQPQLQLQLQSHKGFLEQEGSPLSLGQSQHDLSQSAFLSWLSQTQSHSSLLSSSVLTPDSSPGKLDPAPSQPPEEPEPDEAESSPDPQALWFNISAQMPCNAAPTPPPAVSEDQPTPSPQQLASSKPMNRPSAANPCSPVQFSSTPLAGLAPKRRAGDPGEMPQSPTGLGQPKRRGRPPSKFFKQMEQRYLTQLTAQPVPPEMCSGWWWIRDPEMLDAMLKALHPRGIREKALHKHLNKHRDFLQEVCLRPSADPIFEPRQLPAFQEGIMSWSPKEKTYETDLAVLQWVEELEQRVIMSDLQIRGWTCPSPDSTREDLAYCEHLSDSQEDITWRGRGREGLAPQRKTTNPLDLAVMRLAALEQNVERRYLREPLWPTHEVVLEKALLSTPNGAPEGTTTEISYEITPRIRVWRQTLERCRSAAQVCLCLGQLERSIAWEKSVNKVTCLVCRKGDNDEFLLLCDGCDRGCHIYCHRPKMEAVPEGDWFCTVCLAQQVEGEFTQKPGFPKRGQKRKSGYSLNFSEGDGRRRRVLLRGRESPAAGPRYSEEGLSPSKRRRLSMRNHHSDLTFCEIILMEMESHDAAWPFLEPVNPRLVSGYRRIIKNPMDFSTMRERLLRGGYTSSEEFAADALLVFDNCQTFNEDDSEVGKAGHIMRRFFESRWEEFYQGKQANL	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2721).	0	.	.	WAL family.	.	.	"Bromodomain; DDT domain; Methyl-CpG binding domain; PHD-finger; WSTF, HB1, Itc1p, MBD9 motif 1; Williams-Beuren syndrome DDT (WSD), D-TOX E motif"	PF00439; PF02791; PF01429; PF00628; PF15612; PF15613	PF00439; Bromodomain; PF02791; DDT; PF01429; MBD; PF00628; PHD; PF15612; WHIM1; PF15613; WSD	.	.	.	R-HSA-427413: NoRC negatively regulates rRNA expression	.	Q9UIF9
TT6K8YG	Bromodomain adjacent to zinc finger 2B (BAZ2B)	Q9UIF8	BAZ2B_HUMAN	.	hWALp4; KIAA1476; Bromodomain adjacent to zinc finger domain protein 2B	BAZ2B	May play a role in transcriptional regulation interacting with ISWI.	.	6FI1; 6FHQ; 6FH7; 6FH6; 6FGU	MESGERLPSSAASSTTPTSSSTPSVASVVSKGGLSTGVASLSSTINPCGHLFRTAGDQPFNLSTVSSAFPMVSHPVFGLHSASSGHSEFGGLGTLGTPTALAAHPQLASFPGAEWWRTTDAHTRTGATFFPPLLGIPPLFAPPAQNHDSSSFHSRTSGKSNRNGPEKGVNGSINGSNTSSVIGINTSVLSTTASSSMGQTKSTSSGGGNRKCNQEQSKNQPLDARVDKIKDKKPRKKAMESSSNSDSDSGTSSDTSSEGISSSDSDDLEEDEEEEDQSIEESEDDDSDSESEAQHKSNNQVLLHGISDPKADGQKATEKAQEKRIHQPLPLASESQTHSFQSQQKQPQVLSQQLPFIFQSSQAKEESVNKHTSVIQSTGLVSNVKPLSLVNQAKKETYMKLIVPSPDVLKAGNKNTSEESSLLTSELRSKREQYKQAFPSQLKKQESSKSLKKVIAALSNPKATSSSPAHPKQTLENNHPNPFLTNALLGNHQPNGVIQSVIQEAPLALTTKTKMQSKINENIAAASSTPFSSPVNLSTSGRRTPGNQTPVMPSASPILHSQGKEKAVSNNVNPVKTQHHSHPAKSLVEQFRGTDSDIPSSKDSEDSNEDEEEDDEEEDEEDDEDDESDDSQSESDSNSESDTEGSEEEDDDDKDQDESDSDTEGEKTSMKLNKTTSSVKSPSMSLTGHSTPRNLHIAKAPGSAPAALCSESQSPAFLGTSSSTLTSSPHSGTSKRRRVTDERELRIPLEYGWQRETRIRNFGGRLQGEVAYYAPCGKKLRQYPEVIKYLSRNGIMDISRDNFSFSAKIRVGDFYEARDGPQGMQWCLLKEEDVIPRIRAMEGRRGRPPNPDRQRAREESRMRRRKGRPPNVGNAEFLDNADAKLLRKLQAQEIARQAAQIKLLRKLQKQEQARVAKEAKKQQAIMAAEEKRKQKEQIKIMKQQEKIKRIQQIRMEKELRAQQILEAKKKKKEEAANAKLLEAEKRIKEKEMRRQQAVLLKHQERERRRQHMMLMKAMEARKKAEEKERLKQEKRDEKRLNKERKLEQRRLELEMAKELKKPNEDMCLADQKPLPELPRIPGLVLSGSTFSDCLMVVQFLRNFGKVLGFDVNIDVPNLSVLQEGLLNIGDSMGEVQDLLVRLLSAAVCDPGLITGYKAKTALGEHLLNVGVNRDNVSEILQIFMEAHCGQTELTESLKTKAFQAHTPAQKASVLAFLINELACSKSVVSEIDKNIDYMSNLRRDKWVVEGKLRKLRIIHAKKTGKRDTSGGIDLGEEQHPLGTPTPGRKRRRKGGDSDYDDDDDDDSDDQGDEDDEDEEDKEDKKGKKTDICEDEDEGDQAASVEELEKQIEKLSKQQSQYRRKLFDASHSLRSVMFGQDRYRRRYWILPQCGGIFVEGMESGEGLEEIAKEREKLKKAESVQIKEEMFETSGDSLNCSNTDHCEQKEDLKEKDNTNLFLQKPGSFSKLSKLLEVAKMPPESEVMTPKPNAGANGCTLSYQNSGKHSLGSVQSTATQSNVEKADSNNLFNTGSSGPGKFYSPLPNDQLLKTLTEKNRQWFSLLPRTPCDDTSLTHADMSTASLVTPQSQPPSKSPSPTPAPLGSSAQNPVGLNPFALSPLQVKGGVSMMGLQFCGWPTGVVTSNIPFTSSVPSLGSGLGLSEGNGNSFLTSNVASSKSESPVPQNEKATSAQPAAVEVAKPVDFPSPKPIPEEMQFGWWRIIDPEDLKALLKVLHLRGIREKALQKQIQKHLDYITQACLKNKDVAIIELNENEENQVTRDIVENWSVEEQAMEMDLSVLQQVEDLERRVASASLQVKGWMCPEPASEREDLVYFEHKSFTKLCKEHDGEFTGEDESSAHALERKSDNPLDIAVTRLADLERNIERRIEEDIAPGLRVWRRALSEARSAAQVALCIQQLQKSIAWEKSIMKVYCQICRKGDNEELLLLCDGCDKGCHTYCHRPKITTIPDGDWFCPACIAKASGQTLKIKKLHVKGKKTNESKKGKKVTLTGDTEDEDSASTSSSLKRGNKDLKKRKMEENTSINLSKQESFTSVKKPKRDDSKDLALCSMILTEMETHEDAWPFLLPVNLKLVPGYKKVIKKPMDFSTIREKLSSGQYPNLETFALDVRLVFDNCETFNEDDSDIGRAGHNMRKYFEKKWTDTFKVS	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2722).	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9UIF8
TTH1EQO	Bifidobacterium Exo-alpha sialidase (BB sialidase)	A0A151C7Z8	A0A151C7Z8_BIFBI	.	Exo-alpha-sialidase; BB Sialidase	BB sialidase	Involved in the degradation of sialyloligosaccharides in human milk and intestinal glycoconjugates.	EC 3.2.1.18	.	MVRSTKPSLLRRFGALVAAAAMLVVLPAGVSTASAASDDADMLTVTMTRTDALGDEVYVGDTLTYSFTNTNNTSSAFTAFPAESNLSGVLTTGTPNCRYENLAGGASYPCSTASHTITADDLTAGSFTPRTVWKATSDRGGTQVLQDNIVSTGDTVTVKEGKRPDPATIPTDRADGEAVRLATARQNLGTECYRIPALAEAPNGWILAAFDQRPNTAMANGSGVKCWDAPQPNSIVQRISKDGGKSWTPIQYVAQGKNAPERYGYSDPSYVVDKETGEIFLFFVHSYNKGFADSQLGVDESNRNVLHAVVVSSKDNGETWSKPRDITADITKGYENEWKSRFATSGAGIQLKYGKYKGRLIQQYAVGRTTGSNAAVSVYSDDHGKTWQAGNPVTGMLMDENKVVELSDGRVMLNSRPGNGSGYRRVAISEDGGVNYGTVKNETQLPDPNNNAHITRAFPNAPEGSAKAKVLLYSSPRANNEGRANGVVRISLDDGTTWSSGKLYKEGSMAYSVITALSGAAGGGYGLLYEGAWVTGGGIDSHDIMYTHISMDWLGYLSATADDVTASVEEGASTVDVTVPVSNVGSVDYTGVTVTPADLPTGWSASPVNVGALASGTSKDVTVTVNVPATAKKDDVAKIVLRVTGTSAANADATTGFDGSITVNVTEKSEPDPEPEPTITGVSAVTSQAGVKVGDVFDASKVSVTAAMSDGSSKALAAGEYSLSAVDADGKAVDLAEPFAAAGVVTVTVSVPVEGAGPLTASFTIDVAEKSVDPEPKPEPEPKPEPEKPAGPKVDVPTEQPGLSKTGASTAGMSIVFVLLALSGVAALSLRRRSAH	Literature-reported	An exo-alpha-sialidase from bifidobacteria involved in the degradation of sialyloligosaccharides in human milk and intestinal glycoconjugates. Glycobiology. 2011 Apr;21(4):437-47.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT7JUKC	Bcl-2-binding component 3 (BBC3)	Q9BXH1	BBC3_HUMAN	B-cell lymphoma Bcl-2	p53 upregulated modulator of apoptosis; p53 up-regulated modulator of apoptosis; PUMA; JFY1; JFY-1; Bcl2binding component 3	BBC3	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.	.	5UUL; 4HNJ; 4BPK; 4BPJ; 4BPI	MARARQEGSSPEPVEGLARDGPRPFPLGRLVPSAVSCGLCEPGLAAAPAAPTLLPAAYLCAPTAPPAVTAALGGSRWPGGPRSRPRGPRPDGPQPSLSLAEQHLESPVPSAPGALAGGPTQAAPGVRGEEEQWAREIGAQLRRMADDLNAQYERRRQEEQQRHRPSPWRVLYNLIMGLLPLPRGHRAPEMEPN	Literature-reported	The unhydrolyzable fenretinide analogue 4-hydroxybenzylretinone induces the proapoptotic genes GADD153 (CHOP) and Bcl-2-binding component 3 (PUMA) ... Cancer Res. 2007 Jul 1;67(13):6270-7.	.	TC=1.A.21	.	Bcl-2 family.	.	.	"Bcl-2-binding component 3, p53 upregulated modulator of apoptosis"	PF15826	PF15826; PUMA	.	.	hsa01524: Platinum drug resistance; hsa04115: p53 signaling pathway; hsa04210: Apoptosis; hsa04215: Apoptosis - multiple species; hsa04390: Hippo signaling pathway; hsa05016: Huntington disease; hsa05162: Measles; hsa05200: Pathways in cancer; hsa05210: Colorectal cancer	R-HSA-111453: BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members; R-HSA-139915: Activation of PUMA and translocation to mitochondria; R-HSA-6803204: TP53 Regulates Transcription of Genes Involved in Cytochrome C Release; R-HSA-9614657: FOXO-mediated transcription of cell death genes	.	Q9BXH1
TT9FOLC	Gamma-BBH hydroxylase	.	BODG_HUMAN	Single Protein	"Gamma-butyrobetaine dioxygenase; Gamma-butyrobetaine hydroxylase; Gamma-BBH; Gamma-butyrobetaine,2-oxoglutarate dioxygenase"	BBOX1	Catalyzes the formation of L-carnitine from gamma-butyrobetaine.	.	.	MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDVNIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSELQLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHTWQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIFDVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRRSYEAGTEISRHLEGAYADWDVVMSRLRILRQRVENGN	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	O75936
TTES57P	Branched-chain-amino-acid transaminase 1 (BCAT1)	P54687	BCAT1_HUMAN	Transaminase	"Protein ECA39; ECA39; Branched-chain-amino-acid aminotransferase, cytosolic; BCT1; BCAT(c)"	BCAT1	"Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine."	EC 2.6.1.42	2COJ; 2COI; 2COG; 2ABJ	MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLTDIQYGREESDWTIVLS	Literature-reported	Docking and quantitative structure-activity relationship studies for sulfonyl hydrazides as inhibitors of cytosolic human branched-chain amino acid... Mol Divers. 2009 Nov;13(4):493-500.	.	.	.	.	.	.	.	.	.	.	.	"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"	R-HSA-70895: Branched-chain amino acid catabolism	.	P54687
TTF9OQ6	Branched-chain-amino-acid transaminase 2 (BCAT2)	O15382	BCAT2_HUMAN	Transaminase	Placental protein 18; PP18; ECA39 protein; Branched-chain amino acid aminotransferase; BCAT2; BCAT(m); BCAT	BCAT2	"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."	EC 2.6.1.42	5MPR; 5I60; 5I5Y; 5I5X; 5I5W	MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKTFTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRPWLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSLGVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLVQQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIPTMENGPELILRFQKELKEIQYGIRAHEWMFPV	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	"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"	R-HSA-70895: Branched-chain amino acid catabolism	.	O15382
TT3MSAO	HUMAN cholinesterase (BCHE)	P06276	CHLE_HUMAN	Type-B carboxylesterase/lipase	Pseudocholinesterase; Choline esterase II; CHE1; Butyrylcholine esterase; Acylcholine acylhydrolase	BCHE	Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.	EC 3.1.1.8	6QAE; 6QAD; 6QAC; 6QAB; 6QAA	MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCVGL	.	Hematological Findings and Complications of COVID-19. Am J Hematol. 2020 Apr 13. doi: 10.1002/ajh.25829.	34	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-112311: Neurotransmitter clearance; R-HSA-1483191: Synthesis of PC; R-HSA-422085: Synthesis, secretion, and deacylation of Ghrelin; R-HSA-9749641: Aspirin ADME"	.	P06276
TTEB0GD	Cholinesterase (BCHE)	P06276	CHLE_HUMAN	Type-B carboxylesterase/lipase	Pseudocholinesterase; Choline esterase II; CHE1; Butyrylcholine esterase; Acylcholine acylhydrolase	BCHE	Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.	EC 3.1.1.8	6QAE; 6QAD; 6QAC; 6QAB; 6QAA	MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCVGL	Successful	Synergistic effect of acidosis and succinylcholine-induced hyperkalemia in spinal cord transected rats. Acta Anaesthesiol Scand. 1984 Feb;28(1):87-90.	34	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-112311: Neurotransmitter clearance; R-HSA-1483191: Synthesis of PC; R-HSA-422085: Synthesis, secretion, and deacylation of Ghrelin; R-HSA-9749641: Aspirin ADME"	.	P06276
TT7WD2Q	[3-methyl-2-oxobutanoate dehydrogenase] kinase (BCKDK)	O14874	BCKD_HUMAN	Kinase	Branched-chain alpha-ketoacid dehydrogenase kinase; BCKD-kinase; BCKDHKIN	BCKDK	"Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex. {ECO:0000269|PubMed:24449431}."	EC 2.7.11.4	8F5F;8F5J;8F5S	MILASVLRSGPGGGLPLRPLLGPALALRARSTSATDTHHVEMARERSKTVTSFYNQSAIDAAAEKPSVRLTPTMMLYAGRSQDGSHLLKSARYLQQELPVRIAHRIKGFRCLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIEDEKLVRYFLDKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRISPLFGHLDMHSGAQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRI	Clinical trial	"Clinical pipeline report, company report or official report of Pfizer"	.	.	.	.	.	.	.	.	.	.	.	hsa:10295	R-HSA-70895;	.	O14874;
TTR61MW	B-cell lymphoma/leukemia 11A (BCL11A)	Q9H165	BC11A_HUMAN	.	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	BCL11A	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).	.	.	MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKRKQCNGSLCLEKAVDKPPSPSPIEMKKASNPVEVGIQVTPEDDDCLSTSSRGICPKQEHIADKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGICKDEPSSYTCTTCKQPFTSAWFLLQHAQNTHGLRIYLESEHGSPLTPRVGIPSGLGAECPSQPPLHGIHIADNNPFNLLRIPGSVSREASGLAEGRFPPTPPLFSPPPRHHLDPHRIERLGAEEMALATHHPSAFDRVLRLNPMAMEPPAMDFSRRLRELAGNTSSPPLSPGRPSPMQRLLQPFQPGSKPPFLATPPLPPLQSAPPPSQPPVKSKSCEFCGKTFKFQSNLVVHRRSHTGEKPYKCNLCDHACTQASKLKRHMKTHMHKSSPMTVKSDDGLSTASSPEPGTSDLVGSASSALKSVVAKFKSENDPNLIPENGDEEEEEDDEEEEEEEEEEEEELTESERVDYGFGLSLEAARHHENSSRGAVVGVGDESRALPDVMQGMVLSSMQHFSEAFHQVLGEKHKRGHLAEAEGHRDTCDEDSVAGESDRIDDGTVNGRGCSPGESASGGLSKKLLLGSPSSLSPFSKRIKLEKEFDLPPAAMPNTENVYSQWLAGYAASRQLKDPFLSFGDSRQSPFASSSEHSSENGSLRFSTPPGELDGGISGRSGTGSGGSTPHISGPGPGRPSSKEGRRSDTCEYCGKVFKNCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHGQVGKDVYKCEICKMPFSVYSTLEKHMKKWHSDRVLNNDIKTE	Clinical trial	Off-the-shelf' allogeneic CAR T cells: development and challenges. Nat Rev Drug Discov. 2020 Mar;19(3):185-199.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-9700645: ALK mutants bind TKIs; R-HSA-9725370: Signaling by ALK fusions and activated point mutants	.	Q9H165
TTPLHYK	BCL11A messenger RNA (BCL11A mRNA)	Q9H165	BC11A_HUMAN	.	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	BCL11A	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).	.	.	MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKRKQCNGSLCLEKAVDKPPSPSPIEMKKASNPVEVGIQVTPEDDDCLSTSSRGICPKQEHIADKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGICKDEPSSYTCTTCKQPFTSAWFLLQHAQNTHGLRIYLESEHGSPLTPRVGIPSGLGAECPSQPPLHGIHIADNNPFNLLRIPGSVSREASGLAEGRFPPTPPLFSPPPRHHLDPHRIERLGAEEMALATHHPSAFDRVLRLNPMAMEPPAMDFSRRLRELAGNTSSPPLSPGRPSPMQRLLQPFQPGSKPPFLATPPLPPLQSAPPPSQPPVKSKSCEFCGKTFKFQSNLVVHRRSHTGEKPYKCNLCDHACTQASKLKRHMKTHMHKSSPMTVKSDDGLSTASSPEPGTSDLVGSASSALKSVVAKFKSENDPNLIPENGDEEEEEDDEEEEEEEEEEEEELTESERVDYGFGLSLEAARHHENSSRGAVVGVGDESRALPDVMQGMVLSSMQHFSEAFHQVLGEKHKRGHLAEAEGHRDTCDEDSVAGESDRIDDGTVNGRGCSPGESASGGLSKKLLLGSPSSLSPFSKRIKLEKEFDLPPAAMPNTENVYSQWLAGYAASRQLKDPFLSFGDSRQSPFASSSEHSSENGSLRFSTPPGELDGGISGRSGTGSGGSTPHISGPGPGRPSSKEGRRSDTCEYCGKVFKNCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHGQVGKDVYKCEICKMPFSVYSTLEKHMKKWHSDRVLNNDIKTE	Clinical trial	"Clinical pipeline report, company report or official report of bluebird bio."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-9700645: ALK mutants bind TKIs; R-HSA-9725370: Signaling by ALK fusions and activated point mutants	.	Q9H165
TTFOUV4	BCL-2 messenger RNA (BCL2 mRNA)	P10415	BCL2_HUMAN	mRNA target	Bcl-2 (mRNA); Apoptosis regulator Bcl-2 (mRNA)	BCL2	"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."	.	6GL8; 5VAY; 5VAX; 5VAU; 5JSN	MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK	Clinical trial	"Clinical pipeline report, company report or official report of ProNAi."	21	mRNA	mRNA target	.	.	.	"Apoptosis regulator proteins, Bcl-2 family; Bcl-2 homology region 4"	PF00452; PF02180	PF00452; Bcl-2; PF02180; BH4	.	.	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	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	.	P10415
TTJGNVC	Apoptosis regulator Bcl-2 (BCL-2)	P10415	BCL2_HUMAN	B-cell lymphoma Bcl-2	Bcl-2	BCL2	"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."	.	6GL8; 5VAY; 5VAX; 5VAU; 5JSN	MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK	Successful	Emerging disease-modifying therapies for the treatment of motor neuron disease/amyotropic lateral sclerosis. Expert Opin Emerg Drugs. 2007 May;12(2):229-52.	34	TC=1.A.21	BCL2 family	Bcl-2 family.	.	.	"Apoptosis regulator proteins, Bcl-2 family; Bcl-2 homology region 4"	PF00452; PF02180	PF00452; Bcl-2; PF02180; BH4	.	.	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	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	.	P10415
TTGT9C7	Bcl-2-related protein A1 (BCL2A1)	Q16548	B2LA1_HUMAN	.	Protein GRS; Protein BFL-1; Hemopoietic-specific early response protein; HBPA1; GRS; Bcl2-L-5; Bcl-2-like protein 5; BFL1; BCL2L5	BCL2A1	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).	.	6MBC; 6MBB; 6E3J; 6E3I; 5WHI	MTDCEFGYIYRLAQDYLQCVLQIPQPGSGPSKTSRVLQNVAFSVQKEVEKNLKSCLDNVNVVSVDTARTLFNQVMEKEFEDGIINWGRIVTIFAFEGILIKKLLRQQIAPDVDTYKEISYFVAEFIMNNTGEWIRQNGGWENGFVKKFEPKSGWMTFLEVTGKICEMLSLLKQYC	Patented-recorded	Essential role of the prosurvival bcl-2 homologue A1 in mast cell survival after allergic activation. J Exp Med. 2001 Dec 3;194(11):1561-69.	.	.	.	.	.	.	.	.	.	.	.	hsa04064: NF-kappa B signaling pathway; hsa04210: Apoptosis; hsa05202: Transcriptional misregulation in cancer; hsa05221: Acute myeloid leukemia	R-HSA-9725371: Nuclear events stimulated by ALK signaling in cancer	.	Q16548
TTRE6AX	Bcl-x messenger RNA (BCL2L1 mRNA)	Q07817	B2CL1_HUMAN	mRNA target	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)	BCL2L1	"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."	.	6IJQ; 6F46; 6DCO; 6DCN; 6BF2	MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK	Literature-reported	"Discovery, characterization, and structure-activity relationships studies of proapoptotic polyphenols targeting B-cell lymphocyte/leukemia-2 proteins. J Med Chem. 2003 Sep 25;46(20):4259-64."	2	mRNA	mRNA target	.	.	.	"Apoptosis regulator proteins, Bcl-2 family; Bcl-2 homology region 4"	PF00452; PF02180	PF00452; Bcl-2; PF02180; BH4	.	.	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	R-HSA-111453:BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members; R-HSA-844455:The NLRP1 inflammasome	.	Q07817
TTU1E82	Apoptosis regulator Bcl-xL (BCL-xL)	Q07817	B2CL1_HUMAN	B-cell lymphoma Bcl-2	Bcl2like protein 1; Bcl2L1; Bcl2-L-1; Bcl-XL; Bcl-2-like protein 1; BCLX; BCL2L; Apoptosis regulator Bcl-X	BCL2L1	"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."	.	6IJQ; 6F46; 6DCO; 6DCN; 6BF2	MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK	Clinical trial	"Phase II study of obatoclax mesylate (GX15-070), a small-molecule BCL-2 family antagonist, for patients with myelofibrosis. Clin Lymphoma Myeloma Leuk. 2010 Aug;10(4):285-9."	21	TC=1.A.21	BCL2 family	Bcl-2 family.	.	.	"Apoptosis regulator proteins, Bcl-2 family; Bcl-2 homology region 4"	PF00452; PF02180	PF00452; Bcl-2; PF02180; BH4	1.A.21.1.1	The Bcl-2 (Bcl-2) Family	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	R-HSA-111453:BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members; R-HSA-844455:The NLRP1 inflammasome	.	Q07817
TTQ79W8	Apoptosis regulator Bcl-W (BCL-W)	Q92843	B2CL2_HUMAN	B-cell lymphoma Bcl-2	KIAA0271; Bcl2-L-2; Bcl-2-like protein 2; BCLW	BCL2L2	Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. Promotes cell survival.	.	4CIM; 2Y6W; 1ZY3; 1O0L; 1MK3	MATPASAPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEPLVGQVQEWMVAYLETQLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK	Clinical trial	"Clinical pipeline report, company report or official report of Roche (2009)."	21	TC=1.A.21	BCL2 family	Bcl-2 family.	.	.	"Apoptosis regulator proteins, Bcl-2 family; Bcl-2 homology region 4"	PF00452; PF02180	PF00452; Bcl-2; PF02180; BH4	1.A.21.1.5	The Bcl-2 (Bcl-2) Family	hsa05206:MicroRNAs in cancer	.	.	Q92843
TTC9YX5	B-cell lymphoma 6 protein (BCL-6)	P41182	BCL6_HUMAN	.	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	BCL6	"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."	.	6EW8; 6EW7; 6EW6; 6CQ1; 6C3N	MASPADSCIQFTRHASDVLLNLNRLRSRDILTDVVIVVSREQFRAHKTVLMACSGLFYSIFTDQLKCNLSVINLDPEINPEGFCILLDFMYTSRLNLREGNIMAVMATAMYLQMEHVVDTCRKFIKASEAEMVSAIKPPREEFLNSRMLMPQDIMAYRGREVVENNLPLRSAPGCESRAFAPSLYSGLSTPPASYSMYSHLPVSSLLFSDEEFRDVRMPVANPFPKERALPCDSARPVPGEYSRPTLEVSPNVCHSNIYSPKETIPEEARSDMHYSVAEGLKPAAPSARNAPYFPCDKASKEEERPSSEDEIALHFEPPNAPLNRKGLVSPQSPQKSDCQPNSPTESCSSKNACILQASGSPPAKSPTDPKACNWKKYKFIVLNSLNQNAKPEGPEQAELGRLSPRAYTAPPACQPPMEPENLDLQSPTKLSASGEDSTIPQASRLNNIVNRSMTGSPRSSSESHSPLYMHPPKCTSCGSQSPQHAEMCLHTAGPTFPEEMGETQSEYSDSSCENGAFFCNECDCRFSEEASLKRHTLQTHSDKPYKCDRCQASFRYKGNLASHKTVHTGEKPYRCNICGAQFNRPANLKTHTRIHSGEKPYKCETCGARFVQVAHLRAHVLIHTGEKPYPCEICGTRFRHLQTLKSHLRIHTGEKPYHCEKCNLHFRHKSQLRLHLRQKHGAITNTKVQYRVSATDLPPELPKAC	Literature-reported	Homoharringtonine suppresses imatinib resistance via the Bcl-6/p53 pathway in chronic myeloid leukemia cell lines. Oncotarget. 2017 Jun 6;8(23):37594-37604.	.	.	.	.	.	.	.	.	.	.	.	hsa04068: FoxO signaling pathway; hsa05202: Transcriptional misregulation in cancer; hsa05207: Chemical carcinogenesis - receptor activation	R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6803205: TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain; R-HSA-9614657: FOXO-mediated transcription of cell death genes	.	P41182
TTIV39N	Fusion protein Bcr-Abl T315I mutant (Bcr-Abl T315I)	P11274-P00519	BCR_HUMAN-ABL1_HUMAN	Kinase	T315I BCR-ABL; BCR-ABL T315I mutant	BCR-ABL1	"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."	.	.	MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEVMLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR	Patented-recorded	"Danusertib, an aurora kinase inhibitor.Expert Opin Investig Drugs.2012 Mar;21(3):383-93."	15.5	EC:2.7	.	.	2.7.11.1	Transferring phosphorus-containing groups	Bcr-Abl oncoprotein oligomerisation domain; C2 domain; RhoGAP domain; RhoGEF domain	PF09036; PF00168; PF00620; PF00621	PF09036; Bcr-Abl_Oligo; PF00168; C2; PF00620; RhoGAP; PF00621; RhoGEF	.	.	.	.	.	P11274
TTS7G69	Fusion protein Bcr-Abl (Bcr-Abl)	P11274-P00519	BCR_HUMAN-ABL1_HUMAN	Kinase	BCR-ABL fusion protein; BCR-ABL	BCR-ABL1	"Activates downstream signaling pathways such as STAT5, PI3K/Akt, and Erk1/2 to lead to increased cell transformation, survival, and proliferation."	.	.	MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEVMLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR	Successful	A comparison of physicochemical property profiles of marketed oral drugs and orally bioavailable anti-cancer protein kinase inhibitors in clinical development. Curr Top Med Chem. 2007;7(14):1408-22.	34	EC:2.7	.	.	2.7.11.1	Transferring phosphorus-containing groups	Bcr-Abl oncoprotein oligomerisation domain; C2 domain; RhoGAP domain; RhoGEF domain	PF09036; PF00168; PF00620; PF00621	PF09036; Bcr-Abl_Oligo; PF00168; C2; PF00620; RhoGAP; PF00621; RhoGEF	.	.	.	.	.	P11274
TTE63HY	HUMAN fusion protein Bcr-Abl (Bcr-Abl)	P11274-P00519	BCR_HUMAN/ABL1_HUMAN	Kinase	BCR-ABL fusion protein; BCR-ABL	BCR-ABL1	"Activates downstream signaling pathways such as STAT5, PI3K/Akt, and Erk1/2 to lead to increased cell transformation, survival, and proliferation."	.	.	MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEVMLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR	.	Coronaviruses - drug discovery and therapeutic options. Nat Rev Drug Discov. 2016 May;15(5):327-47.	34	EC:2.7	.	.	2.7.11.1	Transferring phosphorus-containing groups	Bcr-Abl oncoprotein oligomerisation domain; C2 domain; RhoGAP domain; RhoGEF domain	PF09036; PF00168; PF00620; PF00621	PF09036; Bcr-Abl_Oligo; PF00168; C2; PF00620; RhoGAP; PF00621; RhoGEF	.	.	.	.	.	P11274
TTG5QIA	B1 bradykinin receptor (BDKRB1)	P46663	BKRB1_HUMAN	GPCR rhodopsin	BRADYB1; BK-1 receptor; B1R	BDKRB1	This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation.	.	.	MASSWPPLELQSSNQSQLFPQNATACDNAPEAWDLLHRVLPTFIISICFFGLLGNLFVLLVFLLPRRQLNVAEIYLANLAASDLVFVLGLPFWAENIWNQFNWPFGALLCRVINGVIKANLFISIFLVVAISQDRYRVLVHPMASRRQQRRRQARVTCVLIWVVGGLLSIPTFLLRSIQAVPDLNITACILLLPHEAWHFARIVELNILGFLLPLAAIVFFNYHILASLRTREEVSRTRCGGRKDSKTTALILTLVVAFLVCWAPYHFFAFLEFLFQVQAVRGCFWEDFIDLGLQLANFFAFTNSSLNPVIYVFVGRLFRTKVWELYKQCTPKSLAPISSSHRKEIFQLFWRN	Clinical trial	The kinin B1 receptor antagonist SSR240612 reverses tactile and cold allodynia in an experimental rat model of insulin resistance. Br J Pharmacol. 2007 September; 152(2): 280-287.	21	PF00001	.	G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB1 sub-subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	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	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events	.	P46663
TTGY8IW	B2 bradykinin receptor (BDKRB2)	P30411	BKRB2_HUMAN	GPCR rhodopsin	Bradykinin B2 receptor; BKR2; BK-2 receptor; BK B(2) receptor; B2R	BDKRB2	It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. Receptor for bradykinin.	.	.	MFSPWKISMFLSVREDSVPTTASFSADMLNVTLQGPTLNGTFAQSKCPQVEWLGWLNTIQPPFLWVLFVLATLENIFVLSVFCLHKSSCTVAEIYLGNLAAADLILACGLPFWAITISNNFDWLFGETLCRVVNAIISMNLYSSICFLMLVSIDRYLALVKTMSMGRMRGVRWAKLYSLVIWGCTLLLSSPMLVFRTMKEYSDEGHNVTACVISYPSLIWEVFTNMLLNVVGFLLPLSVITFCTMQIMQVLRNNEMQKFKEIQTERRATVLVLVVLLLFIICWLPFQISTFLDTLHRLGILSSCQDERIIDVITQIASFMAYSNSCLNPLVYVIVGKRFRKKSWEVYQGVCQKGGCRSEPIQMENSMGTLRTSISVERQIHKLQDWAGSRQ	Successful	Bradykinin receptor antagonists--a review of the patent literature 2005-2008. Expert Opin Ther Pat. 2009 Jul;19(7):919-41.	34	PF00001	.	G-protein coupled receptor 1 family. Bradykinin receptor subfamily. BDKRB2 sub-subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	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	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events	.	P30411
TTSMLOH	Brain-derived neurotrophic factor (BDNF)	P23560	BDNF_HUMAN	Growth factor	Brainderived neurotrophic factor; Abrineurin	BDNF	"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."	.	1BND; 1B8M	MTILFLTMVISYFGCMKAAPMKEANIRGQGGLAYPGVRTHGTLESVNGPKAGSRGLTSLADTFEHVIEELLDEDQKVRPNEENNKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSISEWVTAADKKTAVDMSGGTVTVLEKVPVSKGQLKQYFYETKCNPMGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDSKKRIGWRFIRIDTSCVCTLTIKRGR	Clinical trial	"PYM50028, a novel, orally active, nonpeptide neurotrophic factor inducer, prevents and reverses neuronal damage induced by MPP+ in mesencephalic neurons and by MPTP in a mouse model of Parkinson's disease. FASEB J. 2008 Jul;22(7):2488-97."	21	Growth factor	Growth factor	NGF-beta family.	.	.	Nerve growth factor family	PF00243	PF00243; NGF	.	.	hsa04010:MAPK signaling pathway; hsa04024:cAMP signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa05016:Huntington's disease; hsa05030:Cocaine addiction; hsa05034:Alcoholism	R-HSA-9022702: MECP2 regulates transcription of neuronal ligands; R-HSA-9024909: BDNF activates NTRK2 (TRKB) signaling; R-HSA-9026519: Activated NTRK2 signals through RAS; R-HSA-9026527: Activated NTRK2 signals through PLCG1; R-HSA-9028335: Activated NTRK2 signals through PI3K; R-HSA-9028731: Activated NTRK2 signals through FRS2 and FRS3; R-HSA-9032500: Activated NTRK2 signals through FYN; R-HSA-9032759: NTRK2 activates RAC1; R-HSA-9032845: Activated NTRK2 signals through CDK5	.	P23560
TT5M7LN	Beclin-1 (BECN1)	Q14457	BECN1_HUMAN	.	Protein GT197; GT197; Coiledcoil myosinlike BCL2interacting protein; Coiled-coil myosin-like BCL2-interacting protein	BECN1	"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."	.	6HOK; 6HOJ; 6HOI; 6DCO; 6DCN	MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK	Literature-reported	Acetylation of Beclin 1 inhibits autophagosome maturation and promotes tumour growth. Nat Commun. 2015 May 26;6:7215.	.	.	Beclin family	beclin family.	.	.	"Apg6 BARA domain; Apg6 coiled-coil region; Beclin-1 BH3 domain, Bcl-2-interacting"	PF04111; PF17675; PF15285	PF04111; APG6; PF17675; APG6_N; PF15285; BH3	.	.	hsa04136: Autophagy - other; hsa04137: Mitophagy - animal; hsa04140: Autophagy - animal; hsa04215: Apoptosis - multiple species; hsa04371: Apelin signaling pathway; hsa05010: Alzheimer disease; hsa05014: Amyotrophic lateral sclerosis; hsa05016: Huntington disease; hsa05017: Spinocerebellar ataxia; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05131: Shigellosis; hsa05167: Kaposi sarcoma-associated herpesvirus infection	"R-HSA-1632852: Macroautophagy; R-HSA-5689880: Ub-specific processing proteases; R-HSA-9679504: Translation of Replicase and Assembly of the Replication Transcription Complex; R-HSA-9694676: Translation of Replicase and Assembly of the Replication Transcription Complex; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses; R-HSA-983170: Antigen Presentation: Folding, assembly and peptide loading of class I MHC"	.	Q14457
TT0JPVF	Bone/cartilage proteoglycan I (BGN)	P21810	PGS1_HUMAN	Small leucine-rich proteoglycan	PGS1; BGN	BGN	May be involved in collagen fiber assembly.	.	.	MWPLWRLVSLLALSQALPFEQRGFWDFTLDDGPFMMNDEEASGADTSGVLDPDSVTPTYSAMCPFGCHCHLRVVQCSDLGLKSVPKEISPDTTLLDLQNNDISELRKDDFKGLQHLYALVLVNNKISKIHEKAFSPLRKLQKLYISKNHLVEIPPNLPSSLVELRIHDNRIRKVPKGVFSGLRNMNCIEMGGNPLENSGFEPGAFDGLKLNYLRISEAKLTGIPKDLPETLNELHLDHNKIQAIELEDLLRYSKLYRLGLGHNQIRMIENGSLSFLPTLRELHLDNNKLARVPSGLPDLKLLQVVYLHSNNITKVGVNDFCPMGFGVKRAYYNGISLFNNPVPYWEVQPATFRCVTDRLAIQFGNYKK	Literature-reported	Serum Decorin and Biglycan as Potential Biomarkers to Predict PPROM in Early Gestation. Reprod Sci. 2019 Mar 21:1933719119831790.	.	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-1971475: A tetrasaccharide linker sequence is required for GAG synthesis; R-HSA-2022870: Chondroitin sulfate biosynthesis; R-HSA-2022923: Dermatan sulfate biosynthesis; R-HSA-2024101: CS/DS degradation; R-HSA-3000178: ECM proteoglycans; R-HSA-3560783: Defective B4GALT7 causes EDS, progeroid type; R-HSA-3560801: Defective B3GAT3 causes JDSSDHD; R-HSA-3595172: Defective CHST3 causes SEDCJD; R-HSA-3595174: Defective CHST14 causes EDS, musculocontractural type; R-HSA-3595177: Defective CHSY1 causes TPBS; R-HSA-4420332: Defective B3GALT6 causes EDSP2 and SEMDJL1"	.	P21810
TTQ5LRD	Cellular inhibitor of apoptosis 1 (BIRC2)	Q13490	BIRC2_HUMAN	Acyltransferase	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	BIRC2	"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."	EC 2.3.2.27	6HPR; 6EXW; 5M6N; 4MU7; 4MTI	MHKTASQRLFPGPSYQNIKSIMEDSTILSDWTNSNKQKMKYDFSCELYRMSTYSTFPAGVPVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKLGDSPIQKHKQLYPSCSFIQNLVSASLGSTSKNTSPMRNSFAHSLSPTLEHSSLFSGSYSSLSPNPLNSRAVEDISSSRTNPYSYAMSTEEARFLTYHMWPLTFLSPSELARAGFYYIGPGDRVACFACGGKLSNWEPKDDAMSEHRRHFPNCPFLENSLETLRFSISNLSMQTHAARMRTFMYWPSSVPVQPEQLASAGFYYVGRNDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEFLIRMKGQEFVDEIQGRYPHLLEQLLSTSDTTGEENADPPIIHFGPGESSSEDAVMMNTPVVKSALEMGFNRDLVKQTVQSKILTTGENYKTVNDIVSALLNAEDEKREEEKEKQAEEMASDDLSLIRKNRMALFQQLTCVLPILDNLLKANVINKQEHDIIKQKTQIPLQARELIDTILVKGNAAANIFKNCLKEIDSTLYKNLFVDKNMKYIPTEDVSGLSLEEQLRRLQEERTCKVCMDKEVSVVFIPCGHLVVCQECAPSLRKCPICRGIIKGTVRTFLS	Clinical trial	cIAPs and XIAP regulate myelopoiesis through cytokine production in an RIPK1- and RIPK3-dependent manner. Blood. 2014 Apr 17;123(16):2562-72.	21	EC:2.3	Carbon-nitrogen ligase	IAP family.	2.3.2.27 	Acyltransferases	Inhibitor of Apoptosis domain; Caspase recruitment domain	PF00653; PF00619	PF00653; BIR; PF00619; CARD	.	.	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	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	.	Q13490
TTAIWZN	Apoptosis-2 messenger RNA (BIRC3 mRNA)	Q13489	BIRC3_HUMAN	mRNA target	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)	BIRC3	"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."	EC 2.3.2.27	3M0D; 3M0A; 3EB6; 3EB5; 2UVL	MNIVENSIFLSNLMKSANTFELKYDLSCELYRMSTYSTFPAGVPVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKRGDSPTEKHKKLYPSCRFVQSLNSVNNLEATSQPTFPSSVTNSTHSLLPGTENSGYFRGSYSNSPSNPVNSRANQDFSALMRSSYHCAMNNENARLLTFQTWPLTFLSPTDLAKAGFYYIGPGDRVACFACGGKLSNWEPKDNAMSEHLRHFPKCPFIENQLQDTSRYTVSNLSMQTHAARFKTFFNWPSSVLVNPEQLASAGFYYVGNSDDVKCFCCDGGLRCWESGDDPWVQHAKWFPRCEYLIRIKGQEFIRQVQASYPHLLEQLLSTSDSPGDENAESSIIHFEPGEDHSEDAIMMNTPVINAAVEMGFSRSLVKQTVQRKILATGENYRLVNDLVLDLLNAEDEIREEERERATEEKESNDLLLIRKNRMALFQHLTCVIPILDSLLTAGIINEQEHDVIKQKTQTSLQARELIDTILVKGNIAATVFRNSLQEAEAVLYEHLFVQQDIKYIPTEDVSDLPVEEQLRRLQEERTCKVCMDKEVSIVFIPCGHLVVCKDCAPSLRKCPICRSTIKGTVRTFLS	Literature-reported	"US patent application no. 5,958,771, Antisense modulation of cellular inhibitor of Apoptosis-2 expression."	0	mRNA	mRNA target	.	.	.	Inhibitor of Apoptosis domain; Caspase recruitment domain	PF00653; PF00619	PF00653; BIR; PF00619; CARD	.	.	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	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	.	Q13489
TTIRY6K	Cellular inhibitor of apoptosis 2 (BIRC3)	Q13489	BIRC3_HUMAN	Acyltransferase	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	BIRC3	"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."	EC 2.3.2.27	3M0D; 3M0A; 3EB6; 3EB5; 2UVL	MNIVENSIFLSNLMKSANTFELKYDLSCELYRMSTYSTFPAGVPVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKRGDSPTEKHKKLYPSCRFVQSLNSVNNLEATSQPTFPSSVTNSTHSLLPGTENSGYFRGSYSNSPSNPVNSRANQDFSALMRSSYHCAMNNENARLLTFQTWPLTFLSPTDLAKAGFYYIGPGDRVACFACGGKLSNWEPKDNAMSEHLRHFPKCPFIENQLQDTSRYTVSNLSMQTHAARFKTFFNWPSSVLVNPEQLASAGFYYVGNSDDVKCFCCDGGLRCWESGDDPWVQHAKWFPRCEYLIRIKGQEFIRQVQASYPHLLEQLLSTSDSPGDENAESSIIHFEPGEDHSEDAIMMNTPVINAAVEMGFSRSLVKQTVQRKILATGENYRLVNDLVLDLLNAEDEIREEERERATEEKESNDLLLIRKNRMALFQHLTCVIPILDSLLTAGIINEQEHDVIKQKTQTSLQARELIDTILVKGNIAATVFRNSLQEAEAVLYEHLFVQQDIKYIPTEDVSDLPVEEQLRRLQEERTCKVCMDKEVSIVFIPCGHLVVCKDCAPSLRKCPICRSTIKGTVRTFLS	Clinical trial	"Debio 1143, an antagonist of multiple inhibitor-of-apoptosis proteins, activates apoptosis and enhances radiosensitization of non-small cell lung c... Am J Cancer Res. 2014 Nov 19;4(6):943-51."	21	EC:2.3	Carbon-nitrogen ligase	IAP family.	2.3.2.27 	Acyltransferases	Inhibitor of Apoptosis domain; Caspase recruitment domain	PF00653; PF00619	PF00653; BIR; PF00619; CARD	.	.	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	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	.	Q13489
TTTPU1G	Apoptosis inhibitor survivin (BIRC5)	O15392	BIRC5_HUMAN	Acyltransferase	Survivin; IAP4; Baculoviral IAP repeat-containing protein 5; Apoptosis inhibitor 4; API4	BIRC5	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.	.	4A0N; 4A0J; 4A0I; 3UIK; 3UIJ	MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD	Clinical trial	Targeted BIRC5 silencing using YM155 causes cell death in neuroblastoma cells with low ABCB1 expression.Eur J Cancer.2012 Mar;48(5):763-71.	25	EC:2.3	Inhibitor of apoptosis	IAP family.	.	.	Inhibitor of Apoptosis domain	PF00653	PF00653; BIR	.	.	hsa04390:Hippo signaling pathway; hsa05161:Hepatitis B; hsa05200:Pathways in cancer; hsa05210:Colorectal cancer	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	.	O15392
TTEWOHV	Survivin messenger RNA (Survivin mRNA)	O15392	BIRC5_HUMAN	mRNA target	Survivin (mRNA); IAP4 (mRNA); Baculoviral IAP repeat-containing protein 5 (mRNA); Apoptosis inhibitor survivin (mRNA); Apoptosis inhibitor 4 (mRNA); API4 (mRNA)	BIRC5	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.	.	4A0N; 4A0J; 4A0I; 3UIK; 3UIJ	MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD	Literature-reported	"US patent application no. 6,165,788, Antisense modulation of Survivin expression."	0	mRNA	mRNA target	.	.	.	Inhibitor of Apoptosis domain	PF00653	PF00653; BIR	.	.	hsa01524: Platinum drug resistance; hsa04210: Apoptosis; hsa04215: Apoptosis - multiple species; hsa04390: Hippo signaling pathway; hsa05161: Hepatitis B; hsa05200: Pathways in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05210: Colorectal cancer	R-HSA-141444: Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal; R-HSA-2467813: Separation of Sister Chromatids; R-HSA-2500257: Resolution of Sister Chromatid Cohesion; R-HSA-4615885: SUMOylation of DNA replication proteins; R-HSA-5663220: RHO GTPases Activate Formins; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6803205: TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain; R-HSA-68877: Mitotic Prometaphase; R-HSA-8951664: Neddylation; R-HSA-9648025: EML4 and NUDC in mitotic spindle formation	.	O15392
TTHZ8TA	Melanoma inhibitor of apoptosis protein (ML-IAP)	Q96CA5	BIRC7_HUMAN	Acyltransferase	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	BIRC7	"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."	EC 2.3.2.27	4AUQ; 3UW5; 3GTA; 3GT9; 3F7I	MGPKDSAKCLHRGPQPSHWAAGDGPTQERCGPRSLGSPVLGLDTCRAWDHVDGQILGQLRPLTEEEEEEGAGATLSRGPAFPGMGSEELRLASFYDWPLTAEVPPELLAAAGFFHTGHQDKVRCFFCYGGLQSWKRGDDPWTEHAKWFPSCQFLLRSKGRDFVHSVQETHSQLLGSWDPWEEPEDAAPVAPSVPASGYPELPTPRREVQSESAQEPGGVSPAEAQRAWWVLEPPGARDVEAQLRRLQEERTCKVCLDRAVSIVFVPCGHLVCAECAPGLQLCPICRAPVRSRVRTFLS	Patented-recorded	Small molecule inhibitor of apoptosis proteins antagonists: a patent review.Expert Opin Ther Pat. 2015 Jul;25(7):755-74.	15.5	EC:2.3	.	IAP family.	2.3.2.27 	Acyltransferases	Inhibitor of Apoptosis domain	PF00653	PF00653; BIR	.	.	hsa04120: Ubiquitin mediated proteolysis; hsa04215: Apoptosis - multiple species; hsa05145: Toxoplasmosis; hsa05200: Pathways in cancer; hsa05222: Small cell lung cancer	.	.	Q96CA5
TT09JLE	BV virus Major capsid protein VP1 (BKV VP1)	P03088	VP1_POVBK	.	Major structural protein VP1	BKV VP1	"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."	.	.	MAPTKRKGECPGAAPKKPKEPVQVPKLLIKGGVEVLEVKTGVDAITEVECFLNPEMGDPDENLRGFSLKLSAENDFSSDSPERKMLPCYSTARIPLPNLNEDLTCGNLLMWEAVTVQTEVIGITSMLNLHAGSQKVHEHGGGKPIQGSNFHFFAVGGEPLEMQGVLMNYRSKYPDGTITPKNPTAQSQVMNTDHKAYLDKNNAYPVECWVPDPSRNENARYFGTFTGGENVPPVLHVTNTATTVLLDEQGVGPLCKADSLYVSAADICGLFTNSSGTQQWRGLARYFKIRLRKRSVKNPYPISFLLSDLINRRTQRVDGQPMYGMESQVEEVRVFDGTERLPGDPDMIRYIDKQGQLQTKML	Clinical trial	"Clinical pipeline report, company report or official report of Amplyx Pharmaceuticals."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNDSC3	B lymphocyte kinase (BLK)	P51451	BLK_HUMAN	Kinase	p55-Blk; Tyrosine-protein kinase Blk	BLK	"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."	EC 2.7.10.2	.	MGLVSSKKPDKEKPIKEKDKGQWSPLKVSAQDKDAPPLPPLVVFNHLTPPPPDEHLDEDKHFVVALYDYTAMNDRDLQMLKGEKLQVLKGTGDWWLARSLVTGREGYVPSNFVARVESLEMERWFFRSQGRKEAERQLLAPINKAGSFLIRESETNKGAFSLSVKDVTTQGELIKHYKIRCLDEGGYYISPRITFPSLQALVQHYSKKGDGLCQRLTLPCVRPAPQNPWAQDEWEIPRQSLRLVRKLGSGQFGEVWMGYYKNNMKVAIKTLKEGTMSPEAFLGEANVMKALQHERLVRLYAVVTKEPIYIVTEYMARGCLLDFLKTDEGSRLSLPRLIDMSAQIAEGMAYIERMNSIHRDLRAANILVSEALCCKIADFGLARIIDSEYTAQEGAKFPIKWTAPEAIHFGVFTIKADVWSFGVLLMEVVTYGRVPYPGMSNPEVIRNLERGYRMPRPDTCPPELYRGVIAECWRSRPEERPTFEFLQSVLEDFYTATERQYELQP	Patented-recorded	"Inhibitors of JAK-family kinases: an update on the patent literature 2013-2015, part 1.Expert Opin Ther Pat. 2017 Feb;27(2):127-143."	15.5	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. SRC subfamily.	2.7.10.2 	Transferring phosphorus-containing groups	Protein tyrosine kinase; SH2 domain; SH3 domain	PF07714; PF00017; PF00018	PF07714; Pkinase_Tyr; PF00017; SH2; PF00018; SH3_1	.	.	.	R-HSA-8939245: RUNX1 regulates transcription of genes involved in BCR signaling; R-HSA-983695: Antigen activates B Cell Receptor (BCR) leading to generation of second messengers	.	P51451
TTJBPN3	Biliverdin reductase A (BLVRA)	P53004	BIEA_HUMAN	CH-CH donor oxidoreductase	Biliverdin-IX alpha-reductase; BVR A; BVR; BLVRA; BLVR	BLVRA	"Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor."	EC 1.3.1.24	2H63	MNAEPERKFGVVVVGVGRAGSVRMRDLRNPHPSSAFLNLIGFVSRRELGSIDGVQQISLEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKVLHEEHVELLMEEFAFLKKEVVGKDLLKGSLLFTAGPLEEERFGFPAFSGISRLTWLVSLFGELSLVSATLEERKEDQYMKMTVCLETEKKSPLSWIEEKGPGLKRNRYLSFHFKSGSLENVPNVGVNKNIFLKDQNIFVQKLLGQFSEKELAAEKKRILHCLGLAEEIQKYCCSRK	Successful	Role of vitamin C transporters and biliverdin reductase in the dual pro-oxidant and anti-oxidant effect of biliary compounds on the placental-fetal... Toxicol Appl Pharmacol. 2008 Oct 15;232(2):327-36.	34	.	.	.	.	.	.	.	.	.	.	hsa00860:Porphyrin and chlorophyll metabolism	R-HSA-189483: Heme degradation; R-HSA-9707564: Cytoprotection by HMOX1	MetaCyc:HS02928-MON	P53004
TTIPNSR	Polycomb complex protein BMI-1 (BMI1)	P35226	BMI1_HUMAN	Zinc-finger	RNF51; RING finger protein 51; Polycomb group RING finger protein 4; PCGF4	BMI1	"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."	.	5FR6; 4R8P; 3RPG; 2NA1; 2H0D	MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEDKRIITDDEIISLSIEFFDQNRLDRKVNKDKEKSKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKISHQRDGLTNAGELESDSGSDKANSPAGGIPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSGNHQSSFANRPRKSSVNGSSATSSG	Literature-reported	"The expression and prognostic value of stem cell markers Bmi-1, HESC5:3, and HES77 in human papillomavirus-positive and -negative oropharyngeal squ... Tumour Biol. 2019 Mar;41(3):1010428319840473."	.	Zinc-finger	Zinc-finger	.	.	.	RAWUL domain RING finger- and  WD40-associated ubiquitin-like	PF16207	PF16207; RAWUL	.	.	hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa05202: Transcriptional misregulation in cancer; hsa05206: MicroRNAs in cancer	R-HSA-2559580: Oxidative Stress Induced Senescence; R-HSA-3108214: SUMOylation of DNA damage response and repair proteins; R-HSA-3899300: SUMOylation of transcription cofactors; R-HSA-4551638: SUMOylation of chromatin organization proteins; R-HSA-4570464: SUMOylation of RNA binding proteins; R-HSA-4655427: SUMOylation of DNA methylation proteins; R-HSA-8939243: RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known; R-HSA-8943724: Regulation of PTEN gene transcription; R-HSA-8953750: Transcriptional Regulation by E2F6	.	P35226
TT0L58T	Bone morphogenetic protein 1 (BMP1)	P13497	BMP1_HUMAN	Peptidase	Procollagen C-proteinase; PCP protein; PCOLC; Mammalian tolloid protein; MTld; BMP-1	BMP1	"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."	EC 3.4.24.19	6BTQ; 6BTP; 6BTO; 6BTN; 6BSM	MPGVARLPLLLGLLLLPRPGRPLDLADYTYDLAEEDDSEPLNYKDPCKAAAFLGDIALDEEDLRAFQVQQAVDLRRHTARKSSIKAAVPGNTSTPSCQSTNGQPQRGACGRWRGRSRSRRAATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPKYEVNGVKPPIGQRTRLSKGDIAQARKLYKCPACGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSKLPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEAICGGDVKKDYGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYEKPDDIKSTSSRLWLKFVSDGSINKAGFAVNFFKEVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRCEAACGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFSDKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDCKEAGCDHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFMEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKKPEPVLATGSRMFLRFYSDNSVQRKGFQASHATECGGQVRADVKTKDLYSHAQFGDNNYPGGVDCEWVIVAEEGYGVELVFQTFEVEEETDCGYDYMELFDGYDSTAPRLGRYCGSGPPEEVYSAGDSVLVKFHSDDTITKKGFHLRYTSTKFQDTLHSRK	Literature-reported	Amino acid derived sulfonamide hydroxamates as inhibitors of procollagen C-proteinase. Part 2: Solid-phase optimization of side chains. Bioorg Med Chem Lett. 2002 Apr 22;12(8):1233-5.	0	EC:3.4	Peptidase	.	3.4.24.19	Acting on peptide bonds (peptidases)	Astacin (Peptidase family M12A); CUB domain; Calcium-binding EGF domain	PF01400; PF00431; PF07645	PF01400; Astacin; PF00431; CUB; PF07645; EGF_CA	.	.	.	R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1650814:Collagen biosynthesis and modifying enzymes; R-HSA-2214320:Anchoring fibril formation	.	P13497
TTTG6H1	Bone morphogenetic protein 10 (BMP10)	O95393	BMP10_HUMAN	Growth factor	BMP10	BMP10	"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."	.	.	MGSLVLTLCALFCLAAYLVSGSPIMNLEQSPLEEDMSLFGDVFSEQDGVDFNTLLQSMKDEFLKTLNLSDIPTQDSAKVDPPEYMLELYNKFATDRTSMPSANIIRSFKNEDLFSQPVSFNGLRKYPLLFNVSIPHHEEVIMAELRLYTLVQRDRMIYDGVDRKITIFEVLESKGDNEGERNMLVLVSGEIYGTNSEWETFDVTDAIRRWQKSGSSTHQLEVHIESKHDEAEDASSGRLEIDTSAQNKHNPLLIVFSDDQSSDKERKEELNEMISHEQLPELDNLGLDSFSSGPGEEALLQMRSNIIYDSTARIRRNAKGNYCKRTPLYIDFKEIGWDSWIIAPPGYEAYECRGVCNYPLAEHLTPTKHAIIQALVHLKNSQKASKACCVPTKLEPISILYLDKGVVTYKFKYEGMAVSECGCR	Literature-reported	The Prodomain-bound Form of Bone Morphogenetic Protein 10 Is Biologically Active on Endothelial Cells. J Biol Chem. 2016 Feb 5;291(6):2954-66.	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction	R-HSA-201451: Signaling by BMP; R-HSA-2129379: Molecules associated with elastic fibres	.	O95393
TTP3IGX	Bone morphogenetic protein 2 (BMP2)	P12643	BMP2_HUMAN	Growth factor	Bone morphogenetic protein 2A; BMP2A; BMP-2A; BMP-2	BMP2	"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."	.	6OMN; 4UI2; 4UI1; 4UI0; 4UHZ	MVAGTRCLLALLLPQVLLGGAAGLVPELGRRKFAAASSGRPSSQPSDEVLSEFELRLLSMFGLKQRPTPSRDAVVPPYMLDLYRRHSGQPGSPAPDHRLERAASRANTVRSFHHEESLEELPETSGKTTRRFFFNLSSIPTEEFITSAELQVFREQMQDALGNNSSFHHRINIYEIIKPATANSKFPVTRLLDTRLVNQNASRWESFDVTPAVMRWTAQGHANHGFVVEVAHLEEKQGVSKRHVRISRSLHQDEHSWSQIRPLLVTFGHDGKGHPLHKREKRQAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR	Clinical trial	Complications with the use of bone morphogenetic protein 2 (BMP-2) in spine surgery. Spine J. 2014 Mar 1;14(3):552-9.	25	Growth factor	Transforming growth factor	TGF-beta family.	.	.	Transforming growth factor beta like domain; TGF-beta propeptide	PF00019; PF00688	PF00019; TGF_beta; PF00688; TGFb_propeptide	.	.	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	R-HSA-2129379:Molecules associated with elastic fibres	.	P12643
TT32VXH	BMP-2-inducible protein kinase (BMP2K)	Q9NSY1	BMP2K_HUMAN	Kinase	HRIHFB2017; BIKe	BMP2K	May be involved in osteoblast differentiation.	EC 2.7.11.1	5IKW; 5I3R; 5I3O; 4W9X; 4W9W	MKKFSRMPKSEGGSGGGAAGGGAGGAGAGAGCGSGGSSVGVRVFAVGRHQVTLEESLAEGGFSTVFLVRTHGGIRCALKRMYVNNMPDLNVCKREITIMKELSGHKNIVGYLDCAVNSISDNVWEVLILMEYCRAGQVVNQMNKKLQTGFTEPEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLNDGGNYVLCDFGSATNKFLNPQKDGVNVVEEEIKKYTTLSYRAPEMINLYGGKPITTKADIWALGCLLYKLCFFTLPFGESQVAICDGNFTIPDNSRYSRNIHCLIRFMLEPDPEHRPDIFQVSYFAFKFAKKDCPVSNINNSSIPSALPEPMTASEAAARKSQIKARITDTIGPTETSIAPRQRPKANSATTATPSVLTIQSSATPVKVLAPGEFGNHRPKGALRPGNGPEILLGQGPPQQPPQQHRVLQQLQQGDWRLQQLHLQHRHPHQQQQQQQQQQQQQQQQQQQQQQQQQQQHHHHHHHHLLQDAYMQQYQHATQQQQMLQQQFLMHSVYQPQPSASQYPTMMPQYQQAFFQQQMLAQHQPSQQQASPEYLTSPQEFSPALVSYTSSLPAQVGTIMDSSYSANRSVADKEAIANFTNQKNISNPPDMSGWNPFGEDNFSKLTEEELLDREFDLLRSNRLEERASSDKNVDSLSAPHNHPPEDPFGSVPFISHSGSPEKKAEHSSINQENGTANPIKNGKTSPASKDQRTGKKTSVQGQVQKGNDESESDFESDPPSPKSSEEEEQDDEEVLQGEQGDFNDDDTEPENLGHRPLLMDSEDEEEEEKHSSDSDYEQAKAKYSDMSSVYRDRSGSGPTQDLNTILLTSAQLSSDVAVETPKQEFDVFGAVPFFAVRAQQPQQEKNEKNLPQHRFPAAGLEQEEFDVFTKAPFSKKVNVQECHAVGPEAHTIPGYPKSVDVFGSTPFQPFLTSTSKSESNEDLFGLVPFDEITGSQQQKVKQRSLQKLSSRQRRTKQDMSKSNGKRHHGTPTSTKKTLKPTYRTPERARRHKKVGRRDSQSSNEFLTISDSKENISVALTDGKDRGNVLQPEESLLDPFGAKPFHSPDLSWHPPHQGLSDIRADHNTVLPGRPRQNSLHGSFHSADVLKMDDFGAVPFTELVVQSITPHQSQQSQPVELDPFGAAPFPSKQ	Literature-reported	"Synthesis and structure-activity relationships of 1,2,3,4-tetrahydropyrido[2,3-b]pyrazines as potent and selective inhibitors of the anaplastic lymphoma kinase. Bioorg Med Chem. 2010 Jun 15;18(12):4351-62."	0	EC:2.7	.	protein kinase superfamily. Ser/Thr protein kinase family.	2.7.11.1	Transferring phosphorus-containing groups	BMP-2-inducible protein kinase C-terminus; Protein kinase domain	PF15282; PF00069	PF15282; BMP2K_C; PF00069; Pkinase	.	.	hsa05202: Transcriptional misregulation in cancer	.	.	Q9NSY1
TTD3BSX	Bone morphogenetic protein 4 (BMP4)	P12644	BMP4_HUMAN	Growth factor	DVR4; Bone morphogenetic protein 2B; BMP2B; BMP-4; BMP-2B	BMP4	"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."	.	.	MIPGNRMLMVVLLCQVLLGGASHASLIPETGKKKVAEIQGHAGGRRSGQSHELLRDFEATLLQMFGLRRRPQPSKSAVIPDYMRDLYRLQSGEEEEEQIHSTGLEYPERPASRANTVRSFHHEEHLENIPGTSENSAFRFLFNLSSIPENEVISSAELRLFREQVDQGPDWERGFHRINIYEVMKPPAEVVPGHLITRLLDTRLVHHNVTRWETFDVSPAVLRWTREKQPNYGLAIEVTHLHQTRTHQGQHVRISRSLPQGSGNWAQLRPLLVTFGHDGRGHALTRRRRAKRSPKHHSQRARKKNKNCRRHSLYVDFSDVGWNDWIVAPPGYQAFYCHGDCPFPLADHLNSTNHAIVQTLVNSVNSSIPKACCVPTELSAISMLYLDEYDKVVLKNYQEMVVEGCGCR	Literature-reported	Bone morphogenetic protein-4: a novel therapeutic target for pathological cardiac hypertrophy/heart failure. Heart Fail Rev. 2014 Nov;19(6):781-8.	.	Growth factor	Transforming growth factor	TGF-beta family.	.	.	Transforming growth factor beta like domain; TGF-beta propeptide	PF00019; PF00688	PF00019; TGF_beta; PF00688; TGFb_propeptide	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04350: TGF-beta signaling pathway; hsa04390: Hippo signaling pathway; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04919: Thyroid hormone signaling pathway; hsa05200: Pathways in cancer; hsa05217: Basal cell carcinoma; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-2129379: Molecules associated with elastic fibres; R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation	.	P12644
TT07RIB	Bone morphogenetic protein 6 (BMP6)	P22004	BMP6_HUMAN	.	BMP-6; VG-1-related protein; VG-1-R; VGR-1	BMP6	Induces cartilage and bone formation.	.	.	MPGLGRRAQWLCWWWGLLCSCCGPPPLRPPLPAAAAAAAGGQLLGDGGSPGRTEQPPPSPQSSSGFLYRRLKTQEKREMQKEILSVLGLPHRPRPLHGLQQPQPPALRQQEEQQQQQQLPRGEPPPGRLKSAPLFMLDLYNALSADNDEDGASEGERQQSWPHEAASSSQRRQPPPGAAHPLNRKSLLAPGSGSGGASPLTSAQDSAFLNDADMVMSFVNLVEYDKEFSPRQRHHKEFKFNLSQIPEGEVVTAAEFRIYKDCVMGSFKNQTFLISIYQVLQEHQHRDSDLFLLDTRVVWASEEGWLEFDITATSNLWVVTPQHNMGLQLSVVTRDGVHVHPRAAGLVGRDGPYDKQPFMVAFFKVSEVHVRTTRSASSRRRQQSRNRSTQSQDVARVSSASDYNSSELKTACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAPTKLNAISVLYFDDNSNVILKKYRNMVVRACGCH	Clinical trial	Targeting the hepcidin-ferroportin pathway in anaemia of chronic kidney disease. Br J Clin Pharmacol. 2019 May;85(5):935-948.	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04350: TGF-beta signaling pathway; hsa04390: Hippo signaling pathway; hsa04913: Ovarian steroidogenesis	.	.	P22004
TTKOBRA	Bone morphogenetic protein 7 (BMP7)	P18075	BMP7_HUMAN	.	BMP-7; Osteogenic protein 1; OP-1; Eptotermin alfa	BMP7	"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."	.	.	MHVRSLRAAAPHSFVALWAPLFLLRSALADFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAMAVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPRYHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLLDSRTLWASEEGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKATEVHFRSIRSTGSKQRSQNRSKTPKNQEALRMANVAENSSSDQRQACKKHELYVSFRDLGWQDWIIAPEGYAAYYCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKPCCAPTQLNAISVLYFDDSSNVILKKYRNMVVRACGCH	Clinical trial	Perioperative THR-184 and AKI after Cardiac Surgery. J Am Soc Nephrol. 2018 Feb;29(2):670-679.	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04350: TGF-beta signaling pathway; hsa04360: Axon guidance; hsa04390: Hippo signaling pathway	R-HSA-2129379: Molecules associated with elastic fibres	.	P18075
TTGKF90	Bone morphogenetic protein receptor (BMPR2)	Q13873	BMPR2_HUMAN	Kinase	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	BMPR2	"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."	EC 2.7.11.30	3G2F; 2HLQ	MTSSLQRPWRVPWLPWTILLVSTAAASQNQERLCAFKDPYQQDLGIGESRISHENGTILCSKGSTCYGLWEKSKGDINLVKQGCWSHIGDPQECHYEECVVTTTPPSIQNGTYRFCCCSTDLCNVNFTENFPPPDTTPLSPPHSFNRDETIIIALASVSVLAVLIVALCFGYRMLTGDRKQGLHSMNMMEAAASEPSLDLDNLKLLELIGRGRYGAVYKGSLDERPVAVKVFSFANRQNFINEKNIYRVPLMEHDNIARFIVGDERVTADGRMEYLLVMEYYPNGSLCKYLSLHTSDWVSSCRLAHSVTRGLAYLHTELPRGDHYKPAISHRDLNSRNVLVKNDGTCVISDFGLSMRLTGNRLVRPGEEDNAAISEVGTIRYMAPEVLEGAVNLRDCESALKQVDMYALGLIYWEIFMRCTDLFPGESVPEYQMAFQTEVGNHPTFEDMQVLVSREKQRPKFPEAWKENSLAVRSLKETIEDCWDQDAEARLTAQCAEERMAELMMIWERNKSVSPTVNPMSTAMQNERNLSHNRRVPKIGPYPDYSSSSYIEDSIHHTDSIVKNISSEHSMSSTPLTIGEKNRNSINYERQQAQARIPSPETSVTSLSTNTTTTNTTGLTPSTGMTTISEMPYPDETNLHTTNVAQSIGPTPVCLQLTEEDLETNKLDPKEVDKNLKESSDENLMEHSLKQFSGPDPLSSTSSSLLYPLIKLAVEATGQQDFTQTANGQACLIPDVLPTQIYPLPKQQNLPKRPTSLPLNTKNSTKEPRLKFGSKHKSNLKQVETGVAKMNTINAAEPHVVTVTMNGVAGRNHSVNSHAATTQYANGTVLSGQTTNIVTHRAQEMLQNQFIGEDTRLNINSSPDEHEPLLRREQQAGHDEGVLDRLVDRRERPLEGGRTNSNNNNSNPCSEQDVLAQGVPSTAADPGPSKPRRAQRPNSLDLSATNVLDGSSIQIGESTQDGKSGSGEKIKKRVKTPYSLKRWRPSTWVISTESLDCEVNNNGSNRAVHSKSSTAVYLAEGGTATTMVSKDIGMNCL	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1794).	0	EC:2.7	Kinase	protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.	2.7.11.30	Transferring phosphorus-containing groups	Activin types I and II receptor domain; Protein kinase domain	PF01064; PF00069	PF01064; Activin_recp; PF00069; Pkinase	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04350:TGF-beta signaling pathway; hsa04390:Hippo signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells	R-HSA-201451: Signaling by BMP	.	Q13873
TTN2I9E	Tyrosine-protein kinase BMX (BMX)	P51813	BMX_HUMAN	Kinase	NTK38; Epithelial and endothelial tyrosine kinase; ETK; Cytoplasmic tyrosine-protein kinase BMX; Bone marrow tyrosine kinase gene in chromosome X protein	BMX	"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."	EC 2.7.10.2	3SXS; 3SXR; 2YS2; 2EKX	MDTKSILEELLLKRSQQKKKMSPNNYKERLFVLTKTNLSYYEYDKMKRGSRKGSIEIKKIRCVEKVNLEEQTPVERQYPFQIVYKDGLLYVYASNEESRSQWLKALQKEIRGNPHLLVKYHSGFFVDGKFLCCQQSCKAAPGCTLWEAYANLHTAVNEEKHRVPTFPDRVLKIPRAVPVLKMDAPSSSTTLAQYDNESKKNYGSQPPSSSTSLAQYDSNSKKIYGSQPNFNMQYIPREDFPDWWQVRKLKSSSSSEDVASSNQKERNVNHTTSKISWEFPESSSSEEEENLDDYDWFAGNISRSQSEQLLRQKGKEGAFMVRNSSQVGMYTVSLFSKAVNDKKGTVKHYHVHTNAENKLYLAENYCFDSIPKLIHYHQHNSAGMITRLRHPVSTKANKVPDSVSLGNGIWELKREEITLLKELGSGQFGVVQLGKWKGQYDVAVKMIKEGSMSEDEFFQEAQTMMKLSHPKLVKFYGVCSKEYPIYIVTEYISNGCLLNYLRSHGKGLEPSQLLEMCYDVCEGMAFLESHQFIHRDLAARNCLVDRDLCVKVSDFGMTRYVLDDQYVSSVGTKFPVKWSAPEVFHYFKYSSKSDVWAFGILMWEVFSLGKQPYDLYDNSQVVLKVSQGHRLYRPHLASDTIYQIMYSCWHELPEKRPTFQQLLSSIEPLREKDKH	Patented-recorded	"Discovery of a series of 2,5-diaminopyrimidine covalent irreversible inhibitors of Bruton's tyrosine kinase with in vivo antitumor activity. J Med Chem. 2014 Jun 26;57(12):5112-28."	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. TEC subfamily.	2.7.10.2	Transferring phosphorus-containing groups	BTK motif; PH domain; Protein tyrosine kinase; SH2 domain	PF00779; PF00169; PF07714; PF00017	PF00779; BTK; PF00169; PH; PF07714; Pkinase_Tyr; PF00017; SH2	.	.	.	R-HSA-111465: Apoptotic cleavage of cellular proteins; R-HSA-1660499: Synthesis of PIPs at the plasma membrane	.	P51813
TTDYAKQ	Borna disease virus Glycoprotein p56 (BoDV p56)	Q89857	Q89857_BDV1	.	Glycoprotein	BoDV p56	Required for neuronal dissemination of Borna disease virus	.	.	MQPSMSFLIGFGTLVLVLSARTFDLQGLSCNTDSTPGLIDLEIRRLCHTPTENVISCEVSYLNHTTISLPAVHTSCLKYHCKTYWGFFGSYSADRIINRYTGTVKGCLNNSAPEDPFECNWFYCCSAITTEICRCSITNVTVAVQTFPPFMYCSFADCSTVSQQELESGKAMLSDGSTLTYTPYILQSEVVNKTLNGTILCNSSSKIVSFDEFRRSYSLTNGSYQSSSINVTCANYTSSCRPRLKRRRRDTQQIEYLVHKLRPTLKDAWEDCEILQSLLLGVFGTGIASASQFLRSWLNHPDIIGYIVNGVGVVWQCHRVNVTFMTWNESTYYPPVDYNGRKYFLNDEGRLQTNTPEARPGLKRVMWFGRYFLGTVGSGVKPRRIRYNKTSHDYHLEEFEASLNMTPQTSIASGHETDPINHAYGTQADLLPYTRSSNITSTDTGSGWVHIGLPSFAFLNPLGWLRDLLAWAAWLGGVLYLISLCVSLPASFARRRRLGRWQE	Literature-reported	Borna disease virus glycoprotein is required for viral dissemination in neurons. J Virol. 2003 Nov;77(22):12222-31.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTTZ3EU	Valacyclovir hydrolase (BPHL)	Q86WA6	BPHL_HUMAN	Carboxylic ester hydrolase	"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"	BPHL	"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."	EC 3.1.-.-	2OCL; 2OCK; 2OCI; 2OCG	MVAVLGGRGVLRLRLLLSALKPGIHVPRAGPAAAFGTSVTSAKVAVNGVQLHYQQTGEGDHAVLLLPGMLGSGETDFGPQLKNLNKKLFTVVAWDPRGYGHSRPPDRDFPADFFERDAKDAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIWGANAYVTDEDSMIYEGIRDVSKWSERTRKPLEALYGYDYFARTCEKWVDGIRQFKHLPDGNICRHLLPRVQCPALIVHGEKDPLVPRFHADFIHKHVKGSRLHLMPEGKHNLHLRFADEFNKLAEDFLQ	Literature-reported	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-211945: Phase I - Functionalization of compounds	.	Q86WA6
TTXCSDR	Protein bactericidal permeability-increasing (BPI)	P17213	BPI_HUMAN	Bactericidal permeability increasing protein	CAP 57; BPI	BPI	"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}."	.	1EWF; 1BP1	MRENMARGPCNAPRWASLMVLVAIGTAVTAAVNPGVVVRISQKGLDYASQQGTAALQKELKRIKIPDYSDSFKIKHLGKGHYSFYSMDIREFQLPSSQISMVPNVGLKFSISNANIKISGKWKAQKRFLKMSGNFDLSIEGMSISADLKLGSNPTSGKPTITCSSCSSHINSVHVHISKSKVGWLIQLFHKKIESALRNKMNSQVCEKVTNSVSSELQPYFQTLPVMTKIDSVAGINYGLVAPPATTAETLDVQMKGEFYSENHHNPPPFAPPVMEFPAAHDRMVYLGLSDYFFNTAGLVYQEAGVLKMTLRDDMIPKESKFRLTTKFFGTFLPEVAKKFPNMKIQIHVSASTPPHLSVQPTGLTFYPAVDVQAFAVLPNSSLASLFLIGMHTTGSMEVSAESNRLVGELKLDRLLLELKHSNIGPFPVELLQDIMNYIVPILVLPRVNEKLQKGFPLPTPARVQLYNVVLQPHQNFLLFGADVVYK	Clinical trial	Modulating immunity as a therapy for bacterial infections. Nat Rev Microbiol. 2012 Mar 16;10(4):243-54.	21	.	.	.	.	.	.	.	.	.	.	.	R-HSA-166016: Toll Like Receptor 4 (TLR4) Cascade; R-HSA-6798695: Neutrophil degranulation; R-HSA-6803157: Antimicrobial peptides	.	P17213
TT0EOB8	B-Raf messenger RNA (BRAF mRNA)	P15056	BRAF_HUMAN	mRNA target	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)	BRAF	"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."	EC 2.7.11.1	6CAD; 6B8U; 5VYK; 5VR3; 5VAM	MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1943).	21	mRNA	mRNA target	.	.	.	Phorbol esters/diacylglycerol binding domain (C1 domain); Protein tyrosine kinase; Raf-like Ras-binding domain	PF00130; PF07714; PF02196	PF00130; C1_1; PF07714; Pkinase_Tyr; PF02196; RBD	.	.	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	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	.	P15056
TTWCGQT	Serine/threonine-protein kinase B-raf (BRAF)	P15056	BRAF_HUMAN	Kinase	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	BRAF	"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."	EC 2.7.11.1	6CAD; 6B8U; 5VYK; 5VR3; 5VAM	MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH	Successful	"Clinical pipeline report, company report or official report of GlaxoSmithKline (2011)."	34	EC:2.7	Kinase	protein kinase superfamily. TKL Ser/Thr protein kinase family. RAF subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Phorbol esters/diacylglycerol binding domain (C1 domain); Protein tyrosine kinase; Raf-like Ras-binding domain	PF00130; PF07714; PF02196	PF00130; C1_1; PF07714; Pkinase_Tyr; PF02196; RBD	.	.	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	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	.	P15056
TT9591D	BRAF V600E mutant (BRAF V600E)	P15056	BRAF_HUMAN	Kinase	Proto-oncogene B-Raf; p94; v-Raf murine sarcoma viral oncogene homolog B1	BRAF	"Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus (Probable). Phosphorylates MAP2K1, and thereby activates the MAP kinase signal transduction pathway (PubMed:21441910, PubMed:29433126). Phosphorylates PFKFB2 (PubMed:36402789). May play a role in the postsynaptic responses of hippocampal neurons (PubMed:1508179). {ECO:0000269|PubMed:1508179, ECO:0000269|PubMed:21441910, ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:36402789, ECO:0000305}."	EC 2.7.11.1	1UWH;1UWJ;2FB8;2L05;3C4C;3D4Q;3IDP;3II5;3NY5;3OG7;3PPJ;3PPK;3PRF;3PRI;3PSB;3PSD;3Q4C;3Q96;3SKC;3TV4;3TV6;4CQE;4DBN;4E26;4E4X;4EHE;4EHG;4FC0;4FK3;4G9C;4G9R;4H58;4JVG;4KSP;4KSQ;4MBJ;4MNE;4MNF;4PP7;4R5Y;4RZV;4RZW;4WO5;4XV1;4XV2;4XV3;4XV9;4YHT;5C9C;5CSW;5CSX;5CT7;5FD2;5HI2;5HID;5HIE;5ITA;5J17;5J18;5J2R;5JRQ;5JSM;5JT2;5VAL;5VAM;5VR3;5VYK;6B8U;6CAD;6N0P;6N0Q;6NSQ;6NYB;6P3D;6P7G;6PP9;6Q0J;6Q0K;6Q0T;6U2G;6U2H;6UAN;6UUO;6V2U;6V2W;6V34;6XAG;6XFP;6XLO;7K0V;7M0T;7M0U;7M0V;7M0W;7M0X;7M0Y;7M0Z;7MFD;7MFE;7MFF;7P3V;7SHV;7ZR0;7ZR5;7ZR6;8C7X;8C7Y;8DGS;8DGT;8F7O;8F7P	MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH	Clinical trial	"Clinical pipeline report, company report or official report of Roche"	.	.	.	.	.	.	.	.	.	.	.	hsa:673	R-HSA-1295596;R-HSA-170968;R-HSA-170984;R-HSA-187706;R-HSA-5673000;R-HSA-5674135;R-HSA-5674499;R-HSA-5675221;R-HSA-6802946;R-HSA-6802948;R-HSA-6802952;R-HSA-6802955;R-HSA-9649948;R-HSA-9656223;R-HSA-9726840;R-HSA-9726842;	.	P15056;
TTUARD6	Breast cancer type 2 susceptibility protein (BRCA2)	P51587	BRCA2_HUMAN	.	Fanconi anemia group D1 protein; FANCD1; FACD	BRCA2	"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."	.	3EU7; 1N0W	MPIGSKERPTFFEIFKTRCNKADLGPISLNWFEELSSEAPPYNSEPAEESEHKNNNYEPNLFKTPQRKPSYNQLASTPIIFKEQGLTLPLYQSPVKELDKFKLDLGRNVPNSRHKSLRTVKTKMDQADDVSCPLLNSCLSESPVVLQCTHVTPQRDKSVVCGSLFHTPKFVKGRQTPKHISESLGAEVDPDMSWSSSLATPPTLSSTVLIVRNEEASETVFPHDTTANVKSYFSNHDESLKKNDRFIASVTDSENTNQREAASHGFGKTSGNSFKVNSCKDHIGKSMPNVLEDEVYETVVDTSEEDSFSLCFSKCRTKNLQKVRTSKTRKKIFHEANADECEKSKNQVKEKYSFVSEVEPNDTDPLDSNVANQKPFESGSDKISKEVVPSLACEWSQLTLSGLNGAQMEKIPLLHISSCDQNISEKDLLDTENKRKKDFLTSENSLPRISSLPKSEKPLNEETVVNKRDEEQHLESHTDCILAVKQAISGTSPVASSFQGIKKSIFRIRESPKETFNASFSGHMTDPNFKKETEASESGLEIHTVCSQKEDSLCPNLIDNGSWPATTTQNSVALKNAGLISTLKKKTNKFIYAIHDETSYKGKKIPKDQKSELINCSAQFEANAFEAPLTFANADSGLLHSSVKRSCSQNDSEEPTLSLTSSFGTILRKCSRNETCSNNTVISQDLDYKEAKCNKEKLQLFITPEADSLSCLQEGQCENDPKSKKVSDIKEEVLAAACHPVQHSKVEYSDTDFQSQKSLLYDHENASTLILTPTSKDVLSNLVMISRGKESYKMSDKLKGNNYESDVELTKNIPMEKNQDVCALNENYKNVELLPPEKYMRVASPSRKVQFNQNTNLRVIQKNQEETTSISKITVNPDSEELFSDNENNFVFQVANERNNLALGNTKELHETDLTCVNEPIFKNSTMVLYGDTGDKQATQVSIKKDLVYVLAEENKNSVKQHIKMTLGQDLKSDISLNIDKIPEKNNDYMNKWAGLLGPISNHSFGGSFRTASNKEIKLSEHNIKKSKMFFKDIEEQYPTSLACVEIVNTLALDNQKKLSKPQSINTVSAHLQSSVVVSDCKNSHITPQMLFSKQDFNSNHNLTPSQKAEITELSTILEESGSQFEFTQFRKPSYILQKSTFEVPENQMTILKTTSEECRDADLHVIMNAPSIGQVDSSKQFEGTVEIKRKFAGLLKNDCNKSASGYLTDENEVGFRGFYSAHGTKLNVSTEALQKAVKLFSDIENISEETSAEVHPISLSSSKCHDSVVSMFKIENHNDKTVSEKNNKCQLILQNNIEMTTGTFVEEITENYKRNTENEDNKYTAASRNSHNLEFDGSDSSKNDTVCIHKDETDLLFTDQHNICLKLSGQFMKEGNTQIKEDLSDLTFLEVAKAQEACHGNTSNKEQLTATKTEQNIKDFETSDTFFQTASGKNISVAKESFNKIVNFFDQKPEELHNFSLNSELHSDIRKNKMDILSYEETDIVKHKILKESVPVGTGNQLVTFQGQPERDEKIKEPTLLGFHTASGKKVKIAKESLDKVKNLFDEKEQGTSEITSFSHQWAKTLKYREACKDLELACETIEITAAPKCKEMQNSLNNDKNLVSIETVVPPKLLSDNLCRQTENLKTSKSIFLKVKVHENVEKETAKSPATCYTNQSPYSVIENSALAFYTSCSRKTSVSQTSLLEAKKWLREGIFDGQPERINTADYVGNYLYENNSNSTIAENDKNHLSEKQDTYLSNSSMSNSYSYHSDEVYNDSGYLSKNKLDSGIEPVLKNVEDQKNTSFSKVISNVKDANAYPQTVNEDICVEELVTSSSPCKNKNAAIKLSISNSNNFEVGPPAFRIASGKIVCVSHETIKKVKDIFTDSFSKVIKENNENKSKICQTKIMAGCYEALDDSEDILHNSLDNDECSTHSHKVFADIQSEEILQHNQNMSGLEKVSKISPCDVSLETSDICKCSIGKLHKSVSSANTCGIFSTASGKSVQVSDASLQNARQVFSEIEDSTKQVFSKVLFKSNEHSDQLTREENTAIRTPEHLISQKGFSYNVVNSSAFSGFSTASGKQVSILESSLHKVKGVLEEFDLIRTEHSLHYSPTSRQNVSKILPRVDKRNPEHCVNSEMEKTCSKEFKLSNNLNVEGGSSENNHSIKVSPYLSQFQQDKQQLVLGTKVSLVENIHVLGKEQASPKNVKMEIGKTETFSDVPVKTNIEVCSTYSKDSENYFETEAVEIAKAFMEDDELTDSKLPSHATHSLFTCPENEEMVLSNSRIGKRRGEPLILVGEPSIKRNLLNEFDRIIENQEKSLKASKSTPDGTIKDRRLFMHHVSLEPITCVPFRTTKERQEIQNPNFTAPGQEFLSKSHLYEHLTLEKSSSNLAVSGHPFYQVSATRNEKMRHLITTGRPTKVFVPPFKTKSHFHRVEQCVRNINLEENRQKQNIDGHGSDDSKNKINDNEIHQFNKNNSNQAAAVTFTKCEEEPLDLITSLQNARDIQDMRIKKKQRQRVFPQPGSLYLAKTSTLPRISLKAAVGGQVPSACSHKQLYTYGVSKHCIKINSKNAESFQFHTEDYFGKESLWTGKGIQLADGGWLIPSNDGKAGKEEFYRALCDTPGVDPKLISRIWVYNHYRWIIWKLAAMECAFPKEFANRCLSPERVLLQLKYRYDTEIDRSRRSAIKKIMERDDTAAKTLVLCVSDIISLSANISETSSNKTSSADTQKVAIIELTDGWYAVKAQLDPPLLAVLKNGRLTVGQKIILHGAELVGSPDACTPLEAPESLMLKISANSTRPARWYTKLGFFPDPRPFPLPLSSLFSDGGNVGCVDVIIQRAYPIQWMEKTSSGLYIFRNEREEEKEAAKYVEAQQKRLEALFTKIQEEFEEHEENTTKPYLPSRALTRQQVRALQDGAELYEAVKNAADPAYLEGYFSEEQLRALNNHRQMLNDKKQAQIQLEIRKAMESAEQKEQGLSRDVTTVWKLRIVSYSKKEKDSVILSIWRPSSDLYSLLTEGKRYRIYHLATSKSKSKSERANIQLAATKKTQYQQLPVSDEILFQIYQPREPLHFSKFLDPDFQPSCSEVDLIGFVVSVVKKTGLAPFVYLSDECYNLLAIKFWIDLNEDIIKPHMLIAASNLQWRPESKSGLLTLFAGDFSVFSASPKEGHFQETFNKMKNTVENIDILCNEAENKLMHILHANDPKWSTPTKDCTSGPYTAQIIPGTGNKLLMSSPNCEIYYQSPLSLCMAKRKSVSTPVSAQMTSKSCKGEKEIDDQKNCKKRRALDFLSRLPLPPPVSPICTFVSPAAQKAFQPPRSCGTKYETPIKKKELNSPQMTPFKKFNEISLLESNSIADEELALINTQALLSGSTGEKQFISVSESTRTAPTSSEDYLRLKRRCTTSLIKEQESSQASTEECEKNKQDTITTKKYI	Literature-reported	Molecular prescreening to select patient population in early clinical trials. Nat Rev Clin Oncol. 2012 Apr 3;9(6):359-66. 	.	.	DNA repair	.	.	.	"BRCA2, helical; BRCA2, oligonucleotide/oligosaccharide-binding, domain 1; BRCA2, oligonucleotide/oligosaccharide-binding, domain 3; BRCA2 repeat; Tower"	PF09169; PF09103; PF09104; PF00634; PF09121	PF09169; BRCA-2_helical; PF09103; BRCA-2_OB1; PF09104; BRCA-2_OB3; PF00634; BRCA2; PF09121; Tower	.	.	hsa03440: Homologous recombination; hsa03460: Fanconi anemia pathway; hsa05200: Pathways in cancer; hsa05212: Pancreatic cancer; hsa05224: Breast cancer	R-HSA-5685939: HDR through MMEJ (alt-NHEJ); R-HSA-5685942: HDR through Homologous Recombination (HRR); R-HSA-5693554: Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA); R-HSA-5693568: Resolution of D-loop Structures through Holliday Junction Intermediates; R-HSA-5693579: Homologous DNA Pairing and Strand Exchange; R-HSA-5693616: Presynaptic phase of homologous DNA pairing and strand exchange; R-HSA-912446: Meiotic recombination; R-HSA-9701192: Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function; R-HSA-9704331: Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function; R-HSA-9704646: Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function; R-HSA-9709275: Impaired BRCA2 translocation to the nucleus; R-HSA-9709570: Impaired BRCA2 binding to RAD51; R-HSA-9709603: Impaired BRCA2 binding to PALB2; R-HSA-9763198: Impaired BRCA2 binding to SEM1 (DSS1)	.	.
TTT09OB	Bromodomain-containing protein 1 (BRD1)	O95696	BRD1_HUMAN	Bromodomain	Bromodomain and PHD finger-containing protein 2; BRPF2; BRL; BR140-like protein	BRD1	Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.	.	5PWB; 5PWA; 5PW9; 5PW8; 5PW7	MRRKGRCHRGSAARHPSSPCSVKHSPTRETLTYAQAQRMVEIEIEGRLHRISIFDPLEIILEDDLTAQEMSECNSNKENSERPPVCLRTKRHKNNRVKKKNEALPSAHGTPASASALPEPKVRIVEYSPPSAPRRPPVYYKFIEKSAEELDNEVEYDMDEEDYAWLEIVNEKRKGDCVPAVSQSMFEFLMDRFEKESHCENQKQGEQQSLIDEDAVCCICMDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRHCLQSRARPADCVLCPNKGGAFKKTDDDRWGHVVCALWIPEVGFANTVFIEPIDGVRNIPPARWKLTCYLCKQKGVGACIQCHKANCYTAFHVTCAQKAGLYMKMEPVKELTGGGTTFSVRKTAYCDVHTPPGCTRRPLNIYGDVEMKNGVCRKESSVKTVRSTSKVRKKAKKAKKALAEPCAVLPTVCAPYIPPQRLNRIANQVAIQRKKQFVERAHSYWLLKRLSRNGAPLLRRLQSSLQSQRSSQQRENDEEMKAAKEKLKYWQRLRHDLERARLLIELLRKREKLKREQVKVEQVAMELRLTPLTVLLRSVLDQLQDKDPARIFAQPVSLKEVPDYLDHIKHPMDFATMRKRLEAQGYKNLHEFEEDFDLIIDNCMKYNARDTVFYRAAVRLRDQGGVVLRQARREVDSIGLEEASGMHLPERPAAAPRRPFSWEDVDRLLDPANRAHLGLEEQLRELLDMLDLTCAMKSSGSRSKRAKLLKKEIALLRNKLSQQHSQPLPTGPGLEGFEEDGAALGPEAGEEVLPRLETLLQPRKRSRSTCGDSEVEEESPGKRLDAGLTNGFGGARSEQEPGGGLGRKATPRRRCASESSISSSNSPLCDSSFNAPKCGRGKPALVRRHTLEDRSELISCIENGNYAKAARIAAEVGQSSMWISTDAAASVLEPLKVVWAKCSGYPSYPALIIDPKMPRVPGHHNGVTIPAPPLDVLKIGEHMQTKSDEKLFLVLFFDNKRSWQWLPKSKMVPLGIDETIDKLKMMEGRNSSIRKAVRIAFDRAMNHLSRVHGEPTSDLSDID	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2724).	0	.	.	.	.	.	Bromodomain; Enhancer of polycomb-like; PWWP domain	PF00439; PF10513; PF00855	PF00439; Bromodomain; PF10513; EPL1; PF00855; PWWP	.	.	.	R-HSA-3214847: HATs acetylate histones; R-HSA-6804758: Regulation of TP53 Activity through Acetylation	.	O95696
TTDP48B	Bromodomain-containing protein 2 (BRD2)	P25440	BRD2_HUMAN	Bromodomain	Really interesting new gene 3 protein; RING3; O27.1.1; KIAA9001	BRD2	"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."	.	6MOA; 6MO9; 6MO8; 6MO7; 6FFG	MLQNVTPHNKLPGEGNAGLLGLGPEAAAPGKRIRKPSLLYEGFESPTMASVPALQLTPANPPPPEVSNPKKPGRVTNQLQYLHKVVMKALWKHQFAWPFRQPVDAVKLGLPDYHKIIKQPMDMGTIKRRLENNYYWAASECMQDFNTMFTNCYIYNKPTDDIVLMAQTLEKIFLQKVASMPQEEQELVVTIPKNSHKKGAKLAALQGSVTSAHQVPAVSSVSHTALYTPPPEIPTTVLNIPHPSVISSPLLKSLHSAGPPLLAVTAAPPAQPLAKKKGVKRKADTTTPTPTAILAPGSPASPPGSLEPKAARLPPMRRESGRPIKPPRKDLPDSQQQHQSSKKGKLSEQLKHCNGILKELLSKKHAAYAWPFYKPVDASALGLHDYHDIIKHPMDLSTVKRKMENRDYRDAQEFAADVRLMFSNCYKYNPPDHDVVAMARKLQDVFEFRYAKMPDEPLEPGPLPVSTAMPPGLAKSSSESSSEESSSESSSEEEEEEDEEDEEEEESESSDSEEERAHRLAELQEQLRAVHEQLAALSQGPISKPKRKREKKEKKKKRKAEKHRGRAGADEDDKGPRAPRPPQPKKSKKASGSGGGSAALGPSGFGPSGGSGTKLPKKATKTAPPALPTGYDSEEEEESRPMSYDEKRQLSLDINKLPGEKLGRVVHIIQAREPSLRDSNPEEIEIDFETLKPSTLRELERYVLSCLRKKPRKPYTIKKPVGKTKEELALEKKRELEKRLQDVSGQLNSTKKPPKKANEKTESSSAQQVAVSRLSASSSSSDSSSSSSSSSSSDTSDSDSG	Clinical trial	Targeting bromodomains: epigenetic readers of lysine acetylation.Nat Rev Drug Discov.2014 May;13(5):337-56.	17	Bromodomain	Bromodomain	.	.	.	Bromodomain extra-terminal - transcription regulation; Bromodomain	PF17035; PF00439	PF17035; BET; PF00439; Bromodomain	.	.	.	R-HSA-8951936: RUNX3 regulates p14-ARF	.	P25440
TTNISW6	HUMAN bromodomain-containing protein 2 (BRD2)	P25440	BRD2_HUMAN	Bromodomain	Really interesting new gene 3 protein; RING3; O27.1.1; KIAA9001	BRD2	"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."	.	6MOA; 6MO9; 6MO8; 6MO7; 6FFG	MLQNVTPHNKLPGEGNAGLLGLGPEAAAPGKRIRKPSLLYEGFESPTMASVPALQLTPANPPPPEVSNPKKPGRVTNQLQYLHKVVMKALWKHQFAWPFRQPVDAVKLGLPDYHKIIKQPMDMGTIKRRLENNYYWAASECMQDFNTMFTNCYIYNKPTDDIVLMAQTLEKIFLQKVASMPQEEQELVVTIPKNSHKKGAKLAALQGSVTSAHQVPAVSSVSHTALYTPPPEIPTTVLNIPHPSVISSPLLKSLHSAGPPLLAVTAAPPAQPLAKKKGVKRKADTTTPTPTAILAPGSPASPPGSLEPKAARLPPMRRESGRPIKPPRKDLPDSQQQHQSSKKGKLSEQLKHCNGILKELLSKKHAAYAWPFYKPVDASALGLHDYHDIIKHPMDLSTVKRKMENRDYRDAQEFAADVRLMFSNCYKYNPPDHDVVAMARKLQDVFEFRYAKMPDEPLEPGPLPVSTAMPPGLAKSSSESSSEESSSESSSEEEEEEDEEDEEEEESESSDSEEERAHRLAELQEQLRAVHEQLAALSQGPISKPKRKREKKEKKKKRKAEKHRGRAGADEDDKGPRAPRPPQPKKSKKASGSGGGSAALGPSGFGPSGGSGTKLPKKATKTAPPALPTGYDSEEEEESRPMSYDEKRQLSLDINKLPGEKLGRVVHIIQAREPSLRDSNPEEIEIDFETLKPSTLRELERYVLSCLRKKPRKPYTIKKPVGKTKEELALEKKRELEKRLQDVSGQLNSTKKPPKKANEKTESSSAQQVAVSRLSASSSSSDSSSSSSSSSSSDTSDSDSG	.	Uncovering the Role of BRD2 in COVID-19. 2020-03-19	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-8951936: RUNX3 regulates p14-ARF	.	P25440
TTHE657	Bromodomain-containing protein 3 (BRD3)	Q15059	BRD3_HUMAN	Bromodomain	RING3like protein; RING3L; RING3-like protein; KIAA0043	BRD3	"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."	.	6I7A; 6I68; 6I5P; 6I41; 6BGH	MSTATTVAPAGIPATPGPVNPPPPEVSNPSKPGRKTNQLQYMQNVVVKTLWKHQFAWPFYQPVDAIKLNLPDYHKIIKNPMDMGTIKKRLENNYYWSASECMQDFNTMFTNCYIYNKPTDDIVLMAQALEKIFLQKVAQMPQEEVELLPPAPKGKGRKPAAGAQSAGTQQVAAVSSVSPATPFQSVPPTVSQTPVIAATPVPTITANVTSVPVPPAAAPPPPATPIVPVVPPTPPVVKKKGVKRKADTTTPTTSAITASRSESPPPLSDPKQAKVVARRESGGRPIKPPKKDLEDGEVPQHAGKKGKLSEHLRYCDSILREMLSKKHAAYAWPFYKPVDAEALELHDYHDIIKHPMDLSTVKRKMDGREYPDAQGFAADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPVEAPALPAPAAPMVSKGAESSRSSEESSSDSGSSDSEEERATRLAELQEQLKAVHEQLAALSQAPVNKPKKKKEKKEKEKKKKDKEKEKEKHKVKAEEEKKAKVAPPAKQAQQKKAPAKKANSTTTAGRQLKKGGKQASASYDSEEEEEGLPMSYDEKRQLSLDINRLPGEKLGRVVHIIQSREPSLRDSNPDEIEIDFETLKPTTLRELERYVKSCLQKKQRKPFSASGKKQAAKSKEELAQEKKKELEKRLQDVSGQLSSSKKPARKEKPGSAPSGGPSRLSSSSSSESGSSSSSGSSSDSSDSE	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	Bromodomain	Bromodomain	.	.	.	Bromodomain extra-terminal - transcription regulation; Bromodomain	PF17035; PF00439	PF17035; BET; PF00439; Bromodomain	.	.	.	.	.	Q15059
TTSRAOU	HUMAN bromodomain-containing protein 4 (BRD4)	O60885	BRD4_HUMAN	Bromodomain	Protein HUNK1; HUNK1	BRD4	"Human protein bromodomain containing 4 interacts with SARS-CoV-2 E protein with high significance, which indicates BRD4 as a potential therapeutic target."	.	6Q3Z; 6Q3Y; 6MNL; 6MAU; 6HDQ	MSAESGPGTRLRNLPVMGDGLETSQMSTTQAQAQPQPANAASTNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKIIKTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQKINELPTEETEIMIVQAKGRGRGRKETGTAKPGVSTVPNTTQASTPPQTQTPQPNPPPVQATPHPFPAVTPDLIVQTPVMTVVPPQPLQTPPPVPPQPQPPPAPAPQPVQSHPPIIAATPQPVKTKKGVKRKADTTTPTTIDPIHEPPSLPPEPKTTKLGQRRESSRPVKPPKKDVPDSQQHPAPEKSSKVSEQLKCCSGILKEMFAKKHAAYAWPFYKPVDVEALGLHDYCDIIKHPMDMSTIKSKLEAREYRDAQEFGADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPEEPVVAVSSPAVPPPTKVVAPPSSSDSSSDSSSDSDSSTDDSEEERAQRLAELQEQLKAVHEQLAALSQPQQNKPKKKEKDKKEKKKEKHKRKEEVEENKKSKAKEPPPKKTKKNNSSNSNVSKKEPAPMKSKPPPTYESEEEDKCKPMSYEEKRQLSLDINKLPGEKLGRVVHIIQSREPSLKNSNPDEIEIDFETLKPSTLRELERYVTSCLRKKRKPQAEKVDVIAGSSKMKGFSSSESESSSESSSSDSEDSETEMAPKSKKKGHPGREQKKHHHHHHQQMQQAPAPVPQQPPPPPQQPPPPPPPQQQQQPPPPPPPPSMPQQAAPAMKSSPPPFIATQVPVLEPQLPGSVFDPIGHFTQPILHLPQPELPPHLPQPPEHSTPPHLNQHAVVSPPALHNALPQQPSRPSNRAAALPPKPARPPAVSPALTQTPLLPQPPMAQPPQVLLEDEEPPAPPLTSMQMQLYLQQLQKVQPPTPLLPSVKVQSQPPPPLPPPPHPSVQQQLQQQPPPPPPPQPQPPPQQQHQPPPRPVHLQPMQFSTHIQQPPPPQGQQPPHPPPGQQPPPPQPAKPQQVIQHHHSPRHHKSDPYSTGHLREAPSPLMIHSPQMSQFQSLTHQSPPQQNVQPKKQELRAASVVQPQPLVVVKEEKIHSPIIRSEPFSPSLRPEPPKHPESIKAPVHLPQRPEMKPVDVGRPVIRPPEQNAPPPGAPDKDKQKQEPKTPVAPKKDLKIKNMGSWASLVQKHPTTPSSTAKSSSDSFEQFRRAAREKEEREKALKAQAEHAEKEKERLRQERMRSREDEDALEQARRAHEEARRRQEQQQQQRQEQQQQQQQQAAAVAAAATPQAQSSQPQSMLDQQRELARKREQERRRREAMAATIDMNFQSDLLSIFEENLF	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-9679191: Potential therapeutics for SARS	.	O60885
TTRA6BO	Bromodomain-containing protein 4 (BRD4)	O60885	BRD4_HUMAN	Bromodomain	Protein HUNK1; HUNK1	BRD4	"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."	.	6Q3Z; 6Q3Y; 6MNL; 6MAU; 6HDQ	MSAESGPGTRLRNLPVMGDGLETSQMSTTQAQAQPQPANAASTNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKIIKTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQKINELPTEETEIMIVQAKGRGRGRKETGTAKPGVSTVPNTTQASTPPQTQTPQPNPPPVQATPHPFPAVTPDLIVQTPVMTVVPPQPLQTPPPVPPQPQPPPAPAPQPVQSHPPIIAATPQPVKTKKGVKRKADTTTPTTIDPIHEPPSLPPEPKTTKLGQRRESSRPVKPPKKDVPDSQQHPAPEKSSKVSEQLKCCSGILKEMFAKKHAAYAWPFYKPVDVEALGLHDYCDIIKHPMDMSTIKSKLEAREYRDAQEFGADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPEEPVVAVSSPAVPPPTKVVAPPSSSDSSSDSSSDSDSSTDDSEEERAQRLAELQEQLKAVHEQLAALSQPQQNKPKKKEKDKKEKKKEKHKRKEEVEENKKSKAKEPPPKKTKKNNSSNSNVSKKEPAPMKSKPPPTYESEEEDKCKPMSYEEKRQLSLDINKLPGEKLGRVVHIIQSREPSLKNSNPDEIEIDFETLKPSTLRELERYVTSCLRKKRKPQAEKVDVIAGSSKMKGFSSSESESSSESSSSDSEDSETEMAPKSKKKGHPGREQKKHHHHHHQQMQQAPAPVPQQPPPPPQQPPPPPPPQQQQQPPPPPPPPSMPQQAAPAMKSSPPPFIATQVPVLEPQLPGSVFDPIGHFTQPILHLPQPELPPHLPQPPEHSTPPHLNQHAVVSPPALHNALPQQPSRPSNRAAALPPKPARPPAVSPALTQTPLLPQPPMAQPPQVLLEDEEPPAPPLTSMQMQLYLQQLQKVQPPTPLLPSVKVQSQPPPPLPPPPHPSVQQQLQQQPPPPPPPQPQPPPQQQHQPPPRPVHLQPMQFSTHIQQPPPPQGQQPPHPPPGQQPPPPQPAKPQQVIQHHHSPRHHKSDPYSTGHLREAPSPLMIHSPQMSQFQSLTHQSPPQQNVQPKKQELRAASVVQPQPLVVVKEEKIHSPIIRSEPFSPSLRPEPPKHPESIKAPVHLPQRPEMKPVDVGRPVIRPPEQNAPPPGAPDKDKQKQEPKTPVAPKKDLKIKNMGSWASLVQKHPTTPSSTAKSSSDSFEQFRRAAREKEEREKALKAQAEHAEKEKERLRQERMRSREDEDALEQARRAHEEARRRQEQQQQQRQEQQQQQQQQAAAVAAAATPQAQSSQPQSMLDQQRELARKREQERRRREAMAATIDMNFQSDLLSIFEENLF	Clinical trial	Targeting bromodomains: epigenetic readers of lysine acetylation.Nat Rev Drug Discov.2014 May;13(5):337-56.	19	Bromodomain	Bromodomain	.	.	.	Bromodomain extra-terminal - transcription regulation; C-terminal domain of bromodomain protein 4; Bromodomain	PF17035; PF17105; PF00439	PF17035; BET; PF17105; BRD4_CDT; PF00439; Bromodomain	.	.	.	R-HSA-9679191: Potential therapeutics for SARS	.	O60885
TT07ZS1	Bromodomain-containing protein 7 (BRD7)	Q9NPI1	BRD7_HUMAN	Bromodomain	Protein CELTIX-1; CELTIX1; BP75; 75 kDa bromodomain protein	BRD7	"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."	.	5MQ1; 2I7K	MGKKHKKHKSDKHLYEEYVEKPLKLVLKVGGNEVTELSTGSSGHDSSLFEDKNDHDKHKDRKRKKRKKGEKQIPGEEKGRKRRRVKEDKKKRDRDRVENEAEKDLQCHAPVRLDLPPEKPLTSSLAKQEEVEQTPLQEALNQLMRQLQRKDPSAFFSFPVTDFIAPGYSMIIKHPMDFSTMKEKIKNNDYQSIEELKDNFKLMCTNAMIYNKPETIYYKAAKKLLHSGMKILSQERIQSLKQSIDFMADLQKTRKQKDGTDTSQSGEDGGCWQREREDSGDAEAHAFKSPSKENKKKDKDMLEDKFKSNNLEREQEQLDRIVKESGGKLTRRLVNSQCEFERRKPDGTTTLGLLHPVDPIVGEPGYCPVRLGMTTGRLQSGVNTLQGFKEDKRNKVTPVLYLNYGPYSSYAPHYDSTFANISKDDSDLIYSTYGEDSDLPSDFSIHEFLATCQDYPYVMADSLLDVLTKGGHSRTLQEMEMSLPEDEGHTRTLDTAKEMEITEVEPPGRLDSSTQDRLIALKAVTNFGVPVEVFDSEEAEIFQKKLDETTRLLRELQEAQNERLSTRPPPNMICLLGPSYREMHLAEQVTNNLKELAQQVTPGDIVSTYGVRKAMGISIPSPVMENNFVDLTEDTEEPKKTDVAECGPGGS	Literature-reported	LP99: Discovery and Synthesis of the First Selective BRD7/9 Bromodomain Inhibitor. Angew Chem Int Ed Engl. 2015 May 18;54(21):6217-21.	0	.	.	.	.	.	Bromodomain; Domain of unknown function (DUF3512)	PF00439; PF12024	PF00439; Bromodomain; PF12024; DUF3512	.	.	hsa05225: Hepatocellular carcinoma	R-HSA-6804758: Regulation of TP53 Activity through Acetylation	.	Q9NPI1
TTR7L5Y	Bromodomain-containing protein 9 (BRD9)	Q9H8M2	BRD9_HUMAN	Bromodomain	Rhabdomyosarcoma antigen MU-RMS-40.8	BRD9	"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."	.	6HM0; 6BQA; 5TWX; 5MKY; 5JI8	MGKKHKKHKAEWRSSYEDYADKPLEKPLKLVLKVGGSEVTELSGSGHDSSYYDDRSDHERERHKEKKKKKKKKSEKEKHLDDEERRKRKEEKKRKREREHCDTEGEADDFDPGKKVEVEPPPDRPVRACRTQPAENESTPIQQLLEHFLRQLQRKDPHGFFAFPVTDAIAPGYSMIIKHPMDFGTMKDKIVANEYKSVTEFKADFKLMCDNAMTYNRPDTVYYKLAKKILHAGFKMMSKQAALLGNEDTAVEEPVPEVVPVQVETAKKSKKPSREVISCMFEPEGNACSLTDSTAEEHVLALVEHAADEARDRINRFLPGGKMGYLKRNGDGSLLYSVVNTAEPDADEEETHPVDLSSLSSKLLPGFTTLGFKDERRNKVTFLSSATTALSMQNNSVFGDLKSDEMELLYSAYGDETGVQCALSLQEFVKDAGSYSKKVVDDLLDQITGGDHSRTLFQLKQRRNVPMKPPDEAKVGDTLGDSSSSVLEFMSMKSYPDVSVDISMLSSLGKVKKELDPDDSHLNLDETTKLLQDLHEAQAERGGSRPSSNLSSLSNASERDQHHLGSPSRLSVGEQPDVTHDPYEFLQSPEPAASAKT	Literature-reported	"Discovery of I-BRD9, a Selective Cell Active Chemical Probe for Bromodomain Containing Protein 9 Inhibition. J Med Chem. 2016 Feb 25;59(4):1425-39."	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9H8M2
TT7CPI5	Bromodomain testis-specific protein (BRDT)	Q58F21	BRDT_HUMAN	Bromodomain	Cancer/testis antigen 9; CT9	BRDT	"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."	.	5VBR; 5VBQ; 4KCX; 4FLP; 2RFJ	MSLPSRQTAIIVNPPPPEYINTKKNGRLTNQLQYLQKVVLKDLWKHSFSWPFQRPVDAVKLQLPDYYTIIKNPMDLNTIKKRLENKYYAKASECIEDFNTMFSNCYLYNKPGDDIVLMAQALEKLFMQKLSQMPQEEQVVGVKERIKKGTQQNIAVSSAKEKSSPSATEKVFKQQEIPSVFPKTSISPLNVVQGASVNSSSQTAAQVTKGVKRKADTTTPATSAVKASSEFSPTFTEKSVALPPIKENMPKNVLPDSQQQYNVVKTVKVTEQLRHCSEILKEMLAKKHFSYAWPFYNPVDVNALGLHNYYDVVKNPMDLGTIKEKMDNQEYKDAYKFAADVRLMFMNCYKYNPPDHEVVTMARMLQDVFETHFSKIPIEPVESMPLCYIKTDITETTGRENTNEASSEGNSSDDSEDERVKRLAKLQEQLKAVHQQLQVLSQVPFRKLNKKKEKSKKEKKKEKVNNSNENPRKMCEQMRLKEKSKRNQPKKRKQQFIGLKSEDEDNAKPMNYDEKRQLSLNINKLPGDKLGRVVHIIQSREPSLSNSNPDEIEIDFETLKASTLRELEKYVSACLRKRPLKPPAKKIMMSKEELHSQKKQELEKRLLDVNNQLNSRKRQTKSDKTQPSKAVENVSRLSESSSSSSSSSESESSSSDLSSSDSSDSESEMFPKFTEVKPNDSPSKENVKKMKNECIPPEGRTGVTQIGYCVQDTTSANTTLVHQTTPSHVMPPNHHQLAFNYQELEHLQTVKNISPLQILPPSGDSEQLSNGITVMHPSGDSDTTMLESECQAPVQKDIKIKNADSWKSLGKPVKPSGVMKSSDELFNQFRKAAIEKEVKARTQELIRKHLEQNTKELKASQENQRDLGNGLTVESFSNKIQNKCSGEEQKEHQQSSEAQDKSKLWLLKDRDLARQKEQERRRREAMVGTIDMTLQSDIMTMFENNFD	Clinical trial	Small-molecule inhibition of BRDT for male contraception. Cell. 2012 Aug 17;150(4):673-84.	17	Bromodomain	Bromodomain	.	.	.	Bromodomain extra-terminal - transcription regulation; C-terminal domain of bromodomain protein 4; Bromodomain	PF17035; PF17105; PF00439	PF17035; BET; PF17105; BRD4_CDT; PF00439; Bromodomain	.	.	.	.	.	Q58F21
TTZV7LJ	BRCA1-associated C-terminal helicase 1 (FANCJ)	Q9BX63	FANCJ_HUMAN	.	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	BRIP1	"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."	EC 3.6.4.13	3AL3; 1T29; 1T15	MSSMWSEYTIGGVKIYFPYKAYPSQLAMMNSILRGLNSKQHCLLESPTGSGKSLALLCSALAWQQSLSGKPADEGVSEKAEVQLSCCCACHSKDFTNNDMNQGTSRHFNYPSTPPSERNGTSSTCQDSPEKTTLAAKLSAKKQASIYRDENDDFQVEKKRIRPLETTQQIRKRHCFGTEVHNLDAKVDSGKTVKLNSPLEKINSFSPQKPPGHCSRCCCSTKQGNSQESSNTIKKDHTGKSKIPKIYFGTRTHKQIAQITRELRRTAYSGVPMTILSSRDHTCVHPEVVGNFNRNEKCMELLDGKNGKSCYFYHGVHKISDQHTLQTFQGMCKAWDIEELVSLGKKLKACPYYTARELIQDADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNIEDCARESASYSVTEVQLRFARDELDSMVNNNIRKKDHEPLRAVCCSLINWLEANAEYLVERDYESACKIWSGNEMLLTLHKMGITTATFPILQGHFSAVLQKEEKISPIYGKEEAREVPVISASTQIMLKGLFMVLDYLFRQNSRFADDYKIAIQQTYSWTNQIDISDKNGLLVLPKNKKRSRQKTAVHVLNFWCLNPAVAFSDINGKVQTIVLTSGTLSPMKSFSSELGVTFTIQLEANHIIKNSQVWVGTIGSGPKGRNLCATFQNTETFEFQDEVGALLLSVCQTVSQGILCFLPSYKLLEKLKERWLSTGLWHNLELVKTVIVEPQGGEKTNFDELLQVYYDAIKYKGEKDGALLVAVCRGKVSEGLDFSDDNARAVITIGIPFPNVKDLQVELKRQYNDHHSKLRGLLPGRQWYEIQAYRALNQALGRCIRHRNDWGALILVDDRFRNNPSRYISGLSKWVRQQIQHHSTFESALESLAEFSKKHQKVLNVSIKDRTNIQDNESTLEVTSLKYSTSPYLLEAASHLSPENFVEDEAKICVQELQCPKIITKNSPLPSSIISRKEKNDPVFLEEAGKAEKIVISRSTSPTFNKQTKRVSWSSFNSLGQYFTGKIPKATPELGSSENSASSPPRFKTEKMESKTVLPFTDKCESSNLTVNTSFGSCPQSETIISSLKIDATLTRKNHSEHPLCSEEALDPDIELSLVSEEDKQSTSNRDFETEAEDESIYFTPELYDPEDTDEEKNDLAETDRGNRLANNSDCILAKDLFEIRTIKEVDSAREVKAEDCIDTKLNGILHIEESKIDDIDGNVKTTWINELELGKTHEIEIKNFKPSPSKNKGMFPGFK	Literature-reported	FANCJ helicase operates in the Fanconi Anemia DNA repair pathway and the response to replicational stress. Curr Mol Med. 2009 May;9(4):470-82.	.	.	.	.	.	.	.	.	.	.	.	hsa03440: Homologous recombination; hsa03460: Fanconi anemia pathway	R-HSA-2564830: Cytosolic iron-sulfur cluster assembly; R-HSA-5685938: HDR through Single Strand Annealing (SSA); R-HSA-5685942: HDR through Homologous Recombination (HRR); R-HSA-5693554: Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA); R-HSA-5693568: Resolution of D-loop Structures through Holliday Junction Intermediates; R-HSA-5693579: Homologous DNA Pairing and Strand Exchange; R-HSA-5693607: Processing of DNA double-strand break ends; R-HSA-5693616: Presynaptic phase of homologous DNA pairing and strand exchange; R-HSA-6804756: Regulation of TP53 Activity through Phosphorylation; R-HSA-69473: G2/M DNA damage checkpoint; R-HSA-9701192: Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function; R-HSA-9704331: Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function; R-HSA-9704646: Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function; R-HSA-9709570: Impaired BRCA2 binding to RAD51; R-HSA-9709603: Impaired BRCA2 binding to PALB2	.	Q9BX63
TTT46BN	Bromodomain and PHD finger containing 1 (BRPF1)	P55201	BRPF1_HUMAN	.	Protein Br140; Peregrin; Bromodomain and PHD finger-containing protein 1; BR140	BRPF1	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.	.	6EKQ; 5T4V; 5T4U; 5OWE; 5OWB	MGVDFDVKTFCHNLRATKPPYECPVETCRKVYKSYSGIEYHLYHYDHDNPPPPQQTPLRKHKKKGRQSRPANKQSPSPSEVSQSPGREVMSYAQAQRMVEVDLHGRVHRISIFDNLDVVSEDEEAPEEAPENGSNKENTETPAATPKSGKHKNKEKRKDSNHHHHHNVSASTTPKLPEVVYRELEQDTPDAPPRPTSYYRYIEKSAEELDEEVEYDMDEEDYIWLDIMNERRKTEGVSPIPQEIFEYLMDRLEKESYFESHNKGDPNALVDEDAVCCICNDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRRCLQSPSRAVDCALCPNKGGAFKQTDDGRWAHVVCALWIPEVCFANTVFLEPIDSIEHIPPARWKLTCYICKQRGSGACIQCHKANCYTAFHVTCAQQAGLYMKMEPVRETGANGTSFSVRKTAYCDIHTPPGSARRLPALSHSEGEEDEDEEEDEGKGWSSEKVKKAKAKSRIKMKKARKILAEKRAAAPVVSVPCIPPHRLSKITNRLTIQRKSQFMQRLHSYWTLKRQSRNGVPLLRRLQTHLQSQRNCDQVGRDSEDKNWALKEQLKSWQRLRHDLERARLLVELIRKREKLKRETIKVQQIAMEMQLTPFLILLRKTLEQLQEKDTGNIFSEPVPLSEVPDYLDHIKKPMDFFTMKQNLEAYRYLNFDDFEEDFNLIVSNCLKYNAKDTIFYRAAVRLREQGGAVLRQARRQAEKMGIDFETGMHIPHSLAGDEATHHTEDAAEEERLVLLENQKHLPVEEQLKLLLERLDEVNASKQSVGRSRRAKMIKKEMTALRRKLAHQRETGRDGPERHGPSSRGSLTPHPAACDKDGQTDSAAEESSSQETSKGLGPNMSSTPAHEVGRRTSVLFSKKNPKTAGPPKRPGRPPKNRESQMTPSHGGSPVGPPQLPIMSSLRQRKRGRSPRPSSSSDSDSDKSTEDPPMDLPANGFSGGNQPVKKSFLVYRNDCSLPRSSSDSESSSSSSSSAASDRTSTTPSKQGRGKPSFSRGTFPEDSSEDTSGTENEAYSVGTGRGVGHSMVRKSLGRGAGWLSEDEDSPLDALDLVWAKCRGYPSYPALIIDPKMPREGMFHHGVPIPVPPLEVLKLGEQMTQEAREHLYLVLFFDNKRTWQWLPRTKLVPLGVNQDLDKEKMLEGRKSNIRKSVQIAYHRALQHRSKVQGEQSSETSDSD	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2730).	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-3214847: HATs acetylate histones; R-HSA-6804758: Regulation of TP53 Activity through Acetylation	.	P55201
TT1CHFI	Bromodomain and PHD finger containing 3 (BRPF3)	Q9ULD4	BRPF3_HUMAN	.	KIAA1286; Bromodomain and PHD finger-containing protein 3	BRPF3	Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.	.	3PFS	MRKPRRKSRQNAEGRRSPSPYSLKCSPTRETLTYAQAQRIVEVDIDGRLHRISIYDPLKIITEDELTAQDITECNSNKENSEQPQFPGKSKKPSSKGKKKESCSKHASGTSFHLPQPSFRMVDSGIQPEAPPLPAAYYRYIEKPPEDLDAEVEYDMDEEDLAWLDMVNEKRRVDGHSLVSADTFELLVDRLEKESYLESRSSGAQQSLIDEDAFCCVCLDDECHNSNVILFCDICNLAVHQECYGVPYIPEGQWLCRCCLQSPSRPVDCILCPNKGGAFKQTSDGHWAHVVCAIWIPEVCFANTVFLEPIEGIDNIPPARWKLTCYICKQKGLGAAIQCHKVNCYTAFHVTCAQRAGLFMKIEPMRETSLNGTIFTVRKTAYCEAHSPPGAATARRKGDSPRSISETGDEEGLKEGDGEEEEEEEVEEEEQEAQGGVSGSLKGVPKKSKMSLKQKIKKEPEEAGQDTPSTLPMLAVPQIPSYRLNKICSGLSFQRKNQFMQRLHNYWLLKRQARNGVPLIRRLHSHLQSQRNAEQREQDEKTSAVKEELKYWQKLRHDLERARLLIELIRKREKLKREQVKVQQAAMELELMPFNVLLRTTLDLLQEKDPAHIFAEPVNLSEVPDYLEFISKPMDFSTMRRKLESHLYRTLEEFEEDFNLIVTNCMKYNAKDTIFHRAAVRLRDLGGAILRHARRQAENIGYDPERGTHLPESPKLEDFYRFSWEDVDNILIPENRAHLSPEVQLKELLEKLDLVSAMRSSGARTRRVRLLRREINALRQKLAQPPPPQPPSLNKTVSNGELPAGPQGDAAVLEQALQEEPEDDGDRDDSKLPPPPTLEPTGPAPSLSEQESPPEPPTLKPINDSKPPSRFLKPRKVEEDELLEKSPLQLGNEPLQRLLSDNGINRLSLMAPDTPAGTPLSGVGRRTSVLFKKAKNGVKLQRSPDRVLENGEDHGVAGSPASPASIEEERHSRKRPRSRSCSESEGERSPQQEEETGMTNGFGKHTESGSDSECSLGLSGGLAFEACSGLTPPKRSRGKPALSRVPFLEGVNGDSDYNGSGRSLLLPFEDRGDLEPLELVWAKCRGYPSYPALIIDPKMPREGLLHNGVPIPVPPLDVLKLGEQKQAEAGEKLFLVLFFDNKRTWQWLPRDKVLPLGVEDTVDKLKMLEGRKTSIRKSVQVAYDRAMIHLSRVRGPHSFVTSSYL	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2731).	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-114608: Platelet degranulation; R-HSA-3214847: HATs acetylate histones; R-HSA-6804758: Regulation of TP53 Activity through Acetylation	.	Q9ULD4
TTKYEPM	Bombesin-like receptor 3 (BRS3)	P32247	BRS3_HUMAN	.	Bombesin receptor subtype-3; BRS-3	BRS3	"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."	.	.	MAQRQPHSPNQTLISITNDTESSSSVVSNDNTNKGWSGDNSPGIEALCAIYITYAVIISVGILGNAILIKVFFKTKSMQTVPNIFITSLAFGDLLLLLTCVPVDATHYLAEGWLFGRIGCKVLSFIRLTSVGVSVFTLTILSADRYKAVVKPLERQPSNAILKTCVKAGCVWIVSMIFALPEAIFSNVYTFRDPNKNMTFESCTSYPVSKKLLQEIHSLLCFLVFYIIPLSIISVYYSLIARTLYKSTLNIPTEEQSHARKQIESRKRIARTVLVLVALFALCWLPNHLLYLYHSFTSQTYVDPSAMHFIFTIFSRVLAFSNSCVNPFALYWLSKSFQKHFKAQLFCCKAERPEPPVADTSLTTLAVMGTVPGTGSIQMSEISVTSFTGCSVKQAEDRF	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Ligand id: 8502).	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-416476: G alpha (q) signalling events	.	P32247
TTV6WMQ	BR serine/threonine kinase 1 (BRSK1)	Q8TDC3	BRSK1_HUMAN	.	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	BRSK1	"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."	EC 2.7.11.1	.	MSSGAKEGGGGSPAYHLPHPHPHPPQHAQYVGPYRLEKTLGKGQTGLVKLGVHCITGQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIVSALDFCHSYSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIKGEKYDGRRADMWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVEPEKRLSLEQIQKHPWYLGGKHEPDPCLEPAPGRRVAMRSLPSNGELDPDVLESMASLGCFRDRERLHRELRSEEENQEKMIYYLLLDRKERYPSCEDQDLPPRNDVDPPRKRVDSPMLSRHGKRRPERKSMEVLSITDAGGGGSPVPTRRALEMAQHSQRSRSVSGASTGLSSSPLSSPRSPVFSFSPEPGAGDEARGGGSPTSKTQTLPSRGPRGGGAGEQPPPPSARSTPLPGPPGSPRSSGGTPLHSPLHTPRASPTGTPGTTPPPSPGGGVGGAAWRSRLNSIRNSFLGSPRFHRRKMQVPTAEEMSSLTPESSPELAKRSWFGNFISLDKEEQIFLVLKDKPLSSIKADIVHAFLSIPSLSHSVLSQTSFRAEYKASGGPSVFQKPVRFQVDISSSEGPEPSPRRDGSGGGGIYSVTFTLISGPSRRFKRVVETIQAQLLSTHDQPSVQALADEKNGAQTRPAGAPPRSLQPPPGRPDPELSSSPRRGPPKDKKLLATNGTPLP	Literature-reported	"Discovery of 3-alkoxyamino-5-(pyridin-2-ylamino)pyrazine-2-carbonitriles as selective, orally bioavailable CHK1 inhibitors. J Med Chem. 2012 Nov 26;55(22):10229-40."	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q8TDC3
TTHZN4X	BR serine/threonine kinase 2 (BRSK2)	Q8IWQ3	BRSK2_HUMAN	.	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	BRSK2	"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."	EC 2.7.11.1	.	MTSTGKDGGAQHAQYVGPYRLEKTLGKGQTGLVKLGVHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQDLLSEEENQEKMIYFLLLDRKERYPSQEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRAIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRARLNSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELAKKSWFGNFISLEKEEQIFVVIKDKPLSSIKADIVHAFLSIPSLSHSVISQTSFRAEYKATGGPAVFQKPVKFQVDITYTEGGEAQKENGIYSVTFTLLSGPSRRFKRVVETIQAQLLSTHDPPAAQHLSDTTNCMEMMTGRLSKCGSPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGPGGDAEYPTGKDTAKMGPPTARREQP	Literature-reported	"Discovery of 3-alkoxyamino-5-(pyridin-2-ylamino)pyrazine-2-carbonitriles as selective, orally bioavailable CHK1 inhibitors. J Med Chem. 2012 Nov 26;55(22):10229-40."	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q8IWQ3
TT5UJWD	Basigin (BSG)	P35613	BASI_HUMAN	Basigin protein	UNQ6505/PRO21383; Tumor cell-derived collagenase stimulatory factor; TCSF; OK blood group antigen; Leukocyte activation antigen M6; Extracellular matrix metalloproteinase inducer; EMMPRIN; 5F7	BSG	"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."	.	5XF0; 5X0T; 4U0Q; 3QR2; 3QQN	MAAALFVLLGFALLGTHGASGAAGFVQAPLSQQRWVGGSVELHCEAVGSPVPEIQWWFEGQGPNDTCSQLWDGARLDRVHIHATYHQHAASTISIDTLVEEDTGTYECRASNDPDRNHLTRAPRVKWVRAQAVVLVLEPGTVFTTVEDLGSKILLTCSLNDSATEVTGHRWLKGGVVLKEDALPGQKTEFKVDSDDQWGEYSCVFLPEPMGTANIQLHGPPRVKAVKSSEHINEGETAMLVCKSESVPPVTDWAWYKITDSEDKALMNGSESRFFVSSSQGRSELHIENLNMEADPGQYRCNGTSSKGSDQAIITLRVRSHLAALWPFLGIVAEVLVLVTIIFIYEKRRKPEDVLDDDDAGSAPLKSSGQHQNDKGKNVRQRNSS	Clinical trial	National Cancer Institute Drug Dictionary (drug id 38221).	24	TC=8.A.23	Basigin family	.	.	.	.	.	.	8.A.23.1.1	The Basigin (Basigin) Family	.	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	.	P35613
TTG21IS	HUMAN basigin (BSG)	P35613	BASI_HUMAN	Basigin protein	UNQ6505/PRO21383; Tumor cell-derived collagenase stimulatory factor; TCSF; OK blood group antigen; Leukocyte activation antigen M6; Extracellular matrix metalloproteinase inducer; EMMPRIN; 5F7	BSG	"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."	.	5XF0; 5X0T; 4U0Q; 3QR2; 3QQN	MAAALFVLLGFALLGTHGASGAAGFVQAPLSQQRWVGGSVELHCEAVGSPVPEIQWWFEGQGPNDTCSQLWDGARLDRVHIHATYHQHAASTISIDTLVEEDTGTYECRASNDPDRNHLTRAPRVKWVRAQAVVLVLEPGTVFTTVEDLGSKILLTCSLNDSATEVTGHRWLKGGVVLKEDALPGQKTEFKVDSDDQWGEYSCVFLPEPMGTANIQLHGPPRVKAVKSSEHINEGETAMLVCKSESVPPVTDWAWYKITDSEDKALMNGSESRFFVSSSQGRSELHIENLNMEADPGQYRCNGTSSKGSDQAIITLRVRSHLAALWPFLGIVAEVLVLVTIIFIYEKRRKPEDVLDDDDAGSAPLKSSGQHQNDKGKNVRQRNSS	.	"Meplazumab treats COVID-19 pneumonia: an open-labelled, concurrent controlled add-on clinical trial"	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1474228: Degradation of the extracellular matrix; R-HSA-210991: Basigin interactions; R-HSA-216083: Integrin cell surface interactions; R-HSA-433692: Proton-coupled monocarboxylate transport; R-HSA-5619070: Defective SLC16A1 causes symptomatic deficiency in lactate transport (SDLT); R-HSA-70268: Pyruvate metabolism; R-HSA-9749641: Aspirin ADME	.	P35613
TT90BJT	Bone marrow stromal antigen 2 (BST2)	Q10589	BST2_HUMAN	Tetherin family	Tetherin; HM1.24 antigen; CD317; BST2	BST2	"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."	.	6DFF; 6D84; 6D83; 6CRI; 6CM9	MASTSYDYCRVPMEDGDKRCKLLLGIGILVLLIIVILGVPLIIFTIKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAATCNHTVMALMASLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRRENQVLSVRIADKKYYPSSQDSSSAAAPQLLIVLLGLSALLQ	Literature-reported	Bone marrow stromal antigen 2 expressed in cancer cells promotes mammary tumor growth and metastasis. Breast Cancer Res. 2014 Dec 13;16(6):493.	.	.	.	.	.	.	.	.	.	.	.	hsa03250: Viral life cycle - HIV-1; hsa05168: Herpes simplex virus 1 infection; hsa05170: Human immunodeficiency virus 1 infection	R-HSA-6798695: Neutrophil degranulation; R-HSA-909733: Interferon alpha/beta signaling	.	Q10589
TTL7N2W	B-cell translocation gene 1 protein (BTG1)	P62324	BTG1_HUMAN	.	Protein BTG1	BTG1	Anti-proliferative protein.	.	.	MHPFYTRAATMIGEIAAAVSFISKFLRTKGLTSERQLQTFSQSLQELLAEHYKHHWFPEKPCKGSGYRCIRINHKMDPLIGQAAQRIGLSSQELFRLLPSELTLWVDPYEVSYRIGEDGSICVLYEASPAGGSTQNSTNVQMVDSRISCKEELLLGRTSPSKNYNMMTVSG	Literature-reported	MicroRNA 301A Promotes Intestinal Inflammation and Colitis-Associated Cancer Development by Inhibiting BTG1. Gastroenterology. 2017 May;152(6):1434-1448.e15.	.	.	.	BTG family.	.	.	BTG family	PF07742	PF07742; BTG	.	.	hsa03018: RNA degradation	R-HSA-9617828: FOXO-mediated transcription of cell cycle genes	.	P62324
TTGM6VW	Tyrosine-protein kinase BTK (ATK)	Q06187	BTK_HUMAN	Kinase	Bruton's tyrosine kinase; Bruton tyrosine kinase; BPK; B-cell progenitor kinase; B cell progenitor kinase; Agammaglobulinemia tyrosine kinase; Agammaglobulinaemia tyrosine kinase; AGMX1	BTK	"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."	EC 2.7.10.2	6O8I; 6NFI; 6NFH; 6N9P; 6HRT	MAAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILENRNGSLKPGSSHRKTKKPLPPTPEEDQILKKPLPPEPAAAPVSTSELKKVVALYDYMPMNANDLQLRKGDEYFILEESNLPWWRARDKNGQEGYIPSNYVTEAEDSIEMYEWYSKHMTRSQAEQLLKQEGKEGGFIVRDSSKAGKYTVSVFAKSTGDPQGVIRHYVVCSTPQSQYYLAEKHLFSTIPELINYHQHNSAGLISRLKYPVSQQNKNAPSTAGLGYGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILLSNILDVMDEES	Successful	"Ibrutinib (PCI-32765), the first BTK (Bruton's tyrosine kinase) inhibitor in clinical trials. Curr Hematol Malig Rep. 2013 Mar;8(1):1-6."	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. TEC subfamily.	2.7.10.2	Transferring phosphorus-containing groups	BTK motif; PH domain; Protein tyrosine kinase; SH2 domain; SH3 domain	PF00779; PF00169; PF07714; PF00017; PF00018	PF00779; BTK; PF00169; PH; PF07714; Pkinase_Tyr; PF00017; SH2; PF00018; SH3_1	.	.	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	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	.	Q06187
TTOWPER	HUMAN bruton tyrosine kinase (BTK)	Q06187	BTK_HUMAN	Kinase	Bruton's tyrosine kinase; Bruton tyrosine kinase; BPK; B-cell progenitor kinase; B cell progenitor kinase; Agammaglobulinemia tyrosine kinase; Agammaglobulinaemia tyrosine kinase; AGMX1	BTK	"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."	EC 2.7.10.2	6O8I; 6NFI; 6NFH; 6N9P; 6HRT	MAAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILENRNGSLKPGSSHRKTKKPLPPTPEEDQILKKPLPPEPAAAPVSTSELKKVVALYDYMPMNANDLQLRKGDEYFILEESNLPWWRARDKNGQEGYIPSNYVTEAEDSIEMYEWYSKHMTRSQAEQLLKQEGKEGGFIVRDSSKAGKYTVSVFAKSTGDPQGVIRHYVVCSTPQSQYYLAEKHLFSTIPELINYHQHNSAGLISRLKYPVSQQNKNAPSTAGLGYGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILLSNILDVMDEES	.	AstraZeneca initiates CALAVI clinical trial with Calquence against COVID-19	.	.	.	.	.	.	.	.	.	.	.	hsa04064: NF-kappa B signaling pathway; hsa04380: Osteoclast differentiation; hsa04611: Platelet activation; hsa04662: B cell receptor signaling pathway; hsa04664: Fc epsilon RI signaling pathway; hsa05169: Epstein-Barr virus infection; hsa05340: Primary immunodeficiency	R-HSA-1236974: ER-Phagosome pathway; R-HSA-166058: MyD88:MAL(TIRAP) 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-416476: G alpha (q) signalling events; R-HSA-416482: G alpha (12/13) signalling events; 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-8964315: G beta:gamma signalling through BTK; R-HSA-9664422: FCGR3A-mediated phagocytosis; R-HSA-983695: Antigen activates B Cell Receptor (BCR) leading to generation of second messengers	.	Q06187
TTER58P	B- and T-lymphocyte attenuator (BTLA)	Q7Z6A9	BTLA_HUMAN	.	CD272; B- and T-lymphocyte-associated protein	BTLA	"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."	.	2AW2	MKTLPAMLGTGKLFWVFFLIPYLDIWNIHGKESCDVQLYIKRQSEHSILAGDPFELECPVKYCANRPHVTWCKLNGTTCVKLEDRQTSWKEEKNISFFILHFEPVLPNDNGSYRCSANFQSNLIESHSTTLYVTDVKSASERPSKDEMASRPWLLYRLLPLGGLPLLITTCFCLFCCLRRHQGKQNELSDTAGREINLVDAHLKSEQTEASTRQNSQVLLSETGIYDNDPDLCFRMQEGSEVYSNPCLEENKPGIVYASLNHSVIGPNSRLARNVKEAPTEYASICVRS	Clinical trial	Decreased B and T lymphocyte attenuator in Behcet's disease may trigger abnormal Th17 and Th1 immune responses. Sci Rep. 2016 Feb 4;6:20401.	.	.	.	.	.	.	Immunoglobulin domain	PF00047	PF00047; ig	.	.	.	R-HSA-388841: Costimulation by the CD28 family	.	Q7Z6A9
TTBGWN3	Butyrophilin-like protein 3 (BTNL3)	Q6UXE8	BTNL3_HUMAN	Immunoglobulin	UNQ744/PRO1472; COLF4100; Butyrophilin-like receptor; BTNLR	BTNL3	Regulate the homing and maturation of V7+ and V4+ T cells to the gut epithelium.	.	.	MAFVLILVLSFYELVSGQWQVTGPGKFVQALVGEDAVFSCSLFPETSAEAMEVRFFRNQFHAVVHLYRDGEDWESKQMPQYRGRTEFVKDSIAGGRVSLRLKNITPSDIGLYGCWFSSQIYDEEATWELRVAALGSLPLISIVGYVDGGIQLLCLSSGWFPQPTAKWKGPQGQDLSSDSRANADGYSLYDVEISIIVQENAGSILCSIHLAEQSHEVESKVLIGETFFQPSPWRLASILLGLLCGALCGVVMGMIIVFFKSKGKIQAELDWRRKHGQAELRDARKHAVEVTLDPETAHPKLCVSDLKTVTHRKAPQEVPHSEKRFTRKSVVASQGFQAGKHYWEVDVGQNVGWYVGVCRDDVDRGKNNVTLSPNNGYWVLRLTTEHLYFTFNPHFISLPPSTPPTRVGVFLDYEGGTISFFNTNDQSLIYTLLTCQFEGLLRPYIQHAMYDEEKGTPIFICPVSWG	Literature-reported	New Insights Into the Regulation of T Cells by BTN3A and Other BTN/BTNL in Tumor Immunity. Front Immunol. 2018 Jul 11;9:1601.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q6UXE8
TT78309	BUB1 mitotic checkpoint serine/threonine kinase (BUB1)	O43683	BUB1_HUMAN	Kinase	hBUB1; Mitotic checkpoint serine/threonine-protein kinase BUB1; BUB1L; BUB1A	BUB1	"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."	EC 2.7.11.1	6F7B; 5DMZ; 4R8Q; 4QPM; 4A1G	MDTPENVLQMLEAHMQSYKGNDPLGEWERYIQWVEENFPENKEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSDLHQFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRGIQNQAEPREFLQQQYRLFQTRLTETHLPAQARTSEPLHNVQVLNQMITSKSNPGNNMACISKNQGSELSGVISSACDKESNMERRVITISKSEYSVHSSLASKVDVEQVVMYCKEKLIRGESEFSFEELRAQKYNQRRKHEQWVNEDRHYMKRKEANAFEEQLLKQKMDELHKKLHQVVETSHEDLPASQERSEVNPARMGPSVGSQQELRAPCLPVTYQQTPVNMEKNPREAPPVVPPLANAISAALVSPATSQSIAPPVPLKAQTVTDSMFAVASKDAGCVNKSTHEFKPQSGAEIKEGCETHKVANTSSFHTTPNTSLGMVQATPSKVQPSPTVHTKEALGFIMNMFQAPTLPDISDDKDEWQSLDQNEDAFEAQFQKNVRSSGAWGVNKIISSLSSAFHVFEDGNKENYGLPQPKNKPTGARTFGERSVSRLPSKPKEEVPHAEEFLDDSTVWGIRCNKTLAPSPKSPGDFTSAAQLASTPFHKLPVESVHILEDKENVVAKQCTQATLDSCEENMVVPSRDGKFSPIQEKSPKQALSSHMYSASLLRLSQPAAGGVLTCEAELGVEACRLTDTDAAIAEDPPDAIAGLQAEWMQMSSLGTVDAPNFIVGNPWDDKLIFKLLSGLSKPVSSYPNTFEWQCKLPAIKPKTEFQLGSKLVYVHHLLGEGAFAQVYEATQGDLNDAKNKQKFVLKVQKPANPWEFYIGTQLMERLKPSMQHMFMKFYSAHLFQNGSVLVGELYSYGTLLNAINLYKNTPEKVMPQGLVISFAMRMLYMIEQVHDCEIIHGDIKPDNFILGNGFLEQDDEDDLSAGLALIDLGQSIDMKLFPKGTIFTAKCETSGFQCVEMLSNKPWNYQIDYFGVAATVYCMLFGTYMKVKNEGGECKPEGLFRRLPHLDMWNEFFHVMLNIPDCHHLPSLDLLRQKLKKVFQQHYTNKIRALRNRLIVLLLECKRSRK	Patented-recorded	Novel cycloalkenepyrazoles as inhibitors of bub1 kinase. ACS Med Chem Lett. 2014 Feb 12;5(4):280-1.	0	EC:2.7	.	protein kinase superfamily. Ser/Thr protein kinase family. BUB1 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Mad3/BUB1 homology region 1; Protein kinase domain	PF08311; PF00069	PF08311; Mad3_BUB1_I; PF00069; Pkinase	.	.	hsa04110: Cell cycle; hsa04114: Oocyte meiosis; hsa04914: Progesterone-mediated oocyte maturation	R-HSA-141444: Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal; 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-9648025: EML4 and NUDC in mitotic spindle formation	.	O43683
TT3EUH1	Burkholderia Glutamate racemase (BURCJ murI)	B4EEM8	B4EEM8_BURCJ	.	Glutamate racemase	BURCJ murI	Provides the (R)-glutamate required for cell wall biosynthesis.	EC 5.1.1.3	.	MTNPSDATALRAAAPVGIFDSGLGGLSVLRAARAHLPDESFVYVADSHHAPYGPRDEAFITERTLAIGEWLAREGAKALVIACNTATARAIAAIRERLSIPLVGVEPGIKPAAALSATGVAGVLATQSTLNSPRFQALLDRYGAGRRFICQPGHGLVEAIERGDTNSPALRALLERYIQPMLDDGADTLVLGCTHYPFFTETIRDLVGERLTIVDTSDAIARQLARVLDERGLRAPAGTHAAPPRFCSTSDGLQLRALASTLLGLDAPVESVTISSPNARACATA	Literature-reported	Biochemical Characterization of Glutamate Racemase-A New Candidate Drug Target against Burkholderia cenocepacia Infections. PLoS One. 2016 Nov 29;11(11):e0167350.	.	.	.	.	.	.	.	.	.	.	.	bcj00470: D-Amino acid metabolism; bcj01100: Metabolic pathways	.	BCEN216591:G1G1V-2522-MON	.
TT8A9DM	Complement C1q component (C1Q)	P02746	C1QB_HUMAN	.	C1QB	C1QB	"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."	.	6FCZ; 5HZF; 5HKJ; 2WNV; 2WNU	MMMKIPWGSIPVLMLLLLLGLIDISQAQLSCTGPPAIPGIPGIPGTPGPDGQPGTPGIKGEKGLPGLAGDHGEFGEKGDPGIPGNPGKVGPKGPMGPKGGPGAPGAPGPKGESGDYKATQKIAFSATRTINVPLRRDQTIRFDHVITNMNNNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNLMRGRERAQKVVTFCDYAYNTFQVTTGGMVLKLEQGENVFLQATDKNSLLGMEGANSIFSGFLLFPDMEA	Literature-reported	Interaction between complement subcomponent C1q and the Klebsiella pneumoniae porin OmpK36. Infect Immun. 1996 Nov;64(11):4719-25.	.	.	.	.	.	.	.	.	.	.	.	hsa04610: Complement and coagulation cascades; hsa04936: Alcoholic liver disease; hsa05020: Prion disease; hsa05133: Pertussis; hsa05142: Chagas disease; hsa05150: Staphylococcus aureus infection; hsa05171: Coronavirus disease - COVID-19; hsa05322: Systemic lupus erythematosus	R-HSA-166663: Initial triggering of complement; R-HSA-173623: Classical antibody-mediated complement activation; R-HSA-977606: Regulation of Complement cascade	.	P02746
TTWTD7F	ASF/SF2-associated protein p32 (C1QBP)	Q07021	C1QBP_HUMAN	.	"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"	C1QBP	"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."	.	3RPX; 1P32	MLPLLRCVPRVLGSSVAGLRAAAPASPFRQLLQPAPRLCTRPFGLLSVRAGSERRPGLLRPRGPCACGCGCGSLHTDGDKAFVDFLSDEIKEERKIQKHKTLPKMSGGWELELNGTEAKLVRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKVEEQEPELTSTPNFVVEVIKNDDGKKALVLDCHYPEDEVGQEDEAESDIFSIREVSFQSTGESEWKDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKSQ	Literature-reported	Mitochondrial/cell-surface protein p32/gC1qR as a molecular target in tumor cells and tumor stroma. Cancer Res. 2008 Sep 1;68(17):7210-8.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-111471: Apoptotic factor-mediated response; R-HSA-140837: Intrinsic Pathway of Fibrin Clot Formation; R-HSA-8980692: RHOA GTPase cycle; R-HSA-9013106: RHOC GTPase cycle; R-HSA-9645722: Defective Intrinsic Pathway for Apoptosis Due to p14ARF Loss of Function	.	Q07021
TT7LRQH	Complement C1s component (C1S)	P09871	C1S_HUMAN	Peptidase	Complement component 1 subcomponent s; Complement C1s subcomponent; C1-esterase; C1 esterase	C1S	"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."	EC 3.4.21.42	6F1H; 6F1C; 4LOT; 4LOS; 4LOR	MWCIVLFSLLAWVYAEPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIELSENCAYDSVQIISGDTEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERFTGFAAYYVATDINECTDFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVFTALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVFVAGDRQFGPYCGHGFPGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPMPCPKEDTPNSVWEPAKAKYVFRDVVQITCLDGFEVVEGRVGATSFYSTCQSNGKWSNSKLKCQPVDCGIPESIENGKVEDPESTLFGSVIRYTCEEPYYYMENGGGGEYHCAGNGSWVNEVLGPELPKCVPVCGVPREPFEEKQRIIGGSDADIKNFPWQVFFDNPWAGGALINEYWVLTAAHVVEGNREPTMYVGSTSVQTSRLAKSKMLTPEHVFIHPGWKLLEVPEGRTNFDNDIALVRLKDPVKMGPTVSPICLPGTSSDYNLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLRKCKEVKVEKPTADAEAYVFTPNMICAGGEKGMDSCKGDSGGAFAVQDPNDKTKFYAAGLVSWGPQCGTYGLYTRVKNYVDWIMKTMQENSTPRED	Successful	2008 FDA drug approvals. Nat Rev Drug Discov. 2009 Feb;8(2):93-6.	34	EC:3.4	Peptidase	peptidase S1 family.	3.4.21.42	Acting on peptide bonds (peptidases)	CUB domain; Sushi repeat (SCR repeat); Trypsin	PF00431; PF00084; PF00089	PF00431; CUB; PF00084; Sushi; PF00089; Trypsin	.	.	hsa04610:Complement and coagulation cascades; hsa05133:Pertussis; hsa05150:Staphylococcus aureus infection; hsa05322:Systemic lupus erythematosus	R-HSA-166663: Initial triggering of complement; R-HSA-173623: Classical antibody-mediated complement activation; R-HSA-977606: Regulation of Complement cascade	.	P09871
TTJGY7A	Complement C3 (CO3)	P01024	CO3_HUMAN	Complement system	C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1; C3	C3	"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)."	.	6EHG; 5O35; 5O32; 5NBQ; 5M6W	MGPTSGPSLLLLLLTHLPLALGSPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDFPGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKSEKGRNKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAERSGIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPAYRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTELRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAGRQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLKIEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAARRRRSVQLTEKRMDKVGKYPKELRKCCEDGMRENPMRFSCQRRTRFISLGEACKKVFLDCCNYITELRRQHARASHLGLARSNLDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLMNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFIDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPAFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVEVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPERLGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMTEDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRIHWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKDQLTCNKFDLKVTIKPAPETEKRPQDAKNTMILEICTRYRGDQDATMSILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDRNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYAYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQKSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEENQKQCQDLGAFTESMVVFGCPN	Clinical trial	Anti-ageing pipeline starts to mature.Nat Rev Drug Discov. 2018 Sep;17(9):609-612.	25	.	.	.	.	.	.	.	.	.	.	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	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	.	P01024
TTXA5VP	Complement C3 messenger RNA (C3 mRNA)	P01024	CO3_HUMAN	mRNA target	C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1 (mRNA)	C3	"C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.; Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. In chronic inflammation, acts as a chemoattractant for neutrophils (By similarity). It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. {ECO:0000250}.; [C3-beta-c]: Acts as a chemoattractant for neutrophils in chronic inflammation. {ECO:0000250}.; [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). {ECO:0000269|PubMed:10432298, ECO:0000269|PubMed:15833747, ECO:0000269|PubMed:16333141, ECO:0000269|PubMed:19615750, ECO:0000269|PubMed:2909530, ECO:0000269|PubMed:8376604, ECO:0000269|PubMed:9059512}."	.	1C3D;1GHQ;1W2S;2A73;2A74;2GOX;2I07;2ICE;2ICF;2NOJ;2QKI;2WII;2WIN;2WY7;2WY8;2XQW;2XWB;2XWJ;3D5R;3D5S;3G6J;3L3O;3L5N;3NMS;3OED;3OHX;3OXU;3RJ3;3T4A;4HW5;4HWJ;4I6O;4M76;4ONT;4ZH1;5FO7;5FO8;5FO9;5FOA;5FOB;5NBQ;5O32;5O35;6EHG;6RMT;6RMU;6RUR;6RUV;6S0B;6YO6;7AKK;7BAG;7NOZ;7PI6;7QIV;7TV9;7UE9;7ZGK;8HK2	MGPTSGPSLLLLLLTHLPLALGSPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDFPGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKSEKGRNKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAERSGIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPAYRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTELRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAGRQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLKIEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAARRRRSVQLTEKRMDKVGKYPKELRKCCEDGMRENPMRFSCQRRTRFISLGEACKKVFLDCCNYITELRRQHARASHLGLARSNLDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLMNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFIDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPAFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVEVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPERLGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMTEDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRIHWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKDQLTCNKFDLKVTIKPAPETEKRPQDAKNTMILEICTRYRGDQDATMSILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDRNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYAYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQKSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEENQKQCQDLGAFTESMVVFGCPN	Clinical trial	"Clinical pipeline report, company report or official report of Alexion"	.	.	.	.	.	.	.	.	.	.	.	hsa:718	R-HSA-173736;R-HSA-174577;R-HSA-198933;R-HSA-375276;R-HSA-381426;R-HSA-418594;R-HSA-6798695;R-HSA-8957275;R-HSA-9660826;R-HSA-977606;	.	P01024;
TTI6B3F	C3a anaphylatoxin chemotactic receptor (C3AR1)	Q16581	C3AR_HUMAN	.	HNFAG09; C3a-R; C3R1; C3AR; AZ3B	C3AR1	"Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production."	.	.	MASFSAETNSTDLLSQPWNEPPVILSMVILSLTFLLGLPGNGLVLWVAGLKMQRTVNTIWFLHLTLADLLCCLSLPFSLAHLALQGQWPYGRFLCKLIPSIIVLNMFASVFLLTAISLDRCLVVFKPIWCQNHRNVGMACSICGCIWVVAFVMCIPVFVYREIFTTDNHNRCGYKFGLSSSLDYPDFYGDPLENRSLENIVQPPGEMNDRLDPSSFQTNDHPWTVPTVFQPQTFQRPSADSLPRGSARLTSQNLYSNVFKPADVVSPKIPSGFPIEDHETSPLDNSDAFLSTHLKLFPSASSNSFYESELPQGFQDYYNLGQFTDDDQVPTPLVAITITRLVVGFLLPSVIMIACYSFIVFRMQRGRFAKSQSKTFRVAVVVVAVFLVCWTPYHIFGVLSLLTDPETPLGKTLMSWDHVCIALASANSCFNPFLYALLGKDFRKKARQSIQGILEAAFSEELTRSTHCPSNNVISERNSTTV	Literature-reported	Identification of a selective nonpeptide antagonist of the anaphylatoxin C3a receptor that demonstrates antiinflammatory activity in animal models. J Immunol. 2001 May 15;166(10):6341-8.	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04610: Complement and coagulation cascades; hsa04936: Alcoholic liver disease; hsa05150: Staphylococcus aureus infection; hsa05171: Coronavirus disease - COVID-19	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-418594: G alpha (i) signalling events; R-HSA-6798695: Neutrophil degranulation; R-HSA-9660826: Purinergic signaling in leishmaniasis infection; R-HSA-977606: Regulation of Complement cascade	.	Q16581
TTKANGO	Complement C5 (CO5)	P01031	CO5_HUMAN	Complement system	C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4	C5	"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."	.	.	MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQNSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETVLTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGYKNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNNKYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVPVTLNAQTIDVNQETSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGEHLNIIVTPKSPYIDKITHYNYLILSKGKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIVTGEQTAELVSDSVWLNIEEKCGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGLNNANVFHLAGLTFLTNANADDSQENDEPCKEILRPRRTLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQGVGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKENSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVHVTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLKALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVCEGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITFIKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC	Successful	2018 FDA drug approvals.Nat Rev Drug Discov. 2019 Feb;18(2):85-89. 	34	.	.	.	.	.	.	.	.	.	.	hsa04610:Complement and coagulation cascades; hsa05020:Prion diseases; hsa05133:Pertussis; hsa05150:Staphylococcus aureus infection; hsa05168:Herpes simplex infection; hsa05322:Systemic lupus erythematosus	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	.	P01031
TTRJ91Q	HUMAN complement C5 alpha (C5A)	P01031 (678-1676)	CO5_HUMAN (678-1676)	Complement system	Complement C5 alpha chain	C5	"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."	.	.	TLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQGVGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKENSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVHVTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLKALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVCEGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITFIKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC	.	03-2020-InflaRx Doses First Patient in Multicenter Randomized Clinical Trial in Severe Progressed COVID-19 Pneumonia in Europe upon Receipt of Initial Positive Human Data with InflaRxs anti-C5a Technology	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P01031
TT2LJRF	C5 messenger RNA (C5 mRNA)	P01031	CO5_HUMAN	.	C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4	C5	"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."	.	.	MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQNSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETVLTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGYKNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNNKYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVPVTLNAQTIDVNQETSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGEHLNIIVTPKSPYIDKITHYNYLILSKGKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIVTGEQTAELVSDSVWLNIEEKCGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGLNNANVFHLAGLTFLTNANADDSQENDEPCKEILRPRRTLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQGVGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKENSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVHVTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLKALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVCEGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITFIKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC	Clinical trial	"Clinical pipeline report, company report or official report of Alnylam Pharmaceuticals."	.	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04610: Complement and coagulation cascades; hsa04613: Neutrophil extracellular trap formation; hsa04936: Alcoholic liver disease; hsa05020: Prion disease; hsa05133: Pertussis; hsa05150: Staphylococcus aureus infection; hsa05168: Herpes simplex virus 1 infection; hsa05171: Coronavirus disease - COVID-19; hsa05322: Systemic lupus erythematosus	R-HSA-166665: Terminal pathway of complement; 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	.	P01031
TTN0GJ5	HUMAN complement C5 protein (C5)	P01031	CO5_HUMAN	Complement system	C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4	C5	"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."	.	.	MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQNSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETVLTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGYKNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNNKYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVPVTLNAQTIDVNQETSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGEHLNIIVTPKSPYIDKITHYNYLILSKGKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIVTGEQTAELVSDSVWLNIEEKCGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGLNNANVFHLAGLTFLTNANADDSQENDEPCKEILRPRRTLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQGVGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKENSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVHVTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLKALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVCEGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITFIKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC	.	Complement as a target in COVID-19 Nat Rev Immunol. 2020 Apr 23.	.	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04610: Complement and coagulation cascades; hsa04613: Neutrophil extracellular trap formation; hsa04936: Alcoholic liver disease; hsa05020: Prion disease; hsa05133: Pertussis; hsa05150: Staphylococcus aureus infection; hsa05168: Herpes simplex virus 1 infection; hsa05171: Coronavirus disease - COVID-19; hsa05322: Systemic lupus erythematosus	R-HSA-166665: Terminal pathway of complement; 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	.	P01031
TTHXFA1	C5a anaphylatoxin chemotactic receptor (C5AR1)	P21730	C5AR1_HUMAN	GPCR rhodopsin	CD88; C5aR; C5a-R; C5a anaphylatoxin chemotactic receptor 1; C5R1	C5AR1	"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."	.	6C1R; 6C1Q; 5O9H	MDSFNYTTPDYGHYDDKDTLDLNTPVDKTSNTLRVPDILALVIFAVVFLVGVLGNALVVWVTAFEAKRTINAIWFLNLAVADFLSCLALPILFTSIVQHHHWPFGGAACSILPSLILLNMYASILLLATISADRFLLVFKPIWCQNFRGAGLAWIACAVAWGLALLLTIPSFLYRVVREEYFPPKVLCGVDYSHDKRRERAVAIVRLVLGFLWPLLTLTICYTFILLRTWSRRATRSTKTLKVVVAVVASFFIFWLPYQVTGIMMSFLEPSSPTFLLLKKLDSLCVSFAYINCCINPIIYVVAGQGFQGRLRKSLPSLLRNVLTEESVVRESKSFTRSTVDTMAQKTQAV	Clinical trial	"Clinical pipeline report, company report or official report of ChemoCentryx."	21	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04610:Complement and coagulation cascades; hsa05150:Staphylococcus aureus infection	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events	.	P21730
TTQLO2H	HUMAN C5a receptor (C5aR)	P21730	C5AR1_HUMAN	GPCR rhodopsin	CD88; C5aR; C5a-R; C5a anaphylatoxin chemotactic receptor 1; C5R1	C5AR1	"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."	.	6C1R; 6C1Q; 5O9H	MDSFNYTTPDYGHYDDKDTLDLNTPVDKTSNTLRVPDILALVIFAVVFLVGVLGNALVVWVTAFEAKRTINAIWFLNLAVADFLSCLALPILFTSIVQHHHWPFGGAACSILPSLILLNMYASILLLATISADRFLLVFKPIWCQNFRGAGLAWIACAVAWGLALLLTIPSFLYRVVREEYFPPKVLCGVDYSHDKRRERAVAIVRLVLGFLWPLLTLTICYTFILLRTWSRRATRSTKTLKVVVAVVASFFIFWLPYQVTGIMMSFLEPSSPTFLLLKKLDSLCVSFAYINCCINPIIYVVAGQGFQGRLRKSLPSLLRNVLTEESVVRESKSFTRSTVDTMAQKTQAV	.	Blockade of the C5a-C5aR axis alleviates lung damage in hDPP4-transgenic mice infected with MERS-CoV. Emerg Microbes Infect. 2018 Apr 24;7(1):77.	.	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04610: Complement and coagulation cascades; hsa04613: Neutrophil extracellular trap formation; hsa04936: Alcoholic liver disease; hsa05150: Staphylococcus aureus infection; hsa05171: Coronavirus disease - COVID-19	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-418594: G alpha (i) signalling events; R-HSA-6798695: Neutrophil degranulation; R-HSA-977606: Regulation of Complement cascade	.	P21730
TTA4SHR	C9orf72 messenger RNA (C9orf72 mRNA)	Q96LT7	CI072_HUMAN	.	.	C9orf72	"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)."	.	.	MSTLCPPPSPAVAKTEIALSGKSPLLAATFAYWDNILGPRVRHIWAPKTEQVLLSDGEITFLANHTLNGEILRNAESGAIDVKFFVLSEKGVIIVSLIFDGNWNGDRSTYGLSIILPQTELSFYLPLHRVCVDRLTHIIRKGRIWMHKERQENVQKIILEGTERMEDQGQSIIPMLTGEVIPVMELLSSMKSHSVPEEIDIADTVLNDDDIGDSCHEGFLLNAISSHLQTCGCSVVVGSSAEKVNKIVRTLCLFLTPAERKCSRLCEAESSFKYESGLFVQGLLKDSTGSFVLPFRQVMYAPYPTTHIDVDVNTVKQMPPCHEHIYNQRRYMRSELTAFWRATSEEDMAQDTIIYTDESFTPDLNIFQDVLHRDTLVKAFLDQVFQLKPGLSLRSTFLAQFLLVLHRKALTLIKYIEDDTQKGKKPFKSLRNLKIDLDLTAEGDLNIIMALAEKIKPGLHSFIFGRPFYTSVQERDVLMTF	Clinical trial	"Clinical pipeline report, company report or official report of Ionis Pharmaceuticals."	.	.	.	.	.	.	.	.	.	.	.	hsa04140: Autophagy - animal; hsa05014: Amyotrophic lateral sclerosis; hsa05022: Pathways of neurodegeneration - multiple diseases	.	.	Q96LT7
TTHQPL7	Carbonic anhydrase I (CA-I)	P00915	CAH1_HUMAN	Alpha-carbonic anhydrase	Carbonic anhydrase B; Carbonic anhydrase 1; Carbonate dehydratase I; CAB	CA1	Can hydrates cyanamide to urea. Reversible hydration of carbon dioxide.	EC 4.2.1.1	6HWZ; 6G3V; 6FAG; 6FAF; 6F3B	MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF	Successful	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2597).	34	EC:4.2	Carbon oxygen lyase	alpha-carbonic anhydrase family.	4.2.1.1	Carbon-oxygen lyases	Eukaryotic-type carbonic anhydrase	PF00194	PF00194; Carb_anhydrase	.	.	hsa00910:Nitrogen metabolism	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	MetaCyc:HS05785-MON	P00915
TTSYM0R	Carbonic anhydrase XII (CA-XII)	O43570	CAH12_HUMAN	Alpha-carbonic anhydrase	Tumor antigen HOM-RCC-3.1.3; Carbonic anhydrase 12; Carbonate dehydratase XII	CA12	Reversible hydration of carbon dioxide.	EC 4.2.1.1	6G7A; 6G5L; 5MSB; 5MSA; 5LLP	MPRRSLHAAAVLLLVILKEQPSSPAPVNGSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGLQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSHLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPREMINNFRQVQKFDERLVYTSFSQVQVCTAAGLSLGIILSLALAGILGICIVVVVSIWLFRRKSIKKGDNKGVIYKPATKMETEAHA	Successful	Sulfonamide linked neoglycoconjugates--a new class of inhibitors for cancer-associated carbonic anhydrases. J Med Chem. 2010 Apr 8;53(7):2913-26.	34	EC:4.2	.	alpha-carbonic anhydrase family.	4.2.1.1	Carbon-oxygen lyases	Eukaryotic-type carbonic anhydrase	PF00194	PF00194; Carb_anhydrase	.	.	hsa00910:Nitrogen metabolism	R-HSA-1475029:Reversible hydration of carbon dioxide	.	O43570
TTQPHSR	Carbonic anhydrase XIII	.	CAH13_HUMAN	Single Protein	Carbonate dehydratase XIII; CA-XIII; Carbonic anhydrase 13	CA13	Reversible hydration of carbon dioxide.	.	.	MSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSVLRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQKITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAAAFLVSNHRPPQPLKGRKVRASFH	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q8N1Q1
TTEYTKG	Carbonic anhydrase XIV (CA-XIV)	Q9ULX7	CAH14_HUMAN	Alpha-carbonic anhydrase	UNQ690/PRO1335; Carbonic anhydrase 14; Carbonate dehydratase XIV	CA14	Reversible hydration of carbon dioxide.	EC 4.2.1.1	5CJF; 4LU3	MLFSALLLEVIWILAADGGQHWTYEGPHGQDHWPASYPECGNNAQSPIDIQTDSVTFDPDLPALQPHGYDQPGTEPLDLHNNGHTVQLSLPSTLYLGGLPRKYVAAQLHLHWGQKGSPGGSEHQINSEATFAELHIVHYDSDSYDSLSEAAERPQGLAVLGILIEVGETKNIAYEHILSHLHEVRHKDQKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEEEPSKLLVQNYRALQPLNQRMVFASFIQAGSSYTTGEMLSLGVGILVGCLCLLLAVYFIARKIRKKRLENRKSVVFTSAQATTEA	Successful	Carbonic anhydrase inhibitors: inhibition of the transmembrane isozyme XIV with sulfonamides. Bioorg Med Chem Lett. 2005 Sep 1;15(17):3828-33.	34	EC:4.2	.	alpha-carbonic anhydrase family.	4.2.1.1	Carbon-oxygen lyases	Eukaryotic-type carbonic anhydrase	PF00194	PF00194; Carb_anhydrase	.	.	hsa00910:Nitrogen metabolism	R-HSA-1475029:Reversible hydration of carbon dioxide	.	Q9ULX7
TTANPDJ	Carbonic anhydrase II (CA-II)	P00918	CAH2_HUMAN	Alpha-carbonic anhydrase	Carbonic anhydrase C; Carbonic anhydrase 2; Carbonate dehydratase II; CAC	CA2	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.	EC 4.2.1.1	9CA2; 8CA2; 7CA2; 6QEB; 6MBY	MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK	Successful	Nature of the inhibition of carbonic anhydrase by acetazolamide and benzthiazide. J Pharmacol Exp Ther. 1961 Mar;131:271-4.	34	EC:4.2	Carbon oxygen lyase	alpha-carbonic anhydrase family.	4.2.1.1	Carbon-oxygen lyases	Eukaryotic-type carbonic anhydrase	PF00194	PF00194; Carb_anhydrase	.	.	hsa00910:Nitrogen metabolism; hsa04964:Proximal tubule bicarbonate reclamation; hsa04966:Collecting duct acid secretion; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04976:Bile secretion	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	.	P00918
TTXUK5D	Carbonic anhydrase III	.	CAH3_HUMAN	Single Protein	Carbonate dehydratase III; Carbonic anhydrase 3; CA-III	CA3	Reversible hydration of carbon dioxide.	.	.	MAKEWGYASHNGPDHWHELFPNAKGENQSPVELHTKDIRHDPSLQPWSVSYDGGSAKTILNNGKTCRVVFDDTYDRSMLRGGPLPGPYRLRQFHLHWGSSDDHGSEHTVDGVKYAAELHLVHWNPKYNTFKEALKQRDGIAVIGIFLKIGHENGEFQIFLDALDKIKTKGKEAPFTKFDPSCLFPACRDYWTYQGSFTTPPCEECIVWLLLKEPMTVSSDQMAKLRSLLSSAENEPPVPLVSNWRPPQPINNRVVRASFK	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P07451
TTZHA0O	Carbonic anhydrase IV (CA-IV)	P22748	CAH4_HUMAN	Alpha-carbonic anhydrase	Carbonic anhydrase 4; Carbonate dehydratase IV; CAIV	CA4	"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."	EC 4.2.1.1	5KU6; 5JNC; 5JNA; 5JN9; 5JN8	MRMLLALLALSAARPSASAESHWCYEVQAESSNYPCLVPVKWGGNCQKDRQSPINIVTTKAKVDKKLGRFFFSGYDKKQTWTVQNNGHSVMMLLENKASISGGGLPAPYQAKQLHLHWSDLPYKGSEHSLDGEHFAMEMHIVHEKEKGTSRNVKEAQDPEDEIAVLAFLVEAGTQVNEGFQPLVEALSNIPKPEMSTTMAESSLLDLLPKEEKLRHYFRYLGSLTTPTCDEKVVWTVFREPIQLHREQILAFSQKLYYDKEQTVSMKDNVRPLQQLGQRTVIKSGAPGRPLPWALPALLGPMLACLLAGFLR	Successful	Carbonic anhydrase inhibitors. Inhibition of the membrane-bound human and bovine isozymes IV with sulfonamides. Bioorg Med Chem Lett. 2005 Feb 15;15(4):1149-54.	34	EC:4.2	.	alpha-carbonic anhydrase family.	4.2.1.1	Carbon-oxygen lyases	Eukaryotic-type carbonic anhydrase	PF00194	PF00194; Carb_anhydrase	.	.	hsa00910:Nitrogen metabolism; hsa04964:Proximal tubule bicarbonate reclamation	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	.	P22748
TT75WPO	Carbonic anhydrase VA	.	CAH5A_HUMAN	Single Protein	"Carbonate dehydratase VA; Carbonic anhydrase 5A; Carbonic anhydrase 5A, mitochondrial; CA-VA"	CA5A	Reversible hydration of carbon dioxide. Low activity.	.	.	MLGRNTWKTSAFSFLVEQMWAPLWSRSMRPGRWCSQRSCAWQTSNNTLHPLWTVPVSVPGGTRQSPINIQWRDSVYDPQLKPLRVSYEAASCLYIWNTGYLFQVEFDDATEASGISGGPLENHYRLKQFHFHWGAVNEGGSEHTVDGHAYPAELHLVHWNSVKYQNYKEAVVGENGLAVIGVFLKLGAHHQTLQRLVDILPEIKHKDARAAMRPFDPSTLLPTCWDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQLSAFRTLLFSALGEEEKMMVNNYRPLQPLMNRKVWASFQATNEGTRS	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P35218
TTB9PKU	Carbonic anhydrase VB	.	CAH5B_HUMAN	Single Protein	"Carbonate dehydratase VB; Carbonic anhydrase 5B; Carbonic anhydrase 5B, mitochondrial; CA-VB"	CA5B	Reversible hydration of carbon dioxide.	.	.	MVVMNSLRVILQASPGKLLWRKFQIPRFMPARPCSLYTCTYKTRNRALHPLWESVDLVPGGDRQSPINIRWRDSVYDPGLKPLTISYDPATCLHVWNNGYSFLVEFEDSTDKSVIKGGPLEHNYRLKQFHFHWGAIDAWGSEHTVDSKCFPAELHLVHWNAVRFENFEDAALEENGLAVIGVFLKLGKHHKELQKLVDTLPSIKHKDALVEFGSFDPSCLMPTCPDYWTYSGSLTTPPLSESVTWIIKKQPVEVDHDQLEQFRTLLFTSEGEKEKRMVDNFRPLQPLMNRTVRSSFRHDYVLNVQAKPKPATSQATP	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9Y2D0
TTCFSPE	Carbonic anhydrase VI (CA-VI)	P23280	CAH6_HUMAN	Alpha-carbonic anhydrase	Secreted carbonic anhydrase; Salivary carbonic anhydrase; Carbonic anhydrase 6; Carbonate dehydratase VI	CA6	Its role in saliva is unknown. Reversible hydration of carbon dioxide.	EC 4.2.1.1	3FE4	MRALVLLLSLFLLGGQAQHVSDWTYSEGALDEAHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMTVADGTVYIAQQMHFHWGGASSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNYPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRNKTIHNDYRRTQPLNHRVVESNFPNQEYTLGSEFQFYLHKIEEILDYLRRALN	Successful	"Cloning, expression, post-translational modifications and inhibition studies on the latest mammalian carbonic anhydrase isoform, CA XV. J Med Chem. 2009 Feb 12;52(3):646-54."	34	EC:4.2	Carbon oxygen lyase	alpha-carbonic anhydrase family.	4.2.1.1	Carbon-oxygen lyases	Eukaryotic-type carbonic anhydrase	PF00194	PF00194; Carb_anhydrase	.	.	hsa00910:Nitrogen metabolism	R-HSA-1475029:Reversible hydration of carbon dioxide	.	P23280
TTJC376	Carbonic anhydrase VII (CA-VII)	P43166	CAH7_HUMAN	Alpha-carbonic anhydrase	Carbonic anhydrase 7; Carbonate dehydratase VII	CA7	Reversible hydration of carbon dioxide.	EC 4.2.1.1	6H38; 6H37; 6H36; 6G4T; 3ML5	MTGHHGWGYGQDDGPSHWHKLYPIAQGDRQSPINIISSQAVYSPSLQPLELSYEACMSLSITNNGHSVQVDFNDSDDRTVVTGGPLEGPYRLKQFHFHWGKKHDVGSEHTVDGKSFPSELHLVHWNAKKYSTFGEAASAPDGLAVVGVFLETGDEHPSMNRLTDALYMVRFKGTKAQFSCFNPKCLLPASRHYWTYPGSLTTPPLSESVTWIVLREPICISERQMGKFRSLLFTSEDDERIHMVNNFRPPQPLKGRVVKASFRA	Patented-recorded	Carbonic anhydrase inhibitors as antitumor/antimetastatic agents: a patent review (2008-2018).Expert Opin Ther Pat. 2018 Oct;28(10):729-740.	15.5	EC:4.2	Alpha-carbonic anhydrase family	alpha-carbonic anhydrase family.	4.2.1.1	Carbon-oxygen lyases	Eukaryotic-type carbonic anhydrase	PF00194	PF00194; Carb_anhydrase	.	.	hsa00910: Nitrogen metabolism; hsa01100: Metabolic pathways	R-HSA-1475029: Reversible hydration of carbon dioxide	.	P43166
TT2LVK8	Carbonic anhydrase IX (CA-IX)	Q16790	CAH9_HUMAN	Alpha-carbonic anhydrase	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	CA9	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.	EC 4.2.1.1	6G9U; 6G98; 6FE2; 6FE1; 6FE0	MAPLCPSPWLPLLIPAPAPGLTVQLLLSLLLLVPVHPQRLPRMQEDSPLGGGSSGEDDPLGEEDLPSEEDSPREEDPPGEEDLPGEEDLPGEEDLPEVKPKSEEEGSLKLEDLPTVEAPGDPQEPQNNAHRDKEGDDQSHWRYGGDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLPELRLRNNGHSVQLTLPPGLEMALGPGREYRALQLHLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGSETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSRLQLNFRATQPLNGRVIEASFPAGVDSSPRAAEPVQLNSCLAAGDILALVFGLLFAVTSVAFLVQMRRQHRRGTKGGVSYRPAEVAETGA	Clinical trial	Sulfonamide linked neoglycoconjugates--a new class of inhibitors for cancer-associated carbonic anhydrases. J Med Chem. 2010 Apr 8;53(7):2913-26.	25	EC:4.2	Carbon oxygen lyase	alpha-carbonic anhydrase family.	4.2.1.1	Carbon-oxygen lyases	Eukaryotic-type carbonic anhydrase	PF00194	PF00194; Carb_anhydrase	.	.	hsa00910:Nitrogen metabolism	R-HSA-1234158:Regulation of gene expression by Hypoxia-inducible Factor; R-HSA-1475029:Reversible hydration of carbon dioxide	.	Q16790
TTX4QDJ	Voltage-gated calcium channel alpha Cav2.1 (CACNA1A)	O00555	CAC1A_HUMAN	Voltage-gated ion channel	"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"	CACNA1A	"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."	.	3BXK	MARFGDEMPARYGGGGSGAAAGVVVGSGGGRGAGGSRQGGQPGAQRMYKQSMAQRARTMALYNPIPVRQNCLTVNRSLFLFSEDNVVRKYAKKITEWPPFEYMILATIIANCIVLALEQHLPDDDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFAFHKGSYLRNGWNVMDFVVVLTGILATVGTEFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMIPLLQIGLLLFFAILIFAIIGLEFYMGKFHTTCFEEGTDDIQGESPAPCGTEEPARTCPNGTKCQPYWEGPNNGITQFDNILFAVLTVFQCITMEGWTDLLYNSNDASGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYMEWISKAEEVILAEDETDGEQRHPFDALRRTTIKKSKTDLLNPEEAEDQLADIASVGSPFARASIKSAKLENSTFFHKKERRMRFYIRRMVKTQAFYWTVLSLVALNTLCVAIVHYNQPEWLSDFLYYAEFIFLGLFMSEMFIKMYGLGTRPYFHSSFNCFDCGVIIGSIFEVIWAVIKPGTSFGISVLRALRLLRIFKVTKYWASLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFDEGTPPTNFDTFPAAIMTVFQILTGEDWNEVMYDGIKSQGGVQGGMVFSIYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEQEEEEAANQKLALQKAKEVAEVSPLSAANMSIAVKEQQKNQKPAKSVWEQRTSEMRKQNLLASREALYNEMDPDERWKAAYTRHLRPDMKTHLDRPLVVDPQENRNNNTNKSRAAEPTVDQRLGQQRAEDFLRKQARYHDRARDPSGSAGLDARRPWAGSQEAELSREGPYGRESDHHAREGSLEQPGFWEGEAERGKAGDPHRRHVHRQGGSRESRSGSPRTGADGEHRRHRAHRRPGEEGPEDKAERRARHREGSRPARGGEGEGEGPDGGERRRRHRHGAPATYEGDARREDKERRHRRRKENQGSGVPVSGPNLSTTRPIQQDLGRQDPPLAEDIDNMKNNKLATAESAAPHGSLGHAGLPQSPAKMGNSTDPGPMLAIPAMATNPQNAASRRTPNNPGNPSNPGPPKTPENSLIVTNPSGTQTNSAKTARKPDHTTVDIPPACPPPLNHTVVQVNKNANPDPLPKKEEEKKEEEEDDRGEDGPKPMPPYSSMFILSTTNPLRRLCHYILNLRYFEMCILMVIAMSSIALAAEDPVQPNAPRNNVLRYFDYVFTGVFTFEMVIKMIDLGLVLHQGAYFRDLWNILDFIVVSGALVAFAFTGNSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVFNILIVYMLFMFIFAVVAVQLFKGKFFHCTDESKEFEKDCRGKYLLYEKNEVKARDREWKKYEFHYDNVLWALLTLFTVSTGEGWPQVLKHSVDATFENQGPSPGYRMEMSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKMMEEYSLEKNERACIDFAISAKPLTRHMPQNKQSFQYRMWQFVVSPPFEYTIMAMIALNTIVLMMKFYGASVAYENALRVFNIVFTSLFSLECVLKVMAFGILNYFRDAWNIFDFVTVLGSITDILVTEFGNNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIGIDVEDEDSDEDEFQITEHNNFRTFFQALMLLFRSATGEAWHNIMLSCLSGKPCDKNSGILTRECGNEFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEYVRVWAEYDPAAWGRMPYLDMYQMLRHMSPPLGLGKKCPARVAYKRLLRMDLPVADDNTVHFNSTLMALIRTALDIKIAKGGADKQQMDAELRKEMMAIWPNLSQKTLDLLVTPHKSTDLTVGKIYAAMMIMEYYRQSKAKKLQAMREEQDRTPLMFQRMEPPSPTQEGGPGQNALPSTQLDPGGALMAHESGLKESPSWVTQRAQEMFQKTGTWSPEQGPPTDMPNSQPNSQSVEMREMGRDGYSDSEHYLPMEGQGRAASMPRLPAENQRRRGRPRGNNLSTISDTSPMKRSASVLGPKARRLDDYSLERVPPEENQRHHQRRRDRSHRASERSLGRYTDVDTGLGTDLSMTTQSGDLPSKERDQERGRPKDRKHRQHHHHHHHHHHPPPPDKDRYAQERPDHGRARARDQRWSRSPSEGREHMAHRQGSSSVSGSPAPSTSGTSTPRRGRRQLPQTPSTPRPHVSYSPVIRKAGGSGPPQQQQQQQQQQQQQAVARPGRAATSGPRRYPGPTAEPLAGDRPPTGGHSSGRSPRMERRVPGPARSESPRACRHGGARWPASGPHVSEGPPGPRHHGYYRGSDYDEADGPGSGGGEEAMAGAYDAPPPVRHASSGATGRSPRTPRASGPACASPSRHGRRLPNGYYPAHGLARPRGPGSRKGLHEPYSESDDDWC	Successful	Antibodies and venom peptides: new modalities for ion channels. Nat Rev Drug Discov. 2019 May;18(5):339-357.	34	.	.	.	.	.	.	.	.	.	.	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	R-HSA-112308:Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels; R-HSA-422356:Regulation of insulin secretion	.	O00555
TT4FDG6	Voltage-gated calcium channel alpha Cav2.2 (CACNA1B)	Q00975	CAC1B_HUMAN	Voltage-gated ion channel	"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"	CACNA1B	"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."	.	2LCM	MVRFGDELGGRYGGPGGGERARGGGAGGAGGPGPGGLQPGQRVLYKQSIAQRARTMALYNPIPVKQNCFTVNRSLFVFSEDNVVRKYAKRITEWPPFEYMILATIIANCIVLALEQHLPDGDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFVFHKGSYLRNGWNVMDFVVVLTGILATAGTDFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMVPLLQIGLLLFFAILMFAIIGLEFYMGKFHKACFPNSTDAEPVGDFPCGKEAPARLCEGDTECREYWPGPNFGITNFDNILFAILTVFQCITMEGWTDILYNTNDAAGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYLEWIFKAEEVMLAEEDRNAEEKSPLDVLKRAATKKSRNDLIHAEEGEDRFADLCAVGSPFARASLKSGKTESSSYFRRKEKMFRFFIRRMVKAQSFYWVVLCVVALNTLCVAMVHYNQPRRLTTTLYFAEFVFLGLFLTEMSLKMYGLGPRSYFRSSFNCFDFGVIVGSVFEVVWAAIKPGSSFGISVLRALRLLRIFKVTKYWSSLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFQDETPTTNFDTFPAAILTVFQILTGEDWNAVMYHGIESQGGVSKGMFSSFYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEEEMEEAANQKLALQKAKEVAEVSPMSAANISIAARQQNSAKARSVWEQRASQLRLQNLRASCEALYSEMDPEERLRFATTRHLRPDMKTHLDRPLVVELGRDGARGPVGGKARPEAAEAPEGVDPPRRHHRHRDKDKTPAAGDQDRAEAPKAESGEPGAREERPRPHRSHSKEAAGPPEARSERGRGPGPEGGRRHHRRGSPEEAAEREPRRHRAHRHQDPSKECAGAKGERRARHRGGPRAGPREAESGEEPARRHRARHKAQPAHEAVEKETTEKEATEKEAEIVEADKEKELRNHQPREPHCDLETSGTVTVGPMHTLPSTCLQKVEEQPEDADNQRNVTRMGSQPPDPNTIVHIPVMLTGPLGEATVVPSGNVDLESQAEGKKEVEADDVMRSGPRPIVPYSSMFCLSPTNLLRRFCHYIVTMRYFEVVILVVIALSSIALAAEDPVRTDSPRNNALKYLDYIFTGVFTFEMVIKMIDLGLLLHPGAYFRDLWNILDFIVVSGALVAFAFSGSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVLNILIVYMLFMFIFAVIAVQLFKGKFFYCTDESKELERDCRGQYLDYEKEEVEAQPRQWKKYDFHYDNVLWALLTLFTVSTGEGWPMVLKHSVDATYEEQGPSPGYRMELSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKVMSECSLEKNERACIDFAISAKPLTRYMPQNRQSFQYKTWTFVVSPPFEYFIMAMIALNTVVLMMKFYDAPYEYELMLKCLNIVFTSMFSMECVLKIIAFGVLNYFRDAWNVFDFVTVLGSITDILVTEIAETNNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIALDDDTSINRHNNFRTFLQALMLLFRSATGEAWHEIMLSCLSNQACDEQANATECGSDFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEFIRVWAEYDPAACGRISYNDMFEMLKHMSPPLGLGKKCPARVAYKRLVRMNMPISNEDMTVHFTSTLMALIRTALEIKLAPAGTKQHQCDAELRKEISVVWANLPQKTLDLLVPPHKPDEMTVGKVYAALMIFDFYKQNKTTRDQMQQAPGGLSQMGPVSLFHPLKATLEQTQPAVLRGARVFLRQKSSTSLSNGGAIQNQESGIKESVSWGTQRTQDAPHEARPPLERGHSTEIPVGRSGALAVDVQMQSITRRGPDGEPQPGLESQGRAASMPRLAAETQPVTDASPMKRSISTLAQRPRGTHLCSTTPDRPPPSQASSHHHHHRCHRRRDRKQRSLEKGPSLSADMDGAPSSAVGPGLPPGEGPTGCRRERERRQERGRSQERRQPSSSSSEKQRFYSCDRFGGREPPKPKPSLSSHPTSPTAGQEPGPHPQGSGSVNGSPLLSTSGASTPGRGGRRQLPQTPLTPRPSITYKTANSSPIHFAGAQTSLPAFSPGRLSRGLSEHNALLQRDPLSQPLAPGSRIGSDPYLGQRLDSEASVHALPEDTLTFEEAVATNSGRSSRTSYVSSLTSQSHPLRRVPNGYHCTLGLSSGGRARHSYHHPDQDHWC	Successful	Emerging treatments for traumatic brain injury. Expert Opin Emerg Drugs. 2009 Mar;14(1):67-84.	34	.	.	.	.	.	.	.	.	.	.	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	R-HSA-112308:Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels	.	Q00975
TTZIFHC	Voltage-gated calcium channel alpha Cav1.2 (CACNA1C)	Q13936	CAC1C_HUMAN	Voltage-gated ion channel	"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"	CACNA1C	"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."	.	6DAF; 6DAE; 6DAD; 6C0A; 5V2Q	MVNENTRMYIPEENHQGSNYGSPRPAHANMNANAAAGLAPEHIPTPGAALSWQAAIDAARQAKLMGSAGNATISTVSSTQRKRQQYGKPKKQGSTTATRPPRALLCLTLKNPIRRACISIVEWKPFEIIILLTIFANCVALAIYIPFPEDDSNATNSNLERVEYLFLIIFTVEAFLKVIAYGLLFHPNAYLRNGWNLLDFIIVVVGLFSAILEQATKADGANALGGKGAGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFMGKMHKTCYNQEGIADVPAEDDPSPCALETGHGRQCQNGTVCKPGWDGPKHGITNFDNFAFAMLTVFQCITMEGWTDVLYWVNDAVGRDWPWIYFVTLIIIGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEDEGMDEEKPRNMSMPTSETESVNTENVAGGDIEGENCGARLAHRISKSKFSRYWRRWNRFCRRKCRAAVKSNVFYWLVIFLVFLNTLTIASEHYNQPNWLTEVQDTANKALLALFTAEMLLKMYSLGLQAYFVSLFNRFDCFVVCGGILETILVETKIMSPLGISVLRCVRLLRIFKITRYWNSLSNLVASLLNSVRSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDEMQTRRSTFDNFPQSLLTVFQILTGEDWNSVMYDGIMAYGGPSFPGMLVCIYFIILFICGNYILLNVFLAIAVDNLADAESLTSAQKEEEEEKERKKLARTASPEKKQELVEKPAVGESKEEKIELKSITADGESPPATKINMDDLQPNENEDKSPYPNPETTGEEDEEEPEMPVGPRPRPLSELHLKEKAVPMPEASAFFIFSSNNRFRLQCHRIVNDTIFTNLILFFILLSSISLAAEDPVQHTSFRNHILFYFDIVFTTIFTIEIALKILGNADYVFTSIFTLEIILKMTAYGAFLHKGSFCRNYFNILDLLVVSVSLISFGIQSSAINVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVIVTTLLQFMFACIGVQLFKGKLYTCSDSSKQTEAECKGNYITYKDGEVDHPIIQPRSWENSKFDFDNVLAAMMALFTVSTFEGWPELLYRSIDSHTEDKGPIYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLRRYIPKNQHQYKVWYVVNSTYFEYLMFVLILLNTICLAMQHYGQSCLFKIAMNILNMLFTGLFTVEMILKLIAFKPKGYFSDPWNVFDFLIVIGSIIDVILSETNHYFCDAWNTFDALIVVGSIVDIAITEVNPAEHTQCSPSMNAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQDIMLACMPGKKCAPESEPSNSTEGETPCGSSFAVFYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVSMNMPLNSDGTVMFNATLFALVRTALRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSLQAGLRTLHDIGPEIRRAISGDLTAEEELDKAMKEAVSAASEDDIFRRAGGLFGNHVSYYQSDGRSAFPQTFTTQRPLHINKAGSSQGDTESPSHEKLVDSTFTPSSYSSTGSNANINNANNTALGRLPRPAGYPSTVSTVEGHGPPLSPAIRVQEVAWKLSSNRERHVPMCEDLELRRDSGSAGTQAHCLLLRKANPSRCHSRESQAAMAGQEETSQDETYEVKMNHDTEACSEPSLLSTEMLSYQDDENRQLTLPEEDKRDIRQSPKRGFLRSASLGRRASFHLECLKRQKDRGGDISQKTVLPLHLVHHQALAVAGLSPLLQRSHSPASFPRPFATPPATPGSRGWPPQPVPTLRLEGVESSEKLNSSFPSIHCGSWAETTPGGGGSSAARRVRPVSLMVPSQAGAPGRQFHGSASSLVEAVLISEGLGQFAQDPKFIEVTTQELADACDMTIEEMESAADNILSGGAPQSPNGALLPFVNCRDAGQDRAGGEEDAGCVRARGRPSEEELQDSRVYVSSL	Successful	Alpha- and beta-adrenoceptors: from the gene to the clinic. 2. Structure-activity relationships and therapeutic applications. J Med Chem. 1995 Sep 15;38(19):3681-716.	34	TC=1.A.1	Voltage-gated ion channel	calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1C subfamily. 	.	.	"Voltage gated calcium channel IQ domain; Voltage-gated calcium channel subunit alpha, C-term; Voltage-dependent L-type calcium channel, IQ-associated; Ion transport protein"	PF08763; PF16885; PF16905; PF00520	PF08763; Ca_chan_IQ; PF16885; CAC1F_C; PF16905; GPHH; PF00520; Ion_trans	1.A.1.11.4	The Voltage-gated Ion Channel (VIC) Superfamily 	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	"R-HSA-400042:Adrenaline,noradrenaline inhibits insulin secretion; R-HSA-419037:NCAM1 interactions; R-HSA-422356:Regulation of insulin secretion"	.	Q13936
TT7RGTM	Voltage-gated calcium channel alpha Cav1.3 (CACNA1D)	Q01668	CAC1D_HUMAN	Voltage-gated ion channel	"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"	CACNA1D	"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)."	.	3LV3	MMMMMMMKKMQHQRQQQADHANEANYARGTRLPLSGEGPTSQPNSSKQTVLSWQAAIDAARQAKAAQTMSTSAPPPVGSLSQRKRQQYAKSKKQGNSSNSRPARALFCLSLNNPIRRACISIVEWKPFDIFILLAIFANCVALAIYIPFPEDDSNSTNHNLEKVEYAFLIIFTVETFLKIIAYGLLLHPNAYVRNGWNLLDFVIVIVGLFSVILEQLTKETEGGNHSSGKSGGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFIGKMHKTCFFADSDIVAEEDPAPCAFSGNGRQCTANGTECRSGWVGPNGGITNFDNFAFAMLTVFQCITMEGWTDVLYWMNDAMGFELPWVYFVSLVIFGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEEEGGEEGKRNTSMPTSETESVNTENVSGEGENRGCCGSLCQAISKSKLSRRWRRWNRFNRRRCRAAVKSVTFYWLVIVLVFLNTLTISSEHYNQPDWLTQIQDIANKVLLALFTCEMLVKMYSLGLQAYFVSLFNRFDCFVVCGGITETILVELEIMSPLGISVFRCVRLLRIFKVTRHWTSLSNLVASLLNSMKSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDETQTKRSTFDNFPQALLTVFQILTGEDWNAVMYDGIMAYGGPSSSGMIVCIYFIILFICGNYILLNVFLAIAVDNLADAESLNTAQKEEAEEKERKKIARKESLENKKNNKPEVNQIANSDNKVTIDDYREEDEDKDPYPPCDVPVGEEEEEEEEDEPEVPAGPRPRRISELNMKEKIAPIPEGSAFFILSKTNPIRVGCHKLINHHIFTNLILVFIMLSSAALAAEDPIRSHSFRNTILGYFDYAFTAIFTVEILLKMTTFGAFLHKGAFCRNYFNLLDMLVVGVSLVSFGIQSSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIMIVTTLLQFMFACIGVQLFKGKFYRCTDEAKSNPEECRGLFILYKDGDVDSPVVRERIWQNSDFNFDNVLSAMMALFTVSTFEGWPALLYKAIDSNGENIGPIYNHRVEISIFFIIYIIIVAFFMMNIFVGFVIVTFQEQGEKEYKNCELDKNQRQCVEYALKARPLRRYIPKNPYQYKFWYVVNSSPFEYMMFVLIMLNTLCLAMQHYEQSKMFNDAMDILNMVFTGVFTVEMVLKVIAFKPKGYFSDAWNTFDSLIVIGSIIDVALSEADPTESENVPVPTATPGNSEESNRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIAMLFFIYAVIGMQMFGKVAMRDNNQINRNNNFQTFPQAVLLLFRCATGEAWQEIMLACLPGKLCDPESDYNPGEEYTCGSNFAIVYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWSEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVAMNMPLNSDGTVMFNATLFALVRTALKIKTEGNLEQANEELRAVIKKIWKKTSMKLLDQVVPPAGDDEVTVGKFYATFLIQDYFRKFKKRKEQGLVGKYPAKNTTIALQAGLRTLHDIGPEIRRAISCDLQDDEPEETKREEEDDVFKRNGALLGNHVNHVNSDRRDSLQQTNTTHRPLHVQRPSIPPASDTEKPLFPPAGNSVCHNHHNHNSIGKQVPTSTNANLNNANMSKAAHGKRPSIGNLEHVSENGHHSSHKHDREPQRRSSVKRTRYYETYIRSDSGDEQLPTICREDPEIHGYFRDPHCLGEQEYFSSEECYEDDSSPTWSRQNYGYYSRYPGRNIDSERPRGYHHPQGFLEDDDSPVCYDSRRSPRRRLLPPTPASHRRSSFNFECLRRQSSQEEVPSSPIFPHRTALPLHLMQQQIMAVAGLDSSKAQKYSPSHSTRSWATPPATPPYRDWTPCYTPLIQVEQSEALDQVNGSLPSLHRSSWYTDEPDISYRTFTPASLTVPSSFRNKNSDKQRSADSLVEAVLISEGLGRYARDPKFVSATKHEIADACDLTIDEMESAASTLLNGNVRPRANGDVGPLSHRQDYELQDFGPGYSDEEPDPGRDEEDLADEMICITTL	Clinical trial	Dihydropyrimidines: novel calcium antagonists with potent and long-lasting vasodilative and antihypertensive activity. J Med Chem. 1989 Oct;32(10):2399-406.	25	.	.	.	.	.	.	.	.	.	.	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	"R-HSA-400042:Adrenaline,noradrenaline inhibits insulin secretion; R-HSA-419037:NCAM1 interactions; R-HSA-422356:Regulation of insulin secretion"	.	Q01668
TTYRP0M	Voltage-gated calcium channel alpha Cav2.3 (CACNA1E)	Q15878	CAC1E_HUMAN	Voltage-gated ion channel	"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"	CACNA1E	"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."	.	3BXL	MARFGEAVVARPGSGDGDSDQSRNRQGTPVPASGQAAAYKQTKAQRARTMALYNPIPVRQNCFTVNRSLFIFGEDNIVRKYAKKLIDWPPFEYMILATIIANCIVLALEQHLPEDDKTPMSRRLEKTEPYFIGIFCFEAGIKIVALGFIFHKGSYLRNGWNVMDFIVVLSGILATAGTHFNTHVDLRTLRAVRVLRPLKLVSGIPSLQIVLKSIMKAMVPLLQIGLLLFFAILMFAIIGLEFYSGKLHRACFMNNSGILEGFDPPHPCGVQGCPAGYECKDWIGPNDGITQFDNILFAVLTVFQCITMEGWTTVLYNTNDALGATWNWLYFIPLIIIGSFFVLNLVLGVLSGEFAKERERVENRRAFMKLRRQQQIERELNGYRAWIDKAEEVMLAEENKNAGTSALEVLRRATIKRSRTEAMTRDSSDEHCVDISSVGTPLARASIKSAKVDGVSYFRHKERLLRISIRHMVKSQVFYWIVLSLVALNTACVAIVHHNQPQWLTHLLYYAEFLFLGLFLLEMSLKMYGMGPRLYFHSSFNCFDFGVTVGSIFEVVWAIFRPGTSFGISVLRALRLLRIFKITKYWASLRNLVVSLMSSMKSIISLLFLLFLFIVVFALLGMQLFGGRFNFNDGTPSANFDTFPAAIMTVFQILTGEDWNEVMYNGIRSQGGVSSGMWSAIYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEQEEEEAFNQKHALQKAKEVSPMSAPNMPSIERDRRRRHHMSMWEPRSSHLRERRRRHHMSVWEQRTSQLRKHMQMSSQEALNREEAPTMNPLNPLNPLSSLNPLNAHPSLYRRPRAIEGLALGLALEKFEEERISRGGSLKGDGGDRSSALDNQRTPLSLGQREPPWLARPCHGNCDPTQQEAGGGEAVVTFEDRARHRQSQRRSRHRRVRTEGKESSSASRSRSASQERSLDEAMPTEGEKDHELRGNHGAKEPTIQEERAQDLRRTNSLMVSRGSGLAGGLDEADTPLVLPHPELEVGKHVVLTEQEPEGSSEQALLGNVQLDMGRVISQSEPDLSCITANTDKATTESTSVTVAIPDVDPLVDSTVVHISNKTDGEASPLKEAEIREDEEEVEKKKQKKEKRETGKAMVPHSSMFIFSTTNPIRRACHYIVNLRYFEMCILLVIAASSIALAAEDPVLTNSERNKVLRYFDYVFTGVFTFEMVIKMIDQGLILQDGSYFRDLWNILDFVVVVGALVAFALANALGTNKGRDIKTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVTSLKNVFNILIVYKLFMFIFAVIAVQLFKGKFFYCTDSSKDTEKECIGNYVDHEKNKMEVKGREWKRHEFHYDNIIWALLTLFTVSTGEGWPQVLQHSVDVTEEDRGPSRSNRMEMSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKMMEECSLEKNERACIDFAISAKPLTRYMPQNRHTFQYRVWHFVVSPSFEYTIMAMIALNTVVLMMKYYSAPCTYELALKYLNIAFTMVFSLECVLKVIAFGFLNYFRDTWNIFDFITVIGSITEIILTDSKLVNTSGFNMSFLKLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIKLDEESHINRHNNFRSFFGSLMLLFRSATGEAWQEIMLSCLGEKGCEPDTTAPSGQNENERCGTDLAYVYFVSFIFFCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEFVRVWAEYDRAACGRIHYTEMYEMLTLMSPPLGLGKRCPSKVAYKRLVLMNMPVAEDMTVHFTSTLMALIRTALDIKIAKGGADRQQLDSELQKETLAIWPHLSQKMLDLLVPMPKASDLTVGKIYAAMMIMDYYKQSKVKKQRQQLEEQKNAPMFQRMEPSSLPQEIIANAKALPYLQQDPVSGLSGRSGYPSMSPLSPQDIFQLACMDPADDGQFQERQSLEPEVSELKSVQPSNHGIYLPSDTQEHAGSGRASSMPRLTVDPQVVTDPSSMRRSFSTIRDKRSNSSWLEEFSMERSSENTYKSRRRSYHSSLRLSAHRLNSDSGHKSDTHRSGGRERGRSKERKHLLSPDVSRCNSEERGTQADWESPERRQSRSPSEGRSQTPNRQGTGSLSESSIPSVSDTSTPRRSRRQLPPVPPKPRPLLSYSSLIRHAGSISPPADGSEEGSPLTSQALESNNACLTESSNSPHPQQSQHASPQRYISEPYLALHEDSHASDCGEEETLTFEAAVATSLGRSNTIGSAPPLRHSWQMPNGHYRRRRRGGPGPGMMCGAVNNLLSDTEEDDKC	Literature-reported	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800008159)"	2	TC=1.A.1	Calcium channel	calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1E subfamily. 	.	.	"Voltage gated calcium channel IQ domain; Voltage-dependent L-type calcium channel, IQ-associated; Ion transport protein"	PF08763; PF16905; PF00520	PF08763; Ca_chan_IQ; PF16905; GPHH; PF00520; Ion_trans	.	.	hsa04010:MAPK signaling pathway; hsa04020:Calcium signaling pathway; hsa04930:Type II diabetes mellitus	R-HSA-112308: Presynaptic depolarization and calcium channel opening; R-HSA-422356: Regulation of insulin secretion	.	Q15878
TTJ0SO4	Voltage-gated calcium channel alpha Cav1.4 (CACNA1F)	O60840	CAC1F_HUMAN	Voltage-gated ion channel	Voltage-gated calcium channel subunit alpha Cav1.4; Voltage-dependent L-type calcium channel subunit alpha-1F; CACNAF1	CACNA1F	"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."	.	.	MSESEGGKDTTPEPSPANGAGPGPEWGLCPGPPAVEGESSGASGLGTPKRRNQHSKHKTVAVASAQRSPRALFCLTLANPLRRSCISIVEWKPFDILILLTIFANCVALGVYIPFPEDDSNTANHNLEQVEYVFLVIFTVETVLKIVAYGLVLHPSAYIRNGWNLLDFIIVVVGLFSVLLEQGPGRPGDAPHTGGKPGGFDVKALRAFRVLRPLRLVSGVPSLHIVLNSIMKALVPLLHIALLVLFVIIIYAIIGLELFLGRMHKTCYFLGSDMEAEEDPSPCASSGSGRACTLNQTECRGRWPGPNGGITNFDNFFFAMLTVFQCVTMEGWTDVLYWMQDAMGYELPWVYFVSLVIFGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKQREKQQMEEDLRGYLDWITQAEELDMEDPSADDNLGSMAEEGRAGHRPQLAELTNRRRGRLRWFSHSTRSTHSTSSHASLPASDTGSMTETQGDEDEEEGALASCTRCLNKIMKTRVCRRLRRANRVLRARCRRAVKSNACYWAVLLLVFLNTLTIASEHHGQPVWLTQIQEYANKVLLCLFTVEMLLKLYGLGPSAYVSSFFNRFDCFVVCGGILETTLVEVGAMQPLGISVLRCVRLLRIFKVTRHWASLSNLVASLLNSMKSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDQTHTKRSTFDTFPQALLTVFQILTGEDWNVVMYDGIMAYGGPFFPGMLVCIYFIILFICGNYILLNVFLAIAVDNLASGDAGTAKDKGGEKSNEKDLPQENEGLVPGVEKEEEEGARREGADMEEEEEEEEEEEEEEEEEGAGGVELLQEVVPKEKVVPIPEGSAFFCLSQTNPLRKGCHTLIHHHVFTNLILVFIILSSVSLAAEDPIRAHSFRNHILGYFDYAFTSIFTVEILLKMTVFGAFLHRGSFCRSWFNMLDLLVVSVSLISFGIHSSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIMIVTTLLQFMFACIGVQLFKGKFYTCTDEAKHTPQECKGSFLVYPDGDVSRPLVRERLWVNSDFNFDNVLSAMMALFTVSTFEGWPALLYKAIDAYAEDHGPIYNYRVEISVFFIVYIIIIAFFMMNIFVGFVIITFRAQGEQEYQNCELDKNQRQCVEYALKAQPLRRYIPKNPHQYRVWATVNSAAFEYLMFLLILLNTVALAMQHYEQTAPFNYAMDILNMVFTGLFTIEMVLKIIAFKPKHYFTDAWNTFDALIVVGSIVDIAVTEVNNGGHLGESSEDSSRISITFFRLFRVMRLVKLLSKGEGIRTLLWTFIKSFQALPYVALLIAMIFFIYAVIGMQMFGKVALQDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEIMLASLPGNRCDPESDFGPGEEFTCGSNFAIAYFISFFMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWSEYDPGAKGRIKHLDVVALLRRIQPPLGFGKLCPHRVACKRLVAMNMPLNSDGTVTFNATLFALVRTSLKIKTEGNLEQANQELRIVIKKIWKRMKQKLLDEVIPPPDEEEVTVGKFYATFLIQDYFRKFRRRKEKGLLGNDAAPSTSSALQAGLRSLQDLGPEMRQALTCDTEEEEEEGQEGVEEEDEKDLETNKATMVSQPSARRGSGISVSLPVGDRLPDSLSFGPSDDDRGTPTSSQPSVPQAGSNTHRRGSGALIFTIPEEGNSQPKGTKGQNKQDEDEEVPDRLSYLDEQAGTPPCSVLLPPHRAQRYMDGHLVPRRRLLPPTPAGRKPSFTIQCLQRQGSCEDLPIPGTYHRGRNSGPNRAQGSWATPPQRGRLLYAPLLLVEEGAAGEGYLGRSSGPLRTFTCLHVPGTHSDPSHGKRGSADSLVEAVLISEGLGLFARDPRFVALAKQEIADACRLTLDEMDNAASDLLAQGTSSLYSDEESILSRFDEEDLGDEMACVHAL	Literature-reported	Functional characterization of the L-type Ca2+ channel Cav1.4alpha1 from mouse retina. Invest Ophthalmol Vis Sci. 2004 Feb;45(2):708-13.	0	.	.	.	.	.	.	.	.	.	.	"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; hsa04723: Retrograde endocannabinoid signaling; hsa04725: Cholinergic synapse; hsa04726: Serotonergic synapse; hsa04727: GABAergic synapse; hsa04911: Insulin secretion; hsa04912: GnRH signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04924: Renin secretion; hsa04925: Aldosterone synthesis and secretion; hsa04927: Cortisol synthesis and secretion; hsa04929: GnRH secretion; hsa04934: Cushing syndrome; hsa04935: Growth hormone synthesis, secretion and action; hsa05010: Alzheimer disease; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05207: Chemical carcinogenesis - receptor activation; hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy"	.	.	O60840
TT729IR	Voltage-gated calcium channel alpha Cav3.1 (CACNA1G)	O43497	CAC1G_HUMAN	Voltage-gated ion channel	Voltage-gated calcium channel alpha subunit Cav3.1; Voltage-dependent T-type calcium channel; NBR13; Cav3.1c; CACNA1G	CACNA1G	"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."	.	.	MDEEEDGAGAEESGQPRSFMRLNDLSGAGGRPGPGSAEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERISMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLERYYQTENEDESPFICSQPRENGMRSCRSVPTLRGDGGGGPPCGLDYEAYNSSSNTTCVNWNQYYTNCSAGEHNPFKGAINFDNIGYAWIAIFQVITLEGWVDIMYFVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRVRFLSNASTLASFSEPGSCYEELLKYLVYILRKAARRLAQVSRAAGVRVGLLSSPAPLGGQETQPSSSCSRSHRRLSVHHLVHHHHHHHHHYHLGNGTLRAPRASPEIQDRDANGSRRLMLPPPSTPALSGAPPGGAESVHSFYHADCHLEPVRCQAPPPRSPSEASGRTVGSGKVYPTVHTSPPPETLKEKALVEVAASSGPPTLTSLNIPPGPYSSMHKLLETQSTGACQSSCKISSPCLKADSGACGPDSCPYCARAGAGEVELADREMPDSDSEAVYEFTQDAQHSDLRDPHSRRQRSLGPDAEPSSVLAFWRLICDTFRKIVDSKYFGRGIMIAILVNTLSMGIEYHEQPEELTNALEISNIVFTSLFALEMLLKLLVYGPFGYIKNPYNIFDGVIVVISVWEIVGQQGGGLSVLRTFRLMRVLKLVRFLPALQRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHLFGCKFASERDGDTLPDRKNFDSLLWAIVTVFQILTQEDWNKVLYNGMASTSSWAALYFIALMTFGNYVLFNLLVAILVEGFQAEEISKREDASGQLSCIQLPVDSQGGDANKSESEPDFFSPSLDGDGDRKKCLALVSLGEHPELRKSLLPPLIIHTAATPMSLPKSTSTGLGEALGPASRRTSSSGSAEPGAAHEMKSPPSARSSPHSPWSAASSWTSRRSSRNSLGRAPSLKRRSPSGERRSLLSGEGQESQDEEESSEEERASPAGSDHRHRGSLEREAKSSFDLPDTLQVPGLHRTASGRGSASEHQDCNGKSASGRLARALRPDDPPLDGDDADDEGNLSKGERVRAWIRARLPACCLERDSWSAYIFPPQSRFRLLCHRIITHKMFDHVVLVIIFLNCITIAMERPKIDPHSAERIFLTLSNYIFTAVFLAEMTVKVVALGWCFGEQAYLRSSWNVLDGLLVLISVIDILVSMVSDSGTKILGMLRVLRLLRTLRPLRVISRAQGLKLVVETLMSSLKPIGNIVVICCAFFIIFGILGVQLFKGKFFVCQGEDTRNITNKSDCAEASYRWVRHKYNFDNLGQALMSLFVLASKDGWVDIMYDGLDAVGVDQQPIMNHNPWMLLYFISFLLIVAFFVLNMFVGVVVENFHKCRQHQEEEEARRREEKRLRRLEKKRRNLMLDDVIASGSSASAASEAQCKPYYSDYSRFRLLVHHLCTSHYLDLFITGVIGLNVVTMAMEHYQQPQILDEALKICNYIFTVIFVLESVFKLVAFGFRRFFQDRWNQLDLAIVLLSIMGITLEEIEVNASLPINPTIIRIMRVLRIARVLKLLKMAVGMRALLDTVMQALPQVGNLGLLFMLLFFIFAALGVELFGDLECDETHPCEGLGRHATFRNFGMAFLTLFRVSTGDNWNGIMKDTLRDCDQESTCYNTVISPIYFVSFVLTAQFVLVNVVIAVLMKHLEESNKEAKEEAELEAELELEMKTLSPQPHSPLGSPFLWPGVEGPDSPDSPKPGALHPAAHARSASHFSLEHPTDRQLFDTISLLIQGSLEWELKLMDELAGPGGQPSAFPSAPSLGGSDPQIPLAEMEALSLTSEIVSEPSCSLALTDDSLPDDMHTLLLSALESNMQPHPTELPGPDLLTVRKSGVSRTHSLPNDSYMCRHGSTAEGPLGHRGWGLPKAQSGSVLSVHSQPADTSYILQLPKDAPHLLQPHSAPTWGTIPKLPPPGRSPLAQRPLRRQAAIRTDSLDVQGLGSREDLLAEVSGPSPPLARAYSFWGQSSTQAQQHSRSHSKISKHMTPPAPCPGPEPNWGKGPPETRSSLELDTELSWISGDLLPPGGQEEPPSPRDLKKCYSVEAQSCQRRPTSWLDEQRRHSIAVSCLDSGSQPHLGTDPSNLGGQPLGGPGSRPKKKLSPPSITIDPPESQGPRTPPSPGICLRRRAPSSDSKDPLASGPPDSMAASPSPKKDVLSLSGLSSDPADLDP	Successful	Mechanism of tissue-selective drug action in the cardiovascular system. Mol Interv. 2005 Apr;5(2):84-93.	34	.	.	.	.	.	.	.	.	.	.	hsa04010:MAPK signaling pathway; hsa04020:Calcium signaling pathway; hsa04713:Circadian entrainment; hsa04930:Type II diabetes mellitus	R-HSA-419037:NCAM1 interactions	.	O43497
TTZPWGN	Voltage-gated calcium channel alpha Cav3.2 (CACNA1H)	O95180	CAC1H_HUMAN	Voltage-gated ion channel	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	CACNA1H	"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."	.	.	MTEGARAADEVRVPLGAPPPGPAALVGASPESPGAPGREAERGSELGVSPSESPAAERGAELGADEEQRVPYPALAATVFFCLGQTTRPRSWCLRLVCNPWFEHVSMLVIMLNCVTLGMFRPCEDVECGSERCNILEAFDAFIFAFFAVEMVIKMVALGLFGQKCYLGDTWNRLDFFIVVAGMMEYSLDGHNVSLSAIRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLDSAFVRNNNLTFLRPYYQTEEGEENPFICSSRRDNGMQKCSHIPGRRELRMPCTLGWEAYTQPQAEGVGAARNACINWNQYYNVCRSGDSNPHNGAINFDNIGYAWIAIFQVITLEGWVDIMYYVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRARHLSNDSTLASFSEPGSCYEELLKYVGHIFRKVKRRSLRLYARWQSRWRKKVDPSAVQGQGPGHRQRRAGRHTASVHHLVYHHHHHHHHHYHFSHGSPRRPGPEPGACDTRLVRAGAPPSPPSPGRGPPDAESVHSIYHADCHIEGPQERARVAHAAATAAASLRLATGLGTMNYPTILPSGVGSGKGSTSPGPKGKWAGGPPGTGGHGPLSLNSPDPYEKIPHVVGEHGLGQAPGHLSGLSVPCPLPSPPAGTLTCELKSCPYCTRALEDPEGELSGSESGDSDGRGVYEFTQDVRHGDRWDPTRPPRATDTPGPGPGSPQRRAQQRAAPGEPGWMGRLWVTFSGKLRRIVDSKYFSRGIMMAILVNTLSMGVEYHEQPEELTNALEISNIVFTSMFALEMLLKLLACGPLGYIRNPYNIFDGIIVVISVWEIVGQADGGLSVLRTFRLLRVLKLVRFLPALRRQLVVLVKTMDNVATFCTLLMLFIFIFSILGMHLFGCKFSLKTDTGDTVPDRKNFDSLLWAIVTVFQILTQEDWNVVLYNGMASTSSWAALYFVALMTFGNYVLFNLLVAILVEGFQAEGDANRSDTDEDKTSVHFEEDFHKLRELQTTELKMCSLAVTPNGHLEGRGSLSPPLIMCTAATPMPTPKSSPFLDAAPSLPDSRRGSSSSGDPPLGDQKPPASLRSSPCAPWGPSGAWSSRRSSWSSLGRAPSLKRRGQCGERESLLSGEGKGSTDDEAEDGRAAPGPRATPLRRAESLDPRPLRPAALPPTKCRDRDGQVVALPSDFFLRIDSHREDAAELDDDSEDSCCLRLHKVLEPYKPQWCRSREAWALYLFSPQNRFRVSCQKVITHKMFDHVVLVFIFLNCVTIALERPDIDPGSTERVFLSVSNYIFTAIFVAEMMVKVVALGLLSGEHAYLQSSWNLLDGLLVLVSLVDIVVAMASAGGAKILGVLRVLRLLRTLRPLRVISRAPGLKLVVETLISSLRPIGNIVLICCAFFIIFGILGVQLFKGKFYYCEGPDTRNISTKAQCRAAHYRWVRRKYNFDNLGQALMSLFVLSSKDGWVNIMYDGLDAVGVDQQPVQNHNPWMLLYFISFLLIVSFFVLNMFVGVVVENFHKCRQHQEAEEARRREEKRLRRLERRRRSTFPSPEAQRRPYYADYSPTRRSIHSLCTSHYLDLFITFIICVNVITMSMEHYNQPKSLDEALKYCNYVFTIVFVFEAALKLVAFGFRRFFKDRWNQLDLAIVLLSLMGITLEEIEMSAALPINPTIIRIMRVLRIARVLKLLKMATGMRALLDTVVQALPQVGNLGLLFMLLFFIYAALGVELFGRLECSEDNPCEGLSRHATFSNFGMAFLTLFRVSTGDNWNGIMKDTLRECSREDKHCLSYLPALSPVYFVTFVLVAQFVLVNVVVAVLMKHLEESNKEAREDAELDAEIELEMAQGPGSARRVDADRPPLPQESPGARDAPNLVARKVSVSRMLSLPNDSYMFRPVVPASAPHPRPLQEVEMETYGAGTPLGSVASVHSPPAESCASLQIPLAVSSPARSGEPLHALSPRGTARSPSLSRLLCRQEAVHTDSLEGKIDSPRDTLDPAEPGEKTPVRPVTQGGSLQSPPRSPRPASVRTRKHTFGQRCVSSRPAAPGGEEAEASDPADEEVSHITSSACPWQPTAEPHGPEASPVAGGERDLRRLYSVDAQGFLDKPGRADEQWRPSAELGSGEPGEAKAWGPEAEPALGARRKKKMSPPCISVEPPAEDEGSARPSAAEGGSTTLRRRTPSCEATPHRDSLEPTEGSGAGGDPAAKGERWGQASCRAEHLTVPSFAFEPLDLGVPSGDPFLDGSHSVTPESRASSSGAIVPLEPPESEPPMPVGDPPEKRRGLYLTVPQCPLEKPGSPSATPAPGGGADDPV	Successful	Acute renal failure. Clin Evid (Online). 2008 Sep 3;2008. pii: 2001.	34	.	.	.	.	.	.	.	.	.	.	hsa04010:MAPK signaling pathway; hsa04020:Calcium signaling pathway; hsa04713:Circadian entrainment	R-HSA-419037:NCAM1 interactions	.	O95180
TTQZFTH	Voltage-gated calcium channel alpha Cav3.3 (CACNA1I)	Q9P0X4	CAC1I_HUMAN	Voltage-gated ion channel	Voltage-gated calcium channel subunit alpha Cav3.3; Voltage-dependent T-type calcium channel subunit alpha-1I; KIAA1120; Ca(v)3.3	CACNA1I	"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)."	.	.	MAESASPPSSSAAAPAAEPGVTTEQPGPRSPPSSPPGLEEPLDGADPHVPHPDLAPIAFFCLRQTTSPRNWCIKMVCNPWFECVSMLVILLNCVTLGMYQPCDDMDCLSDRCKILQVFDDFIFIFFAMEMVLKMVALGIFGKKCYLGDTWNRLDFFIVMAGMVEYSLDLQNINLSAIRTVRVLRPLKAINRVPSMRILVNLLLDTLPMLGNVLLLCFFVFFIFGIIGVQLWAGLLRNRCFLEENFTIQGDVALPPYYQPEEDDEMPFICSLSGDNGIMGCHEIPPLKEQGRECCLSKDDVYDFGAGRQDLNASGLCVNWNRYYNVCRTGSANPHKGAINFDNIGYAWIVIFQVITLEGWVEIMYYVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQREHRLMLEQRQRYLSSSTVASYAEPGDCYEEIFQYVCHILRKAKRRALGLYQALQSRRQALGPEAPAPAKPGPHAKEPRHYHGKTKGQGDEGRHLGSRHCQTLHGPASPGNDHSGRELCPQHSPLDATPHTLVQPIPATLASDPASCPCCQHEDGRRPSGLGSTDSGQEGSGSGSSAGGEDEADGDGARSSEDGASSELGKEEEEEEQADGAVWLCGDVWRETRAKLRGIVDSKYFNRGIMMAILVNTVSMGIEHHEQPEELTNILEICNVVFTSMFALEMILKLAAFGLFDYLRNPYNIFDSIIVIISIWEIVGQADGGLSVLRTFRLLRVLKLVRFMPALRRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHIFGCKFSLRTDTGDTVPDRKNFDSLLWAIVTVFQILTQEDWNVVLYNGMASTSPWASLYFVALMTFGNYVLFNLLVAILVEGFQAEGDANRSYSDEDQSSSNIEEFDKLQEGLDSSGDPKLCPIPMTPNGHLDPSLPLGGHLGPAGAAGPAPRLSLQPDPMLVALGSRKSSVMSLGRMSYDQRSLSSSRSSYYGPWGRSAAWASRRSSWNSLKHKPPSAEHESLLSAERGGGARVCEVAADEGPPRAAPLHTPHAHHIHHGPHLAHRHRHHRRTLSLDNRDSVDLAELVPAVGAHPRAAWRAAGPAPGHEDCNGRMPSIAKDVFTKMGDRGDRGEDEEEIDYTLCFRVRKMIDVYKPDWCEVREDWSVYLFSPENRFRVLCQTIIAHKLFDYVVLAFIFLNCITIALERPQIEAGSTERIFLTVSNYIFTAIFVGEMTLKVVSLGLYFGEQAYLRSSWNVLDGFLVFVSIIDIVVSLASAGGAKILGVLRVLRLLRTLRPLRVISRAPGLKLVVETLISSLKPIGNIVLICCAFFIIFGILGVQLFKGKFYHCLGVDTRNITNRSDCMAANYRWVHHKYNFDNLGQALMSLFVLASKDGWVNIMYNGLDAVAVDQQPVTNHNPWMLLYFISFLLIVSFFVLNMFVGVVVENFHKCRQHQEAEEARRREEKRLRRLEKKRRKAQRLPYYATYCHTRLLIHSMCTSHYLDIFITFIICLNVVTMSLEHYNQPTSLETALKYCNYMFTTVFVLEAVLKLVAFGLRRFFKDRWNQLDLAIVLLSVMGITLEEIEINAALPINPTIIRIMRVLRIARVLKLLKMATGMRALLDTVVQALPQVGNLGLLFMLLFFIYAALGVELFGKLVCNDENPCEGMSRHATFENFGMAFLTLFQVSTGDNWNGIMKDTLRDCTHDERSCLSSLQFVSPLYFVSFVLTAQFVLINVVVAVLMKHLDDSNKEAQEDAEMDAELELEMAHGLGPGPRLPTGSPGAPGRGPGGAGGGGDTEGGLCRRCYSPAQENLWLDSVSLIIKDSLEGELTIIDNLSGSIFHHYSSPAGCKKCHHDKQEVQLAETEAFSLNSDRSSSILLGDDLSLEDPTACPPGRKDSKGELDPPEPMRVGDLGECFFPLSSTAVSPDPENFLCEMEEIPFNPVRSWLKHDSSQAPPSPFSPDASSPLLPMPAEFFHPAVSASQKGPEKGTGTGTLPKIALQGSWASLRSPRVNCTLLRQATGSDTSLDASPSSSAGSLQTTLEDSLTLSDSPRRALGPPAPAPGPRAGLSPAARRRLSLRGRGLFSLRGLRAHQRSHSSGGSTSPGCTHHDSMDPSDEEGRGGAGGGGAGSEHSETLSSLSLTSLFCPPPPPPAPGLTPARKFSSTSSLAAPGRPHAAALAHGLARSPSWAADRSKDPPGRAPLPMGLGPLAPPPQPLPGELEPGDAASKRKR	Literature-reported	"Discovery of (2S)-1-(4-amino-2,3,5- trimethylphenoxy)-3-[4-[4-(4- fluorobenzyl)phenyl]-1-piperazinyl]-2-propanol dimethanesulfonate (SUN N8075): a ... J Med Chem. 2000 Sep 7;43(18):3372-6."	2	.	.	.	.	.	.	.	.	.	.	rno04010:MAPK signaling pathway; rno04020:Calcium signaling pathway; rno04713:Circadian entrainment	R-HSA-419037: NCAM1 interactions	.	Q9P0X4
TT94HRF	Voltage-gated calcium channel alpha Cav1.1 (CACNA1S)	Q13698	CAC1S_HUMAN	Voltage-gated ion channel	"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"	CACNA1S	"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."	.	6B27; 2VAY	MEPSSPQDEGLRKKQPKKPVPEILPRPPRALFCLTLENPLRKACISIVEWKPFETIILLTIFANCVALAVYLPMPEDDNNSLNLGLEKLEYFFLIVFSIEAAMKIIAYGFLFHQDAYLRSGWNVLDFTIVFLGVFTVILEQVNVIQSHTAPMSSKGAGLDVKALRAFRVLRPLRLVSGVPSLQVVLNSIFKAMLPLFHIALLVLFMVIIYAIIGLELFKGKMHKTCYFIGTDIVATVENEEPSPCARTGSGRRCTINGSECRGGWPGPNHGITHFDNFGFSMLTVYQCITMEGWTDVLYWVNDAIGNEWPWIYFVTLILLGSFFILNLVLGVLSGEFTKEREKAKSRGTFQKLREKQQLDEDLRGYMSWITQGEVMDVEDFREGKLSLDEGGSDTESLYEIAGLNKIIQFIRHWRQWNRIFRWKCHDIVKSKVFYWLVILIVALNTLSIASEHHNQPLWLTRLQDIANRVLLSLFTTEMLMKMYGLGLRQYFMSIFNRFDCFVVCSGILEILLVESGAMTPLGISVLRCIRLLRIFKITKYWTSLSNLVASLLNSIRSIASLLLLLFLFIVIFALLGMQLFGGRYDFEDTEVRRSNFDNFPQALISVFQVLTGEDWTSMMYNGIMAYGGPSYPGMLVCIYFIILFVCGNYILLNVFLAIAVDNLAEAESLTSAQKAKAEEKKRRKMSKGLPDKSEEEKSTMAKKLEQKPKGEGIPTTAKLKIDEFESNVNEVKDPYPSADFPGDDEEDEPEIPLSPRPRPLAELQLKEKAVPIPEASSFFIFSPTNKIRVLCHRIVNATWFTNFILLFILLSSAALAAEDPIRADSMRNQILKHFDIGFTSVFTVEIVLKMTTYGAFLHKGSFCRNYFNMLDLLVVAVSLISMGLESSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCMFVAISTIGNIVLVTTLLQFMFACIGVQLFKGKFFRCTDLSKMTEEECRGYYYVYKDGDPMQIELRHREWVHSDFHFDNVLSAMMSLFTVSTFEGWPQLLYKAIDSNAEDVGPIYNNRVEMAIFFIIYIILIAFFMMNIFVGFVIVTFQEQGETEYKNCELDKNQRQCVQYALKARPLRCYIPKNPYQYQVWYIVTSSYFEYLMFALIMLNTICLGMQHYNQSEQMNHISDILNVAFTIIFTLEMILKLMAFKARGYFGDPWNVFDFLIVIGSIIDVILSEIDTFLASSGGLYCLGGGCGNVDPDESARISSAFFRLFRVMRLIKLLSRAEGVRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQMFGKIALVDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEILLACSYGKLCDPESDYAPGEEYTCGTNFAYYYFISFYMLCAFLVINLFVAVIMDNFDYLTRDWSILGPHHLDEFKAIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKFCPHRVACKRLVGMNMPLNSDGTVTFNATLFALVRTALKIKTEGNFEQANEELRAIIKKIWKRTSMKLLDQVIPPIGDDEVTVGKFYATFLIQEHFRKFMKRQEEYYGYRPKKDIVQIQAGLRTIEEEAAPEICRTVSGDLAAEEELERAMVEAAMEEGIFRRTGGLFGQVDNFLERTNSLPPVMANQRPLQFAEIEMEEMESPVFLEDFPQDPRTNPLARANTNNANANVAYGNSNHSNSHVFSSVHYEREFPEETETPATRGRALGQPCRVLGPHSKPCVEMLKGLLTQRAMPRGQAPPAPCQCPRVESSMPEDRKSSTPGSLHEETPHSRSTRENTSRCSAPATALLIQKALVRGGLGTLAADANFIMATGQALADACQMEPEEVEIMATELLKGREAPEGMASSLGCLNLGSSLGSLDQHQGSQETLIPPRL	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 528).	0	.	.	.	.	.	.	.	.	.	.	"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; hsa04723: Retrograde endocannabinoid signaling; hsa04725: Cholinergic synapse; hsa04726: Serotonergic synapse; hsa04727: GABAergic synapse; hsa04911: Insulin secretion; hsa04912: GnRH signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04924: Renin secretion; hsa04925: Aldosterone synthesis and secretion; hsa04927: Cortisol synthesis and secretion; hsa04929: GnRH secretion; hsa04934: Cushing syndrome; hsa04935: Growth hormone synthesis, secretion and action; hsa05010: Alzheimer disease; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05207: Chemical carcinogenesis - receptor activation; hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy"	R-HSA-419037: NCAM1 interactions	.	Q13698
TTFK1JQ	Voltage-gated calcium channel alpha-2/delta-1 (CACNA2D1)	P54289	CA2D1_HUMAN	Voltage-gated ion channel	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	CACNA2D1	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.	.	.	MAAGCLLALTLTLFQSLLIGPSSEEPFPSAVTIKSWVDKMQEDLVTLAKTASGVNQLVDIYEKYQDLYTVEPNNARQLVEIAARDIEKLLSNRSKALVRLALEAEKVQAAHQWREDFASNEVVYYNAKDDLDPEKNDSEPGSQRIKPVFIEDANFGRQISYQHAAVHIPTDIYEGSTIVLNELNWTSALDEVFKKNREEDPSLLWQVFGSATGLARYYPASPWVDNSRTPNKIDLYDVRRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVSCFQHLVQANVRNKKVLKDAVNNITAKGITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDGGEERAQEIFNKYNKDKKVRVFTFSVGQHNYDRGPIQWMACENKGYYYEIPSIGAIRINTQEYLDVLGRPMVLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNITGQFENKTNLKNQLILGVMGVDVSLEDIKRLTPRFTLCPNGYYFAIDPNGYVLLHPNLQPKPIGVGIPTINLRKRRPNIQNPKSQEPVTLDFLDAELENDIKVEIRNKMIDGESGEKTFRTLVKSQDERYIDKGNRTYTWTPVNGTDYSLALVLPTYSFYYIKAKLEETITQARYSETLKPDNFEESGYTFIAPRDYCNDLKISDNNTEFLLNFNEFIDRKTPNNPSCNADLINRVLLDAGFTNELVQNYWSKQKNIKGVKARFVVTDGGITRVYPKEAGENWQENPETYEDSFYKRSLDNDNYVFTAPYFNKSGPGAYESGIMVSKAVEIYIQGKLLKPAVVGIKIDVNSWIENFTKTSIRDPCAGPVCDCKRNSDVMDCVILDDGGFLLMANHDDYTNQIGRFFGEIDPSLMRHLVNISVYAFNKSYDYQSVCEPGAAPKQGAGHRSAYVPSVADILQIGWWATAAAWSILQQFLLSLTFPRLLEAVEMEDDDFTASLSKQSCITEQTQYFFDNDSKSFSGVLDCGNCSRIFHGEKLMNTNLIFIMVESKGTCPCDTRLLIQAEQTSDGPNPCDMVKQPRYRKGPDVCFDNNVLEDYTDCGGVSGLNPSLWYIIGIQFLLLWLVSGSTHRLL	Successful	A first drug combination for the treatment of arterial hypertension with a calcium channel antagonist (amlodipine besylate) and an angiotensin receptor blocker (valsartan): Exforge. Rev Med Liege. 2007 Nov;62(11):688-94.	34	.	.	.	.	.	.	.	.	.	.	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	.	.	P54289
TTU8P3M	Voltage-gated calcium channel alpha-2/delta-2 (CACNA2D2)	Q9NY47	CA2D2_HUMAN	Voltage-gated ion channel	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	CACNA2D2	"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."	.	.	MAVPARTCGASRPGPARTARPWPGCGPHPGPGTRRPTSGPPRPLWLLLPLLPLLAAPGASAYSFPQQHTMQHWARRLEQEVDGVMRIFGGVQQLREIYKDNRNLFEVQENEPQKLVEKVAGDIESLLDRKVQALKRLADAAENFQKAHRWQDNIKEEDIVYYDAKADAELDDPESEDVERGSKASTLRLDFIEDPNFKNKVNYSYAAVQIPTDIYKGSTVILNELNWTEALENVFMENRRQDPTLLWQVFGSATGVTRYYPATPWRAPKKIDLYDVRRRPWYIQGASSPKDMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQPVSCFTHLVQANVRNKKVFKEAVQGMVAKGTTGYKAGFEYAFDQLQNSNITRANCNKMIMMFTDGGEDRVQDVFEKYNWPNRTVRVFTFSVGQHNYDVTPLQWMACANKGYYFEIPSIGAIRINTQEYLDVLGRPMVLAGKEAKQVQWTNVYEDALGLGLVVTGTLPVFNLTQDGPGEKKNQLILGVMGIDVALNDIKRLTPNYTLGANGYVFAIDLNGYVLLHPNLKPQTTNFREPVTLDFLDAELEDENKEEIRRSMIDGNKGHKQIRTLVKSLDERYIDEVTRNYTWVPIRSTNYSLGLVLPPYSTFYLQANLSDQILQVKLPISKLKDFEFLLPSSFESEGHVFIAPREYCKDLNASDNNTEFLKNFIELMEKVTPDSKQCNNFLLHNLILDTGITQQLVERVWRDQDLNTYSLLAVFAATDGGITRVFPNKAAEDWTENPEPFNASFYRRSLDNHGYVFKPPHQDALLRPLELENDTVGILVSTAVELSLGRRTLRPAVVGVKLDLEAWAEKFKVLASNRTHQDQPQKCGPNSHCEMDCEVNNEDLLCVLIDDGGFLVLSNQNHQWDQVGRFFSEVDANLMLALYNNSFYTRKESYDYQAACAPQPPGNLGAAPRGVFVPTVADFLNLAWWTSAAAWSLFQQLLYGLIYHSWFQADPAEAEGSPETRESSCVMKQTQYYFGSVNASYNAIIDCGNCSRLFHAQRLTNTNLLFVVAEKPLCSQCEAGRLLQKETHSDGPEQCELVQRPRYRRGPHICFDYNATEDTSDCGRGASFPPSLGVLVSLQLLLLLGLPPRPQPQVLVHASRRL	Literature-reported	"Enantioselective synthesis of PD144723: a potent stereospecific anticonvulsant, Bioorg. Med. Chem. Lett. 4(6):823-826 (1994)."	0	.	.	.	.	.	.	.	.	.	.	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	"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"	.	Q9NY47
TTN7T29	Voltage-gated calcium channel alpha-2/delta-3 (CACNA2D3)	Q8IZS8	CA2D3_HUMAN	Voltage-gated ion channel	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	CACNA2D3	"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)."	.	.	MAGPGSPRRASRGASALLAAALLYAALGDVVRSEQQIPLSVVKLWASAFGGEIKSIAAKYSGSQLLQKKYKEYEKDVAIEEIDGLQLVKKLAKNMEEMFHKKSEAVRRLVEAAEEAHLKHEFDADLQYEYFNAVLINERDKDGNFLELGKEFILAPNDHFNNLPVNISLSDVQVPTNMYNKDPAIVNGVYWSESLNKVFVDNFDRDPSLIWQYFGSAKGFFRQYPGIKWEPDENGVIAFDCRNRKWYIQAATSPKDVVILVDVSGSMKGLRLTIAKQTVSSILDTLGDDDFFNIIAYNEELHYVEPCLNGTLVQADRTNKEHFREHLDKLFAKGIGMLDIALNEAFNILSDFNHTGQGSICSQAIMLITDGAVDTYDTIFAKYNWPDRKVRIFTYLIGREAAFADNLKWMACANKGFFTQISTLADVQENVMEYLHVLSRPKVIDQEHDVVWTEAYIDSTLPQAQKLTDDQGPVLMTTVAMPVFSKQNETRSKGILLGVVGTDVPVKELLKTIPKYKLGIHGYAFAITNNGYILTHPELRLLYEEGKKRRKPNYSSVDLSEVEWEDRDDVLRNAMVNRKTGKFSMEVKKTVDKGKRVLVMTNDYYYTDIKGTPFSLGVALSRGHGKYFFRGNVTIEEGLHDLEHPDVSLADEWSYCNTDLHPEHRHLSQLEAIKLYLKGKEPLLQCDKELIQEVLFDAVVSAPIEAYWTSLALNKSENSDKGVEVAFLGTRTGLSRINLFVGAEQLTNQDFLKAGDKENIFNADHFPLWYRRAAEQIPGSFVYSIPFSTGPVNKSNVVTASTSIQLLDERKSPVVAAVGIQMKLEFFQRKFWTASRQCASLDGKCSISCDDETVNCYLIDNNGFILVSEDYTQTGDFFGEIEGAVMNKLLTMGSFKRITLYDYQAMCRANKESSDGAHGLLDPYNAFLSAVKWIMTELVLFLVEFNLCSWWHSDMTAKAQKLKQTLEPCDTEYPAFVSERTIKETTGNIACEDCSKSFVIQQIPSSNLFMVVVDSSCLCESVAPITMAPIEIRYNESLKCERLKAQKIRRRPESCHGFHPEENARECGGAPSLQAQTVLLLLPLLLMLFSR	Literature-reported	"Enantioselective synthesis of PD144723: a potent stereospecific anticonvulsant, Bioorg. Med. Chem. Lett. 4(6):823-826 (1994)."	0	.	.	.	.	.	.	.	.	.	.	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	R-HSA-112308:Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels	.	Q8IZS8
TT2YT1K	Aspartate carbamoyltransferase (CAD)	P27708	PYR1_HUMAN	Carbon-nitrogen ligase	CAD	CAD	"This protein is a ""fusion"" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase)."	.	6HG1; 6HFU; 6HFS; 6HFR; 6HFQ	MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEMDEFGLCKWFESSGIHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLPFLDPNARPLVPEVSIKTPRVFNTGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEATAGNPGGQTVRERLTERLCPPGIPTPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHTSQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILEQLAEKNFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQLPPSAPATSEMTTTPERPRRGIPGLPDGRFHLPPRIHRASDPGLPAEEPKEKSSRKVAEPELMGTPDGTCYPPPPVPRQASPQNLGTPGLLHPQTSPLLHSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	"hsa00240:Pyrimidine metabolism; hsa00250:Alanine, aspartate and glutamate metabolism; hsa01100:Metabolic pathways"	R-HSA-500753:Pyrimidine biosynthesis	MetaCyc:ENSG00000084774-MON	P27708
TTVSFJW	Calcitonin gene-related peptide 1 (CALCA)	P06881	CALCA_HUMAN	Cytotoxic amylin family	Calcitonin gene-related peptide I; CGRP-I; CALCA; CALC1; Alpha-type CGRP	CALCA	"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."	.	6E3Y; 1LS7	MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSRIIAQKRACDTATCVTHRLAGLLSRSGGVVKNNFVPTNVGSKAFGRRRRDLQA	Clinical trial	Emerging drugs in neuropathic pain. Expert Opin Emerg Drugs. 2007 Mar;12(1):113-26.	21	.	.	.	.	.	.	.	.	.	.	.	R-HSA-418555:G alpha (s) signalling events; R-HSA-419812:Calcitonin-like ligand receptors	.	P06881
TTUZ9GV	Calcitonin gene-related peptide 2 (CALCB)	P10092	CALCB_HUMAN	.	Calcitonin gene-related peptide II; CGRP-II; CALC2; Beta-type CGRP; Beta-CGRP	CALCB	"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."	.	.	MGFRKFSPFLALSILVLYQAGSLQAAPFRSALESSPDPATLSKEDARLLLAALVQDYVQMKASELKQEQETQGSSSAAQKRACNTATCVTHRLAGLLSRSGGMVKSNFVPTNVGSKAFGRRRRDLQA	Literature-reported	"CGRP receptors: a headache to study, but will antagonists prove therapeutic in migraine Trends Pharmacol Sci. 2002 Feb;23(2):51-3."	.	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04270: Vascular smooth muscle contraction	R-HSA-418555: G alpha (s) signalling events; R-HSA-419812: Calcitonin-like ligand receptors; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production	.	P10092
TTLWS2O	Calcitonin receptor (CALCR)	P30988	CALCR_HUMAN	GPCR secretin	CT-R	CALCR	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.	.	6NIY; 5UZ7; 5II0	MRFTFTSRCLALFLLLNHPTPILPAFSNQTYPTIEPKPFLYVVGRKKMMDAQYKCYDRMQQLPAYQGEGPYCNRTWDGWLCWDDTPAGVLSYQFCPDYFPDFDPSEKVTKYCDEKGVWFKHPENNRTWSNYTMCNAFTPEKLKNAYVLYYLAIVGHSLSIFTLVISLGIFVFFRSLGCQRVTLHKNMFLTYILNSMIIIIHLVEVVPNGELVRRDPVSCKILHFFHQYMMACNYFWMLCEGIYLHTLIVVAVFTEKQRLRWYYLLGWGFPLVPTTIHAITRAVYFNDNCWLSVETHLLYIIHGPVMAALVVNFFFLLNIVRVLVTKMRETHEAESHMYLKAVKATMILVPLLGIQFVVFPWRPSNKMLGKIYDYVMHSLIHFQGFFVATIYCFCNNEVQTTVKRQWAQFKIQWNQRWGRRPSNRSARAAAAAAEAGDIPIYICHQEPRNEPANNQGEESAEIIPLNIIEQESSA	Successful	Improved absorption of salmon calcitonin by ultraflexible liposomes through intranasal delivery. Peptides. 2009 Jul;30(7):1288-95.	34	PF00002	GPCR secretin	G-protein coupled receptor 2 family.	.	.	7 transmembrane receptor (Secretin family); Hormone receptor domain	PF00002; PF02793	PF00002; 7tm_2; PF02793; HRM	9.A.14.4.1	The G-protein-coupled receptor (GPCR) Family	hsa04080:Neuroactive ligand-receptor interaction; hsa04380:Osteoclast differentiation	R-HSA-418555:G alpha (s) signalling events; R-HSA-419812:Calcitonin-like ligand receptors	.	P30988
TTY6O0Q	Calcitonin gene-related peptide receptor (CGRPR)	Q16602	CALRL_HUMAN	GPCR secretin	Calcitonin receptor-like receptor; Calcitonin gene-related peptide type 1 receptor; CGRPR; CGRP type 1 receptor	CALCRL	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.	.	6E3Y; 6D1U; 5V6Y; 4RWG; 4RWF	MEKKCTLNFLVLLPFFMILVTAELEESPEDSIQLGVTRNKIMTAQYECYQKIMQDPIQQAEGVYCNRTWDGWLCWNDVAAGTESMQLCPDYFQDFDPSEKVTKICDQDGNWFRHPASNRTWTNYTQCNVNTHEKVKTALNLFYLTIIGHGLSIASLLISLGIFFYFKSLSCQRITLHKNLFFSFVCNSVVTIIHLTAVANNQALVATNPVSCKVSQFIHLYLMGCNYFWMLCEGIYLHTLIVVAVFAEKQHLMWYYFLGWGFPLIPACIHAIARSLYYNDNCWISSDTHLLYIIHGPICAALLVNLFFLLNIVRVLITKLKVTHQAESNLYMKAVRATLILVPLLGIEFVLIPWRPEGKIAEEVYDYIMHILMHFQGLLVSTIFCFFNGEVQAILRRNWNQYKIQFGNSFSNSEALRSASYTVSTISDGPGYSHDCPSEHLNGKSIHDIENVLLKPENLYN	Successful	"BMS-927711 for the acute treatment of migraine: a double-blind, randomized, placebo controlled, dose-ranging trial. Cephalalgia. 2014 Feb;34(2):114-25."	25	PF00002	GPCR secretin	G-protein coupled receptor 2 family.	.	.	7 transmembrane receptor (Secretin family); Hormone receptor domain	PF00002; PF02793	PF00002; 7tm_2; PF02793; HRM	9.A.14.4.12	The G-protein-coupled receptor (GPCR) Family	hsa04080:Neuroactive ligand-receptor interaction; hsa04270:Vascular smooth muscle contraction	R-HSA-418555:G alpha (s) signalling events; R-HSA-419812:Calcitonin-like ligand receptors	.	Q16602
TT67OLB	HUMAN calcitonin gene-related peptide type 1 receptor (CALCRL)	Q16602	CALRL_HUMAN	GPCR secretin	Calcitonin receptor-like receptor; Calcitonin gene-related peptide type 1 receptor; CGRPR; CGRP type 1 receptor	CALCRL	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.	.	6E3Y; 6D1U; 5V6Y; 4RWG; 4RWF	MEKKCTLNFLVLLPFFMILVTAELEESPEDSIQLGVTRNKIMTAQYECYQKIMQDPIQQAEGVYCNRTWDGWLCWNDVAAGTESMQLCPDYFQDFDPSEKVTKICDQDGNWFRHPASNRTWTNYTQCNVNTHEKVKTALNLFYLTIIGHGLSIASLLISLGIFFYFKSLSCQRITLHKNLFFSFVCNSVVTIIHLTAVANNQALVATNPVSCKVSQFIHLYLMGCNYFWMLCEGIYLHTLIVVAVFAEKQHLMWYYFLGWGFPLIPACIHAIARSLYYNDNCWISSDTHLLYIIHGPICAALLVNLFFLLNIVRVLITKLKVTHQAESNLYMKAVRATLILVPLLGIEFVLIPWRPEGKIAEEVYDYIMHILMHFQGLLVSTIFCFFNGEVQAILRRNWNQYKIQFGNSFSNSEALRSASYTVSTISDGPGYSHDCPSEHLNGKSIHDIENVLLKPENLYN	.	Safety and Efficacy Trial of Zavegepant* Intranasal for Hospitalized Patients With COVID-19 Requiring Supplemental Oxygen	.	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04270: Vascular smooth muscle contraction	R-HSA-418555: G alpha (s) signalling events; R-HSA-419812: Calcitonin-like ligand receptors; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production	.	Q16602
TTAT87F	Amylin receptor (IAPPR)	P30988-O60894/O60895/O60896	CALCR_HUMAN-RAMP1_HUMAN/RAMP2_HUMAN/RAMP3_HUMAN	.	Complex of Calcitonin receptor and Receptor activity-modifying protein	CALCR-RAMP1/RAMP2/RAMP3	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.	.	.	MRFTFTSRCLALFLLLNHPTPILPAFSNQTYPTIEPKPFLYVVGRKKMMDAQYKCYDRMQQLPAYQGEGPYCNRTWDGWLCWDDTPAGVLSYQFCPDYFPDFDPSEKVTKYCDEKGVWFKHPENNRTWSNYTMCNAFTPEKLKNAYVLYYLAIVGHSLSIFTLVISLGIFVFFRSLGCQRVTLHKNMFLTYILNSMIIIIHLVEVVPNGELVRRDPVSCKILHFFHQYMMACNYFWMLCEGIYLHTLIVVAVFTEKQRLRWYYLLGWGFPLVPTTIHAITRAVYFNDNCWLSVETHLLYIIHGPVMAALVVNFFFLLNIVRVLVTKMRETHEAESHMYLKAVKATMILVPLLGIQFVVFPWRPSNKMLGKIYDYVMHSLIHFQGFFVATIYCFCNNEVQTTVKRQWAQFKIQWNQRWGRRPSNRSARAAAAAAEAGDIPIYICHQEPRNEPANNQGEESAEIIPLNIIEQESSAMARALCRLPRRGLWLLLAHHLFMTTACQEANYGALLRELCLTQFQVDMEAVGETLWCDWGRTIRSYRELADCTWHMAEKLGCFWPNAEVDRFFLAVHGRYFRSCPISGRAVRDPPGSILYPFIVVPITVTLLVTALVVWQSKRTEGIV	Clinical trial	"Davalintide (AC2307), a novel amylin-mimetic peptide: enhanced pharmacological properties over native amylin to reduce food intake and body weight. Int J Obes (Lond). 2010 Feb;34(2):385-95."	5	.	.	.	.	.	.	.	.	.	.	hsa04270:Vascular smooth muscle contraction	.	.	P30988
TTV3NH6	Calmodulin (CALM)	P0DP23; P0DP24; P0DP25	CALM1_HUMAN; CALM2_HUMAN; CALM3_HUMAN	Calmodulin-dependent secretion	CaM; CALM2	CALM	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.	.	.	MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK	Successful	Inhibitory effect of jujuboside A on glutamate-mediated excitatory signal pathway in hippocampus. Planta Med. 2003 Aug;69(8):692-5.	34	.	.	.	.	.	.	.	.	.	.	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	"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"	.	P0DP23
TTUZ7OA	Calreticulin (CALR)	P27797	CALR_HUMAN	.	grp60; HACBP; Endoplasmic reticulum resident protein 60; ERp60; ERC; Calregulin; CRTC; CRP55	CALR	"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)."	.	6ENY; 5V90; 5LK5; 3POW; 3POS	MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL	Literature-reported	Identification of an endoplasmic reticulum-resident calcium-binding protein with multiple EF-hand motifs in asexual stages of Plasmodium falciparum. Mol Biochem Parasitol. 1997 Nov;89(2):283-93.	.	.	.	calreticulin family.	.	.	Calreticulin family	PF00262	PF00262; Calreticulin	.	.	hsa04141: Protein processing in endoplasmic reticulum; hsa04145: Phagosome; hsa04612: Antigen processing and presentation; hsa05142: Chagas disease; hsa05163: Human cytomegalovirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection	"R-HSA-1236974: ER-Phagosome pathway; R-HSA-168316: Assembly of Viral Components at the Budding Site; R-HSA-3000480: Scavenging by Class A Receptors; R-HSA-3000484: Scavenging by Class F Receptors; R-HSA-381183: ATF6 (ATF6-alpha) activates chaperone genes; R-HSA-901042: Calnexin/calreticulin cycle; R-HSA-983170: Antigen Presentation: Folding, assembly and peptide loading of class I MHC"	.	P27797
TT0R12H	Neuron-specific vesicular protein calcyon (CALY)	Q9NYX4	CALY_HUMAN	.	Neuronspecific vesicular protein calcyon; CALY	CALY	Interacts with clathrin light chain A and stimulates clathrin self-assembly and clathrin-mediated endocytosis.	.	.	MVKLGCSFSGKPGKDPGDQDGAAMDSVPLISPLDISQLQPPLPDQVVIKTQTEYQLSSPDQQNFPDLEGQRLNCSHPEEGRRLPTARMIAFAMALLGCVLIMYKAIWYDQFTCPDGFLLRHKICTPLTLEMYYTEMDPERHRSILAAIGAYPLSRKHGTETPAAWGDGYRAAKEERKGPTQAGAAAAATEPPGKPSAKAEKEAARKAAGSAAPPPAQ	Discontinued	Dopamine D1 receptor agonists induce penile erections in rats. Eur J Pharmacol. 2003 Jan 26;460(1):71-4.	5	.	.	.	.	.	.	.	.	.	.	hsa04728:Dopaminergic synapse	.	.	Q9NYX4
TTGFLXM	Campylobacter Flavodoxin:quinone reductase (CAMJU FqrB)	A0A0M4UFG9	A0A0M4UFG9_CAMJU	Iron-sulfur protein donor oxidoreductase	"NADPH oxidoreductase, putative flavodoxin quinone reductase FqrB"	CAMJU FqrB	"Exhibited NADPH quinone reductase activity with menadione or benzoquinone. Reduced flavodoxin (FldA), the electron carrier of PFOR."	.	.	MKKIDLIVVGAGPTGIGCAVEAKLKNKEVLILEKSNNICQTLMQFYKDGKRVDKAYKGCEGTNHGHVPFEDGTKESTIETFQNALKEHNIEVEFGSEVESVKNENGVFLVSTAKGVYGCKNIIVAIGRMGKPNKPDYKLPMTLTKIINFNANSVLGNEKILVVGGGNSAAEYAVDLANSNQVSLCYRKKEFTRLNDINLKDIHEAGNSGEVELKLGIDINEVEDDNGKAKVNFTDGTSDIYDRIIYAIGGSTPLDFLQKCGINVDDKGVPLMDENKQSNVKGIFVAGDITTKNGASIVTGLNDAVKILSVL	Literature-reported	Flavodoxin:quinone reductase (FqrB): a redox partner of pyruvate:ferredoxin oxidoreductase that reversibly couples pyruvate oxidation to NADPH prod... J Bacteriol. 2007 Jul;189(13):4764-73.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTFYL58	CaM-kinase II (CAMK2)	Q9UQM7; Q13554; Q13557; Q13555	KCC2A_HUMAN; KCC2B_HUMAN; KCC2D_HUMAN; KCC2G_HUMAN	Kinase	Calcium/calmodulin-dependent protein kinase type II; CaMK-II; CaM kinase II; CAMK	CAMK2A	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.	.	.	MATITCTRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSGGKSGGNKKSDGVKESSESTNTTIEDEDTKVRKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDESACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGAPSVLPH	Clinical trial	Role for CaMKII inhibition in rheumatoid arthritis: effects on HIF-1-induced VEGF production by rheumatoid synovial fibroblasts. Ann N Y Acad Sci. 2009 Sep;1173:706-11.	21	.	.	.	.	.	.	.	.	.	.	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	"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"	.	Q9UQM7
TTGLQWZ	CaM-kinase IV kinase (CAMKK1)	Q8N5S9	KKCC1_HUMAN	Kinase	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	CAMKK1	"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."	EC 2.7.11.17	6CD6; 6CCF	MEGGPAVCCQDPRAELVERVAAIDVTHLEEADGGPEPTRNGVDPPPRARAASVIPGSTSRLLPARPSLSARKLSLQERPAGSYLEAQAGPYATGPASHISPRAWRRPTIESHHVAISDAEDCVQLNQYKLQSEIGKGAYGVVRLAYNESEDRHYAMKVLSKKKLLKQYGFPRRPPPRGSQAAQGGPAKQLLPLERVYQEIAILKKLDHVNVVKLIEVLDDPAEDNLYLVFDLLRKGPVMEVPCDKPFSEEQARLYLRDVILGLEYLHCQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDAQLSSTAGTPAFMAPEAISDSGQSFSGKALDVWATGVTLYCFVYGKCPFIDDFILALHRKIKNEPVVFPEEPEISEELKDLILKMLDKNPETRIGVPDIKLHPWVTKNGEEPLPSEEEHCSVVEVTEEEVKNSVRLIPSWTTVILVKSMLRKRSFGNPFEPQARREERSMSAPGNLLVKEGFGEGGKSPELPGVQEDEAAS	Literature-reported	"STO-609, a specific inhibitor of the Ca(2+)/calmodulin-dependent protein kinase kinase. J Biol Chem. 2002 May 3;277(18):15813-8."	0	.	.	.	.	.	.	.	.	.	.	hsa05034: Alcoholism	R-HSA-111932: CaMK IV-mediated phosphorylation of CREB; R-HSA-442729: CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde; R-HSA-9619229: Activation of RAC1 downstream of NMDARs	.	Q8N5S9
TTV298Y	Calmodulin-dependent kinase II (CAMKK2)	Q96RR4	KKCC2_HUMAN	Kinase	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	CAMKK2	"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."	EC 2.7.11.17	6FEL; 6EWW; 6CMJ; 6BRC; 6BQQ	MSSCVSSQPSSNRAAPQDELGGRGSSSSESQKPCEALRGLSSLSIHLGMESFIVVTECEPGCAVDLGLARDRPLEADGQEVPLDTSGSQARPHLSGRKLSLQERSQGGLAAGGSLDMNGRCICPSLPYSPVSSPQSSPRLPRRPTVESHHVSITGMQDCVQLNQYTLKDEIGKGSYGVVKLAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELVNQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLSETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHGAEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTRECESLSELKEARQRRQPPGHRPAPRGGGGSALVRGSPCVESCWAPAPGSPARMHPLRPEEAMEPE	Patented-recorded	"STO-609, a specific inhibitor of the Ca(2+)/calmodulin-dependent protein kinase kinase. J Biol Chem. 2002 May 3;277(18):15813-8."	0	.	.	.	.	.	.	.	.	.	.	hsa04140: Autophagy - animal; hsa04152: AMPK signaling pathway; hsa04211: Longevity regulating pathway; hsa04920: Adipocytokine signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04936: Alcoholic liver disease; hsa05034: Alcoholism	R-HSA-111932: CaMK IV-mediated phosphorylation of CREB; R-HSA-442729: CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde; R-HSA-9619229: Activation of RAC1 downstream of NMDARs; R-HSA-9619483: Activation of AMPK downstream of NMDARs	.	Q96RR4
TTATDGJ	Calcium signal-modulating cyclophilin ligand (CAML)	P49069	CAMLG_HUMAN	.	cyclophilin	CAMLG	Likely involved in the mobilization of calcium as a result of the TCR/CD3 complex interaction. Binds to cyclophilin B.	.	.	MESMAVATDGGERPGVPAGSGLSASQRRAELRRRKLLMNSEQRINRIMGFHRPGSGAEEESQTKSKQQDSDKLNSLSVPSVSKRVVLGDSVSTGTTDQQGGVAEVKGTQLGDKLDSFIKPPECSSDVNLELRQRNRGDLTADSVQRGSRHGLEQYLSRFEEAMKLRKQLISEKPSQEDGNTTEEFDSFRIFRLVGCALLALGVRAFVCKYLSIFAPFLTLQLAYMGLYKYFPKSEKKIKTTVLTAALLLSGIPAEVINRSMDTYSKMGEVFTDLCVYFFTFIFCHELLDYWGSEVP	Clinical trial	DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5A. PLoS One. 2010 Oct 27;5(10):e13687.	25	.	.	.	.	.	.	.	.	.	.	.	R-HSA-9609523: Insertion of tail-anchored proteins into the endoplasmic reticulum membrane	.	P49069
TTULOB6	Cathelicidin antimicrobial peptide (CAMP)	P49913	CAMP_HUMAN	Cathelicidin family	upregulating cAMP; hCAP18; CAP18; CAMP; Antibacterial protein LL37; 18 kDa cationic antimicrobial protein	CAMP	"Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity."	.	.	MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES	Successful	Natural products as sources of new drugs over the last 25 years. J Nat Prod. 2007 Mar;70(3):461-77.	34	.	.	.	.	.	.	.	.	.	.	hsa04970:Salivary secretion; hsa05152:Tuberculosis	R-HSA-1222556:ROS production in response to bacteria	MetaCyc:ENSG00000164047-MON	P49913
TT1YHKR	Candida AIR carboxylase (Candi ADE2)	Q92210	PUR6_CANAL	Carbon-carbon lyase	Phosphoribosylaminoimidazole carboxylase; AIRC; AIR carboxylase	Candi ADE2	Catalyzes the sixth step of the de novo purine biosynthesis pathway.	EC 4.1.1.21	.	MDSKTVGILGGGQLGRMIVEAAHRLNIKTVILDAAKSPAKQINALDDHVDGSFTNYDSIVKLAEKADVLTVEIEHVDVDALIKVQEKFPKVEIYPLPETIRLIQDKYLQKNHLIKHDVAVTESVAVETNTVDDLLHIGEKFGYPYMLKSRTLAYDGRGNFVVKDKSYCEKALEFLKDRPLYAEKWCPFTKELAVMVVRSLEGEVFAYPTVETIHENNICHLVYAPARIPDTLAKKASILAKNAVKSFLGCGIFGVEMFLLENNELLINEIAPRPHNSGHYTIDACVTSQFEAHVRAVTGLPMPKGFTEFSTSITNAIMLNVLGDKATPNKELEICRRALETPHASVYLYGKTTRPERKMGHINVVTSSMQDAESRLSYILGDTTEIPKSLATDKESPLVGIIMGSDSDLPVMAVGARILKQFGVPFELTIVSAHRTPHRMSEYAIEAPKRGLKCIIAGAGGAAHLPGMVAAMTPLPVIGVPVKGSTLDGVDSLHSIVQMPRGIPVATVAINNSTNAALLAIRILGAYDSKWLTEMNQYMLNMETEVLGKAETLEEIGYEDYLTDKLKK	Literature-reported	Virulence of a phosphoribosylaminoimidazole carboxylase-deficient Candida albicans strain in an immunosuppressed murine model of systemic candidiasis. Infect Immun. 2001 Apr;69(4):2542-8.	.	.	.	.	.	.	.	.	.	.	.	cal00230: Purine metabolism; cal01100: Metabolic pathways; cal01110: Biosynthesis of secondary metabolites	.	.	Q92210
TTRIFQ7	Candida Histidine kinase (Candi chik1)	O74271	O74271_CANAX	Kinase	Histidine kinase	Candi chik1	"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. "	.	.	MNPTKKPRLSPMQPSVFEILNDPELYSQHCHSLRETLLDHFNHQATLIDTYEHELEKSKNANKAFQQALSEIGTVVISVAMGDLSKKVEIHTVENDPEILKVKITINTMMDQLQTFANEVTKVATEVANGELGGQAKNDGSVGIWRSLTDNVNIMALNLTNQVREIADVTRAVAKGDLSRKINVHAQGEILQLQRTINTMVDQLRTFAFEVSKVARDVGVLGILGGQALIENVEGIWEELTDNVNAMALNLTTQVRNIANVTTAVAKGDLSKKVTADCKGEILDLKLTINQMVDRLQNFALAVTTLSREVGTLGIWGGQANVQDVEGAWKQVTENVNLMATNLTNQVRSIATVTTAVAHGDLSQKIDVHAQGEILQLKNTINKMVDSLQLFASEVSKVAQDVGINGKLGIQAQVSDVDGLWKEITSNVNTMASNLTSQVRAFAQITAAATDGDFTRFITVEASGEMDALKTKINQMVFNLRESLQRNTAAREAAELANSAKSEFLANMSHEIRTPLNGIIGMTQLSLDTELTQYQREMLSIVHNLANSLLTIIDDILDISKIEANRMTVEQIDFSLRGTVFGALKTLAVKAIEKNLDLTYQCDSSFPDNLIGDSFRLRQVILNLAGNAIKFTKEGKVSVSVKKSDKMVLDSKLLLEVCVSDTGIGIEKDKLGLIFDTFCQADGSTTRKFGGTGLGLSISKQLIHLMGGEIWVTSEYGSGSNFYFTVCVSPSNIRYTRQTEQLLPFSSHYVLFVSTEHTQEELDVLRDGIIELGLIPIIVRNIEDATLTEPVKYDIIMIDSIEIAKKLRLLSEVKYIPLVLVHHSIPQLNMRVCIDLGISSYANTPCSITDLASAIIPALESRSISQNSDESVRYKILLAEDNLVNQKLAVRILEKQGHSVEVVENGLEAYEAIKRNKYDVVLMDVQMPVMGGFEATEKIRQWEKKSNPIDSLTFRTPIIALTAHAMLGDREKSLAKGMDDYVSKPLKPKLLMQTINKCIHNINQLKELSRNSRGSDFAKKMTRNTPGSTTRQGSDEGSVEDMIGDTPRQGSVEGGGTSSRPVQRRSATEGSITTISEQIDR	Literature-reported	"COS-l, a putative two-component histidine kinase of Candida albicans, is an in vivo virulence factor. Med Mycol. 2001 Feb;39(1):69-74."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTK3CAQ	Candida Chitin synthase 1 (Candi CHS1)	P23316	CHS1_CANAX	Hexosyltransferase	Chitin-UDP acetyl-glucosaminyl transferase 1; CHS1	Candi CHS1	Formation and repair of the disk-shaped septumin yeast and the cross walls of the hyphal phase.	EC 2.4.1.16	.	MHNINNGYVPNREKTITKRKVRLVGGKAGNLVLENPVPTELRKVLTRTESPFGEFTNMTYTACTSQPDTFSAEGFTLRAAKYGRETEIVICITMYNEDEVAFARTMHGVMKNIAHLCSRHKSKIWGKDSWKKVQVIIVADGRNKVQQSVLELLTATGCYQENLARPYVNNSKVNAHLFEYTTQISIDENLKFKGDEKNLAPVQVLFCLKESNQKKINSHRWLFNAFCPVLDPNVIVLLDVGTKPDNHAIYNLWKAFDRDSNVAGAAGEIKAMKGKGWINLTNPLVASQNFEYKLSNILDKPLESLFGYISVLPGALSAYRYIALKNHDDGTGPLASYFKGEDLLCSHDKDKENTKANFFEANMYLAEDRILCWELVSKRNDNWVLKFVKSATGETDVPETIAEFLSQRRRWINGAFFAALYSLYHFRKIWTTDHSYARKFWLHVEEFIYQLVSLLFSFFSLSNFYLTFYFLTGSLVSYKSLGKKGGFWIFTLFNYLCIGVLTSLFIVSIGNRPHASKNIFKTLIILLTICALYALVVGFVFVINTIATFGTGGTSTYVLVSIVVSLLSTYGLYTLMSILYLDPWHMLTCSVQYFLMIPSYTCTLQIFAFCNTHDVSWGTKGDNNPKEDLSNQYIIEKNASGEFEAVIVDTNIDEDYLETLYNIRSKRSNKKVALGHSEKTPLDGDDYAKDVRTRVVLFWMIANLVFIMTMVQVYEPGDTGRNIYLAFILWAVAVLALVRAIGSLGYLIQTYARFFVESKSKWMKRGYTAPSHNPLN	Literature-reported	"Novel antifungal agents, targets or therapeutic strategies for the treatment of invasive fungal diseases: a review of the literature (2005-2009). Rev Iberoam Micol. 2009 Mar 31;26(1):15-22."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P23316
TTBGVF1	Candida Chitin synthase 3 (Candi CHS3)	P30573	CHS3_CANAX	Hexosyltransferase	ClassIV chitin synthase3; ChitinUDP acetylglucosaminyl transferase 3; Chitin synthase 3; CHS3	Candi CHS3	Formation and repair ofthe disk-shaped septum in yeast and the cross walls of the hyphal phase.	EC 2.4.1.16	.	MSNFRDSSSPRRGYSEFDPESGEGLGRKKSLIRPERSRMDESHPRFHYTQVANQESNHIKVQPSSTGVDPRKSNELSTSRSHLSNYATPPHQEEEEDEGIPLMDIHNASPNVSSDQNNDLKGGREVYGLNDEINDYGSSPKKNQVISSSRPMNNEKPAKPKHDIYFWKVYCYAITFWAPAPLLKLFGLPTKDRQFAWREKIGLISCILYVGAFVAYLTFGFTKTVCSSQVVRTQINHVNGGYLIINGRAYDLTSSQHPKAAGIQAGSNVLYPPMNAGGKDASFLFQNVNGNCKGLIKPRDNCSIPYDGDELAWYMPCRLFNQDGSTKPNNTFAYYKGWACHTSETARDAYYKLKVNGDVYFTWDDVKNSSRNLVVYSGNVLDLDLINWIETDDVTYPELFDKLRDDETYRGLDISLVLTNSEERQAARCLTEIIKVGSIDTDTIGCIASKVVLYMSLVFILSVVVVKFIMACWFKWVTSRKQGATMYDSKAWAKRNREIEDWVDHDHGIGAEVKTVPVKARANYKAAKTNRQSVFHRAQKLSLGPNADLSQYYDNPNALSKTFKYTTMSTQAALLGRNGYGKRGNNANKSVSGGFNGRQSNLYLTDQGSSTDLLNRPVSSYNPFDSMGDDSIVINGLSPDIIHPDVVPQPPVEYQPFGYPLAHTINLVTCYSEDEEGIRITLDSIATTDYPNSHKLILVICDGIIKGSGNDETTPDIVLDMMSDLTVPRDEVEAYSYVAVAQGSKRHNMAKVYAGFYKYNDETVPPEKQQRIPMITIVKCGTPEEASAPKPGNRGKRDSQIILMSFLQKVVFDERMTSLEYEMLQSIWRITGLMAEFYEIVLMVDADTKVFPDSLTHMVAEMVKDPTIMGLCGETKISNKAQTWVTAIQVFEYYISHHQAKAFESIFGGVTCLPGCFCMYRIKAPKGSDGYWVPILANPDIVERYSDNVVDTLHRKNLLLLGEDRYLSSLMLRTFPTRKQVFVPKAACKTVVPDKFKVLLSQRRRWINSTVHNLFELVLVKDLCGTFCFSMQFVIFIELIGTLVLPAAITFTIYVIIVAIVSKPTPVMSLVLLAVIFGLPGCLIVITVSSLSYLVYFVIYLFALPIWNFVLPSYAYWKFDDFSWGETRTVAGGDKGDHSAVEGKFDSSKIAMKRWREWERERRSTENRKQQQQQQLTNNSSNNLAVPGAAWDPSNTGGNLIDDLSQGSSSGSS	Clinical trial	Inhibitory effect of nikkomycin Z on chitin synthases in Candida albicans. Yeast. 2002 Mar 15;19(4):341-9.	19	.	.	.	.	.	.	.	.	.	.	.	.	.	P30573
TTCNGJ5	Candida Elongation factor 2 (Candi EFT2)	Q5A0M4	EF2_CANAL	Acid anhydrides hydrolase	EFT2; EF2	Candi EFT2	"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."	.	.	MVAFTIEQIRGLMDKVTNVRNMSVIAHVDHGKSTLSDSLVQKAGIISAAKAGDARFMDTRKDEQERGITIKSTAISLYASMTDEDVKDIKQKTDGNSFLVNLIDSPGHVDFSSEVTAALRVTDGALVVVDTVEGVCVQTETVLRQALGERIKPVVVINKVDRALLELQTTKEDLYQTFARTVESVNVIISTYCDPVLGDVQVYPQKGTVAFASGLHGWAFTVRQFANKYSKKFGVDKEKMMERLWGDSYFNPKTKKWTNKDKDADGKPLERAFNMFILDPIFRLFAAIMNFKKDEIPVLLEKLEIQLKGDEKDLEGKALLKVVMRKFLPAADALLEMIVLHLPSPVTAQAYRAETLYEGPSDDPFCTAIRNCDPNADLMLYVSKMVPTSDKGRFYAFGRVFAGTVKSGQKVRIQGPNYQVGKKEDLFLKSIQRTVLMMGRSVEQIDDCPAGNIIGLVGIDQFLLKSGTITTNEAAHNMKVMKFSVSPVVQVAVEVKNANDLPKLVEGLKRLSKSDPCVLTYMSESGEHIVAGTGELHLEICLQDLENDHAGVPLRISPPVVSYRETVEGESSMVALSKSPNKHNRIYVKAQPIDEEVSLDIENGVINPRDDFKARARILADKHGWDVVDARKIWCFGPDGNGPNLVVDQTKAVQYLNEIKDSVVAAFQWATKEGPIFGENCRSVRVNILDVTLHADAIHRGGGQIIPTMRRVTYASMLLAEPAIQEPVFLVEIQCPENAIGGIYSVLNKKRGQVISEEQRPGTPLFTVKAYLPVNESFGFTGELRQATGGQAFPQLIFDHWQVMSGDVTDENSKPGAIVKEKRVRAGLKPEVPEYTEYYDKL	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q5A0M4
TTM9XSU	Candida Squalene epoxidase (Candi ERG1)	Q92206	ERG1_CANAL	.	Candi Squalene monooxygenase; Candi Squalene epoxidase; Candi SE	Candi ERG1	"Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis."	.	.	MSSVKYDAIIIGAGVIGPTIATAFARQGRKVLIVERDWSKPDRIVGELMQPAGIKALRELGMIKAINNIRAVDCTGYYIKYYDETITIPYPLKKDACITNPVKPVPDAVDGVNDKLDSDSTLNVDDWDFDERVRGAAFHHGDFLMNLRQICRDEPNVTAVEATVTKILRDPSDPNTVIGVQTKQPSGTVDYHAKLTISCDGIYSKFRKELSPTNVPTIGSYFIGLYLKNAELPAKGKGHVLLGGHAPALIYSVSPTETRVLCVYVSSKPPSAANDAVYKYLRDNILPAIPKETVPAFKEALEERKFRIMPNQYLSAMKQGSENHKGFILLGDSLNMRHPLTGGGMTVGLNDSVLLAKLLHPKFVEDFDDHQLIAKRLKTFHRKRKNLDAVINTLSISLYSLFAADKKPLRILRNGCFKYFQRGGECVNGPIGLLSGMLPFPMLLFNHFFSVAFYSVYLNFIERGLLGFPLALFEAFEVLFTAIVIFTPYLWNEIVR	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	cal00100: Steroid biosynthesis; cal00909: Sesquiterpenoid and triterpenoid biosynthesis; cal01100: Metabolic pathways; cal01110: Biosynthesis of secondary metabolites	.	.	Q92206
TTTSOUD	Candida Cytochrome P450 51 (Candi ERG11)	P10613	CP51_CANAL	Paired donor oxygen oxidoreductase	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	Candi ERG11	"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."	.	5V5Z; 5TZ1; 5FSA	MAIVETVIDGINYFLSLSVTQQISILLGVPFVYNLVWQYLYSLRKDRAPLVFYWIPWFGSAASYGQQPYEFFESCRQKYGDVFSFMLLGKIMTVYLGPKGHEFVFNAKLSDVSAEDAYKHLTTPVFGKGVIYDCPNSRLMEQKKFAKFALTTDSFKRYVPKIREEILNYFVTDESFKLKEKTHGVANVMKTQPEITIFTASRSLFGDEMRRIFDRSFAQLYSDLDKGFTPINFVFPNLPLPHYWRRDAAQKKISATYMKEIKSRRERGDIDPNRDLIDSLLIHSTYKDGVKMTDQEIANLLIGILMGGQHTSASTSAWFLLHLGEKPHLQDVIYQEVVELLKEKGGDLNDLTYEDLQKLPSVNNTIKETLRMHMPLHSIFRKVTNPLRIPETNYIVPKGHYVLVSPGYAHTSERYFDNPEDFDPTRWDTAAAKANSVSFNSSDEVDYGFGKVSKGVSSPYLPFGGGRHRCIGEQFAYVQLGTILTTFVYNLRWTIDGYKVPDPDYSSMVVLPTEPAEIIWEKRETCMF	Successful	Investigation of the role of cytochrome P450 2B4 active site residues in substrate metabolism based on crystal structures of the ligand-bound enzyme. Arch Biochem Biophys. 2006 Nov 1;455(1):61-7.	34	.	.	.	.	.	.	.	.	.	.	cal00100: Steroid biosynthesis; cal01100: Metabolic pathways; cal01110: Biosynthesis of secondary metabolites	.	.	P10613
TTLAK5E	Candida Mannan polymerase complex MNN9 (Candi MNN9)	P53697	MNN9_CANAL	.	MNN9; C. albicans MNN9	Candi MNN9	"Required for the addition of the long alpha 1,6-mannose backbone ofN-linked glycans on cell wall and periplasmic proteins."	.	.	MVHYRNRYLNYIRRKPLALLAPITLLVVIYFYFFSAHGFSSNKQKYNYNKKSRGWFYKNRDTVILKDLPKNHISHYDLNKLTASKDALNKREEVLILTPMSKFLPEYWENINKLTYDHSLISLGFIFPRTTQGDDALKELENALKKTKREKRLNFKKITILRQDSNSLQSQLEKDRHAFKVQKERRSMMALARNSLVFSTILPSTSWVLWLDADIVETPVTLIQDLTGHNKPVVSANVHQRFINQDTKQPDIRPYDFNNWVESEEGLKLAASLPDDEIIVEGYSEMVTHRALMAHFYDPKGDPSTEMTLDGVGGGAVMVKADVHRDGAMFPSFPFYHLIETEGFAKMAKRLGYEVYGLPNYLVFHYNE	Literature-reported	"Molecular analysis of the Candida albicans homolog of Saccharomyces cerevisiae MNN9, required for glycosylation of cell wall mannoproteins. J Bacteriol. 1999 Dec;181(24):7439-48."	.	.	.	.	.	.	.	.	.	.	.	cal00513: Various types of N-glycan biosynthesis; cal01100: Metabolic pathways	.	.	P53697
TTBAF05	Candida Peptide N-myristoyltransferase (Candi NMT1)	P30418	NMT_CANAL	Acyltransferase	Peptide N-myristoyltransferase; NMT1; NMT; Myristoyl-CoA:protein N-myristoyltransferase	Candi NMT1	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.	EC 2.3.1.97	1NMT; 1IYL; 1IYK	MSGDNTGNKSNSAPSKSIEELLKLLAMGQELSPAQQKEMKDYKFWKTQPVPSLSETVTEEGPIDKLKTPEDVPNDPLPLISDFEWSTLDIDDNLQLDELYKLLYDNYVEDIDATFRFKYSHEFFQWALKPPGWRKDWHVGVRVKSTGKLVAFIAATPVTFKLNKSNKVIDSVEINFLCIHKKLRNKRLAPVLIKEITRRVNKQNIWQALYTGGSILPTPLTTCRYQHRPINWSKLHDVGFSHLPPNQTKSSMVASYTLPNNPKLKGLRPMTGKDVSTVLSLLYKYQERFDIVQLFTEEEFKHWMLGHDENSDSNVVKSYVVEDENGVITDYFSYYLLPFTVLDNAQHDELGIAYLFYYASDSFEKPNYKKRLNELITDALITSKKFGVDVFNCLTCQDNTYFLKDCKFGSGDGFLNYYLFNYRTFPMDGGIDKKTKEVVEDQTSGIGVVLL	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P30418
TT915ZD	Candida Mannose-6-phosphate isomerase (Candi PMI1)	P34948	MPI_CANAL	Intramolecular oxidoreductases	Phosphomannose isomerase; Phosphohexomutase; PMI1; PMI	Candi PMI1	Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.	.	5NW7; 1PMI	MSSEKLFRIQCGYQNYDWGKIGSSSAVAQFVHNSDPSITIDETKPYAELWMGTHPSVPSKAIDLNNQTLRDLVTAKPQEYLGESIITKFGSSKELPFLFKVLSIEKVLSIQAHPDKKLGAQLHAADPKNYPDDNHKPEMAIAVTDFEGFCGFKPLDQLAKTLATVPELNEIIGQELVDEFISGIKLPAEVGSQDDVNNRKLLQKVFGKLMNTDDDVIKQQTAKLLERTDREPQVFKDIDSRLPELIQRLNKQFPNDIGLFCGCLLLNHVGLNKGEAMFLQAKDPHAYISGDIIECMAASDNVVRAGFTPKFKDVKNLVEMLTYSYESVEKQKMPLQEFPRSKGDAVKSVLYDPPIAEFSVLQTIFDKSKGGKQVIEGLNGPSIVIATNGKGTIQITGDDSTKQKIDTGYVFFVAPGSSIELTADSANQDQDFTTYRAFVEA	Successful	Antifungal Activity of Ag(I) and Zn(II) Complexes of Sulfacetamide Derivatives. Met Based Drugs. 2000;7(1):49-54.	34	.	.	.	.	.	.	.	.	.	.	cal00051: Fructose and mannose metabolism; cal00520: Amino sugar and nucleotide sugar metabolism; cal01100: Metabolic pathways; cal01110: Biosynthesis of secondary metabolites; cal01240: Biosynthesis of cofactors; cal01250: Biosynthesis of nucleotide sugars	.	.	P34948
TTR7YAT	Candida Co-chaperone SGT1 (Candi SGT1)	A0A1D8PIG5	A0A1D8PIG5_CANAL	.	orf19.4089; CAALFM_C209270CA	Candi SGT1	"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."	.	.	MAIEQFITKGDDALKSKDYLGAISYYSQAIKENPQAFSPYLKRSTAYQKLKNNDKAKADISSAFSIATEKGKRVDIGLCYFKLGLVYYQEKKVKLSLTQFEKAVEYDCKEPTLSMWKAKAEYDLKNHPEWNVEGDKEEDDDIDLVLGVENEYTQSMANTEKDKSHEPKIVELDANEESSEKKSNQESTSSAPAAQATTQAPKSTNVDVINKIAPLNVKFRDDWYQSNEEVIITIYAKKVNEEKLKVEFDTNSVCISFPSAAASEYKYYLDPLFAEIVPSESKYKVYSTKLEITLKKKDANKWPELEKQAVEGVTDNQDKDKKVDPSELVYPTSSKKKINWNNFKIDDDDKEEGNENDFFRKIFKDVDEDSRRAMMKSYVQSNGTVLTTSWDEAKDKEFEVLPPDGMEVKKWDT	Literature-reported	The Hsp90 co-chaperone Sgt1 governs Candida albicans morphogenesis and drug resistance. PLoS One. 2012;7(9):e44734.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	A0A1D8PIG5
TTIV0HD	Candida Elongation factor 3 (Candi TEF3)	O93796	EF3_CANGA	ABC transporter	TEF3; EF-3	Candi TEF3	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.	.	.	MTDSDQSLKVLEELFKNLSVATADNRVEAAQEVASFLNGNIIEHDIPEKFFEELAKAVKDKKTSANFLEAVAHIANEANLSPSVEPFVITLVPEICAKAGDKDKDVQAVASKTLVAISKAINPVAIKAYLPHLTKSLETTNKWQEKVSVLAAISALVDAAKEQVALRMPELIPVLSETMWDTKKEVKEAATATMTKATETVDNKDIERFIPQLISCIADPKQVPETVHLLGATTFVAEVTPATLSIMVPLLSRGLAERETSIKRKAAVIIDNMCKLVEDPQVVAPFLDKLLPGLKNNYATIADPEAREVTLRGLKTLRRVGNVTEDDVLPEISHAGDIETTLGVINELLKGENVAPRFKIVVEYIAAMAGDLIDERVIDQQAWFTHITPYMTIFMHERNAKDVLDEFRKRAVDNIPVGPNFDDEEDEGEDLCNCEFSLAYGAKILLNKTQLRLKRGRRYGLCGPNGAGKSTLMRAIANGQVDGFPTPEECMTVYVEHDIDGTHADTSVLDFVVSSEVGTKEAITAKLVEFGFTEEMINMPISSLSGGWKMKLALARAVLKNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSVIVSHDSGFLDNVCQYIIHYEGLKLRKYKGNLSEFVKKCPTAQSYYELGASDLEFKFPEPGYLEGVKTKQKAIVKVSNMTFQYPGTSKPQISDISFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHAFAHIESHLDKTPSEYIQWRFQTGEDRETMDRANRQINENDAEAMNKIFKIEGTPRRIAGIHARRKFKNTYEYECSFLLGENIGMKSERWVPMMSVDNAWIPRGELVESHSKMVAEVDMKEALASGQFRPLTRKEIEEHCAMLGLDAELVSHSRIRGLSGGQKVKLVLAACSWQRPHLIVLDEPTNYLDRDSLGALSKALKAFEGGVIIITHSAEFTKNLTEEVWAVKDGKMTPSGHNWVSGQGAGPRIEKKEDEEDKFDAMGNKIAGGKKKKKLSSAELRKKKKERMKKKKELGDAYVSSDDEDF	Literature-reported	Evolutionary divergence of an elongation factor 3 from Cryptococcus neoformans. J Bacteriol. 2001 Apr;183(7):2241-8.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	O93796
TTU6BFZ	Candida Thymidylate synthase (Candi TMP1)	P12461	TYSY_CANAL	Methyltransferase	Tsase of Candida albicans; TS of Candida albicans; TMP1; Human recombinant thymidylate synthase; HrTS	Candi TMP1	Contributes to thede novo mitochondrial thymidylate biosynthesis pathway.	EC 2.1.1.45	.	MTVSPNTAEQAYLDLCKRIIDEGEHRPDRTGTGTKSLFAPPQLRFDLSNDTFPLLTTKKVFSKGIIHELLWFVAGSTDAKILSEKGVKIWEGNGSREFLDKLGLTHRREGDLGPVYGFQWRHFGAEYKDCDSDYTGQGFDQLQDVIKKLKTNPYDRRIIMSAWNPPDFAKMALPPCHVFCQFYVNFPTSSPDPNNPKQAKTAKPKLSCLLYQRSCDMGLGVPFNIASYALLTKMIAHVVDMDCGEFIHTLGDAHVYLDHIDALKEQFERIPKQFPKLVIKEERKNEIKSIDDFKFEDFEIVGYEPYPPIKMKMSV	Successful	Updated clinical information on multitargeted antifolates in lung cancer. Clin Lung Cancer. 2009 Mar;10 Suppl 1:S35-40.	34	.	.	.	.	.	.	.	.	.	.	hsa00240:Pyrimidine metabolism; hsa00670:One carbon pool by folate; hsa01100:Metabolic pathways	R-HSA-113510:E2F mediated regulation of DNA replication; R-HSA-500753:Pyrimidine biosynthesis; R-HSA-69205:G1/S-Specific Transcription	.	P12461
TT6TDPW	Candida PtdIns-3-kinase VPS34 (Candi VPS34)	Q92213	VPS34_CANAX	Kinase	Vacuolar sorting protein 34; VPS34; PtdIns-3-kinase; Phosphatidylinositol 3-kinase VPS34	Candi VPS34	Phosphatidylinositol 3-kinase homolog required for vacuolar sorting and segregation.	EC 2.7.1.137	.	MATLSQPQSALPKTKIATTFGLSKDLKSPISVKVCYLECTRNNVSLVPLSTKFEDPTVFKKLSQIYKNSDLFVEIRVYDGKNNNLISTPVRTSYKAFNNKGRTWNQQLKLNIDYNQISIDAYLKFSICEIIDTKPSVFGVSYLSLFSHDSSTLRSGSHKIPVFMEDDPQYSKNIQYGTLIGLTDLEKRLIDYENGKYPRLNWLDKMVLPKVDATFLKTNNKDHDYYLYIELPQFEFPIVYSDIIYQIPTIEPITETTSKIPPDDTLNSNIIINSIDIPMATSHDPSIMKVYDPDFHITANNHLNPNATTFDPVELKYRKLERNIDNNTILDKELKPTPQLRDELLRIMIKPSNAESTDNEKNLIWKFRYYFSKNNSGNDPSNKSVKSFLPKFLRSINWENDYELDHTFKEIIPFYWNVDKLQIGDALELLGDYFNPYTLGKPTYQDDSMTSKSSKMKSDEKRFIKIYNNVCFLRKLAVERLKLANSEELLLYLLQLVQALKYEALIYEKSPPFCERSDQIEDNASSTLKSPLADFLIERAVENEKLGNFFYWYVKVENEDQLNNPHIDGPIKIYMDILNRYIELLKAHCHENRLPYYKHLKHQIWFIKKLTSLVELLRASFKKNEATAKKVEYLREYLANSGNELLKFPEPFPLPLDPSVMICGCYPEESSVFKSSLAPLKITLKTIEKKKHGHATSQLFGKRSRYGKYPLMFKIGDDLRQDQLVIQIIDLMDQLLKNENLDLKLTPYKILATSPISGLIQFVPNETLDSILSKTYPTSVTYSGGGETSDGPPSVSNNGILNYLRLHSQEQQSEEPISKSILSTNTSQSNTEIPVLPRQPKPTITSDLGVSPILMDNYVKSCAGYCVITYILGVGDRHLDNLLLSPNGKFWHADFGYILGRDPKPFPPLMKLPIQVIDGMGGLHHENYNVFKSYCFITYTTLRKNSNLILNLFQLMLDANIPDIQFDPSRVIEKVQEKFCLQMTEEEAILHFQNLINDSVNAFLPVVIDRLHSLAQYWRA	Literature-reported	"A phosphatidylinositol 3-kinase of Candida albicans influences adhesion, filamentous growth and virulence. Microbiology. 2000 Nov;146 ( Pt 11):2755-64."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q92213
TT1WBIJ	Calpain-1 (CAPN1)	P07384	CAN1_HUMAN	Peptidase	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	CAPN1	Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.	EC 3.4.22.52	.	MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLGQDYEQLRVRCLQSGTLFRDEAFPPVPQSLGYKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQVVSLIRMRNPWGEVEWTGAWSDSSSEWNNVDPYERDQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKSRTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPAVHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTVELDDQIQANLPDEQVLSEEEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA	Patented-recorded	An updated patent review of calpain inhibitors (2012 - 2014).Expert Opin Ther Pat. 2015 Jan;25(1):17-31.	15.5	EC:3.4	Peptidase C2 family	peptidase C2 family.	3.4.22.52 	Acting on peptide bonds (peptidases)	"Calpain large subunit, domain III; EF-hand domain pair; Calpain family cysteine protease"	PF01067; PF13833; PF00648	PF01067; Calpain_III; PF13833; EF-hand_8; PF00648; Peptidase_C2	.	.	hsa04141:Protein processing in endoplasmic reticulum; hsa04210:Apoptosis; hsa04217:Necroptosis; hsa04218:Cellular senescence; hsa05010:Alzheimer disease	R-HSA-1474228: Degradation of the extracellular matrix; R-HSA-6798695: Neutrophil degranulation; R-HSA-6809371: Formation of the cornified envelope; R-HSA-8862803: Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models	.	P07384
TTG5QB7	Calpain-2 (CAPN2)	P17655	CAN2_HUMAN	Peptidase	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	CAPN2	"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."	EC 3.4.22.53	.	MAGIAAKLAKDREAAEGLGSHDRAIKYLNQDYEALRNECLEAGTLFQDPSFPAIPSALGFKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPLNQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELKKPPPNLFKIIQKALQKGSLLGCSIDITSAADSEAITFQKLVKGHAYSVTGAEEVESNGSLQKLIRIRNPWGEVEWTGRWNDNCPSWNTIDPEERERLTRRHEDGEFWMSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDEEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELSGQTNIHLSKNFFLTNRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDFCIRVFSEKKADYQAVDDEIEANLEEFDISEDDIDDGFRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDSDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKMPCQLHQVIVARFADDQLIIDFDNFVRCLVRLETLFKIFKQLDPENTGTIELDLISWLCFSVL	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	17	EC:3.4	Peptidase C2 family	peptidase C2 family.	3.4.22.53	Acting on peptide bonds (peptidases)	"Calpain large subunit, domain III; EF-hand domain pair; Calpain family cysteine protease"	PF01067; PF13833; PF00648	PF01067; Calpain_III; PF13833; EF-hand_8; PF00648; Peptidase_C2	.	.	hsa04141:Protein processing in endoplasmic reticulum; hsa04210:Apoptosis; hsa05010:Alzheimer's disease	R-HSA-1474228:Degradation of the extracellular matrix	.	P17655
TTIZQFJ	Histone-arginine methyltransferase CARM1 (CARM1)	Q86X55	CARM1_HUMAN	Methyltransferase	Protein arginine N-methyltransferase 4; PRMT4; Histonearginine methyltransferase CARM1; Coactivatorassociated arginine methyltransferase 1; Coactivator-associated arginine methyltransferase 1	CARM1	"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."	EC 2.1.1.319	.	MAAAAAAVGPGAGGAGSAVPGGAGPCATVSVFPGARLLTIGDANGEIQRHAEQQALRLEVRAGPDSAGIALYSHEDVCVFKCSVSRETECSRVGKQSFIITLGCNSVLIQFATPNDFCSFYNILKTCRGHTLERSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGTTPSPPPGSHYTSPSENMWNTGSTYNLSSGMAVAGMPTAYDLSSVIASGSSVGHNNLIPLANTGIVNHTHSRMGSIMSTGIVQGSSGAQGSGGGSTSAHYAVNSQFTMGGPAISMASPMSIPTNTMHYGS	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1255).	0	EC:2.1	Methyltransferase superfamily	class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.	2.1.1.319 	Transferring one-carbon groups	Coactivator-associated arginine methyltransferase 1 N terminal	PF11531	PF11531; CARM1	.	.	hsa01522: Endocrine resistance	"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"	MetaCyc:HS13925-MON	Q86X55
TTCQIBE	Caspase-1 (CASP1)	P29466	CASP1_HUMAN	Peptidase	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	CASP1	"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."	EC 3.4.22.36	.	MADKVLKEKRKLFIRSMGEGTINGLLDELLQTRVLNKEEMEKVKRENATVMDKTRALIDSVIPKGAQACQICITYICEEDSYLAGTLGLSADQTSGNYLNMQDSQGVLSSFPAPQAVQDNPAMPTSSGSEGNVKLCSLEEAQRIWKQKSAEIYPIMDKSSRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFLVFMSHGIREGICGKKHSEQVPDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDSPGVVWFKDSVGVSGNLSLPTTEEFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDGRAQMPTTERVTLTRCFYLFPGH	Clinical trial	"(S)-1-((S)-2-{[1-(4-amino-3-chloro-phenyl)-methanoyl]-amino}-3,3-dimethyl-butanoyl)-pyrrolidine-2-carboxylic acid ((2R,3S)-2-ethoxy-5-oxo-tetrahydr... J Pharmacol Exp Ther. 2007 May;321(2):509-16."	21	EC:3.4	Peptidase	peptidase C14A family.	3.4.22.36	Acting on peptide bonds (peptidases)	Caspase recruitment domain	PF00619	PF00619; CARD	.	.	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	R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-448706:Interleukin-1 processing; R-HSA-844456:The NLRP3 inflammasome	.	P29466
TTX5HEK	Caspase-10 (CASP10)	Q92851	CASPA_HUMAN	Peptidase	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	CASP10	"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."	EC 3.4.22.63	.	MKSQGQHWYSSSDKNCKVSFREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEKSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQHLNCTKEEVERLLPTRQRVSLFRNLLYELSEGIDSENLKDMIFLLKDSLPKTEMTSLSFLAFLEKQGKIDEDNLTCLEDLCKTVVPKLLRNIEKYKREKAIQIVTPPVDKEAESYQGEEELVSQTDVKTFLEALPQESWQNKHAGSNGNRATNGAPSLVSRGMQGASANTLNSETSTKRAAVYRMNRNHRGLCVIVNNHSFTSLKDRQGTHKDAEILSHVFQWLGFTVHIHNNVTKVEMEMVLQKQKCNPAHADGDCFVFCILTHGRFGAVYSSDEALIPIREIMSHFTALQCPRLAEKPKLFFIQACQGEEIQPSVSIEADALNPEQAPTSLQDSIPAEADFLLGLATVPGYVSFRHVEEGSWYIQSLCNHLKKLVPRMLKFLEKTMEIRGRKRTVWGAKQISATSLPTAISAQTPRPPMRRWSSVS	Patented-recorded	Caspase inhibitors: a review of recently patented compounds (2013-2015).Expert Opin Ther Pat. 2018 Jan;28(1):47-59.	15.5	EC:3.4	Peptidase C14A family	peptidase C14A family.	3.4.22.63	Acting on peptide bonds (peptidases)	Death effector domain	PF01335	PF01335; DED	.	.	hsa04210:Apoptosis; hsa04622:RIG-I-like receptor signaling pathway; hsa04668:TNF signaling pathway; hsa05152:Tuberculosis; hsa05161:Hepatitis B	R-HSA-6803207: TP53 Regulates Transcription of Caspase Activators and Caspases; 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	.	Q92851
TT12VNG	Caspase 2 messenger RNA (CASP2 mRNA)	P42575	CASP2_HUMAN	mRNA target	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)	CASP2	"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."	EC 3.4.22.55	.	MAAPSAGSWSTFQHKELMAADRGRRILGVCGMHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDMLLTTLSGLQHVLPPLSCDYDLSLPFPVCESCPLYKKLRLSTDTVEHSLDNKDGPVCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT	Clinical trial	"Toxicological and pharmacokinetic properties of QPI-1007, a chemically modified synthetic siRNA targeting caspase 2 mRNA, following intravitreal injection. Nucleic Acid Ther. 2014 Aug;24(4):258-66."	25	mRNA	mRNA target	.	.	.	Caspase recruitment domain	PF00619	PF00619; CARD	.	.	hsa04210: Apoptosis	R-HSA-168638:NOD1/2 Signaling Pathway; R-HSA-205025:NADE modulates death signalling	.	P42575
TTC6S84	Caspase-2 (CASP2)	P42575	CASP2_HUMAN	Peptidase	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	CASP2	"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."	EC 3.4.22.55	.	MAAPSAGSWSTFQHKELMAADRGRRILGVCGMHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDMLLTTLSGLQHVLPPLSCDYDLSLPFPVCESCPLYKKLRLSTDTVEHSLDNKDGPVCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT	Patented-recorded	Caspase inhibitors: a review of recently patented compounds (2013-2015).Expert Opin Ther Pat. 2018 Jan;28(1):47-59.	15.5	EC:3.4	Peptidase	peptidase C14A family.	3.4.22.55	Acting on peptide bonds (peptidases)	Caspase recruitment domain	PF00619	PF00619; CARD	.	.	hsa04210: Apoptosis	R-HSA-168638: NOD1/2 Signaling Pathway; R-HSA-205025: NADE modulates death signalling; R-HSA-6803207: TP53 Regulates Transcription of Caspase Activators and Caspases	.	P42575
TTPF2QI	Caspase-3 (CASP3)	P42574	CASP3_HUMAN	Peptidase	Yama protein; SREBP cleavage activity 1; SCA-1; Protein Yama; Cysteine protease CPP32; Caspase 3; CPP32; CPP-32; CASP-3; Apopain	CASP3	"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."	EC 3.4.22.56	.	MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH	Clinical trial	Small-molecule activation of procaspase-3 to caspase-3 as a personalized anticancer strategy. Nat Chem Biol. 2006 Oct;2(10):543-50.	17	EC:3.4	Peptidase	peptidase C14A family.	3.4.22.56	Acting on peptide bonds (peptidases)	.	.	.	.	.	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	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	.	P42574
TT6KIOT	Caspase-11 (CASP11)	P49662	CASP4_HUMAN	Peptidase	ICH-3 protease; Casp4 of Mus musculus	Casp4	"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."	EC 3.4.22.57	.	MAEGNHRKKPLKVLESLGKDFLTGVLDNLVEQNVLNWKEEEKKKYYDAKTEDKVRVMADSMQEKQRMAGQMLLQTFFNIDQISPNKKAHPNMEAGPPESGESTDALKLCPHEEFLRLCKERAEEIYPIKERNNRTRLALIICNTEFDHLPPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATRPEHKSSDSTFLVLMSHGILEGICGTVHDEKKPDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGANRGELWVRDSPASLEVASSQSSENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPRAKAQMPTIERLSMTRYFYLFPGN	Literature-reported	"Grassystatins A-C from marine cyanobacteria, potent cathepsin E inhibitors that reduce antigen presentation. J Med Chem. 2009 Sep 24;52(18):5732-47."	0	.	.	.	.	.	.	.	.	.	.	hsa04613: Neutrophil extracellular trap formation; hsa04621: NOD-like receptor signaling pathway; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05132: Salmonella infection	R-HSA-168638: NOD1/2 Signaling Pathway; R-HSA-5620971: Pyroptosis	.	P49662
TT3VZ8D	Caspase-4 (CASP4)	P49662	CASP4_HUMAN	Peptidase	Protease TX; Mih1; ICH2; ICH-2; ICE(rel)-II; ICE and Ced-3 homolog 2; CASP-4	CASP4	"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."	EC 3.4.22.57	.	MAEGNHRKKPLKVLESLGKDFLTGVLDNLVEQNVLNWKEEEKKKYYDAKTEDKVRVMADSMQEKQRMAGQMLLQTFFNIDQISPNKKAHPNMEAGPPESGESTDALKLCPHEEFLRLCKERAEEIYPIKERNNRTRLALIICNTEFDHLPPRNGADFDITGMKELLEGLDYSVDVEENLTARDMESALRAFATRPEHKSSDSTFLVLMSHGILEGICGTVHDEKKPDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGANRGELWVRDSPASLEVASSQSSENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPRAKAQMPTIERLSMTRYFYLFPGN	Patented-recorded	Caspase inhibitors: a review of recently patented compounds (2013-2015).Expert Opin Ther Pat. 2018 Jan;28(1):47-59.	15.5	EC:3.4	.	peptidase C14A family.	3.4.22.57 	Acting on peptide bonds (peptidases)	Caspase recruitment domain	PF00619	PF00619; CARD	.	.	hsa04613: Neutrophil extracellular trap formation; hsa04621: NOD-like receptor signaling pathway; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05132: Salmonella infection	R-HSA-168638: NOD1/2 Signaling Pathway; R-HSA-5620971: Pyroptosis	.	P49662
TTWR48J	Caspase-5 (CASP5)	P51878	CASP5_HUMAN	Peptidase	Protease TY; Protease ICH-3; ICH3; ICE(rel)-III; CASP-5	CASP5	"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)."	EC 3.4.22.58	.	MAEDSGKKKRRKNFEAMFKGILQSGLDNFVINHMLKNNVAGQTSIQTLVPNTDQKSTSVKKDNHKKKTVKMLEYLGKDVLHGVFNYLAKHDVLTLKEEEKKKYYDTKIEDKALILVDSLRKNRVAHQMFTQTLLNMDQKITSVKPLLQIEAGPPESAESTNILKLCPREEFLRLCKKNHDEIYPIKKREDRRRLALIICNTKFDHLPARNGAHYDIVGMKRLLQGLGYTVVDEKNLTARDMESVLRAFAARPEHKSSDSTFLVLMSHGILEGICGTAHKKKKPDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGEKHGELWVRDSPASLALISSQSSENLEADSVCKIHEEKDFIAFCSSTPHNVSWRDRTRGSIFITELITCFQKYSCCCHLMEIFRKVQKSFEVPQAKAQMPTIERATLTRDFYLFPGN	Patented-recorded	Caspase inhibitors: a review of recently patented compounds (2013-2015).Expert Opin Ther Pat. 2018 Jan;28(1):47-59.	15.5	EC:3.4	.	peptidase C14A family.	3.4.22.58	Acting on peptide bonds (peptidases)	Caspase recruitment domain	PF00619	PF00619; CARD	.	.	hsa04621: NOD-like receptor signaling pathway; hsa05132: Salmonella infection	R-HSA-5620971: Pyroptosis	.	P51878
TTKW4ML	Caspase 6 messenger RNA (CASP6 mRNA)	P55212	CASP6_HUMAN	mRNA target	MCH2 (mRNA); Caspase-6 subunit p18 (mRNA); Caspase-6 subunit p11 (mRNA); CASP-6 (mRNA); Apoptotic protease Mch-2 (mRNA)	CASP6	"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."	EC 3.4.22.59	6DEV; 6DEU; 4NBN; 4NBL; 4NBK	MSSASGLRRGHPAGGEENMTETDAFYKREMFDPAEKYKMDHRRRGIALIFNHERFFWHLTLPERRGTCADRDNLTRRFSDLGFEVKCFNDLKAEELLLKIHEVSTVSHADADCFVCVFLSHGEGNHIYAYDAKIEIQTLTGLFKGDKCHSLVGKPKIFIIQACRGNQHDVPVIPLDVVDNQTEKLDTNITEVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLGKYGSSLEFTELLTLVNRKVSQRRVDFCKDPSAIGKKQVPCFASMLTKKLHFFPKSN	Literature-reported	"US patent application no. 6,566,135, Antisense modulation of caspase 6 expression."	0	mRNA	mRNA target	.	.	.	.	.	.	.	.	hsa04210:Apoptosis	R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-264870:Caspase-mediated cleavage of cytoskeletal proteins	.	P55212
TT1OPCB	Caspase-6 (CASP6)	P55212	CASP6_HUMAN	Peptidase	MCH2; Caspase-6 subunit p18; Caspase-6 subunit p11; CASP-6; Apoptotic protease Mch-2	CASP6	"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."	EC 3.4.22.59	6DEV; 6DEU; 4NBN; 4NBL; 4NBK	MSSASGLRRGHPAGGEENMTETDAFYKREMFDPAEKYKMDHRRRGIALIFNHERFFWHLTLPERRGTCADRDNLTRRFSDLGFEVKCFNDLKAEELLLKIHEVSTVSHADADCFVCVFLSHGEGNHIYAYDAKIEIQTLTGLFKGDKCHSLVGKPKIFIIQACRGNQHDVPVIPLDVVDNQTEKLDTNITEVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLGKYGSSLEFTELLTLVNRKVSQRRVDFCKDPSAIGKKQVPCFASMLTKKLHFFPKSN	Patented-recorded	Caspase inhibitors: a review of recently patented compounds (2013-2015).Expert Opin Ther Pat. 2018 Jan;28(1):47-59.	15.5	EC:3.4	Peptidase C14A family	peptidase C14A family.	3.4.22.59	Acting on peptide bonds (peptidases)	.	.	.	.	.	hsa04210:Apoptosis	R-HSA-111465: Apoptotic cleavage of cellular proteins; R-HSA-264870: Caspase-mediated cleavage of cytoskeletal proteins; R-HSA-352238: Breakdown of the nuclear lamina; R-HSA-6803207: TP53 Regulates Transcription of Caspase Activators and Caspases	.	P55212
TTM7Y45	Caspase-7 (CASP7)	P55210	CASP7_HUMAN	Peptidase	MCH3; ICE-like apoptotic protease 3; ICE-LAP3; CMH-1; CASP-7; Apoptotic protease Mch-3	CASP7	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.	EC 3.4.22.60	5V6Z; 5V6U; 5K20; 5IC6; 4ZVU	MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLFSKKKKNVTMRSIKTTRDRVPTYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ	Clinical trial	Potent and selective nonpeptide inhibitors of caspases 3 and 7. J Med Chem. 2001 Jun 7;44(12):2015-26.	16	EC:3.4	.	peptidase C14A family.	3.4.22.60	Acting on peptide bonds (peptidases)	.	.	.	.	.	hsa04210: Apoptosis; hsa04215: Apoptosis - multiple species; hsa04668: TNF signaling pathway; hsa04932: Non-alcoholic fatty liver disease; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05130: Pathogenic Escherichia coli infection; hsa05132: Salmonella infection; hsa05133: Pertussis; hsa05134: Legionellosis; hsa05200: Pathways in cancer; hsa05417: Lipid and atherosclerosis	"R-HSA-111459: Activation of caspases through apoptosome-mediated cleavage; R-HSA-111463: SMAC (DIABLO) binds to IAPs; R-HSA-111464: SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes; R-HSA-111465: Apoptotic cleavage of cellular proteins; R-HSA-111469: SMAC, XIAP-regulated apoptotic response; R-HSA-264870: Caspase-mediated cleavage of cytoskeletal proteins"	.	P55210
TT6SZNG	Caspase 8 messenger RNA (CASP8 mRNA)	Q14790	CASP8_HUMAN	mRNA target	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)	CASP8	"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."	EC 3.4.22.61	5L08; 5JQE; 5H33; 5H31; 4ZBW	MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMERELQTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEEFSKERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMDLSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRGDDILTILTEVNYEVSNKDDKKNMGKQMPQPTFTLRKKLVFPSD	Literature-reported	"US patent application no. 6,258,600, Antisense modulation of caspase 8 expression."	0	mRNA	mRNA target	.	.	.	Death effector domain	PF01335	PF01335; DED	.	.	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	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	.	Q14790
TTEVCT0	Caspase-8 (CASP8)	Q14790	CASP8_HUMAN	Peptidase	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	CASP8	"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."	EC 3.4.22.61	5L08; 5JQE; 5H33; 5H31; 4ZBW	MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMERELQTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEEFSKERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMDLSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRGDDILTILTEVNYEVSNKDDKKNMGKQMPQPTFTLRKKLVFPSD	Patented-recorded	Caspase inhibitors: a review of recently patented compounds (2013-2015).Expert Opin Ther Pat. 2018 Jan;28(1):47-59.	15.5	EC:3.4	Peptidase	peptidase C14A family.	3.4.22.61	Acting on peptide bonds (peptidases)	Death effector domain	PF01335	PF01335; DED	.	.	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	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	.	Q14790
TTB6T7O	Caspase-9 (CASP9)	P55211	CASP9_HUMAN	Peptidase	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	CASP9	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.	EC 3.4.22.62	5WVE; 5WVC; 5JUY; 4RHW; 3YGS	MDEADRRLLRRCRLRLVEELQVDQLWDALLSRELFRPHMIEDIQRAGSGSRRDQARQLIIDLETRGSQALPLFISCLEDTGQDMLASFLRTNRQAAKLSKPTLENLTPVVLRPEIRKPEVLRPETPRPVDIGSGGFGDVGALESLRGNADLAYILSMEPCGHCLIINNVNFCRESGLRTRTGSNIDCEKLRRRFSSLHFMVEVKGDLTAKKMVLALLELAQQDHGALDCCVVVILSHGCQASHLQFPGAVYGTDGCPVSVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGSNPEPDATPFQEGLRTFDQLDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSEDLQSLLLRVANAVSVKGIYKQMPGCFNFLRKKLFFKTS	Clinical trial	Potent and selective nonpeptide inhibitors of caspases 3 and 7. J Med Chem. 2001 Jun 7;44(12):2015-26.	16	EC:3.4	Peptidase	peptidase C14A family.	3.4.22.62 	Acting on peptide bonds (peptidases)	Caspase recruitment domain	PF00619	PF00619; CARD	.	.	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	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	.	P55211
TTBUYHA	Extracellular calcium-sensing receptor (CASR)	P41180	CASR_HUMAN	GPCR glutamate	hCasR; Parathyroid cell calciumreceptor; Parathyroid cell calcium-sensing receptor 1; Parathyroid calcium receptor; Parathyroid Cell calcium-sensing receptor; PCaR1; GPRC2A; CaSR	CASR	"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."	.	5K5T; 5K5S; 5FBK; 5FBH	MAFYSCCWVLLALTWHTSAYGPDQRAQKKGDIILGGLFPIHFGVAAKDQDLKSRPESVECIRYNFRGFRWLQAMIFAIEEINSSPALLPNLTLGYRIFDTCNTVSKALEATLSFVAQNKIDSLNLDEFCNCSEHIPSTIAVVGATGSGVSTAVANLLGLFYIPQVSYASSSRLLSNKNQFKSFLRTIPNDEHQATAMADIIEYFRWNWVGTIAADDDYGRPGIEKFREEAEERDICIDFSELISQYSDEEEIQHVVEVIQNSTAKVIVVFSSGPDLEPLIKEIVRRNITGKIWLASEAWASSSLIAMPQYFHVVGGTIGFALKAGQIPGFREFLKKVHPRKSVHNGFAKEFWEETFNCHLQEGAKGPLPVDTFLRGHEESGDRFSNSSTAFRPLCTGDENISSVETPYIDYTHLRISYNVYLAVYSIAHALQDIYTCLPGRGLFTNGSCADIKKVEAWQVLKHLRHLNFTNNMGEQVTFDECGDLVGNYSIINWHLSPEDGSIVFKEVGYYNVYAKKGERLFINEEKILWSGFSREVPFSNCSRDCLAGTRKGIIEGEPTCCFECVECPDGEYSDETDASACNKCPDDFWSNENHTSCIAKEIEFLSWTEPFGIALTLFAVLGIFLTAFVLGVFIKFRNTPIVKATNRELSYLLLFSLLCCFSSSLFFIGEPQDWTCRLRQPAFGISFVLCISCILVKTNRVLLVFEAKIPTSFHRKWWGLNLQFLLVFLCTFMQIVICVIWLYTAPPSSYRNQELEDEIIFITCHEGSLMALGFLIGYTCLLAAICFFFAFKSRKLPENFNEAKFITFSMLIFFIVWISFIPAYASTYGKFVSAVEVIAILAASFGLLACIFFNKIYIILFKPSRNTIEEVRCSTAAHAFKVAARATLRRSNVSRKRSSSLGGSTGSTPSSSISSKSNSEDPFPQPERQKQQQPLALTQQEQQQQPLTLPQQQRSQQQPRCKQKVIFGSGTVTFSLSFDEPQKNAMAHRNSTHQNSLEAQKSSDTLTRHEPLLPLQCGETDLDLTVQETGLQGPVGGDQRPEVEDPEELSPALVVSSSQSFVISGGGSTVTENVVNS	Successful	"Clinical pipeline report, company report or official report of Amgen (2009)."	34	PF00003	GPCR glutamate	G-protein coupled receptor 3 family.	.	.	7 transmembrane sweet-taste receptor of 3 GCPR; Receptor family ligand binding region; Nine Cysteines Domain of family 3 GPCR	PF00003; PF01094; PF07562	PF00003; 7tm_3; PF01094; ANF_receptor; PF07562; NCD3G	9.A.14.7.2	The G-protein-coupled receptor (GPCR) Family	"hsa04621: NOD-like receptor signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action"	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)	.	P41180
TTPS279	Catalase (CAT)	P04040	CATA_HUMAN	Peroxide acceptor oxidoreductase	Human catalase	CAT	"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."	EC 1.11.1.6	1QQW; 1F4J; 1DGH; 1DGG; 1DGF	MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL	Clinical trial	"Evaluation of EUK-189, a synthetic superoxide dismutase/catalase mimetic as a radiation countermeasure. Immunopharmacol Immunotoxicol. 2008;30(2):271-90."	17	EC:1.11	Peroxidases	catalase family.	1.11.1.6	Acting on a peroxide as acceptor	Catalase; Catalase-related immune-responsive	PF00199; PF06628	PF00199; Catalase; PF06628; Catalase-rel	.	.	hsa00380:Tryptophan metabolism; hsa00630:Glyoxylate and dicarboxylate metabolism; hsa01130:Biosynthesis of antibiotics; hsa04068:FoxO signaling pathway; hsa04146:Peroxisome; hsa05014:Amyotrophic lateral sclerosis (ALS)	R-HSA-3299685:Detoxification of Reactive Oxygen Species; R-HSA-74259:Purine catabolism	MetaCyc:MON66-341	P04040
TT5CISB	Cation channel sperm-associated protein 1 (CatSper1)	Q8NEC5	CTSR1_HUMAN	.	hCatSper; CatSper1	CATSPER1	"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."	.	.	MDQNSVPEKAQNEADTNNADRFFRSHSSPPHHRPGHSRALHHYELHHHGVPHQRGESHHPPEFQDFHDQALSSHVHQSHHHSEARNHGRAHGPTGFGLAPSQGAVPSHRSYGEDYHDELQRDGRRHHDGSQYGGFHQQSDSHYHRGSHHGRPQYLGENLSHYSSGVPHHGEASHHGGSYLPHGPNPYSESFHHSEASHLSGLQHDESQHHQVPHRGWPHHHQVHHHGRSRHHEAHQHGKSPHHGETISPHSSVGSYQRGISDYHSEYHQGDHHPSEYHHGDHPHHTQHHYHQTHRHRDYHQHQDHHGAYHSSYLHGDYVQSTSQLSIPHTSRSLIHDAPGPAASRTGVFPYHVAHPRGSAHSMTRSSSTIRSRVTQMSKKVHTQDISTKHSEDWGKEEGQFQKRKTGRLQRTRKKGHSTNLFQWLWEKLTFLIQGFREMIRNLTQSLAFETFIFFVVCLNTVMLVAQTFAEVEIRGEWYFMALDSIFFCIYVVEALLKIIALGLSYFFDFWNNLDFFIMAMAVLDFLLMQTHSFAIYHQSLFRILKVFKSLRALRAIRVLRRLSFLTSVQEVTGTLGQSLPSIAAILILMFTCLFLFSAVLRALFRKSDPKRFQNIFTTIFTLFTLLTLDDWSLIYMDSRAQGAWYIIPILVIYIIIQYFIFLNLVITVLVDSFQTALFKGLEKAKQERAARIQEKLLEDSLTELRAAEPKEVASEGTMLKRLIEKKFGTMTEKQQELLFHYLQLVASVEQEQQKFRSQAAVIDEIVDTTFEAGEEDFRN	Literature-reported	Pharmacological targeting of native CatSper channels reveals a required role in maintenance of sperm hyperactivation. PLoS One. 2009 Aug 31;4(8):e6844.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1300642: Sperm Motility And Taxes	.	Q8NEC5
TTOEGC4	Cation channel sperm-associated protein 2 (CatSper2)	Q96P56	CTSR2_HUMAN	.	CatSper2	CATSPER2	"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."	.	.	MAAYQQEEQMQLPRADAIRSRLIDTFSLIEHLQGLSQAVPRHTIRELLDPSRQKKLVLGDQHQLVRFSIKPQRIEQISHAQRLLSRLHVRCSQRPPLSLWAGWVLECPLFKNFIIFLVFLNTIILMVEIELLESTNTKLWPLKLTLEVAAWFILLIFILEILLKWLSNFSVFWKSAWNVFDFVVTMLSLLPEVVVLVGVTGQSVWLQLLRICRVLRSLKLLAQFRQIQIIILVLVRALKSMTFLLMLLLIFFYIFAVTGVYVFSEYTRSPRQDLEYHVFFSDLPNSLVTVFILFTLDHWYALLQDVWKVPEVSRIFSSIYFILWLLLGSIIFRSIIVAMMVTNFQNIRKELNEEMARREVQLKADMFKRQIIQRRKNMSHEALTSSHSKIEDSSRGASQQRESLDLSEVSEVESNYGATEEDLITSASKTEETLSKKREYQSSSCVSSTSSSYSSSSESRFSESIGRLDWETLVHENLPGLMEMDQDDRVWPRDSLFRYFELLEKLQYNLEERKKLQEFAVQALMNLEDK	Literature-reported	The CatSper channel mediates progesterone-induced Ca2+ influx in human sperm. Nature. 2011 Mar 17;471(7338):382-6.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1300642: Sperm Motility And Taxes	.	Q96P56
TTP52ZV	Cation channel sperm-associated protein 3 (CatSper3)	Q86XQ3	CTSR3_HUMAN	.	One-repeat calcium channel-like protein; CatSper3; Ca(v)-like protein	CATSPER3	"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."	.	.	MSQHRHQRHSRVISSSPVDTTSVGFCPTFKKFKRNDDECRAFVKRVIMSRFFKIIMISTVTSNAFFMALWTSYDIRYRLFRLLEFSEIFFVSICTSELSMKVYVDPINYWKNGYNLLDVIIIIVMFLPYALRQLMGKQFTYLYIADGMQSLRILKLIGYSQGIRTLITAVGQTVYTVASVLLLLFLLMYIFAILGFCLFGSPDNGDHDNWGNLAAAFFTLFSLATVDGWTDLQKQLDNREFALSRAFTIIFILLASFIFLNMFVGVMIMHTEDSIRKFERELMLEQQEMLMGEKQVILQRQQEEISRLMHIQKNADCTSFSELVENFKKTLSHTDPMVLDDFGTSLPFIDIYFSTLDYQDTTVHKLQELYYEIVHVLSLMLEDLPQEKPQSLEKVDEK	Literature-reported	The CatSper channel mediates progesterone-induced Ca2+ influx in human sperm. Nature. 2011 Mar 17;471(7338):382-6.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1300642: Sperm Motility And Taxes	.	Q86XQ3
TTXUBN2	Caveolin 1 (CAV1)	Q03135	CAV1_HUMAN	Caveolin protein	Caveolin1; Caveolin-1; Cav-1	CAV1	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.	.	.	MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADELSEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTVCDPLFEAVGKIFSNVRINLQKEI	Literature-reported	Caveolin-1: An Oxidative Stress-Related Target for Cancer Prevention. Oxid Med Cell Longev. 2017;2017:7454031.	.	TC=8.A.26	Caveolin family	caveolin family.	.	.	Caveolin	PF01146	PF01146; Caveolin	8.A.26.1.1	The Caveolin (Caveolin) Family	hsa04144: Endocytosis; hsa04510: Focal adhesion; hsa05020: Prion disease; hsa05100: Bacterial invasion of epithelial cells; hsa05205: Proteoglycans in cancer; hsa05416: Viral myocarditis; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-163560: Triglyceride catabolism; R-HSA-203615: eNOS activation; R-HSA-203641: NOSTRIN mediated eNOS trafficking; R-HSA-210991: Basigin interactions; R-HSA-4641262: Disassembly of the destruction complex and recruitment of AXIN to the membrane; R-HSA-5218920: VEGFR2 mediated vascular permeability; R-HSA-8980692: RHOA GTPase cycle; R-HSA-9009391: Extra-nuclear estrogen signaling; R-HSA-9013026: RHOB GTPase cycle; R-HSA-9013106: RHOC GTPase cycle; R-HSA-9013148: CDC42 GTPase cycle; R-HSA-9013149: RAC1 GTPase cycle; R-HSA-9013404: RAC2 GTPase cycle; R-HSA-9013405: RHOD GTPase cycle; R-HSA-9013406: RHOQ GTPase cycle; R-HSA-9013407: RHOH GTPase cycle; R-HSA-9013408: RHOG GTPase cycle; R-HSA-9013409: RHOJ GTPase cycle; R-HSA-9013423: RAC3 GTPase cycle; R-HSA-9035034: RHOF GTPase cycle; R-HSA-9617828: FOXO-mediated transcription of cell cycle genes; R-HSA-9696264: RND3 GTPase cycle; R-HSA-9696270: RND2 GTPase cycle; R-HSA-9696273: RND1 GTPase cycle; R-HSA-9755779: SARS-CoV-2 targets host intracellular signalling and regulatory pathways; R-HSA-9767675: SARS-CoV-1-host interactions	.	Q03135
TTHJVXA	Clostridium botulinum Botulinum neurotoxin (CB bot)	P0DPI0; P10844; Q00496	BXA1_CLOBH; BXB_CLOBO; BXE_CLOBO	.	Botulinum neurotoxin; Bontoxilysin; BoNT	CB botA	"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."	.	.	MPFVNKQFNYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLFFSPSEDNFTNDLNKGEEITSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKYELDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVSTTDKIADITIIIPYIGPALNIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRNEKWDEVYKYIVTNWLAKVNTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMININKFLNQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLLSTFTEYIKNIINTSILNLRYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFSTSFWIRIPKYFNSISLNNEYTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNRLNNSKIYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGDYLQYDKPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGTKFIIKKYASGNKDNIVRNNDRVYINVVVKNKEYRLATNASQAGVEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVASNWYNRQIERSSRTLGCSWEFIPVDDGWGERPL	Literature-reported	Botulinum Toxin for the Treatment of Neuropathic Pain. Toxins (Basel). 2017 Aug 24;9(9). pii: E260.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-5250968: Toxicity of botulinum toxin type A (botA)	.	P0DPI1
TT7QT13	Signal transduction protein CBL (CBL)	P22681	CBL_HUMAN	Acyltransferase	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	CBL	"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."	EC 2.3.2.27	5O76; 5J3X; 5HL0; 5HKZ; 5HKY	MAGNVKKSSGAGGGSGSGGSGSGGLIGLMKDAFQPHHHHHHHLSPHPPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPFDPRGSGSLLRQGAEGAPSPNYDDDDDERADDTLFMMKELAGAKVERPPSPFSMAPQASLPPVPPRLDLLPQRVCVPSSASALGTASKAASGSLHKDKPLPVPPTLRDLPPPPPPDRPYSVGAESRPQRRPLPCTPGDCPSRDKLPPVPSSRLGDSWLPRPIPKVPVSAPSSSDPWTGRELTNRHSLPFSLPSQMEPRPDVPRLGSTFSLDTSMSMNSSPLVGPECDHPKIKPSSSANAIYSLAARPLPVPKLPPGEQCEGEEDTEYMTPSSRPLRPLDTSQSSRACDCDQQIDSCTYEAMYNIQSQAPSITESSTFGEGNLAAAHANTGPEESENEDDGYDVPKPPVPAVLARRTLSDISNASSSFGWLSLDGDPTTNVTEGSQVPERPPKPFPRRINSERKAGSCQQGSGPAASAATASPQLSSEIENLMSQGYSYQDIQKALVIAQNNIEMAKNILREFVSISSPAHVAT	Literature-reported	c-Cbl is a suppressor of the neu oncogene. J Biol Chem. 2000 Nov 10;275(45):35532-9.	.	EC:2.3	Carbon-nitrogen ligase	.	2.3.2.27 	Acyltransferases	"CBL proto-oncogene N-terminal domain 1; CBL proto-oncogene N-terminus, EF hand-like domain; CBL proto-oncogene N-terminus, SH2-like domain; UBA/TS-N domain"	PF02262; PF02761; PF02762; PF00627	PF02262; Cbl_N; PF02761; Cbl_N2; PF02762; Cbl_N3; PF00627; UBA	.	.	hsa04012: ErbB signaling pathway; hsa04120: Ubiquitin mediated proteolysis; hsa04144: Endocytosis; hsa04910: Insulin signaling pathway; hsa05100: Bacterial invasion of epithelial cells; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05220: Chronic myeloid leukemia	R-HSA-1059683: Interleukin-6 signaling; R-HSA-1236382: Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-1295596: Spry regulation of FGF signaling; R-HSA-1433559: Regulation of KIT signaling; R-HSA-182971: EGFR downregulation; R-HSA-2173789: TGF-beta receptor signaling activates SMADs; R-HSA-5637810: Constitutive Signaling by EGFRvIII; 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-6807004: Negative regulation of MET activity; R-HSA-8849469: PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis; R-HSA-8875360: InlB-mediated entry of Listeria monocytogenes into host cell; R-HSA-912631: Regulation of signaling by CBL; R-HSA-9706369: Negative regulation of FLT3; R-HSA-9706377: FLT3 signaling by CBL mutants	.	P22681
TTHRAIJ	CBLB messenger RNA (CBLB mRNA)	Q13191	CBLB_HUMAN	.	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	CBLB	"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)."	EC 2.3.2.27	.	MANSMNGRNPGGRGGNPRKGRILGIIDAIQDAVGPPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFDPRDEGSRCCSIIDPFGMPMLDLDDDDDREESLMMNRLANVRKCTDRQNSPVTSPGSSPLAQRRKPQPDPLQIPHLSLPPVPPRLDLIQKGIVRSPCGSPTGSPKSSPCMVRKQDKPLPAPPPPLRDPPPPPPERPPPIPPDNRLSRHIHHVESVPSRDPPMPLEAWCPRDVFGTNQLVGCRLLGEGSPKPGITASSNVNGRHSRVGSDPVLMRKHRRHDLPLEGAKVFSNGHLGSEEYDVPPRLSPPPPVTTLLPSIKCTGPLANSLSEKTRDPVEEDDDEYKIPSSHPVSLNSQPSHCHNVKPPVRSCDNGHCMLNGTHGPSSEKKSNIPDLSIYLKGDVFDSASDPVPLPPARPPTRDNPKHGSSLNRTPSDYDLLIPPLGEDAFDALPPSLPPPPPPARHSLIEHSKPPGSSSRPSSGQDLFLLPSDPFVDLASGQVPLPPARRLPGENVKTNRTSQDYDQLPSCSDGSQAPARPPKPRPRRTAPEIHHRKPHGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFPPPVSPRLNL	Clinical trial	"Clinical pipeline report, company report or official report of Apeiron Biologics."	.	.	.	.	.	.	.	.	.	.	.	hsa04012: ErbB signaling pathway; hsa04120: Ubiquitin mediated proteolysis; hsa04144: Endocytosis; hsa04625: C-type lectin receptor signaling pathway; hsa04660: T cell receptor signaling pathway; hsa04910: Insulin signaling pathway; hsa05162: Measles	R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	Q13191
TTGT3RQ	E3 ubiquitin protein ligase CBLB (CBLB)	Q13191	CBLB_HUMAN	Acyltransferase	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	CBLB	"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."	EC 2.3.2.27	3ZNI; 3VGO; 3PFV; 2OOB; 2OOA	MANSMNGRNPGGRGGNPRKGRILGIIDAIQDAVGPPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFDPRDEGSRCCSIIDPFGMPMLDLDDDDDREESLMMNRLANVRKCTDRQNSPVTSPGSSPLAQRRKPQPDPLQIPHLSLPPVPPRLDLIQKGIVRSPCGSPTGSPKSSPCMVRKQDKPLPAPPPPLRDPPPPPPERPPPIPPDNRLSRHIHHVESVPSRDPPMPLEAWCPRDVFGTNQLVGCRLLGEGSPKPGITASSNVNGRHSRVGSDPVLMRKHRRHDLPLEGAKVFSNGHLGSEEYDVPPRLSPPPPVTTLLPSIKCTGPLANSLSEKTRDPVEEDDDEYKIPSSHPVSLNSQPSHCHNVKPPVRSCDNGHCMLNGTHGPSSEKKSNIPDLSIYLKGDVFDSASDPVPLPPARPPTRDNPKHGSSLNRTPSDYDLLIPPLGEDAFDALPPSLPPPPPPARHSLIEHSKPPGSSSRPSSGQDLFLLPSDPFVDLASGQVPLPPARRLPGENVKTNRTSQDYDQLPSCSDGSQAPARPPKPRPRRTAPEIHHRKPHGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFPPPVSPRLNL	Literature-reported	Targeting CBLB as a potential therapeutic approach for disseminated candidiasis. Nat Med. 2016 Aug;22(8):906-14.	.	EC:2.3	Carbon-nitrogen ligase	.	2.3.2.27 	Acyltransferases	"CBL proto-oncogene N-terminal domain 1; CBL proto-oncogene N-terminus, EF hand-like domain; CBL proto-oncogene N-terminus, SH2-like domain"	PF02262; PF02761; PF02762	PF02262; Cbl_N; PF02761; Cbl_N2; PF02762; Cbl_N3	.	.	hsa04012: ErbB signaling pathway; hsa04120: Ubiquitin mediated proteolysis; hsa04144: Endocytosis; hsa04625: C-type lectin receptor signaling pathway; hsa04660: T cell receptor signaling pathway; hsa04910: Insulin signaling pathway; hsa05162: Measles	R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	Q13191
TTVG0SN	S-nitrosoglutathione reductase (CBR1)	P16152	CBR1_HUMAN	Short-chain dehydrogenases reductase	ProstaglandinE(2) 9reductase; Prostaglandin 9ketoreductase; NADPHdependent carbonyl reductase 1; Carbonyl reductase [NADPH] 1; CBR1; 15hydroxyprostaglandin dehydrogenase [NADP(+)]	CBR1	"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."	EC 1.1.1.184	4Z3D; 3BHM; 3BHJ; 3BHI; 2PFG	MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTKKGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW	Clinical trial	"Mechanism of inhibition for N6022, a first-in-class drug targeting S-nitrosoglutathione reductase. Biochemistry. 2012 Mar 13;51(10):2157-68."	21	.	.	.	.	.	.	.	.	.	.	hsa00590: Arachidonic acid metabolism; hsa00790: Folate biosynthesis; hsa00980: Metabolism of xenobiotics by cytochrome P450; hsa01100: Metabolic pathways; hsa05204: Chemical carcinogenesis - DNA adducts; hsa05208: Chemical carcinogenesis - reactive oxygen species	R-HSA-2162123: Synthesis of Prostaglandins (PG) and Thromboxanes (TX)	.	P16152
TTVZJ7G	Cystathionine beta-synthase (CBS)	P35520	CBS_HUMAN	Alpha-carbonic anhydrase	Serine sulfhydrase; Beta-thionase	CBS	"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."	EC 4.2.1.22	5MMS; 4UUU; 4PCU; 4L3V; 4L28	MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLLNFVAAQERDQK	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1443).	0	EC:4.2	Carbon-oxygen lyases	cysteine synthase/cystathionine beta-synthase family.	4.2.1.22 	Carbon-oxygen lyases	CBS domain; Pyridoxal-phosphate dependent enzyme	PF00571; PF00291	PF00571; CBS; PF00291; PALP	.	.	"hsa00260:Glycine, serine and threonine metabolism; hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01230:Biosynthesis of amino acids"	"R-HSA-1614603: Cysteine formation from homocysteine; R-HSA-2408508: Metabolism of ingested SeMet, Sec, MeSec into H2Se"	MetaCyc:HS08461-MON	P35520
TTBN3HC	Chromobox protein homolog 7 (CBX7)	O95931	CBX7_HUMAN	.	Chromobox 7	CBX7	"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."	.	5EPJ; 4MN3; 3GS2; 2L1B; 2L12	MELSAIGEQVFAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHILDPRLVMAYEEKEERDRASGYRKRGPKPKRLLLQRLYSMDLRSSHKAKGKEKLCFSLTCPLGSGSPEGVVKAGAPELVDKGPLVPTLPFPLRKPRKAHKYLRLSRKKFPPRGPNLESHSHRRELFLQEPPAPDVLQAAGEWEPAAQPPEEEADADLAEGPPPWTPALPSSEVTVTDITANSITVTFREAQAAEGFFRDRSGKF	Literature-reported	CBX7 is a glioma prognostic marker and induces G1/S arrest via the silencing of CCNE1. Oncotarget. 2017 Apr 18;8(16):26637-26647.	.	.	.	.	.	.	CBX family C-terminal motif; Chromo (CHRromatin Organisation MOdifier) domain	PF17218; PF00385	PF17218; CBX7_C; PF00385; Chromo	.	.	.	.	.	O95931
TT90CMU	Cholecystokinin (CCK)	P06307	CCKN_HUMAN	Gastrin cholecystokinin	Procholecystokinin; CCK	CCK	"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."	.	.	MNSGVCLCVLMAVLAAGALTQPVPPADPAGSGLQRAEEAPRRQLRVSQRTDGESRAHLGALLARYIQQARKAPSGRMSIVKNLQNLDPSHRISDRDYMGWMDFGRRSAEEYEYPS	Literature-reported	Role of cholecystokinin in the development and progression of acute pancreatitis and the potential of therapeutic application of cholecystokinin re... Digestion. 1999;60 Suppl 1:69-74.	.	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04911: Insulin secretion; hsa04972: Pancreatic secretion	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-416476: G alpha (q) signalling events	.	P06307
TTCG0AL	Cholecystokinin receptor type A (CCKAR)	P32238	CCKAR_HUMAN	GPCR rhodopsin	CCKAR; CCK-AR; CCK-A receptor	CCKAR	"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."	.	1PB2; 1HZN; 1D6G	MDVVDSLLVNGSNITPPCELGLENETLFCLDQPRPSKEWQPAVQILLYSLIFLLSVLGNTLVITVLIRNKRMRTVTNIFLLSLAVSDLMLCLFCMPFNLIPNLLKDFIFGSAVCKTTTYFMGTSVSVSTFNLVAISLERYGAICKPLQSRVWQTKSHALKVIAATWCLSFTIMTPYPIYSNLVPFTKNNNQTANMCRFLLPNDVMQQSWHTFLLLILFLIPGIVMMVAYGLISLELYQGIKFEASQKKSAKERKPSTTSSGKYEDSDGCYLQKTRPPRKLELRQLSTGSSSRANRIRSNSSAANLMAKKRVIRMLIVIVVLFFLCWMPIFSANAWRAYDTASAERRLSGTPISFILLLSYTSSCVNPIIYCFMNKRFRLGFMATFPCCPNPGPPGARGEVGEEEEGGTTGASLSRFSYSHMSASVPPQ	Clinical trial	Pharmacological properties of lorglumide as a member of a new class of cholecystokinin antagonists. Arzneimittelforschung. 1987 Nov;37(11):1265-8.	21	.	.	.	.	.	.	.	.	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04911:Insulin secretion; hsa04972:Pancreatic secretion	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events	.	P32238
TTVFO0U	Gastrin/cholecystokinin type B receptor (CCKBR)	P32239	GASR_HUMAN	GPCR rhodopsin	Cholecystokinin-2 receptor; CCKRB; CCK2-R; CCK-BR; CCK-B receptor	CCKBR	"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."	.	1L4T	MELLKLNRSVQGTGPGPGASLCRPGAPLLNSSSVGNLSCEPPRIRGAGTRELELAIRITLYAVIFLMSVGGNMLIIVVLGLSRRLRTVTNAFLLSLAVSDLLLAVACMPFTLLPNLMGTFIFGTVICKAVSYLMGVSVSVSTLSLVAIALERYSAICRPLQARVWQTRSHAARVIVATWLLSGLLMVPYPVYTVVQPVGPRVLQCVHRWPSARVRQTWSVLLLLLLFFIPGVVMAVAYGLISRELYLGLRFDGDSDSDSQSRVRNQGGLPGAVHQNGRCRPETGAVGEDSDGCYVQLPRSRPALELTALTAPGPGSGSRPTQAKLLAKKRVVRMLLVIVVLFFLCWLPVYSANTWRAFDGPGAHRALSGAPISFIHLLSYASACVNPLVYCFMHRRFRQACLETCARCCPRPPRARPRALPDEDPPTPSIASLSRLSYTTISTLGPG	Successful	Functional interactions between endocannabinoid and CCK neurotransmitter systems may be critical for extinction learning. Neuropsychopharmacology. 2009 Jan;34(2):509-21.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04971:Gastric acid secretion	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	.	P32239
TTCF05Y	Small-inducible cytokine A11 (CCL11)	P51671	CCL11_HUMAN	Cytokine: CC chemokine	Smallinducible cytokine A11; SCYA11; Eotaxin; Eosinophil chemotactic protein; CC motif chemokine 11; C-C motif chemokine 11	CCL11	"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."	.	2MPM; 2EOT; 1EOT	MKVSAALLWLLLIAAAFSPQGLAGPASVPTTCCFNLANRKIPLQRLESYRRITSGKCPQKAVIFKTKLAKDICADPKKKWVQDSMKYLDQKSPTPKP	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	21	Cytokine	.	intercrine beta (chemokine CC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway; hsa04657: IL-17 signaling pathway; hsa05310: Asthma	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling	.	P51671
TTMPHAE	C-C motif chemokine 17 (CCL17)	Q92583	CCL17_HUMAN	.	CC chemokine TARC; Small-inducible cytokine A17; Thymus and activation-regulated chemokine	CCL17	"Chemokine, which displays chemotactic activity for T lymphocytes, preferentially Th2 cells, but not monocytes or granulocytes. Therefore plays an important role in a wide range of inflammatory and immunological processes (PubMed:8702936, PubMed:9169480). Acts by binding to CCR4 at T-cell surface (PubMed:9169480, PubMed:10540332). Mediates GM-CSF/CSF2-driven pain and inflammation (PubMed:27525438). In the brain, required to maintain the typical, highly branched morphology of hippocampal microglia under homeostatic conditions. May be important for the appropriate adaptation of microglial morphology and synaptic plasticity to acute lipopolysaccharide (LPS)-induced neuroinflammation (By similarity). Plays a role in wound healing, mainly by inducing fibroblast migration into the wound (By similarity). {ECO:0000250|UniProtKB:Q9WUZ6, ECO:0000269|PubMed:10540332, ECO:0000269|PubMed:27525438, ECO:0000269|PubMed:8702936, ECO:0000269|PubMed:9169480}."	.	1NR2;1NR4;5WK3;7S4N;7SCV;8FJ2;8SKK	MAPLKMLALVTLLLGASLQHIHAARGTNVGRECCLEYFKGAIPLRKLKTWYQTSEDCSRDAIVFVTVQGRAICSDPNNKRVKNAVKYLQSLERS	Clinical trial	Therapeutic options for targeting inflammatory osteoarthritis pain. Nat Rev Rheumatol. 2019 Jun;15(6):355-363.	.	.	.	.	.	.	.	.	.	.	.	hsa:6361	R-HSA-380108;	.	Q92583;
TTNAY0P	Monocyte chemotactic and activating factor (CCL2)	P13500	CCL2_HUMAN	Cytokine: CC chemokine	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	CCL2	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.	.	4ZK9; 4R8I; 4DN4; 3IFD; 2NZ1	MKVSAALLCLLLIAATFIPQGLAQPDAINAPVTCCYNFTNRKISVQRLASYRRITSSKCPKEAVIFKTIVAKEICADPKQKWVQDSMDHLDKQTQTPKT	Clinical trial	Bindarit: an anti-inflammatory small molecule that modulates the NF B pathway. Cell Cycle. 2012 Jan 1;11(1):159-69.	25	Cytokine	Cytokine: CC chemokine	intercrine beta (chemokine CC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	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	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-380994:ATF4 activates genes	.	P13500
TT2XAZY	Liver and activation-regulated chemokine (CCL20)	P78556	CCL20_HUMAN	Cytokine: CC chemokine	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	CCL20	"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."	.	5UR7; 2JYO; 2HCI; 1M8A	MCCTKSLLLAALMSVLLLHLCGESEAASNFDCCLGYTDRILHPKFIVGFTRQLANEGCDINAIIFHTKKKLSVCANPKQTWVKYIVRLLSKKVKNM	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	Cytokine	Cytokine: intecrine/chemokine	intercrine beta (chemokine CC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway; hsa04657: IL-17 signaling pathway; hsa04668: TNF signaling pathway; hsa05323: Rheumatoid arthritis	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-418594: G alpha (i) signalling events; R-HSA-6783783: Interleukin-10 signaling	.	P78556
TTLZK1U	Secondary lymphoid-tissue chemokine (CCL21)	O00585	CCL21_HUMAN	Cytokine: CC chemokine	UNQ784/PRO1600; Small-inducible cytokine A21; SLC; SCYA21; C-C motif chemokine 21; Beta-chemokine exodus-2; 6Ckine	CCL21	"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."	.	5EKI; 2L4N	MAQSLALSLLILVLAFGIPRTQGSDGGAQDCCLKYSQRKIPAKVVRSYRKQEPSLGCSIPAILFLPRKRSQAELCADPKELWVQQLMQHLDKTPSPQKPAQGCRKDRGASKTGKKGKGSKGCKRTERSQTPKGP	Literature-reported	Genetic markers of cardiovascular disease in rheumatoid arthritis. Mediators Inflamm. 2012;2012:574817. 	.	Cytokine	.	intercrine beta (chemokine CC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway; hsa04064: NF-kappa B signaling pathway	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-418594: G alpha (i) signalling events	.	O00585
TTBTWI1	Macrophage-derived chemokine (MDC)	O00626	CCL22_HUMAN	Cytokine: CC chemokine	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	CCL22	"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."	.	.	MDRLQTALLVVLVLLAVALQATEAGPYGANMEDSVCCRDYVRYRLPLRVVKHFYWTSDSCPRPGVVLLTFRDKEICADPRVPWVKMILNKLSQ	Literature-reported	Mononuclear cell-infiltrate inhibition by blocking macrophage-derived chemokine results in attenuation of developing crescentic glomerulonephritis. Am J Pathol. 2003 Apr;162(4):1061-73.	.	Cytokine	Cytokine: intecrine/chemokine	intercrine beta (chemokine CC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway; hsa04625: C-type lectin receptor signaling pathway	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-6783783: Interleukin-10 signaling; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling	.	O00626
TTHAPJK	C-C motif chemokine 23 (CCL23)	P55773	CCL23_HUMAN	Cytokine: CC chemokine	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	CCL23	"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."	.	1G91	MKVSVAALSCLMLVTALGSQARVTKDAETEFMMSKLPLENPVLLDRFHATSADCCISYTPRSIPCSLLESYFETNSECSKPGVIFLTKKGRRFCANPSDKQVQVCVRMLKLDTRIKTRKN	Literature-reported	Serum CCL23 levels are increased in patients with systemic sclerosis. Arch Dermatol Res. 2011 Jan;303(1):29-34.	.	Cytokine	.	intercrine beta (chemokine CC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway	R-HSA-416476: G alpha (q) signalling events; R-HSA-418594: G alpha (i) signalling events; R-HSA-444473: Formyl peptide receptors bind formyl peptides and many other ligands	.	P55773
TT8I4WB	Macrophage inflammatory protein 1-alpha (CCL3)	P10147	CCL3_HUMAN	Cytokine: CC chemokine	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	CCL3	"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."	.	5D65; 5COR; 4ZKB; 4RA8; 3KBX	MQVSTAALAVLLCTMALCNQFSASLAADTPTACCFSYTSRQIPQNFIADYFETSSQCSKPGVIFLTKRSRQVCADPSEEWVQKYVSDLELSA	Clinical trial	Macrophage inflammatory protein derivative ECI301 enhances the alarmin-associated abscopal benefits of tumor radiotherapy. Cancer Res. 2014 Sep 15;74(18):5070-8.	17	Cytokine	Cytokine: CC chemokine	intercrine beta (chemokine CC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	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	R-HSA-380108:Chemokine receptors bind chemokines	.	P10147
TT9DWLC	T-cell-specific protein RANTES (CCL5)	P13501	CCL5_HUMAN	Cytokine: CC chemokine	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	CCL5	"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."	.	6FGP; 6C6D; 5UIW; 5L2U; 5DNF	MKVSAAALAVILIATALCAPASASPYSSDTTPCCFAYIARPLPRAHIKEYFYTSGKCSNPAVVFVTRKNRQVCANPEKKWVREYINSLEMS	Clinical trial	"Handbook of Therapeutic Antibodies. Stefan D bel, Janice M. Reichert, 2014. Page(1021)."	17	Cytokine	Cytokine: CC chemokine	intercrine beta (chemokine CC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	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	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P13501
TTPK79J	Cellular communication network factor 1 (CCN1)	O00622	CCN1_HUMAN	.	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	CCN1	"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."	.	4D11; 4D0Z	MSSRIARALALVVTLLHLTRLALSTCPAACHCPLEAPKCAPGVGLVRDGCGCCKVCAKQLNEDCSKTQPCDHTKGLECNFGASSTALKGICRAQSEGRPCEYNSRIYQNGESFQPNCKHQCTCIDGAVGCIPLCPQELSLPNLGCPNPRLVKVTGQCCEEWVCDEDSIKDPMEDQDGLLGKELGFDASEVELTRNNELIAVGKGSSLKRLPVFGMEPRILYNPLQGQKCIVQTTSWSQCSKTCGTGISTRVTNDNPECRLVKETRICEVRPCGQPVYSSLKKGKKCSKTKKSPEPVRFTYAGCLSVKKYRPKYCGSCVDGRCCTPQLTRTVKMRFRCEDGETFSKNVMMIQSCKCNYNCPHANEAAFPFYRLFNDIHKFRD	Literature-reported	CCN1: a novel target for pancreatic cancer. J Cell Commun Signal. 2011 Jun;5(2):123-4.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation	.	O00622
TTIL516	CCN2 messenger RNA (CCN2 mRNA)	P29279	CCN2_HUMAN	.	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	CCN2	"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."	.	.	MTAASMGPVRVAFVVLLALCSRPAVGQNCSGPCRCPDEPAPRCPAGVSLVLDGCGCCRVCAKQLGELCTERDPCDPHKGLFCHFGSPANRKIGVCTAKDGAPCIFGGTVYRSGESFQSSCKYQCTCLDGAVGCMPLCSMDVRLPSPDCPFPRRVKLPGKCCEEWVCDEPKDQTVVGPALAAYRLEDTFGPDPTMIRANCLVQTTEWSACSKTCGMGISTRVTNDNASCRLEKQSRLCMVRPCEADLEENIKKGKKCIRTPKISKPIKFELSGCTSMKTYRAKFCGVCTDGRCCTPHRTTTLPVEFKCPDGEVMKKNMMFIKTCACHYNCPGDNDIFESLYYRKMYGDMA	Clinical trial	A Placebo-controlled Study of PF-06473871 (Anti-Connective Tissue Growth Factor Antisense Oligonucleotide) in Reducing Hypertrophic Skin Scarring. Plast Reconstr Surg Glob Open. 2018 Sep 6;6(9):e1861.	.	.	.	.	.	.	.	.	.	.	.	hsa04371: Apelin signaling pathway; hsa04390: Hippo signaling pathway	R-HSA-2032785: YAP1- and WWTR1 (TAZ)-stimulated gene expression; R-HSA-8951671: RUNX3 regulates YAP1-mediated transcription	.	P29279
TTAMQ62	Cyclin A2 (CCNA2)	P20248	CCNA2_HUMAN	.	Cyclin-A2; Cyclin-A; Cyclin A; CCNA	CCNA2	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.	.	6GVA; 6ATH; 5NEV; 5LMK; 5IF1	MLGNSAPGPATREAGSALLALQQTALQEDQENINPEKAAPVQQPRTRAALAVLKSGNPRGLAQQQRPKTRRVAPLKDLPVNDEHVTVPPWKANSKQPAFTIHVDEAEKEAQKKPAESQKIEREDALAFNSAISLPGPRKPLVPLDYPMDGSFESPHTMDMSIILEDEKPVSVNEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKNSKYHGVSLLNPPETLNL	Literature-reported	"Pyrido[2,3-d]pyrimidin-7-one inhibitors of cyclin-dependent kinases. J Med Chem. 2000 Nov 30;43(24):4606-16."	2	.	.	cyclin family. Cyclin AB subfamily.	.	.	"Cyclin, C-terminal domain; Cyclin, N-terminal domain; N-terminal region of cyclin_N"	PF02984; PF00134; PF16500	PF02984; Cyclin_C; PF00134; Cyclin_N; PF16500; Cyclin_N2	.	.	hsa03030:DNA replication; hsa03410:Base excision repair; hsa03420:Nucleotide excision repair; hsa03430:Mismatch repair; hsa04110:Cell cycle; hsa05161:Hepatitis B; hsa05166:HTLV-I infection	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	.	P20248
TT9P6OW	G2/mitotic-specific cyclin B1 (CCNB1)	P14635	CCNB1_HUMAN	Eukaryotic nuclear pore complex	G2/mitotic-specific cyclin-B1; Cyclin B1; CCNB	CCNB1	Essential for the control of the cell cycle at the G2/M (mitosis) transition.	.	6GU4; 6GU3; 6GU2; 5LQF; 5HQ0	MALRVTRNSKINAENKAKINMAGAKRVPTAPAATSKPGLRPRTALGDIGNKVSEQLQAKMPMKKEAKPSATGKVIDKKLPKPLEKVPMLVPVPVSEPVPEPEPEPEPEPVKEEKLSPEPILVDTASPSPMETSGCAPAEEDLCQAFSDVILAVNDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVRPKYLLGREVTGNMRAILIDWLVQVQMKFRLLQETMYMTVSIIDRFMQNNCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTDNTYTKHQIRQMEMKILRALNFGLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELTMLDYDMVHFPPSQIAAGAFCLALKILDNGEWTPTLQHYLSYTEESLLPVMQHLAKNVVMVNQGLTKHMTVKNKYATSKHAKISTLPQLNSALVQDLAKAVAKV	Patented-recorded	"Discovery of novel CDK1 inhibitors by combining pharmacophore modeling, QSAR analysis and in silico screening followed by in vitro bioassay. Eur J Med Chem. 2010 Sep;45(9):4316-30."	15.5	TC=1.I.1	.	cyclin family. Cyclin AB subfamily.	.	.	"Cyclin, C-terminal domain; Cyclin, N-terminal domain"	PF02984; PF00134	PF02984; Cyclin_C; PF00134; Cyclin_N	1.I.1.1.3	The Eukaryotic Nuclear Pore Complex (E-NPC) Family	hsa04068:FoxO signaling pathway; hsa04110:Cell cycle; hsa04114:Oocyte meiosis; hsa04115:p53 signaling pathway; hsa04914:Progesterone-mediated oocyte maturation	"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"	.	P14635
TTFCJ7S	G1/S-specific cyclin-D1 (CCND1)	P24385	CCND1_HUMAN	.	PRAD1 oncogene; PRAD1; Cyclin D1; BCL1; BCL-1 oncogene; BCL-1; B-cell lymphoma 1 protein	CCND1	"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."	.	5VZU; 2W9Z; 2W9F; 2W99; 2W96	MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	cyclin family. Cyclin D subfamily.	.	.	"Cyclin, C-terminal domain; Cyclin, N-terminal domain"	PF02984; PF00134	PF02984; Cyclin_C; PF00134; Cyclin_N	.	.	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	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	.	P24385
TT1JXNR	Cyclin D (CCND3)	P30281	CCND3_HUMAN	.	G1/S-specific cyclin-D3	CCND3	"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."	.	3G33	MELLCCEGTRHAPRAGPDPRLLGDQRVLQSLLRLEERYVPRASYFQCVQREIKPHMRKMLAYWMLEVCEEQRCEEEVFPLAMNYLDRYLSCVPTRKAQLQLLGAVCMLLASKLRETTPLTIEKLCIYTDHAVSPRQLRDWEVLVLGKLKWDLAAVIAHDFLAFILHRLSLPRDRQALVKKHAQTFLALCATDYTFAMYPPSMIATGSIGAAVQGLGACSMSGDELTELLAGITGTEVDCLRACQEQIEAALRESLREASQTSSSPAPKAPRGSSSQGPSQTSTPTDVTAIHL	Literature-reported	Cyclin D activates the Rb tumor suppressor by mono-phosphorylation. Elife. 2014 Jun 4;3.	.	.	.	cyclin family. Cyclin D subfamily.	.	.	"Cyclin, C-terminal domain; Cyclin, N-terminal domain"	PF02984; PF00134	PF02984; Cyclin_C; PF00134; Cyclin_N	.	.	hsa04110: Cell cycle; hsa04115: p53 signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04218: Cellular senescence; hsa04310: Wnt signaling pathway; hsa04390: Hippo signaling pathway; hsa04510: Focal adhesion; hsa04630: JAK-STAT signaling pathway; hsa05162: Measles; hsa05164: Influenza A; hsa05165: Human papillomavirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05200: Pathways in cancer; hsa05203: Viral carcinogenesis; hsa05207: Chemical carcinogenesis - receptor activation	"R-HSA-381340: Transcriptional regulation of white adipocyte differentiation; R-HSA-5687128: MAPK6/MAPK4 signaling; R-HSA-69231: Cyclin D associated events in G1; R-HSA-8934593: Regulation of RUNX1 Expression and Activity; R-HSA-9661069: Defective binding of RB1 mutants to E2F1,(E2F2, E2F3); R-HSA-9754119: Drug-mediated inhibition of CDK4/CDK6 activity"	.	P30281
TTCEJ4F	G1/S-specific cyclin-E1 (CCNE1)	P24864	CCNE1_HUMAN	.	G1/S-specific cyclin E; Cyclin E; CCNE	CCNE1	Essential for the control of the cell cycle at the G1/S (start) transition.	.	5L2W; 1W98	MPRERRERDAKERDTMKEDGGAEFSARSRKRKANVTVFLQDPDEEMAKIDRTARDQCGSQPWDNNAVCADPCSLIPTPDKEDDDRVYPNSTCKPRIIAPSRGSPLPVLSWANREEVWKIMLNKEKTYLRDQHFLEQHPLLQPKMRAILLDWLMEVCEVYKLHRETFYLAQDFFDRYMATQENVVKTLLQLIGISSLFIAAKLEEIYPPKLHQFAYVTDGACSGDEILTMELMIMKALKWRLSPLTIVSWLNVYMQVAYLNDLHEVLLPQYPQQIFIQIAELLDLCVLDVDCLEFPYGILAASALYHFSSSELMQKVSGYQWCDIENCVKWMVPFAMVIRETGSSKLKHFRGVADEDAHNIQTHRDSLDLLDKARAKKAMLSEQNRASPLPSGLLTPPQSGKKQSSGPEMA	Literature-reported	"Pyrido[2,3-d]pyrimidin-7-one inhibitors of cyclin-dependent kinases. J Med Chem. 2000 Nov 30;43(24):4606-16."	2	.	.	cyclin family. Cyclin E subfamily.	.	.	"Cyclin, C-terminal domain; Cyclin, N-terminal domain"	PF02984; PF00134	PF02984; Cyclin_C; PF00134; Cyclin_N	.	.	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	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	.	P24864
TTLDRGX	G1/S-specific cyclin-E2 (CCNE2)	O96020	CCNE2_HUMAN	.	G1/Sspecific cyclinE2	CCNE2	Essential for the control of the cell cycle at the late G1 and early S phase.	.	.	MSRRSSRLQAKQQPQPSQTESPQEAQIIQAKKRKTTQDVKKRREEVTKKHQYEIRNCWPPVLSGGISPCIIIETPHKEIGTSDFSRFTNYRFKNLFINPSPLPDLSWGCSKEVWLNMLKKESRYVHDKHFEVLHSDLEPQMRSILLDWLLEVCEVYTLHRETFYLAQDFFDRFMLTQKDINKNMLQLIGITSLFIASKLEEIYAPKLQEFAYVTDGACSEEDILRMELIILKALKWELCPVTIISWLNLFLQVDALKDAPKVLLPQYSQETFIQIAQLLDLCILAIDSLEFQYRILTAAALCHFTSIEVVKKASGLEWDSISECVDWMVPFVNVVKSTSPVKLKTFKKIPMEDRHNIQTHTNYLAMLEEVNYINTFRKGGQLSPVCNGGIMTPPKSTEKPPGKH	Literature-reported	Cyclin D1 and cyclin E2 are differentially expressed in gastric cancer. Med Oncol. 2016 May;33(5):40.	.	.	.	cyclin family. Cyclin E subfamily.	.	.	"Cyclin, C-terminal domain; Cyclin, N-terminal domain"	PF02984; PF00134	PF02984; Cyclin_C; PF00134; Cyclin_N	.	.	hsa04110: Cell cycle; hsa04114: Oocyte meiosis; hsa04115: p53 signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04218: Cellular senescence; hsa04934: Cushing syndrome; hsa05161: Hepatitis B; hsa05162: Measles; hsa05165: Human papillomavirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05200: Pathways in cancer; hsa05203: Viral carcinogenesis; hsa05206: MicroRNAs in cancer; hsa05215: Prostate cancer; hsa05222: Small cell lung cancer; hsa05226: Gastric cancer	"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-390471: Association of TriC/CCT with target proteins during biosynthesis; R-HSA-6804116: TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest; R-HSA-69017: CDK-mediated phosphorylation and removal of Cdc6; R-HSA-69200: Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes; R-HSA-69202: Cyclin E associated events during G1/S transition; R-HSA-69231: Cyclin D associated events in G1; R-HSA-69563: p53-Dependent G1 DNA Damage Response; R-HSA-9661069: Defective binding of RB1 mutants to E2F1,(E2F2, E2F3)"	.	O96020
TTC24WT	C-C chemokine receptor type 1 (CCR1)	P32246	CCR1_HUMAN	GPCR rhodopsin	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	CCR1	"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."	.	1Y5D	METPNTTEDYDTTTEFDYGDATPCQKVNERAFGAQLLPPLYSLVFVIGLVGNILVVLVLVQYKRLKNMTSIYLLNLAISDLLFLFTLPFWIDYKLKDDWVFGDAMCKILSGFYYTGLYSEIFFIILLTIDRYLAIVHAVFALRARTVTFGVITSIIIWALAILASMPGLYFSKTQWEFTHHTCSLHFPHESLREWKLFQALKLNLFGLVLPLLVMIICYTGIIKILLRRPNEKKSKAVRLIFVIMIIFFLFWTPYNLTILISVFQDFLFTHECEQSRHLDLAVQVTEVIAYTHCCVNPVIYAFVGERFRKYLRQLFHRRVAVHLVKWLPFLSVDRLERVSSTSPSTGEHELSAGF	Clinical trial	"Chemokine receptor CCR1 antagonist CCX354-C treatment for rheumatoid arthritis: CARAT-2, a randomised, placebo controlled clinical trial. Ann Rheum Dis. 2013 Mar;72(3):337-44."	21	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P32246
TTFZYTO	C-C chemokine receptor type 2 (CCR2)	P41597	CCR2_HUMAN	GPCR rhodopsin	Monocyte chemoattractant protein 1 receptor; MCP-1-R; Chemokine receptor CCR2B; CMKBR2; CD192; CCR-2; CC-CKR-2; C-C CKR-2	CCR2	"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."	.	5T1A; 2MLQ; 2MLO; 1KP1; 1KAD	MLSTSRSRFIRNTNESGEEVTTFFDYDYGAPCHKFDVKQIGAQLLPPLYSLVFIFGFVGNMLVVLILINCKKLKCLTDIYLLNLAISDLLFLITLPLWAHSAANEWVFGNAMCKLFTGLYHIGYFGGIFFIILLTIDRYLAIVHAVFALKARTVTFGVVTSVITWLVAVFASVPGIIFTKCQKEDSVYVCGPYFPRGWNNFHTIMRNILGLVLPLLIMVICYSGILKTLLRCRNEKKRHRAVRVIFTIMIVYFLFWTPYNIVILLNTFQEFFGLSNCESTSQLDQATQVTETLGMTHCCINPIIYAFVGEKFRSLFHIALGCRIAPLQKPVCGGPGVRPGKNVKVTTQGLLDGRGKGKSIGRAPEASLQDKEGA	Clinical trial	Present and future in the treatment of diabetic kidney disease. J Diabetes Res. 2015;2015:801348.	21	PF00001	.	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway	R-HSA-1461957:Beta defensins; R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P41597
TTD3XFU	C-C chemokine receptor type 3 (CCR3)	P51677	CCR3_HUMAN	GPCR rhodopsin	Eosinophil eotaxin receptor; Chemokine receptor CCR3; CMKBR3; CKR3; CD193; CCR-3; CC-CKR-3; C-C CKR-3	CCR3	"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."	.	.	MTTSLDTVETFGTTSYYDDVGLLCEKADTRALMAQFVPPLYSLVFTVGLLGNVVVVMILIKYRRLRIMTNIYLLNLAISDLLFLVTLPFWIHYVRGHNWVFGHGMCKLLSGFYHTGLYSEIFFIILLTIDRYLAIVHAVFALRARTVTFGVITSIVTWGLAVLAALPEFIFYETEELFEETLCSALYPEDTVYSWRHFHTLRMTIFCLVLPLLVMAICYTGIIKTLLRCPSKKKYKAIRLIFVIMAVFFIFWTPYNVAILLSSYQSILFGNDCERSKHLDLVMLVTEVIAYSHCCMNPVIYAFVGERFRKYLRHFFHRHLLMHLGRYIPFLPSEKLERTSSVSPSTAEPELSIVF	Discontinued	Emerging drugs for asthma. Expert Opin Emerg Drugs. 2008 Dec;13(4):643-53.	3	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa05203:Viral carcinogenesis	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P51677
TTU3Y87	CCR3 messenger RNA (CCR3 mRNA)	P51677	CCR3_HUMAN	mRNA target	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)	CCR3	"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."	.	.	MTTSLDTVETFGTTSYYDDVGLLCEKADTRALMAQFVPPLYSLVFTVGLLGNVVVVMILIKYRRLRIMTNIYLLNLAISDLLFLVTLPFWIHYVRGHNWVFGHGMCKLLSGFYHTGLYSEIFFIILLTIDRYLAIVHAVFALRARTVTFGVITSIVTWGLAVLAALPEFIFYETEELFEETLCSALYPEDTVYSWRHFHTLRMTIFCLVLPLLVMAICYTGIIKTLLRCPSKKKYKAIRLIFVIMAVFFIFWTPYNVAILLSSYQSILFGNDCERSKHLDLVMLVTEVIAYSHCCMNPVIYAFVGERFRKYLRHFFHRHLLMHLGRYIPFLPSEKLERTSSVSPSTAEPELSIVF	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 60).	21	mRNA	mRNA target	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway; hsa05163: Human cytomegalovirus infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05203: Viral carcinogenesis	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-418594: G alpha (i) signalling events	.	P51677
TT7HQD0	C-C chemokine receptor type 4 (CCR4)	P51679	CCR4_HUMAN	GPCR rhodopsin	K5-5; CMKBR4; CD194; CCR-4; CC-CKR-4; CC chemokine receptor 4; C-CCKR-4; C-C CKR-4	CCR4	"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."	.	.	MNPTDIADTTLDESIYSNYYLYESIPKPCTKEGIKAFGELFLPPLYSLVFVFGLLGNSVVVLVLFKYKRLRSMTDVYLLNLAISDLLFVFSLPFWGYYAADQWVFGLGLCKMISWMYLVGFYSGIFFVMLMSIDRYLAIVHAVFSLRARTLTYGVITSLATWSVAVFASLPGFLFSTCYTERNHTYCKTKYSLNSTTWKVLSSLEINILGLVIPLGIMLFCYSMIIRTLQHCKNEKKNKAVKMIFAVVVLFLGFWTPYNIVLFLETLVELEVLQDCTFERYLDYAIQATETLAFVHCCLNPIIYFFLGEKFRKYILQLFKTCRGLFVLCQYCGLLQIYSADTPSSSYTQSTMDHDLHDAL	Successful	"Mogamulizumab, a humanized mAb against C-C chemokine receptor 4 for the potential treatment of T-cell lymphomas and asthma. Curr Opin Mol Ther. 2010 Dec;12(6):770-9."	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa05203:Viral carcinogenesis	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P51679
TTJIH8Q	CCR5 messenger RNA (CCR5 mRNA)	P51681	CCR5_HUMAN	mRNA target	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)	CCR5	"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."	.	6MET; 6MEO; 6FGP; 5YY4; 5YD5	MDYQVSSPIYDINYYTSEPCQKINVKQIAARLLPPLYSLVFIFGFVGNMLVILILINCKRLKSMTDIYLLNLAISDLFFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFIILLTIDRYLAVVHAVFALKARTVTFGVVTSVITWVVAVFASLPGIIFTRSQKEGLHYTCSSHFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPIIYAFVGEKFRNYLLVFFQKHIAKRFCKCCSIFQQEAPERASSVYTRSTGEQEISVGL	Successful	Molecular cloning and radioligand binding characterization of the chemokine receptor CCR5 from rhesus macaque and human. Biochem Pharmacol. 2005 Dec 19;71(1-2):163-72.	34	mRNA	mRNA target	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04144:Endocytosis; hsa05145:Toxoplasmosis; hsa05203:Viral carcinogenesis	R-HSA-173107:Binding and entry of HIV virion; R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P51681
TT2CEJG	C-C chemokine receptor type 5 (CCR5)	P51681	CCR5_HUMAN	GPCR rhodopsin	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	CCR5	"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."	.	6MET; 6MEO; 6FGP; 5YY4; 5YD5	MDYQVSSPIYDINYYTSEPCQKINVKQIAARLLPPLYSLVFIFGFVGNMLVILILINCKRLKSMTDIYLLNLAISDLFFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFIILLTIDRYLAVVHAVFALKARTVTFGVVTSVITWVVAVFASLPGIIFTRSQKEGLHYTCSSHFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPIIYAFVGEKFRNYLLVFFQKHIAKRFCKCCSIFQQEAPERASSVYTRSTGEQEISVGL	Successful	Rapamycin enhances aplaviroc anti-HIV activity: implications for the clinical development of novel CCR5 antagonists. Antiviral Res. 2009 Jul;83(1):86-9.	34	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04144:Endocytosis; hsa05145:Toxoplasmosis; hsa05203:Viral carcinogenesis	R-HSA-173107:Binding and entry of HIV virion; R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P51681
TTH91NV	HUMAN C-C chemokine receptor 5 (CCR5)	P51681	CCR5_HUMAN	GPCR rhodopsin	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	CCR5	"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."	.	6MET; 6MEO; 6FGP; 5YY4; 5YD5	MDYQVSSPIYDINYYTSEPCQKINVKQIAARLLPPLYSLVFIFGFVGNMLVILILINCKRLKSMTDIYLLNLAISDLFFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFIILLTIDRYLAVVHAVFALKARTVTFGVVTSVITWVVAVFASLPGIIFTRSQKEGLHYTCSSHFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPIIYAFVGEKFRNYLLVFFQKHIAKRFCKCCSIFQQEAPERASSVYTRSTGEQEISVGL	.	Disruption of the CCL5/RANTES-CCR5 Pathway Restores Immune Homeostasis and Reduces Plasma Viral Load in Critical COVID-19	.	.	.	.	.	.	.	.	.	.	.	hsa03250: Viral life cycle - HIV-1; hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway; hsa04144: Endocytosis; hsa05145: Toxoplasmosis; hsa05163: Human cytomegalovirus infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05203: Viral carcinogenesis	R-HSA-173107: Binding and entry of HIV virion; R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-418594: G alpha (i) signalling events; R-HSA-6783783: Interleukin-10 signaling	.	P51681
TTFDB30	C-C chemokine receptor type 6 (CCR6)	P51684	CCR6_HUMAN	G-protein coupled receptor 1 family	C-C CKR-6; CC-CKR-6; CCR-6; Chemokine receptor-like 3; CKR-L3; DRY6; G-protein coupled receptor 29; GPR-CY4; GPRCY4; LARC receptor; CD196	CCR6	"Receptor for the C-C type chemokine CCL20 (PubMed:9169459). Binds to CCL20 and subsequently transduces a signal by increasing the intracellular calcium ion levels (PubMed:20068036). Although CCL20 is its major ligand it can also act as a receptor for non-chemokine ligands such as beta-defensins (PubMed:25585877). Binds to defensin DEFB1 leading to increase in intracellular calcium ions and cAMP levels. Its binding to DEFB1 is essential for the function of DEFB1 in regulating sperm motility and bactericidal activity (PubMed:25122636). Binds to defensins DEFB4 and DEFB4A/B and mediates their chemotactic effects (PubMed:20068036). 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. CCR6-mediated signals are essential for immune responses to microbes in the intestinal mucosa and in the modulation of inflammatory responses initiated by tissue insult and trauma (PubMed:21376174). CCR6 is essential for the recruitment of both the pro-inflammatory IL17 producing helper T-cells (Th17) and the regulatory T-cells (Treg) to sites of inflammation. Required for the normal migration of Th17 cells in Peyers-patches and other related tissue sites of the intestine and plays a role in regulating effector T-cell balance and distribution in inflamed intestine. Plays an important role in the coordination of early thymocyte precursor migration events important for normal subsequent thymocyte precursor development, but is not required for the formation of normal thymic natural regulatory T-cells (nTregs). Required for optimal differentiation of DN2 and DN3 thymocyte precursors. Essential for B-cell localization in the subepithelial dome of Peyers-patches and for efficient B-cell isotype switching to IgA in the Peyers-patches. Essential for appropriate anatomical distribution of memory B-cells in the spleen and for the secondary recall response of memory B-cells (By similarity). Positively regulates sperm motility and chemotaxis via its binding to CCL20 (PubMed:23765988). {ECO:0000250|UniProtKB:O54689, ECO:0000269|PubMed:20068036, ECO:0000269|PubMed:23765988, ECO:0000269|PubMed:25122636, ECO:0000269|PubMed:9169459, ECO:0000303|PubMed:21376174, ECO:0000303|PubMed:25585877}."	.	6WWZ	MSGESMNFSDVFDSSEDYFVSVNTSYYSVDSEMLLCSLQEVRQFSRLFVPIAYSLICVFGLLGNILVVITFAFYKKARSMTDVYLLNMAIADILFVLTLPFWAVSHATGAWVFSNATCKLLKGIYAINFNCGMLLLTCISMDRYIAIVQATKSFRLRSRTLPRSKIICLVVWGLSVIISSSTFVFNQKYNTQGSDVCEPKYQTVSEPIRWKLLMLGLELLFGFFIPLMFMIFCYTFIVKTLVQAQNSKRHKAIRVIIAVVLVFLACQIPHNMVLLVTAANLGKMNRSCQSEKLIGYTKTVTEVLAFLHCCLNPVLYAFIGQKFRNYFLKILKDLWCVRRKYKSSGFSCAGRYSENISRQTSETADNDNASSFTM	Clinical trial	"A Novel C-C Chemoattractant Cytokine (Chemokine) Receptor 6 (CCR6) Antagonist (PF-07054894) Distinguishes between Homologous Chemokine Receptors, Increases Basal Circulating CCR6(+) T Cells, and Ameliorates Interleukin-23-Induced Skin Inflammation. J Pharmacol Exp Ther. 2023 Jul;386(1):80-92."	.	.	.	.	.	.	.	.	.	.	.	hsa:1235	R-HSA-1461957;R-HSA-380108;R-HSA-418594;	.	P51684;
TT2GIDQ	C-C chemokine receptor type 7 (CCR7)	P32248	CCR7_HUMAN	GPCR rhodopsin	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	CCR7	Probable mediator of EBV effects on B-lymphocytes or of normal lymphocyte functions. Receptor for the MIP-3-beta chemokine.	.	.	MDLGKPMKSVLVVALLVIFQVCLCQDEVTDDYIGDNTTVDYTLFESLCSKKDVRNFKAWFLPIMYSIICFVGLLGNGLVVLTYIYFKRLKTMTDTYLLNLAVADILFLLTLPFWAYSAAKSWVFGVHFCKLIFAIYKMSFFSGMLLLLCISIDRYVAIVQAVSAHRHRARVLLISKLSCVGIWILATVLSIPELLYSDLQRSSSEQAMRCSLITEHVEAFITIQVAQMVIGFLVPLLAMSFCYLVIIRTLLQARNFERNKAIKVIIAVVVVFIVFQLPYNGVVLAQTVANFNITSSTCELSKQLNIAYDVTYSLACVRCCVNPFLYAFIGVKFRNDLFKLFKDLGCLSQEQLRQWSSCRHIRRSSMSVEAETTTTFSP	Clinical trial	Biomarkers in psoriasis and psoriatic arthritis. Ann Rheum Dis. 2013 Apr;72 Suppl 2:ii104-10. 	.	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-418594: G alpha (i) signalling events	.	P32248
TTE836A	C-C chemokine receptor type 8 (CCR8)	P51685	CCR8_HUMAN	GPCR rhodopsin	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	CCR8	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.	.	.	MDYTLDLSVTTVTDYYYPDIFSSPCDAELIQTNGKLLLAVFYCLLFVFSLLGNSLVILVLVVCKKLRSITDVYLLNLALSDLLFVFSFPFQTYYLLDQWVFGTVMCKVVSGFYYIGFYSSMFFITLMSVDRYLAVVHAVYALKVRTIRMGTTLCLAVWLTAIMATIPLLVFYQVASEDGVLQCYSFYNQQTLKWKIFTNFKMNILGLLIPFTIFMFCYIKILHQLKRCQNHNKTKAIRLVLIVVIASLLFWVPFNVVLFLTSLHSMHILDGCSISQQLTYATHVTEIISFTHCCVNPVIYAFVGEKFKKHLSEIFQKSCSQIFNYLGRQMPRESCEKSSSCQQHSSRSSSVDYIL	Discontinued	Increased Expression of Chemerin in Squamous Esophageal Cancer Myofibroblasts and Role in Recruitment of Mesenchymal Stromal Cells. PLoS One. 2014; 9(8): e104877.	3	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa05203:Viral carcinogenesis	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P51685
TTIPS8B	C-C chemokine receptor type 9 (CCR9)	P51686	CCR9_HUMAN	GPCR rhodopsin	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	CCR9	Subsequently transduces a signal by increasing the intracellular calcium ions level. Receptor for chemokine SCYA25/TECK.	.	5LWE	MTPTDFTSPIPNMADDYGSESTSSMEDYVNFNFTDFYCEKNNVRQFASHFLPPLYWLVFIVGALGNSLVILVYWYCTRVKTMTDMFLLNLAIADLLFLVTLPFWAIAAADQWKFQTFMCKVVNSMYKMNFYSCVLLIMCISVDRYIAIAQAMRAHTWREKRLLYSKMVCFTIWVLAAALCIPEILYSQIKEESGIAICTMVYPSDESTKLKSAVLTLKVILGFFLPFVVMACCYTIIIHTLIQAKKSSKHKALKVTITVLTVFVLSQFPYNCILLVQTIDAYAMFISNCAVSTNIDICFQVTQTIAFFHSCLNPVLYVFVGERFRRDLVKTLKNLGCISQAQWVSFTRREGSLKLSSMLLETTSGALSL	Clinical trial	"GSK-1605786, a selective small-molecule antagonist of the CCR9 chemokine receptor for the treatment of Crohn's disease. IDrugs. 2010 Jul;13(7):472-81."	25	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04672:Intestinal immune network for IgA production	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P51686
TTPBZUO	Clostridium difficile DNA gyrase (CD gyr)	P94605; P94604	GYRA_CLOAB; GYRB_CLOAB	.	.	CD gyrA	.	.	.	.	Clinical trial	"In Vitro and In Vivo Activities of DS-2969b, a Novel GyrB Inhibitor, against Clostridium difficile. Antimicrob Agents Chemother. 2018 Mar 27;62(4):e02157-17."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P94605
TT64H8L	Clostridium difficile Toxin A (CD toxA)	P16154	TOXA_CLODI	.	Toxin A	CD toxA	Only after the enteral delivery of the enterotoxin A may the characteristic disease called pseudomembranous colitis be induced.	EC 3.4.22.-	5UQL; 5UQK; 5UMI; 4R04; 4DMW	MSLISKEELIKLAYSIRPRENEYKTILTNLDEYNKLTTNNNENKYLQLKKLNESIDVFMNKYKTSSRNRALSNLKKDILKEVILIKNSNTSPVEKNLHFVWIGGEVSDIALEYIKQWADINAEYNIKLWYDSEAFLVNTLKKAIVESSTTEALQLLEEEIQNPQFDNMKFYKKRMEFIYDRQKRFINYYKSQINKPTVPTIDDIIKSHLVSEYNRDETVLESYRTNSLRKINSNHGIDIRANSLFTEQELLNIYSQELLNRGNLAAASDIVRLLALKNFGGVYLDVDMLPGIHSDLFKTISRPSSIGLDRWEMIKLEAIMKYKKYINNYTSENFDKLDQQLKDNFKLIIESKSEKSEIFSKLENLNVSDLEIKIAFALGSVINQALISKQGSYLTNLVIEQVKNRYQFLNQHLNPAIESDNNFTDTTKIFHDSLFNSATAENSMFLTKIAPYLQVGFMPEARSTISLSGPGAYASAYYDFINLQENTIEKTLKASDLIEFKFPENNLSQLTEQEINSLWSFDQASAKYQFEKYVRDYTGGSLSEDNGVDFNKNTALDKNYLLNNKIPSNNVEEAGSKNYVHYIIQLQGDDISYEATCNLFSKNPKNSIIIQRNMNESAKSYFLSDDGESILELNKYRIPERLKNKEKVKVTFIGHGKDEFNTSEFARLSVDSLSNEISSFLDTIKLDISPKNVEVNLLGCNMFSYDFNVEETYPGKLLLSIMDKITSTLPDVNKNSITIGANQYEVRINSEGRKELLAHSGKWINKEEAIMSDLSSKEYIFFDSIDNKLKAKSKNIPGLASISEDIKTLLLDASVSPDTKFILNNLKLNIESSIGDYIYYEKLEPVKNIIHNSIDDLIDEFNLLENVSDELYELKKLNNLDEKYLISFEDISKNNSTYSVRFINKSNGESVYVETEKEIFSKYSEHITKEISTIKNSIITDVNGNLLDNIQLDHTSQVNTLNAAFFIQSLIDYSSNKDVLNDLSTSVKVQLYAQLFSTGLNTIYDSIQLVNLISNAVNDTINVLPTITEGIPIVSTILDGINLGAAIKELLDEHDPLLKKELEAKVGVLAINMSLSIAATVASIVGIGAEVTIFLLPIAGISAGIPSLVNNELILHDKATSVVNYFNHLSESKKYGPLKTEDDKILVPIDDLVISEIDFNNNSIKLGTCNILAMEGGSGHTVTGNIDHFFSSPSISSHIPSLSIYSAIGIETENLDFSKKIMMLPNAPSRVFWWETGAVPGLRSLENDGTRLLDSIRDLYPGKFYWRFYAFFDYAITTLKPVYEDTNIKIKLDKDTRNFIMPTITTNEIRNKLSYSFDGAGGTYSLLLSSYPISTNINLSKDDLWIFNIDNEVREISIENGTIKKGKLIKDVLSKIDINKNKLIIGNQTIDFSGDIDNKDRYIFLTCELDDKISLIIEINLVAKSYSLLLSGDKNYLISNLSNTIEKINTLGLDSKNIAYNYTDESNNKYFGAISKTSQKSIIHYKKDSKNILEFYNDSTLEFNSKDFIAEDINVFMKDDINTITGKYYVDNNTDKSIDFSISLVSKNQVKVNGLYLNESVYSSYLDFVKNSDGHHNTSNFMNLFLDNISFWKLFGFENINFVIDKYFTLVGKTNLGYVEFICDNNKNIDIYFGEWKTSSSKSTIFSGNGRNVVVEPIYNPDTGEDISTSLDFSYEPLYGIDRYINKVLIAPDLYTSLININTNYYSNEYYPEIIVLNPNTFHKKVNINLDSSSFEYKWSTEGSDFILVRYLEESNKKILQKIRIKGILSNTQSFNKMSIDFKDIKKLSLGYIMSNFKSFNSENELDRDHLGFKIIDNKTYYYDEDSKLVKGLININNSLFYFDPIEFNLVTGWQTINGKKYYFDINTGAALTSYKIINGKHFYFNNDGVMQLGVFKGPDGFEYFAPANTQNNNIEGQAIVYQSKFLTLNGKKYYFDNNSKAVTGWRIINNEKYYFNPNNAIAAVGLQVIDNNKYYFNPDTAIISKGWQTVNGSRYYFDTDTAIAFNGYKTIDGKHFYFDSDCVVKIGVFSTSNGFEYFAPANTYNNNIEGQAIVYQSKFLTLNGKKYYFDNNSKAVTGLQTIDSKKYYFNTNTAEAATGWQTIDGKKYYFNTNTAEAATGWQTIDGKKYYFNTNTAIASTGYTIINGKHFYFNTDGIMQIGVFKGPNGFEYFAPANTDANNIEGQAILYQNEFLTLNGKKYYFGSDSKAVTGWRIINNKKYYFNPNNAIAAIHLCTINNDKYYFSYDGILQNGYITIERNNFYFDANNESKMVTGVFKGPNGFEYFAPANTHNNNIEGQAIVYQNKFLTLNGKKYYFDNDSKAVTGWQTIDGKKYYFNLNTAEAATGWQTIDGKKYYFNLNTAEAATGWQTIDGKKYYFNTNTFIASTGYTSINGKHFYFNTDGIMQIGVFKGPNGFEYFAPANTDANNIEGQAILYQNKFLTLNGKKYYFGSDSKAVTGLRTIDGKKYYFNTNTAVAVTGWQTINGKKYYFNTNTSIASTGYTIISGKHFYFNTDGIMQIGVFKGPDGFEYFAPANTDANNIEGQAIRYQNRFLYLHDNIYYFGNNSKAATGWVTIDGNRYYFEPNTAMGANGYKTIDNKNFYFRNGLPQIGVFKGSNGFEYFAPANTDANNIEGQAIRYQNRFLHLLGKIYYFGNNSKAVTGWQTINGKVYYFMPDTAMAAAGGLFEIDGVIYFFGVDGVKAPGIYG	Clinical trial	ClinicalTrials.gov (NCT01513239) A Study of MK-6072 and MK-3415A in Participants Receiving Antibiotic Therapy for Clostridium Difficile Infection (MK-3415A-002). U.S. National Institutes of Health.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQH65V	Clostridium difficile Toxin B (CD toxB)	P18177 	TOXB_CLODI	.	Toxin B	CD toxB	Cytotoxin.	EC 3.4.22.-	6C0B; 6AR6; 5UQT; 5UQN; 5UQM	MSLVNRKQLEKMANVRFRTQEDEYVAILDALEEYHNMSENTVVEKYLKLKDINSLTDIYIDTYKKSGRNKALKKFKEYLVTEVLELKNNNLTPVEKNLHFVWIGGQINDTAINYINQWKDVNSDYNVNVFYDSNAFLINTLKKTVVESAINDTLESFRENLNDPRFDYNKFFRKRMEIIYDKQKNFINYYKAQREENPELIIDDIVKTYLSNEYSKEIDELNTYIEESLNKITQNSGNDVRNFEEFKNGESFNLYEQELVERWNLAAASDILRISALKEIGGMYLDVDMLPGIQPDLFESIEKPSSVTVDFWEMTKLEAIMKYKEYIPEYTSEHFDMLDEEVQSSFESVLASKSDKSEIFSSLGDMEASPLEVKIAFNSKGIINQGLISVKDSYCSNLIVKQIENRYKILNNSLNPAISEDNDFNTTTNTFIDSIMAEANADNGRFMMELGKYLRVGFFPDVKTTINLSGPEAYAAAYQDLLMFKEGSMNIHLIEADLRNFEISKTNISQSTEQEMASLWSFDDARAKAQFEEYKRNYFEGSLGEDDNLDFSQNIVVDKEYLLEKISSLARSSERGYIHYIVQLQGDKISYEAACNLFAKTPYDSVLFQKNIEDSEIAYYYNPGDGEIQEIDKYKIPSIISDRPKIKLTFIGHGKDEFNTDIFAGFDVDSLSTEIEAAIDLAKEDISPKSIEINLLGCNMFSYSINVEETYPGKLLLKVKDKISELMPSISQDSIIVSANQYEVRINSEGRRELLDHSGEWINKEESIIKDISSKEYISFNPKENKITVKSKNLPELSTLLQEIRNNSNSSDIELEEKVMLTECEINVISNIDTQIVEERIEEAKNLTSDSINYIKDEFKLIESISDALCDLKQQNELEDSHFISFEDISETDEGFSIRFINKETGESIFVETEKTIFSEYANHITEEISKIKGTIFDTVNGKLVKKVNLDTTHEVNTLNAAFFIQSLIEYNSSKESLSNLSVAMKVQVYAQLFSTGLNTITDAAKVVELVSTALDETIDLLPTLSEGLPIIATIIDGVSLGAAIKELSETSDPLLRQEIEAKIGIMAVNLTTATTAIITSSLGIASGFSILLVPLAGISAGIPSLVNNELVLRDKATKVVDYFKHVSLVETEGVFTLLDDKIMMPQDDLVISEIDFNNNSIVLGKCEIWRMEGGSGHTVTDDIDHFFSAPSITYREPHLSIYDVLEVQKEELDLSKDLMVLPNAPNRVFAWETGWTPGLRSLENDGTKLLDRIRDNYEGEFYWRYFAFIADALITTLKPRYEDTNIRINLDSNTRSFIVPIITTEYIREKLSYSFYGSGGTYALSLSQYNMGINIELSESDVWIIDVDNVVRDVTIESDKIKKGDLIEGILSTLSIEENKIILNSHEINFSGEVNGSNGFVSLTFSILEGINAIIEVDLLSKSYKLLISGELKILMLNSNHIQQKIDYIGFNSELQKNIPYSFVDSEGKENGFINGSTKEGLFVSELPDVVLISKVYMDDSKPSFGYYSNNLKDVKVITKDNVNILTGYYLKDDIKISLSLTLQDEKTIKLNSVHLDESGVAEILKFMNRKGNTNTSDSLMSFLESMNIKSIFVNFLQSNIKFILDANFIISGTTSIGQFEFICDENDNIQPYFIKFNTLETNYTLYVGNRQNMIVEPNYDLDDSGDISSTVINFSQKYLYGIDSCVNKVVISPNIYTDEINITPVYETNNTYPEVIVLDANYINEKINVNINDLSIRYVWSNDGNDFILMSTSEENKVSQVKIRFVNVFKDKTLANKLSFNFSDKQDVPVSEIILSFTPSYYEDGLIGYDLGLVSLYNEKFYINNFGMMVSGLIYINDSLYYFKPPVNNLITGFVTVGDDKYYFNPINGGAASIGETIIDDKNYYFNQSGVLQTGVFSTEDGFKYFAPANTLDENLEGEAIDFTGKLIIDENIYYFDDNYRGAVEWKELDGEMHYFSPETGKAFKGLNQIGDYKYYFNSDGVMQKGFVSINDNKHYFDDSGVMKVGYTEIDGKHFYFAENGEMQIGVFNTEDGFKYFAHHNEDLGNEEGEEISYSGILNFNNKIYYFDDSFTAVVGWKDLEDGSKYYFDEDTAEAYIGLSLINDGQYYFNDDGIMQVGFVTINDKVFYFSDSGIIESGVQNIDDNYFYIDDNGIVQIGVFDTSDGYKYFAPANTVNDNIYGQAVEYSGLVRVGEDVYYFGETYTIETGWIYDMENESDKYYFNPETKKACKGINLIDDIKYYFDEKGIMRTGLISFENNNYYFNENGEMQFGYINIEDKMFYFGEDGVMQIGVFNTPDGFKYFAHQNTLDENFEGESINYTGWLDLDEKRYYFTDEYIAATGSVIIDGEEYYFDPDTAQLVISE	Successful	2016 FDA drug approvals. Nat Rev Drug Discov. 2017 Feb 2;16(2):73-76. 	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT6I7DC	Monocyte differentiation antigen CD14 (CD14)	P08571	CD14_HUMAN	.	Myeloid cell-specific leucine-rich glycoprotein	CD14	"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."	.	4GLP	MERASCLLLLLLPLVHVSATTPEPCELDDEDFRCVCNFSEPQPDWSEAFQCVSAVEVEIHAGGLNLEPFLKRVDADADPRQYADTVKALRVRRLTVGAAQVPAQLLVGALRVLAYSRLKELTLEDLKITGTMPPLPLEATGLALSSLRLRNVSWATGRSWLAELQQWLKPGLKVLSIAQAHSPAFSCEQVRAFPALTSLDLSDNPGLGERGLMAALCPHKFPAIQNLALRNTGMETPTGVCAALAAAGVQPHSLDLSHNSLRATVNPSAPRCMWSSALNSLNLSFAGLEQVPKGLPAKLRVLDLSCNRLNRAPQPDELPEVDNLTLDGNPFLVPGTALPHEGSMNSGVVPACARSTLSVGVSGTLVLLQGARGFA	Clinical trial	"IC14, a CD14 specific monoclonal antibody, is a potential treatment for patients with severe sepsis. J Endotoxin Res. 2001;7(4):310-4."	21	.	Leucine rich repeat	.	.	.	.	.	.	.	.	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	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	.	P08571
TTCLGZ8	HUAMN monocyte differentiation antigen CD14 (CD14)	P08571	CD14_HUMAN	.	Myeloid cell-specific leucine-rich glycoprotein	CD14	"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."	.	4GLP	MERASCLLLLLLPLVHVSATTPEPCELDDEDFRCVCNFSEPQPDWSEAFQCVSAVEVEIHAGGLNLEPFLKRVDADADPRQYADTVKALRVRRLTVGAAQVPAQLLVGALRVLAYSRLKELTLEDLKITGTMPPLPLEATGLALSSLRLRNVSWATGRSWLAELQQWLKPGLKVLSIAQAHSPAFSCEQVRAFPALTSLDLSDNPGLGERGLMAALCPHKFPAIQNLALRNTGMETPTGVCAALAAAGVQPHSLDLSHNSLRATVNPSAPRCMWSSALNSLNLSFAGLEQVPKGLPAKLRVLDLSCNRLNRAPQPDELPEVDNLTLDGNPFLVPGTALPHEGSMNSGVVPACARSTLSVGVSGTLVLLQGARGFA	.	IC14 (Anti-CD14) Treatment in Patients With SARS-CoV-2 (COVID-19)	.	.	.	.	.	.	.	.	.	.	.	hsa04010: MAPK signaling pathway; hsa04064: NF-kappa B signaling pathway; hsa04145: Phagosome; hsa04620: Toll-like receptor signaling pathway; hsa04640: Hematopoietic cell lineage; hsa04936: Alcoholic liver disease; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05133: Pertussis; hsa05134: Legionellosis; hsa05146: Amoebiasis; hsa05152: Tuberculosis; hsa05202: Transcriptional misregulation in cancer; hsa05221: Acute myeloid leukemia; hsa05417: Lipid and atherosclerosis	R-HSA-1236974: ER-Phagosome pathway; R-HSA-140534: Caspase activation via Death Receptors in the presence of ligand; R-HSA-166016: Toll Like Receptor 4 (TLR4) Cascade; R-HSA-166020: Transfer of LPS from LBP carrier to CD14; R-HSA-166058: MyD88:MAL(TIRAP) cascade initiated on plasma membrane; R-HSA-166166: MyD88-independent TLR4 cascade; R-HSA-168179: Toll Like Receptor TLR1:TLR2 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-5686938: Regulation of TLR by endogenous ligand; R-HSA-6798695: Neutrophil degranulation; 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 within TLR4 complex; R-HSA-975163: IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation	.	P08571
TTOFEAS	Natural killer cell receptor BY55 (CD160)	O95971	BY55_HUMAN	.	CD160 antigen; BY55	CD160	"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."	.	.	MLLEPGRGCCALAILLAIVDIQSGGCINITSSASQEGTRLNLICTVWHKKEEAEGFVVFLCKDRSGDCSPETSLKQLRLKRDPGIDGVGEISSQLMFTISQVTPLHSGTYQCCARSQKSGIRLQGHFFSILFTETGNYTVTGLKQRQHLEFSHNEGTLSSGFLQEKVWVMLVTSLVALQAL	Literature-reported	A novel antiangiogenic and vascular normalization therapy targeted against human CD160 receptor. J Exp Med. 2011 May 9;208(5):973-86.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	O95971
TTTZ9DE	Hemoglobin scavenger receptor (CD163)	Q86VB7	C163A_HUMAN	.	sCD163; Soluble CD163; Scavenger receptor cysteine-rich type 1 protein M130; M130	CD163	"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."	.	.	MSKLRMVLLEDSGSADFRRHFVNLSPFTITVVLLLSACFVTSSLGGTDKELRLVDGENKCSGRVEVKVQEEWGTVCNNGWSMEAVSVICNQLGCPTAIKAPGWANSSAGSGRIWMDHVSCRGNESALWDCKHDGWGKHSNCTHQQDAGVTCSDGSNLEMRLTRGGNMCSGRIEIKFQGRWGTVCDDNFNIDHASVICRQLECGSAVSFSGSSNFGEGSGPIWFDDLICNGNESALWNCKHQGWGKHNCDHAEDAGVICSKGADLSLRLVDGVTECSGRLEVRFQGEWGTICDDGWDSYDAAVACKQLGCPTAVTAIGRVNASKGFGHIWLDSVSCQGHEPAIWQCKHHEWGKHYCNHNEDAGVTCSDGSDLELRLRGGGSRCAGTVEVEIQRLLGKVCDRGWGLKEADVVCRQLGCGSALKTSYQVYSKIQATNTWLFLSSCNGNETSLWDCKNWQWGGLTCDHYEEAKITCSAHREPRLVGGDIPCSGRVEVKHGDTWGSICDSDFSLEAASVLCRELQCGTVVSILGGAHFGEGNGQIWAEEFQCEGHESHLSLCPVAPRPEGTCSHSRDVGVVCSRYTEIRLVNGKTPCEGRVELKTLGAWGSLCNSHWDIEDAHVLCQQLKCGVALSTPGGARFGKGNGQIWRHMFHCTGTEQHMGDCPVTALGASLCPSEQVASVICSGNQSQTLSSCNSSSLGPTRPTIPEESAVACIESGQLRLVNGGGRCAGRVEIYHEGSWGTICDDSWDLSDAHVVCRQLGCGEAINATGSAHFGEGTGPIWLDEMKCNGKESRIWQCHSHGWGQQNCRHKEDAGVICSEFMSLRLTSEASREACAGRLEVFYNGAWGTVGKSSMSETTVGVVCRQLGCADKGKINPASLDKAMSIPMWVDNVQCPKGPDTLWQCPSSPWEKRLASPSEETWITCDNKIRLQEGPTSCSGRVEIWHGGSWGTVCDDSWDLDDAQVVCQQLGCGPALKAFKEAEFGQGTGPIWLNEVKCKGNESSLWDCPARRWGHSECGHKEDAAVNCTDISVQKTPQKATTGRSSRQSSFIAVGILGVVLLAIFVALFFLTKKRRQRQRLAVSSRGENLVHQIQYREMNSCLNADDLDLMNSSENSHESADFSAAELISVSKFLPISGMEKEAILSHTEKENGNL	Literature-reported	Targeting the hemoglobin scavenger receptor CD163 in macrophages highly increases the anti-inflammatory potency of dexamethasone. Mol Ther. 2012 Aug;20(8):1550-8.	.	.	.	.	.	.	Scavenger receptor cysteine-rich domain	PF00530	PF00530; SRCR	.	.	.	R-HSA-2168880: Scavenging of heme from plasma; R-HSA-9662834: CD163 mediating an anti-inflammatory response	.	Q86VB7
TTW640A	B-lymphocyte surface antigen B4 (CD19)	P15391	CD19_HUMAN	Immunoglobulin	T-cell surface antigen Leu-12; Leu-12; Differentiation antigen CD19; B-lymphocyte antigen CD19	CD19	"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."	.	6AL5	MPPPRLLFFLLFLTPMEVRPEEPLVVKVEEGDNAVLQCLKGTSDGPTQQLTWSRESPLKPFLKLSLGLPGLGIHMRPLAIWLFIFNVSQQMGGFYLCQPGPPSEKAWQPGWTVNVEGSGELFRWNVSDLGGLGCGLKNRSSEGPSSPSGKLMSPKLYVWAKDRPEIWEGEPPCLPPRDSLNQSLSQDLTMAPGSTLWLSCGVPPDSVSRGPLSWTHVHPKGPKSLLSLELKDDRPARDMWVMETGLLLPRATAQDAGKYYCHRGNLTMSFHLEITARPVLWHWLLRTGGWKVSAVTLAYLIFCLCSLVGILHLQRALVLRRKRKRMTDPTRRFFKVTPPPGSGPQNQYGNVLSLPTPTSGLGRAQRWAAGLGGTAPSYGNPSSDVQADGALGSRSPPGVGPEEEEGEGYEEPDSEEDSEFYENDSNLGQDQLSQDGSGYENPEDEPLGPEDEDSFSNAESYENEDEELTQPVARTMDFLSPHGSAWDPSREATSLGSQSYEDMRGILYAAPQLRSIRGQPGPNHEEDADSYENMDNPDGPDPAWGGGGRMGTWSTR	Successful	2014 FDA drug approvals. Nat Rev Drug Discov. 2015 Feb;14(2):77-81.	34	Immunoglobulin	Immunoglobulin	.	.	.	.	.	.	.	.	hsa04151:PI3K-Akt signaling pathway; hsa04640:Hematopoietic cell lineage; hsa04662:B cell receptor signaling pathway; hsa05169:Epstein-Barr virus infection; hsa05340:Primary immunodeficiency	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	.	P15391
TTBGTFN	T-cell surface glycoprotein CD1a (CD1A)	P06126	CD1A_HUMAN	Immunoglobulin	hTa1 thymocyteantigen; hTa1 thymocyte antigen; T-cell surfaceantigen T6/Leu-6; T-cell surface antigen T6/Leu-6; CD1a	CD1A	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.	.	5J1A; 4X6F; 4X6E; 4X6D; 4X6C	MLFLLLPLLAVLPGDGNADGLKEPLSFHVTWIASFYNHSWKQNLVSGWLSDLQTHTWDSNSSTIVFLCPWSRGNFSNEEWKELETLFRIRTIRSFEGIRRYAHELQFEYPFEIQVTGGCELHSGKVSGSFLQLAYQGSDFVSFQNNSWLPYPVAGNMAKHFCKVLNQNQHENDITHNLLSDTCPRFILGLLDAGKAHLQRQVKPEAWLSHGPSPGPGHLQLVCHVSGFYPKPVWVMWMRGEQEQQGTQRGDILPSADGTWYLRATLEVAAGEAADLSCRVKHSSLEGQDIVLYWEHHSSVGFIILAVIVPLLLLIGLALWFRKRCFC	Successful	Acute sensory neuropathy associated with rabbit antithymocyte globulin. Am J Transplant. 2007 Feb;7(2):484-6.	34	Immunoglobulin	.	.	.	.	Immunoglobulin C1-set domain; MHC-I family domain	PF07654; PF16497	PF07654; C1-set; PF16497; MHC_I_3	.	.	hsa04640:Hematopoietic cell lineage	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	P06126
TTJDUNO	T-cell surface antigen CD2 (CD2)	P06729	CD2_HUMAN	.	T-cell surface antigen T11/Leu-5; SRBC; Rosette receptor; LFA-3 receptor; LFA-2; Erythrocyte receptor	CD2	"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."	.	2J7I; 2J6O; 1QA9; 1L2Z; 1HNF	MSFPCKFVASFLLIFNVSSKGAVSKEITNALETWGALGQDINLDIPSFQMSDDIDDIKWEKTSDKKKIAQFRKEKETFKEKDTYKLFKNGTLKIKHLKTDDQDIYKVSIYDTKGKNVLEKIFDLKIQERVSKPKISWTCINTTLTCEVMNGTDPELNLYQDGKHLKLSQRVITHKWTTSLSAKFKCTAGNKVSKESSVEPVSCPEKGLDIYLIIGICGGGSLLMVFVALLVFYITKRKKQRSRRNDEELETRAHRVATEERGRKPHQIPASTPQNPATSQHPPPPPGHRSQAPSHRPPPPGHRVQHQPQKRPPAPSGTQVHQQKGPPLPRPRVQPKPPHGAAENSLSPSSN	Clinical trial	Emerging drugs for moderate-to-severe psoriasis. Expert Opin Emerg Drugs. 2005 Feb;10(1):35-52.	21	.	Transmembrane protein	.	.	.	Immunoglobulin C2-set domain; Immunoglobulin V-set domain	PF05790; PF07686	PF05790; C2-set; PF07686; V-set	.	.	hsa04514:Cell adhesion molecules (CAMs); hsa04640:Hematopoietic cell lineage	R-HSA-202733:Cell surface interactions at the vascular wall	.	P06729
TT0BE68	Membrane glycoprotein OX2 (CD200)	P41217	OX2G_HUMAN	Immunoglobulin	OX2 membrane glycoprotein; OX-2 membrane glycoprotein; My033; MOX2; MOX1	CD200	May regulate myeloid cell activity in a variety of tissues. Costimulates T-cell proliferation.	.	.	MERLVIRMPFSHLSTYSLVWVMAAVVLCTAQVQVVTQDEREQLYTPASLKCSLQNAQEALIVTWQKKKAVSPENMVTFSENHGVVIQPAYKDKINITQLGLQNSTITFWNITLEDEGCYMCLFNTFGFGKISGTACLTVYVQPIVSLHYKFSEDHLNITCSATARPAPMVFWKVPRSGIENSTVTLSHPNGTTSVTSILHIKDPKNQVGKEVICQVLHLGTVTDFKQTVNKGYWFSVPLLLSIVSLVILLVLISILLYWKRHRNQDRGELSQGVQKMT	Clinical trial	"American Society of Hematology, 52nd Annual Meeting and Exposition. P T. 2011 February; 36(2): 100-103."	21	Immunoglobulin	Immunoglobulin superfamily	.	.	.	Immunoglobulin domain	PF00047	PF00047; ig	.	.	.	R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	P41217
TTBXIM9	Membrane-associated lectin type-C (CD209)	Q9NNX6	CD209_HUMAN	.	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	CD209	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.	.	2XR6; 2XR5; 2IT6; 2IT5; 2B6B	MSDSKEPRLQQLGLLEEEQLRGLGFRQTRGYKSLAGCLGHGPLVLQLLSFTLLAGLLVQVSKVPSSISQEQSRQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTWLKAAVGELPEKSKMQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTQLKAAVERLCHPCPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLLPSFKQYWNRGEPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	Transmembrane protein	.	.	.	Lectin C-type domain	PF00059	PF00059; Lectin_C	.	.	hsa04145:Phagosome; hsa05152:Tuberculosis; hsa05162:Measles	R-HSA-5621575:CD209 (DC-SIGN) signaling	.	Q9NNX6
TTM6QSK	B-cell receptor CD22 (CD22)	P20273	CD22_HUMAN	Immunoglobulin	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	CD22	"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."	.	5VL3; 5VKM; 5VKJ	MHLLGPWLLLLVLEYLAFSDSSKWVFEHPETLYAWEGACVWIPCTYRALDGDLESFILFHNPEYNKNTSKFDGTRLYESTKDGKVPSEQKRVQFLGDKNKNCTLSIHPVHLNDSGQLGLRMESKTEKWMERIHLNVSERPFPPHIQLPPEIQESQEVTLTCLLNFSCYGYPIQLQWLLEGVPMRQAAVTSTSLTIKSVFTRSELKFSPQWSHHGKIVTCQLQDADGKFLSNDTVQLNVKHTPKLEIKVTPSDAIVREGDSVTMTCEVSSSNPEYTTVSWLKDGTSLKKQNTFTLNLREVTKDQSGKYCCQVSNDVGPGRSEEVFLQVQYAPEPSTVQILHSPAVEGSQVEFLCMSLANPLPTNYTWYHNGKEMQGRTEEKVHIPKILPWHAGTYSCVAENILGTGQRGPGAELDVQYPPKKVTTVIQNPMPIREGDTVTLSCNYNSSNPSVTRYEWKPHGAWEEPSLGVLKIQNVGWDNTTIACAACNSWCSWASPVALNVQYAPRDVRVRKIKPLSEIHSGNSVSLQCDFSSSHPKEVQFFWEKNGRLLGKESQLNFDSISPEDAGSYSCWVNNSIGQTASKAWTLEVLYAPRRLRVSMSPGDQVMEGKSATLTCESDANPPVSHYTWFDWNNQSLPYHSQKLRLEPVKVQHSGAYWCQGTNSVGKGRSPLSTLTVYYSPETIGRRVAVGLGSCLAILILAICGLKLQRRWKRTQSQQGLQENSSGQSFFVRNKKVRRAPLSEGPHSLGCYNPMMEDGISYTTLRFPEMNIPRTGDAESSEMQRPPPDCDDTVTYSALHKRQVGDYENVIPDFPEDEGIHYSELIQFGVGERPQAQENVDYVILKH	Successful	Safety and immunogenicity of recombinant Bacille Calmette-Gu |rin (rBCG) expressing Borrelia burgdorferi outer surface protein A (OspA) lipoprotein in adult volunteers: a candidate Lyme disease vaccine. Vaccine. 1999 Feb 26;17(7-8):904-14.	34	Immunoglobulin	Immunoglobulin	immunoglobulin superfamily. SIGLEC (sialic acid binding Ig-like lectin) family.	.	.	CD80-like C2-set immunoglobulin domain ; Immunoglobulin domain	PF08205; PF13895	PF08205; C2-set_2; PF13895; Ig_2	.	.	hsa04514:Cell adhesion molecules (CAMs); hsa04640:Hematopoietic cell lineage; hsa04662:B cell receptor signaling pathway	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	.	P20273
TTCTYNP	Small cell lung carcinoma cluster 4 antigen (CD24)	P25063	CD24_HUMAN	.	Signal transducer CD24; CD24A	CD24	"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."	.	.	MGRAMVARLGLGLLLLALLLPTQIYSSETTTGTSSNSSQSTSNSGLAPNPTNATTKAAGGALQSTASLFVVSLSLLHLYS	Literature-reported	Targeting CD24 for treatment of colorectal and pancreatic cancer by monoclonal antibodies or small interfering RNA. Cancer Res. 2008 Apr 15;68(8):2803-12.	0	.	.	CD24 family.	.	.	CD24 protein	PF14984	PF14984; CD24	.	.	hsa04640: Hematopoietic cell lineage	R-HSA-373760: L1CAM interactions	.	P25063
TTYJWT7	Endosialin (CD248)	Q9HCU0	CD248_HUMAN	.	Tumor endothelial marker 1; Tumor Endothelial Marker 1 (TEM-1); TEM1; CD164L1	CD248	May play a role in tumor angiogenesis.	.	.	MLLRLLLAWAAAGPTLGQDPWAAEPRAACGPSSCYALFPRRRTFLEAWRACRELGGDLATPRTPEEAQRVDSLVGAGPASRLLWIGLQRQARQCQLQRPLRGFTWTTGDQDTAFTNWAQPASGGPCPAQRCVALEASGEHRWLEGSCTLAVDGYLCQFGFEGACPALQDEAGQAGPAVYTTPFHLVSTEFEWLPFGSVAAVQCQAGRGASLLCVKQPEGGVGWSRAGPLCLGTGCSPDNGGCEHECVEEVDGHVSCRCTEGFRLAADGRSCEDPCAQAPCEQQCEPGGPQGYSCHCRLGFRPAEDDPHRCVDTDECQIAGVCQQMCVNYVGGFECYCSEGHELEADGISCSPAGAMGAQASQDLGDELLDDGEDEEDEDEAWKAFNGGWTEMPGILWMEPTQPPDFALAYRPSFPEDREPQIPYPEPTWPPPLSAPRVPYHSSVLSVTRPVVVSATHPTLPSAHQPPVIPATHPALSRDHQIPVIAANYPDLPSAYQPGILSVSHSAQPPAHQPPMISTKYPELFPAHQSPMFPDTRVAGTQTTTHLPGIPPNHAPLVTTLGAQLPPQAPDALVLRTQATQLPIIPTAQPSLTTTSRSPVSPAHQISVPAATQPAALPTLLPSQSPTNQTSPISPTHPHSKAPQIPREDGPSPKLALWLPSPAPTAAPTALGEAGLAEHSQRDDRWLLVALLVPTCVFLVVLLALGIVYCTRCGPHAPNKRITDCYRWVIHAGSKSPTEPMPPRGSLTGVQTCRTSV	Clinical trial	"A first-in-human phase I study of MORAb-004, a monoclonal antibody to endosialin in patients with advanced solid tumors. Clin Cancer Res. 2015 Mar 15;21(6):1281-8."	21	.	.	.	.	.	Lectin C-type domain	PF00059	PF00059; Lectin_C	.	.	.	.	.	Q9HCU0
TTDO1MV	T-cell activation antigen CD27 (CD27)	P26842	CD27_HUMAN	Cytokine receptor	Tumor necrosis factor receptor superfamily member 7; Tcell activation antigen CD27; TNFRSF7; T14; CD27L receptor; CD27 antigen	CD27	May play a role in survival of activated T-cells. May play a role in apoptosis through association with SIVA1. Receptor for CD70/CD27L.	.	5TLK; 5TLJ; 5TL5	MARPHPWWLCVLGTLVGLSATPAPKSCPERHYWAQGKLCCQMCEPGTFLVKDCDQHRKAAQCDPCIPGVSFSPDHHTRPHCESCRHCNSGLLVRNCTITANAECACRNGWQCRDKECTECDPLPNPSLTARSSQALSPHPQPTHLPYVSEMLEARTAGHMQTLADFRQLPARTLSTHWPPQRSLCSSDFIRILVIFSGMFLVFTLAGALFLHQRRKYRSNKGESPVEPAEPCHYSCPREEEGSTIPIQEDYRKPEPACSP	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	Cytokine receptor	Cytokine receptor	.	.	.	TNFR/NGFR cysteine-rich region	PF00020	PF00020; TNFR_c6	.	.	hsa04060:Cytokine-cytokine receptor interaction	R-HSA-5669034:TNFs bind their physiological receptors	.	P26842
TT8ZLTI	Programmed cell death 1 ligand 1 (PD-L1)	Q9NZQ7	PD1L1_HUMAN	Immunoglobulin	hPD-L1; Programmed death ligand 1; PDL1; PDCD1LG1; PDCD1L1; PDCD1 ligand 1; B7H1; B7-H1; B7 homolog 1	CD274	"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."	.	6R3K; 6NP9; 6NOS; 6NOJ; 6NNV	MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHLEET	Successful	PD-1 as a potential target in cancer therapy. Cancer Med. 2013 October; 2(5): 662-673.	34	Immunoglobulin	Immunoglobulin	immunoglobulin superfamily. BTN/MOG family.	.	.	CD80-like C2-set immunoglobulin domain ; Immunoglobulin V-set domain	PF08205; PF07686	PF08205; C2-set_2; PF07686; V-set	.	.	hsa04514:Cell adhesion molecules (CAMs)	R-HSA-389948:PD-1 signaling	.	Q9NZQ7
TTFAOU7	CD274 messenger RNA (CD274 mRNA)	Q9NZQ7	PD1L1_HUMAN	.	PD-L1; PDCD1 ligand 1; Programmed death ligand 1; hPD-L1; B7 homolog 1; B7-H1; DE   AltName: CD_antigen=CD274	CD274	"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)."	.	.	MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHLEET	Clinical trial	"Clinical pipeline report, company report or official report of Roche."	.	.	.	.	.	.	.	.	.	.	.	hsa04514: Cell adhesion molecules; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer	R-HSA-389948: PD-1 signaling; R-HSA-9701898: STAT3 nuclear events downstream of ALK signaling	.	Q9NZQ7
TT6CQUM	B7 homolog 3 (CD276)	Q5ZPR3	CD276_HUMAN	Immunoglobulin	UNQ309/PRO352; PSEC0249; Costimulatory molecule; CD276 antigen; B7H3; B7-H3; 4IgB7H3; 4Ig-B7-H3	CD276	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.	.	.	MLRRRGSPGMGVHVGAALGALWFCLTGALEVQVPEDPVVALVGTDATLCCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFAEGQDQGSAYANRTALFPDLLAQGNASLRLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPYSKPSMTLEPNKDLRPGDTVTITCSSYQGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFDVHSILRVVLGANGTYSCLVRNPVLQQDAHSSVTITPQRSPTGAVEVQVPEDPVVALVGTDATLRCSFSPEPGFSLAQLNLIWQLTDTKQLVHSFTEGRDQGSAYANRTALFPDLLAQGNASLRLQRVRVADEGSFTCFVSIRDFGSAAVSLQVAAPYSKPSMTLEPNKDLRPGDTVTITCSSYRGYPEAEVFWQDGQGVPLTGNVTTSQMANEQGLFDVHSVLRVVLGANGTYSCLVRNPVLQQDAHGSVTITGQPMTFPPEALWVTVGLSVCLIALLVALAFVCWRKIKQSCEEENAGAEDQDGEGEGSKTALQPLKHSDSKEDDGQEIA	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	19	Immunoglobulin	Immunoglobulin superfamily	immunoglobulin superfamily. BTN/MOG family.	.	.	Immunoglobulin V-set domain	PF07686	PF07686; V-set	.	.	hsa04514:Cell adhesion molecules (CAMs)	.	.	Q5ZPR3
TTQ13FT	T-cell-specific surface glycoprotein CD28 (CD28)	P10747	CD28_HUMAN	.	TP44; CD28-S2	CD28	"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."	.	5GJI; 5GJH; 5AUL; 3WA4; 1YJD	MLRLLLALNLFPSIQVTGNKILVKQSPMLVAYDNAVNLSCKYSYNLFSREFRASLHKGLDSAVEVCVVYGNYSQQLQVYSKTGFNCDGKLGNESVTFYLQNLYVNQTDIYFCKIEVMYPPPYLDNEKSNGTIIHVKGKHLCPSPLFPGPSKPFWVLVVVGGVLACYSLLVTVAFIIFWVRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS	Successful	New developments in immunosuppressive therapy for heart transplantation. Expert Opin Emerg Drugs. 2009 Mar;14(1):1-21.	34	.	Transmembrane protein	.	.	.	ICOS V-set domain	PF15910	PF15910; V-set_2	.	.	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	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	.	P10747
TTI2YFK	CMRF35-like molecule 8 (CD300A)	Q9UGN4	CLM8_HUMAN	.	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	CD300A	"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."	.	2Q87	MWLPWALLLLWVPGCFALSKCRTVAGPVGGSLSVQCPYEKEHRTLNKYWCRPPQIFLCDKIVETKGSAGKRNGRVSIRDSPANLSFTVTLENLTEEDAGTYWCGVDTPWLRDFHDPVVEVEVSVFPASTSMTPASITAAKTSTITTAFPPVSSTTLFAVGATHSASIQEETEEVVNSQLPLLLSLLALLLLLLVGASLLAWRMFQKWIKAGDHSELSQNPKQAATQSELHYANLELLMWPLQEKPAPPREVEVEYSTVASPREELHYASVVFDSNTNRIAAQRPREEEPDSDYSVIRKT	Literature-reported	"CD300A promotes tumor progression by PECAM1, ADCY7 and AKT pathway in acute myeloid leukemia. Oncotarget. 2018 Jan 11;9(44):27574-27584."	.	.	.	CD300 family.	.	.	Immunoglobulin V-set domain	PF07686	PF07686; V-set	.	.	.	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-6798695: Neutrophil degranulation	.	Q9UGN4
TT0KV32	Transcobalamin receptor (CD320)	Q9NPF0	CD320_HUMAN	.	UNQ198/PRO224; TCblR; FDCsignaling molecule 8D6; FDCSM8D6; FDC-signaling molecule 8D6; FDC-SM-8D6; CD320 antigen; 8D6A; 8D6 antigen	CD320	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).	.	4ZRQ; 4ZRP	MSGGWMAQVGAWRTGALGLALLLLLGLGLGLEAAASPLSTPTSAQAAGPSSGSCPPTKFQCRTSGLCVPLTWRCDRDLDCSDGSDEEECRIEPCTQKGQCPPPPGLPCPCTGVSDCSGGTDKKLRNCSRLACLAGELRCTLSDDCIPLTWRCDGHPDCPDSSDELGCGTNEILPEGDATTMGPPVTLESVTSLRNATTMGPPVTLESVPSVGNATSSSAGDQSGSPTAYGVIAAAAVLSASLVTATLLLLSWLRAQERLRPLGLLVAMKESLLLSEQKTSLP	Literature-reported	"Targeted delivery of saporin toxin by monoclonal antibody to the transcobalamin receptor, TCblR/CD320. Mol Cancer Ther. 2010 Nov;9(11):3033-40."	.	.	.	.	.	.	Low-density lipoprotein receptor domain class A	PF00057	PF00057; Ldl_recept_a	.	.	.	R-HSA-3359485: Defective CD320 causes MMATC; R-HSA-9758890: Transport of RCbl within the body	.	Q9NPF0
TTJVYO3	Myeloid cell surface antigen CD33 (CD33)	P20138	CD33_HUMAN	Immunoglobulin	Siglec-3; Sialic acid-binding Ig-like lectin 3; SIGLEC3; Gp67	CD33	"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."	.	6D4A; 6D49; 6D48; 5J0B; 5J06	MPLLLLLPLLWAGALAMDPNFWLQVQESVTVQEGLCVLVPCTFFHPIPYYDKNSPVHGYWFREGAIISRDSPVATNKLDQEVQEETQGRFRLLGDPSRNNCSLSIVDARRRDNGSYFFRMERGSTKYSYKSPQLSVHVTDLTHRPKILIPGTLEPGHSKNLTCSVSWACEQGTPPIFSWLSAAPTSLGPRTTHSSVLIITPRPQDHGTNLTCQVKFAGAGVTTERTIQLNVTYVPQNPTTGIFPGDGSGKQETRAGVVHGAIGGAGVTALLALCLCLIFFIVKTHRRKAARTAVGRNDTHPTTGSASPKHQKKSKLHGPTETSSCSGAAPTVEMDEELHYASLNFHGMNPSKDTSTEYSEVRTQ	Successful	Targeted treatment of acute myeloid leukemia in older adults: role of gemtuzumab ozogamicin. Clin Interv Aging. 2009;4:197-205.	34	Immunoglobulin	.	immunoglobulin superfamily. SIGLEC (sialic acid binding Ig-like lectin) family.	.	.	Immunoglobulin domain; Immunoglobulin V-set domain	PF00047; PF07686	PF00047; ig; PF07686; V-set	.	.	hsa04640:Hematopoietic cell lineage	R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	P20138
TTZAVYN	Hematopoietic progenitor cell antigen CD34 (CD34)	P28906	CD34_HUMAN	.	CD34 molecule	CD34	"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."	.	.	MLVRRGARAGPRMPRGWTALCLLSLLPSGFMSLDNNGTATPELPTQGTFSNVSTNVSYQETTTPSTLGSTSLHPVSQHGNEATTNITETTVKFTSTSVITSVYGNTNSSVQSQTSVISTVFTTPANVSTPETTLKPSLSPGNVSDLSTTSTSLATSPTKPYTSSSPILSDIKAEIKCSGIREVKLTQGICLEQNKTSSCAEFKKDRGEGLARVLCGEEQADADAGAQVCSLLLAQSEVRPQCLLLVLANRTEISSKLQLMKKHQSDLKKLGILDFTEQDVASHQSYSQKTLIALVTSGALLAVLGITGYFLMNRRSWSPTGERLGEDPYYTENGGGQGYSSGPGTSPEAQGKASVNRGAQENGTGQATSRNGHSARQHVVADTEL	Clinical trial	National Cancer Institute Drug Dictionary (drug id 743421).	21	.	.	CD34 family.	.	.	CD34/Podocalyxin family	PF06365	PF06365; CD34_antigen	.	.	hsa04514: Cell adhesion molecules; hsa04640: Hematopoietic cell lineage	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	P28906
TTPJMCU	Platelet glycoprotein 4 (CD36)	P16671	CD36_HUMAN	Long chain fatty acid translocase	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	CD36	"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."	.	5LGD	MGCDRNCGLIAGAVIGAVLAVFGGILMPVGDLLIQKTIKKQVVLEEGTIAFKNWVKTGTEVYRQFWIFDVQNPQEVMMNSSNIQVKQRGPYTYRVRFLAKENVTQDAEDNTVSFLQPNGAIFEPSLSVGTEADNFTVLNLAVAAASHIYQNQFVQMILNSLINKSKSSMFQVRTLRELLWGYRDPFLSLVPYPVTTTVGLFYPYNNTADGVYKVFNGKDNISKVAIIDTYKGKRNLSYWESHCDMINGTDAASFPPFVEKSQVLQFFSSDICRSIYAVFESDVNLKGIPVYRFVLPSKAFASPVENPDNYCFCTEKIISKNCTSYGVLDISKCKEGRPVYISLPHFLYASPDVSEPIDGLNPNEEEHRTYLDIEPITGFTLQFAKRLQVNLLVKPSEKIQVLKNLKRNYIVPILWLNETGTIGDEKANMFRSQVTGKINLLGLIEMILLSVGVVMFVAFMISYCACRSKTIK	Literature-reported	Biological markers in osteoarthritis. Nat Clin Pract Rheumatol. 2007 Jun;3(6):346-56.	.	TC=9.B.39	.	CD36 family.	.	.	CD36 family	PF01130	PF01130; CD36	9.B.39.1.4	The Long Chain Fatty Acid Translocase (lcFAT) Family	hsa03320: PPAR signaling pathway; hsa04145: Phagosome; hsa04152: AMPK signaling pathway; hsa04512: ECM-receptor interaction; hsa04640: Hematopoietic cell lineage; hsa04920: Adipocytokine signaling pathway; hsa04931: Insulin resistance; hsa04975: Fat digestion and absorption; hsa04979: Cholesterol metabolism; hsa05144: Malaria; hsa05415: Diabetic cardiomyopathy; hsa05417: Lipid and atherosclerosis	R-HSA-114608: Platelet degranulation; R-HSA-1236973: Cross-presentation of particulate exogenous antigens (phagosomes); R-HSA-1236974: ER-Phagosome pathway; R-HSA-166058: MyD88:MAL(TIRAP) cascade initiated on plasma membrane; R-HSA-168188: Toll Like Receptor TLR6:TLR2 Cascade; R-HSA-1989781: PPARA activates gene expression; R-HSA-3000471: Scavenging by Class B Receptors; R-HSA-381340: Transcriptional regulation of white adipocyte differentiation; R-HSA-434313: Intracellular metabolism of fatty acids regulates insulin secretion; R-HSA-5602498: MyD88 deficiency (TLR2/4); R-HSA-5603041: IRAK4 deficiency (TLR2/4); R-HSA-5686938: Regulation of TLR by endogenous ligand; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6798695: Neutrophil degranulation	.	P16671
TTFCW29	Leukocyte antigen CD37 (CD37)	P11049	CD37_HUMAN	Tetraspanin	Tspan26; Tspan-26; Tetraspanin26; Tetraspanin-26	CD37	"extracellular exosome, immunological synapse, integral component of plasma membrane, membrane, cell surface receptor signaling pathway."	.	.	MSAQESCLSLIKYFLFVFNLFFFVLGSLIFCFGIWILIDKTSFVSFVGLAFVPLQIWSKVLAISGIFTMGIALLGCVGALKELRCLLGLYFGMLLLLFATQITLGILISTQRAQLERSLRDVVEKTIQKYGTNPEETAAEESWDYVQFQLRCCGWHYPQDWFQVLILRGNGSEAHRVPCSCYNLSATNDSTILDKVILPQLSRLGHLARSRHSADICAVPAESHIYREGCAQGLQKWLHNNLISIVGICLGVGLLELGFMTLSIFLCRNLDHVYNRLARYR	Clinical trial	The CD37-targeted antibody-drug conjugate IMGN529 is highly active against human CLL and in a novel CD37 transgenic murine leukemia model. Leukemia. 2014 Jul;28(7):1501-10.	21	TC=8.A.40	.	tetraspanin (TM4SF) family.	.	.	Tetraspanin family	PF00335	PF00335; Tetraspanin	.	.	hsa04640:Hematopoietic cell lineage	.	.	P11049
TTPURFN	Cyclic ADP-ribose hydrolase 1 (CD38)	P28907	CD38_HUMAN	Glycosylase	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	CD38	"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."	EC 3.2.2.6	6EDR; 5F21; 5F1O; 5F1K; 4XJT	MANCEFSPVSGDKPCCRLSRRAQLCLGVSILVLILVVVLAVVVPRWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCNKILLWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVHVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKFLQCVKNPEDSSCTSEI	Successful	Targeting CD38 with Daratumumab Monotherapy in Multiple Myeloma. N Engl J Med. 2015 Sep 24;373(13):1207-19.	34	EC:3.2	Glycosylase	ADP-ribosyl cyclase family.	3.2.2.6	Glycosylases	ADP-ribosyl cyclase	PF02267	PF02267; Rib_hydrolayse	.	.	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	R-HSA-196807: Nicotinate metabolism	MetaCyc:HS00103-MON	P28907
TTZAT79	T-cell surface glycoprotein CD3 epsilon (CD3E)	P07766	CD3E_HUMAN	.	T3E; T-cell surface glycoprotein CD3 epsilon chain; T-cell surface antigen T3/Leu-4 epsilon chain; CD3e	CD3E	"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."	.	2ROL; 1XIW; 1SY6; 1A81	MQSGTHWRVLGLCLLSVGVWGQDGNEEMGGITQTPYKVSISGTTVILTCPQYPGSEILWQHNDKNIGGDEDDKNIGSDEDHLSLKEFSELEQSGYYVCYPRGSKPEDANFYLYLRARVCENCMEMDVMSVATIVIVDICITGGLLLLVYYWSKNRKAKAKPVTRGAGAGGRQRGQNKERPPPVPNPDYEPIRKGQRDLYSGLNQRRI	Successful	Basiliximab: a review of its use as induction therapy in renal transplantation. Drugs. 2003;63(24):2803-35.	34	.	.	.	.	.	Immunoreceptor tyrosine-based activation motif	PF02189	PF02189; ITAM	.	.	hsa04640:Hematopoietic cell lineage; hsa04660:T cell receptor signaling pathway; hsa05142:Chagas disease (American trypanosomiasis); hsa05162:Measles; hsa05166:HTLV-I infection; hsa05340:Primary immunodeficiency	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	.	P07766
TTV3XPL	T-cell surface glycoprotein CD3 gamma (CD3G)	P09693	CD3G_HUMAN	.	T3G; T-cell surface glycoprotein CD3 gamma chain; T-cell receptor T3 gamma chain; CD3g	CD3G	"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."	.	1SY6	MEQGKGLAVLILAIILLQGTLAQSIKGNHLVKVYDYQEDGSVLLTCDAEAKNITWFKDGKMIGFLTEDKKKWNLGSNAKDPRGMYQCKGSQNKSKPLQVYYRMCQNCIELNAATISGFLFAEIVSIFVLAVGVYFIAGQDGVRQSRASDKQTLLPNDQLYQPLKDREDDQYSHLQGNQLRRN	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	.	.	.	.	.	T-cell surface glycoprotein CD3 delta chain ; Immunoreceptor tyrosine-based activation motif	PF16680; PF02189	PF16680; Ig_4; PF02189; ITAM	.	.	hsa04640:Hematopoietic cell lineage; hsa04660:T cell receptor signaling pathway; hsa05142:Chagas disease (American trypanosomiasis); hsa05162:Measles; hsa05166:HTLV-I infection	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	.	P09693
TTN2JFW	T-cell surface glycoprotein CD4 (CD4)	P01730	CD4_HUMAN	Immunoglobulin	T-cell surface antigen T4/Leu-3	CD4	"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."	.	6MET; 6MEO; 6EDU; 6CM3; 5VN3	MNRGVPFRHLLLVLQLALLPAATQGKKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQLLVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSGTWTCTVLQNQKKVEFKIDIVVLAFQKASSIVYKKEGEQVEFSFPLAFTVEKLTGSGELWWQAERASSSKSWITFDLKNKEVSVKRVTQDPKLQMGKKLPLHLTLPQALPQYAGSGNLTLALEAKTGKLHQEVNLVVMRATQLQKNLTCEVWGPTSPKLMLSLKLENKEAKVSKREKAVWVLNPEAGMWQCLLSDSGQVLLESNIKVLPTWSTPVQPMALIVLGGVAGLLLFIGLGIFFCVRCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI	Successful	2018 FDA drug approvals.Nat Rev Drug Discov. 2019 Feb;18(2):85-89. 	34	Immunoglobulin	Immunoglobulin	.	.	.	"Immunoglobulin C2-set domain; CD4, extracellular; Immunoglobulin domain; T cell CD4 receptor C terminal region"	PF05790; PF09191; PF00047; PF12104	PF05790; C2-set; PF09191; CD4-extracel; PF00047; ig; PF12104; Tcell_CD4_C	.	.	hsa04514:Cell adhesion molecules (CAMs); hsa04612:Antigen processing and presentation; hsa04640:Hematopoietic cell lineage; hsa04660:T cell receptor signaling pathway; hsa05340:Primary immunodeficiency	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	.	P01730
TT1ERKL	CD40 messenger RNA (CD40 mRNA)	P25942	TNR5_HUMAN	mRNA target	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)	CD40	"Transduces TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and B cells, leading to induction of immunoglobulin secretion. Receptor for TNFSF5/CD40LG."	.	6FAX; 5IHL; 5DMJ; 5DMI; 3QD6	MVRLPLQCVLWGCLLTAVHPEPPTACREKQYLINSQCCSLCQPGQKLVSDCTEFTETECLPCGESEFLDTWNRETHCHQHKYCDPNLGLRVQQKGTSETDTICTCEEGWHCTSEACESCVLHRSCSPGFGVKQIATGVSDTICEPCPVGFFSNVSSAFEKCHPWTSCETKDLVVQQAGTNKTDVVCGPQDRLRALVVIPIIFGILFAILLVLVFIKKVAKKPTNKAPHPKQEPQEINFPDDLPGSNTAAPVQETLHGCQPVTQEDGKESRISVQERQ	Clinical trial	"US patent application no. 6,197,584, Antisense modulation of CD40 expression."	0	mRNA	mRNA target	.	.	.	TNFR/NGFR cysteine-rich region	PF00020	PF00020; TNFR_c6	.	.	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	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	.	P25942
TTN6Y9A	CD40L receptor (CD40)	P25942	TNR5_HUMAN	Cytokine receptor	Tumor necrosis factor receptor superfamily member 5; TNFRSF5; CDw40; Bp50; B-cell surfaceantigen CD40; B-cell surface antigen CD40	CD40	"Transduces TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and B cells, leading to induction of immunoglobulin secretion. Receptor for TNFSF5/CD40LG."	.	6FAX; 5IHL; 5DMJ; 5DMI; 3QD6	MVRLPLQCVLWGCLLTAVHPEPPTACREKQYLINSQCCSLCQPGQKLVSDCTEFTETECLPCGESEFLDTWNRETHCHQHKYCDPNLGLRVQQKGTSETDTICTCEEGWHCTSEACESCVLHRSCSPGFGVKQIATGVSDTICEPCPVGFFSNVSSAFEKCHPWTSCETKDLVVQQAGTNKTDVVCGPQDRLRALVVIPIIFGILFAILLVLVFIKKVAKKPTNKAPHPKQEPQEINFPDDLPGSNTAAPVQETLHGCQPVTQEDGKESRISVQERQ	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1874).	21	Cytokine receptor	Cytokine receptor	.	.	.	TNFR/NGFR cysteine-rich region	PF00020	PF00020; TNFR_c6	.	.	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	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	.	P25942
TTIJP3Q	TNF related activation protein (CD40LG)	P29965	CD40L_HUMAN	Cytokine: tumor necrosis factor	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	CD40LG	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.	.	6BRB; 3QD6; 3LKJ; 1I9R; 1ALY	MIETYNQTSPRSAATGLPISMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLHEDFVFMKTIQRCNTGERSLSLLNCEEIKSQFEGFVKDIMLNKEETKKENSFEMQKGDQNPQIAAHVISEASSKTTSVLQWAEKGYYTMSNNLVTLENGKQLTVKRQGLYYIYAQVTFCSNREASSQAPFIASLCLKSPGRFERILLRAANTHSSAKPCGQQSIHLGGVFELQPGASVFVNVTDPSQVSHGTGFTSFGLLKL	Clinical trial	Immunotherapy of high-risk acute leukemia with a recipient (autologous) vaccine expressing transgenic human CD40L and IL-2 after chemotherapy and a... Blood. 2006 Feb 15;107(4):1332-41.	21	Cytokine	Tumor necrosis factor	tumor necrosis factor family.	.	.	TNF(Tumour Necrosis Factor) family 	PF00229	PF00229; TNF	.	.	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	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	.	P29965
TT7ORQ6	CD40LG messenger RNA (CD40LG mRNA)	P29965	CD40L_HUMAN	mRNA target	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)	CD40LG	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.	.	6BRB; 3QD6; 3LKJ; 1I9R; 1ALY	MIETYNQTSPRSAATGLPISMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLHEDFVFMKTIQRCNTGERSLSLLNCEEIKSQFEGFVKDIMLNKEETKKENSFEMQKGDQNPQIAAHVISEASSKTTSVLQWAEKGYYTMSNNLVTLENGKQLTVKRQGLYYIYAQVTFCSNREASSQAPFIASLCLKSPGRFERILLRAANTHSSAKPCGQQSIHLGGVFELQPGASVFVNVTDPSQVSHGTGFTSFGLLKL	Literature-reported	NCBI GEO: archive for functional genomics data sets--update. Nucleic Acids Res. 2013 Jan;41(Database issue):D991-5.	.	mRNA	mRNA target	.	.	.	TNF(Tumour Necrosis Factor) family 	PF00229	PF00229; TNF	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04064: NF-kappa B signaling pathway; hsa04514: Cell adhesion molecules; 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; hsa05417: Lipid and atherosclerosis	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	.	P29965
TTWFBT7	Extracellular matrix receptor III (CD44)	P16070	CD44_HUMAN	.	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	CD44	"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."	.	4PZ4; 4PZ3; 2I83; 1UUH; 1POZ	MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSSGSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSNTISAGWEPNEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWNPEAHPPLIHHEHHEEEETPHSTSTIQATPSSTTEETATQKEQWFGNRWHEGYRQTPKEDSHSTTGTAAASAHTSHPMQGRTTPSPEDSSWTDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGSFGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGAVEDRKPSGLNGEASKSQEMVHLVNKESSETPDQFMTADETRNLQNVDMKIGV	Clinical trial	Modulation of CD44 Activity by A6-Peptide.Front Immunol.2015 Mar 30;6:135.	21	.	Transmembrane protein	.	.	.	Extracellular link domain	PF00193	PF00193; Xlink	.	.	hsa04512:ECM-receptor interaction; hsa04640:Hematopoietic cell lineage; hsa05131:Shigellosis; hsa05169:Epstein-Barr virus infection; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer	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	.	P16070
TTMS7DF	Membrane cofactor protein (CD46)	P15529	MCP_HUMAN	.	Trophoblast leukocyte common antigen; TLX; MIC10; MCP	CD46	"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."	.	5FO8; 3O8E; 3L89; 3INB; 2O39	MEPPGRRECPFPSWRFPGLLLAAMVLLLYSFSDACEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDACYRETCPYIRDPLNGQAVPANGTYEFGYQMHFICNEGYYLIGEEILYCELKGSVAIWSGKPPICEKVLCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPFSLIGESTIYCGDNSVWSRAAPECKVVKCRFPVVENGKQISGFGKKFYYKATVMFECDKGFYLDGSDTIVCDSNSTWDPPVPKCLKVLPPSSTKPPALSHSVSTSSTTKSPASSASGPRPTYKPPVSNYPGYPKPEEGILDSLDVWVIAVIVIAIVVGVAVICVVPYRYLQRRKKKGTYLTDETHREVKFTSL	Clinical trial	Antibody-drug conjugate targeting CD46 eliminates multiple myeloma cells. J Clin Invest. 2016 Dec 1;126(12):4640-4653.	.	.	.	.	.	.	Sushi repeat (SCR repeat)	PF00084	PF00084; Sushi	.	.	hsa04610: Complement and coagulation cascades; hsa05162: Measles	R-HSA-977606: Regulation of Complement cascade	.	P15529
TT28S46	Leukocyte surface antigen CD47 (CD47)	Q08722	CD47_HUMAN	Osteoclast fusion complex	Protein MER6; MER6; Integrinassociated protein; Integrin-associated protein; IAP; Antigenic surface determinant protein OA3	CD47	"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."	.	5TZU; 5TZT; 5TZ2; 5IWL; 4KJY	MWPLVAALLLGSACCGSAQLLFNKTKSVEFTFCNDTVVIPCFVTNMEAQNTTEVYVKWKFKGRDIYTFDGALNKSTVPTDFSSAKIEVSQLLKGDASLKMDKSDAVSHTGNYTCEVTELTREGETIIELKYRVVSWFSPNENILIVIFPIFAILLFWGQFGIKTLKYRSGGMDEKTIALLVAGLVITVIVIVGAILFVPGEYSLKNATGLGLIVTSTGILILLHYYVFSTAIGLTSFVIAILVIQVIAYILAVVGLSLCIAACIPMHGPLLISGLSILALAQLLGLVYMKFVASNQKTIQPPRKAVEEPLNAFKESKGMMNDE	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	TC=1.N.1	Transmembrane protein	.	.	.	CD47 transmembrane region; CD47 immunoglobulin-like domain	PF04549; PF08204	PF04549; CD47; PF08204; V-set_CD47	1.N.1.1.1	The Osteoclast Fusion Complex (OFC) Family	hsa04512: ECM-receptor interaction	R-HSA-202733: Cell surface interactions at the vascular wall; R-HSA-216083: Integrin cell surface interactions; R-HSA-391160: Signal regulatory protein family interactions; R-HSA-6798695: Neutrophil degranulation	.	Q08722
TTEGYK1	T-cell surface glycoprotein CD5 (CD5)	P06127	CD5_HUMAN	.	Lymphocyte antigen T1/Leu-1; LEU1	CD5	May act as a receptor in regulating T-cell proliferation.	.	2OTT; 2JP0; 2JOP; 2JA4	MPMGSLQPLATLYLLGMLVASCLGRLSWYDPDFQARLTRSNSKCQGQLEVYLKDGWHMVCSQSWGRSSKQWEDPSQASKVCQRLNCGVPLSLGPFLVTYTPQSSIICYGQLGSFSNCSHSRNDMCHSLGLTCLEPQKTTPPTTRPPPTTTPEPTAPPRLQLVAQSGGQHCAGVVEFYSGSLGGTISYEAQDKTQDLENFLCNNLQCGSFLKHLPETEAGRAQDPGEPREHQPLPIQWKIQNSSCTSLEHCFRKIKPQKSGRVLALLCSGFQPKVQSRLVGGSSICEGTVEVRQGAQWAALCDSSSARSSLRWEEVCREQQCGSVNSYRVLDAGDPTSRGLFCPHQKLSQCHELWERNSYCKKVFVTCQDPNPAGLAAGTVASIILALVLLVVLLVVCGPLAYKKLVKKFRQKKQRQWIGPTGMNQNMSFHRNHTATVRSHAENPTASHVDNEYSQPPRNSHLSAYPALEGALHRSSMQPDNSSDSDYDLHGAQRL	Literature-reported	CD5 as a Target for Immune-Based Therapies. Crit Rev Immunol. 2015;35(2):85-115.	.	.	.	.	.	.	Scavenger receptor cysteine-rich domain	PF00530	PF00530; SRCR	.	.	hsa04640: Hematopoietic cell lineage	.	.	P06127
TTQT5S9	Cambridge pathology 1 antigen (CD52)	P31358	CD52_HUMAN	.	Epididymal secretory protein E5; CDW52; CD52 antigen; CD52	CD52	"May play a role in carrying and orienting carbohydrate, as well as having a more specific role."	.	.	MKRFLFLLLTISLLVMVQIQTGLSGQNDTSQTSSPSASSNISGGIFLFFVANAIIHLFCFS	Successful	Identifying alemtuzumab as an anti-myeloid cell antiangiogenic therapy for the treatment of ovarian cancer. J Transl Med. 2009 Jun 19;7:49.	34	.	.	.	.	.	.	.	.	.	.	.	R-HSA-163125: Post-translational modification: synthesis of GPI-anchored proteins	.	P31358
TT5Z9WY	Complement decay-accelerating factor (CD55)	P08174	DAF_HUMAN	.	DAF; Complement decayaccelerating factor; CR	CD55	"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."	.	6ILK; 6ILJ; 5FOA; 3J24; 3IYP	MTVARPSVPAALPLLGELPRLLLLVLLCLPAVWGDCGLPPDVPNAQPALEGRTSFPEDTVITYKCEESFVKIPGEKDSVICLKGSQWSDIEEFCNRSCEVPTRLNSASLKQPYITQNYFPVGTVVEYECRPGYRREPSLSPKLTCLQNLKWSTAVEFCKKKSCPNPGEIRNGQIDVPGGILFGATISFSCNTGYKLFGSTSSFCLISGSSVQWSDPLPECREIYCPAPPQIDNGIIQGERDHYGYRQSVTYACNKGFTMIGEHSIYCTVNNDEGEWSGPPPECRGKSLTSKVPPTVQKPTTVNVPTTEVSPTSQKTTTKTTTPNAQATRSTPVSRTTKHFHETTPNKGSGTTSGTTRLLSGHTCFTLTGLLGTLVTMGLLT	Clinical trial	Oncolytic Coxsackievirus A21 as a novel therapy for multiple myeloma. Br J Haematol. 2007 Apr;137(2):133-41.	21	.	.	receptors of complement activation (RCA) family.	.	.	Sushi repeat (SCR repeat)	PF00084	PF00084; Sushi	.	.	hsa04610:Complement and coagulation cascades; hsa04640:Hematopoietic cell lineage; hsa05416:Viral myocarditis	R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-977606:Regulation of Complement cascade	.	P08174
TT5KSBY	Surface glycoprotein LFA-3 (CD58)	P19256	LFA3_HUMAN	.	Surface glycoprotein LFA3; Lymphocyte functionassociated antigen 3; Lymphocyte function-associated antigen 3; LFA3; Ag3	CD58	"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."	.	1QA9; 1CI5; 1CCZ	MVAGSDAGRALGVLSVVCLLHCFGFISCFSQQIYGVVYGNVTFHVPSNVPLKEVLWKKQKDKVAELENSEFRAFSSFKNRVYLDTVSGSLTIYNLTSSDEDEYEMESPNITDTMKFFLYVLESLPSPTLTCALTNGSIEVQCMIPEHYNSHRGLIMYSWDCPMEQCKRNSTSIYFKMENDLPQKIQCTLSNPLFNTTSSIILTTCIPSSGHSRHRYALIPIPLAVITTCIVLYMNGILKCDRKPDRTNSN	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	hsa04514: Cell adhesion molecules; hsa05169: Epstein-Barr virus infection	R-HSA-202733: Cell surface interactions at the vascular wall; R-HSA-6798695: Neutrophil degranulation	.	P19256
TTBGTEJ	Membrane inhibitor of reactive lysis (CD59)	P13987	CD59_HUMAN	.	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	CD59	"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."	.	5IMY; 5IMT; 4BIK; 2UX2; 2UWR	MGIQGGSVLFGLLLVLAVFCHSGHSLQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENELTYYCCKKDLCNFNEQLENGGTSLSEKTVLLLVTPFLAAAWSLHP	Clinical trial	Isolation and functional assay of the membrane complement inhibitors CD55 (DAF) and CD59 (MIRL). Curr Protoc Immunol. 2001 May;Chapter 13:Unit 13.5.	.	.	.	.	.	.	u-PAR/Ly-6 domain	PF00021	PF00021; UPAR_LY6	.	.	hsa04610: Complement and coagulation cascades; hsa04640: Hematopoietic cell lineage	R-HSA-204005: COPII-mediated vesicle transport; R-HSA-5694530: Cargo concentration in the ER; R-HSA-6798695: Neutrophil degranulation; R-HSA-6807878: COPI-mediated anterograde transport; R-HSA-977606: Regulation of Complement cascade	.	P13987
TTMF6KC	T-cell differentiation antigen CD6 (TP120)	P30203	CD6_HUMAN	.	T12	CD6	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.	.	5A2E	MWLFFGITGLLTAALSGHPSPAPPDQLNTSSAESELWEPGERLPVRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGGAEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCAENRALRLVDGGGACAGRVEMLEHGEWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCSEHQSWRLTGGADRCEGQVEVHFRGVWNTVCDSEWYPSEAKVLCQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLCSQSLAARVLCSASRSLHNLSTPEVPASVQTVTIESSVTVKIENKESRELMLLIPSIVLGILLLGSLIFIAFILLRIKGKYALPVMVNHQHLPTTIPAGSNSYQPVPITIPKEVFMLPIQVQAPPPEDSDSGSDSDYEHYDFSAQPPVALTTFYNSQRHRVTDEEVQQSRFQMPPLEEGLEELHASHIPTANPGHCITDPPSLGPQYHPRSNSESSTSSGEDYCNSPKSKLPPWNPQVFSSERSSFLEQPPNLELAGTQPAFSAGPPADDSSSTSSGEWYQNFQPPPQPPSEEQFGCPGSPSPQPDSTDNDDYDDISAA	Clinical trial	"Efficacy and safety of itolizumab, a novel anti-CD6 monoclonal antibody, in patients with moderate to severe chronic plaque psoriasis: results of a double-blind, randomized, placebo-controlled, phase-III study. J Am Acad Dermatol. 2014 Sep;71(3):484-92."	25	.	.	.	.	.	Scavenger receptor cysteine-rich domain	PF00530	PF00530; SRCR	.	.	hsa04514:Cell adhesion molecules (CAMs)	.	.	P30203
TTPQE9F	Early activation antigen CD69 (CD69)	Q07108	CD69_HUMAN	.	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	CD69	"Involved in lymphocyte proliferation and functions as a signal transmitting receptor in lymphocytes, natural killer (NK) cells, and platelets."	.	3HUP; 3CCK; 1FM5; 1E8I; 1.00E+87	MSSENCFVAENSSLHPESGQENDATSPHFSTRHEGSFQVPVLCAVMNVVFITILIIALIALSVGQYNCPGQYTFSMPSDSHVSSCSEDWVGYQRKCYFISTVKRSWTSAQNACSEHGATLAVIDSEKDMNFLKRYAGREEHWVGLKKEPGHPWKWSNGKEFNNWFNVTGSDKCVFLKNTEVSSMECEKNLYWICNKPYK	Literature-reported	Is CD69 an effective brake to control inflammatory diseases Trends Mol Med. 2013 Oct;19(10):625-32.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q07108
TTP6B8O	T-cell antigen CD7 (CD7)	P09564	CD7_HUMAN	.	Tp40; TP41; T-cell surface antigen Leu-9; T-cell leukemia antigen; LEU-9; GP40; CD7 molecule	CD7	Not yet known.	.	.	MAGPPRLLLLPLLLALARGLPGALAAQEVQQSPHCTTVPVGASVNITCSTSGGLRGIYLRQLGPQPQDIIYYEDGVVPTTDRRFRGRIDFSGSQDNLTITMHRLQLSDTGTYTCQAITEVNVYGSGTLVLVTEEQSQGWHRCSDAPPRASALPAPPTGSALPDPQTASALPDPPAASALPAALAVISFLLGLGLGVACVLARTQIKKLCSWRDKNSAACVVYEDMSHSRCNTLSSPNQYQ	Clinical trial	ClinicalTrials.gov (NCT03690011) Cell Therapy for High Risk T-Cell Malignancies Using CD7-Specific CAR Expressed On Autologous T Cells	17	.	.	.	.	.	Immunoglobulin V-set domain	PF07686	PF07686; V-set	.	.	hsa04640: Hematopoietic cell lineage	.	.	P09564
TTNCIE0	CD70 antigen (CD27-L)	P32970	CD70_HUMAN	Cytokine: tumor necrosis factor	Tumor necrosis factor ligandsuperfamily member 7; Tumor necrosis factor ligand superfamily member 7; TNFSF7; CD27LG; CD27L; CD27 ligand	CD70	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.	.	.	MPEEGSGCSVRRRPYGCVLRAALVPLVAGLVICLVVCIQRFAQAQQQLPLESLGWDVAELQLNHTGPQQDPRLYWQGGPALGRSFLHGPELDKGQLRIHRDGIYMVHIQVTLAICSSTTASRHHPTTLAVGICSPASRSISLLRLSFHQGCTIASQRLTPLARGDTLCTNLTGTLLPSRNTDETFFGVQWVRP	Clinical trial	ClinicalTrials.gov (NCT03125577) Combination CAR-T Cell Therapy Targeting Hematological Malignancies	19	Cytokine	.	tumor necrosis factor family.	.	.	TNF(Tumour Necrosis Factor) family 	PF00229	PF00229; TNF	.	.	hsa04060:Cytokine-cytokine receptor interaction	R-HSA-5669034:TNFs bind their physiological receptors	.	P32970
TTCMYP9	HLA-DR antigens-associated invariant (CD74)	P04233	HG2A_HUMAN	.	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	CD74	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.	.	5KSV; 5KSU; 4X5W; 4AH2; 4AEN	MHRRRSRSCREDQKPVMDDQRDLISNNEQLPMLGRRPGAPESKCSRGALYTGFSILVTLLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMKLPKPPKPVSKMRMATPLLMQALPMGALPQGPMQNATKYGNMTEDHVMHLLQNADPLKVYPPLKGSFPENLRHLKNTMETIDWKVFESWMHHWLLFEMSRHSLEQKPTDAPPKVLTKCQEEVSHIPAVHPGSFRPKCDENGNYLPLQCYGSIGYCWCVFPNGTEVPNTRSRGHHNCSESLELEDPSSGLGVTKQDLGPVPM	Clinical trial	Combination anti-CD74 (milatuzumab) and anti-CD20 (rituximab) monoclonal antibody therapy has in vitro and in vivo activity in mantle cell lymphoma. Blood. 2011 Apr 28;117(17):4530-41.	19	.	.	.	.	.	"CLIP, MHC2 interacting; Class II MHC-associated invariant chain trimerisation domain; Thyroglobulin type-1 repeat"	PF09307; PF08831; PF00086	PF09307; MHC2-interact; PF08831; MHCassoc_trimer; PF00086; Thyroglobulin_1	.	.	hsa04612:Antigen processing and presentation; hsa05152:Tuberculosis; hsa05168:Herpes simplex infection	R-HSA-2132295:MHC class II antigen presentation	.	P04233
TTI6LBU	CD74 messenger RNA (CD74 mRNA)	P04233	HG2A_HUMAN	mRNA target	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)	CD74	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.	.	5KSV; 5KSU; 4X5W; 4AH2; 4AEN	MHRRRSRSCREDQKPVMDDQRDLISNNEQLPMLGRRPGAPESKCSRGALYTGFSILVTLLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMKLPKPPKPVSKMRMATPLLMQALPMGALPQGPMQNATKYGNMTEDHVMHLLQNADPLKVYPPLKGSFPENLRHLKNTMETIDWKVFESWMHHWLLFEMSRHSLEQKPTDAPPKVLTKCQEEVSHIPAVHPGSFRPKCDENGNYLPLQCYGSIGYCWCVFPNGTEVPNTRSRGHHNCSESLELEDPSSGLGVTKQDLGPVPM	Literature-reported	CD74 is expressed by multiple myeloma and is a promising target for therapy. Clin Cancer Res. 2004 Oct 1;10(19):6606-11.	.	mRNA	mRNA target	.	.	.	"CLIP, MHC2 interacting; Class II MHC-associated invariant chain trimerisation domain; Thyroglobulin type-1 repeat"	PF09307; PF08831; PF00086	PF09307; MHC2-interact; PF08831; MHCassoc_trimer; PF00086; Thyroglobulin_1	.	.	hsa04612: Antigen processing and presentation; hsa05152: Tuberculosis; hsa05168: Herpes simplex virus 1 infection	R-HSA-202733: Cell surface interactions at the vascular wall; R-HSA-2132295: MHC class II antigen presentation	.	P04233
TTBN5I7	B-cell-specific glycoprotein B29 (CD79B)	P40259	CD79B_HUMAN	Immunoglobulin	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	CD79B	"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."	.	3KG5	MARLALSPVPSHWMVALLLLLSAEPVPAARSEDRYRNPKGSACSRIWQSPRFIARKRGFTVKMHCYMNSASGNVSWLWKQEMDENPQQLKLEKGRMEESQNESLATLTIQGIRFEDNGIYFCQQKCNNTSEVYQGCGTELRVMGFSTLAQLKQRNTLKDGIIMIQTLLIILFIIVPIFLLLDKDDSKAGMEEDHTYEGLDIDQTATYEDIVTLRTGEVKWSVGEHPGQE	Successful	Safety and activity of the anti-CD79B antibody-drug conjugate polatuzumab vedotin in relapsed or refractory B-cell non-Hodgkin lymphoma and chronic lymphocytic leukaemia: a phase 1 study. Lancet Oncol. 2015 Jun;16(6):704-15.	25	Immunoglobulin	.	.	.	.	Immunoglobulin V-set domain	PF07686	PF07686; V-set	.	.	hsa04662:B cell receptor signaling pathway	R-HSA-983695:Antigen activates B Cell Receptor (BCR) leading to generation of second messengers	.	P40259
TT89Z17	B7 translation initiation codon region messenger RNA (CD80 mRNA)	P33681	CD80_HUMAN	mRNA target	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)	CD80	"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."	.	1I8L; 1DR9	MGHTRRQGTSPSKCPYLNFFQLLVLAGLSHFCSGVIHVTKEVKEVATLSCGHNVSVEELAQTRIYWQKEKKMVLTMMSGDMNIWPEYKNRTIFDITNNLSIVILALRPSDEGTYECVVLKYEKDAFKREHLAEVTLSVKADFPTPSISDFEIPTSNIRRIICSTSGGFPEPHLSWLENGEELNAINTTVSQDPETELYAVSSKLDFNMTTNHSFMCLIKYGHLRVNQTFNWNTTKQEHFPDNLLPSWAITLISVNGIFVICCLTYCFAPRCRERRRNERLRRESVRPV	Literature-reported	"US patent application no. 6,319,906, Oligonucleotide compositions and methods for the modulation of the expression of B7 protein."	0	mRNA	mRNA target	.	.	.	CD80-like C2-set immunoglobulin domain ; Immunoglobulin V-set domain	PF08205; PF07686	PF08205; C2-set_2; PF07686; V-set	.	.	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	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	.	P33681
TTFZDNP	Activation B7-1 antigen (CD80)	P33681	CD80_HUMAN	.	T-lymphocyte activation antigen CD80; LAB7; CTLA-4 counter-receptor B7.1; CD28LG1; CD28LG; BB1; B7	CD80	"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."	.	1I8L; 1DR9	MGHTRRQGTSPSKCPYLNFFQLLVLAGLSHFCSGVIHVTKEVKEVATLSCGHNVSVEELAQTRIYWQKEKKMVLTMMSGDMNIWPEYKNRTIFDITNNLSIVILALRPSDEGTYECVVLKYEKDAFKREHLAEVTLSVKADFPTPSISDFEIPTSNIRRIICSTSGGFPEPHLSWLENGEELNAINTTVSQDPETELYAVSSKLDFNMTTNHSFMCLIKYGHLRVNQTFNWNTTKQEHFPDNLLPSWAITLISVNGIFVICCLTYCFAPRCRERRRNERLRRESVRPV	Successful	Selective modulation of T-cell co-stimulation: a novel mode of action for the treatment of rheumatoid arthritis. Clin Exp Rheumatol. 2009 May-Jun;27(3):510-8.	34	.	.	.	.	.	CD80-like C2-set immunoglobulin domain ; Immunoglobulin V-set domain	PF08205; PF07686	PF08205; C2-set_2; PF07686; V-set	.	.	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	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	.	P33681
TT5YPJF	CD80-PD-L1 interaction (CD80/PD-L1 PPI)	P33681-Q9NZQ7	CD80_HUMAN-PD1L1_HUMAN	.	T-lymphocyte activation antigen CD80/Programmed cell death 1 ligand 1 PPI	CD80-CD274	Augments activated alloreactive CD4+ T cell proliferation and apoptosis and ameliorates acute graft versus host disease	.	.	MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHLEETMGHTRRQGTSPSKCPYLNFFQLLVLAGLSHFCSGVIHVTKEVKEVATLSCGHNVSVEELAQTRIYWQKEKKMVLTMMSGDMNIWPEYKNRTIFDITNNLSIVILALRPSDEGTYECVVLKYEKDAFKREHLAEVTLSVKADFPTPSISDFEIPTSNIRRIICSTSGGFPEPHLSWLENGEELNAINTTVSQDPETELYAVSSKLDFNMTTNHSFMCLIKYGHLRVNQTFNWNTTKQEHFPDNLLPSWAITLISVNGIFVICCLTYCFAPRCRERRRNERLRRESVRPV	Patented-recorded	"A patent review on PD-1/PD-L1 antagonists: small molecules, peptides, and macrocycles (2015-2018).Expert Opin Ther Pat. 2018 Sep;28(9):665-678."	15.5	.	.	.	.	.	.	.	.	.	.	.	.	.	P33681
TTT9MRQ	Cell surface protein HB15 (CD83)	Q01151	CD83_HUMAN	Immunoglobulin	hCD83; CD83 antigen; Bcell activation protein; B-cell activation protein	CD83	May play a significant role in antigen presentation or the cellular interactions that follow lymphocyte activation.	.	5MJ2; 5MJ1; 5MJ0; 5MIX	MSRGLQLLLLSCAYSLAPATPEVKVACSEDVDLPCTAPWDPQVPYTVSWVKLLEGGEERMETPQEDHLRGQHYHQKGQNGSFDAPNERPYSLKIRNTTSCNSGTYRCTLQDPDGQRNLSGKVILRVTGCPAQRKEETFKKYRAEIVLLLALVIFYLTLIIFTCKFARLQSIFPDFSKAGMERAFLPVTSPNKHLGLVTPHKTELV	Literature-reported	CD83 is a new potential biomarker and therapeutic target for Hodgkin lymphoma. Haematologica. 2018 Apr;103(4):655-665.	.	Immunoglobulin	Immunoglobulin superfamily	.	.	.	Immunoglobulin V-set domain	PF07686	PF07686; V-set	.	.	.	.	.	Q01151
TT53XHB	CD86 messenger RNA (CD86 mRNA)	P42081	CD86_HUMAN	mRNA target	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)	CD86	"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."	.	5YXK; 1NCN; 1I85	MDPQCTMGLSNILFVMAFLLSGAAPLKIQAYFNETADLPCQFANSQNQSLSELVVFWQDQENLVLNEVYLGKEKFDSVHSKYMGRTSFDSDSWTLRLHNLQIKDKGLYQCIIHHKKPTGMIRIHQMNSELSVLANFSQPEIVPISNITENVYINLTCSSIHGYPEPKKMSVLLRTKNSTIEYDGVMQKSQDNVTELYDVSISLSVSFPDVTSNMTIFCILETDKTRLLSSPFSIELEDPQPPPDHIPWITAVLPTVIICVMVFCLILWKWKKKKRPRNSYKCGTNTMEREESEQTKKREKIHIPERSDEAQRVFKSSKTSSCDKSDTCF	Literature-reported	"US patent application no. 6,319,906, Oligonucleotide compositions and methods for the modulation of the expression of B7 protein."	0	mRNA	mRNA target	.	.	.	Immunoglobulin domain; Immunoglobulin V-set domain	PF13895; PF07686	PF13895; Ig_2; PF07686; V-set	.	.	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	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	.	P42081
TTHGXBU	T-lymphocyte activation antigen CD86 (FUN1)	P42081	CD86_HUMAN	Immunoglobulin	FUN-1; CTLA-4 counter-receptor B7.2; CD86; CD28LG2; BU63; B70; Activation B7-2 antigen	CD86	"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."	.	5YXK; 1NCN; 1I85	MDPQCTMGLSNILFVMAFLLSGAAPLKIQAYFNETADLPCQFANSQNQSLSELVVFWQDQENLVLNEVYLGKEKFDSVHSKYMGRTSFDSDSWTLRLHNLQIKDKGLYQCIIHHKKPTGMIRIHQMNSELSVLANFSQPEIVPISNITENVYINLTCSSIHGYPEPKKMSVLLRTKNSTIEYDGVMQKSQDNVTELYDVSISLSVSFPDVTSNMTIFCILETDKTRLLSSPFSIELEDPQPPPDHIPWITAVLPTVIICVMVFCLILWKWKKKKRPRNSYKCGTNTMEREESEQTKKREKIHIPERSDEAQRVFKSSKTSSCDKSDTCF	Successful	Selective modulation of T-cell co-stimulation: a novel mode of action for the treatment of rheumatoid arthritis. Clin Exp Rheumatol. 2009 May-Jun;27(3):510-8.	34	.	.	.	.	.	.	.	.	.	.	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	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	.	P42081
TTMHA6L	T-cell surface glycoprotein CD8 (CD8)	P01732; P10966	CD8A_HUMAN; CD8B_HUMAN	.	T-lymphocyte differentiation antigen T8/Leu-2; CD8	CD8A	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.	.	.	MALPVTALLLPLALLLHAARPSQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKAAEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPAKPTTTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV	Clinical trial	"A novel peptide-based pan-influenza A vaccine: a double blind, randomised clinical trial of immunogenicity and safety. Vaccine. 2015 Jan 3;33(2):396-402."	21	.	.	.	.	.	.	.	.	.	.	hsa04514:Cell adhesion molecules (CAMs); hsa04612:Antigen processing and presentation; hsa04640:Hematopoietic cell lineage; hsa04660:T cell receptor signaling pathway; hsa05340:Primary immunodeficiency	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	P01732
TTZEIBV	Leukocyte antigen MIC3 (CD9)	P21926	CD9_HUMAN	Tetraspanin	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	CD9	"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."	.	.	MPVKGGTKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNNNNSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAIWGYSHKDEVIKEVQEFYKDTYNKLKTKDEPQRETLKAIHYALNCCGLAGGVEQFISDICPKKDVLETFTVKSCPDAIKEVFDNKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRNREMV	Literature-reported	CD9 Expression in Colorectal Carcinomas and Its Prognostic Significance. J Pathol Transl Med. 2016 Nov;50(6):459-468.	.	TC=8.A.40	Tetraspanin family	tetraspanin (TM4SF) family.	.	.	Tetraspanin family	PF00335	PF00335; Tetraspanin	8.A.40.1.9	The Tetraspanin (Tetraspanin) Family	hsa04640: Hematopoietic cell lineage	R-HSA-114608: Platelet degranulation; R-HSA-1300645: Acrosome Reaction and Sperm:Oocyte Membrane Binding; R-HSA-5336415: Uptake and function of diphtheria toxin	.	P21926
TT83C4X	T-cell surface protein tactile (CD96)	P40200	TACT_HUMAN	.	Cell surface antigen CD96; T cell-activated increased late expression protein; DE   AltName: CD_antigen=CD96	CD96	"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."	.	.	MEKKWKYCAVYYIIQIHFVKGVWEKTVNTEENVYATLGSDVNLTCQTQTVGFFVQMQWSKVTNKIDLIAVYHPQYGFYCAYGRPCESLVTFTETPENGSKWTLHLRNMSCSVSGRYECMLVLYPEGIQTKIYNLLIQTHVTADEWNSNHTIEIEINQTLEIPCFQNSSSKISSEFTYAWSVENSSTDSWVLLSKGIKEDNGTQETLISQNHLISNSTLLKDRVKLGTDYRLHLSPVQIFDDGRKFSCHIRVGPNKILRSSTTVKVFAKPEIPVIVENNSTDVLVERRFTCLLKNVFPKANITWFIDGSFLHDEKEGIYITNEERKGKDGFLELKSVLTRVHSNKPAQSDNLTIWCMALSPVPGNKVWNISSEKITFLLGSEISSTDPPLSVTESTLDTQPSPASSVSPARYPATSSVTLVDVSALRPNTTPQPSNSSMTTRGFNYPWTSSGTDTKKSVSRIPSETYSSSPSGAGSTLHDNVFTSTARAFSEVPTTANGSTKTNHVHITGIVVNKPKDGMSWPVIVAALLFCCMILFGLGVRKWCQYQKEIMERPPPFKPPPPPIKYTCIQEPNESDLPYHEMETL	Clinical trial	National Cancer Institute Drug Dictionary (drug name GSK6097608).	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	P40200
TTTK61E	Leukocyte antigen CD97 (CD97)	P48960	CD97_HUMAN	GPCR secretin	CD97 antigen subunit beta; CD97 antigen	CD97	Plays an essential role in leukocyte migration. Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation.	.	2BOU	MGGRVFLAFCVWLTLPGAETQDSRGCARWCPQNSSCVNATACRCNPGFSSFSEIITTPTETCDDINECATPSKVSCGKFSDCWNTEGSYDCVCSPGYEPVSGAKTFKNESENTCQDVDECQQNPRLCKSYGTCVNTLGSYTCQCLPGFKFIPEDPKVCTDVNECTSGQNPCHSSTHCLNNVGSYQCRCRPGWQPIPGSPNGPNNTVCEDVDECSSGQHQCDSSTVCFNTVGSYSCRCRPGWKPRHGIPNNQKDTVCEDMTFSTWTPPPGVHSQTLSRFFDKVQDLGRDSKTSSAEVTIQNVIKLVDELMEAPGDVEALAPPVRHLIATQLLSNLEDIMRILAKSLPKGPFTYISPSNTELTLMIQERGDKNVTMGQSSARMKLNWAVAAGAEDPGPAVAGILSIQNMTTLLANASLNLHSKKQAELEEIYESSIRGVQLRRLSAVNSIFLSHNNTKELNSPILFAFSHLESSDGEAGRDPPAKDVMPGPRQELLCAFWKSDSDRGGHWATEGCQVLGSKNGSTTCQCSHLSSFAILMAHYDVEDWKLTLITRVGLALSLFCLLLCILTFLLVRPIQGSRTTIHLHLCICLFVGSTIFLAGIENEGGQVGLRCRLVAGLLHYCFLAAFCWMSLEGLELYFLVVRVFQGQGLSTRWLCLIGYGVPLLIVGVSAAIYSKGYGRPRYCWLDFEQGFLWSFLGPVTFIILCNAVIFVTTVWKLTQKFSEINPDMKKLKKARALTITAIAQLFLLGCTWVFGLFIFDDRSLVLTYVFTILNCLQGAFLYLLHCLLNKKVREEYRKWACLVAGGSKYSEFTSTTSGTGHNQTRALRASESGI	Literature-reported	Effects of siRNAs targeting CD97 immune epitopes on biological behavior in breast cancer cell line MDA-MB231. Zhejiang Da Xue Xue Bao Yi Xue Ban. 2017 Jul 25;46(4):341-348.	.	PF00002	.	G-protein coupled receptor 2 family. LN-TM7 subfamily.	.	.	"7 transmembrane receptor (Secretin family); Calcium-binding EGF domain; GPCR proteolysis site, GPS, motif "	PF00002; PF07645; PF01825	PF00002; 7tm_2; PF07645; EGF_CA; PF01825; GPS	9.A.14.6.2	The G-protein-coupled receptor (GPCR) Family	.	R-HSA-373080: Class B/2 (Secretin family receptors); R-HSA-6798695: Neutrophil degranulation	.	.
TTQ12RK	Cytidine deaminase (CDA)	P32320	CDD_HUMAN	Carbon-nitrogen hydrolase	Cytidine aminohydrolase; CDA	CDA	This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.	EC 3.5.4.5	1MQ0	MAQKRPACTLKPECVQQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMQDDFISPCGACRQVMREFGTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDLQKTQ	Clinical trial	Tetrahydrouridine inhibits cell proliferation through cell cycle regulation regardless of cytidine deaminase expression levels. PLoS One. 2012;7(5):e37424.	21	.	.	.	.	.	.	.	.	.	.	hsa00240:Pyrimidine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways	R-HSA-6798695: Neutrophil degranulation; R-HSA-73614: Pyrimidine salvage	MetaCyc:HS08334-MON	P32320
TT3PRUG	Cell division cycle protein 123 (CDC123)	O75794	CD123_HUMAN	.	Protein D123; HT-1080; PZ32	CDC123	Required for S phase entry of the cell cycle. {ECO:0000250}.	.	.	MKKEHVLHCQFSAWYPFFRGVTIKSVILPLPQNVKDYLLDDGTLVVSGRDDPPTHSQPDSDDEAEEIQWSDDENTATLTAPEFPEFATKVQEAINSLGGSVFPKLNWSAPRDAYWIAMNSSLKCKTLSDIFLLFKSSDFITRDFTQPFIHCTDDSPDPCIEYELVLRKWCELIPGAEFRCFVKENKLIGISQRDYTQYYDHISKQKEEIRRCIQDFFKKHIQYKFLDEDFVFDIYRDSRGKVWLIDFNPFGEVTDSLLFTWEELISENNLNGDFSEVDAQEQDSPAFRCTNSEVTVQPSPYLSYRLPKDFVDLSTGEDAHKLIDFLKLKRNQQEDD	Clinical trial	"Clinical pipeline report, company report or official report of Sanofi "	.	.	.	.	.	.	.	.	.	.	.	hsa:8872	.	.	O75794;
TTBKFDV	Cell division cycle protein 20 homolog (CDC20)	Q12834	CDC20_HUMAN	.	p55CDC	CDC20	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.	.	.	MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYIPHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGSSRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNYLAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPDGRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHSQVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARRREREKASAAKSSLIHQGIR	Preclinical	Targeting Cdc20 as a novel cancer therapeutic strategy. Pharmacol Ther. 2015 Jul;151:141-51.	.	.	.	.	.	.	.	.	.	.	.	hsa04110: Cell cycle; hsa04114: Oocyte meiosis; hsa04120: Ubiquitin mediated proteolysis; hsa05166: Human T-cell leukemia virus 1 infection; hsa05203: Viral carcinogenesis	R-HSA-141405: Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components; R-HSA-141430: Inactivation of APC/C via direct inhibition of the APC/C complex; R-HSA-141444: Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal; R-HSA-174048: APC/C:Cdc20 mediated degradation of Cyclin B; R-HSA-174113: SCF-beta-TrCP mediated degradation of Emi1; R-HSA-174154: APC/C:Cdc20 mediated degradation of Securin; R-HSA-174178: APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1; R-HSA-174184: Cdc20:Phospho-APC/C mediated degradation of Cyclin A; R-HSA-176407: Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase; R-HSA-176408: Regulation of APC/C activators between G1/S and early anaphase; R-HSA-176409: APC/C:Cdc20 mediated degradation of mitotic proteins; R-HSA-176417: Phosphorylation of Emi1; R-HSA-179409: APC-Cdc20 mediated degradation of Nek2A; R-HSA-2467813: Separation of Sister Chromatids; R-HSA-2500257: Resolution of Sister Chromatid Cohesion; R-HSA-5663220: RHO GTPases Activate Formins; R-HSA-5689880: Ub-specific processing proteases; R-HSA-68877: Mitotic Prometaphase; R-HSA-9648025: EML4 and NUDC in mitotic spindle formation; R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	Q12834
TTLZS4Q	M-phase inducer phosphatase 1 (MPIP1)	P30304	MPIP1_HUMAN	Phosphoric monoester hydrolase	Dual specificity phosphatase Cdc25A; Cdc25A phosphatase	CDC25A	"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."	EC 3.1.3.48	1C25	MELGPEPPHRRRLLFACSPPPASQPVVKALFGASAAGGLSPVTNLTVTMDQLQGLGSDYEQPLEVKNNSNLQRMGSSESTDSGFCLDSPGPLDSKENLENPMRRIHSLPQKLLGCSPALKRSHSDSLDHDIFQLIDPDENKENEAFEFKKPVRPVSRGCLHSHGLQEGKDLFTQRQNSAPARMLSSNERDSSEPGNFIPLFTPQSPVTATLSDEDDGFVDLLDGENLKNEEETPSCMASLWTAPLVMRTTNLDNRCKLFDSPSLCSSSTRSVLKRPERSQEESPPGSTKRRKSMSGASPKESTNPEKAHETLHQSLSLASSPKGTIENILDNDPRDLIGDFSKGYLFHTVAGKHQDLKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSERGPRMCRYVRERDRLGNEYPKLHYPELYVLKGGYKEFFMKCQSYCEPPSYRPMHHEDFKEDLKKFRTKSRTWAGEKSKREMYSRLKKL	Literature-reported	"Handbook of Assay Development in Drug Discovery, Lisa K. Minor, 2013. Page(11)."	2	EC:3.1.3	Phosphoric monoester hydrolases	MPI phosphatase family.	3.1.3.48	Acting on ester bonds	M-phase inducer phosphatase; Rhodanese-like domain	PF06617; PF00581	PF06617; M-inducer_phosp; PF00581; Rhodanese	.	.	hsa04110:Cell cycle; hsa04914:Progesterone-mediated oocyte maturation; hsa05206:MicroRNAs in cancer	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	.	P30304
TT9C46Y	Dual specificity phosphatase Cdc25 (CDC25)	P30304; P30305; P30307	MPIP1_HUMAN; MPIP2_HUMAN; MPIP3_HUMAN	.	M-phase inducer phosphatase	CDC25A	"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."	.	.	MELGPEPPHRRRLLFACSPPPASQPVVKALFGASAAGGLSPVTNLTVTMDQLQGLGSDYEQPLEVKNNSNLQRMGSSESTDSGFCLDSPGPLDSKENLENPMRRIHSLPQKLLGCSPALKRSHSDSLDHDIFQLIDPDENKENEAFEFKKPVRPVSRGCLHSHGLQEGKDLFTQRQNSAPARMLSSNERDSSEPGNFIPLFTPQSPVTATLSDEDDGFVDLLDGENLKNEEETPSCMASLWTAPLVMRTTNLDNRCKLFDSPSLCSSSTRSVLKRPERSQEESPPGSTKRRKSMSGASPKESTNPEKAHETLHQSLSLASSPKGTIENILDNDPRDLIGDFSKGYLFHTVAGKHQDLKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSERGPRMCRYVRERDRLGNEYPKLHYPELYVLKGGYKEFFMKCQSYCEPPSYRPMHHEDFKEDLKKFRTKSRTWAGEKSKREMYSRLKKL	Literature-reported	Identification of a potent and selective pharmacophore for Cdc25 dual specificity phosphatase inhibitors. Mol Pharmacol. 2002 Apr;61(4):720-8.	.	.	.	.	.	.	.	.	.	.	.	hsa04110: Cell cycle; hsa04218: Cellular senescence; hsa04914: Progesterone-mediated oocyte maturation; hsa05206: MicroRNAs in cancer; hsa05207: Chemical carcinogenesis - receptor activation	R-HSA-1362277: Transcription of E2F targets under negative control by DREAM complex; R-HSA-156711: Polo-like kinase mediated events; R-HSA-176187: Activation of ATR in response to replication stress; R-HSA-5689880: Ub-specific processing proteases; R-HSA-69202: Cyclin E associated events during G1/S transition; R-HSA-69273: Cyclin A/B1/B2 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; R-HSA-8862803: Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models	.	P30304
TTR0SWN	M-phase inducer phosphatase 2 (MPIP2)	P30305	MPIP2_HUMAN	Phosphoric monoester hydrolase	Dual specificity phosphatase Cdc25B; Cdc25B phosphatase; CDC25HU2	CDC25B	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.	EC 3.1.3.48	4WH9; 4WH7; 3FQU; 3FQT; 2UZQ	MEVPQPEPAPGSALSPAGVCGGAQRPGHLPGLLLGSHGLLGSPVRAAASSPVTTLTQTMHDLAGLGSETPKSQVGTLLFRSRSRLTHLSLSRRASESSLSSESSESSDAGLCMDSPSPMDPHMAEQTFEQAIQAASRIIRNEQFAIRRFQSMPVRLLGHSPVLRNITNSQAPDGRRKSEAGSGAASSSGEDKENDGFVFKMPWKPTHPSSTHALAEWASRREAFAQRPSSAPDLMCLSPDRKMEVEELSPLALGRFSLTPAEGDTEEDDGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQNKRRRSVTPPEEQQEAEEPKARVLRSKSLCHDEIENLLDSDHRELIGDYSKAFLLQTVDGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIAPCSLDKRVILIFHCEFSSERGPRMCRFIRERDRAVNDYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPMNHEAFKDELKTFRLKTRSWAGERSRRELCSRLQDQ	Clinical trial	"Bioactivities of simplified adociaquinone B and naphthoquinone derivatives against Cdc25B, MKP-1, and MKP-3 phosphatases. Bioorg Med Chem. 2009 Mar 15;17(6):2276-81."	25	EC:3.1.3	Phosphoric monoester hydrolases	MPI phosphatase family.	3.1.3.48	Acting on ester bonds	M-phase inducer phosphatase; Rhodanese-like domain	PF06617; PF00581	PF06617; M-inducer_phosp; PF00581; Rhodanese	.	.	hsa04010:MAPK signaling pathway; hsa04110:Cell cycle; hsa04914:Progesterone-mediated oocyte maturation; hsa05206:MicroRNAs in cancer	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	.	P30305
TTESBNC	M-phase inducer phosphatase 3 (MPIP3)	P30307	MPIP3_HUMAN	Phosphoric monoester hydrolase	Dual specificity phosphatase Cdc25C; Cdc25C phosphatase	CDC25C	"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."	EC 3.1.3.48	5M37; 5M36; 5M35; 3OP3; 3BZI	MSTELFSSTREEGSSGSGPSFRSNQRKMLNLLLERDTSFTVCPDVPRTPVGKFLGDSANLSILSGGTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSPAQLLCSTPNGLDRGHRKRDAMCSSSANKENDNGNLVDSEMKYLGSPITTVPKLDKNPNLGEDQAEEISDELMEFSLKDQEAKVSRSGLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVKKKYFSGQGKLRKGLCLKKTVSLCDITITQMLEEDSNQGHLIGDFSKVCALPTVSGKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIVFHCEFSSERGPRMCRCLREEDRSLNQYPALYYPELYILKGGYRDFFPEYMELCEPQSYCPMHHQDHKTELLRCRSQSKVQEGERQLREQIALLVKDMSP	Literature-reported	"Handbook of Assay Development in Drug Discovery, Lisa K. Minor, 2013. Page(11)."	2	EC:3.1.3	Phosphoric monoester hydrolases	MPI phosphatase family.	3.1.3.48	Acting on ester bonds	M-phase inducer phosphatase; Rhodanese-like domain	PF06617; PF00581	PF06617; M-inducer_phosp; PF00581; Rhodanese	.	.	hsa04110:Cell cycle; hsa04114:Oocyte meiosis; hsa04914:Progesterone-mediated oocyte maturation; hsa05206:MicroRNAs in cancer	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	.	P30307
TT5SOEU	Hsp90 co-chaperone Cdc37 (CDC37)	Q16543	CDC37_HUMAN	.	"p50Cdc37; Hsp90 co-chaperone Cdc37, N-terminally processed; Hsp90 chaperone protein kinase-targeting subunit; CDC37A"	CDC37	"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."	.	5HPE; 5FWP; 5FWM; 5FWL; 5FWK	MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLSKDGFSKSMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTKIKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKEGEEAGPGDPLLEAVPKTGDEKDVSV	Literature-reported	The Hsp90 kinase co-chaperone Cdc37 regulates tau stability and phosphorylation dynamics. J Biol Chem. 2011 May 13;286(19):16976-83.	.	.	.	CDC37 family.	.	.	Cdc37 C terminal domain; Cdc37 Hsp90 binding domain; Cdc37 N terminal kinase binding	PF08564; PF08565; PF03234	PF08564; CDC37_C; PF08565; CDC37_M; PF03234; CDC37_N	.	.	hsa04151:PI3K-Akt signaling pathway	R-HSA-1227986: Signaling by ERBB2; R-HSA-1236382: Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-5637810: Constitutive Signaling by EGFRvIII; R-HSA-5675482: Regulation of necroptotic cell death; R-HSA-8863795: Downregulation of ERBB2 signaling; R-HSA-9013418: RHOBTB2 GTPase cycle; R-HSA-9634285: Constitutive Signaling by Overexpressed ERBB2; R-HSA-9652282: Drug-mediated inhibition of ERBB2 signaling; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665233: Resistance of ERBB2 KD mutants to trastuzumab; R-HSA-9665244: Resistance of ERBB2 KD mutants to sapitinib; R-HSA-9665245: Resistance of ERBB2 KD mutants to tesevatinib; R-HSA-9665246: Resistance of ERBB2 KD mutants to neratinib; R-HSA-9665247: Resistance of ERBB2 KD mutants to osimertinib; R-HSA-9665249: Resistance of ERBB2 KD mutants to afatinib; R-HSA-9665250: Resistance of ERBB2 KD mutants to AEE788; R-HSA-9665251: Resistance of ERBB2 KD mutants to lapatinib; R-HSA-9665348: Signaling by ERBB2 ECD mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants; R-HSA-9665737: Drug resistance in ERBB2 TMD/JMD mutants	.	Q16543
TT5Z0EF	CDC42 binding protein kinase alpha (DMPK-like alpha)	Q5VT25	MRCKA_HUMAN	Kinase	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	CDC42BPA	"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."	EC 2.7.11.1	.	MSGEVRLRQLEQFILDGPAQTNGQCFSVETLLDILICLYDECNNSPLRREKNILEYLEWAKPFTSKVKQMRLHREDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDNKWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEDMARFYLAEMVIAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQSSVAVGTPDYISPEILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKERFQFPAQVTDVSENAKDLIRRLICSREHRLGQNGIEDFKKHPFFSGIDWDNIRNCEAPYIPEVSSPTDTSNFDVDDDCLKNSETMPPPTHTAFSGHHLPFVGFTYTSSCVLSDRSCLRVTAGPTSLDLDVNVQRTLDNNLATEAYERRIKRLEQEKLELSRKLQESTQTVQALQYSTVDGPLTASKDLEIKNLKEEIEKLRKQVTESSHLEQQLEEANAVRQELDDAFRQIKAYEKQIKTLQQEREDLNKELVQASERLKNQSKELKDAHCQRKLAMQEFMEINERLTELHTQKQKLARHVRDKEEEVDLVMQKVESLRQELRRTERAKKELEVHTEALAAEASKDRKLREQSEHYSKQLENELEGLKQKQISYSPGVCSIEHQQEITKLKTDLEKKSIFYEEELSKREGIHANEIKNLKKELHDSEGQQLALNKEIMILKDKLEKTRRESQSEREEFESEFKQQYEREKVLLTEENKKLTSELDKLTTLYENLSIHNQQLEEEVKDLADKKESVAHWEAQITEIIQWVSDEKDARGYLQALASKMTEELEALRNSSLGTRATDMPWKMRRFAKLDMSARLELQSALDAEIRAKQAIQEELNKVKASNIITECKLKDSEKKNLELLSEIEQLIKDTEELRSEKGIEHQDSQHSFLAFLNTPTDALDQFERSPSCTPASKGRRTVDSTPLSVHTPTLRKKGCPGSTGFPPKRKTHQFFVKSFTTPTKCHQCTSLMVGLIRQGCSCEVCGFSCHITCVNKAPTTCPVPPEQTKGPLGIDPQKGIGTAYEGHVRIPKPAGVKKGWQRALAIVCDFKLFLYDIAEGKASQPSVVISQVIDMRDEEFSVSSVLASDVIHASRKDIPCIFRVTASQLSASNNKCSILMLADTENEKNKWVGVLSELHKILKKNKFRDRSVYVPKEAYDSTLPLIKTTQAAAIIDHERIALGNEEGLFVVHVTKDEIIRVGDNKKIHQIELIPNDQLVAVISGRNRHVRLFPMSALDGRETDFYKLSETKGCQTVTSGKVRHGALTCLCVAMKRQVLCYELFQSKTRHRKFKEIQVPYNVQWMAIFSEQLCVGFQSGFLRYPLNGEGNPYSMLHSNDHTLSFIAHQPMDAICAVEISSKEYLLCFNSIGIYTDCQGRRSRQQELMWPANPSSCCYNAPYLSVYSENAVDIFDVNSMEWIQTLPLKKVRPLNNEGSLNLLGLETIRLIYFKNKMAEGDELVVPETSDNSRKQMVRNINNKRRYSFRVPEEERMQQRREMLRDPEMRNKLISNPTNFNHIAHMGPGDGIQILKDLPMNPRPQESRTVFSGSVSIPSITKSRPEPGRSMSASSGLSARSSAQNGSALKREFSGGSYSAKRQPMPSPSEGSLSSGGMDQGSDAPARDFDGEDSDSPRHSTASNSSNLSSPPSPASPRKTKSLSLESTDRGSWDP	Literature-reported	Pyridylthiazole-based ureas as inhibitors of Rho associated protein kinases (ROCK1 and 2). Medchemcomm. 2012 Jun 1;3(6):699-709.	0	EC:2.7	.	protein kinase superfamily. AGC Ser/Thr protein kinase family. DMPK subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Phorbol esters/diacylglycerol binding domain (C1 domain); CNH domain; DMPK coiled coil domain like; KELK-motif containing domain of MRCK Ser/Thr protein kinase; Protein kinase domain; Protein kinase C terminal domain	PF00130; PF00780; PF08826; PF15796; PF00069; PF00433	PF00130; C1_1; PF00780; CNH; PF08826; DMPK_coil; PF15796; KELK; PF00069; Pkinase; PF00433; Pkinase_C	.	.	.	R-HSA-9013148: CDC42 GTPase cycle; R-HSA-9013149: RAC1 GTPase cycle; R-HSA-9013406: RHOQ GTPase cycle; R-HSA-9013409: RHOJ GTPase cycle	.	Q5VT25
TTSMTDI	CDC7-related kinase (CDC7)	O00311	CDC7_HUMAN	Kinase	huCdc7; HsCdc7; Cell division cycle 7related protein kinase; Cell division cycle 7-related protein kinase; CDC7related kinase; CDC7L1	CDC7	Can phosphorylates MCM2 and MCM3. Seems to phosphorylate critical substrates that regulate the G1/S phase transition and/or DNA replication.	EC 2.7.11.1	5UWR; 5UWQ; 4F9C; 4F9B; 4F9A	MEASLGIQMDEPMAFSPQRDRFQAEGSLKKNEQNFKLAGVKKDIEKLYEAVPQLSNVFKIEDKIGEGTFSSVYLATAQLQVGPEEKIALKHLIPTSHPIRIAAELQCLTVAGGQDNVMGVKYCFRKNDHVVIAMPYLEHESFLDILNSLSFQEVREYMLNLFKALKRIHQFGIVHRDVKPSNFLYNRRLKKYALVDFGLAQGTHDTKIELLKFVQSEAQQERCSQNKSHIITGNKIPLSGPVPKELDQQSTTKASVKRPYTNAQIQIKQGKDGKEGSVGLSVQRSVFGERNFNIHSSISHESPAVKLMKQSKTVDVLSRKLATKKKAISTKVMNSAVMRKTASSCPASLTCDCYATDKVCSICLSRRQQVAPRAGTPGFRAPEVLTKCPNQTTAIDMWSAGVIFLSLLSGRYPFYKASDDLTALAQIMTIRGSRETIQAAKTFGKSILCSKEVPAQDLRKLCERLRGMDSSTPKLTSDIQGHASHQPAISEKTDHKASCLVQTPPGQYSGNSFKKGDSNSCEHCFDEYNTNLEGWNEVPDEAYDLLDKLLDLNPASRITAEEALLHPFFKDMSL	Clinical trial	"Discovery of XL413, a potent and selective CDC7 inhibitor. Bioorg Med Chem Lett. 2012 Jun 1;22(11):3727-31."	19	EC:2.7	Kinase	protein kinase superfamily. Ser/Thr protein kinase family. CDC7 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04110: Cell cycle	R-HSA-176187: Activation of ATR in response to replication stress; R-HSA-68962: Activation of the pre-replicative complex; R-HSA-8953750: Transcriptional Regulation by E2F6	.	O00311
TT04YCM	Borealin (CDCA8)	Q53HL2	BOREA_HUMAN	.	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	CDCA8	"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."	.	2RAX; 2RAW; 2QFA; 2KDD	MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK	Literature-reported	"Hepatic Loss of Borealin Impairs Postnatal Liver Development, Regeneration, and Hepatocarcinogenesis. J Biol Chem. 2016 Sep 30;291(40):21137-21147."	.	.	.	borealin family.	.	.	Cell division cycle-associated protein 8 ; Nbl1 / Borealin N terminal	PF10512; PF10444	PF10512; Borealin; PF10444; Nbl1_Borealin_N	.	.	.	R-HSA-141444: Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal; R-HSA-2467813: Separation of Sister Chromatids; R-HSA-2500257: Resolution of Sister Chromatid Cohesion; R-HSA-4615885: SUMOylation of DNA replication proteins; R-HSA-5663220: RHO GTPases Activate Formins; R-HSA-68877: Mitotic Prometaphase; R-HSA-9648025: EML4 and NUDC in mitotic spindle formation	.	Q53HL2
TTLAWO6	Epithelial cadherin (CDH1)	P12830	CADH1_HUMAN	.	Uvomorulin; UVO; E-cadherin gene; E-cadherin; Cadherin-1; CDHE; CD324; CAM 120/80	CDH1	"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."	.	6CXY; 4ZTE; 4ZT1; 3L6Y; 3L6X	MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPAILGILGGILALLILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD	Literature-reported	The role of the E-cadherin gene (CDH1) in diffuse gastric cancer susceptibility: from the laboratory to clinical practice. Ann Oncol. 2003 Dec;14(12):1705-13.	.	.	Transmembrane protein	.	.	.	Cadherin domain; Cadherin cytoplasmic region; Cadherin prodomain like	PF00028; PF01049; PF08758	PF00028; Cadherin; PF01049; Cadherin_C; PF08758; Cadherin_pro	.	.	hsa04015: Rap1 signaling pathway; hsa04371: Apelin signaling pathway; hsa04390: Hippo signaling pathway; hsa04514: Cell adhesion molecules; hsa04520: Adherens junction; hsa05100: Bacterial invasion of epithelial cells; hsa05200: Pathways in cancer; hsa05213: Endometrial cancer; hsa05216: Thyroid cancer; hsa05218: Melanoma; hsa05219: Bladder cancer; hsa05226: Gastric cancer	R-HSA-1474228: Degradation of the extracellular matrix; R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-216083: Integrin cell surface interactions; R-HSA-351906: Apoptotic cleavage of cell adhesion proteins; R-HSA-418990: Adherens junctions interactions; R-HSA-5626467: RHO GTPases activate IQGAPs; R-HSA-8876493: InlA-mediated entry of Listeria monocytogenes into host cells	.	P12830
TTRGWZC	Osteoblast cadherin (CDH11)	P55287	CAD11_HUMAN	.	OSF4; OSF-4; OBcadherin; OB-cadherin; Cadherin-11	CDH11	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.	.	.	MKENYCLQAALVCLGMLCHSHAFAPERRGHLRPSFHGHHEKGKEGQVLQRSKRGWVWNQFFVIEEYTGPDPVLVGRLHSDIDSGDGNIKYILSGEGAGTIFVIDDKSGNIHATKTLDREERAQYTLMAQAVDRDTNRPLEPPSEFIVKVQDINDNPPEFLHETYHANVPERSNVGTSVIQVTASDADDPTYGNSAKLVYSILEGQPYFSVEAQTGIIRTALPNMDREAKEEYHVVIQAKDMGGHMGGLSGTTKVTITLTDVNDNPPKFPQSVYQMSVSEAAVPGEEVGRVKAKDPDIGENGLVTYNIVDGDGMESFEITTDYETQEGVIKLKKPVDFETKRAYSLKVEAANVHIDPKFISNGPFKDTVTVKISVEDADEPPMFLAPSYIHEVQENAAAGTVVGRVHAKDPDAANSPIRYSIDRHTDLDRFFTINPEDGFIKTTKPLDREETAWLNITVFAAEIHNRHQEAKVPVAIRVLDVNDNAPKFAAPYEGFICESDQTKPLSNQPIVTISADDKDDTANGPRFIFSLPPEIIHNPNFTVRDNRDNTAGVYARRGGFSRQKQDLYLLPIVISDGGIPPMSSTNTLTIKVCGCDVNGALLSCNAEAYILNAGLSTGALIAILACIVILLVIVVLFVTLRRQKKEPLIVFEEEDVRENIITYDDEGGGEEDTEAFDIATLQNPDGINGFIPRKDIKPEYQYMPRPGLRPAPNSVDVDDFINTRIQEADNDPTAPPYDSIQIYGYEGRGSVAGSLSSLESATTDSDLDYDYLQNWGPRFKKLADLYGSKDTFDDDS	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	Cadherin domain; Cadherin cytoplasmic region	PF00028; PF01049	PF00028; Cadherin; PF01049; Cadherin_C	.	.	.	R-HSA-418990: Adherens junctions interactions	.	P55287
TT1WS0T	Neural cadherin (CDH2)	P19022	CADH2_HUMAN	Cadherin protein	NCAD; N-cadherin; Cadherin-2; CDw325; CDHN; CD325	CDH2	"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."	.	.	MCRIAGALRTLLPLLAALLQASVEASGEIALCKTGFPEDVYSAVLSKDVHEGQPLLNVKFSNCNGKRKVQYESSEPADFKVDEDGMVYAVRSFPLSSEHAKFLIYAQDKETQEKWQVAVKLSLKPTLTEESVKESAEVEEIVFPRQFSKHSGHLQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDREQIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGTVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRIVSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYTLIIQATDMEGNPTYGLSNTATAVITVTDVNDNPPEFTAMTFYGEVPENRVDIIVANLTVTDKDQPHTPAWNAVYRISGGDPTGRFAIQTDPNSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHAGTMLTTFTAQDPDRYMQQNIRYTKLSDPANWLKIDPVNGQITTIAVLDRESPNVKNNIYNATFLASDNGIPPMSGTGTLQIYLLDINDNAPQVLPQEAETCETPDPNSINITALDYDIDPNAGPFAFDLPLSPVTIKRNWTITRLNGDFAQLNLKIKFLEAGIYEVPIIITDSGNPPKSNISILRVKVCQCDSNGDCTDVDRIVGAGLGTGAIIAILLCIIILLILVLMFVVWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTVEPDAIKPVGIRRMDERPIHAEPQYPVRSAAPHPGDIGDFINEGLKAADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGEQDYDYLNDWGPRFKKLADMYGGGDD	Clinical trial	"Clinical and pharmacological phase I evaluation of Exherin (ADH-1), a selective anti-N-cadherin peptide in patients with N-cadherin-expressing soli... Ann Oncol. 2009 Apr;20(4):741-5."	21	Cadherin	Cadherin	.	.	.	Cadherin domain; Cadherin cytoplasmic region; Cadherin prodomain like	PF00028; PF01049; PF08758	PF00028; Cadherin; PF01049; Cadherin_C; PF08758; Cadherin_pro	.	.	hsa04514:Cell adhesion molecules (CAMs); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC)	R-HSA-375170:CDO in myogenesis; R-HSA-418990:Adherens junctions interactions	.	P19022
TTARMD9	Placental cadherin (CDH3)	P22223	CADH3_HUMAN	Cadherin protein	Pcadherin; P-cadherin; Cadherin-3; CDHP	CDH3	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.	.	5JYM; 5JYL; 4ZMZ; 4ZMY; 4ZMX	MGLPRGPLASLLLLQVCWLQCAASEPCRAVFREAEVTLEAGGAEQEPGQALGKVFMGCPGQEPALFSTDNDDFTVRNGETVQERRSLKERNPLKIFPSKRILRRHKRDWVVAPISVPENGKGPFPQRLNQLKSNKDRDTKIFYSITGPGADSPPEGVFAVEKETGWLLLNKPLDREEIAKYELFGHAVSENGASVEDPMNISIIVTDQNDHKPKFTQDTFRGSVLEGVLPGTSVMQVTATDEDDAIYTYNGVVAYSIHSQEPKDPHDLMFTIHRSTGTISVISSGLDREKVPEYTLTIQATDMDGDGSTTTAVAVVEILDANDNAPMFDPQKYEAHVPENAVGHEVQRLTVTDLDAPNSPAWRATYLIMGGDDGDHFTITTHPESNQGILTTRKGLDFEAKNQHTLYVEVTNEAPFVLKLPTSTATIVVHVEDVNEAPVFVPPSKVVEVQEGIPTGEPVCVYTAEDPDKENQKISYRILRDPAGWLAMDPDSGQVTAVGTLDREDEQFVRNNIYEVMVLAMDNGSPPTTGTGTLLLTLIDVNDHGPVPEPRQITICNQSPVRQVLNITDKDLSPHTSPFQAQLTDDSDIYWTAEVNEEGDTVVLSLKKFLKQDTYDVHLSLSDHGNKEQLTVIRATVCDCHGHVETCPGPWKGGFILPVLGAVLALLFLLLVLLLLVRKKRKIKEPLLLPEDDTRDNVFYYGEEGGGEEDQDYDITQLHRGLEARPEVVLRNDVAPTIIPTPMYRPRPANPDEIGNFIIENLKAANTDPTAPPYDTLLVFDYEGSGSDAASLSSLTSSASDQDQDYDYLNEWGSRFKKLADMYGGGEDD	Clinical trial	National Cancer Institute Drug Dictionary (drug id 580366).	17	Cadherin	Cadherin	.	.	.	Cadherin domain; Cadherin cytoplasmic region	PF00028; PF01049	PF00028; Cadherin; PF01049; Cadherin_C	.	.	hsa04514:Cell adhesion molecules (CAMs)	R-HSA-418990:Adherens junctions interactions	.	P22223
TTXLCFO	Vascular endothelial cadherin (CDH5)	P33151	CADH5_HUMAN	Cadherin protein	VE-cadherin; VE-cad; Cadherin-5; CD144 antigen; CD144; 7B4 antigen	CDH5	"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."	.	.	MQRLMMLLATSGACLGLLAVAAVAAAGANPAQRDTHSLLPTHRRQKRDWIWNQMHIDEEKNTSLPHHVGKIKSSVSRKNAKYLLKGEYVGKVFRVDAETGDVFAIERLDRENISEYHLTAVIVDKDTGENLETPSSFTIKVHDVNDNWPVFTHRLFNASVPESSAVGTSVISVTAVDADDPTVGDHASVMYQILKGKEYFAIDNSGRIITITKSLDREKQARYEIVVEARDAQGLRGDSGTATVLVTLQDINDNFPFFTQTKYTFVVPEDTRVGTSVGSLFVEDPDEPQNRMTKYSILRGDYQDAFTIETNPAHNEGIIKPMKPLDYEYIQQYSFIVEATDPTIDLRYMSPPAGNRAQVIINITDVDEPPIFQQPFYHFQLKENQKKPLIGTVLAMDPDAARHSIGYSIRRTSDKGQFFRVTKKGDIYNEKELDREVYPWYNLTVEAKELDSTGTPTGKESIVQVHIEVLDENDNAPEFAKPYQPKVCENAVHGQLVLQISAIDKDITPRNVKFKFILNTENNFTLTDNHDNTANITVKYGQFDREHTKVHFLPVVISDNGMPSRTGTSTLTVAVCKCNEQGEFTFCEDMAAQVGVSIQAVVAILLCILTITVITLLIFLRRRLRKQARAHGKSVPEIHEQLVTYDEEGGGEMDTTSYDVSVLNSVRRGGAKPPRPALDARPSLYAQVQKPPRHAPGAHGGPGEMAAMIEVKKDEADHDGDGPPYDTLHIYGYEGSESIAESLSSLGTDSSDSDVDYDFLNDWGPRFKMLAELYGSDPREELLY	Literature-reported	Vascular endothelial cadherin and vascular endothelial growth factor in periodontitis and smoking. Oral Dis. 2015 Mar;21(2):263-9.	.	Cadherin	Cadherin	.	.	.	Cadherin domain; Cadherin cytoplasmic region	PF00028; PF01049	PF00028; Cadherin; PF01049; Cadherin_C	.	.	hsa04514: Cell adhesion molecules; hsa04670: Leukocyte transendothelial migration; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-418990: Adherens junctions interactions; R-HSA-5218920: VEGFR2 mediated vascular permeability	.	P33151
TT9QHUK	Cadherin-6 (CDH6)	P55285	CADH6_HUMAN	.	Kidney cadherin; K-cadherin	CDH6	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.	.	5VEB	MRTYRYFLLLFWVGQPYPTLSTPLSKRTSGFPAKKRALELSGNSKNELNRSKRSWMWNQFFLLEEYTGSDYQYVGKLHSDQDRGDGSLKYILSGDGAGDLFIINENTGDIQATKRLDREEKPVYILRAQAINRRTGRPVEPESEFIIKIHDINDNEPIFTKEVYTATVPEMSDVGTFVVQVTATDADDPTYGNSAKVVYSILQGQPYFSVESETGIIKTALLNMDRENREQYQVVIQAKDMGGQMGGLSGTTTVNITLTDVNDNPPRFPQSTYQFKTPESSPPGTPIGRIKASDADVGENAEIEYSITDGEGLDMFDVITDQETQEGIITVKKLLDFEKKKVYTLKVEASNPYVEPRFLYLGPFKDSATVRIVVEDVDEPPVFSKLAYILQIREDAQINTTIGSVTAQDPDAARNPVKYSVDRHTDMDRIFNIDSGNGSIFTSKLLDRETLLWHNITVIATEINNPKQSSRVPLYIKVLDVNDNAPEFAEFYETFVCEKAKADQLIQTLHAVDKDDPYSGHQFSFSLAPEAASGSNFTIQDNKDNTAGILTRKNGYNRHEMSTYLLPVVISDNDYPVQSSTGTVTVRVCACDHHGNMQSCHAEALIHPTGLSTGALVAILLCIVILLVTVVLFAALRRQRKKEPLIISKEDIRDNIVSYNDEGGGEEDTQAFDIGTLRNPEAIEDNKLRRDIVPEALFLPRRTPTARDNTDVRDFINQRLKENDTDPTAPPYDSLATYAYEGTGSVADSLSSLESVTTDADQDYDYLSDWGPRFKKLADMYGGVDSDKDS	Clinical trial	"ClinicalTrials.gov (NCT04707248) Phase I, Two-Part, Multi-Center, First-in-Human Study of DS-6000a in Subjects With Advanced Renal Cell Carcinoma and Ovarian Tumors. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	hsa:1004	R-HSA-418990;	.	P55285;
TTH6V3D	Cyclin-dependent kinase 1 (CDK1)	P06493	CDK1_HUMAN	Kinase	P34CDC2; P34 protein kinase; CDKN1; CDC28A; CDC2	CDK1	"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."	EC 2.7.11.22	6GU7; 6GU6; 6GU4; 6GU3; 6GU2	MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDLDNQIKKM	Clinical trial	Cell cycle kinases as therapeutic targets for cancer. Nat Rev Drug Discov. 2009 Jul;8(7):547-66.	21	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.	2.7.11.22	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	1.I.1.1.3	The Eukaryotic Nuclear Pore Complex (E-NPC) Family	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	"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"	.	P06493
TT5Q79O	Cyclin-dependent kinase 11B (CDK11B)	P21127	CD11B_HUMAN	Kinase	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	CDK11B	"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."	EC 2.7.11.22	.	MGDEKDSWKVKTLDEILQEKKRRKEQEEKAEIKRLKNSDDRDSKRDSLEEGELRDHRMEITIRNSPYRREDSMEDRGEEDDSLAIKPPQQMSRKEKAHHRKDEKRKEKRRHRSHSAEGGKHARVKEKEREHERRKRHREEQDKARREWERQKRREMAREHSRRERDRLEQLERKRERERKMREQQKEQREQKERERRAEERRKEREARREVSAHHRTMREDYSDKVKASHWSRSPPRPPRERFELGDGRKPGEARPAPAQKPAQLKEEKMEERDLLSDLQDISDSERKTSSAESSSAESGSGSEEEEEEEEEEEEEGSTSEESEEEEEEEEEEEEETGSNSEEASEQSAEEVSEEEMSEDEERENENHLLVVPESRFDRDSGESEEAEEEVGEGTPQSSALTEGDYVPDSPALSPIELKQELPKYLPALQGCRSVEEFQCLNRIEEGTYGVVYRAKDKKTDEIVALKRLKMEKEKEGFPITSLREINTILKAQHPNIVTVREIVVGSNMDKIYIVMNYVEHDLKSLMETMKQPFLPGEVKTLMIQLLRGVKHLHDNWILHRDLKTSNLLLSHAGILKVGDFGLAREYGSPLKAYTPVVVTLWYRAPELLLGAKEYSTAVDMWSVGCIFGELLTQKPLFPGKSEIDQINKVFKDLGTPSEKIWPGYSELPAVKKMTFSEHPYNNLRKRFGALLSDQGFDLMNKFLTYFPGRRISAEDGLKHEYFRETPLPIDPSMFPTWPAKSEQQRVKRGTSPRPPEGGLGYSQLGDDDLKETGFHLTTTNQGASAAGPGFSLKF	Literature-reported	Identification and characterization of the BmCyclin L1-BmCDK11A/B complex in relation to cell cycle regulation. Cell Cycle. 2017 May 3;16(9):861-868.	.	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.	2.7.11.22	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	R-HSA-380270: Recruitment of mitotic centrosome proteins and complexes	.	P21127
TTJ21A9	Cyclin-dependent kinase 12 (CDK12)	Q9NYV4	CDK12_HUMAN	.	"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"	CDK12	"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."	EC 2.7.11.22	.	MPNSERHGGKKDGSGGASGTLQPSSGGGSSNSRERHRLVSKHKRHKSKHSKDMGLVTPEAASLGTVIKPLVEYDDISSDSDTFSDDMAFKLDRRENDERRGSDRSDRLHKHRHHQHRRSRDLLKAKQTEKEKSQEVSSKSGSMKDRISGSSKRSNEETDDYGKAQVAKSSSKESRSSKLHKEKTRKERELKSGHKDRSKSHRKRETPKSYKTVDSPKRRSRSPHRKWSDSSKQDDSPSGASYGQDYDLSPSRSHTSSNYDSYKKSPGSTSRRQSVSPPYKEPSAYQSSTRSPSPYSRRQRSVSPYSRRRSSSYERSGSYSGRSPSPYGRRRSSSPFLSKRSLSRSPLPSRKSMKSRSRSPAYSRHSSSHSKKKRSSSRSRHSSISPVRLPLNSSLGAELSRKKKERAAAAAAAKMDGKESKGSPVFLPRKENSSVEAKDSGLESKKLPRSVKLEKSAPDTELVNVTHLNTEVKNSSDTGKVKLDENSEKHLVKDLKAQGTRDSKPIALKEEIVTPKETETSEKETPPPLPTIASPPPPLPTTTPPPQTPPLPPLPPIPALPQQPPLPPSQPAFSQVPASSTSTLPPSTHSKTSAVSSQANSQPPVQVSVKTQVSVTAAIPHLKTSTLPPLPLPPLLPGDDDMDSPKETLPSKPVKKEKEQRTRHLLTDLPLPPELPGGDLSPPDSPEPKAITPPQQPYKKRPKICCPRYGERRQTESDWGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLIHRSVVNMKEIVTDKQDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLEYCHKKNFLHRDIKCSNILLNNSGQIKLADFGLARLYNSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKMAPPDLPHWQDCHELWSKKRRRQRQSGVVVEEPPPSKTSRKETTSGTSTEPVKNSSPAPPQPAPGKVESGAGDAIGLADITQQLNQSELAVLLNLLQSQTDLSIPQMAQLLNIHSNPEMQQQLEALNQSISALTEATSQQQDSETMAPEESLKEAPSAPVILPSAEQTTLEASSTPADMQNILAVLLSQLMKTQEPAGSLEENNSDKNSGPQGPRRTPTMPQEEAAACPPHILPPEKRPPEPPGPPPPPPPPPLVEGDLSSAPQELNPAVTAALLQLLSQPEAEPPGHLPHEHQALRPMEYSTRPRPNRTYGNTDGPETGFSAIDTDERNSGPALTESLVQTLVKNRTFSGSLSHLGESSSYQGTGSVQFPGDQDLRFARVPLALHPVVGQPFLKAEGSSNSVVHAETKLQNYGELGPGTTGASSSGAGLHWGGPTQSSAYGKLYRGPTRVPPRGGRGRGVPY	Clinical trial	"Clinical pipeline report, company report or official report of GlaxoSmithKline."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-6796648: TP53 Regulates Transcription of DNA Repair Genes	.	Q9NYV4
TTRIM0E	Cyclin-dependent kinase 13 (CDK13)	Q14004	CDK13_HUMAN	.	CDC2-related protein kinase 5; Cell division cycle 2-like protein kinase 5; Cell division protein kinase 13; hCDK13; Cholinesterase-related cell division controller	CDK13	"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."	EC 2.7.11.22	.	MPSSSDTALGGGGGLSWAEKKLEERRKRRRFLSPQQPPLLLPLLQPQLLQPPPPPPPLLFLAAPGTAAAAAAAAAASSSCFSPGPPLEVKRLARGKRRAGGRQKRRRGPRAGQEAEKRRVFSLPQPQQDGGGGASSGGGVTPLVEYEDVSSQSEQGLLLGGASAATAATAAGGTGGSGGSPASSSGTQRRGEGSERRPRRDRRSSSGRSKERHREHRRRDGQRGGSEASKSRSRHSHSGEERAEVAKSGSSSSSGGRRKSASATSSSSSSRKDRDSKAHRSRTKSSKEPPSAYKEPPKAYREDKTEPKAYRRRRSLSPLGGRDDSPVSHRASQSLRSRKSPSPAGGGSSPYSRRLPRSPSPYSRRRSPSYSRHSSYERGGDVSPSPYSSSSWRRSRSPYSPVLRRSGKSRSRSPYSSRHSRSRSRHRLSRSRSRHSSISPSTLTLKSSLAAELNKNKKARAAEAARAAEAAKAAEATKAAEAAAKAAKASNTSTPTKGNTETSASASQTNHVKDVKKIKIEHAPSPSSGGTLKNDKAKTKPPLQVTKVENNLIVDKATKKAVIVGKESKSAATKEESVSLKEKTKPLTPSIGAKEKEQHVALVTSTLPPLPLPPMLPEDKEADSLRGNISVKAVKKEVEKKLRCLLADLPLPPELPGGDDLSKSPEEKKTATQLHSKRRPKICGPRYGETKEKDIDWGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKMPPPDLPLWQDCHELWSKKRRRQKQMGMTDDVSTIKAPRKDLSLGLDDSRTNTPQGVLPSSQLKSQGSSNVAPVKTGPGQHLNHSELAILLNLLQSKTSVNMADFVQVLNIKVNSETQQQLNKINLPAGILATGEKQTDPSTPQQESSKPLGGIQPSSQTIQPKVETDAAQAAVQSAFAVLLTQLIKAQQSKQKDVLLEERENGSGHEASLQLRPPPEPSTPVSGQDDLIQHQDMRILELTPEPDRPRILPPDQRPPEPPEPPPVTEEDLDYRTENQHVPTTSSSLTDPHAGVKAALLQLLAQHQPQDDPKREGGIDYQAGDTYVSTSDYKDNFGSSSFSSAPYVSNDGLGSSSAPPLERRSFIGNSDIQSLDNYSTASSHSGGPPQPSAFSESFPSSVAGYGDIYLNAGPMLFSGDKDHRFEYSHGPIAVLANSSDPSTGPESTHPLPAKMHNYNYGGNLQENPSGPSLMHGQTWTSPAQGPGYSQGYRGHISTSTGRGRGRGLPY	Literature-reported	Covalent targeting of remote cysteine residues to develop CDK12 and CDK13 inhibitors. Nat Chem Biol. 2016 Oct;12(10):876-84.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-6796648: TP53 Regulates Transcription of DNA Repair Genes; R-HSA-6798695: Neutrophil degranulation	.	Q14004
TTUMFAR	Cyclin-dependent kinase 18 (CDK18)	Q07002	CDK18_HUMAN	Kinase	Serine/threonine-protein kinase PCTAIRE-3; PCTK3; PCTAIRE3; PCTAIRE-motif protein kinase 3; Cell division protein kinase 18	CDK18	May play a role in signal transduction cascades in terminally differentiated cells.	EC 2.7.11.22	.	MIMNKMKNFKRRFSLSVPRTETIEESLAEFTEQFNQLHNRRNENLQLGPLGRDPPQECSTFSPTDSGEEPGQLSPGVQFQRRQNQRRFSMEDVSKRLSLPMDIRLPQEFLQKLQMESPDLPKPLSRMSRRASLSDIGFGKLETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDLIHTDRSLTLVFEYLDSDLKQYLDHCGNLMSMHNVKIFMFQLLRGLAYCHHRKILHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLGSTEYSTPIDMWGVGCIHYEMATGRPLFPGSTVKEELHLIFRLLGTPTEETWPGVTAFSEFRTYSFPCYLPQPLINHAPRLDTDGIHLLSSLLLYESKSRMSAEAALSHSYFRSLGERVHQLEDTASIFSLKEIQLQKDPGYRGLAFQQPGRGKNRRQSIF	Literature-reported	Synthesis and structure-activity relationship of trisubstituted thiazoles as Cdc7 kinase inhibitors. Eur J Med Chem. 2014 Jun 10;80:364-82.	0	EC:2.7	.	protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.	2.7.11.22	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	.	Q07002
TTNABU9	Cyclin-dependent kinase 19 (CDK19)	Q9BWU1	CDK19_HUMAN	.	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	CDK19	"cytosol, mediator complex, nucleus, cyclin-dependent protein serine/threonine kinase activity, RNA polymerase II CTD heptapeptide repeat kinase activity, protein phosphorylation"	EC 2.7.11.22	.	MDYDFKAKLAAERERVEDLFEYEGCKVGRGTYGHVYKARRKDGKDEKEYALKQIEGTGISMSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQEDPLPTLDVFAGCQIPYPKREFLNEDDPEEKGDKNQQQQQNQHQQPTAPPQQAAAPPQAPPPQQNSTQTNGTAGGAGAGVGGTGAGLQHSQDSSLNQVPPNKKPRLGPSGANSGGPVMPSDYQHSSSRLNYQSSVQGSSQSQSTLGYSSSSQQSSQYHPSHQAHRY	Clinical trial	"Clinical pipeline report, company report or official report of Ryvu Therapeutics."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1989781: PPARA activates gene expression; R-HSA-381340: Transcriptional regulation of white adipocyte differentiation	.	Q9BWU1
TT7HF4W	Cyclin-dependent kinase 2 (CDK2)	P24941	CDK2_HUMAN	Kinase	Sin3 associated polypeptide; SIN3-associated protein; P33 protein kinase; Cell division protein kinase 2; CDKN2	CDK2	"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."	EC 2.7.11.22	6Q4K; 6Q4J; 6Q4I; 6Q4H; 6Q4G	MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL	Clinical trial	"Agreement signed with Prostagenics to develop prostate cancer treatment. Innovate Oncology, Inc. 2005."	21	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.	2.7.11.22 	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	P24941
TTMYWL7	Cyclin-dependent kinase 3 (CDK3)	Q00526	CDK3_HUMAN	Kinase	Cyclindependent kinase 3; Cell division protein kinase 3; CDKN3	CDK3	"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."	EC 2.7.11.22	1LFN	MDMFQKVEKIGEGTYGVVYKAKNRETGQLVALKKIRLDLEMEGVPSTAIREISLLKELKHPNIVRLLDVVHNERKLYLVFEFLSQDLKKYMDSTPGSELPLHLIKSYLFQLLQGVSFCHSHRVIHRDLKPQNLLINELGAIKLADFGLARAFGVPLRTYTHEVVTLWYRAPEILLGSKFYTTAVDIWSIGCIFAEMVTRKALFPGDSEIDQLFRIFRMLGTPSEDTWPGVTQLPDYKGSFPKWTRKGLEEIVPNLEPEGRDLLMQLLQYDPSQRITAKTALAHPYFSSPEPSPAARQYVLQRFRH	Clinical trial	Small-molecule multi-targeted kinase inhibitor RGB-286638 triggers P53-dependent and -independent anti-multiple myeloma activity through inhibition of transcriptional CDKs. Leukemia. 2013 Dec;27(12):2366-75.	17	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.	2.7.11.22	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	.	Q00526
TT0PG8F	Cyclin-dependent kinase 4 (CDK4)	P11802	CDK4_HUMAN	Kinase	PSK-J3; Cell division protein kinase 4	CDK4	"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."	EC 2.7.11.22	5FWP; 5FWM; 5FWL; 5FWK; 3G33	MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGNPE	Successful	"Agreement signed with Prostagenics to develop prostate cancer treatment. Innovate Oncology, Inc. 2005."	34	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.	2.7.11.22	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	P11802
TTL4Q97	Cyclin-dependent kinase 5 (CDK5)	Q00535	CDK5_HUMAN	Kinase	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	CDK5	"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."	EC 2.7.11.1	4AU8; 3O0G; 1UNL; 1UNH; 1UNG	MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFCDQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNLLINRNGELKLADFGLARAFGIPVRCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKPYPMYPATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSDFCPP	Patented-recorded	1-Azakenpaullone is a selective inhibitor of glycogen synthase kinase-3 beta. Bioorg Med Chem Lett. 2004 Jan 19;14(2):413-6.	15.5	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04360:Axon guidance; hsa05010:Alzheimer's disease; hsa05030:Cocaine addiction	R-HSA-180024:DARPP-32 events; R-HSA-399956:CRMPs in Sema3A signaling; R-HSA-983231:Factors involved in megakaryocyte development and platelet production	.	Q00535
TTBYM6V	CDK5 activator 1 (CDK5R1)	Q15078	CD5R1_HUMAN	.	"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"	CDK5R1	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.	.	3O0G; 1UNL; 1UNH; 1UNG; 1H4L	MGTVLSLSPSYRKATLFEDGAATVGHYTAVQNSKNAKDKNLKRHSIISVLPWKRIVAVSAKKKNSKKVQPNSSYQNNITHLNNENLKKSLSCANLSTFAQPPPAQPPAPPASQLSGSQTGGSSSVKKAPHPAVTSAGTPKRVIVQASTSELLRCLGEFLCRRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNEISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR	Literature-reported	Cdk5r1 Overexpression Induces Primary -Cell Proliferation. J Diabetes Res. 2016;2016:6375804.	.	.	Cyclin-dependent kinase 5 activator	cyclin-dependent kinase 5 activator family.	.	.	Cyclin-dependent kinase 5 activator protein	PF03261	PF03261; CDK5_activator	.	.	hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05030: Cocaine addiction	R-HSA-399956: CRMPs in Sema3A signaling; R-HSA-6804756: Regulation of TP53 Activity through Phosphorylation; R-HSA-8862803: Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models; R-HSA-9031628: NGF-stimulated transcription; R-HSA-9032845: Activated NTRK2 signals through CDK5	.	Q15078
TTO0FDJ	Cyclin-dependent kinase 6 (CDK6)	Q00534	CDK6_HUMAN	Kinase	Serine/threonine-protein kinase PLSTIRE; Serine/threonine protein kinase PLSTIRE; Cell division protein kinase 6; CDKN6	CDK6	"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."	EC 2.7.11.22	5L2T; 5L2S; 5L2I; 4TTH; 4EZ5	MEKDGLCRADQQYECVAEIGEGAYGKVFKARDLKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLETFEHPNVVRLFDVCTVSRTDRETKLTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPGEEDWPRDVALPRQAFHSKSAQPIEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPYFQDLERCKENLDSHLPPSQNTSELNTA	Successful	"Agreement signed with Prostagenics to develop prostate cancer treatment. Innovate Oncology, Inc. 2005."	34	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.	2.7.11.22	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	Q00534
TTQYF7G	Cyclin-dependent kinase 7 (CDK7)	P50613	CDK7_HUMAN	Kinase	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	CDK7	"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."	EC 2.7.11.22	2HIC; 1UA2; 1PA8; 1LG3	MALDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDAFGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNRAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDMCSLPDYVTFKSFPGIPLHHIFSAAGDDLLDLIQGLFLFNPCARITATQALKMKYFSNRPGPTPGCQLPRPNCPVETLKEQSNPALAIKRKRTEALEQGGLPKKLIF	Clinical trial	Cell cycle kinases as therapeutic targets for cancer. Nat Rev Drug Discov. 2009 Jul;8(7):547-66.	21	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.	2.7.11.22	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa03022:Basal transcription factors; hsa03420:Nucleotide excision repair; hsa04110:Cell cycle	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	.	P50613
TTBJR4L	Cyclin-dependent kinase 8 (CDK8)	P49336	CDK8_HUMAN	Kinase	Protein kinase K35; Mediator of RNA polymerase II transcription subunit CDK8; Mediator complex subunit CDK8; Cell division protein kinase 8	CDK8	"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."	EC 2.7.11.22	5XS2; 5XQX; 5IDP; 5IDN; 5ICP	MDYDFKVKLSSERERVEDLFEYEGCKVGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSACREIALLRELKHPNVISLQKVFLSHADRKVWLLFDYAEHDLWHIIKFHRASKANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPYHHDQLDRIFNVMGFPADKDWEDIKKMPEHSTLMKDFRRNTYTNCSLIKYMEKHKVKPDSKAFHLLQKLLTMDPIKRITSEQAMQDPYFLEDPLPTSDVFAGCQIPYPKREFLTEEEPDDKGDKKNQQQQQGNNHTNGTGHPGNQDSSHTQGPPLKKVRVVPPTTTSGGLIMTSDYQRSNPHAAYPNPGPSTSQPQSSMGYSATSQQPPQYSHQTHRY	Clinical trial	Cyclin-dependent kinase inhibitors for cancer therapy: a patent review (2009 - 2014).Expert Opin Ther Pat. 2015;25(9):953-70.	15.5	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.	2.7.11.22	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	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	.	P49336
TT1LVF2	Cyclin-dependent kinase 9 (CDK9)	P50750	CDK9_HUMAN	Kinase	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	CDK9	"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."	EC 2.7.11.22	6GZH; 6CYT; 5L1Z; 4OR5; 4OGR	MAKQYDSVECPFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQKVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKASPYNRCKGSIYLVFDFCEHDLAGLLSNVLVKFTLSEIKRVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLALISQLCGSITPEVWPNVDNYELYEKLELVKGQKRKVKDRLKAYVRDPYALDLIDKLLVLDPAQRIDSDDALNHDFFWSDPMPSDLKGMLSTHLTSMFEYLAPPRRKGSQITQQSTNQSRNPATTNQTEFERVF	Clinical trial	Cell cycle kinases as therapeutic targets for cancer. Nat Rev Drug Discov. 2009 Jul;8(7):547-66.	21	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.	2.7.11.22	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa05202:Transcriptional misregulation in cancer	R-HSA-2173796:SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription	.	P50750
TTQ7ABG	Positive transcription elongation factor b (P-TEFb)	P50750-O60563	CDK9_HUMAN-CCNT1_HUMAN	S-phase kinase-associated protein	P-TEFb	CDK9-CCNT1	"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."	.	.	MEGERKNNNKRWYFTREQLENSPSRRFGVDPDKELSYRQQAANLLQDMGQRLNVSQLTINTAIVYMHRFYMIQSFTQFPGNSVAPAALFLAAKVEEQPKKLEHVIKVAHTCLHPQESLPDTRSEAYLQQVQDLVILESIILQTLGFELTIDHPHTHVVKCTQLVRASKDLAQTSYFMATNSLHLTTFSLQYTPPVVACVCIHLACKWSNWEIPVSTDGKHWWEYVDATVTLELLDELTHEFLQILEKTPNRLKRIWNWRACEAAKKTKADDRGTDEKTSEQTILNMISQSSSDTTIAGLMSMSTSTTSAVPSLPVSEESSSNLTSVEMLPGKRWLSSQPSFKLEPTQGHRTSENLALTGVDHSLPQDGSNAFISQKQNSKSVPSAKVSLKEYRAKHAEELAAQKRQLENMEANVKSQYAYAAQNLLSHHDSHSSVILKMPIEGSENPERPFLEKADKTALKMRIPVAGGDKAASSKPEEIKMRIKVHAAADKHNSVEDSVTKSREHKEKHKTHPSNHHHHHNHHSHKHSHSQLPVGTGNKRPGDPKHSSQTSNLAHKTYSLSSSFSSSSSTRKRGPSEETGGAVFDHPAKIAKSTKSSSLNFSFPSLPTMGQMPGHSSDTSGLSFSQPSCKTRVPHSKLDKGPTGANGHNTTQTIDYQDTVNMLHSLLSAQGVQPTQPTAFEFVRPYSDYLNPRSGGISSRSGNTDKPRPPPLPSEPPPPLPPLPKMAKQYDSVECPFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQKVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKASPYNRCKGSIYLVFDFCEHDLAGLLSNVLVKFTLSEIKRVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLALISQLCGSITPEVWPNVDNYELYEKLELVKGQKRKVKDRLKAYVRDPYALDLIDKLLVLDPAQRIDSDDALNHDFFWSDPMPSDLKGMLSTHLTSMFEYLAPPRRKGSQITQQSTNQSRNPATTNQTEFERVF	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	17	.	.	.	.	.	.	.	.	.	.	hsa04066:HIF-1 signaling pathway; hsa04120:Ubiquitin mediated proteolysis; hsa05200:Pathways in cancer; hsa05211:Renal cell carcinoma	.	.	P50750
TTBTI6P	Cyclin-dependent kinase-like 1 (CDKL1)	Q00532	CDKL1_HUMAN	Kinase	Serine/threonine-protein kinase KKIALRE; Protein kinase p42 KKIALRE	CDKL1	"Ciliary transition zone, extracellular exosome, intracellular membrane-bounded organelle, nucleoplasm, nucleus, cyclin-dependent protein serine/threonine kinase activity, protein phosphorylation, regulation of cilium assembly."	EC 2.7.11.22	4AGU	MMEKYEKIGKIGEGSYGVVFKCRNRDTGQIVAIKKFLESEDDPVIKKIALREIRMLKQLKHPNLVNLLEVFRRKRRLHLVFEYCDHTVLHELDRYQRGVPEHLVKSITWQTLQAVNFCHKHNCIHRDVKPENILITKHSVIKLCDFGFARLLAGPSDYYTDYVATRWYRSPELLVGDTQYGPPVDVWAIGCVFAELLSGVPLWPGKSDVDQLYLIRKTLGDLIPRHQQVFSTNQYFSGVKIPDPEDMEPLELKFPNISYPALGLLKGCLHMDPTQRLTCEQLLHHPYFENIREIEDLAKEHNKPTRKTLRKSRKHHCFTETSKLQYLPQLTGSSILPALDNKKYYCDTKKLNYRFPNI	Literature-reported	"Imidazole pyrimidine amides as potent, orally bioavailable cyclin-dependent kinase inhibitors. Bioorg Med Chem Lett. 2008 Dec 15;18(24):6486-9."	0	EC:2.7	.	protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.	2.7.11.22	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	.	Q00532
TTMO45N	Cyclin-dependent kinase-like 2 (CDKL2)	Q92772	CDKL2_HUMAN	Kinase	Serine/threonine-protein kinase KKIAMRE; Protein kinase p56 KKIAMRE	CDKL2	"centrosome, nucleus, cyclin-dependent protein serine/threonine kinase activity, protein kinase activity, protein phosphorylation, sex differentiation, signal transduction."	EC 2.7.11.22	4BBM; 4AAA	MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVRLPEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQMDGFAERFSQELQLKVQKDARNVSLSKKSQNRKKEKEKDDSLVEERKTLVVQDTNADPKIKDYKLFKIKGSKIDGEKAEKGNRASNASCLHDSRTSHNKIVPSTSLKDCSNVSVDHTRNPSVAIPPLTHNLSAVAPSINSGMGTETIPIQGYRVDEKTKKCSIPFVKPNRHSPSGIYNINVTTLVSGPPLSDDSGADLPQMEHQH	Literature-reported	"Discovery, synthesis, and characterization of an orally bioavailable, brain penetrant inhibitor of mixed lineage kinase 3. J Med Chem. 2013 Oct 24;56(20):8032-48."	0	EC:2.7	.	protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.	2.7.11.22	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	.	Q92772
TT9GUW0	Melanoma differentiation-associated protein 6 (CDKN1A)	P38936	CDN1A_HUMAN	.	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	CDKN1A	"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."	.	6CIX; 6CIV; 6CEJ; 6CBI; 5E0U	MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP	Literature-reported	p21(WAF1) Gene Transfection Inhibits Proliferation of Leukemia Cell Line K562 Zhongguo Shi Yan Xue Ye Xue Za Zhi. 2001 Jun;9(2):115-118.	.	.	.	CDI family.	.	.	Cyclin-dependent kinase inhibitor	PF02234	PF02234; CDI	.	.	"hsa01522: Endocrine resistance; hsa01524: Platinum drug resistance; hsa04012: ErbB signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04068: FoxO signaling pathway; hsa04110: Cell cycle; hsa04115: p53 signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04218: Cellular senescence; hsa04630: JAK-STAT signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04934: Cushing syndrome; 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; 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; hsa05211: Renal cell carcinoma; 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; hsa05224: Breast cancer; hsa05225: Hepatocellular carcinoma; hsa05226: Gastric cancer"	"R-HSA-187577: SCF(Skp2)-mediated degradation of p27/p21; R-HSA-198323: AKT phosphorylates targets in the cytosol; R-HSA-2559582: Senescence-Associated Secretory Phenotype (SASP); R-HSA-2559586: DNA Damage/Telomere Stress Induced Senescence; R-HSA-5674400: Constitutive Signaling by AKT1 E17K in Cancer; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6804116: TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest; R-HSA-69202: Cyclin E associated events during G1/S transition; R-HSA-69231: Cyclin D associated events in G1; R-HSA-69563: p53-Dependent G1 DNA Damage Response; R-HSA-69656: Cyclin A:Cdk2-associated events at S phase entry; R-HSA-69895: Transcriptional activation of cell cycle inhibitor p21; R-HSA-8852276: The role of GTSE1 in G2/M progression after G2 checkpoint; R-HSA-8866911: TFAP2 (AP-2) family regulates transcription of cell cycle factors; R-HSA-8878166: Transcriptional regulation by RUNX2; R-HSA-8941855: RUNX3 regulates CDKN1A transcription; R-HSA-9616222: Transcriptional regulation of granulopoiesis; R-HSA-9617828: FOXO-mediated transcription of cell cycle genes; R-HSA-9661069: Defective binding of RB1 mutants to E2F1,(E2F2, E2F3); R-HSA-9702518: STAT5 activation downstream of FLT3 ITD mutants; R-HSA-9703465: Signaling by FLT3 fusion proteins"	.	P38936
TTLGFVW	CDK inhibitor 1B p27Kip1 (CDKN1B)	P46527	CDN1B_HUMAN	.	p27Kip1; KIP1; Cyclindependent kinase inhibitor p27; Cyclin-dependent kinase inhibitor p27; Cyclin-dependent kinase inhibitor 1B	CDKN1B	"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."	.	6ATH; 5UQ3; 2AST; 1JSU; 1H27	MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT	Literature-reported	Roles of CDKN1B in cancer Aging (Albany NY). 2015 Aug;7(8):529-30.	.	.	.	CDI family.	.	.	Cyclin-dependent kinase inhibitor	PF02234	PF02234; CDI	.	.	hsa01522: Endocrine resistance; hsa04012: ErbB signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04068: FoxO signaling pathway; hsa04110: Cell cycle; hsa04151: PI3K-Akt signaling pathway; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04934: Cushing syndrome; hsa05162: Measles; hsa05165: Human papillomavirus infection; hsa05169: Epstein-Barr virus infection; hsa05200: Pathways in cancer; hsa05202: Transcriptional misregulation in cancer; hsa05203: Viral carcinogenesis; hsa05206: MicroRNAs in cancer; hsa05215: Prostate cancer; hsa05220: Chronic myeloid leukemia; hsa05222: Small cell lung cancer; hsa05226: Gastric cancer	"R-HSA-187577: SCF(Skp2)-mediated degradation of p27/p21; R-HSA-198323: AKT phosphorylates targets in the cytosol; R-HSA-2559582: Senescence-Associated Secretory Phenotype (SASP); R-HSA-2559586: DNA Damage/Telomere Stress Induced Senescence; R-HSA-5625900: RHO GTPases activate CIT; R-HSA-5674400: Constitutive Signaling by AKT1 E17K in Cancer; R-HSA-6804116: TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest; R-HSA-69202: Cyclin E associated events during G1/S transition; R-HSA-69231: Cyclin D associated events in G1; R-HSA-69563: p53-Dependent G1 DNA Damage Response; R-HSA-69656: Cyclin A:Cdk2-associated events at S phase entry; R-HSA-8849470: PTK6 Regulates Cell Cycle; R-HSA-9607240: FLT3 Signaling; R-HSA-9617828: FOXO-mediated transcription of cell cycle genes; R-HSA-9634638: Estrogen-dependent nuclear events downstream of ESR-membrane signaling; R-HSA-9661069: Defective binding of RB1 mutants to E2F1,(E2F2, E2F3)"	.	P46527
TTBSUAR	CDK inhibitor 1C p57Kip2 (CDKN1C)	P49918	CDN1C_HUMAN	.	P57KIP2; P57(KIP2); KIP2; Cyclin-dependent kinase inhibitor p57; Cyclin-dependent kinase inhibitor 1C	CDKN1C	"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."	.	.	MSDASLRSTSTMERLVARGTFPVLVRTSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFYRETVQVGRCRLLLAPRPVAVAVAVSPPLEPAAESLDGLEEAPEQLPSVPVPAPASTPPPVPVLAPAPAPAPAPVAAPVAAPVAVAVLAPAPAPAPAPAPAPAPVAAPAPAPAPAPAPAPAPAPAPDAAPQESAEQGANQGQRGQEPLADQLHSGISGRPAAGTAAASANGAAIKKLSGPLISDFFAKRKRSAPEKSSGDVPAPCPSPSAAPGVGSVEQTPRKRLR	Literature-reported	p57(KIP2) expression in normal islet cells and in hyperinsulinism of infancy. Diabetes. 2001 Dec;50(12):2763-9.	.	.	.	CDI family.	.	.	Cyclin-dependent kinase inhibitor	PF02234	PF02234; CDI	.	.	hsa04110: Cell cycle	"R-HSA-69231: Cyclin D associated events in G1; R-HSA-9661069: Defective binding of RB1 mutants to E2F1,(E2F2, E2F3)"	.	P49918
TTFTWQ8	Multiple tumor suppressor 1 (CDKN2A)	P42771	CDN2A_HUMAN	.	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	CDKN2A	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.	.	2A5E; 1DC2; 1BI7; 1A5E	MEPAAGSSMEPSADWLATAAARGRVEEVRALLEAGALPNAPNSYGRRPIQVMMMGSARVAELLLLHGAEPNCADPATLTRPVHDAAREGFLDTLVVLHRAGARLDVRDAWGRLPVDLAEELGHRDVARYLRAAAGGTRGSNHARIDAAEGPSDIPD	Literature-reported	"Analysis of the p16INK4A, p15INK4B and p18INK4C genes in multiple myeloma. Br J Haematol. 1997 Jan;96(1):98-102."	.	.	CDKN2 cyclin-dependent kinase inhibitor	CDKN2 cyclin-dependent kinase inhibitor family.	.	.	.	.	.	.	.	hsa01522: Endocrine resistance; hsa01524: Platinum drug resistance; hsa04110: Cell cycle; hsa04115: p53 signaling pathway; hsa04218: Cellular senescence; hsa04934: Cushing syndrome; hsa05163: Human cytomegalovirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05200: Pathways in cancer; hsa05203: Viral carcinogenesis; hsa05206: MicroRNAs in cancer; hsa05212: Pancreatic cancer; hsa05214: Glioma; hsa05218: Melanoma; hsa05219: Bladder cancer; hsa05220: Chronic myeloid leukemia; hsa05223: Non-small cell lung cancer; hsa05225: Hepatocellular carcinoma	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; R-HSA-8853884: Transcriptional Regulation by VENTX; R-HSA-9630791: Evasion of Oncogene Induced Senescence Due to Defective p16INK4A binding to CDK4; R-HSA-9630794: Evasion of Oncogene Induced Senescence Due to Defective p16INK4A binding to CDK4 and CDK6; R-HSA-9632697: Evasion of Oxidative Stress Induced Senescence Due to Defective p16INK4A binding to CDK4; R-HSA-9632700: Evasion of Oxidative Stress Induced Senescence Due to Defective p16INK4A binding to CDK4 and CDK6	.	P42771
TTBRUGA	CDK inhibitor 4C p18-INK4c (CDKN2C)	P42773	CDN2C_HUMAN	.	P18-INK6; P18-INK4c; P18(INK4c) protein; P18(INK4c); P18 INK4c protein; Cyclin-dependent kinase 6 inhibitor; Cyclin-dependent kinase 4 inhibitor C	CDKN2C	"Inhibits cell growth and proliferation with a correlated dependence on endogenous retinoblastoma protein RB. Interacts strongly with CDK6, weakly with CDK4."	.	1MX6; 1MX4; 1MX2; 1IHB; 1G3N	MAEPWGNELASAAARGDLEQLTSLLQNNVNVNAQNGFGRTALQVMKLGNPEIARRLLLRGANPDLKDRTGFAVIHDAARAGFLDTLQTLLEFQADVNIEDNEGNLPLHLAAKEGHLRVVEFLVKHTASNVGHRNHKGDTACDLARLYGRNEVVSLMQANGAGGATNLQ	Literature-reported	An important role of CDK inhibitor p18(INK4c) in modulating antigen receptor-mediated T cell proliferation. J Immunol. 2001 Sep 15;167(6):3285-92.	.	.	.	CDKN2 cyclin-dependent kinase inhibitor family.	.	.	.	.	.	.	.	hsa01522: Endocrine resistance; hsa04110: Cell cycle; hsa04934: Cushing syndrome; hsa05166: Human T-cell leukemia virus 1 infection; hsa05202: Transcriptional misregulation in cancer	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	.	P42773
TTA9CK4	Biliary glycoprotein 1 (CEACAM1)	P13688	CEAM1_HUMAN	.	Biliary glycoprotein 1; BGP-1; DE   AltName: CD_antigen=CD66a	CEACAM1	"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)."	.	.	MGHLSAPLHRVRVPWQGLLLTASLLTFWNPPTTAQLTTESMPFNVAEGKEVLLLVHNLPQQLFGYSWYKGERVDGNRQIVGYAIGTQQATPGPANSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPETQDTTYLWWINNQSLPVSPRLQLSNGNRTLTLLSVTRNDTGPYECEIQNPVSANRSDPVTLNVTYGPDTPTISPSDTYYRPGANLSLSCYAASNPPAQYSWLINGTFQQSTQELFIPNITVNNSGSYTCHANNSVTGCNRTTVKTIIVTELSPVVAKPQIKASKTTVTGDKDSVNLTCSTNDTGISIRWFFKNQSLPSSERMKLSQGNTTLSINPVKREDAGTYWCEVFNPISKNQSDPIMLNVNYNALPQENGLSPGAIAGIVIGVVALVALIAVALACFLHFGKTGRASDQRDLTEHKPSVSNHTQDHSNDPPNKMNEVTYSTLNFEAQQPTQPTSASPSLTATEIIYSEVKKQ	Clinical trial	The Monoclonal Antibody NEO-201 Enhances Natural Killer Cell Cytotoxicity Against Tumor Cells Through Blockade of the Inhibitory CEACAM5/CEACAM1 Immune Checkpoint Pathway. Cancer Biother Radiopharm. 2020 Apr;35(3):190-198.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1566977: Fibronectin matrix formation; R-HSA-202733: Cell surface interactions at the vascular wall; R-HSA-6798695: Neutrophil degranulation	.	P13688
TTPX7I5	Carcinoembryonic antigen CGM1 (CD66d)	P40198	CEAM3_HUMAN	Immunoglobulin	CGM1; CEACAM3; CD66d	CEACAM3	"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."	.	6AW3; 6AW1; 6AW0; 6AVZ	MGPPSASPHRECIPWQGLLLTASLLNFWNPPTTAKLTIESMPLSVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNSLIVGYVIGTQQATPGAAYSGRETIYTNASLLIQNVTQNDIGFYTLQVIKSDLVNEEATGQFHVYQENAPGLPVGAVAGIVTGVLVGVALVAALVCFLLLAKTGRTSIQRDLKEQQPQALAPGRGPSHSSAFSMSPLSTAQAPLPNPRTAASIYEELLKHDTNIYCRMDHKAEVAS	Successful	In vivo near-infrared fluorescence imaging of carcinoembryonic antigen-expressing tumor cells in mice. Radiology. 2008 Jun;247(3):779-87.	34	.	.	.	.	.	.	.	.	.	.	.	R-HSA-202733: Cell surface interactions at the vascular wall; R-HSA-6798695: Neutrophil degranulation	.	P40198
TTY6DTE	Carcinoembryonic antigen CEA (CD66e)	P06731	CEAM5_HUMAN	Immunoglobulin	Meconium antigen 100; Carcinoembryonic antigen-related cell adhesion molecule 5; CEA; CD66e antigen	CEACAM5	"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."	.	2VER; 2QST; 2QSQ; 1.00E+07	MESPSAPPHRWCIPWQRLLLTASLLTFWNPPTTAKLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNIIQNDTGFYTLHVIKSDLVNEEATGQFRVYPELPKPSISSNNSKPVEDKDAVAFTCEPETQDATYLWWVNNQSLPVSPRLQLSNGNRTLTLFNVTRNDTASYKCETQNPVSARRSDSVILNVLYGPDAPTISPLNTSYRSGENLNLSCHAASNPPAQYSWFVNGTFQQSTQELFIPNITVNNSGSYTCQAHNSDTGLNRTTVTTITVYAEPPKPFITSNNSNPVEDEDAVALTCEPEIQNTTYLWWVNNQSLPVSPRLQLSNDNRTLTLLSVTRNDVGPYECGIQNKLSVDHSDPVILNVLYGPDDPTISPSYTYYRPGVNLSLSCHAASNPPAQYSWLIDGNIQQHTQELFISNITEKNSGLYTCQANNSASGHSRTTVKTITVSAELPKPSISSNNSKPVEDKDAVAFTCEPEAQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLFNVTRNDARAYVCGIQNSVSANRSDPVTLDVLYGPDTPIISPPDSSYLSGANLNLSCHSASNPSPQYSWRINGIPQQHTQVLFIAKITPNNNGTYACFVSNLATGRNNSIVKSITVSASGTSPGLSAGATVGIMIGVLVGVALI	Clinical trial	Identification of an enhancer agonist cytotoxic T lymphocyte peptide from human carcinoembryonic antigen. Cancer Res. 1997 Oct 15;57(20):4570-7.	21	Immunoglobulin	.	immunoglobulin superfamily. CEA family.	.	.	Immunoglobulin domain; Immunoglobulin V-set domain	PF13895; PF07686	PF13895; Ig_2; PF07686; V-set	.	.	.	R-HSA-163125: Post-translational modification: synthesis of GPI-anchored proteins; R-HSA-202733: Cell surface interactions at the vascular wall	.	P06731
TTIGH2W	Normal cross-reacting antigen (CD66c)	P40199	CEAM6_HUMAN	Immunoglobulin	Nonspecific crossreacting antigen; Non-specific crossreacting antigen; NCA; Carcinoembryonic antigen-related cell adhesion molecule 6; CD66c antigen	CEACAM6	"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."	.	4YIQ; 4Y8A; 4WTZ; 4WHC	MGPPSAPPCRLHVPWKEVLLTASLLTFWNPPTTAKLTIESTPFNVAEGKEVLLLAHNLPQNRIGYSWYKGERVDGNSLIVGYVIGTQQATPGPAYSGRETIYPNASLLIQNVTQNDTGFYTLQVIKSDLVNEEATGQFHVYPELPKPSISSNNSNPVEDKDAVAFTCEPEVQNTTYLWWVNGQSLPVSPRLQLSNGNMTLTLLSVKRNDAGSYECEIQNPASANRSDPVTLNVLYGPDGPTISPSKANYRPGENLNLSCHAASNPPAQYSWFINGTFQQSTQELFIPNITVNNSGSYMCQAHNSATGLNRTTVTMITVSGSAPVLSAVATVGITIGVLARVALI	Clinical trial	CEACAM6 gene silencing impairs anoikis resistance and in vivo metastatic ability of pancreatic adenocarcinoma cells. Oncogene. 2004 Jan 15;23(2):465-73.	.	Immunoglobulin	Immunoglobulin superfamily	immunoglobulin superfamily. CEA family.	.	.	Immunoglobulin domain; Immunoglobulin V-set domain	PF13895; PF07686	PF13895; Ig_2; PF07686; V-set	.	.	.	R-HSA-1566977: Fibronectin matrix formation; R-HSA-202733: Cell surface interactions at the vascular wall; R-HSA-6798695: Neutrophil degranulation	.	P40199
TT5LWG1	CEBPA messenger RNA (CEBPA mRNA)	P49715	CEBPA_HUMAN	.	C/EBP alpha	CEBPA	"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)."	.	.	MESADFYEAEPRPPMSSHLQSPPHAPSSAAFGFPRGAGPAQPPAPPAAPEPLGGICEHETSIDISAYIDPAAFNDEFLADLFQHSRQQEKAKAAVGPTGGGGGGDFDYPGAPAGPGGAVMPGGAHGPPPGYGCAAAGYLDGRLEPLYERVGAPALRPLVIKQEPREEDEAKQLALAGLFPYQPPPPPPPSHPHPHPPPAHLAAPHLQFQIAHCGQTTMHLQPGHPTPPPTPVPSPHPAPALGAAGLPGPGSALKGLGAAHPDLRASGGSGAGKAKKSVDKNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTSDNDRLRKRVEQLSRELDTLRGIFRQLPESSLVKAMGNCA	Clinical trial	"MTL-CEBPA, a Small Activating RNA Therapeutic Upregulating C/EBP-alpha, in Patients with Advanced Liver Cancer: A First-in-Human, Multicenter, Open-Label, Phase I Trial. Clin Cancer Res. 2020 Aug 1;26(15):3936-3946."	.	.	.	.	.	.	.	.	.	.	.	hsa04932: Non-alcoholic fatty liver disease; hsa05200: Pathways in cancer; hsa05202: Transcriptional misregulation in cancer; hsa05221: Acute myeloid leukemia	R-HSA-381340: Transcriptional regulation of white adipocyte differentiation; R-HSA-9616222: Transcriptional regulation of granulopoiesis	.	P49715
TTUI35N	C/EBP beta messenger RNA (CEBPB mRNA)	P17676	CEBPB_HUMAN	mRNA target	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)	CEBPB	"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."	.	6MG3; 6MG2; 6MG1; 2.00E+43; 2.00E+42	MQRLVAWDPACLPLPPPPPAFKSMEVANFYYEADCLAAAYGGKAAPAAPPAARPGPRPPAGELGSIGDHERAIDFSPYLEPLGAPQAPAPATATDTFEAAPPAPAPAPASSGQHHDFLSDLFSDDYGGKNCKKPAEYGYVSLGRLGAAKGALHPGCFAPLHPPPPPPPPPAELKAEPGFEPADCKRKEEAGAPGGGAGMAAGFPYALRAYLGYQAVPSGSSGSLSTSSSSSPPGTPSPADAKAPPTACYAGAAPAPSQVKSKAKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASSGHC	Literature-reported	"US patent application no. 6,271,030, Antisense inhibition of C/EBP beta expression."	0	mRNA	mRNA target	.	.	.	Basic region leucine zipper	PF07716	PF07716; bZIP_2	.	.	hsa04668:TNF signaling pathway; hsa05152:Tuberculosis; hsa05202:Transcriptional misregulation in cancer	R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-381340:Transcriptional regulation of white adipocyte differentiation	.	P17676
TTRSJH4	CCAAT/enhancer binding protein beta (CEBPB)	P17676	CEBPB_HUMAN	Basic leucine zipper bZIP	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	CEBPB	"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."	.	6MG3; 6MG2; 6MG1; 2.00E+43; 2.00E+42	MQRLVAWDPACLPLPPPPPAFKSMEVANFYYEADCLAAAYGGKAAPAAPPAARPGPRPPAGELGSIGDHERAIDFSPYLEPLGAPQAPAPATATDTFEAAPPAPAPAPASSGQHHDFLSDLFSDDYGGKNCKKPAEYGYVSLGRLGAAKGALHPGCFAPLHPPPPPPPPPAELKAEPGFEPADCKRKEEAGAPGGGAGMAAGFPYALRAYLGYQAVPSGSSGSLSTSSSSSPPGTPSPADAKAPPTACYAGAAPAPSQVKSKAKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASSGHC	Literature-reported	Retinoid antagonism of NF-IL6: insight into the mechanism of antiproliferative effects of retinoids in Kaposi's sarcoma. Mol Cell Biol. 1997 Jul;17(7):4159-68.	.	bZIP	.	bZIP family. C/EBP subfamily.	.	.	Basic region leucine zipper	PF07716	PF07716; bZIP_2	.	.	hsa04657: IL-17 signaling pathway; hsa04668: TNF signaling pathway; hsa05152: Tuberculosis; hsa05202: Transcriptional misregulation in cancer	R-HSA-2559582: Senescence-Associated Secretory Phenotype (SASP); R-HSA-380994: ATF4 activates genes in response to endoplasmic reticulum stress; R-HSA-381340: Transcriptional regulation of white adipocyte differentiation; R-HSA-8853884: Transcriptional Regulation by VENTX; R-HSA-9616222: Transcriptional regulation of granulopoiesis; R-HSA-9633012: Response of EIF2AK4 (GCN2) to amino acid deficiency; R-HSA-9648895: Response of EIF2AK1 (HRI) to heme deficiency; R-HSA-9725371: Nuclear events stimulated by ALK signaling in cancer	.	P17676
TTTRNQW	Bile-salt-activated lipase (CEL)	P19835	CEL_HUMAN	Carboxylic ester hydrolase	Pancreatic lysophospholipase; Pancreatic cholesterol esterase; Cholesterol esterase; Carboxyl ester lipase; CEL; Bile-salt-stimulated lipase; BSSL; BAL	CEL	Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.	EC 3.1.1.13	6H1A; 6H19; 6H18; 6H0V; 6H0T	MGRLQLVVLGLTCCWAVASAAKLGAVYTEGGFVEGVNKKLGLLGDSVDIFKGIPFAAPTKALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGDEDCLYLNIWVPQGRKQVSRDLPVMIWIYGGAFLMGSGHGANFLNNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPGNYGLRDQHMAIAWVKRNIAAFGGDPNNITLFGESAGGASVSLQTLSPYNKGLIRRAISQSGVALSPWVIQKNPLFWAKKVAEKVGCPVGDAARMAQCLKVTDPRALTLAYKVPLAGLEYPMLHYVGFVPVIDGDFIPADPINLYANAADIDYIAGTNNMDGHIFASIDMPAINKGNKKVTEEDFYKLVSEFTITKGLRGAKTTFDVYTESWAQDPSQENKKKTVVDFETDVLFLVPTEIALAQHRANAKSAKTYAYLFSHPSRMPVYPKWVGADHADDIQYVFGKPFATPTGYRPQDRTVSKAMIAYWTNFAKTGDPNMGDSAVPTHWEPYTTENSGYLEITKKMGSSSMKRSLRTNFLRYWTLTYLALPTVTDQEATPVPPTGDSEATPVPPTGDSETAPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDAGPPPVPPTGDSGAPPVPPTGDSGAPPVTPTGDSETAPVPPTGDSGAPPVPPTGDSEAAPVPPTDDSKEAQMPAVIRF	Clinical trial	ClinicalTrials.gov (NCT00743483) Efficacy of Bucelipase Alfa (BSSL) in Patients With Cystic Fibrosis and Pancreatic Insufficiency. U.S. National Institutes of Health.	25	.	.	.	.	.	.	.	.	.	.	.	R-HSA-192456: Digestion of dietary lipid	.	P19835
TT3NKIB	Pancreatic elastase 1 (CELA1)	Q9UNI1	CELA1_HUMAN	Peptidase	Elastase; CELA1	CELA1	Acts upon elastin.	EC 3.4.21.36	.	MLVLYGHSTQDLPETNARVVGGTEAGRNSWPSQISLQYRSGGSRYHTCGGTLIRQNWVMTAAHCVDYQKTFRVVAGDHNLSQNDGTEQYVSVQKIVVHPYWNSDNVAAGYDIALLRLAQSVTLNSYVQLGVLPQEGAILANNSPCYITGWGKTKTNGQLAQTLQQAYLPSVDYAICSSSSYWGSTVKNTMVCAGGDGVRSGCQGDSGGPLHCLVNGKYSVHGVTSFVSSRGCNVSRKPTVFTQVSAYISWINNVIASN	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. 2015	34	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9UNI1
TTZD5QR	Centromeric protein E (CENPE)	Q02224	CENPE_HUMAN	TRAFAC class myosin-kinesin ATPase	Centromere-associated protein E; CENPE; CENP-E	CENPE	"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."	.	5JVP; 1T5C	MAEEGAVAVCVRVRPLNSREESLGETAQVYWKTDNNVIYQVDGSKSFNFDRVFHGNETTKNVYEEIAAPIIDSAIQGYNGTIFAYGQTASGKTYTMMGSEDHLGVIPRAIHDIFQKIKKFPDREFLLRVSYMEIYNETITDLLCGTQKMKPLIIREDVNRNVYVADLTEEVVYTSEMALKWITKGEKSRHYGETKMNQRSSRSHTIFRMILESREKGEPSNCEGSVKVSHLNLVDLAGSERAAQTGAAGVRLKEGCNINRSLFILGQVIKKLSDGQVGGFINYRDSKLTRILQNSLGGNAKTRIICTITPVSFDETLTALQFASTAKYMKNTPYVNEVSTDEALLKRYRKEIMDLKKQLEEVSLETRAQAMEKDQLAQLLEEKDLLQKVQNEKIENLTRMLVTSSSLTLQQELKAKRKRRVTWCLGKINKMKNSNYADQFNIPTNITTKTHKLSINLLREIDESVCSESDVFSNTLDTLSEIEWNPATKLLNQENIESELNSLRADYDNLVLDYEQLRTEKEEMELKLKEKNDLDEFEALERKTKKDQEMQLIHEISNLKNLVKHAEVYNQDLENELSSKVELLREKEDQIKKLQEYIDSQKLENIKMDLSYSLESIEDPKQMKQTLFDAETVALDAKRESAFLRSENLELKEKMKELATTYKQMENDIQLYQSQLEAKKKMQVDLEKELQSAFNEITKLTSLIDGKVPKDLLCNLELEGKITDLQKELNKEVEENEALREEVILLSELKSLPSEVERLRKEIQDKSEELHIITSEKDKLFSEVVHKESRVQGLLEEIGKTKDDLATTQSNYKSTDQEFQNFKTLHMDFEQKYKMVLEENERMNQEIVNLSKEAQKFDSSLGALKTELSYKTQELQEKTREVQERLNEMEQLKEQLENRDSTLQTVEREKTLITEKLQQTLEEVKTLTQEKDDLKQLQESLQIERDQLKSDIHDTVNMNIDTQEQLRNALESLKQHQETINTLKSKISEEVSRNLHMEENTGETKDEFQQKMVGIDKKQDLEAKNTQTLTADVKDNEIIEQQRKIFSLIQEKNELQQMLESVIAEKEQLKTDLKENIEMTIENQEELRLLGDELKKQQEIVAQEKNHAIKKEGELSRTCDRLAEVEEKLKEKSQQLQEKQQQLLNVQEEMSEMQKKINEIENLKNELKNKELTLEHMETERLELAQKLNENYEEVKSITKERKVLKELQKSFETERDHLRGYIREIEATGLQTKEELKIAHIHLKEHQETIDELRRSVSEKTAQIINTQDLEKSHTKLQEEIPVLHEEQELLPNVKEVSETQETMNELELLTEQSTTKDSTTLARIEMERLRLNEKFQESQEEIKSLTKERDNLKTIKEALEVKHDQLKEHIRETLAKIQESQSKQEQSLNMKEKDNETTKIVSEMEQFKPKDSALLRIEIEMLGLSKRLQESHDEMKSVAKEKDDLQRLQEVLQSESDQLKENIKEIVAKHLETEEELKVAHCCLKEQEETINELRVNLSEKETEISTIQKQLEAINDKLQNKIQEIYEKEEQFNIKQISEVQEKVNELKQFKEHRKAKDSALQSIESKMLELTNRLQESQEEIQIMIKEKEEMKRVQEALQIERDQLKENTKEIVAKMKESQEKEYQFLKMTAVNETQEKMCEIEHLKEQFETQKLNLENIETENIRLTQILHENLEEMRSVTKERDDLRSVEETLKVERDQLKENLRETITRDLEKQEELKIVHMHLKEHQETIDKLRGIVSEKTNEISNMQKDLEHSNDALKAQDLKIQEELRIAHMHLKEQQETIDKLRGIVSEKTDKLSNMQKDLENSNAKLQEKIQELKANEHQLITLKKDVNETQKKVSEMEQLKKQIKDQSLTLSKLEIENLNLAQKLHENLEEMKSVMKERDNLRRVEETLKLERDQLKESLQETKARDLEIQQELKTARMLSKEHKETVDKLREKISEKTIQISDIQKDLDKSKDELQKKIQELQKKELQLLRVKEDVNMSHKKINEMEQLKKQFEAQNLSMQSVRMDNFQLTKKLHESLEEIRIVAKERDELRRIKESLKMERDQFIATLREMIARDRQNHQVKPEKRLLSDGQQHLTESLREKCSRIKELLKRYSEMDDHYECLNRLSLDLEKEIEFQKELSMRVKANLSLPYLQTKHIEKLFTANQRCSMEFHRIMKKLKYVLSYVTKIKEEQHESINKFEMDFIDEVEKQKELLIKIQHLQQDCDVPSRELRDLKLNQNMDLHIEEILKDFSESEFPSIKTEFQQVLSNRKEMTQFLEEWLNTRFDIEKLKNGIQKENDRICQVNNFFNNRIIAIMNESTEFEERSATISKEWEQDLKSLKEKNEKLFKNYQTLKTSLASGAQVNPTTQDNKNPHVTSRATQLTTEKIRELENSLHEAKESAMHKESKIIKMQKELEVTNDIIAKLQAKVHESNKCLEKTKETIQVLQDKVALGAKPYKEEIEDLKMKLVKIDLEKMKNAKEFEKEISATKATVEYQKEVIRLLRENLRRSQQAQDTSVISEHTDPQPSNKPLTCGGGSGIVQNTKALILKSEHIRLEKEISKLKQQNEQLIKQKNELLSNNQHLSNEVKTWKERTLKREAHKQVTCENSPKSPKVTGTASKKKQITPSQCKERNLQDPVPKESPKSCFFDSRSKSLPSPHPVRYFDNSSLGLCPEVQNAGAESVDSQPGPWHASSGKDVPECKTQ	Literature-reported	"Cytokinetics Announces Non-Clinical Trial Data Presented at 2007 AACR Annual Meeting. Cytokinetics, Incorporated. 2007."	2	.	.	.	.	.	.	.	.	.	.	.	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	.	.
TTPOA6U	HUMAN centrosomal protein 250 (Cep250)	Q9BV73	CP250_HUMAN	.	C-Nap1; Centrosome-associated protein CEP250; Centrosomal protein 2; Centrosomal Nek2-associated protein 1; 250 kDa centrosomal protein	CEP250	"Human protein centrosomal protein 250 interacts with SARS-CoV-2 Nsp13 protein with high significance, which indicates CEP250 as a potential therapeutic target."	.	.	METRSPGLNNMKPQSLQLVLEEQVLALQQQMAENQAASWRKLKNSQEAQQRQATLVRKLQAKVLQYRSWCQELEKRLEATGGPIPQRWENVEEPNLDELLVRLEEEQQRCESLAEVNTQLRLHMEKADVVNKALREDVEKLTVDWSRARDELMRKESQWQMEQEFFKGYLKGEHGRLLSLWREVVTFRRHFLEMKSATDRDLMELKAEHVRLSGSLLTCCLRLTVGAQSREPNGSGRMDGREPAQLLLLLAKTQELEKEAHERSQELIQLKSQGDLEKAELQDRVTELSALLTQSQKQNEDYEKMIKALRETVEILETNHTELMEHEASLSRNAQEEKLSLQQVIKDITQVMVEEGDNIAQGSGHENSLELDSSIFSQFDYQDADKALTLVRSVLTRRRQAVQDLRQQLAGCQEAVNLLQQQHDQWEEEGKALRQRLQKLTGERDTLAGQTVDLQGEVDSLSKERELLQKAREELRQQLEVLEQEAWRLRRVNVELQLQGDSAQGQKEEQQEELHLAVRERERLQEMLMGLEAKQSESLSELITLREALESSHLEGELLRQEQTEVTAALARAEQSIAELSSSENTLKTEVADLRAAAVKLSALNEALALDKVGLNQQLLQLEEENQSVCSRMEAAEQARNALQVDLAEAEKRREALWEKNTHLEAQLQKAEEAGAELQADLRDIQEEKEEIQKKLSESRHQQEAATTQLEQLHQEAKRQEEVLARAVQEKEALVREKAALEVRLQAVERDRQDLAEQLQGLSSAKELLESSLFEAQQQNSVIEVTKGQLEVQIQTVTQAKEVIQGEVRCLKLELDTERSQAEQERDAAARQLAQAEQEGKTALEQQKAAHEKEVNQLREKWEKERSWHQQELAKALESLEREKMELEMRLKEQQTEMEAIQAQREEERTQAESALCQMQLETEKERVSLLETLLQTQKELADASQQLERLRQDMKVQKLKEQETTGILQTQLQEAQRELKEAARQHRDDLAALQEESSSLLQDKMDLQKQVEDLKSQLVAQDDSQRLVEQEVQEKLRETQEYNRIQKELEREKASLTLSLMEKEQRLLVLQEADSIRQQELSALRQDMQEAQGEQKELSAQMELLRQEVKEKEADFLAQEAQLLEELEASHITEQQLRASLWAQEAKAAQLQLRLRSTESQLEALAAEQQPGNQAQAQAQLASLYSALQQALGSVCESRPELSGGGDSAPSVWGLEPDQNGARSLFKRGPLLTALSAEAVASALHKLHQDLWKTQQTRDVLRDQVQKLEERLTDTEAEKSQVHTELQDLQRQLSQNQEEKSKWEGKQNSLESELMELHETMASLQSRLRRAELQRMEAQGERELLQAAKENLTAQVEHLQAAVVEARAQASAAGILEEDLRTARSALKLKNEEVESERERAQALQEQGELKVAQGKALQENLALLTQTLAEREEEVETLRGQIQELEKQREMQKAALELLSLDLKKRNQEVDLQQEQIQELEKCRSVLEHLPMAVQEREQKLTVQREQIRELEKDRETQRNVLEHQLLELEKKDQMIESQRGQVQDLKKQLVTLECLALELEENHHKMECQQKLIKELEGQRETQRVALTHLTLDLEERSQELQAQSSQIHDLESHSTVLARELQERDQEVKSQREQIEELQRQKEHLTQDLERRDQELMLQKERIQVLEDQRTRQTKILEEDLEQIKLSLRERGRELTTQRQLMQERAEEGKGPSKAQRGSLEHMKLILRDKEKEVECQQEHIHELQELKDQLEQQLQGLHRKVGETSLLLSQREQEIVVLQQQLQEAREQGELKEQSLQSQLDEAQRALAQRDQELEALQQEQQQAQGQEERVKEKADALQGALEQAHMTLKERHGELQDHKEQARRLEEELAVEGRRVQALEEVLGDLRAESREQEKALLALQQQCAEQAQEHEVETRALQDSWLQAQAVLKERDQELEALRAESQSSRHQEEAARARAEALQEALGKAHAALQGKEQHLLEQAELSRSLEASTATLQASLDACQAHSRQLEEALRIQEGEIQDQDLRYQEDVQQLQQALAQRDEELRHQQEREQLLEKSLAQRVQENMIQEKQNLGQEREEEEIRGLHQSVRELQLTLAQKEQEILELRETQQRNNLEALPHSHKTSPMEEQSLKLDSLEPRLQRELERLQAALRQTEAREIEWREKAQDLALSLAQTKASVSSLQEVAMFLQASVLERDSEQQRLQDELELTRRALEKERLHSPGATSTAELGSRGEQGVQLGEVSGVEAEPSPDGMEKQSWRQRLEHLQQAVARLEIDRSRLQRHNVQLRSTLEQVERERRKLKREAMRAAQAGSLEISKATASSPTQQDGRGQKNSDAKCVAELQKEVVLLQAQLTLERKQKQDYITRSAQTSRELAGLHHSLSHSLLAVAQAPEATVLEAETRRLDESLTQSLTSPGPVLLHPSPSTTQAASR	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	.	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-380320: Recruitment of NuMA to mitotic centrosomes; R-HSA-5620912: Anchoring of the basal body to the plasma membrane; R-HSA-8854518: AURKA Activation by TPX2	.	Q9BV73
TT3XBOV	CEP290 messenger RNA (CEP290 mRNA)	O15078	CE290_HUMAN	.	Cep290; Bardet-Biedl syndrome 14 protein; Cancer/testis antigen 87; CT87; Nephrocystin-6; Tumor antigen se2-2	CEP290	"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."	.	.	MPPNINWKEIMKVDPDDLPRQEELADNLLISLSKVEVNELKSEKQENVIHLFRITQSLMKMKAQEVELALEEVEKAGEEQAKFENQLKTKVMKLENELEMAQQSAGGRDTRFLRNEICQLEKQLEQKDRELEDMEKELEKEKKVNEQLALRNEEAENENSKLRRENKRLKKKNEQLCQDIIDYQKQIDSQKETLLSRRGEDSDYRSQLSKKNYELIQYLDEIQTLTEANEKIEVQNQEMRKNLEESVQEMEKMTDEYNRMKAIVHQTDNVIDQLKKENDHYQLQVQELTDLLKSKNEEDDPIMVAVNAKVEEWKLILSSKDDEIIEYQQMLHNLREKLKNAQLDADKSNVMALQQGIQERDSQIKMLTEQVEQYTKEMEKNTCIIEDLKNELQRNKGASTLSQQTHMKIQSTLDILKEKTKEAERTAELAEADAREKDKELVEALKRLKDYESGVYGLEDAVVEIKNCKNQIKIRDREIEILTKEINKLELKISDFLDENEALRERVGLEPKTMIDLTEFRNSKHLKQQQYRAENQILLKEIESLEEERLDLKKKIRQMAQERGKRSATSGLTTEDLNLTENISQGDRISERKLDLLSLKNMSEAQSKNEFLSRELIEKERDLERSRTVIAKFQNKLKELVEENKQLEEGMKEILQAIKEMQKDPDVKGGETSLIIPSLERLVNAIESKNAEGIFDASLHLKAQVDQLTGRNEELRQELRESRKEAINYSQQLAKANLKIDHLEKETSLLRQSEGSNVVFKGIDLPDGIAPSSASIINSQNEYLIHLLQELENKEKKLKNLEDSLEDYNRKFAVIRHQQSLLYKEYLSEKETWKTESKTIKEEKRKLEDQVQQDAIKVKEYNNLLNALQMDSDEMKKILAENSRKITVLQVNEKSLIRQYTTLVELERQLRKENEKQKNELLSMEAEVCEKIGCLQRFKEMAIFKIAALQKVVDNSVSLSELELANKQYNELTAKYRDILQKDNMLVQRTSNLEHLECENISLKEQVESINKELEITKEKLHTIEQAWEQETKLGNESSMDKAKKSITNSDIVSISKKITMLEMKELNERQRAEHCQKMYEHLRTSLKQMEERNFELETKFAELTKINLDAQKVEQMLRDELADSVSKAVSDADRQRILELEKNEMELKVEVSKLREISDIARRQVEILNAQQQSRDKEVESLRMQLLDYQAQSDEKSLIAKLHQHNVSLQLSEATALGKLESITSKLQKMEAYNLRLEQKLDEKEQALYYARLEGRNRAKHLRQTIQSLRRQFSGALPLAQQEKFSKTMIQLQNDKLKIMQEMKNSQQEHRNMENKTLEMELKLKGLEELISTLKDTKGAQKVINWHMKIEELRLQELKLNRELVKDKEEIKYLNNIISEYERTISSLEEEIVQQNKFHEERQMAWDQREVDLERQLDIFDRQQNEILNAAQKFEEATGSIPDPSLPLPNQLEIALRKIKENIRIILETRATCKSLEEKLKEKESALRLAEQNILSRDKVINELRLRLPATAEREKLIAELGRKEMEPKSHHTLKIAHQTIANMQARLNQKEEVLKKYQRLLEKAREEQREIVKKHEEDLHILHHRLELQADSSLNKFKQTAWDLMKQSPTPVPTNKHFIRLAEMEQTVAEQDDSLSSLLVKLKKVSQDLERQREITELKVKEFENIKLQLQENHEDEVKKVKAEVEDLKYLLDQSQKESQCLKSELQAQKEANSRAPTTTMRNLVERLKSQLALKEKQQKALSRALLELRAEMTAAAEERIISATSQKEAHLNVQQIVDRHTRELKTQVEDLNENLLKLKEALKTSKNRENSLTDNLNDLNNELQKKQKAYNKILREKEEIDQENDELKRQIKRLTSGLQGKPLTDNKQSLIEELQRKVKKLENQLEGKVEEVDLKPMKEKNAKEELIRWEEGKKWQAKIEGIRNKLKEKEGEVFTLTKQLNTLKDLFAKADKEKLTLQRKLKTTGMTVDQVLGIRALESEKELEELKKRNLDLENDILYMRAHQALPRDSVVEDLHLQNRYLQEKLHALEKQFSKDTYSKPSISGIESDDHCQREQELQKENLKLSSENIELKFQLEQANKDLPRLKNQVRDLKEMCEFLKKEKAEVQRKLGHVRGSGRSGKTIPELEKTIGLMKKVVEKVQRENEQLKKASGILTSEKMANIEQENEKLKAELEKLKAHLGHQLSMHYESKTKGTEKIIAENERLRKELKKETDAAEKLRIAKNNLEILNEKMTVQLEETGKRLQFAESRGPQLEGADSKSWKSIVVTRMYETKLKELETDIAKKNQSITDLKQLVKEATEREQKVNKYNEDLEQQIKILKHVPEGAETEQGLKRELQVLRLANHQLDKEKAELIHQIEANKDQSGAESTIPDADQLKEKIKDLETQLKMSDLEKQHLKEEIKKLKKELENFDPSFFEEIEDLKYNYKEEVKKNILLEEKVKKLSEQLGVELTSPVAASEEFEDEEESPVNFPIY	Clinical trial	"Clinical pipeline report, company report or official report of ProQR Therapeutics."	.	.	.	.	.	.	.	.	.	.	.	.	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-380320: Recruitment of NuMA to mitotic centrosomes; R-HSA-5620912: Anchoring of the basal body to the plasma membrane; R-HSA-6798695: Neutrophil degranulation; R-HSA-8854518: AURKA Activation by TPX2	.	O15078
TT9XRNV	Ceramide kinase (CERK)	Q8TCT0	CERK1_HUMAN	.	hCERK; Lipid kinase 4; LK4; KIAA1646; Acylsphingosine kinase	CERK	"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."	EC 2.7.1.138	.	MGATGAAEPLQSVLWVKQQRCAVSLEPARALLRWWRSPGPGAGAPGADACSVPVSEIIAVEETDVHGKHQGSGKWQKMEKPYAFTVHCVKRARRHRWKWAQVTFWCPEEQLCHLWLQTLREMLEKLTSRPKHLLVFINPFGGKGQGKRIYERKVAPLFTLASITTDIIVTEHANQAKETLYEINIDKYDGIVCVGGDGMFSEVLHGLIGRTQRSAGVDQNHPRAVLVPSSLRIGIIPAGSTDCVCYSTVGTSDAETSALHIVVGDSLAMDVSSVHHNSTLLRYSVSLLGYGFYGDIIKDSEKKRWLGLARYDFSGLKTFLSHHCYEGTVSFLPAQHTVGSPRDRKPCRAGCFVCRQSKQQLEEEQKKALYGLEAAEDVEEWQVVCGKFLAINATNMSCACRRSPRGLSPAAHLGDGSSDLILIRKCSRFNFLRFLIRHTNQQDQFDFTFVEVYRVKKFQFTSKHMEDEDSDLKEGGKKRFGHICSSHPSCCCTVSNSSWNCDGEVLHSPAIEVRVHCQLVRLFARGIEENPKPDSHS	Literature-reported	Targeting ceramide metabolism with a potent and specific ceramide kinase inhibitor. Mol Pharmacol. 2008 Oct;74(4):925-32.	0	.	.	.	.	.	.	.	.	.	.	hsa00600: Sphingolipid metabolism; hsa01100: Metabolic pathways	R-HSA-1660662: Glycosphingolipid metabolism	.	Q8TCT0
TTMF541	Liver carboxylesterase (CES1)	P23141	EST1_HUMAN	Carboxylic ester hydrolase	Serine esterase 1; Monocyte/macrophage serine esterase; Human carboxylesterase 1; HMSE; HCE1; CES1; Brain carboxylesterase hBr1; Acyl coenzyme A:cholesterol acyltransferase	CES1	"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."	EC 3.1.1.1	5A7H; 5A7G; 5A7F; 4AB1; 3K9B	MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSELFTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGDVKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLKMKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERNFHTVPYMVGINKQEFGWLIPMQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDLIADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLKDKEVAFWTNLFAKKAVEKPPQTEHIEL	Successful	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	34	.	.	.	.	.	.	.	.	.	.	hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways	R-HSA-2022377: Metabolism of Angiotensinogen to Angiotensins; R-HSA-211945: Phase I - Functionalization of compounds; R-HSA-9749641: Aspirin ADME	MetaCyc:HS11616-MON	P23141
TTFQAYR	Cholesteryl ester transfer protein (CETP)	P11597	CETP_HUMAN	Bactericidal permeability increasing protein	Lipid transfer protein I; Cholesterol ester transfer protein	CETP	"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."	.	4F2A; 4EWS; 2OBD	MLAATVLTLALLGNAHACSKGTSHEAGIVCRITKPALLVLNHETAKVIQTAFQRASYPDITGEKAMMLLGQVKYGLHNIQISHLSIASSQVELVEAKSIDVSIQNVSVVFKGTLKYGYTTAWWLGIDQSIDFEIDSAIDLQINTQLTCDSGRVRTDAPDCYLSFHKLLLHLQGEREPGWIKQLFTNFISFTLKLVLKGQICKEINVISNIMADFVQTRAASILSDGDIGVDISLTGDPVITASYLESHHKGHFIYKNVSEDLPLPTFSPTLLGDSRMLYFWFSERVFHSLAKVAFQDGRLMLSLMGDEFKAVLETWGFNTNQEIFQEVVGGFPSQAQVTVHCLKMPKISCQNKGVVVNSSVMVKFLFPRPDQQHSVAYTFEEDIVTTVQASYSKKKLFLSLLDFQITPKTVSNLTESSSESVQSFLQSMITAVGIPEVMSRLEVVFTALMNSKGVSLFDIINPEIITRDGFLLLQMDFGFPEHLLVDFLQSLS	Clinical trial	"Clinical pipeline report, company report or official report of Roche (2009)."	25	TC=1.C.40	Bactericidal permeability increasing protein	BPI/LBP/Plunc superfamily. BPI/LBP family.	.	.	"LBP / BPI / CETP family, N-terminal domain; LBP / BPI / CETP family, C-terminal domain"	PF01273; PF02886	PF01273; LBP_BPI_CETP; PF02886; LBP_BPI_CETP_C	1.C.40.1.8	The Bactericidal Permeability Increasing Protein (BPIP) Family	hsa04979: Cholesterol metabolism	R-HSA-171052:LDL-mediated lipid transport; R-HSA-194223:HDL-mediated lipid transport	.	P11597
TTA0P7K	Complement factor B (CFB)	P00751	CFAB_HUMAN	Peptidase	Properdin factor B; PBF2; Glycinerich beta glycoprotein; Glycine-rich beta glycoprotein; GBG; Complement factor B Bb fragment; C3/C5 convertase; BFD; BF	CFB	"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."	EC 3.4.21.47	6RAV; 6QSX; 6QSW; 5M6W; 3HS0	MGSNLSPQLCLMPFILGLLSGGVTTTPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL	Clinical trial	"A soluble chimeric inhibitor of C3 and C5 convertases, complement activation blocker-2, prolongs graft survival in pig-to-rhesus monkey heart transplantation. Xenotransplantation. 2002 Mar;9(2):125-34."	3	EC:3.4	Peptidase	peptidase S1 family.	3.4.21.47	Acting on peptide bonds (peptidases)	Sushi repeat (SCR repeat); Trypsin; von Willebrand factor type A domain	PF00084; PF00089; PF00092	PF00084; Sushi; PF00089; Trypsin; PF00092; VWA	.	.	hsa04610:Complement and coagulation cascades; hsa05150:Staphylococcus aureus infection	R-HSA-173736:Alternative complement activation; R-HSA-174577:Activation of C3 and C5; R-HSA-977606:Regulation of Complement cascade	.	P00751
TT3SGK7	CFB messenger RNA (CFB mRNA)	P00751	CFAB_HUMAN	.	C3/C5 convertase; Glycine-rich beta glycoprotein; GBG; PBF2; Properdin factor B	CFB	"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."	EC 3.4.21.47	.	MGSNLSPQLCLMPFILGLLSGGVTTTPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL	Clinical trial	"Clinical pipeline report, company report or official report of Ionis Pharmaceuticals."	.	.	.	.	.	.	.	.	.	.	.	hsa04610: Complement and coagulation cascades; hsa05150: Staphylococcus aureus infection; hsa05171: Coronavirus disease - COVID-19	R-HSA-173736: Alternative complement activation; R-HSA-174577: Activation of C3 and C5; R-HSA-977606: Regulation of Complement cascade	.	P00751
TT8D13I	Complement factor D (CFD)	P00746	CFAD_HUMAN	Peptidase	Properdin factor D; PFD; DF; C3 convertase activator; Adipsin	CFD	"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."	EC 3.4.21.46	6QMT; 6QMR; 6FUT; 6FUJ; 6FUI	MHSWERLAVLVLLGAAACAAPPRGRILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGKVQVLLGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKATLGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLDRATCNRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSGSRVCGNRKKPGIYTRVASYAAWIDSVLA	Clinical trial	Association for Research in Vision and Ophthalmology (ARVO)--2010 Annual Meeting. For Sight: The Future of Eye and Vision Research--part 1. IDrugs. 2010 Jul;13(7):427-9.	19	.	.	.	.	.	.	.	.	.	.	hsa04610:Complement and coagulation cascades; hsa05150:Staphylococcus aureus infection	R-HSA-114608:Platelet degranulation; R-HSA-173736:Alternative complement activation	.	P00746
TTUW6OP	Complement factor H (CFH)	P08603	CFAH_HUMAN	.	HF2; HF1; HF; H factor 1	CFH	"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."	.	6ATG; 5WTB; 5O35; 5O32; 5NBQ	MRLLAKIICLMLWAICVAEDCNELPPRRNTEILTGSWSDQTYPEGTQAIYKCRPGYRSLGNVIMVCRKGEWVALNPLRKCQKRPCGHPGDTPFGTFTLTGGNVFEYGVKAVYTCNEGYQLLGEINYRECDTDGWTNDIPICEVVKCLPVTAPENGKIVSSAMEPDREYHFGQAVRFVCNSGYKIEGDEEMHCSDDGFWSKEKPKCVEISCKSPDVINGSPISQKIIYKENERFQYKCNMGYEYSERGDAVCTESGWRPLPSCEEKSCDNPYIPNGDYSPLRIKHRTGDEITYQCRNGFYPATRGNTAKCTSTGWIPAPRCTLKPCDYPDIKHGGLYHENMRRPYFPVAVGKYYSYYCDEHFETPSGSYWDHIHCTQDGWSPAVPCLRKCYFPYLENGYNQNYGRKFVQGKSIDVACHPGYALPKAQTTVTCMENGWSPTPRCIRVKTCSKSSIDIENGFISESQYTYALKEKAKYQCKLGYVTADGETSGSITCGKDGWSAQPTCIKSCDIPVFMNARTKNDFTWFKLNDTLDYECHDGYESNTGSTTGSIVCGYNGWSDLPICYERECELPKIDVHLVPDRKKDQYKVGEVLKFSCKPGFTIVGPNSVQCYHFGLSPDLPICKEQVQSCGPPPELLNGNVKEKTKEEYGHSEVVEYYCNPRFLMKGPNKIQCVDGEWTTLPVCIVEESTCGDIPELEHGWAQLSSPPYYYGDSVEFNCSESFTMIGHRSITCIHGVWTQLPQCVAIDKLKKCKSSNLIILEEHLKNKKEFDHNSNIRYRCRGKEGWIHTVCINGRWDPEVNCSMAQIQLCPPPPQIPNSHNMTTTLNYRDGEKVSVLCQENYLIQEGEEITCKDGRWQSIPLCVEKIPCSQPPQIEHGTINSSRSSQESYAHGTKLSYTCEGGFRISEENETTCYMGKWSSPPQCEGLPCKSPPEISHGVVAHMSDSYQYGEEVTYKCFEGFGIDGPAIAKCLGEKWSHPPSCIKTDCLSLPSFENAIPMGEKKDVYKAGEQVTYTCATYYKMDGASNVTCINSRWTGRPTCRDTSCVNPPTVQNAYIVSRQMSKYPSGERVRYQCRSPYEMFGDEEVMCLNGNWTEPPQCKDSTGKCGPPPPIDNGDITSFPLSVYAPASSVEYQCQNLYQLEGNKRITCRNGQWSEPPKCLHPCVISREIMENYNIALRWTAKQKLYSRTGESVEFVCKRGYRLSSRSHTLRTTCWDGKLEYPTCAKR	Clinical trial	The complement receptor 2/factor H fusion protein TT30 protects paroxysmal nocturnal hemoglobinuria erythrocytes from complement-mediated hemolysis and C3 fragment. Blood. 2012 Jun 28;119(26):6307-16.	17	.	Complement system	.	.	.	Sushi repeat (SCR repeat)	PF00084	PF00084; Sushi	.	.	hsa04610:Complement and coagulation cascades; hsa05150:Staphylococcus aureus infection	R-HSA-977606:Regulation of Complement cascade	.	P08603
TT6ATLX	Complement factor I (CFI)	P05156	CFAI_HUMAN	Peptidase	IF; Complement factor I light chain; C3B/C4B inactivator	CFI	"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."	EC 3.4.21.45	5O32; 2XRC	MKLLHVFLLFLCFHLRFCKVTYTSQEDLVEKKCLAKKYTHLSCDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVCATNRRSFPTYCQQKSLECLHPGTKFLNNGTCTAEGKFSVSLKHGNTDSEGIVEVKLVDQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSINSTECLHVHCRGLETSLAECTFTKRRTMGYQDFADVVCYTQKADSPMDDFFQCVNGKYISQMKACDGINDCGDQSDELCCKACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGCAGFASVTQEETEILTADMDAERRRIKSLLPKLSCGVKNRMHIRRKRIVGGKRAQLGDLPWQVAIKDASGITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEYVDRIIFHENYNAGTYQNDIALIEMKKDGNKKDCELPRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERVFSLQWGEVKLISNCSKFYGNRFYEKEMECAGTYDGSIDACKGDSGGPLVCMDANNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYHVGRPFISQYNV	Literature-reported	Endothelial targeting and enhanced antiinflammatory effects of complement inhibitors possessing sialyl Lewisx moieties. J Immunol. 1999 Apr 15;162(8):4952-9.	2	EC:3.4	Peptidase	peptidase S1 family.	3.4.21.45	Acting on peptide bonds (peptidases)	Low-density lipoprotein receptor domain class A; Scavenger receptor cysteine-rich domain; Trypsin	PF00057; PF00530; PF00089	PF00057; Ldl_recept_a; PF00530; SRCR; PF00089; Trypsin	.	.	hsa04610:Complement and coagulation cascades; hsa05150:Staphylococcus aureus infection	R-HSA-977606:Regulation of Complement cascade	.	P05156
TTJZQYH	CASP8-FADD-like regulator (CFLAR)	O15519	CFLAR_HUMAN	Peptidase	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	CFLAR	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.	.	3H13; 3H11; 2N5R	MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVETHLLRNPHLVSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKYKQSVQGAGTSYRNVLQAAIQKSLKDPSNNFRLHNGRSKEQRLKEQLGAQQEPVKKSIQESEAFLPQSIPEERYKMKSKPLGICLIIDCIGNETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLVSRGGSQSVYGVDQTHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYVVSEGQLEDSSLLEVDGPAMKNVEFKAQKRGLCTVHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQERKRPLLDLHIELNGYMYDWNSRVSAKEKYYVWLQHTLRKKLILSYT	Literature-reported	Targeting CASP8 and FADD-like apoptosis regulator ameliorates nonalcoholic steatohepatitis in mice and nonhuman primates. Nat Med. 2017 Apr;23(4):439-449.	.	EC:3.4	.	peptidase C14A family.	.	.	Death effector domain	PF01335	PF01335; DED	.	.	hsa04064: NF-kappa B signaling pathway; hsa04140: Autophagy - animal; hsa04210: Apoptosis; hsa04217: Necroptosis; hsa04668: TNF signaling pathway; hsa05142: Chagas disease; hsa05160: Hepatitis C	R-HSA-3371378: Regulation by c-FLIP; R-HSA-5213460: RIPK1-mediated regulated necrosis; R-HSA-5218900: CASP8 activity is inhibited; R-HSA-5357905: Regulation of TNFR1 signaling; R-HSA-69416: Dimerization of procaspase-8; R-HSA-75158: TRAIL signaling	.	O15519
TTLA0VS	Complement factor P (CFP)	P27918	PROP_HUMAN	.	Properdin; CFP	CFP	A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes.	.	1W0S; 1W0R	MITEGAQAPRLLLPPLLLLLTLPATGSDPVLCFTQYEESSGKCKGLLGGGVSVEDCCLNTAFAYQKRSGGLCQPCRSPRWSLWSTWAPCSVTCSEGSQLRYRRCVGWNGQCSGKVAPGTLEWQLQACEDQQCCPEMGGWSGWGPWEPCSVTCSKGTRTRRRACNHPAPKCGGHCPGQAQESEACDTQQVCPTHGAWATWGPWTPCSASCHGGPHEPKETRSRKCSAPEPSQKPPGKPCPGLAYEQRRCTGLPPCPVAGGWGPWGPVSPCPVTCGLGQTMEQRTCNHPVPQHGGPFCAGDATRTHICNTAVPCPVDGEWDSWGEWSPCIRRNMKSISCQEIPGQQSRGRTCRGRKFDGHRCAGQQQDIRHCYSIQHCPLKGSWSEWSTWGLCMPPCGPNPTRARQRLCTPLLPKYPPTVSMVEGQGEKNVTFWGRPLPRCEELQGQKLVVEEKRPCLHVPACKDPEEEEL	Clinical trial	Properdin in complement activation and tissue injury. Mol Immunol. 2013 Dec 15;56(3):191-8.	.	.	.	.	.	.	.	.	.	.	.	hsa05168: Herpes simplex virus 1 infection	R-HSA-173736: Alternative complement activation; R-HSA-174577: Activation of C3 and C5; R-HSA-5083635: Defective B3GALTL causes PpS; R-HSA-5173214: O-glycosylation of TSR domain-containing proteins; R-HSA-6798695: Neutrophil degranulation; R-HSA-977606: Regulation of Complement cascade	.	P27918
TTRLZHP	cAMP-dependent chloride channel (CFTR)	P13569	CFTR_HUMAN	ABC transporter	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	CFTR	"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."	EC 5.6.1.6	6MSM; 6HEP; 5UAK; 5TGK; 5TFJ	MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. 2015	34	TC=3.A.1	Acid anhydrides hydrolase	ABC transporter superfamily. ABCC family. CFTR transporter (TC 3.A.1.202) subfamily. 	5.6.1.6 	Isomerases altering macromolecular conformation	"ABC transporter transmembrane region; ABC transporter; Cystic fibrosis TM conductance regulator (CFTR), regulator domain"	PF00664; PF00005; PF14396	PF00664; ABC_membrane; PF00005; ABC_tran; PF14396; CFTR_R	3.A.1.202.1	The ATP-binding Cassette (ABC) Superfamily	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	R-HSA-382556:ABC-family proteins mediated transport	MetaCyc:HS00075-MON	P13569
TTFPKRB	cAMP-dependent chloride channel F508 deletion (CFTR del F508)	P13569 (del F508)	CFTR_HUMAN	ABC transporter	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)	CFTR	"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."	EC 5.6.1.6	6MSM; 6HEP; 5UAK; 5TGK; 5TFJ	MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL	Successful	Antibodies and venom peptides: new modalities for ion channels. Nat Rev Drug Discov. 2019 May;18(5):339-357.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	P13569
TTFC29G	Glycoprotein hormones alpha (CGA)	P01215	GLHA_HUMAN	Glycoprotein hormone	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	CGA	"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."	.	4MQW; 4AY9; 1XWD; 1XUL; 1QFW	MDYYRKYAAIFLVTLSVFLHVLHSAPDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04912:GnRH signaling pathway; hsa04913:Ovarian steroidogenesis; hsa04917:Prolactin signaling pathway; hsa04918:Thyroid hormone synthesis; hsa05320:Autoimmune thyroid disease	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	.	P01215
TTUH273	Choriogonadotropin beta (CG-beta)	P0DN86	CGB3_HUMAN	Hormone	Chorionic gonadotropin beta subunit; Chorionic gonadotrophin beta subunit; CG-beta	CGB3	Stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy.	.	1XUL; 1QFW; 1HRP; 1HCN	MEMFQGLLLLLLLSMGGTWASKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ	Clinical trial	CDX-1307: a novel vaccine under study as treatment for muscle-invasive bladder cancer. Expert Rev Vaccines. 2011 Jun;10(6):733-42.	21	.	.	.	.	.	.	.	.	.	.	.	R-HSA-209822: Glycoprotein hormones; R-HSA-8866910: TFAP2 (AP-2) family regulates transcription of growth factors and their receptors	.	P0DN86
TTCSI1E	Clostridium histolyticum Collagenase (CH colG)	Q9X721	COLG_HATHI	.	Microbial collagenase; Gelatinase ColG; Collagenase ColG; Class I collagenase	CH colG	"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."	EC 3.4.24.3	5IKU; 4TN9; 4JRW; 4HPK; 4ARE	MKKNILKILMDSYSKESKIQTVRRVTSVSLLAVYLTMNTSSLVLAKPIENTNDTSIKNVEKLRNAPNEENSKKVEDSKNDKVEHVKNIEEAKVEQVAPEVKSKSTLRSASIANTNSEKYDFEYLNGLSYTELTNLIKNIKWNQINGLFNYSTGSQKFFGDKNRVQAIINALQESGRTYTANDMKGIETFTEVLRAGFYLGYYNDGLSYLNDRNFQDKCIPAMIAIQKNPNFKLGTAVQDEVITSLGKLIGNASANAEVVNNCVPVLKQFRENLNQYAPDYVKGTAVNELIKGIEFDFSGAAYEKDVKTMPWYGKIDPFINELKALGLYGNITSATEWASDVGIYYLSKFGLYSTNRNDIVQSLEKAVDMYKYGKIAFVAMERITWDYDGIGSNGKKVDHDKFLDDAEKHYLPKTYTFDNGTFIIRAGDKVSEEKIKRLYWASREVKSQFHRVVGNDKALEVGNADDVLTMKIFNSPEEYKFNTNINGVSTDNGGLYIEPRGTFYTYERTPQQSIFSLEELFRHEYTHYLQARYLVDGLWGQGPFYEKNRLTWFDEGTAEFFAGSTRTSGVLPRKSILGYLAKDKVDHRYSLKKTLNSGYDDSDWMFYNYGFAVAHYLYEKDMPTFIKMNKAILNTDVKSYDEIIKKLSDDANKNTEYQNHIQELADKYQGAGIPLVSDDYLKDHGYKKASEVYSEISKAASLTNTSVTAEKSQYFNTFTLRGTYTGETSKGEFKDWDEMSKKLDGTLESLAKNSWSGYKTLTAYFTNYRVTSDNKVQYDVVFHGVLTDNADISNNKAPIAKVTGPSTGAVGRNIEFSGKDSKDEDGKIVSYDWDFGDGATSRGKNSVHAYKKAGTYNVTLKVTDDKGATATESFTIEIKNEDTTTPITKEMEPNDDIKEANGPIVEGVTVKGDLNGSDDADTFYFDVKEDGDVTIELPYSGSSNFTWLVYKEGDDQNHIASGIDKNNSKVGTFKSTKGRHYVFIYKHDSASNISYSLNIKGLGNEKLKEKENNDSSDKATVIPNFNTTMQGSLLGDDSRDYYSFEVKEEGEVNIELDKKDEFGVTWTLHPESNINDRITYGQVDGNKVSNKVKLRPGKYYLLVYKYSGSGNYELRVNK	Literature-reported	"DrugBank: a knowledgebase for drugs, drug actions and drug targets. Nucleic Acids Res. 2008 Jan;36(Database issue):D901-6."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9X721
TTKYFSB	Choline acetylase	.	CLAT_HUMAN	Single Protein	Choline O-acetyltransferase; CHOACTase; ChAT	CHAT	Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.	.	.	MGLRTAKKRGLGGGGKWKREEGGGTRGRREVRPACFLQSGGRGDPGDVGGPAGNPGCSPHPRAATRPPPLPAHTPAHTPEWCGAASAEAAEPRRAGPHLCIPAPGLTKTPILEKVPRKMAAKTPSSEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQQKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLISGVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFSSYRLPGHTQDTLVAQNSSIMPEPEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNEDERLPPIGLLTSDGRSEWAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANRWYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHVTQSSRKLIRADSVSELPAPRRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDAFIQVALQLAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLLKDAIRAQTAYTVMAITGMAIDNHLLALRELARAMCKELPEMFMDETYLMSNRFVLSTSQVPTTTEMFCCYGPVVPNGYGACYNPQPETILFCISSFHSCKETSSSKFAKAVEESLIDMRDLCSLLPPTESKPLATKEKATRPSQGHQP	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P28329
TTTU902	Checkpoint kinase-1 (CHK1)	O14757	CHK1_HUMAN	Kinase	Serine/threonine-protein kinase Chk1; Chk1; Cell cycle checkpoint kinase; CHK1 checkpoint homolog	CHEK1	"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."	EC 2.7.11.1	6FCK; 6FCF; 6FC8; 5WI2; 5OQ8	MAVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINKMLNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLKRREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRPRVTSGGVSESPSGFSKHIQSNLDFSPVNSASSEENVKYSSSQPEPRTGLSLWDTSPSYIDKLVQGISFSQPTCPDHMLLNSQLLGTPGSSQNPWQRLVKRMTRFFTKLDADKSYQCLKETCEKLGYQWKKSCMNQVTISTTDRRNNKLIFKVNLLEMDDKILVDFRLSKGDGLEFKRHFLKIKGKLIDIVSSQKIWLPAT	Clinical trial	Characterization of an inhibitory dynamic pharmacophore for the ERCC1-XPA interaction using a combined molecular dynamics and virtual screening app... J Mol Graph Model. 2009 Sep;28(2):113-30.	21	EC:2.7	Kinase	protein kinase superfamily. CAMK Ser/Thr protein kinase family. NIM1 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04110:Cell cycle; hsa04115:p53 signaling pathway; hsa05166:HTLV-I infection; hsa05203:Viral carcinogenesis	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	.	O14757
TT9ABMF	Serine/threonine-protein kinase Chk2 (RAD53)	O96017	CHK2_HUMAN	Kinase	hCds1; Hucds1; Checkpoint kinase 2; Cds1 homolog; Cds1; CHK2 checkpoint homolog; CHK2	CHEK2	"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."	EC 2.7.11.1	4BDK; 4BDJ; 4BDI; 4BDH; 4BDG	MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTPAPWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKRRPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDLLSEENESTALPQVLAQPSTSRKRPREGEAEGAETTKRPAVCAAVL	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1988).	21	EC:2.7	Kinase	protein kinase superfamily. CAMK Ser/Thr protein kinase family. CHK2 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	FHA domain; Protein kinase domain	PF00498; PF00069	PF00498; FHA; PF00069; Pkinase	.	.	hsa04110:Cell cycle; hsa04115:p53 signaling pathway; hsa05166:HTLV-I infection	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	.	O96017
TTJB1O0	Acidic mammalian chitinase (CHIA)	Q9BZP6	CHIA_HUMAN	Glycosylase	Lung-specific protein TSA1902; CHIA; AMCase	CHIA	"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. ."	EC 3.2.1.14	3RME; 3RM9; 3RM8; 3RM4; 3FY1	MTKLILLTGLVLILNLQLGSAYQLTCYFTNWAQYRPGLGRFMPDNIDPCLCTHLIYAFAGRQNNEITTIEWNDVTLYQAFNGLKNKNSQLKTLLAIGGWNFGTAPFTAMVSTPENRQTFITSVIKFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSGSSSSGGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA	Literature-reported	Acidic mammalian chitinase tuning after enteric helminths eradication in inflammatory respiratory disease patients. Parasite Immunol. 2018 Nov;40(11):e12583.	.	.	.	.	.	.	.	.	.	.	.	hsa00520: Amino sugar and nucleotide sugar metabolism; hsa01100: Metabolic pathways	R-HSA-189085: Digestion of dietary carbohydrate	.	Q9BZP6
TTDYX6T	Chitinase (CHIT1)	Q13231	CHIT1_HUMAN	Glycosylase	Chitotriosidase1; Chitinase1; CHIT1	CHIT1	"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}."	EC 3.2.1.14	5NRF; 5NRA; 5NR8; 5HBF; 4WKH	MVRSVAWAGFMVLLMIPWGSAAKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAGMTNHQLSTTEWNDETLYQEFNGLKKMNPKLKTLLAIGGWNFGTQKFTDMVATANNRQTFVNSAIRFLRKYSFDGLDLDWEYPGSQGSPAVDKERFTTLVQDLANAFQQEAQTSGKERLLLSAAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESGAAASLNVDAAVQQWLQKGTPASKLILGMPTYGRSFTLASSSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSWKGATKQRIQDQKVPYIFRDNQWVGFDDVESFKTKVSYLKQKGLGGAMVWALDLDDFAGFSCNQGRYPLIQTLRQELSLPYLPSGTPELEVPKPGQPSEPEHGPSPGQDTFCQGKADGLYPNPRERSSFYSCAAGRLFQQSCPTGLVFSNSCKCCTWN	Literature-reported	"Role of chitin and chitinase/chitinase-like proteins in inflammation, tissue remodeling, and injury. Annu Rev Physiol. 2011;73:479-501."	.	.	.	.	.	.	.	.	.	.	.	hsa00520: Amino sugar and nucleotide sugar metabolism; hsa01100: Metabolic pathways	R-HSA-189085: Digestion of dietary carbohydrate; R-HSA-6798695: Neutrophil degranulation	.	Q13231
TT10AWB	Choline kinase (CHKA)	P35790	CHKA_HUMAN	Kinase	ChoK; CHKA; CHETK-alpha	CHKA	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.	EC 2.7.1.32	5W6O; 5FUT; 5FTG; 5EQY; 5EQP	MKTKFCTGGEAEPSPLGLLLSCGSGSAAPAPGVGQQRDAASDLESKQLGGQQPPLALPPPPPLPLPLPLPQPPPPQPPADEQPEPRTRRRAYLWCKEFLPGAWRGLREDEFHISVIRGGLSNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQMRSCNKEGSEQAQKENEFQGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKLGV	Clinical trial	National Cancer Institute Drug Dictionary (drug id 687183).	17	.	.	.	.	.	.	.	.	.	.	hsa00564:Glycerophospholipid metabolism; hsa01100:Metabolic pathways; hsa05231:Choline metabolism in cancer	R-HSA-1483191: Synthesis of PC; R-HSA-1483213: Synthesis of PE	MetaCyc:HS03334-MON	P35790
TTOA18V	Rab proteins geranylgeranyltransferase component A 1 (CHM)	P24386	RAE1_HUMAN	.	Choroideremia protein; Rab escort protein 1; REP-1; TCD protein	CHM	"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."	.	.	MADTLPSEFDVIVIGTGLPESIIAAACSRSGRRVLHVDSRSYYGGNWASFSFSGLLSWLKEYQENSDIVSDSPVWQDQILENEEAIALSRKDKTIQHVEVFCYASQDLHEDVEEAGALQKNHALVTSANSTEAADSAFLPTEDESLSTMSCEMLTEQTPSSDPENALEVNGAEVTGEKENHCDDKTCVPSTSAEDMSENVPIAEDTTEQPKKNRITYSQIIKEGRRFNIDLVSKLLYSRGLLIDLLIKSNVSRYAEFKNITRILAFREGRVEQVPCSRADVFNSKQLTMVEKRMLMKFLTFCMEYEKYPDEYKGYEEITFYEYLKTQKLTPNLQYIVMHSIAMTSETASSTIDGLKATKNFLHCLGRYGNTPFLFPLYGQGELPQCFCRMCAVFGGIYCLRHSVQCLVVDKESRKCKAIIDQFGQRIISEHFLVEDSYFPENMCSRVQYRQISRAVLITDRSVLKTDSDQQISILTVPAEEPGTFAVRVIELCSSTMTCMKGTYLVHLTCTSSKTAREDLESVVQKLFVPYTEMEIENEQVEKPRILWALYFNMRDSSDISRSCYNDLPSNVYVCSGPDCGLGNDNAVKQAETLFQEICPNEDFCPPPPNPEDIILDGDSLQPEASESSAIPEANSETFKESTNLGNLEESSE	Clinical trial	"Clinical pipeline report, company report or official report of Spark Therapeutics."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-6803205: TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain; R-HSA-8873719: RAB geranylgeranylation; R-HSA-8876198: RAB GEFs exchange GTP for GDP on RABs	.	P24386
TT09EZF	Charged multivesicular body protein 4B (CHMP4B)	Q9H444	CHM4B_HUMAN	.	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	CHMP4B	"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."	.	5MK2; 4ABM; 3UM3; 3C3Q	MSVFGKLFGAGGGKAGKGGPTPQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDEDELMAELEELEQEELDKNLLEISGPETVPLPNVPSIALPSKPAKKKEEEDDDMKELENWAGSM	Literature-reported	High CHMP4B expression is associated with accelerated cell proliferation and resistance to doxorubicin in hepatocellular carcinoma. Tumour Biol. 2015 Apr;36(4):2569-81.	.	.	.	SNF7 family.	.	.	Snf7	PF03357	PF03357; Snf7	.	.	hsa03250: Viral life cycle - HIV-1; hsa04144: Endocytosis; hsa04217: Necroptosis	R-HSA-162588: Budding and maturation of HIV virion; R-HSA-1632852: Macroautophagy; R-HSA-5620971: Pyroptosis; R-HSA-917729: Endosomal Sorting Complex Required For Transport (ESCRT); R-HSA-9610379: HCMV Late Events; R-HSA-9615710: Late endosomal microautophagy; R-HSA-9668328: Sealing of the nuclear envelope (NE) by ESCRT-III; R-HSA-9679504: Translation of Replicase and Assembly of the Replication Transcription Complex; R-HSA-9694676: Translation of Replicase and Assembly of the Replication Transcription Complex	.	Q9H444
TT39YVO	Beta-chimaerin (CHN2)	P52757	CHIO_HUMAN	Zinc-finger	Rho-GTPase-activating protein 3; CHN2; Beta2-chimaerin; Beta-chimerin	CHN2	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.	.	1XA6	MAASSNSSLSGSSVSSDAEEYQPPIWKSYLYQLQQEAPRPKRIICPREVENRPKYYGREFHGIISREQADELLGGVEGAYILRESQRQPGCYTLALRFGNQTLNYRLFHDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYISKMTTNPIYEHIGYATLLREKVSRRLSRSKNEPRKTNVTHEEHTAVEKISSLVRRAALTHNDNHFNYEKTHNFKVHTFRGPHWCEYCANFMWGLIAQGVRCSDCGLNVHKQCSKHVPNDCQPDLKRIKKVYCCDLTTLVKAHNTQRPMVVDICIREIEARGLKSEGLYRVSGFTEHIEDVKMAFDRDGEKADISANVYPDINIITGALKLYFRDLPIPVITYDTYSKFIDAAKISNADERLEAVHEVLMLLPPAHYETLRYLMIHLKKVTMNEKDNFMNAENLGIVFGPTLMRPPEDSTLTTLHDMRYQKLIVQILIENEDVLF	Literature-reported	Beta2-chimaerin is a high affinity receptor for the phorbol ester tumor promoters. J Biol Chem. 1997 Oct 17;272(42):26488-96.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-9013149: RAC1 GTPase cycle	.	P52757
TTAZB7S	N-acetylgalactosaminyltransferase 2 (CHPF)	Q8IZ52	CHSS2_HUMAN	Hexosyltransferase	Nacetylgalactosaminylproteoglycan 3betaglucuronosyltransferase II; GlucuronosylNacetylgalactosaminylproteoglycan 4betaNacetylgalactosaminyltransferase II; Chondroitinpolymerizing factor; Chondroitin sulfate synthase 2; Chondroitin glucuronyltransferase 2; ChPF	CHPF	"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."	EC 2.4.1.175	.	MRASLLLSVLRPAGPVAVGISLGFTLSLLSVTWVEEPCGPGPPQPGDSELPPRGNTNAARRPNSVQPGAEREKPGAGEGAGENWEPRVLPYHPAQPGQAAKKAVRTRYISTELGIRQRLLVAVLTSQTTLPTLGVAVNRTLGHRLERVVFLTGARGRRAPPGMAVVTLGEERPIGHLHLALRHLLEQHGDDFDWFFLVPDTTYTEAHGLARLTGHLSLASAAHLYLGRPQDFIGGEPTPGRYCHGGFGVLLSRMLLQQLRPHLEGCRNDIVSARPDEWLGRCILDATGVGCTGDHEGVHYSHLELSPGEPVQEGDPHFRSALTAHPVRDPVHMYQLHKAFARAELERTYQEIQELQWEIQNTSHLAVDGDQAAAWPVGIPAPSRPASRFEVLRWDYFTEQHAFSCADGSPRCPLRGADRADVADVLGTALEELNRRYHPALRLQKQQLVNGYRRFDPARGMEYTLDLQLEALTPQGGRRPLTRRVQLLRPLSRVEILPVPYVTEASRLTVLLPLAAAERDLAPGFLEAFATAALEPGDAAAALTLLLLYEPRQAQRVAHADVFAPVKAHVAELERRFPGARVPWLSVQTAAPSPLRLMDLLSKKHPLDTLFLLAGPDTVLTPDFLNRCRMHAISGWQAFFPMHFQAFHPAVAPPQGPGPPELGRDTGRFDRQAASEACFYNSDYVAARGRLAAASEQEEELLESLDVYELFLHFSSLHVLRAVEPALLQRYRAQTCSARLSEDLYHRCLQSVLEGLGSRTQLAMLLFEQEQGNST	Literature-reported	Polypeptide N-acetylgalactosaminyltransferase 2 regulates cellular metastasis-associated behavior in gastric cancer. Int J Mol Med. 2012 Dec;30(6):1267-74.	.	.	.	.	.	.	.	.	.	.	.	hsa00532: Glycosaminoglycan biosynthesis - chondroitin sulfate / dermatan sulfate; hsa01100: Metabolic pathways	R-HSA-2022870: Chondroitin sulfate biosynthesis	MetaCyc:HS13103-MON	Q8IZ52
TTZ9SOR	Muscarinic acetylcholine receptor M1 (CHRM1)	P11229	ACM1_HUMAN	GPCR rhodopsin	M1 receptor	CHRM1	"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."	.	6OIJ; 5CXV	MNTSAPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPETPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPTKQPPRSSPNTVKRPTKKGRDRAGKGQKPRGKEQLAKRKTFSLVKEKKAARTLSAILLAFILTWTPYNIMVLVSTFCKDCVPETLWELGYWLCYVNSTINPMCYALCNKAFRDTFRLLLLCRWDKRRWRKIPKRPGSVHRTPSRQC	Successful	Negative crosstalk between M1 and M2 muscarinic autoreceptors involves endogenous adenosine activating A1 receptors at the rat motor endplate. Neurosci Lett. 2009 Aug 14;459(3):127-31.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family. Muscarinic acetylcholine receptor subfamily. CHRM1 sub-subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	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	R-HSA-390648:Muscarinic acetylcholine receptors; R-HSA-416476:G alpha (q) signalling events	.	P11229
TTYEG6Q	Muscarinic acetylcholine receptor M2 (CHRM2)	P08172	ACM2_HUMAN	GPCR rhodopsin	M2 receptor; CHRM2	CHRM2	"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."	.	6OIK; 5ZKC; 5ZKB; 5ZK8; 5ZK3	MNNSTNSSNNSLALTSPYKTFEVVFIVLVAGSLSLVTIIGNILVMVSIKVNRHLQTVNNYFLFSLACADLIIGVFSMNLYTLYTVIGYWPLGPVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPVKRTTKMAGMMIAAAWVLSFILWAPAILFWQFIVGVRTVEDGECYIQFFSNAAVTFGTAIAAFYLPVIIMTVLYWHISRASKSRIKKDKKEPVANQDPVSPSLVQGRIVKPNNNNMPSSDDGLEHNKIQNGKAPRDPVTENCVQGEEKESSNDSTSVSAVASNMRDDEITQDENTVSTSLGHSKDENSKQTCIRIGTKTPKSDSCTPTNTTVEVVGSSGQNGDEKQNIVARKIVKMTKQPAKKKPPPSREKKVTRTILAILLAFIITWAPYNVMVLINTFCAPCIPNTVWTIGYWLCYINSTINPACYALCNATFKKTFKHLLMCHYKNIGATR	Successful	The amygdala modulates morphine-induced state-dependent memory retrieval via muscarinic acetylcholine receptors. Neuroscience. 2009 May 5;160(2):255-63.	34	.	.	.	.	.	.	.	.	.	.	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	R-HSA-390648:Muscarinic acetylcholine receptors; R-HSA-418594:G alpha (i) signalling events	.	P08172
TTQ13Z5	Muscarinic acetylcholine receptor M3 (CHRM3)	P20309	ACM3_HUMAN	GPCR rhodopsin	M3 receptor; CHRM3	CHRM3	"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."	.	2CSA	MTLHNNSTTSPLFPNISSSWIHSPSDAGLPPGTVTHFGSYNVSRAAGNFSSPDGTTDDPLGGHTVWQVVFIAFLTGILALVTIIGNILVIVSFKVNKQLKTVNNYFLLSLACADLIIGVISMNLFTTYIIMNRWALGNLACDLWLAIDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTTKRAGVMIGLAWVISFVLWAPAILFWQYFVGKRTVPPGECFIQFLSEPTITFGTAIAAFYMPVTIMTILYWRIYKETEKRTKELAGLQASGTEAETENFVHPTGSSRSCSSYELQQQSMKRSNRRKYGRCHFWFTTKSWKPSSEQMDQDHSSSDSWNNNDAAASLENSASSDEEDIGSETRAIYSIVLKLPGHSTILNSTKLPSSDNLQVPEEELGMVDLERKADKLQAQKSVDDGGSFPKSFSKLPIQLESAVDTAKTSDVNSSVGKSTATLPLSFKEATLAKRFALKTRSQITKRKRMSLVKEKKAAQTLSAILLAFIITWTPYNIMVLVNTFCDSCIPKTFWNLGYWLCYINSTVNPVCYALCNKTFRTTFKMLLLCQCDKKKRRKQQYQQRQSVIFHKRAPEQAL	Successful	"DrugBank: a knowledgebase for drugs, drug actions and drug targets. Nucleic Acids Res. 2008 Jan;36(Database issue):D901-6."	34	.	.	.	.	.	.	.	.	.	.	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	R-HSA-390648:Muscarinic acetylcholine receptors; R-HSA-399997:Acetylcholine regulates insulin secretion; R-HSA-416476:G alpha (q) signalling events	.	P20309
TTQ3JTF	Muscarinic acetylcholine receptor M4 (CHRM4)	P08173	ACM4_HUMAN	GPCR rhodopsin	M4 receptor; CHRM4	CHRM4	"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."	.	6D9H; 5DSG	MANFTPVNGSSGNQSVRLVTSSSHNRYETVEMVFIATVTGSLSLVTVVGNILVMLSIKVNRQLQTVNNYFLFSLACADLIIGAFSMNLYTVYIIKGYWPLGAVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPARRTTKMAGLMIAAAWVLSFVLWAPAILFWQFVVGKRTVPDNQCFIQFLSNPAVTFGTAIAAFYLPVVIMTVLYIHISLASRSRVHKHRPEGPKEKKAKTLAFLKSPLMKQSVKKPPPGEAAREELRNGKLEEAPPPALPPPPRPVADKDTSNESSSGSATQNTKERPATELSTTEATTPAMPAPPLQPRALNPASRWSKIQIVTKQTGNECVTAIEIVPATPAGMRPAANVARKFASIARNQVRKKRQMAARERKVTRTIFAILLAFILTWTPYNVMVLVNTFCQSCIPDTVWSIGYWLCYVNSTINPACYALCNATFKKTFRHLLLCQYRNIGTAR	Successful	The muscarinic receptor antagonist tropicamide suppresses tremulous jaw movements in a rodent model of parkinsonian tremor: possible role of M4 rec... Psychopharmacology (Berl). 2007 Oct;194(3):347-59.	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04725:Cholinergic synapse; hsa04810:Regulation of actin cytoskeleton	R-HSA-390648:Muscarinic acetylcholine receptors; R-HSA-418594:G alpha (i) signalling events	.	P08173
TTH18TF	Muscarinic acetylcholine receptor M5 (CHRM5)	P08912	ACM5_HUMAN	GPCR rhodopsin	CHRM5	CHRM5	"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."	.	.	MEGDSYHNATTVNGTPVNHQPLERHRLWEVITIAAVTAVVSLITIVGNVLVMISFKVNSQLKTVNNYYLLSLACADLIIGIFSMNLYTTYILMGRWALGSLACDLWLALDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTPKRAGIMIGLAWLISFILWAPAILCWQYLVGKRTVPLDECQIQFLSEPTITFGTAIAAFYIPVSVMTILYCRIYRETEKRTKDLADLQGSDSVTKAEKRKPAHRALFRSCLRCPRPTLAQRERNQASWSSSRRSTSTTGKPSQATGPSANWAKAEQLTTCSSYPSSEDEDKPATDPVLQVVYKSQGKESPGEEFSAEETEETFVKAETEKSDYDTPNYLLSPAAAHRPKSQKCVAYKFRLVVKADGNQETNNGCHKVKIMPCPFPVAKEPSTKGLNPNPSHQMTKRKRVVLVKERKAAQTLSAILLAFIITWTPYNIMVLVSTFCDKCVPVTLWHLGYWLCYVNSTVNPICYALCNRTFRKTFKMLLLCRWKKKKVEEKLYWQGNSKLP	Successful	"Some neurochemical properties of pramiracetam (CI-879), a new cognition-enhancing agent. Article first published online: 5 OCT 2004."	34	.	.	.	.	.	.	.	.	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04725:Cholinergic synapse; hsa04810:Regulation of actin cytoskeleton	R-HSA-390648:Muscarinic acetylcholine receptors; R-HSA-416476:G alpha (q) signalling events	.	P08912
TT54JVQ	Neuronal acetylcholine receptor alpha-1 (CHRNA1)	P02708	ACHA_HUMAN	Neurotransmitter receptor	CHNRA; Acetylcholine receptor subunit alpha; ACHRA	CHRNA1	"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."	.	5HBT; 4ZJS; 1Y6C; 1Y5T; 1Y5P	MEPWPLLLLFSLCSAGLVLGSEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTVGLQLIQLINVDEVNQIVTTNVRLKQGDMVDLPRPSCVTLGVPLFSHLQNEQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLQYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKESRGWKHSVTYSCCPDTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHVMPNWVRKVFIDTIPNIMFFSTMKRPSREKQDKKIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGIKYIAETMKSDQESNNAAAEWKYVAMVMDHILLGVFMLVCIIGTLAVFAGRLIELNQQG	Successful	Potency of nondepolarizing muscle relaxants on muscle-type acetylcholine receptors in denervated mouse skeletal muscle.Acta Pharmacol Sin.2010 Dec;31(12):1541-6.	34	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction	R-HSA-629594: Highly calcium permeable postsynaptic nicotinic acetylcholine receptors; R-HSA-629597: Highly calcium permeable nicotinic acetylcholine receptors	.	P02708
TTJ49OM	Neuronal acetylcholine receptor alpha-10 (CHRNA10)	Q9GZZ6	ACH10_HUMAN	Neurotransmitter receptor	Nicotinic acetylcholine receptor subunit alpha 10; NACHR alpha 10; CHRNA10	CHRNA10	"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."	.	.	MGLRSHHLSLGLLLLFLLPAECLGAEGRLALKLFRDLFANYTSALRPVADTDQTLNVTLEVTLSQIIDMDERNQVLTLYLWIRQEWTDAYLRWDPNAYGGLDAIRIPSSLVWRPDIVLYNKADAQPPGSASTNVVLRHDGAVRWDAPAITRSSCRVDVAAFPFDAQHCGLTFGSWTHGGHQLDVRPRGAAASLADFVENVEWRVLGMPARRRVLTYGCCSEPYPDVTFTLLLRRRAAAYVCNLLLPCVLISLLAPLAFHLPADSGEKVSLGVTVLLALTVFQLLLAESMPPAESVPLIGKYYMATMTMVTFSTALTILIMNLHYCGPSVRPVPAWARALLLGHLARGLCVRERGEPCGQSRPPELSPSPQSPEGGAGPPAGPCHEPRCLCRQEALLHHVATIANTFRSHRAAQRCHEDWKRLARVMDRFFLAIFFSMALVMSLLVLVQAL	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	17	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-9667769: Acetylcholine inhibits contraction of outer hair cells	.	Q9GZZ6
TTF4E0J	Neuronal acetylcholine receptor alpha-2 (CHRNA2)	Q15822	ACHA2_HUMAN	Neurotransmitter receptor	CHRNA2	CHRNA2	"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."	.	5FJV	MGPSCPVFLSFTKLSLWWLLLTPAGGEEAKRPPPRAPGDPLSSPSPTALPQGGSHTETEDRLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSDCGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHTMPHWVRGALLGCVPRWLLMNRPPPPVELCHPLRLKLSPSYHWLESNVDAEEREVVVEEEDRWACAGHVAPSVGTLCSHGHLHSGASGPKAEALLQEGELLLSPHMQKALEGVHYIADHLRSEDADSSVKEDWKYVAMVIDRIFLWLFIIVCFLGTIGLFLPPFLAGMI	Successful	Synergy between pairs of competitive antagonists at adult human muscle acetylcholine receptors. Anesth Analg. 2008 Aug;107(2):525-33.	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-629594:Highly calcium permeable postsynaptic nicotinic acetylcholine receptors; R-HSA-629597:Highly calcium permeable nicotinic acetylcholine receptors	.	Q15822
TTMT0HG	Neuronal acetylcholine receptor alpha-2/alpha-3 (CHRNA2/A3)	Q15822-P32297	ACHA2_HUMAN; ACHA3_HUMAN	Neurotransmitter receptor	CHRNA; nAChR	CHRNA2-CHRNA3	"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."	.	.	MGPSCPVFLSFTKLSLWWLLLTPAGGEEAKRPPPRAPGDPLSSPSPTALPQGGSHTETEDRLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKLRWNPTDFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTYNSKKYDCCAEIYPDVTYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSDCGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHTMPHWVRGALLGCVPRWLLMNRPPPPVELCHPLRLKLSPSYHWLESNVDAEEREVVVEEEDRWACAGHVAPSVGTLCSHGHLHSGASGPKAEALLQEGELLLSPHMQKALEGVHYIADHLRSEDADSSVKEDWKYVAMVIDRIFLWLFIIVCFLGTIGLFLPPFLAGMI	Discontinued	Blockade and activation of the human neuronal nicotinic acetylcholine receptors by atracurium and laudanosine. Anesthesiology. 2001 Apr;94(4):643-51.	5	.	.	.	.	.	.	.	.	.	.	.	.	.	Q15822
TT35UGH	Neuronal acetylcholine receptor alpha-3/beta-4 (CHRNA3/B4)	P32297-P30926	ACHA3_HUMAN-ACHB4_HUMAN	Neurotransmitter receptor	Neuronal acetylcholine receptor	CHRNA3-CHRNB4	"A type of nicotinic acetylcholine receptor, consisting of 3 and 4 subunits."	.	.	MRRAPSLVLFFLVALCGRGNCRVANAEEKLMDDLLNKTRYNNLIRPATSSSQLISIKLQLSLAQLISVNEREQIMTTNVWLKQEWTDYRLTWNSSRYEGVNILRIPAKRIWLPDIVLYNNADGTYEVSVYTNLIVRSNGSVLWLPPAIYKSACKIEVKYFPFDQQNCTLKFRSWTYDHTEIDMVLMTPTASMDDFTPSGEWDIVALPGRRTVNPQDPSYVDVTYDFIIKRKPLFYTINLIIPCVLTTLLAILVFYLPSDCGEKMTLCISVLLALTFFLLLISKIVPPTSLDVPLIGKYLMFTMVLVTFSIVTSVCVLNVHHRSPSTHTMAPWVKRCFLHKLPTFLFMKRPGPDSSPARAFPPSKSCVTKPEATATSTSPSNFYGNSMYFVNPASAASKSPAGSTPVAIPRDFWLRSSGRFRQDVQEALEGVSFIAQHMKNDDEDQSVVEDWKYVAMVVDRLFLWVFMFVCVLGTVGLFLPPLFQTHAASEGPYAAQRDMGSGPLSLPLALSPPRLLLLLLLSLLPVARASEAEHRLFERLFEDYNEIIRPVANVSDPVIIHFEVSMSQLVKVDEVNQIMETNLWLKQIWNDYKLKWNPSDYGGAEFMRVPAQKIWKPDIVLYNNAVGDFQVDDKTKALLKYTGEVTWIPPAIFKSSCKIDVTYFPFDYQNCTMKFGSWSYDKAKIDLVLIGSSMNLKDYWESGEWAIIKAPGYKHDIKYNCCEEIYPDITYSLYIRRLPLFYTINLIIPCLLISFLTVLVFYLPSDCGEKVTLCISVLLSLTVFLLVITETIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHYRTPTTHTMPSWVKTVFLNLLPRVMFMTRPTSNEGNAQKPRPLYGAELSNLNCFSRAESKGCKEGYPCQDGMCGYCHHRRIKISNFSANLTRSSSSESVDAVLSLSALSPEIKEAIQSVKYIAENMKAQNEAKEIQDDWKYVAMVIDRIFLWVFTLVCILGTAGLFLQPLMAREDA	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	P32297
TT4H1MQ	Neuronal acetylcholine receptor alpha-4 (CHRNA4)	P43681	ACHA4_HUMAN	Neurotransmitter receptor	Nicotinic acetylcholine receptor alpha4; CHRNA4; Alpha-4 nAChR	CHRNA4	"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."	.	6CNK; 6CNJ; 5KXI; 2LLY; 2GVT	MELGGPGAPRLLPPLLLLLGTGLLRASSHVETRAHAEERLLKKLFSGYNKWSRPVANISDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPADYENVTSIRIPSELIWRPDIVLYNNADGDFAVTHLTKAHLFHDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMKFGSWTYDKAKIDLVNMHSRVDQLDFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPRTHTMPTWVRRVFLDIVPRLLLMKRPSVVKDNCRRLIESMHKMASAPRFWPEPEGEPPATSGTQSLHPPSPSFCVPLDVPAEPGPSCKSPSDQLPPQQPLEAEKASPHPSPGPCRPPHGTQAPGLAKARSLSVQHMSSPGEAVEGGVRCRSRSIQYCVPRDDAAPEADGQAAGALASRNTHSAELPPPDQPSPCKCTCKKEPSSVSPSATVKTRSTKAPPPHLPLSPALTRAVEGVQYIADHLKAEDTDFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPWLAGMI	Successful	Mechanism of long-lasting block of ganglion nicotinic receptors by mono-ammonium compounds with long aliphatic chain. J Auton Nerv Syst. 1994 Aug;48(3):231-40.	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04725:Cholinergic synapse; hsa05033:Nicotine addiction	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	.	P43681
TTL1ATN	Neuronal acetylcholine receptor alpha-4/beta-2 (CHRNA4/B2)	P43681-P17787	ACHA4_HUMAN; ACHB2_HUMAN	Neurotransmitter receptor	CHRN; nAChR	CHRNA4-CHRNB2	"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."	.	.	MELGGPGAPRLLPPLLLLLGTGLLRASSHVETRAHAEERLLKKLFSGYNKWSRPVANISDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPADYENVTSIRIPSELIWRPDIVLYNNADGDFAVTHLTKAHLFHDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMKFGSWTYDKAKIDLVNMHSRVDQLDFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPRTHTMPTWVRRVFLDIVPRLLLMKRPSVVKDNCRRLIESMHKMASAPRFWPEPEGEPPATSGTQSLHPPSPSFCVPLDVPAEPGPSCKSPSDQLPPQQPLEAEKASPHPSPGPCRPPHGTQAPGLAKARSLSVQHMSSPGEAVEGGVRCRSRSIQYCVPRDDAAPEADGQAAGALASRNTHSAELPPPDQPSPCKCTCKKEPSSVSPSATVKTRSTKAPPPHLPLSPALTRAVEGVQYIADHLKAEDTDFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPWLAGMI	Successful	2006 drug approvals: finding the niche. Nat Rev Drug Discov. 2007 Feb;6(2):99-101.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	P43681
TTH2QRX	Neuronal acetylcholine receptor alpha-5 (CHRNA5)	P30532	ACHA5_HUMAN	Neurotransmitter receptor	NACHRA5; CHRNA5	CHRNA5	"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."	.	.	MAARGSGPRALRLLLLVQLVAGRCGLAGAAGGAQRGLSEPSSIAKHEDSLLKDLFQDYERWVRPVEHLNDKIKIKFGLAISQLVDVDEKNQLMTTNVWLKQEWIDVKLRWNPDDYGGIKVIRVPSDSVWTPDIVLFDNADGRFEGTSTKTVIRYNGTVTWTPPANYKSSCTIDVTFFPFDLQNCSMKFGSWTYDGSQVDIILEDQDVDKRDFFDNGEWEIVSATGSKGNRTDSCCWYPYVTYSFVIKRLPLFYTLFLIIPCIGLSFLTVLVFYLPSNEGEKICLCTSVLVSLTVFLLVIEEIIPSSSKVIPLIGEYLVFTMIFVTLSIMVTVFAINIHHRSSSTHNAMAPLVRKIFLHTLPKLLCMRSHVDRYFTQKEETESGSGPKSSRNTLEAALDSIRYITRHIMKENDVREVVEDWKFIAQVLDRMFLWTFLFVSIVGSLGLFVPVIYKWANILIPVHIGNANK	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 466).	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction	R-HSA-629594:Highly calcium permeable postsynaptic nicotinic acetylcholine receptors; R-HSA-629597:Highly calcium permeable nicotinic acetylcholine receptors	.	P30532
TTLA931	Neuronal acetylcholine receptor alpha-7 (CHRNA7)	P36544	ACHA7_HUMAN	Neurotransmitter receptor	Nicotinic acetylcholine receptor subunit alpha 7; Nicotinic acetylcholine receptor alpha7; CHRNA7; Alpha7 nicotinic receptor; Alpha7 nAChR; Alpha-7 nAChR; Alpha(7) nicotinic receptor	CHRNA7	"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."	.	5AFN; 5AFM; 5AFL; 5AFK; 5AFJ	MRCSPGGVWLALAASLLHVSLQGEFQRKLYKELVKNYNPLERPVANDSQPLTVYFSLSLLQIMDVDEKNQVLTTNIWLQMSWTDHYLQWNVSEYPGVKTVRFPDGQIWKPDILLYNSADERFDATFHTNVLVNSSGHCQYLPPGIFKSSCYIDVRWFPFDVQHCKLKFGSWSYGGWSLDLQMQEADISGYIPNGEWDLVGIPGKRSERFYECCKEPYPDVTFTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKISLGITVLLSLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLQYHHHDPDGGKMPKWTRVILLNWCAWFLRMKRPGEDKVRPACQHKQRRCSLASVEMSAVAPPPASNGNLLYIGFRGLDGVHCVPTPDSGVVCGRMACSPTHDEHLLHGGQPPEGDPDLAKILEEVRYIANRFRCQDESEAVCSEWKFAACVVDRLCLMAFSVFTIICTIGILMSAPNFVEAVSKDFA	Successful	The pipeline and future of drug development in schizophrenia. Mol Psychiatry. 2007 Oct;12(10):904-22.	34	.	.	.	.	.	.	.	.	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04725:Cholinergic synapse; hsa05033:Nicotine addiction; hsa05204:Chemical carcinogenesis	R-HSA-629594:Highly calcium permeable postsynaptic nicotinic acetylcholine receptors	.	P36544
TTQACP9	Neuronal acetylcholine receptor alpha-9 (CHRNA9)	Q9UGM1	ACHA9_HUMAN	Neurotransmitter receptor	Nicotinic acetylcholine receptor subunit alpha 9; NACHR alpha 9; CHRNA9	CHRNA9	"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)."	.	6HY7; 4UY2; 4UXU; 4D01	MNWSHSCISFCWIYFAASRLRAAETADGKYAQKLFNDLFEDYSNALRPVEDTDKVLNVTLQITLSQIKDMDERNQILTAYLWIRQIWHDAYLTWDRDQYDGLDSIRIPSDLVWRPDIVLYNKADDESSEPVNTNVVLRYDGLITWDAPAITKSSCVVDVTYFPFDNQQCNLTFGSWTYNGNQVDIFNALDSGDLSDFIEDVEWEVHGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSSFYIVNLLIPCVLISFLAPLSFYLPAASGEKVSLGVTILLAMTVFQLMVAEIMPASENVPLIGKYYIATMALITASTALTIMVMNIHFCGAEARPVPHWARVVILKYMSRVLFVYDVGESCLSPHHSRERDHLTKVYSKLPESNLKAARNKDLSRKKDMNKRLKNDLGCQGKNPQEAESYCAQYKVLTRNIEYIAKCLKDHKATNSKGSEWKKVAKVIDRFFMWIFFIMVFVMTILIIARAD	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 469).	0	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-629594:Highly calcium permeable postsynaptic nicotinic acetylcholine receptors	.	Q9UGM1
TT5KPZR	Neuronal acetylcholine receptor beta-2 (CHRNB2)	P17787	ACHB2_HUMAN	Neurotransmitter receptor	Nicotinic acetylcholine receptor beta2; Nicotinic acetylcholine receptor beta 2-subunit protein; CHRNB2; Beta-2 nAChR; Alpha-4/beta-2 nicotinic receptor	CHRNB2	"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."	.	6CNK; 6CNJ; 5KXI; 2LM2; 2KSR	MARRCGPVALLLGFGLLRLCSGVWGTDTEERLVEHLLDPSRYNKLIRPATNGSELVTVQLMVSLAQLISVHEREQIMTTNVWLTQEWEDYRLTWKPEEFDNMKKVRLPSKHIWLPDVVLYNNADGMYEVSFYSNAVVSYDGSIFWLPPAIYKSACKIEVKHFPFDQQNCTMKFRSWTYDRTEIDLVLKSEVASLDDFTPSGEWDIVALPGRRNENPDDSTYVDITYDFIIRRKPLFYTINLIIPCVLITSLAILVFYLPSDCGEKMTLCISVLLALTVFLLLISKIVPPTSLDVPLVGKYLMFTMVLVTFSIVTSVCVLNVHHRSPTTHTMAPWVKVVFLEKLPALLFMQQPRHHCARQRLRLRRRQREREGAGALFFREAPGADSCTCFVNRASVQGLAGAFGAEPAPVAGPGRSGEPCGCGLREAVDGVRFIADHMRSEDDDQSVSEDWKYVAMVIDRLFLWIFVFVCVFGTIGMFLQPLFQNYTTTTFLHSDHSAPSSK	Clinical trial	Epibatidine isomers and analogues: structure-activity relationships. Bioorg Med Chem Lett. 2006 Nov 1;16(21):5493-7.	25	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04725:Cholinergic synapse; hsa05033:Nicotine addiction	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	.	P17787
TTTVAFQ	Neuronal acetylcholine receptor beta-4 (CHRNB4)	P30926	ACHB4_HUMAN	Neurotransmitter receptor	CHRNB4; Beta-4 nAChR	CHRNB4	"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."	.	2ASG	MRRAPSLVLFFLVALCGRGNCRVANAEEKLMDDLLNKTRYNNLIRPATSSSQLISIKLQLSLAQLISVNEREQIMTTNVWLKQEWTDYRLTWNSSRYEGVNILRIPAKRIWLPDIVLYNNADGTYEVSVYTNLIVRSNGSVLWLPPAIYKSACKIEVKYFPFDQQNCTLKFRSWTYDHTEIDMVLMTPTASMDDFTPSGEWDIVALPGRRTVNPQDPSYVDVTYDFIIKRKPLFYTINLIIPCVLTTLLAILVFYLPSDCGEKMTLCISVLLALTFFLLLISKIVPPTSLDVPLIGKYLMFTMVLVTFSIVTSVCVLNVHHRSPSTHTMAPWVKRCFLHKLPTFLFMKRPGPDSSPARAFPPSKSCVTKPEATATSTSPSNFYGNSMYFVNPASAASKSPAGSTPVAIPRDFWLRSSGRFRQDVQEALEGVSFIAQHMKNDDEDQSVVEDWKYVAMVVDRLFLWVFMFVCVLGTVGLFLPPLFQTHAASEGPYAAQRD	Clinical trial	"Deconstructing cytisine: The syntheses of (+/-)-cyfusine and (+/-)-cyclopropylcyfusine, fused ring analogs of cytisine. Bioorg Med Chem Lett. 2008 Apr 1;18(7):2316-9."	25	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04725:Cholinergic synapse	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	.	P30926
TTFK7E1	Carbohydrate sulfotransferase 15 (CHST15)	Q7LFX5	CHSTF_HUMAN	.	hBRAG; N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase; KIAA0598; GalNAc4S-6ST; GALNAC4S6ST; BRAG; B-cell RAG-associated gene protein	CHST15	"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."	EC 2.8.2.33	.	MRHCINCCIQLLPDGAHKQQVNCQGGPHHGHQACPTCKGENKILFRVDSKQMNLLAVLEVRTEGNENWGGFLRFKKGKRCSLVFGLIIMTLVMASYILSGAHQELLISSPFHYGGFPSNPSLMDSENPSDTKEHHHQSSVNNISYMKDYPSIKLIINSITTRIEFTTRQLPDLEDLKKQELHMFSVIPNKFLPNSKSPCWYEEFSGQNTTDPYLTNSYVLYSKRFRSTFDALRKAFWGHLAHAHGKHFRLRCLPHFYIIGQPKCGTTDLYDRLRLHPEVKFSAIKEPHWWTRKRFGIVRLRDGLRDRYPVEDYLDLFDLAAHQIHQGLQASSAKEQSKMNTIIIGEASASTMWDNNAWTFFYDNSTDGEPPFLTQDFIHAFQPNARLIVMLRDPVERLYSDYLYFASSNKSADDFHEKVTEALQLFENCMLDYSLRACVYNNTLNNAMPVRLQVGLYAVYLLDWLSVFDKQQFLILRLEDHASNVKYTMHKVFQFLNLGPLSEKQEALMTKSPASNARRPEDRNLGPMWPITQKILRDFYRPFNARLAQVLADEAFAWKTT	Literature-reported	Inhibition of Cell Proliferation and Growth of Pancreatic Cancer by Silencing of Carbohydrate Sulfotransferase 15 In Vitro and in a Xenograft Model. PLoS One. 2015 Dec 7;10(12):e0142981.	.	.	.	.	.	.	.	.	.	.	.	hsa00532: Glycosaminoglycan biosynthesis - chondroitin sulfate / dermatan sulfate	R-HSA-2022870: Chondroitin sulfate biosynthesis	MetaCyc:HS11694-MON	Q7LFX5
TTP4ICS	Intestinal GlcNAc-6-sulfotransferase (CHST5)	Q9GZS9	CHST5_HUMAN	Transferases of sulfur-containing groups	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	CHST5	"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."	EC 2.8.2.-	.	MGMRARVPKVAHSTRRPPAARMWLPRFSSKTVTVLLLAQTTCLLLFIISRPGPSSPAGGEDRVHVLVLSSWRSGSSFLGQLFSQHPDVFYLMEPAWHVWTTLSQGSAATLHMAVRDLMRSIFLCDMDVFDAYMPQSRNLSAFFNWATSRALCSPPACSAFPRGTISKQDVCKTLCTRQPFSLAREACRSYSHVVLKEVRFFNLQVLYPLLSDPALNLRIVHLVRDPRAVLRSREAAGPILARDNGIVLGTNGKWVEADPHLRLIREVCRSHVRIAEAATLKPPPFLRGRYRLVRFEDLAREPLAEIRALYAFTGLTLTPQLEAWIHNITHGSGIGKPIEAFHTSSRNARNVSQAWRHALPFTKILRVQEVCAGALQLLGYRPVYSADQQRDLTLDLVLPRGPDHFSWASPD	Literature-reported	"Carbohydrate sulfotransferases: novel therapeutic targets for inflammation, viral infection and cancer. Drug Discov Today. 2001 Jan 1;6(1):27-35."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2022854: Keratan sulfate biosynthesis	.	Q9GZS9
TT1F8OQ	IKKA messenger RNA (IKKA mRNA)	O15111	IKKA_HUMAN	mRNA target	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)	CHUK	"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."	EC 2.7.11.10	5TQY; 5TQX; 5TQW; 5EBZ; 3BRT	MERPPGLRPGAGGPWEMRERLGTGGFGNVCLYQHRELDLKIAIKSCRLELSTKNRERWCHEIQIMKKLNHANVVKACDVPEELNILIHDVPLLAMEYCSGGDLRKLLNKPENCCGLKESQILSLLSDIGSGIRYLHENKIIHRDLKPENIVLQDVGGKIIHKIIDLGYAKDVDQGSLCTSFVGTLQYLAPELFENKPYTATVDYWSFGTMVFECIAGYRPFLHHLQPFTWHEKIKKKDPKCIFACEEMSGEVRFSSHLPQPNSLCSLVVEPMENWLQLMLNWDPQQRGGPVDLTLKQPRCFVLMDHILNLKIVHILNMTSAKIISFLLPPDESLHSLQSRIERETGINTGSQELLSETGISLDPRKPASQCVLDGVRGCDSYMVYLFDKSKTVYEGPFASRSLSDCVNYIVQDSKIQLPIIQLRKVWAEAVHYVSGLKEDYSRLFQGQRAAMLSLLRYNANLTKMKNTLISASQQLKAKLEFFHKSIQLDLERYSEQMTYGISSEKMLKAWKEMEEKAIHYAEVGVIGYLEDQIMSLHAEIMELQKSPYGRRQGDLMESLEQRAIDLYKQLKHRPSDHSYSDSTEMVKIIVHTVQSQDRVLKELFGHLSKLLGCKQKIIDLLPKVEVALSNIKEADNTVMFMQGKRQKEIWHLLKIACTQSSARSLVGSSLEGAVTPQTSAWLPPTSAEHDHSLSCVVTPQDGETSAQMIEENLNCLGHLSTIIHEANEEQGNSMMNLDWSWLTE	Literature-reported	"US patent application no. 6,395,545, Antisense modulation of inhibitor-kappa B kinase-alpha expression."	0	mRNA	mRNA target	.	.	.	IQBAL scaffold dimerization domain; I-kappa-kinase-beta NEMO binding domain; Protein kinase domain	PF18397; PF12179; PF00069	PF18397; IKBKB_SDD; PF12179; IKKbetaNEMObind; PF00069; Pkinase	.	.	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	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	.	O15111
TTWLVKG	Inhibitor of nuclear factor kappa-B kinase alpha (IKKA)	O15111	IKKA_HUMAN	Kinase	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	CHUK	"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."	EC 2.7.11.10	5TQY; 5TQX; 5TQW; 5EBZ; 3BRT	MERPPGLRPGAGGPWEMRERLGTGGFGNVCLYQHRELDLKIAIKSCRLELSTKNRERWCHEIQIMKKLNHANVVKACDVPEELNILIHDVPLLAMEYCSGGDLRKLLNKPENCCGLKESQILSLLSDIGSGIRYLHENKIIHRDLKPENIVLQDVGGKIIHKIIDLGYAKDVDQGSLCTSFVGTLQYLAPELFENKPYTATVDYWSFGTMVFECIAGYRPFLHHLQPFTWHEKIKKKDPKCIFACEEMSGEVRFSSHLPQPNSLCSLVVEPMENWLQLMLNWDPQQRGGPVDLTLKQPRCFVLMDHILNLKIVHILNMTSAKIISFLLPPDESLHSLQSRIERETGINTGSQELLSETGISLDPRKPASQCVLDGVRGCDSYMVYLFDKSKTVYEGPFASRSLSDCVNYIVQDSKIQLPIIQLRKVWAEAVHYVSGLKEDYSRLFQGQRAAMLSLLRYNANLTKMKNTLISASQQLKAKLEFFHKSIQLDLERYSEQMTYGISSEKMLKAWKEMEEKAIHYAEVGVIGYLEDQIMSLHAEIMELQKSPYGRRQGDLMESLEQRAIDLYKQLKHRPSDHSYSDSTEMVKIIVHTVQSQDRVLKELFGHLSKLLGCKQKIIDLLPKVEVALSNIKEADNTVMFMQGKRQKEIWHLLKIACTQSSARSLVGSSLEGAVTPQTSAWLPPTSAEHDHSLSCVVTPQDGETSAQMIEENLNCLGHLSTIIHEANEEQGNSMMNLDWSWLTE	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1989).	0	EC:2.7	Kinase	protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily.	2.7.11.10	Transferring phosphorus-containing groups	IQBAL scaffold dimerization domain; I-kappa-kinase-beta NEMO binding domain; Protein kinase domain	PF18397; PF12179; PF00069	PF18397; IKBKB_SDD; PF12179; IKKbetaNEMObind; PF00069; Pkinase	.	.	hsa01523: Antifolate resistance; 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; hsa04625: C-type lectin receptor signaling pathway; hsa04657: IL-17 signaling pathway; hsa04658: Th1 and Th2 cell differentiation; hsa04659: Th17 cell differentiation; hsa04660: T cell receptor signaling pathway; hsa04662: B cell receptor signaling pathway; hsa04668: TNF signaling pathway; hsa04920: Adipocytokine signaling pathway; hsa04936: Alcoholic liver disease; hsa05010: Alzheimer disease; hsa05120: Epithelial cell signaling in Helicobacter pylori infection; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05135: Yersinia infection; hsa05142: Chagas disease; hsa05145: Toxoplasmosis; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05162: Measles; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; hsa05165: Human papillomavirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05212: Pancreatic cancer; hsa05215: Prostate cancer; hsa05220: Chronic myeloid leukemia; hsa05221: Acute myeloid leukemia; hsa05222: Small cell lung cancer; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer; hsa05417: Lipid and atherosclerosis; hsa05418: Fluid shear stress and atherosclerosis	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	.	O15111
TT3BKTU	Citron Rho-interacting kinase (CIT)	O14578	CTRO_HUMAN	.	Serine/threonine-protein kinase 21; STK21; KIAA0949; CRIK	CIT	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.	EC 2.7.11.1	.	MLKFKYGARNPLDAGAAEPIASRASRLNLFFQGKPPFMTQQQMSPLSREGILDALFVLFEECSQPALMKIKHVSNFVRKYSDTIAELQELQPSAKDFEVRSLVGCGHFAEVQVVREKATGDIYAMKVMKKKALLAQEQVSFFEEERNILSRSTSPWIPQLQYAFQDKNHLYLVMEYQPGGDLLSLLNRYEDQLDENLIQFYLAELILAVHSVHLMGYVHRDIKPENILVDRTGHIKLVDFGSAAKMNSNKMVNAKLPIGTPDYMAPEVLTVMNGDGKGTYGLDCDWWSVGVIAYEMIYGRSPFAEGTSARTFNNIMNFQRFLKFPDDPKVSSDFLDLIQSLLCGQKERLKFEGLCCHPFFSKIDWNNIRNSPPPFVPTLKSDDDTSNFDEPEKNSWVSSSPCQLSPSGFSGEELPFVGFSYSKALGILGRSESVVSGLDSPAKTSSMEKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVSEVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLHDIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFKRKATECQHKLLKAKDQGKPEVGEYAKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQNIRQAKERAERELEKLQNREDSSEGIRKKLVEAEELEEKHREAQVSAQHLEVHLKQKEQHYEEKIKVLDNQIKKDLADKETLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQRIVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKISHQDHSDKNRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAALESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDNAELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCTMLEEQVMDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQRITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQKLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLENIQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNELKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPATARQQIAMSAIVRSPEHQPSAMSLLAPPSSRRKESSTPEEFSRRLKERMHHNIPHRFNVGLNMRATKCAVCLDTVHFGRQASKCLECQVMCHPKCSTCLPATCGLPAEYATHFTEAFCRDKMNSPGLQTKEPSSSLHLEGWMKVPRNNKRGQQGWDRKYIVLEGSKVLIYDNEAREAGQRPVEEFELCLPDGDVSIHGAVGASELANTAKADVPYILKMESHPHTTCWPGRTLYLLAPSFPDKQRWVTALESVVAGGRVSREKAEADAKLLGNSLLKLEGDDRLDMNCTLPFSDQVVLVGTEEGLYALNVLKNSLTHVPGIGAVFQIYIIKDLEKLLMIAGEERALCLVDVKKVKQSLAQSHLPAQPDISPNIFEAVKGCHLFGAGKIENGLCICAAMPSKVVILRYNENLSKYCIRKEIETSEPCSCIHFTNYSILIGTNKFYEIDMKQYTLEEFLDKNDHSLAPAVFAASSNSFPVSIVQVNSAGQREEYLLCFHEFGVFVDSYGRRSRTDDLKWSRLPLAFAYREPYLFVTHFNSLEVIEIQARSSAGTPARAYLDIPNPRYLGPAISSGAIYLASSYQDKLRVICCKGNLVKESGTEHHRGPSTSRSSPNKRGPPTYNEHITKRVASSPAPPEGPSHPREPSTPHRYREGRTELRRDKSPGRPLEREKSPGRMLSTRRERSPGRLFEDSSRGRLPAGAVRTPLSQVNKVWDQSSV	Literature-reported	Role of citron kinase as a target of the small GTPase Rho in cytokinesis. Nature. 1998 Jul 30;394(6692):491-4.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-5625900: RHO GTPases activate CIT; R-HSA-8980692: RHOA GTPase cycle; R-HSA-9013026: RHOB GTPase cycle; R-HSA-9013106: RHOC GTPase cycle; R-HSA-9013149: RAC1 GTPase cycle	.	O14578
TT9INHD	Creatine kinase (CK)	P12277; P17540; P12532; P06732	KCRB_HUMAN; KCRS_HUMAN; KCRU_HUMAN; KCRM_HUMAN	Kinase	Creatine kinase	CKB	"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."	.	.	MPFSNSHNALKLRFPAEDEFPDLSAHNNHMAKVLTPELYAELRAKSTPSGFTLDDVIQTGVDNPGHPYIMTVGCVAGDEESYEVFKDLFDPIIEDRHGGYKPSDEHKTDLNPDNLQGGDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLAGRYYALKSMTEAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISMQKGGNMKEVFTRFCTGLTQIETLFKSKDYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPNLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEMEQRLEQGQAIDDLMPAQK	Literature-reported	Creatine kinase inhibitor iodoacetamide antagonizes calcium-stimulated inotropy in cardiomyocytes. Clin Exp Pharmacol Physiol. 2009 Feb;36(2):141-5.	0	.	.	.	.	.	.	.	.	.	.	hsa00330: Arginine and proline metabolism; hsa01100: Metabolic pathways	R-HSA-71288: Creatine metabolism; R-HSA-9696264: RND3 GTPase cycle	MetaCyc:HS09344-MON	P12277
TT3AF4R	Calcium-activated chloride channel protein 1 (CaCC-1)	A8K7I4	CLCA1_HUMAN	Voltage-gated ion channel	hCaCC-1; hCLCA1; Calcium-activated chloride channel regulator 1; Calcium-activated chloride channel family member 1; CaCC-1; CACC1	CLCA1	"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."	EC 3.4.-.-	.	MGPFKSSVFILILHLLEGALSNSLIQLNNNGYEGIVVAIDPNVPEDETLIQQIKDMVTQASLYLLEATGKRFYFKNVAILIPETWKTKADYVRPKLETYKNADVLVAESTPPGNDEPYTEQMGNCGEKGERIHLTPDFIAGKKLAEYGPQGRAFVHEWAHLRWGVFDEYNNDEKFYLSNGRIQAVRCSAGITGTNVVKKCQGGSCYTKRCTFNKVTGLYEKGCEFVLQSRQTEKASIMFAQHVDSIVEFCTEQNHNKEAPNKQNQKCNLRSTWEVIRDSEDFKKTTPMTTQPPNPTFSLLQIGQRIVCLVLDKSGSMATGNRLNRLNQAGQLFLLQTVELGSWVGMVTFDSAAHVQNELIQINSGSDRDTLAKRLPAAASGGTSICSGLRSAFTVIRKKYPTDGSEIVLLTDGEDNTISGCFNEVKQSGAIIHTVALGPSAAQELEELSKMTGGLQTYASDQVQNNGLIDAFGALSSGNGAVSQRSIQLESKGLTLQNSQWMNGTVIVDSTVGKDTLFLITWTMQPPQILLWDPSGQKQGGFVVDKNTKMAYLQIPGIAKVGTWKYSLQASSQTLTLTVTSRASNATLPPITVTSKTNKDTSKFPSPLVVYANIRQGASPILRASVTALIESVNGKTVTLELLDNGAGADATKDDGVYSRYFTTYDTNGRYSVKVRALGGVNAARRRVIPQQSGALYIPGWIENDEIQWNPPRPEINKDDVQHKQVCFSRTSSGGSFVASDVPNAPIPDLFPPGQITDLKAEIHGGSLINLTWTAPGDDYDHGTAHKYIIRISTSILDLRDKFNESLQVNTTALIPKEANSEEVFLFKPENITFENGTDLFIAIQAVDKVDLKSEISNIARVSLFIPPQTPPETPSPDETSAPCPNIHINSTIPGIHILKIMWKWIGELQLSIA	Literature-reported	Association of the hCLCA1 gene with childhood and adult asthma. Genes Immun. 2004 Nov;5(7):540-7.	.	.	.	.	.	.	.	.	.	.	.	hsa04924: Renin secretion; hsa04972: Pancreatic secretion	R-HSA-2672351: Stimuli-sensing channels	.	A8K7I4
TTI6V13	Cardiotrophin-like cytokine factor 1 (CLCF1)	Q9UBD9	CLCF1_HUMAN	.	Novel neurotrophin1; NNT1; CLCF1; Bcellstimulating factor 3; BSF3	CLCF1	Cytokine with B-cell stimulating capability. Binds to and activates the ILST/gp130 receptor.	.	.	MDLRAGDSWGMLACLCTVLWHLPAVPALNRTGDPGPGPSIQKTYDLTRYLEHQLRSLAGTYLNYLGPPFNEPDFNPPRLGAETLPRATVDLEVWRSLNDKLRLTQNYEAYSHLLCYLRGLNRQAATAELRRSLAHFCTSLQGLLGSIAGVMAALGYPLPQPLPGTEPTWTPGPAHSDFLQKMDDFWLLKELQTWLWRSAKDFNRLKKKMQPPAAAVTLHLGAHGF	Literature-reported	"Cardiotrophin-like cytokine factor 1 (CLCF1) and neuropoietin (NP) signalling and their roles in development, adulthood, cancer and degenerative di... Cytokine Growth Factor Rev. 2015 Oct;26(5):517-22."	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction	R-HSA-6788467: IL-6-type cytokine receptor ligand interactions	.	Q9UBD9
TTUYAF3	Chloride channel protein 1 (ClC-1)	P35523	CLCN1_HUMAN	Chloride channel	"ClC-1; Chloride channel protein, skeletal muscle; CLC1"	CLCN1	Voltage-gated chloride channel. Plays an important role in membrane repolarization in skeletal muscle cells after muscle contraction.	.	6QVU; 6QVD; 6QVC; 6QVB; 6QV6	MEQSRSQQRGGEQSWWGSDPQYQYMPFEHCTSYGLPSENGGLQHRLRKDAGPRHNVHPTQIYGHHKEQFSDREQDIGMPKKTGSSSTVDSKDEDHYSKCQDCIHRLGQVVRRKLGEDGIFLVLLGLLMALVSWSMDYVSAKSLQAYKWSYAQMQPSLPLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMKTILRGVVLKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSVFCGVYEQPYYYSDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDAVTITALFRTNFRMDFPFDLKELPAFAAIGICCGLLGAVFVYLHRQVMLGVRKHKALSQFLAKHRLLYPGIVTFVIASFTFPPGMGQFMAGELMPREAISTLFDNNTWVKHAGDPESLGQSAVWIHPRVNVVIIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGILFDDIIYKILPGGYAVIGAAALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLYDSIIQVKKLPYLPDLGWNQLSKYTIFVEDIMVRDVKFVSASYTYGELRTLLQTTTVKTLPLVDSKDSMILLGSVERSELQALLQRHLCPERRLRAAQEMARKLSELPYDGKARLAGEGLPGAPPGRPESFAFVDEDEDEDLSGKSELPPSLALHPSTTAPLSPEEPNGPLPGHKQQPEAPEPAGQRPSIFQSLLHCLLGRARPTKKKTTQDSTDLVDNMSPEEIEAWEQEQLSQPVCFDSCCIDQSPFQLVEQTTLHKTHTLFSLLGLHLAYVTSMGKLRGVLALEELQKAIEGHTKSGVQLRPPLASFRNTTSTRKSTGAPPSSAENWNLPEDRPGATGTGDVIAASPETPVPSPSPEPPLSLAPGKVEGELEELELVESPGLEEELADILQGPSLRSTDEEDEDELIL	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 698).	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2672351: Stimuli-sensing channels	.	P35523
TT30NW6	Chloride channel protein 2 (CLC-2)	P51788	CLCN2_HUMAN	Chloride channel	ClC-2 chloride channel; ClC-2 Cl- channel; ClC-2; CLCN2	CLCN2	"Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport."	.	.	MAAAAAEEGMEPRALQYEQTLMYGRYTQDLGAFAKEEAARIRLGGPEPWKGPPSSRAAPELLEYGRSRCARCRVCSVRCHKFLVSRVGEDWIFLVLLGLLMALVSWVMDYAIAACLQAQQWMSRGLNTSILLQYLAWVTYPVVLITFSAGFTQILAPQAVGSGIPEMKTILRGVVLKEYLTLKTFIAKVIGLTCALGSGMPLGKEGPFVHIASMCAALLSKFLSLFGGIYENESRNTEMLAAACAVGVGCCFAAPIGGVLFSIEVTSTFFAVRNYWRGFFAATFSAFIFRVLAVWNRDEETITALFKTRFRLDFPFDLQELPAFAVIGIASGFGGALFVYLNRKIVQVMRKQKTINRFLMRKRLLFPALVTLLISTLTFPPGFGQFMAGQLSQKETLVTLFDNRTWVRQGLVEELEPPSTSQAWNPPRANVFLTLVIFILMKFWMSALATTIPVPCGAFMPVFVIGAAFGRLVGESMAAWFPDGIHTDSSTYRIVPGGYAVVGAAALAGAVTHTVSTAVIVFELTGQIAHILPVMIAVILANAVAQSLQPSLYDSIIRIKKLPYLPELGWGRHQQYRVRVEDIMVRDVPHVALSCTFRDLRLALHRTKGRMLALVESPESMILLGSIERSQVVALLGAQLSPARRRQHMQERRATQTSPLSDQEGPPTPEASVCFQVNTEDSAFPAARGETHKPLKPALKRGPSVTRNLGESPTGSAESAGIALRSLFCGSPPPEAASEKLESCEKRKLKRVRISLASDADLEGEMSPEEILEWEEQQLDEPVNFSDCKIDPAPFQLVERTSLHKTHTIFSLLGVDHAYVTSIGRLIGIVTLKELRKAIEGSVTAQGVKVRPPLASFRDSATSSSDTETTEVHALWGPHSRHGLPREGSPSDSDDKCQ	Successful	"Lubiprostone stimulates secretion from tracheal submucosal glands of sheep, pigs, and humans. Am J Physiol Lung Cell Mol Physiol. 2009 May;296(5):L811-24."	34	.	.	.	.	.	.	.	.	.	.	hsa04978:Mineral absorption	R-HSA-2672351:Stimuli-sensing channels	.	P51788
TT8XNZ7	Chloride channel protein 3 (CLC-3)	P51790	CLCN3_HUMAN	Chloride channel	H(+)/Cl(-) exchange transporter 3; ClC-3	CLCN3	"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."	.	.	MESEQLFHRGYYRNSYNSITSASSDEELLDGAGVIMDFQTSEDDNLLDGDTAVGTHYTMTNGGSINSSTHLLDLLDEPIPGVGTYDDFHTIDWVREKCKDRERHRRINSKKKESAWEMTKSLYDAWSGWLVVTLTGLASGALAGLIDIAADWMTDLKEGICLSALWYNHEQCCWGSNETTFEERDKCPQWKTWAELIIGQAEGPGSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELFTDCGPLESSSLCDYRNDMNASKIVDDIPDRPAGIGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLAYYHHDWFIFKEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIRLNGYPFLDAKEEFTHTTLAADVMRPRRNDPPLAVLTQDNMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESARKKQEGIVGSSRVCFAQHTPSLPAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRHMAQTANQDPASIMFN	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 702).	0	.	.	chloride channel (TC 2.A.49) family. ClC-3/CLCN3 subfamily. 	.	.	CBS domain; Voltage gated chloride channel	PF00571; PF00654	PF00571; CBS; PF00654; Voltage_CLC	.	.	hsa04613: Neutrophil extracellular trap formation	R-HSA-2672351: Stimuli-sensing channels	.	P51790
TTCJRDO	Chloride channel protein 6 (ClC-6)	P51797	CLCN6_HUMAN	Chloride channel	KIAA0046; ClC-6; Chloride transport protein 6	CLCN6	"Chloride transport protein, initially identified as voltage-gated chloride channel. The presence of the conserved gating glutamate residues suggests that is functions as antiporter."	.	.	MAGCRGSLCCCCRWCCCCGERETRTPEELTILGETQEEEDEILPRKDYESLDYDRCINDPYLEVLETMDNKKGRRYEAVKWMVVFAIGVCTGLVGLFVDFFVRLFTQLKFGVVQTSVEECSQKGCLALSLLELLGFNLTFVFLASLLVLIEPVAAGSGIPEVKCYLNGVKVPGIVRLRTLLCKVLGVLFSVAGGLFVEKEGPMIHSGSVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFRSGIQFGSWGSFQLPGLLNFGEFKCSDSDKKCHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVHPKPKLVRVLESLLVSLVTTVVVFVASMVLGECRQMSSSSQIGNDSFQLQVTEDVNSSIKTFFCPNDTYNDMATLFFNPQESAILQLFHQDGTFSPVTLALFFVLYFLLACWTYGISVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHIYSGTFALIGAAAFLGGVVRMTISLTVILIESTNEITYGLPIMVTLMVAKWTGDFFNKGIYDIHVGLRGVPLLEWETEVEMDKLRASDIMEPNLTYVYPHTRIQSLVSILRTTVHHAFPVVTENRGNEKEFMKGNQLISNNIKFKKSSILTRAGEQRKRSQSMKSYPSSELRNMCDEHIASEEPAEKEDLLQQMLERRYTPYPNLYPDQSPSEDWTMEERFRPLTFHGLILRSQLVTLLVRGVCYSESQSSASQPRLSYAEMAEDYPRYPDIHDLDLTLLNPRMIVDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTYEFLQARLRQHYQTI	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 705).	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2672351: Stimuli-sensing channels; R-HSA-6802952: Signaling by BRAF and RAF1 fusions	.	P51797
TTST1AJ	Chloride channel protein 7 (ClC-7)	P51798	CLCN7_HUMAN	Chloride channel	H(+)/Cl(-) exchange transporter 7; ClC-7; Chloride channel 7 alpha subunit	CLCN7	Slowly voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the lysosome lumen.	.	.	MANVSKKVSWSGRDRDDEEAAPLLRRTARPGGGTPLLNGAGPGAARQSPRSALFRVGHMSSVELDDELLDPDMDPPHPFPKEIPHNEKLLSLKYESLDYDNSENQLFLEEERRINHTAFRTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIKGNIDKFTEKGGLSFSLLLWATLNAAFVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMISTFTLNFVLSIYHGNMWDLSSPGLINFGRFDSEKMAYTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHRPCLQVIEAVLVAAVTATVAFVLIYSSRDCQPLQGGSMSYPLQLFCADGEYNSMAAAFFNTPEKSVVSLFHDPPGSYNPLTLGLFTLVYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLFGISLSYLTGAAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKIVGDVFIEGLYDMHIQLQSVPFLHWEAPVTSHSLTAREVMSTPVTCLRRREKVGVIVDVLSDTASNHNGFPVVEHADDTQPARLQGLILRSQLIVLLKHKVFVERSNLGLVQRRLRLKDFRDAYPRFPPIQSIHVSQDERECTMDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARYRLGKRGLEELSLAQT	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 709).	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2672351: Stimuli-sensing channels	.	P51798
TT823N1	Chloride channel protein ClC-Ka (ClC-K1)	P51800	CLCKA_HUMAN	Chloride channel	ClC-K1; Chloride channel Ka	CLCNKA	"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."	.	2PFI	MEELVGLREGFSGDPVTLQELWGPCPHIRRAIQGGLEWLKQKVFRLGEDWYFLMTLGVLMALVSYAMNFAIGCVVRAHQWLYREIGDSHLLRYLSWTVYPVALVSFSSGFSQSITPSSGGSGIPELKTMLAGVILEDYLDIKNFGAKVVGLSCTLATGSTLFLGKVGPFVHLSVMIAAYLGRVRTTTIGEPENKSKQNEMLVAAAAVGVATVFAAPFSGVLFSIEVMSSHFSVRDYWRGFFAATCGAFIFRLLAVFNSEQETITSLYKTSFRVDVPFDLPEIFFFVALGGICGVLSCAYLFCQRTFLSFIKTNRYSSKLLATSKPVYSALATLLLASITYPPGVGHFLASRLSMKQHLDSLFDNHSWALMTQNSSPPWPEELDPQHLWWEWYHPRFTIFGTLAFFLVMKFWMLILATTIPMPAGYFMPIFILGAAIGRLLGEALAVAFPEGIVTGGVTNPIMPGGYALAGAAAFSGAVTHTISTALLAFELTGQIVHALPVLMAVLAANAIAQSCQPSFYDGTIIVKKLPYLPRILGRNIGSHHVRVEHFMNHSITTLAKDTPLEEVVKVVTSTDVTEYPLVESTESQILVGIVQRAQLVQALQAEPPSRAPGHQQCLQDILARGCPTEPVTLTLFSETTLHQAQNLFKLLNLQSLFVTSRGRAVGCVSWVEMKKAISNLTNPPAPK	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 700).	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2672351: Stimuli-sensing channels	.	P51800
TTR68GQ	Chloride channel protein ClC-Kb (ClC-K2)	P51801	CLCKB_HUMAN	Chloride channel	ClC-K2; Chloride channel Kb	CLCNKB	"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."	.	.	MEEFVGLREGSSGNPVTLQELWGPCPRIRRGIRGGLEWLKQKLFRLGEDWYFLMTLGVLMALVSCAMDLAVESVVRAHQWLYREIGDSHLLRYLSWTVYPVALVSFSSGFSQSITPSSGGSGIPEVKTMLAGVVLEDYLDIKNFGAKVVGLSCTLACGSTLFLGKVGPFVHLSVMMAAYLGRVRTTTIGEPENKSKQNEMLVAAAAVGVATVFAAPFSGVLFSIEVMSSHFSVWDYWRGFFAATCGAFMFRLLAVFNSEQETITSLYKTSFRVDVPFDLPEIFFFVALGGLCGILGSAYLFCQRIFFGFIRNNRFSSKLLATSKPVYSALATLVLASITYPPSAGRFLASRLSMKQHLDSLFDNHSWALMTQNSSPPWPEELDPQHLWWEWYHPRFTIFGTLAFFLVMKFWMLILATTIPMPAGYFMPIFVYGAAIGRLFGETLSFIFPEGIVAGGITNPIMPGGYALAGAAAFSGAVTHTISTALLAFEVTGQIVHALPVLMAVLAANAIAQSCQPSFYDGTVIVKKLPYLPRILGRNIGSHRVRVEHFMNHSITTLAKDMPLEEVVKVVTSTDVAKYPLVESTESQILVGIVRRAQLVQALKAEPPSWAPGHQQCLQDILAAGCPTEPVTLKLSPETSLHEAHNLFELLNLHSLFVTSRGRAVGCVSWVEMKKAISNLTNPPAPK	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 701).	0	.	.	.	.	.	.	.	.	.	.	hsa04966: Collecting duct acid secretion	R-HSA-2672351: Stimuli-sensing channels	.	P51801
TT6PKBX	Claudin-18 (CLDN18)	P56856	CLD18_HUMAN	.	UNQ778/PRO1572; Claudin18	CLDN18	"Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity."	.	.	MSTTTCQVVAFLLSILGLAGCIAATGMDMWSTQDLYDNPVTSVFQYEGLWRSCVRQSSGFTECRPYFTILGLPAMLQAVRALMIVGIVLGAIGLLVSIFALKCIRIGSMEDSAKANMTLTSGIMFIVSGLCAIAGVSVFANMLVTNFWMSTANMYTGMGGMVQTVQTRYTFGAALFVGWVAGGLTLIGGVMMCIACRGLAPEETNYKAVSYHASGHSVAYKPGGFKASTGFGSNTKNKKIYDGGARTEDEVQSYPSKHDYV	Clinical trial	Claudin 18.2 is a target for IMAB362 antibody in pancreatic neoplasms. Int J Cancer. 2014 Feb 1;134(3):731-9.	25	.	.	claudin family.	.	.	PMP-22/EMP/MP20/Claudin family	PF00822	PF00822; PMP22_Claudin	.	.	hsa04514:Cell adhesion molecules (CAMs); hsa04530:Tight junction; hsa04670:Leukocyte transendothelial migration; hsa05160:Hepatitis C	R-HSA-420029:Tight junction interactions	.	P56856
TTMTS9H	Claudin-4 (CLDN4)	O14493	CLD4_HUMAN	.	WilliamsBeuren syndrome chromosomal region 8 protein; Clostridium perfringens enterotoxin receptor; Claudin4; CPEreceptor; CPER; CLDN4	CLDN4	Plays a major role in tight junction-specific obliteration of the intercellularspace.	.	5B2G	MASMGLQVMGIALAVLGWLAVMLCCALPMWRVTAFIGSNIVTSQTIWEGLWMNCVVQSTGQMQCKVYDSLLALPQDLQAARALVIISIIVAALGVLLSVVGGKCTNCLEDESAKAKTMIVAGVVFLLAGLMVIVPVSWTAHNIIQDFYNPLVASGQKREMGASLYVGWAASGLLLLGGGLLCCNCPPRTDKPYSAKYSAARSAAASNYV	Literature-reported	Claudin-4: a new target for pancreatic cancer treatment using Clostridium perfringens enterotoxin. Gastroenterology. 2001 Sep;121(3):678-84.	.	.	.	.	.	.	.	.	.	.	.	hsa04514: Cell adhesion molecules; hsa04530: Tight junction; hsa04670: Leukocyte transendothelial migration; hsa05130: Pathogenic Escherichia coli infection; hsa05160: Hepatitis C	R-HSA-420029: Tight junction interactions	.	O14493
TTKSV48	Claudin-6 (CLDN6)	P56747	CLD6_HUMAN	.	Skullin	CLDN6	"Plays a major role in tight junction-specific obliteration of the intercellular space. {ECO:0000250}.; (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) entry into hepatic cells. {ECO:0000269|PubMed:17804490, ECO:0000269|PubMed:20375010}."	.	.	MASAGMQILGVVLTLLGWVNGLVSCALPMWKVTAFIGNSIVVAQVVWEGLWMSCVVQSTGQMQCKVYDSLLALPQDLQAARALCVIALLVALFGLLVYLAGAKCTTCVEEKDSKARLVLTSGIVFVISGVLTLIPVCWTAHAIIRDFYNPLVAEAQKRELGASLYLGWAASGLLLLGGGLLCCTCPSGGSQGPSHYMARYSTSAPAISRGPSEYPTKNYV	Clinical trial	"ClinicalTrials.gov (NCT05317078) Phase 1 First-In-Human Study to Explore the Safety, Tolerability, and Pharmacokinetics of AMG 794 in Participants With Claudin 6-positive Advanced/Metastatic Non-small Cell Lung Cancer, Epithelial Ovarian Cancer, and Other Malignant Solid Tumor Indications. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	hsa:9074	R-HSA-420029;	.	P56747;
TT70N8V	Myeloid inhibitory C-type lectin-like receptor (CD371)	Q5QGZ9	CL12A_HUMAN	.	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	CLEC12A	Cell surface receptor that modulates signaling cascades and mediates tyrosine phosphorylation of target MAP kinases.	.	.	MSEEVTYADLQFQNSSEMEKIPEIGKFGEKAPPAPSHVWRPAALFLTLLCLLLLIGLGVLASMFHVTLKIEMKKMNKLQNISEELQRNISLQLMSNMNISNKIRNLSTTLQTIATKLCRELYSKEQEHKCKPCPRRWIWHKDSCYFLSDDVQTWQESKMACAAQNASLLKINNKNALEFIKSQSRSYDYWLGLSPEEDSTRGMRVDNIINSSAWVIRNAPDLNNMYCGYINRLYVQYYHCTYKKRMICEKMANPVQLGSTYFREA	Clinical trial	ClinicalTrials.gov (NCT03631576) CD123/CLL1 CAR-T Cells for R/R AML	24	.	.	.	.	.	Lectin C-type domain	PF00059	PF00059; Lectin_C	.	.	.	R-HSA-6798695: Neutrophil degranulation	.	Q5QGZ9
TT7YT06	C-type lectin domain family 4 member C (CLEC4C)	Q8WTT0	CLC4C_HUMAN	.	Blood dendritic cell antigen 2; BDCA-2; C-type lectin superfamily member 7; Dendritic lectin; CD303	CLEC4C	"Lectin-type cell surface receptor which may play a role in antigen capturing by dendritic cells (PubMed:11748283, PubMed:21880719, PubMed:25995448). Specifically recognizes non-sialylated galactose-terminated biantennary glycans containing the trisaccharide epitope Gal(beta1-3/4)GlcNAc(beta1-2)Man (PubMed:21880719, PubMed:25995448). Binds to serum IgG (PubMed:25995448). Efficiently targets ligand into antigen-processing and peptide-loading compartments for presentation to T-cells (PubMed:11748283). May mediate potent inhibition of induction of IFN-alpha/beta expression in plasmacytoid dendritic cells (PubMed:11748283, PubMed:21880719). May act as a signaling receptor that activates protein-tyrosine kinases and mobilizes intracellular calcium (PubMed:11748283). {ECO:0000269|PubMed:11748283, ECO:0000269|PubMed:21880719, ECO:0000269|PubMed:25995448}."	.	3WBP;3WBQ;3WBR;4ZES;4ZET	MVPEEEPQDREKGLWWFQLKVWSMAVVSILLLSVCFTVSSVVPHNFMYSKTVKRLSKLREYQQYHPSLTCVMEGKDIEDWSCCPTPWTSFQSSCYFISTGMQSWTKSQKNCSVMGADLVVINTREEQDFIIQNLKRNSSYFLGLSDPGGRRHWQWVDQTPYNENVTFWHSGEPNNLDERCAIINFRSSEEWGWNDIHCHVPQKSICKMKKIYI	Clinical trial	Trial of Anti-BDCA2 Antibody Litifilimab for Cutaneous Lupus Erythematosus. N Engl J Med. 2022 Jul 28;387(4):321-331.	.	.	.	.	.	.	.	.	.	.	.	hsa:170482	R-HSA-5621480;R-HSA-6798695;	.	Q8WTT0;
TTQ02HK	Dendritic cell-associated C-type lectin 2 (CLEC6A)	Q6EIG7	CLC6A_HUMAN	.	Dectin-2; DECTIN2; DC-associated C-type lectin 2; CLECSF10; C-type lectin superfamily member 10; C-type lectin domain family 6 member A	CLEC6A	"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)."	.	5VYB	MMQEQQPQSTEKRGWLSLRLWSVAGISIALLSACFIVSCVVTYHFTYGETGKRLSELHSYHSSLTCFSEGTKVPAWGCCPASWKSFGSSCYFISSEEKVWSKSEQNCVEMGAHLVVFNTEAEQNFIVQQLNESFSYFLGLSDPQGNNNWQWIDKTPYEKNVRFWHLGEPNHSAEQCASIVFWKPTGWGWNDVICETRRNSICEMNKIYL	Literature-reported	C-Type Lectin Receptor Dectin-2 Binds to an Endogenous Protein -Glucuronidase on Dendritic Cells. PLoS One. 2017 Jan 3;12(1):e0169562.	.	.	.	.	.	.	.	.	.	.	.	hsa04625: C-type lectin receptor signaling pathway	R-HSA-5621480: Dectin-2 family	.	Q6EIG7
TTGUSRB	C-type lectin domain containing 9A (CLEC9A)	Q6UXN8	CLC9A_HUMAN	.	CLEC9A	CLEC9A	"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."	.	3VPP	MHEEEIYTSLQWDSPAPDTYQKCLSSNKCSGACCLVMVISCVFCMGLLTASIFLGVKLLQVSTIAMQQQEKLIQQERALLNFTEWKRSCALQMKYCQAFMQNSLSSAHNSSPCPNNWIQNRESCYYVSEIWSIWHTSQENCLKEGSTLLQIESKEEMDFITGSLRKIKGSYDYWVGLSQDGHSGRWLWQDGSSPSPGLLPAERSQSANQVCGYVKSNSLLSSNCSTWKYFICEKYALRSSV	Literature-reported	Self-adjuvanting nanoemulsion targeting dendritic cell receptor Clec9A enables antigen-specific immunotherapy. J Clin Invest. 2018 May 1;128(5):1971-1984.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q6UXN8
TT8KZG6	Chloride intracellular channel protein 1 (CLIC1)	O00299	CLIC1_HUMAN	.	hRNCC; Regulatory nuclear chloride ion channel protein; Nuclear chloride ion channel 27; NCC27; G6; Chloride channel ABP	CLIC1	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.	.	4K0N; 4K0G; 4JZQ; 4IQA; 3UVH	MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGVSQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKALK	Literature-reported	Identification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein. Sci Rep. 2017 Aug 17;7(1):8500.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	O00299
TTE6YDG	CDC-like kinase 1 (CLK1)	P49759	CLK1_HUMAN	Kinase	Dual specificity protein kinase CLK1; CLK; CDClike kinase 1	CLK1	"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."	EC 2.7.12.1	6RAA; 6Q8P; 6Q8K; 6I5L; 6I5K	MRHSKRTYCPDWDDKDWDYGKWRSSSSHKRRKRSHSSAQENKRCKYNHSKMCDSHYLESRSINEKDYHSRRYIDEYRNDYTQGCEPGHRQRDHESRYQNHSSKSSGRSGRSSYKSKHRIHHSTSHRRSHGKSHRRKRTRSVEDDEEGHLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNPKIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDVEHERLFDLIQKMLEYDPAKRITLREALKHPFFDLLKKSI	Patented-recorded	A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases. Proc Natl Acad Sci U S A. 2007 Dec 18;104(51):20523-8.	15.5	EC:2.7	.	protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily.	2.7.12.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa05134: Legionellosis	.	.	P49759
TT85TPS	CDC-like kinase 2 (CLK2)	P49760	CLK2_HUMAN	Kinase	Dual specificity protein kinase CLK2	CLK2	"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."	EC 2.7.12.1	6FYL; 6FYK; 6FYI; 5UNP; 3NR9	MPHPRRYHSSERGSRGSYREHYRSRKHKRRRSRSWSSSSDRTRRRRREDSYHVRSRSSYDDRSSDRRVYDRRYCGSYRRNDYSRDRGDAYYDTDYRHSYEYQRENSSYRSQRSSRRKHRRRRRRSRTFSRSSSQHSSRRAKSVEDDAEGHLIYHVGDWLQERYEIVSTLGEGTFGRVVQCVDHRRGGARVALKIIKNVEKYKEAARLEINVLEKINEKDPDNKNLCVQMFDWFDYHGHMCISFELLGLSTFDFLKDNNYLPYPIHQVRHMAFQLCQAVKFLHDNKLTHTDLKPENILFVNSDYELTYNLEKKRDERSVKSTAVRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERILGPIPSRMIRKTRKQKYFYRGRLDWDENTSAGRYVRENCKPLRRYLTSEAEEHHQLFDLIESMLEYEPAKRLTLGEALQHPFFARLRAEPPNKLWDSSRDISR	Patented-recorded	A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases. Proc Natl Acad Sci U S A. 2007 Dec 18;104(51):20523-8.	15.5	EC:2.7	.	protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily.	2.7.12.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	.	P49760
TTQPE1U	CDC-like kinase 3 (CLK3)	P49761	CLK3_HUMAN	Kinase	Dual specificity protein kinase CLK3	CLK3	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.	EC 2.7.12.1	6RCT; 6FYR; 6FYP; 6FT7; 3RAW	MPVLSARRRELADHAGSGRRSGPSPTARSGPHLSALRAQPARAAHLSGRGTYVRRDTAGGGPGQARPLGPPGTSLLGRGARRSGEGWCPGAFESGARAARPPSRVEPRLATAASREGAGLPRAEVAAGSGRGARSGEWGLAAAGAWETMHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRLPYQRRYRERRDSDTYRCEERSPSFGEDYYGPSRSRHRRRSRERGPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWLQERYEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHVRHMAYQLCHALRFLHENQLTHTDLKPENILFVNSEFETLYNEHKSCEEKSVKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSIGCILFEYYRGFTLFQTHENREHLVMMEKILGPIPSHMIHRTRKQKYFYKGGLVWDENSSDGRYVKENCKPLKSYMLQDSLEHVQLFDLMRRMLEFDPAQRITLAEALLHPFFAGLTPEERSFHTSRNPSR	Literature-reported	Specific CLK inhibitors from a novel chemotype for regulation of alternative splicing. Chem Biol. 2011 Jan 28;18(1):67-76.	0	EC:2.7	.	protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily.	2.7.12.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	.	P49761
TT1RFQP	CDC-like kinase 4 (CLK4)	Q9HAZ1	CLK4_HUMAN	Kinase	Dual specificity protein kinase CLK4	CLK4	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.	EC 2.7.12.1	6FYV	MRHSKRTHCPDWDSRESWGHESYRGSHKRKRRSHSSTQENRHCKPHHQFKESDCHYLEARSLNERDYRDRRYVDEYRNDYCEGYVPRHYHRDIESGYRIHCSKSSVRSRRSSPKRKRNRHCSSHQSRSKSHRRKRSRSIEDDEEGHLICQSGDVLRARYEIVDTLGEGAFGKVVECIDHGMDGMHVAVKIVKNVGRYREAARSEIQVLEHLNSTDPNSVFRCVQMLEWFDHHGHVCIVFELLGLSTYDFIKENSFLPFQIDHIRQMAYQICQSINFLHHNKLTHTDLKPENILFVKSDYVVKYNSKMKRDERTLKNTDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAMMERILGPIPQHMIQKTRKRKYFHHNQLDWDEHSSAGRYVRRRCKPLKEFMLCHDEEHEKLFDLVRRMLEYDPTQRITLDEALQHPFFDLLKKK	Literature-reported	Small-molecule pyrimidine inhibitors of the cdc2-like (Clk) and dual specificity tyrosine phosphorylation-regulated (Dyrk) kinases: development of chemical probe ML315. Bioorg Med Chem Lett. 2013 Jun15;23(12):3654-61.	0	EC:2.7	.	protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily.	2.7.12.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa05134: Legionellosis	.	.	Q9HAZ1
TTORF9W	Battenin (CLN3)	Q13286	CLN3_HUMAN	.	Batten disease protein; Protein CLN3	CLN3	"Mediates microtubule-dependent, anterograde transport connecting the Golgi network, endosomes, autophagosomes, lysosomes and plasma membrane, and participates in several cellular processes such as regulation of lysosomal pH, lysosome protein degradation, receptor-mediated endocytosis, autophagy, transport of proteins and lipids from the TGN, apoptosis and synaptic transmission (PubMed:10924275, PubMed:18817525, PubMed:18317235, PubMed:22261744, PubMed:15471887, PubMed:20850431). Facilitates the proteins transport from trans-Golgi network (TGN)-to other membrane compartments such as transport of microdomain-associated proteins to the plasma membrane, IGF2R transport to the lysosome where it regulates the CTSD release leading to regulation of CTSD maturation and thereby APP intracellular processing (PubMed:10924275, PubMed:18817525). Moreover regulates CTSD activity in response to osmotic stress (PubMed:23840424, PubMed:28390177). Also binds galactosylceramide and transports it from the trans Golgi to the rafts, which may have immediate and downstream effects on cell survival by modulating ceramide synthesis (PubMed:18317235). At the plasma membrane, regulates actin-dependent events including filopodia formation, cell migration, and pinocytosis through ARF1-CDC42 pathway and also the cytoskeleton organization through interaction with MYH10 and fodrin leading to the regulation of the plasma membrane association of Na+, K+ ATPase complex (PubMed:20850431). Regulates synaptic transmission in the amygdala, hippocampus, and cerebellum through regulation of synaptic vesicles density and their proximity to active zones leading to modulation of short-term plasticity and age-dependent anxious behavior, learning and memory (By similarity). Regulates autophagic vacuoles (AVs) maturation by modulating the trafficking between endocytic and autophagolysosomal/lysosomal compartments, which involves vesicle fusion leading to regulation of degradation process (By similarity). Participates also in cellular homeostasis of compounds such as, water, ions, amino acids, proteins and lipids in several tissue namely in brain and kidney through regulation of their transport and synthesis (PubMed:17482562). {ECO:0000250|UniProtKB:Q61124, ECO:0000269|PubMed:10924275, ECO:0000269|PubMed:15471887, ECO:0000269|PubMed:17482562, ECO:0000269|PubMed:18317235, ECO:0000269|PubMed:18817525, ECO:0000269|PubMed:20850431, ECO:0000269|PubMed:22261744, ECO:0000269|PubMed:23840424, ECO:0000269|PubMed:28390177}."	.	.	MGGCAGSRRRFSDSEGEETVPEPRLPLLDHQGAHWKNAVGFWLLGLCNNFSYVVMLSAAHDILSHKRTSGNQSHVDPGPTPIPHNSSSRFDCNSVSTAAVLLADILPTLVIKLLAPLGLHLLPYSPRVLVSGICAAGSFVLVAFSHSVGTSLCGVVFASISSGLGEVTFLSLTAFYPRAVISWWSSGTGGAGLLGALSYLGLTQAGLSPQQTLLSMLGIPALLLASYFLLLTSPEAQDPGGEEEAESAARQPLIRTEAPESKPGSSSSLSLRERWTVFKGLLWYIVPLVVVYFAEYFINQGLFELLFFWNTSLSHAQQYRWYQMLYQAGVFASRSSLRCCRIRFTWALALLQCLNLVFLLADVWFGFLPSIYLVFLIILYEGLLGGAAYVNTFHNIALETSDEHREFAMAATCISDTLGISLSGLLALPLHDFLCQLS	Clinical trial	"ClinicalTrials.gov (NCT03770572) Phase I/IIa Gene Transfer Clinical Trial for Juvenile Neuronal Ceroid Lipofuscinosis, Delivering the CLN3 Gene by Self-Complementary AAV9. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	hsa:1201	.	.	Q13286;
TTJCOQ7	Ceroid-lipofuscinosis neuronal protein 6 (CLN6)	Q9NWW5	CLN6_HUMAN	.	Protein CLN6	CLN6	.	.	.	MEATRRRQHLGATGGPGAQLGASFLQARHGSVSADEAARTAPFHLDLWFYFTLQNWVLDFGRPIAMLVFPLEWFPLNKPSVGDYFHMAYNVITPFLLLKLIERSPRTLPRSITYVSIIIFIMGASIHLVGDSVNHRLLFSGYQHHLSVRENPIIKNLKPETLIDSFELLYYYDEYLGHCMWYIPFFLILFMYFSGCFTASKAESLIPGPALLLVAPSGLYYWYLVTEGQIFILFIFTFFAMLALVLHQKRKRLFLDSNGLFLFSSFALTLLLVALWVAWLWNDPVLRKKYPGVIYVPEPWAFYTLHVSSRH	Clinical trial	"ClinicalTrials.gov (NCT02725580) Phase I/IIa Gene Transfer Clinical Trial for Variant Late Infantile Neuronal Ceroid Lipofuscinosis, Delivering the CLN6 Gene by Self-Complementary AAV9. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	hsa:54982	.	.	Q9NWW5;
TTRL76H	Clusterin messenger RNA (Clusterin mRNA)	P10909	CLUS_HUMAN	mRNA target	"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)"	CLU	"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."	.	.	MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQAKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVPVEVSRKNPKFMETVAEKALQEYRKKHREE	Clinical trial	Over-expression of clusterin is a resistance factor to the anti-cancer effect of histone deacetylase inhibitors. Eur J Cancer. 2009 Jul;45(10):1846-54.	25	mRNA	mRNA target	.	.	.	Clusterin	PF01093	PF01093; Clusterin	.	.	hsa04610: Complement and coagulation cascades	R-HSA-114608:Platelet degranulation	.	P10909
TTN8T0E	Clusterin (CLU)	P10909	CLUS_HUMAN	.	"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"	CLU	"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."	.	.	MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQAKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVPVEVSRKNPKFMETVAEKALQEYRKKHREE	Literature-reported	Clusterin is a gene-specific target of microRNA-21 in head and neck squamous cell carcinoma. Clin Cancer Res. 2014 Feb 15;20(4):868-77.	.	.	.	clusterin family.	.	.	Clusterin	PF01093	PF01093; Clusterin	.	.	hsa04610: Complement and coagulation cascades	R-HSA-114608: Platelet degranulation; R-HSA-166665: Terminal pathway of complement; R-HSA-6803157: Antimicrobial peptides; R-HSA-977606: Regulation of Complement cascade	.	P10909
TT8VUE0	Chymase (CYM)	P23946	CMA1_HUMAN	Peptidase	Mast cell protease I; CYH; Alpha-chymase	CMA1	"Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion."	EC 3.4.21.39	5YJP; 5YJM; 4KP0; 4K69; 4K60	MLLLPLPLLLFLLCSRAEAGEIIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPKYNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDFDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN	Clinical trial	ClinicalTrials.gov (NCT02452515) A Single-blind Pilot Study to Investigate Safety and Tolerability of the Chymase Inhibitor BAY1142524 in Clinically Stable Patients With Left-ventricular Dysfunction.	21	EC:3.4	Peptidase	peptidase S1 family. Granzyme subfamily.	3.4.21.39	Acting on peptide bonds (peptidases)	Trypsin	PF00089	PF00089; Trypsin	.	.	hsa04614:Renin-angiotensin system	R-HSA-1592389:Activation of Matrix Metalloproteinases; R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins	.	P23946
TT4UGZL	Chemerin receptor (CMKLR1)	Q99788	CML1_HUMAN	.	G-protein coupled receptor DEZ; G-protein coupled receptor ChemR23; DEZ; Chemokine-like receptor 1; CHEMR23	CMKLR1	"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)."	.	.	MRMEDEDYNTSISYGDEYPDYLDSIVVLEDLSPLEARVTRIFLVVVYSIVCFLGILGNGLVIIIATFKMKKTVNMVWFLNLAVADFLFNVFLPIHITYAAMDYHWVFGTAMCKISNFLLIHNMFTSVFLLTIISSDRCISVLLPVWSQNHRSVRLAYMACMVIWVLAFFLSSPSLVFRDTANLHGKISCFNNFSLSTPGSSSWPTHSQMDPVGYSRHMVVTVTRFLCGFLVPVLIITACYLTIVCKLQRNRLAKTKKPFKIIVTIIITFFLCWCPYHTLNLLELHHTAMPGSVFSLGLPLATALAIANSCMNPILYVFMGQDFKKFKVALFSRLVNALSEDTGHSSYPSHRSFTKMSSMNERTSMNERETGML	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 79).	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-373076: Class A/1 (Rhodopsin-like receptors)	.	Q99788
TTS92NQ	Cytomegalovirus DNA polymerase messenger RNA (CMV DNA polymerase mRNA)	P08546	DPOL_HCMVA	mRNA target	UL54 (mRNA); HFLF2 (mRNA); DNA polymerase catalytic subunit (mRNA)	CMV DNA polymerase mRNA	"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."	EC 2.7.7.7	1YYP	MFFNPYLSGGVTGGAVAGGRRQRSQPGSAQGSGKRPPQKQFLQIVPRGVMFDGQTGLIKHKTGRLPLMFYREIKHLLSHDMVWPCPWRETLVGRVVGPIRFHTYDQTDAVLFFDSPENVSPRYRQHLVPSGNVLRFFGATEHGYSICVNVFGQRSYFYCEYSDTDRLREVIASVGELVPEPRTPYAVSVTPATKTSIYGYGTRPVPDLQCVSISNWTMARKIGEYLLEQGFPVYEVRVDPLTRLVIDRRITTFGWCSVNRYDWRQQGRASTCDIEVDCDVSDLVAVPDDSSWPRYRCLSFDIECMSGEGGFPCAEKSDDIVIQISCVCYETGGNTAVDQGIPNGNDGRGCTSEGVIFGHSGLHLFTIGTCGQVGPDVDVYEFPSEYELLLGFMLFFQRYAPAFVTGYNINSFDLKYILTRLEYLYKVDSQRFCKLPTAQGGRFFLHSPAVGFKRQYAAAFPSASHNNPASTAATKVYIAGSVVIDMYPVCMAKTNSPNYKLNTMAELYLRQRKDDLSYKDIPRCFVANAEGRAQVGRYCLQDAVLVRDLFNTINFHYEAGAIARLAKIPLRRVIFDGQQIRIYTSLLDECACRDFILPNHYSKGTTVPETNSVAVSPNAAIISTAAVPGDAGSVAAMFQMSPPLQSAPSSQDGVSPGSGSNSSSSVGVFSVGSGSSGGVGVSNDNHGAGGTAAVSYQGATVFEPEVGYYNDPVAVFDFASLYPSIIMAHNLCYSTLLVPGGEYPVDPADVYSVTLENGVTHRFVRASVRVSVLSELLNKWVSQRRAVRECMRECQDPVRRMLLDKEQMALKVTCNAFYGFTGVVNGMMPCLPIAASITRIGRDMLERTARFIKDNFSEPCFLHNFFNQEDYVVGTREGDSEESSALPEGLETSSGGSNERRVEARVIYGDTDSVFVRFRGLTPQALVARGPSLAHYVTACLFVEPVKLEFEKVFVSLMMICKKRYIGKVEGASGLSMKGVDLVRKTACEFVKGVTRDVLSLLFEDREVSEAAVRLSRLSLDEVKKYGVPRGFWRILRRLVQARDDLYLHRVRVEDLVLSSVLSKDISLYRQSNLPHIAVIKRLAARSEELPSVGDRVFYVLTAPGVRTAPQGSSDNGDSVTAGVVSRSDAIDGTDDDADGGGVEESNRRGGEPAKKRARKPPSAVCNYEVAEDPSYVREHGVPIHADKYFEQVLKAVTNVLSPVFPGGETARKDKFLHMVLPRRLHLEPAFLPYSVKAHECC	Discontinued	"US patent application no. 5,442,049, Oligonucleotides for modulating the effects of cytomegalovirus infections."	12	mRNA	mRNA target	.	.	.	"DNA polymerase family B; DNA polymerase family B, exonuclease domain"	PF00136; PF03104	PF00136; DNA_pol_B; PF03104; DNA_pol_B_exo1	.	.	.	.	.	.
TTUR18Y	Cytomegalovirus Glycoprotein B (CMV gB)	P06473	GB_HCMVA	Hepacivirus polyprotein	gB; Envelope glycoprotein B	CMV gB	"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."	.	5CXF	MESRIWCLVVCVNLCIVCLGAAVSSSSTSHATSSTHNGSHTSRTTSAQTRSVYSQHVTSSEAVSHRANETIYNTTLKYGDVVGVNTTKYPYRVCSMAQGTDLIRFERNIICTSMKPINEDLDEGIMVVYKRNIVAHTFKVRVYQKVLTFRRSYAYIYTTYLLGSNTEYVAPPMWEIHHINKFAQCYSSYSRVIGGTVFVAYHRDSYENKTMQLIPDDYSNTHSTRYVTVKDQWHSRGSTWLYRETCNLNCMLTITTARSKYPYHFFATSTGDVVYISPFYNGTNRNASYFGENADKFFIFPNYTIVSDFGRPNAAPETHRLVAFLERADSVISWDIQDEKNVTCQLTFWEASERTIRSEAEDSYHFSSAKMTATFLSKKQEVNMSDSALDCVRDEAINKLQQIFNTSYNQTYEKYGNVSVFETSGGLVVFWQGIKQKSLVELERLANRSSLNITHRTRRSTSDNNTTHLSSMESVHNLVYAQLQFTYDTLRGYINRALAQIAEAWCVDQRRTLEVFKELSKINPSAILSAIYNKPIAARFMGDVLGLASCVTINQTSVKVLRDMNVKESPGRCYSRPVVIFNFANSSYVQYGQLGEDNEILLGNHRTEECQLPSLKIFIAGNSAYEYVDYLFKRMIDLSSISTVDSMIALDIDPLENTDFRVLELYSQKELRSSNVFDLEEIMREFNSYKQRVKYVEDKVVDPLPPYLKGLDDLMSGLGAAGKAVGVAIGAVGGAVASVVEGVATFLKNPFGAFTIILVAIAVVIITYLIYTRQRRLCTQPLQNLFPYLVSADGTTVTSGSTKDTSLQAPPSYEESVYNSGRKGPGPPSSDASTAAPPYTNEQAYQMLLALARLDAEQRAQQNGTDSLDGQTGTQDKGQKPNLLDRLRHRKNGYRHLKDSDEEENV	Clinical trial	"Clinical pipeline report, company report or official report of GlaxoSmithKline."	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5UHA6	Cytomegalovirus Immediate-early protein messenger RNA (CMV IE mRNA)	P03169; Q6SWP7; P06434	VIE1_HCMVT; VIE2_HCMVT; VIE3_HCMVT	mRNA target	Human cytomegalovirus immediate-early protein (mRNA)	CMV IE mRNA	"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."	.	.	MESSAKRKMDPDNPDEGPSSKVPRPETPVTKATTFLQTMLRKEVNSQLSLGDPLFPELAEESLKTFERVTEDCNENPEKDVLAELVKQIKVRVDMVRHRIKEHMLKKYTQTEEKFTGAFNMMGGCLQNALDILDKVHEPFEEMKCIGLTMQSMYENYIVPEDKREMWMACIKELHDVSKGAANKLGGALQAKARAKKDELRRKMMYMCYRNIEFFTKNSAFPKTTNGCSQAMAALQNLPQCSPDEIMAYAQKIFKILDEERDKVLTHIDHIFMDILTTCVETMCNEYKVTSDACMMTMYGGISLLSEFCRVLSCYVLEETSVMLAKRPLITKPEVISVMKRRIEEICMKVFAQYILGADPLRVCSPSVDDLRAIAEESDEEEAIVAYTLATRGASSSDSLVSPPESPVPATIPLSSVIVAENSDQEESEQSDEEEEEGAQEEREDTVSVKSEPVSEIEEVAPEEEEDGAEEPTASGGKSTHPMVTRSKADQ	Literature-reported	Fomivirsen: clinical pharmacology and potential drug interactions. Clin Pharmacokinet. 2002;41(4):255-60.	.	mRNA	mRNA target	.	.	.	.	.	.	.	.	.	.	.	.
TT4SCBE	Cytomegalovirus IE2 region messenger RNA (CMV IE2 mRNA)	P19893	VIE2_HCMVA	mRNA target	Viral transcription factor IE2 (mRNA); UL122 (mRNA); Protein UL122 (mRNA); IE2 (mRNA)	CMV IE2 mRNA	"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."	.	.	MESSAKRKMDPDNPDEGPSSKVPRPETPVTKATTFLQTMLRKEVNSQLSLGDPLFPELAEESLKTFEQVTEDCNENPEKDVLAELGDILAQAVNHAGIDSSSTGPTLTTHSCSVSSAPLNKPTPTSVAVTNTPLPGASATPELSPRKKPRKTTRPFKVIIKPPVPPAPIMLPLIKQEDIKPEPDFTIQYRNKIIDTAGCIVISDSEEEQGEEVETRGATASSPSTGSGTPRVTSPTHPLSQMNHPPLPDPLGRPDEDSSSSSSSSCSSASDSESESEEMKCSSGGGASVTSSHHGRGGFGGAASSSLLSCGHQSSGGASTGPRKKKSKRISELDNEKVRNIMKDKNTPFCTPNVQTRRGRVKIDEVSRMFRNTNRSLEYKNLPFTIPSMHQVLDEAIKACKTMQVNNKGIQIIYTRNHEVKSEVDAVRCRLGTMCNLALSTPFLMEHTMPVTHPPEVAQRTADACNEGVKAAWSLKELHTHQLCPRSSDYRNMIIHAATPVDLLGALNLCLPLMQKFPKQVMVRIFSTNQGGFMLPIYETAAKAYAVGQFEQPTETPPEDLDTLSLAIEAAIQDLRNKSQ	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	mRNA	mRNA target	.	.	.	Cytomegalovirus IE1 protein; Herpes virus intermediate/early protein 2/3	PF07340; PF03361	PF07340; Herpes_IE1; PF03361; Herpes_IE2_3	.	.	.	.	.	.
TTUTKV4	Cytomegalovirus Phosphorylated tegument protein UL51 homolog (CMV pUL71)	F5HEA3 (phosphorylated)	TEG7_HCMVM	.	Tegument protein UL51 homolog	CMV pUL71	"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."	.	.	MQLAQRLCELLMCRRKAAPVADYVLLQPSEDVELRELQAFLDENFKQLEITPADLRTFSRDTDVVNHLLKLLPLYRQCQSKCAFLKGYLSEGCLPHTRPAAEVECKKSQRILEALDILILKLVVGEFAMSEADSLEMLLDKFSTDQASLVEVQRVMGLVDMDCEKSAYMLEAGAAATVAPPTPPAVVQGESGVREDGETVAAVSAFACSSVSDSLIPEETGVTRPMMSLAHINTVSCPTVMRFDQRLLEEGDEEDEVTVMSPSPEPVQQQPPVEPVQQQPQGRGSHRRRYKESAPQETLPTNHEREILDLMRHSPDVPREAVMSPTMVTIPPPQIPFVGSARELRGVKKKKPTAAALLSSA	Literature-reported	The tegument protein UL71 of human cytomegalovirus is involved in late envelopment and affects multivesicular bodies. J Virol. 2011 Apr;85(8):3821-32.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOGPL1	Cytomegalovirus Terminase UL56 (CMV TRM1)	P16724	TRM1_HCMVA	Herpesviridae UL28	UL56; Tripartite terminase subunit UL28 homolog; TRM1; Protein HFLF0	CMV TRM1	"Component of the terminase, molecular motor that packages genomic DNA in empty capsid during assembly."	.	.	MEMNLLQKLCVVCSKCNEYAMELECLKYCDPNVLLAESTPFKRNAAAIVYLYRKIYPEVVAQNRTQSSLLTLYLEMLLKALHEDTALLDRALMAYSRQPDRAAFYRTVLRLDRCDRHHTVELQFTDNVRFSVSLATLNDIERFLCKMNYVYGILAPEAGLEVCAQLLELLRRLCGISPVARQEVYVEGTTCAQCYEELTIIPNQGRSLNKRLQGLLCNHIAVHRPSSQSDVNIQTVEQDLLDLTTRIPHLAGVLSALKSLFSSSSAYHSYIQEAEEALREYNLFTDIPERIYSLSDFTYWSRTSEVIVKRVGITIQQLNVYHQLCRALMNGISRHLYGEDVEDIFVLGEKALDGEERMFVGSVFAAPNRIIDLITSLSIQAFEDNPVFNKLHESNEMYTKIKHILEEIRRPLPDGTGGDGPEGEAIHLRGREAMSGTGTTLMTASNSSNSSTHSQRNNGGGGRARGGGKKVVGGGVNGQDGDGSENGLRVRNCDEHEALDLVDARSRIHNVTREVNVRKRAYLQKVSEVGYGKVIRCIKTQERLTSKLIDVNLVGPLCLDFISKLMNGFLYRSQYHQDQDVVDVGDQFTYDEHLYVVNNLIHKSLPVESLPLLGQQIYELCNGPLFTHCTDRYPLSHNVDMAYACDNAGVLPHVKDDLVKCAEGTVYPSEWMVVKYMGFFNFSDCQDLNVLQKEMWMHVRELVLSVALYNETFGKQLSIACLRDELHPDRDVILTYNKEWPLLLRHEGSLYKSKDLYLLLYRHLSRPDESGDVPTAPVAKPSTLTAAAAVSGVFREPDRPWLPSPYPSSSTAGVSRRVRATRKRPRRASSLLDLARDEHGIQDLVPGSLR	Successful	The novel anticytomegalovirus compound AIC246 (Letermovir) inhibits human cytomegalovirus replication through a specific antiviral mechanism that involves the viral terminase. J Virol. 2011 Oct;85(20):10884-93.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT1U2YM	Cytomegalovirus DNA polymerase (CMV UL54)	P08546	DPOL_HCMVA	DNA polymerase type-B family	UL54; DNA polymerase of Human herpesvirus 5	CMV UL54	"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."	EC 2.7.7.7	1YYP	MFFNPYLSGGVTGGAVAGGRRQRSQPGSAQGSGKRPPQKQFLQIVPRGVMFDGQTGLIKHKTGRLPLMFYREIKHLLSHDMVWPCPWRETLVGRVVGPIRFHTYDQTDAVLFFDSPENVSPRYRQHLVPSGNVLRFFGATEHGYSICVNVFGQRSYFYCEYSDTDRLREVIASVGELVPEPRTPYAVSVTPATKTSIYGYGTRPVPDLQCVSISNWTMARKIGEYLLEQGFPVYEVRVDPLTRLVIDRRITTFGWCSVNRYDWRQQGRASTCDIEVDCDVSDLVAVPDDSSWPRYRCLSFDIECMSGEGGFPCAEKSDDIVIQISCVCYETGGNTAVDQGIPNGNDGRGCTSEGVIFGHSGLHLFTIGTCGQVGPDVDVYEFPSEYELLLGFMLFFQRYAPAFVTGYNINSFDLKYILTRLEYLYKVDSQRFCKLPTAQGGRFFLHSPAVGFKRQYAAAFPSASHNNPASTAATKVYIAGSVVIDMYPVCMAKTNSPNYKLNTMAELYLRQRKDDLSYKDIPRCFVANAEGRAQVGRYCLQDAVLVRDLFNTINFHYEAGAIARLAKIPLRRVIFDGQQIRIYTSLLDECACRDFILPNHYSKGTTVPETNSVAVSPNAAIISTAAVPGDAGSVAAMFQMSPPLQSAPSSQDGVSPGSGSNSSSSVGVFSVGSGSSGGVGVSNDNHGAGGTAAVSYQGATVFEPEVGYYNDPVAVFDFASLYPSIIMAHNLCYSTLLVPGGEYPVDPADVYSVTLENGVTHRFVRASVRVSVLSELLNKWVSQRRAVRECMRECQDPVRRMLLDKEQMALKVTCNAFYGFTGVVNGMMPCLPIAASITRIGRDMLERTARFIKDNFSEPCFLHNFFNQEDYVVGTREGDSEESSALPEGLETSSGGSNERRVEARVIYGDTDSVFVRFRGLTPQALVARGPSLAHYVTACLFVEPVKLEFEKVFVSLMMICKKRYIGKVEGASGLSMKGVDLVRKTACEFVKGVTRDVLSLLFEDREVSEAAVRLSRLSLDEVKKYGVPRGFWRILRRLVQARDDLYLHRVRVEDLVLSSVLSKDISLYRQSNLPHIAVIKRLAARSEELPSVGDRVFYVLTAPGVRTAPQGSSDNGDSVTAGVVSRSDAIDGTDDDADGGGVEESNRRGGEPAKKRARKPPSAVCNYEVAEDPSYVREHGVPIHADKYFEQVLKAVTNVLSPVFPGGETARKDKFLHMVLPRRLHLEPAFLPYSVKAHECC	Clinical trial	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5DOVB	Cytomegalovirus Protease (CMV UL80)	P16753	SCAF_HCMVA	Peptidase	UL80; Capsid protein P40; Assemblin	CMV UL80	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.	.	2WPO; 1WPO; 1NKM; 1NKK; 1NJU	MTMDEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWLHAQGQGQPSLSVALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSRRCDDVEAATSLSGSETTPFKHVALCSVGRRRGTLAVYGRDPEWVTQRFPDLTAADRDGLRAQWQRCGSTAVDASGDPFRSDSYGLLGNSVDALYIRERLPKLRYDKQLVGVTERESYVKASVSPEAACDIKAASAERSGDSRSQAATPAAGARVPSSSPSPPVEPPSPVQPPALPASPSVLPAESPPSLSPSEPAEAASMSHPLSAAVPAATAPPGATVAGASPAVSSLAWPHDGVYLPKDAFFSLLGASRSAVPVMYPGAVAAPPSASPAPLPLPSYPASYGAPVVGYDQLAARHFADYVDPHYPGWGRRYEPAPSLHPSYPVPPPPSPAYYRRRDSPGGMDEPPSGWERYDGGHRGQSQKQHRHGGSGGHNKRRKETAAASSSSSDEDLSFPGEAEHGRARKRLKSHVNSDGGSGGHAGSNQQQQQRYDELRDAIHELKRDLFAARQSSTLLSAALPSAASSSPTTTTVCTPTGELTSGGGETPTALLSGGAKVAERAQAGVVNASCRLATASGSEAATAGPSTAGSSSCPASVVLAAAAAQAAAASQSPPKDMVDLNRRIFVAALNKLE	Patented-recorded	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXQ04B	Cytomegalovirus Ganciclovir kinase (CMV UL97)	P16788	UL97_HCMVA	Kinase	UL97; Human cytomegalovirus UL97 protein kinase; HSRF3 protein	CMV UL97	Phosphorylates the antiviral nucleoside analog ganciclovir.	EC 2.7.1.-	.	MSSALRSRARSASLGTTTQGWDPPPLRRPSRARRRQWMREAAQAAAQAAVQAAQAAAAQVAQAHVDENEVVDLMADEAGGGVTTLTTLSSVSTTTVLGHATFSACVRSDVMRDGEKEDAASDKENLRRPVVPSTSSRGSAASGDGYHGLRCRETSAMWSFEYDRDGDVTSVRRALFTGGSDPSDSVSGVRGGRKRPLRPPLVSLARTPLCRRRVGGVDAVLEENDVELRAESQDSAVASGPGRIPQPLSGSSGEESATAVEADSTSHDDVHCTCSNDQIITTSIRGLTCDPRMFLRLTHPELCELSISYLLVYVPKEDDFCHKICYAVDMSDESYRLGQGSFGEVWPLDRYRVVKVARKHSETVLTVWMSGLIRTRAAGEQQQPPSLVGTGVHRGLLTATGCCLLHNVTVHRRFHTDMFHHDQWKLACIDSYRRAFCTLADAIKFLNHQCRVCHFDITPMNVLIDVNPHNPSEIVRAALCDYSLSEPYPDYNERCVAVFQETGTARRIPNCSHRLRECYHPAFRPMPLQKLLICDPHARFPVAGLRRYCMSELSALGNVLGFCLMRLLDRRGLDEVRMGTEALLFKHAGAACRALENGKLTHCSDACLLILAAQMSYGACLLGEHGAALVSHTLRFVEAKMSSCRVRAFRRFYHECSQTMLHEYVRKNVERLLATSDGLYLYNAFRRTTSIICEEDLDGDCRQLFPE	Clinical trial	"The human cytomegalovirus UL97 protein kinase, an antiviral drug target, is required at the stage of nuclear egress. J Virol. 2003 Jan;77(2):905-14."	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUX6KI	Cytomegalovirus Glycoprotein coupled receptor (CMV US28)	P69333	US28_HCMVT	GPCR rhodopsin	HHRF3; G-protein coupled receptor homolog US28	CMV US28	"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."	.	5WB2; 5WB1	MTPTTTTAELTTEFDYDEDATPCVFTDVLNQSKPVTLFLYGVVFLFGSIGNFLVIFTITWRRRIQCSGDVYFINLAAADLLFVCTLPLWMQYLLDHNSLASVPCTLLTACFYVAMFASLCFITEIALDRYYAIVYMRYRPVKQACLFSIFWWIFAVIIAIPHFMVVTKKDNQCMTDYDYLEVSYPIILNVELMLGAFVIPLSVISYCYYRISRIVAVSQSRHKGRIVRVLIAVVLVFIIFWLPYHLTLFVDTLKLLKWISSSCEFERSLKRALILTESLAFCHCCLNPLLYVFVGTKFRQELHCLLAEFRQRLFSRDVSWYHSMSFSRRSSPSRRETSSDTLSDEVCRVSQIIP	Literature-reported	The HCMV chemokine receptor US28 is a potential target in vascular disease. Curr Drug Targets Infect Disord. 2001 Aug;1(2):151-8.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHIQMC	Cyclic nucleotide-gated channel alpha-1 (CNGA1)	P29973	CNGA1_HUMAN	.	"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"	CNGA1	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.	.	.	MKLSMKNNIINTQQSFVTMPNVIVPDIEKEIRRMENGACSSFSEDDDSASTSEESENENPHARGSFSYKSLRKGGPSQREQYLPGAIALFNVNNSSNKDQEPEEKKKKKKEKKSKSDDKNENKNDPEKKKKKKDKEKKKKEEKSKDKKEEEKKEVVVIDPSGNTYYNWLFCITLPVMYNWTMVIARACFDELQSDYLEYWLILDYVSDIVYLIDMFVRTRTGYLEQGLLVKEELKLINKYKSNLQFKLDVLSLIPTDLLYFKLGWNYPEIRLNRLLRFSRMFEFFQRTETRTNYPNIFRISNLVMYIVIIIHWNACVFYSISKAIGFGNDTWVYPDINDPEFGRLARKYVYSLYWSTLTLTTIGETPPPVRDSEYVFVVVDFLIGVLIFATIVGNIGSMISNMNAARAEFQARIDAIKQYMHFRNVSKDMEKRVIKWFDYLWTNKKTVDEKEVLKYLPDKLRAEIAINVHLDTLKKVRIFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVVLSDGSYFGEISILNIKGSKAGNRRTANIKSIGYSDLFCLSKDDLMEALTEYPDAKTMLEEKGKQILMKDGLLDLNIANAGSDPKDLEEKVTRMEGSVDLLQTRFARILAEYESMQQKLKQRLTKVEKFLKPLIDTEFSSIEGPGAESGPIDST	Clinical trial	"Dequalinium: a novel, high-affinity blocker of CNGA1 channels. J Gen Physiol. 2003 Jan;121(1):37-47."	16	.	.	.	.	.	.	.	.	.	.	hsa04022: cGMP-PKG signaling pathway; hsa04024: cAMP signaling pathway; hsa04744: Phototransduction	"R-HSA-2485179: Activation of the phototransduction cascade; R-HSA-2514859: Inactivation, recovery and regulation of the phototransduction cascade"	.	P29973
TT8SJGB	Cyclic nucleotide-gated channel alpha-2 (CNGA2)	Q16280	CNGA2_HUMAN	.	Cyclic nucleotide-gated olfactory channel; Cyclic nucleotide-gated cation channel 2; CNG2; CNG-2; CNG channel alpha-2; CNCG2; CNCA1; CNCA	CNGA2	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.	.	.	MTEKTNGVKSSPANNHNHHAPPAIKANGKDDHRTSSRPHSAADDDTSSELQRLADVDAPQQGRSGFRRIVRLVGIIREWANKNFREEEPRPDSFLERFRGPELQTVTTQEGDGKGDKDGEDKGTKKKFELFVLDPAGDWYYCWLFVIAMPVLYNWCLLVARACFSDLQKGYYLVWLVLDYVSDVVYIADLFIRLRTGFLEQGLLVKDTKKLRDNYIHTLQFKLDVASIIPTDLIYFAVDIHSPEVRFNRLLHFARMFEFFDRTETRTNYPNIFRISNLVLYILVIIHWNACIYYAISKSIGFGVDTWVYPNITDPEYGYLAREYIYCLYWSTLTLTTIGETPPPVKDEEYLFVIFDFLIGVLIFATIVGNVGSMISNMNATRAEFQAKIDAVKHYMQFRKVSKGMEAKVIRWFDYLWTNKKTVDEREILKNLPAKLRAEIAINVHLSTLKKVRIFHDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVVADDGVTQYALLSAGSCFGEISILNIKGSKMGNRRTANIRSLGYSDLFCLSKDDLMEAVTEYPDAKKVLEERGREILMKEGLLDENEVATSMEVDVQEKLGQLETNMETLYTRFGRLLAEYTGAQQKLKQRITVLETKMKQNNEDDYLSDGMNSPELAAADEP	Clinical trial	State-dependent block of CNG channels by dequalinium. J Gen Physiol. 2004 Mar;123(3):295-304.	16	.	.	.	.	.	.	.	.	.	.	hsa04024: cAMP signaling pathway; hsa04740: Olfactory transduction	R-HSA-381753: Olfactory Signaling Pathway; R-HSA-5620916: VxPx cargo-targeting to cilium	.	Q16280
TTW0QOV	Cyclic nucleotide-gated channel alpha-3 (CNGA3)	Q16281	CNGA3_HUMAN	.	Cyclic nucleotide-gated cation channel alpha-3; Cone photoreceptor cGMP-gated channel subunit alpha; CNG3; CNG-3; CNG channel alpha-3; CNCG3	CNGA3	"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."	.	3SWY	MAKINTQYSHPSRTHLKVKTSDRDLNRAENGLSRAHSSSEETSSVLQPGIAMETRGLADSGQGSFTGQGIARLSRLIFLLRRWAARHVHHQDQGPDSFPDRFRGAELKEVSSQESNAQANVGSQEPADRGRSAWPLAKCNTNTSNNTEEEKKTKKKDAIVVDPSSNLYYRWLTAIALPVFYNWYLLICRACFDELQSEYLMLWLVLDYSADVLYVLDVLVRARTGFLEQGLMVSDTNRLWQHYKTTTQFKLDVLSLVPTDLAYLKVGTNYPEVRFNRLLKFSRLFEFFDRTETRTNYPNMFRIGNLVLYILIIIHWNACIYFAISKFIGFGTDSWVYPNISIPEHGRLSRKYIYSLYWSTLTLTTIGETPPPVKDEEYLFVVVDFLVGVLIFATIVGNVGSMISNMNASRAEFQAKIDSIKQYMQFRKVTKDLETRVIRWFDYLWANKKTVDEKEVLKSLPDKLKAEIAINVHLDTLKKVRIFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGKEMYIINEGKLAVVADDGVTQFVVLSDGSYFGEISILNIKGSKSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPEAKKALEEKGRQILMKDNLIDEELARAGADPKDLEEKVEQLGSSLDTLQTRFARLLAEYNATQMKMKQRLSQLESQVKGGGDKPLADGEVPGDATKTEDKQQ	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 396).	0	.	.	.	.	.	.	.	.	.	.	hsa04024: cAMP signaling pathway; hsa04740: Olfactory transduction	.	.	Q16281
TT0LJCG	Cyclic nucleotide-gated channel beta-3 (CNGB3)	Q9NQW8	CNGB3_HUMAN	.	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	CNGB3	"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."	.	.	MFKSLTKVNKVKPIGENNENEQSSRRNEEGSHPSNQSQQTTAQEENKGEEKSLKTKSTPVTSEEPHTNIQDKLSKKNSSGDLTTNPDPQNAAEPTGTVPEQKEMDPGKEGPNSPQNKPPAAPVINEYADAQLHNLVKRMRQRTALYKKKLVEGDLSSPEASPQTAKPTAVPPVKESDDKPTEHYYRLLWFKVKKMPLTEYLKRIKLPNSIDSYTDRLYLLWLLLVTLAYNWNCCFIPLRLVFPYQTADNIHYWLIADIICDIIYLYDMLFIQPRLQFVRGGDIIVDSNELRKHYRTSTKFQLDVASIIPFDICYLFFGFNPMFRANRMLKYTSFFEFNHHLESIMDKAYIYRVIRTTGYLLFILHINACVYYWASNYEGIGTTRWVYDGEGNEYLRCYYWAVRTLITIGGLPEPQTLFEIVFQLLNFFSGVFVFSSLIGQMRDVIGAATANQNYFRACMDDTIAYMNNYSIPKLVQKRVRTWYEYTWDSQRMLDESDLLKTLPTTVQLALAIDVNFSIISKVDLFKGCDTQMIYDMLLRLKSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVLGGPDGTKVLVTLKAGSVFGEISLLAAGGGNRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILMKKARVLLKQKAKTAEATPPRKDLALLFPPKEETPKLFKTLLGGTGKASLARLLKLKREQAAQKKENSEGGEEEGKENEDKQKENEDKQKENEDKGKENEDKDKGREPEEKPLDRPECTASPIAVEEEPHSVRRTVLPRGTSRQSLIISMAPSAEGGEEVLTIEVKEKAKQ	Clinical trial	Molecular cloning and functional characterization of a new modulatory cyclic nucleotide-gated channel subunit from mouse retina. J Neurosci. 2000 Feb 15;20(4):1324-32.	0	.	.	cyclic nucleotide-gated cation channel (TC 1.A.1.5) family. CNGB3 subfamily. 	.	.	Cyclic nucleotide-binding domain	PF00027	PF00027; cNMP_binding	.	.	hsa04024:cAMP signaling pathway	.	.	Q9NQW8
TT71P0H	Cyclic nucleotide phosphodiesterase (CNP)	P09543	CN37_HUMAN	Phosphoric diester hydrolase	"CNPase; CNP; 2',3'-cyclic-nucleotide 3'-phosphodiesterase"	CNP	"May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin."	EC 3.1.4.37	1WOJ	MNRGFSRKSHTFLPKIFFRKMSSSGAKDKPELQFPFLQDEDTVATLLECKTLFILRGLPGSGKSTLARVIVDKYRDGTKMVSADAYKITPGARGAFSEEYKRLDEDLAAYCRRRDIRILVLDDTNHERERLEQLFEMADQYQYQVVLVEPKTAWRLDCAQLKEKNQWQLSADDLKKLKPGLEKDFLPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKELRQFVPGDEPREKMDLVTYFGKRPPGVLHCTTKFCDYGKAPGAEEYAQQDVLKKSYSKAFTLTISALFVTPKTTGARVELSEQQLQLWPSDVDKLSPTDNLPRGSRAHITLGCAADVEAVQTGLDLLEILRQEKGGSRGEEVGELSRGKLYSLGNGRWMLTLAKNMEVRAIFTGYYGKGKPVPTQGSRKGGALQSCTII	Literature-reported	"T cell response to 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) in multiple sclerosis patients. J Neuroimmunol. 2002 Sep;130(1-2):233-42."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P09543
TT6OEDT	Cannabinoid receptor 1 (CB1)	P21554	CNR1_HUMAN	GPCR rhodopsin	Cannabinoid CB1 receptor; CNR; CB-R; CANN6	CNR1	"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)."	.	6N4B; 5XRA; 5XR8; 5U09; 5TGZ	MKSILDGLADTTFRTITTDLLYVGSNDIQYEDIKGDMASKLGYFPQKFPLTSFRGSPFQEKMTAGDNPQLVPADQVNITEFYNKSLSSFKENEENIQCGENFMDIECFMVLNPSQQLAIAVLSLTLGTFTVLENLLVLCVILHSRSLRCRPSYHFIGSLAVADLLGSVIFVYSFIDFHVFHRKDSRNVFLFKLGGVTASFTASVGSLFLTAIDRYISIHRPLAYKRIVTRPKAVVAFCLMWTIAIVIAVLPLLGWNCEKLQSVCSDIFPHIDETYLMFWIGVTSVLLLFIVYAYMYILWKAHSHAVRMIQRGTQKSIIIHTSEDGKVQVTRPDQARMDIRLAKTLVLILVVLIICWGPLLAIMVYDVFGKMNKLIKTVFAFCSMLCLLNSTVNPIIYALRSKDLRHAFRSMFPSCEGTAQPLDNSMGDSDCLHKHANNAASVHRAAESCIKSTVKIAKVTMSVSTDTSAEAL	Successful	Emerging strategies for exploiting cannabinoid receptor agonists as medicines. Br J Pharmacol. 2009 Feb;156(3):397-411.	34	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.2.2	The G-protein-coupled receptor (GPCR) Family	hsa04015:Rap1 signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling	R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418594:G alpha (i) signalling events	.	P21554
TTMSFAW	Cannabinoid receptor 2 (CB2)	P34972	CNR2_HUMAN	GPCR rhodopsin	hCB2; Cannabinoid CB2 receptor; CX5; CB2B; CB2A; CB-2	CNR2	"May function in inflammatory response, nociceptive transmission and bone homeostasis. Heterotrimeric G protein-coupled receptor for endocannabinoid 2-arachidonoylglycerol mediating inhibition of adenylate cyclase."	.	5ZTY; 2KI9	MEECWVTEIANGSKDGLDSNPMKDYMILSGPQKTAVAVLCTLLGLLSALENVAVLYLILSSHQLRRKPSYLFIGSLAGADFLASVVFACSFVNFHVFHGVDSKAVFLLKIGSVTMTFTASVGSLLLTAIDRYLCLRYPPSYKALLTRGRALVTLGIMWVLSALVSYLPLMGWTCCPRPCSELFPLIPNDYLLSWLLFIAFLFSGIIYTYGHVLWKAHQHVASLSGHQDRQVPGMARMRLDVRLAKTLGLVLAVLLICWFPVLALMAHSLATTLSDQVKKAFAFCSMLCLINSMVNPVIYALRSGEIRSSAHHCLAHWKKCVRGLGSEAKEEAPRSSVTETEADGKITPWPDSRDLDLSDC	Successful	Posttraining activation of CB1 cannabinoid receptors in the CA1 region of the dorsal hippocampus impairs object recognition long-term memory. Neurobiol Learn Mem. 2008 Sep;90(2):374-81.	34	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.2.6	The G-protein-coupled receptor (GPCR) Family	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418594:G alpha (i) signalling events	.	P34972
TTGEM5Q	Ciliary neurotrophic factor (CNTF)	P26441	CNTF_HUMAN	Ciliary neurotrophic factor	CNTF	CNTF	CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.	.	1CNT	MAFTEHSPLTPHRRDLCSRSIWLARKIRSDLTALTESYVKHQGLNKNINLDSADGMPVASTDQWSELTEAERLQENLQAYRTFHVLLARLLEDQQVHFTPTEGDFHQAIHTLLLQVAAFAYQIEELMILLEYKIPRNEADGMPINVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRFISSHQTGIPARGSHYIANNKKM	Clinical trial	Reliability of maximal voluntary isometric contraction testing in a multicenter study of patients with amyotrophic lateral sclerosis. Syntex/Synergen Neuroscience Joint Venture rhCNTF ALS Study Group. Muscle Nerve. 1997 Jun;20(6):691-5.	21	.	.	.	.	.	.	.	.	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway	R-HSA-6788467: IL-6-type cytokine receptor ligand interactions	.	P26441
TTT2F9E	Ciliary neurotrophic factor receptor alpha (CNTFR)	P26992	CNTFR_HUMAN	Cytokine receptor	Ciliary neurotrophic factor receptor subunit alpha; CNTFR-alpha; CNTFR alpha; CNTF receptor subunit alpha	CNTFR	The alpha subunit provides the receptor specificity. Binds to CNTF.	.	1UC6	MAAPVPWACCAVLAAAAAVVYAQRHSPQEAPHVQYERLGSDVTLPCGTANWDAAVTWRVNGTDLAPDLLNGSQLVLHGLELGHSGLYACFHRDSWHLRHQVLLHVGLPPREPVLSCRSNTYPKGFYCSWHLPTPTYIPNTFNVTVLHGSKIMVCEKDPALKNRCHIRYMHLFSTIKYKVSISVSNALGHNATAITFDEFTIVKPDPPENVVARPVPSNPRRLEVTWQTPSTWPDPESFPLKFFLRYRPLILDQWQHVELSDGTAHTITDAYAGKEYIIQVAAKDNEIGTWSDWSVAAHATPWTEEPRHLTTEAQAAETTTSTTSSLAPPPTTKICDPGELGSGGGPSAPFLVSVPITLALAAAAATASSLLI	Clinical trial	"Clinical pipeline report, company report or official report of Neurotech."	24	Cytokine receptor	Cytokine receptor	type I cytokine receptor family. Type 3 subfamily.	.	.	Fibronectin type III domain	PF00041	PF00041; fn3	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway	R-HSA-6788467: IL-6-type cytokine receptor ligand interactions	.	P26992
TT8MI6U	Centrosomal protein (CNTLN)	Q9NXG0	CNTLN_HUMAN	.	Centlein; C9orf39; C9orf101	CNTLN	Required for centrosome cohesion and recruitment of CEP68 to centrosomes.	.	.	MAARSPPSPHPSPPARQLGPRSPRVGRGAEVHAMRSEASGFAGAAREVVADESDKIWVGEEGSGGRRGPGGAAPAHAPLLSAPMGSRRLEGISVEEAMVTRTQLLEEELSSLKEELALCQADKEFVWSLWKRLQVTNPDLTQVVSLVVEREKQKSEAKDRKVLEILQVKDAKIQEFEQRESVLKQEINDLVKRKIAVDEENAFLRKEFSDLEKKFKDKSQEIKDTKECVQNKEEQNRLVIKNLEEENKKLSTRCTDLLNDLEKLRKQEAHLRKEKYSTDAKIKTFEDNLIEARKEVEVSQSKYNALSLQLSNKQTELIQKDMDITLVRKELQELQNLYKQNSTHTAQQAELIQQLQVLNMDTQKVLRNQEDVHTAESISYQKLYNELHICFETTKSNEAMLRQSVTNLQDQLLQKEQENAKLKEKLQESQGAPLPLPQESDPDYSAQVPHRPSLSSLETLMVSQKSEIEYLQEKLKIANEKLSENISANKGFSRKSIMTSAEGKHKEPPVKRSRSLSPKSSFTDSEELQKLRKAERKIENLEKALQLKSQENDELRDAHEKRKERLQMLQTNYRAVKEQLKQWEEGSGMTEIRKIKRADPQQLRQEDSDAVWNELAYFKRENQELMIQKMNLEEELDELKVHISIDKAAIQELNRCVAERREEQLFRSGEDDEVKRSTPEKNGKEMLEQTLQKVTELENRLKSFEKRSRKLKEGNKKLMKENDFLKSLLKQQQEDTETREKELEQIIKGSKDVEKENTELQVKISELETEVTSLRRQVAEANALRNENEELINPMEKSHQSADRAKSEMATMKVRSGRYDCKTTMTKVKFKAAKKNCSVGRHHTVLNHSIKVMSNVFENLSKDGWEDVSESSSDSEAQTSQTLGTIIVETSQKISPTEDGKDQKESDPTEDSQTQGKEIVQTYLNIDGKTPKDYFHDKNAKKPTFQKKNCKMQKSSHTAVPTRVNREKYKNITAQKSSSNIILLRERIISLQQQNSVLQNAKKTAELSVKEYKEVNEKLLHQQQVSDQRFQTSRQTIKKLNLDLAGLRKEKEDLLKKLESSSEITSLAEENSQVTFPRIQVTSLSPSRSMDLEMKQLQYKLKNATNELTKQSSNVKTLKFELLAKEEHIKEMHEKISRMERDITMKRHLIEDLKFRQKVNLESNKSFSEMLQNLDKKVKTLTEECSNKKVSIDSLKQRLNVAVKEKSQYEQMYQKSKEELEKKDLKLTLLVSRISETESAMAEIETAASKQLQELALQSEQVLEGAQKTLLLANEKVEEFTTFVKALAKELQNDVHVVRRQIRELKKMKKNRDACKTSTHKAQTLAASILNISRSDLEEILDTEDQVEIEKTKIDAENDKEWMLYIQKLLEGQSLTLSPRLKCNGAIVAHQNLRLPDSSSSASAS	Literature-reported	The centrosomal protein Lats2 is a phosphorylation target of Aurora-A kinase. Genes Cells. 2004 May;9(5):383-97.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9NXG0
TTPR8FK	Contactin-1 (CNTN1)	Q12860	CNTN1_HUMAN	Immunoglobulin	Neural cell surface protein F3; Glycoprotein gp135; CNTN1	CNTN1	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.	.	3S97; 2EE2	MKMWLLVSHLVIISITTCLAEFTWYRRYGHGVSEEDKGFGPIFEEQPINTIYPEESLEGKVSLNCRARASPFPVYKWRMNNGDVDLTSDRYSMVGGNLVINNPDKQKDAGIYYCLASNNYGMVRSTEATLSFGYLDPFPPEERPEVRVKEGKGMVLLCDPPYHFPDDLSYRWLLNEFPVFITMDKRRFVSQTNGNLYIANVEASDKGNYSCFVSSPSITKSVFSKFIPLIPIPERTTKPYPADIVVQFKDVYALMGQNVTLECFALGNPVPDIRWRKVLEPMPSTAEISTSGAVLKIFNIQLEDEGIYECEAENIRGKDKHQARIYVQAFPEWVEHINDTEVDIGSDLYWPCVATGKPIPTIRWLKNGYAYHKGELRLYDVTFENAGMYQCIAENTYGAIYANAELKILALAPTFEMNPMKKKILAAKGGRVIIECKPKAAPKPKFSWSKGTEWLVNSSRILIWEDGSLEINNITRNDGGIYTCFAENNRGKANSTGTLVITDPTRIILAPINADITVGENATMQCAASFDPALDLTFVWSFNGYVIDFNKENIHYQRNFMLDSNGELLIRNAQLKHAGRYTCTAQTIVDNSSASADLVVRGPPGPPGGLRIEDIRATSVALTWSRGSDNHSPISKYTIQTKTILSDDWKDAKTDPPIIEGNMEAARAVDLIPWMEYEFRVVATNTLGRGEPSIPSNRIKTDGAAPNVAPSDVGGGGGRNRELTITWAPLSREYHYGNNFGYIVAFKPFDGEEWKKVTVTNPDTGRYVHKDETMSPSTAFQVKVKAFNNKGDGPYSLVAVINSAQDAPSEAPTEVGVKVLSSSEISVHWEHVLEKIVESYQIRYWAAHDKEEAANRVQVTSQEYSARLENLLPDTQYFIEVGACNSAGCGPPSDMIEAFTKKAPPSQPPRIISSVRSGSRYIITWDHVVALSNESTVTGYKVLYRPDGQHDGKLYSTHKHSIEVPIPRDGEYVVEVRAHSDGGDGVVSQVKISGAPTLSPSLLGLLLPAFGILVYLEF	Literature-reported	Contactin 1 IgG4 associates to chronic inflammatory demyelinating polyneuropathy with sensory ataxia. Brain. 2015 Jun;138(Pt 6):1484-91.	.	.	.	.	.	.	.	.	.	.	.	hsa04514: Cell adhesion molecules	R-HSA-2122948: Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-2979096: NOTCH2 Activation and Transmission of Signal to the Nucleus; R-HSA-373760: L1CAM interactions; R-HSA-447043: Neurofascin interactions	.	Q12860
TT2Z1WB	Contactin-2 (CNTN2)	Q02246	CNTN2_HUMAN	Basigin family	Transient axonal glycoprotein 1; TAX-1 gene; TAX-1; CNTN2; Axonin-1; Axonal glycoprotein TAG-1	CNTN2	"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."	.	2OM5	MGTATRRKPHLLLVAAVALVSSSAWSSALGSQTTFGPVFEDQPLSVLFPEESTEEQVLLACRARASPPATYRWKMNGTEMKLEPGSRHQLVGGNLVIMNPTKAQDAGVYQCLASNPVGTVVSREAILRFGFLQEFSKEERDPVKAHEGWGVMLPCNPPAHYPGLSYRWLLNEFPNFIPTDGRHFVSQTTGNLYIARTNASDLGNYSCLATSHMDFSTKSVFSKFAQLNLAAEDTRLFAPSIKARFPAETYALVGQQVTLECFAFGNPVPRIKWRKVDGSLSPQWTTAEPTLQIPSVSFEDEGTYECEAENSKGRDTVQGRIIVQAQPEWLKVISDTEADIGSNLRWGCAAAGKPRPTVRWLRNGEPLASQNRVEVLAGDLRFSKLSLEDSGMYQCVAENKHGTIYASAELAVQALAPDFRLNPVRRLIPAARGGEILIPCQPRAAPKAVVLWSKGTEILVNSSRVTVTPDGTLIIRNISRSDEGKYTCFAENFMGKANSTGILSVRDATKITLAPSSADINLGDNLTLQCHASHDPTMDLTFTWTLDDFPIDFDKPGGHYRRTNVKETIGDLTILNAQLRHGGKYTCMAQTVVDSASKEATVLVRGPPGPPGGVVVRDIGDTTIQLSWSRGFDNHSPIAKYTLQARTPPAGKWKQVRTNPANIEGNAETAQVLGLTPWMDYEFRVIASNILGTGEPSGPSSKIRTREAAPSVAPSGLSGGGGAPGELIVNWTPMSREYQNGDGFGYLLSFRRQGSTHWQTARVPGADAQYFVYSNESVRPYTPFEVKIRSYNRRGDGPESLTALVYSAEEEPRVAPTKVWAKGVSSSEMNVTWEPVQQDMNGILLGYEIRYWKAGDKEAAADRVRTAGLDTSARVSGLHPNTKYHVTVRAYNRAGTGPASPSANATTMKPPPRRPPGNISWTFSSSSLSIKWDPVVPFRNESAVTGYKMLYQNDLHLTPTLHLTGKNWIEIPVPEDIGHALVQIRTTGPGGDGIPAEVHIVRNGGTSMMVENMAVRPAPHPGTVISHSVAMLILIGSLEL	Literature-reported	The gene for the axonal cell adhesion molecule TAX-1 is amplified and aberrantly expressed in malignant gliomas. Cancer Res. 2001 Mar 1;61(5):2162-8.	.	.	.	.	.	.	.	.	.	.	.	hsa04514: Cell adhesion molecules	R-HSA-373760: L1CAM interactions; R-HSA-419037: NCAM1 interactions; R-HSA-447038: NrCAM interactions	.	Q02246
TT4YO0Z	Phosphopantetheine adenylyltransferase (PPAT)	Q13057 (180-358)	COASY_HUMAN	Kinase	Pantetheine-phosphate adenylyltransferase; Dephospho-CoA pyrophosphorylase; COASY	COASY	"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."	EC 2.7.7.3	.	VAGSPKQPVRGYYRGAVGGTFDRLHNAHKVLLSVACILAQEQLVVGVADKDLLKSKLLPELLQPYTERVEHLSEFLVDIKPSLTFDVIPLLDPYGPAGSDPSLEFLVVSEETYRGGMAINRFRLENDLEELALYQIQLLKDLRHTENEEDKVSSSSFRQRMLGNLLRPPYERPELPTCL	Literature-reported	"NME DIGEST. Drug News & Perspect 2002, 15(8):519, ISSN 0214-0934."	2	.	.	.	.	.	.	.	.	.	.	hsa00770:Pantothenate and CoA biosynthesis; hsa01100:Metabolic pathways	.	.	Q13057
TT63DI9	Endostatin (COL18A1)	P39060	COIA1_HUMAN	.	Collagen alpha1(XVIII) chain; Collagen alpha-1(XVIII) chain	COL18A1	Probably plays a major role in determining the retinal structure as well as in the closure of the neural tube.	.	3HSH; 3HON; 1BNL	MAPYPCGCHILLLLFCCLAAARANLLNLNWLWFNNEDTSHAATTIPEPQGPLPVQPTADTTTHVTPRNGSTEPATAPGSPEPPSELLEDGQDTPTSAESPDAPEENIAGVGAEILNVAKGIRSFVQLWNDTVPTESLARAETLVLETPVGPLALAGPSSTPQENGTTLWPSRGIPSSPGAHTTEAGTLPAPTPSPPSLGRPWAPLTGPSVPPPSSGRASLSSLLGGAPPWGSLQDPDSQGLSPAAAAPSQQLQRPDVRLRTPLLHPLVMGSLGKHAAPSAFSSGLPGALSQVAVTTLTRDSGAWVSHVANSVGPGLANNSALLGADPEAPAGRCLPLPPSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCCQFCEALQDACWSRLGGGRLPVACASLPTQEDGYCVLIGPAAERISEEVGLLQLLGDPPPQQVTQTDDPDVGLAYVFGPDANSGQVARYHFPSLFFRDFSLLFHIRPATEGPGVLFAITDSAQAMVLLGVKLSGVQDGHQDISLLYTEPGAGQTHTAASFRLPAFVGQWTHLALSVAGGFVALYVDCEEFQRMPLARSSRGLELEPGAGLFVAQAGGADPDKFQGVIAELKVRRDPQVSPMHCLDEEGDDSDGASGDSGSGLGDARELLREETGAALKPRLPAPPPVTTPPLAGGSSTEDSRSEEVEEQTTVASLGAQTLPGSDSVSTWDGSVRTPGGRVKEGGLKGQKGEPGVPGPPGRAGPPGSPCLPGPPGLPCPVSPLGPAGPALQTVPGPQGPPGPPGRDGTPGRDGEPGDPGEDGKPGDTGPQGFPGTPGDVGPKGDKGDPGVGERGPPGPQGPPGPPGPSFRHDKLTFIDMEGSGFGGDLEALRGPRGFPGPPGPPGVPGLPGEPGRFGVNSSDVPGPAGLPGVPGREGPPGFPGLPGPPGPPGREGPPGRTGQKGSLGEAGAPGHKGSKGAPGPAGARGESGLAGAPGPAGPPGPPGPPGPPGPGLPAGFDDMEGSGGPFWSTARSADGPQGPPGLPGLKGDPGVPGLPGAKGEVGADGVPGFPGLPGREGIAGPQGPKGDRGSRGEKGDPGKDGVGQPGLPGPPGPPGPVVYVSEQDGSVLSVPGPEGRPGFAGFPGPAGPKGNLGSKGERGSPGPKGEKGEPGSIFSPDGGALGPAQKGAKGEPGFRGPPGPYGRPGYKGEIGFPGRPGRPGMNGLKGEKGEPGDASLGFGMRGMPGPPGPPGPPGPPGTPVYDSNVFAESSRPGPPGLPGNQGPPGPKGAKGEVGPPGPPGQFPFDFLQLEAEMKGEKGDRGDAGQKGERGEPGGGGFFGSSLPGPPGPPGPPGPRGYPGIPGPKGESIRGQPGPPGPQGPPGIGYEGRQGPPGPPGPPGPPSFPGPHRQTISVPGPPGPPGPPGPPGTMGASSGVRLWATRQAMLGQVHEVPEGWLIFVAEQEELYVRVQNGFRKVQLEARTPLPRGTDNEVAALQPPVVQLHDSNPYPRREHPHPTARPWRADDILASPPRLPEPQPYPGAPHHSSYVHLRPARPTSPPAHSHRDFQPVLHLVALNSPLSGGMRGIRGADFQCFQQARAVGLAGTFRAFLSSRLQDLYSIVRRADRAAVPIVNLKDELLFPSWEALFSGSEGPLKPGARIFSFDGKDVLRHPTWPQKSVWHGSDPNGRRLTESYCETWRTEAPSATGQASSLLGGRLLGQSAASCHHAYIVLCIENSFMTASK	Clinical trial	"Safety and biodistribution of an equine infectious anemia virus-based gene therapy, RetinoStat( ), for age-related macular degeneration. Hum Gene Ther. 2012 Sep;23(9):980-91."	21	.	.	multiplexin collagen family.	.	.	Collagen triple helix repeat (20 copies); Domain of Unknown Function (DUF959) ; Collagenase NC10 and Endostatin; Fz domain	PF01391; PF06121; PF06482; PF01392	PF01391; Collagen; PF06121; DUF959; PF06482; Endostatin; PF01392; Fz	.	.	hsa04974:Protein digestion and absorption	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	.	P39060
TTUABC1	Collagen I (COL1A2)	P08123	CO1A2_HUMAN	.	Collagen alpha-2(I) chain; Alpha-2 type I collagen	COL1A2	Type I collagen is a member of group I collagen (fibrillar forming collagen).	.	5CVA; 5CTI; 5CTD	MLSFVDTRTLLLLAVTLCLATCQSLQEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQYDGKGVGLGPGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGAVGNAGPAGPAGPRGEVGLPGLSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGEPGPAGSKGESGNKGEPGSAGPQGPPGPSGEEGKRGPNGEAGSAGPPGPPGLRGSPGSRGLPGADGRAGVMGPPGSRGASGPAGVRGPNGDAGRPGEPGLMGPRGLPGSPGNIGPAGKEGPVGLPGIDGRPGPIGPAGARGEPGNIGFPGPKGPTGDPGKNGDKGHAGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPPGPPGFQGLPGPSGPAGEVGKPGERGLHGEFGLPGPAGPRGERGPPGESGAAGPTGPIGSRGPSGPPGPDGNKGEPGVVGAVGTAGPSGPSGLPGERGAAGIPGGKGEKGEPGLRGEIGNPGRDGARGAPGAVGAPGPAGATGDRGEAGAAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGAKGPKGENGVVGPTGPVGAAGPAGPNGPPGPAGSRGDGGPPGMTGFPGAAGRTGPPGPSGISGPPGPPGPAGKEGLRGPRGDQGPVGRTGEVGAVGPPGFAGEKGPSGEAGTAGPPGTPGPQGLLGAPGILGLPGSRGERGLPGVAGAVGEPGPLGIAGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNIGPVGAAGAPGPHGPVGPAGKHGNRGETGPSGPVGPAGAVGPRGPSGPQGIRGDKGEPGEKGPRGLPGLKGHNGLQGLPGIAGHHGDQGAPGSVGPAGPRGPAGPSGPAGKDGRTGHPGTVGPAGIRGPQGHQGPAGPPGPPGPPGPPGVSGGGYDFGYDGDFYRADQPRSAPSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPENIPAKNWYRSSKDKKHVWLGETINAGSQFEYNVEGVTSKEMATQLAFMRLLANYASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWGKTIIEYKTNKPSRLPFLDIAPLDIGGADQEFFVDIGPVCFK	Clinical trial	Company report (Argentisrx)	21	.	Fibrillar collagen family	fibrillar collagen family.	.	.	Fibrillar collagen C-terminal domain; Collagen triple helix repeat (20 copies)	PF01410; PF01391	PF01410; COLFI; PF01391; Collagen	.	.	hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion; hsa04512:ECM-receptor interaction; hsa04611:Platelet activation; hsa04974:Protein digestion and absorption; hsa05146:Amoebiasis	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	.	P08123
TT5WCAH	Collagen VI (COL6A3)	P12111	CO6A3_HUMAN	.	COL6A3	COL6A3	Collagen VI acts as a cell-binding protein.	.	2KNT; 1KUN; 1KTH; 1KNT	MRKHRHLPLVAVFCLFLSGFPTTHAQQQQADVKNGAAADIIFLVDSSWTIGEEHFQLVREFLYDVVKSLAVGENDFHFALVQFNGNPHTEFLLNTYRTKQEVLSHISNMSYIGGTNQTGKGLEYIMQSHLTKAAGSRAGDGVPQVIVVLTDGHSKDGLALPSAELKSADVNVFAIGVEDADEGALKEIASEPLNMHMFNLENFTSLHDIVGNLVSCVHSSVSPERAGDTETLKDITAQDSADIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELANIGLALDFVVENHFTRAGGSRVEEGVPQVLVLISAGPSSDEIRYGVVALKQASVFSFGLGAQAASRAELQHIATDDNLVFTVPEFRSFGDLQEKLLPYIVGVAQRHIVLKPPTIVTQVIEVNKRDIVFLVDGSSALGLANFNAIRDFIAKVIQRLEIGQDLIQVAVAQYADTVRPEFYFNTHPTKREVITAVRKMKPLDGSALYTGSALDFVRNNLFTSSAGYRAAEGIPKLLVLITGGKSLDEISQPAQELKRSSIMAFAIGNKGADQAELEEIAFDSSLVFIPAEFRAAPLQGMLPGLLAPLRTLSGTPEVHSNKRDIIFLLDGSANVGKTNFPYVRDFVMNLVNSLDIGNDNIRVGLVQFSDTPVTEFSLNTYQTKSDILGHLRQLQLQGGSGLNTGSALSYVYANHFTEAGGSRIREHVPQLLLLLTAGQSEDSYLQAANALTRAGILTFCVGASQANKAELEQIAFNPSLVYLMDDFSSLPALPQQLIQPLTTYVSGGVEEVPLAQPESKRDILFLFDGSANLVGQFPVVRDFLYKIIDELNVKPEGTRIAVAQYSDDVKVESRFDEHQSKPEILNLVKRMKIKTGKALNLGYALDYAQRYIFVKSAGSRIEDGVLQFLVLLVAGRSSDRVDGPASNLKQSGVVPFIFQAKNADPAELEQIVLSPAFILAAESLPKIGDLHPQIVNLLKSVHNGAPAPVSGEKDVVFLLDGSEGVRSGFPLLKEFVQRVVESLDVGQDRVRVAVVQYSDRTRPEFYLNSYMNKQDVVNAVRQLTLLGGPTPNTGAALEFVLRNILVSSAGSRITEGVPQLLIVLTADRSGDDVRNPSVVVKRGGAVPIGIGIGNADITEMQTISFIPDFAVAIPTFRQLGTVQQVISERVTQLTREELSRLQPVLQPLPSPGVGGKRDVVFLIDGSQSAGPEFQYVRTLIERLVDYLDVGFDTTRVAVIQFSDDPKVEFLLNAHSSKDEVQNAVQRLRPKGGRQINVGNALEYVSRNIFKRPLGSRIEEGVPQFLVLISSGKSDDEVDDPAVELKQFGVAPFTIARNADQEELVKISLSPEYVFSVSTFRELPSLEQKLLTPITTLTSEQIQKLLASTRYPPPAVESDAADIVFLIDSSEGVRPDGFAHIRDFVSRIVRRLNIGPSKVRVGVVQFSNDVFPEFYLKTYRSQAPVLDAIRRLRLRGGSPLNTGKALEFVARNLFVKSAGSRIEDGVPQHLVLVLGGKSQDDVSRFAQVIRSSGIVSLGVGDRNIDRTELQTITNDPRLVFTVREFRELPNIEERIMNSFGPSAATPAPPGVDTPPPSRPEKKKADIVFLLDGSINFRRDSFQEVLRFVSEIVDTVYEDGDSIQVGLVQYNSDPTDEFFLKDFSTKRQIIDAINKVVYKGGRHANTKVGLEHLRVNHFVPEAGSRLDQRVPQIAFVITGGKSVEDAQDVSLALTQRGVKVFAVGVRNIDSEEVGKIASNSATAFRVGNVQELSELSEQVLETLHDAMHETLCPGVTDAAKACNLDVILGFDGSRDQNVFVAQKGFESKVDAILNRISQMHRVSCSGGRSPTVRVSVVANTPSGPVEAFDFDEYQPEMLEKFRNMRSQHPYVLTEDTLKVYLNKFRQSSPDSVKVVIHFTDGADGDLADLHRASENLRQEGVRALILVGLERVVNLERLMHLEFGRGFMYDRPLRLNLLDLDYELAEQLDNIAEKACCGVPCKCSGQRGDRGPIGSIGPKGIPGEDGYRGYPGDEGGPGERGPPGVNGTQGFQGCPGQRGVKGSRGFPGEKGEVGEIGLDGLDGEDGDKGLPGSSGEKGNPGRRGDKGPRGEKGERGDVGIRGDPGNPGQDSQERGPKGETGDLGPMGVPGRDGVPGGPGETGKNGGFGRRGPPGAKGNKGGPGQPGFEGEQGTRGAQGPAGPAGPPGLIGEQGISGPRGSGGAAGAPGERGRTGPLGRKGEPGEPGPKGGIGNRGPRGETGDDGRDGVGSEGRRGKKGERGFPGYPGPKGNPGEPGLNGTTGPKGIRGRRGNSGPPGIVGQKGDPGYPGPAGPKGNRGDSIDQCALIQSIKDKCPCCYGPLECPVFPTELAFALDTSEGVNQDTFGRMRDVVLSIVNDLTIAESNCPRGARVAVVTYNNEVTTEIRFADSKRKSVLLDKIKNLQVALTSKQQSLETAMSFVARNTFKRVRNGFLMRKVAVFFSNTPTRASPQLREAVLKLSDAGITPLFLTRQEDRQLINALQINNTAVGHALVLPAGRDLTDFLENVLTCHVCLDICNIDPSCGFGSWRPSFRDRRAAGSDVDIDMAFILDSAETTTLFQFNEMKKYIAYLVRQLDMSPDPKASQHFARVAVVQHAPSESVDNASMPPVKVEFSLTDYGSKEKLVDFLSRGMTQLQGTRALGSAIEYTIENVFESAPNPRDLKIVVLMLTGEVPEQQLEEAQRVILQAKCKGYFFVVLGIGRKVNIKEVYTFASEPNDVFFKLVDKSTELNEEPLMRFGRLLPSFVSSENAFYLSPDIRKQCDWFQGDQPTKNLVKFGHKQVNVPNNVTSSPTSNPVTTTKPVTTTKPVTTTTKPVTTTTKPVTIINQPSVKPAAAKPAPAKPVAAKPVATKMATVRPPVAVKPATAAKPVAAKPAAVRPPAAAAAKPVATKPEVPRPQAAKPAATKPATTKPMVKMSREVQVFEITENSAKLHWERAEPPGPYFYDLTVTSAHDQSLVLKQNLTVTDRVIGGLLAGQTYHVAVVCYLRSQVRATYHGSFSTKKSQPPPPQPARSASSSTINLMVSTEPLALTETDICKLPKDEGTCRDFILKWYYDPNTKSCARFWYGGCGGNENKFGSQKECEKVCAPVLAKPGVISVMGT	Literature-reported	Collagen VI disorders: Insights on form and function in the extracellular matrix and beyond. Matrix Biol. 2018 Oct;71-72:348-367.	.	.	.	.	.	.	.	.	.	.	.	hsa04151: PI3K-Akt signaling pathway; hsa04510: Focal adhesion; hsa04512: ECM-receptor interaction; hsa04974: Protein digestion and absorption; hsa05165: Human papillomavirus infection	R-HSA-1442490: Collagen degradation; R-HSA-1650814: Collagen biosynthesis and modifying enzymes; R-HSA-186797: Signaling by PDGF; R-HSA-2022090: Assembly of collagen fibrils and other multimeric structures; R-HSA-216083: Integrin cell surface interactions; R-HSA-3000178: ECM proteoglycans; R-HSA-419037: NCAM1 interactions; R-HSA-8948216: Collagen chain trimerization	.	.
TTBCOKN	Collagen VII (COL7A1)	Q02388	CO7A1_HUMAN	.	Longchain collagen; Long-chain collagen; LC collagen; Collagen alpha1(VII) chain; Collagen alpha-1(VII) chain	COL7A1	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.	.	.	MTLRLLVAALCAGILAEAPRVRAQHRERVTCTRLYAADIVFLLDGSSSIGRSNFREVRSFLEGLVLPFSGAASAQGVRFATVQYSDDPRTEFGLDALGSGGDVIRAIRELSYKGGNTRTGAAILHVADHVFLPQLARPGVPKVCILITDGKSQDLVDTAAQRLKGQGVKLFAVGIKNADPEELKRVASQPTSDFFFFVNDFSILRTLLPLVSRRVCTTAGGVPVTRPPDDSTSAPRDLVLSEPSSQSLRVQWTAASGPVTGYKVQYTPLTGLGQPLPSERQEVNVPAGETSVRLRGLRPLTEYQVTVIALYANSIGEAVSGTARTTALEGPELTIQNTTAHSLLVAWRSVPGATGYRVTWRVLSGGPTQQQELGPGQGSVLLRDLEPGTDYEVTVSTLFGRSVGPATSLMARTDASVEQTLRPVILGPTSILLSWNLVPEARGYRLEWRRETGLEPPQKVVLPSDVTRYQLDGLQPGTEYRLTLYTLLEGHEVATPATVVPTGPELPVSPVTDLQATELPGQRVRVSWSPVPGATQYRIIVRSTQGVERTLVLPGSQTAFDLDDVQAGLSYTVRVSARVGPREGSASVLTVRREPETPLAVPGLRVVVSDATRVRVAWGPVPGASGFRISWSTGSGPESSQTLPPDSTATDITGLQPGTTYQVAVSVLRGREEGPAAVIVARTDPLGPVRTVHVTQASSSSVTITWTRVPGATGYRVSWHSAHGPEKSQLVSGEATVAELDGLEPDTEYTVHVRAHVAGVDGPPASVVVRTAPEPVGRVSRLQILNASSDVLRITWVGVTGATAYRLAWGRSEGGPMRHQILPGNTDSAEIRGLEGGVSYSVRVTALVGDREGTPVSIVVTTPPEAPPALGTLHVVQRGEHSLRLRWEPVPRAQGFLLHWQPEGGQEQSRVLGPELSSYHLDGLEPATQYRVRLSVLGPAGEGPSAEVTARTESPRVPSIELRVVDTSIDSVTLAWTPVSRASSYILSWRPLRGPGQEVPGSPQTLPGISSSQRVTGLEPGVSYIFSLTPVLDGVRGPEASVTQTPVCPRGLADVVFLPHATQDNAHRAEATRRVLERLVLALGPLGPQAVQVGLLSYSHRPSPLFPLNGSHDLGIILQRIRDMPYMDPSGNNLGTAVVTAHRYMLAPDAPGRRQHVPGVMVLLVDEPLRGDIFSPIREAQASGLNVVMLGMAGADPEQLRRLAPGMDSVQTFFAVDDGPSLDQAVSGLATALCQASFTTQPRPEPCPVYCPKGQKGEPGEMGLRGQVGPPGDPGLPGRTGAPGPQGPPGSATAKGERGFPGADGRPGSPGRAGNPGTPGAPGLKGSPGLPGPRGDPGERGPRGPKGEPGAPGQVIGGEGPGLPGRKGDPGPSGPPGPRGPLGDPGPRGPPGLPGTAMKGDKGDRGERGPPGPGEGGIAPGEPGLPGLPGSPGPQGPVGPPGKKGEKGDSEDGAPGLPGQPGSPGEQGPRGPPGAIGPKGDRGFPGPLGEAGEKGERGPPGPAGSRGLPGVAGRPGAKGPEGPPGPTGRQGEKGEPGRPGDPAVVGPAVAGPKGEKGDVGPAGPRGATGVQGERGPPGLVLPGDPGPKGDPGDRGPIGLTGRAGPPGDSGPPGEKGDPGRPGPPGPVGPRGRDGEVGEKGDEGPPGDPGLPGKAGERGLRGAPGVRGPVGEKGDQGDPGEDGRNGSPGSSGPKGDRGEPGPPGPPGRLVDTGPGAREKGEPGDRGQEGPRGPKGDPGLPGAPGERGIEGFRGPPGPQGDPGVRGPAGEKGDRGPPGLDGRSGLDGKPGAAGPSGPNGAAGKAGDPGRDGLPGLRGEQGLPGPSGPPGLPGKPGEDGKPGLNGKNGEPGDPGEDGRKGEKGDSGASGREGRDGPKGERGAPGILGPQGPPGLPGPVGPPGQGFPGVPGGTGPKGDRGETGSKGEQGLPGERGLRGEPGSVPNVDRLLETAGIKASALREIVETWDESSGSFLPVPERRRGPKGDSGEQGPPGKEGPIGFPGERGLKGDRGDPGPQGPPGLALGERGPPGPSGLAGEPGKPGIPGLPGRAGGVGEAGRPGERGERGEKGERGEQGRDGPPGLPGTPGPPGPPGPKVSVDEPGPGLSGEQGPPGLKGAKGEPGSNGDQGPKGDRGVPGIKGDRGEPGPRGQDGNPGLPGERGMAGPEGKPGLQGPRGPPGPVGGHGDPGPPGAPGLAGPAGPQGPSGLKGEPGETGPPGRGLTGPTGAVGLPGPPGPSGLVGPQGSPGLPGQVGETGKPGAPGRDGASGKDGDRGSPGVPGSPGLPGPVGPKGEPGPTGAPGQAVVGLPGAKGEKGAPGGLAGDLVGEPGAKGDRGLPGPRGEKGEAGRAGEPGDPGEDGQKGAPGPKGFKGDPGVGVPGSPGPPGPPGVKGDLGLPGLPGAPGVVGFPGQTGPRGEMGQPGPSGERGLAGPPGREGIPGPLGPPGPPGSVGPPGASGLKGDKGDPGVGLPGPRGERGEPGIRGEDGRPGQEGPRGLTGPPGSRGERGEKGDVGSAGLKGDKGDSAVILGPPGPRGAKGDMGERGPRGLDGDKGPRGDNGDPGDKGSKGEPGDKGSAGLPGLRGLLGPQGQPGAAGIPGDPGSPGKDGVPGIRGEKGDVGFMGPRGLKGERGVKGACGLDGEKGDKGEAGPPGRPGLAGHKGEMGEPGVPGQSGAPGKEGLIGPKGDRGFDGQPGPKGDQGEKGERGTPGIGGFPGPSGNDGSAGPPGPPGSVGPRGPEGLQGQKGERGPPGERVVGAPGVPGAPGERGEQGRPGPAGPRGEKGEAALTEDDIRGFVRQEMSQHCACQGQFIASGSRPLPSYAADTAGSQLHAVPVLRVSHAEEEERVPPEDDEYSEYSEYSVEEYQDPEAPWDSDDPCSLPLDEGSCTAYTLRWYHRAVTGSTEACHPFVYGGCGGNANRFGTREACERRCPPRVVQSQGTGTAQD	Literature-reported	COL7A1 Editing via CRISPR/Cas9 in Recessive Dystrophic Epidermolysis Bullosa. Mol Ther. 2017 Nov 1;25(11):2573-2584.	.	.	.	.	.	.	Collagen triple helix repeat (20 copies); Fibronectin type III domain; Kunitz/Bovine pancreatic trypsin inhibitor domain; von Willebrand factor type A domain	PF01391; PF00041; PF00014; PF00092	PF01391; Collagen; PF00041; fn3; PF00014; Kunitz_BPTI; PF00092; VWA	.	.	hsa04974: Protein digestion and absorption	R-HSA-1442490: Collagen degradation; R-HSA-1474244: Extracellular matrix organization; R-HSA-1650814: Collagen biosynthesis and modifying enzymes; R-HSA-2022090: Assembly of collagen fibrils and other multimeric structures; R-HSA-204005: COPII-mediated vesicle transport; R-HSA-216083: Integrin cell surface interactions; R-HSA-2214320: Anchoring fibril formation; R-HSA-3000157: Laminin interactions; R-HSA-5694530: Cargo concentration in the ER; R-HSA-8948216: Collagen chain trimerization	.	.
TTKWFB8	Catechol-O-methyl-transferase (COMT)	P21964	COMT_HUMAN	Methyltransferase	S-COMT; MB-COMT; Catechol-O-methyltransferase; COMT	COMT	"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."	EC 2.1.1.6	5LSA; 4XUE; 4XUD; 4XUC; 4PYK	MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRILNHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCGYSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFECTHYQSFLEYREVVDGLEKAIYKGPGSEAGP	Successful	Catechol-O-methyltransferase inhibitors in the management of Parkinson's disease. Semin Neurol. 2001;21(1):15-22.	34	.	.	.	.	.	.	.	.	.	.	hsa00140:Steroid hormone biosynthesis; hsa00350:Tyrosine metabolism; hsa01100:Metabolic pathways; hsa04728:Dopaminergic synapse	R-HSA-156581: Methylation; R-HSA-379397: Enzymatic degradation of dopamine by COMT; R-HSA-379398: Enzymatic degradation of Dopamine by monoamine oxidase; R-HSA-9679191: Potential therapeutics for SARS	MetaCyc:HS01791-MON	P21964
TTUJ0G5	HUMAN catechol-O-methyl-transferase (COMT)	P21964	COMT_HUMAN	Methyltransferase	S-COMT; MB-COMT; Catechol-O-methyltransferase; COMT	COMT	"Human protein catechol-O-methyltransferase interacts with SARS-CoV-2 Nsp7 protein with high significance, which indicates COMT as a potential therapeutic target."	EC 2.1.1.6	5LSA; 4XUE; 4XUD; 4XUC; 4PYK	MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRILNHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCGYSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFECTHYQSFLEYREVVDGLEKAIYKGPGSEAGP	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa00140: Steroid hormone biosynthesis; hsa00350: Tyrosine metabolism; hsa01100: Metabolic pathways; hsa04728: Dopaminergic synapse	R-HSA-156581: Methylation; R-HSA-379397: Enzymatic degradation of dopamine by COMT; R-HSA-379398: Enzymatic degradation of Dopamine by monoamine oxidase; R-HSA-9679191: Potential therapeutics for SARS	MetaCyc:HS01791-MON	P21964
TTJMY6S	Catechol O-methyltransferase	.	COMT_HUMAN	Single Protein	Catechol O-methyltransferase; COMT	COMT	"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."	.	.	MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRILNHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCGYSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFECTHYQSFLEYREVVDGLEKAIYKGPGSEAGP	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P21964
TTSTNJR	COPS5 messenger RNA (COPS5 mRNA)	Q92905	CSN5_HUMAN	mRNA target	Signalosome subunit 5 (mRNA); SGN5 (mRNA); Jun activation domain-binding protein 1 (mRNA); JAB1 (mRNA); CSN5 (mRNA); COP9 signalosome complex subunit 5 (mRNA)	COPS5	"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."	EC 3.4.-.-	5M5Q; 5JOH; 5JOG; 4WSN; 4F7O	MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINIS	Literature-reported	Analysis of RNA expression of normal and cancer tissues reveals high correlation of COP9 gene expression with respiratory chain complex components. BMC Genomics. 2016 Dec 1;17(1):983.	.	mRNA	mRNA target	.	.	.	Cop9 signalosome subunit 5 C-terminal domain; JAB1/Mov34/MPN/PAD-1 ubiquitin protease	PF18323; PF01398	PF18323; CSN5_C; PF01398; JAB	.	.	.	R-HSA-5696394: DNA Damage Recognition in GG-NER; R-HSA-6781823: Formation of TC-NER Pre-Incision Complex; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8951664: Neddylation	.	Q92905
TT87E24	JUN activation domain binding protein (COPS5)	Q92905	CSN5_HUMAN	Peptidase	Signalosome subunit 5; SGN5; Jun activation domain-binding protein 1; JAB1; CSN5; COP9 signalosome complex subunit 5	COPS5	"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."	EC 3.4.-.-	5M5Q; 5JOH; 5JOG; 4WSN; 4F7O	MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINIS	Literature-reported	Jun activation domain-binding protein 1 expression in breast cancer inversely correlates with the cell cycle inhibitor p27(Kip1). Cancer Res. 2003 Jun 1;63(11):2977-81.	.	EC:3.4	Peptidase	peptidase M67A family. CSN5 subfamily.	3.4.-.-	Acting on peptide bonds (peptidases)	Cop9 signalosome subunit 5 C-terminal domain; JAB1/Mov34/MPN/PAD-1 ubiquitin protease	PF18323; PF01398	PF18323; CSN5_C; PF01398; JAB	.	.	.	R-HSA-5696394: DNA Damage Recognition in GG-NER; R-HSA-6781823: Formation of TC-NER Pre-Incision Complex; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8951664: Neddylation	.	Q92905
TTY4IQ9	Corynebacterium Mutated CRM197 (Cory mTOX)	Q6NK15 (mutated)	Q6NK15_CORDI	.	Diphtheria toxin; DIP0222	Cory mTOX	Contains a single base change in the structural gene resulting in the substitution of glutamic acid for glycine which blocks ADP-ribosylation.	EC 2.4.2.36	5I82	MSRKLFASILIGALLGIGAPPSAHAGADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALSVELEINFETRGKRGQDAMYEYMAQACAGNRVRRSVGSSLSCINLDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVSEEKAKQYLEEFHQTALEHPELSELKTVTGTNPVFAGANYAAWAVNVAQVIDSETADNLEKTTAALSILPGIGSVMGIADGAVHHNTEEIVAQSIALSSLMVAQAIPLVGELVDIGFAAYNFVESIINLFQVVHNSYNRPAYSPGHKTQPFLHDGYAVSWNTVEDSIIRTGFQGESGHDIKITAENTPLPIAGVLLPTIPGKLDVNKSKTHISVNGRKIRMRCRAIDGDVTFCRPKSPVYVGNGVHANLHVAFHRSSSEKIHSNEISSDSIGVLGYQKTVDHTKVNSKLSLFFEIKS	Successful	Mullard A: 2010 FDA drug approvals. Nat Rev Drug Discov. 2011 Feb;10(2):82-5.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTX0S7F	Corynebacterium Pup-protein ligase (Cory pafA)	Q8NQE1	PAFA_CORGL	.	Pup-conjugating enzyme; Pup--protein ligase; Proteasome accessory factor A	Cory pafA	"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."	.	4BJR; 4B0T	MSTVESALTRRIMGIETEYGLTFVDGDSKKLRPDEIARRMFRPIVEKYSSSNIFIPNGSRLYLDVGSHPEYATAECDNLTQLINFEKAGDVIADRMAVDAEESLAKEDIAGQVYLFKNNVDSVGNSYGCHENYLVGRSMPLKALGKRLMPFLITRQLICGAGRIHHPNPLDKGESFPLGYCISQRSDHVWEGVSSATTRSRPIINTRDEPHADSHSYRRLHVIVGDANMAEPSIALKVGSTLLVLEMIEADFGLPSLELANDIASIREISRDATGSTLLSLKDGTTMTALQIQQVVFEHASKWLEQRPEPEFSGTSNTEMARVLDLWGRMLKAIESGDFSEVDTEIDWVIKKKLIDRFIQRGNLGLDDPKLAQVDLTYHDIRPGRGLFSVLQSRGMIKRWTTDEAILAAVDTAPDTTRAHLRGRILKAADTLGVPVTVDWMRHKVNRPEPQSVELGDPFSAVNSEVDQLIEYMTVHAESYRS	Literature-reported	"An Extended Loop of the Pup Ligase, PafA, Mediates Interaction with Protein Targets. J Mol Biol. 2016 Oct 9;428(20):4143-4153."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q8NQE1
TTJLVBO	Coronavirus Main proteinase (CoV 1a)	P0C6U8	R1A_CVHSA	.	pp1a; Replicase polyprotein 1a; ORF1a polyprotein	CoV 1a	"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."	.	5Y3Q; 5Y3E; 5F22; 4OW0; 4OVZ	MESLVLGVNEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDALSTNHGHKVVELVAEMDGIQYGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSYGIDLKSYDLGDELGTDPIEDYEQNWNTKHGSGALRELTRELNGGAVTRYVDNNFCGPDGYPLDCIKDFLARAGKSMCTLSEQLDYIESKRGVYCCRDHEHEIAWFTERSDKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVASPQECNNMHLSTLMKCNHCDEVSWQTCDFLKATCEHCGTENLVIEGPTTCGYLPTNAVVKMPCPACQDPEIGPEHSVADYHNHSNIETRLRKGGRTRCFGGCVFAYVGCYNKRAYWVPRASADIGSGHTGITGDNVETLNEDLLEILSRERVNINIVGDFHLNEEVAIILASFSASTSAFIDTIKSLDYKSFKTIVESCGNYKVTKGKPVKGAWNIGQQRSVLTPLCGFPSQAAGVIRSIFARTLDAANHSIPDLQRAAVTILDGISEQSLRLVDAMVYTSDLLTNSVIIMAYVTGGLVQQTSQWLSNLLGTTVEKLRPIFEWIEAKLSAGVEFLKDAWEILKFLITGVFDIVKGQIQVASDNIKDCVKCFIDVVNKALEMCIDQVTIAGAKLRSLNLGEVFIAQSKGLYRQCIRGKEQLQLLMPLKAPKEVTFLEGDSHDTVLTSEEVVLKNGELEALETPVDSFTNGAIVGTPVCVNGLMLLEIKDKEQYCALSPGLLATNNVFRLKGGAPIKGVTFGEDTVWEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAVVKTLQPVSDLLTNMGIDLDEWSVATFYLFDDAGEENFSSRMYCSFYPPDEEEEDDAECEEEEIDETCEHEYGTEDDYQGLPLEFGASAETVRVEEEEEEDWLDDTTEQSEIEPEPEPTPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQSANPMVIVNAANIHLKHGGGVAGALNKATNGAMQKESDDYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQDILLAPLLSAGIFGAKPLQSLQVCVQTVRTQVYIAVNDKALYEQVVMDYLDNLKPRVEAPKQEEPPNTEDSKTEEKSVVQKPVDVKPKIKACIDEVTTTLEETKFLTNKLLLFADINGKLYHDSQNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSKKAGGTTEMLSRALKKVPVDEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSEAPNAKEEILGTVSWNLREMLAHAEETRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAARCMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPSDDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQLEVKFNAPALQEAYYRARAGDAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKTGVSIPCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLCANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPVTDVFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKFADDLNQMTGFTKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSNSFEVLAVEDTQGMDNLACESQQPTSEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELGHEDLMAAYVENTSITIKKPNELSLALGLKTIATHGIAAINSVPWSKILAYVKPFLGQAAITTSNCAKRLAQRVFNNYMPYVFTLLFQLCTFTKSTNSRIRASLPTTIAKNSVKSVAKLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLICVTAAFGVLLSNFGAPSYCNGVRELYLNSSNVTTMDFCEGSFPCSICLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWVLAYMLFTKFFYLLGLSAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVECTTIVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCTGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVAVKNGALHLYFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESASKSASVYYSQLMCQPILLLDQALVSDVGDSTEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDLEVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLTCATTRQVVNVITTKISLKGGKIVSTCFKLMLKATLLCVLAALVCYIVMPVHTLSIHDGYTNEIIGYKAIQDGVTRDIISTDDCFANKHAGFDAWFSQRGGSYKNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICYTPSKLIEYSDFATSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDAEYCRHGTCERSEVGICLSTSGRWVLNNEHYRALSGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYYFMKFRRVFGEYNHVVAANALLFLMSFTILCLVPAYSFLPGVYSVFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAIYVFCISLKHCHWFFNNYLRKRVMFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYFSGALDTTSYREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTILGSTILEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLGIMAIAACAMLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLILMTARTVYDDAARRVWTLMNVITLVYKVYYGNALDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVYCFLGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINRLCEEMLDNRATLQAIASEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVDADSKIVQLSEINMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLALLSDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPLMQSADASTFLNGFAV	Literature-reported	Sabadinine: a potential non-peptide anti-severe acute-respiratory-syndrome agent identified using structure-aided design. J Med Chem. 2004 Feb 26;47(5):1079-80.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-9679504: Translation of Replicase and Assembly of the Replication Transcription Complex; R-HSA-9682706: Replication of the SARS-CoV-1 genome; R-HSA-9682708: Transcription of SARS-CoV-1 sgRNAs; R-HSA-9683439: Assembly of the SARS-CoV-1 Replication-Transcription Complex (RTC); R-HSA-9684325: Maturation of replicase proteins	.	.
TTC2DS7	COVID-19 non-structural protein 14 (nsp14)	P0DTD1 (59266452)	R1AB_SARS2	Coronaviruses polyprotein 1ab family	COVID-19 Proofreading exoribonuclease; COVID-19 ExoN; COVID-19 Guanine-N7 methyltransferase	COVID-19 rep	"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."	EC 3.1.13.-	.	AENVTGLFKDCSKVITGLHPTQAPTHLSVDTKFKTEGLCVDIPGIPKDMTYRRLISMMGFKMNYQVNGYPNMFITREEAIRHVRAWIGFDVEGCHATREAVGTNLPLQLGFSTGVNLVAVPTGYVDTPNNTDFSRVSAKPPPGDQFKHLIPLMYKGLPWNVVRIKIVQMLSDTLKNLSDRVVFVLWAHGFELTSMKYFVKIGPERTCCLCDRRATCFSTASDTYACWHHSIGFDYVYNPFMIDVQQWGFTGNLQSNHDLYCQVHGNAHVASCDAIMTRCLAVHECFVKRVDWTIEYPIIGDELKINAACRKVQHMVVKAALLADKFPVLHDIGNPKAIKCVPQADVEWKFYDAQPCSDKAYKIEELFYSYATHSDKFTDGVCLFWNCNVDRYPANSIVCRFDTRVLSNLNLPGCDGGSLYVNKHAFHTPAFDKSAFVNLKQLPFFYYSDSPCESHGKQVVSDIDYVPLKSATCITRCNLGGAVCRHHANEYRLYLDAYNMMISAGFSLWVYKQFDTYNLWNTFTRLQ	.	"Repurposing of FDA-Approved Toremifene to Treat COVID-19 by Blocking the Spike Glycoprotein and NSP14 of SARS-CoV-2.  June 5, 2020."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT1D53B	COVID-19 3C-like protease (3CLpro)	P0DTD1 (3264-3569)	R1AB_SARS2 (3264-3569)	Coronaviruses polyprotein 1ab family	COVID-19 3CL-PRO; COVID-19 3CLp; COVID-19 nsp5	COVID-19 rep	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).	EC 3.4.22.69	5R7Y; 5R7Z; 5R80; 5R81; 5R82	SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ	.	Coronavirus puts drug repurposing on the fast track. Nat Biotechnol. 2020 Apr;38(4):379-381.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTS824E	COVID-19 replicase polyprotein 1ab (pp1ab)	P0DTD1	R1AB_SARS2	Coronaviruses polyprotein 1ab family	ORF1ab polyprotein; pp1ab	COVID-19 rep	Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.	.	.	.	.	Current knowledge about the antivirals remdesivir (GS-5734) and GS-441524 as therapeutic options for coronaviruses. One Health. 2020 Mar 27;9:100128.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-191859: snRNP Assembly; R-HSA-918233: TRAF3-dependent IRF activation pathway; R-HSA-9694271: Assembly of the SARS-CoV-2 Replication-Transcription Complex (RTC); R-HSA-9694301: Maturation of replicase proteins; R-HSA-9694676: Translation of Replicase and Assembly of the Replication Transcription Complex; R-HSA-9694686: Replication of the SARS-CoV-2 genome; R-HSA-9694786: Transcription of SARS-CoV-2 sgRNAs; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses; R-HSA-9754678: SARS-CoV-2 modulates host translation machinery	.	.
TTNHMO8	COVID-19 papain-like proteinase (PL-PRO)	P0DTD1 (819-2763)	R1AB_SARS2 (819-2763)	Coronaviruses polyprotein 1ab family	COVID-19 papain-like proteinase; COVID-19 PL2-PRO; COVID-19 PL-PRO;  COVID-19 main proteinase; COVID-19 non-structural protein 3	COVID-19 rep	"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."	EC 3.4.19.12	5R7Y; 5R7Z; 5R80; 5R81; 5R82	APTKVTFGDDTVIEVQGYKSVNITFELDERIDKVLNEKCSAYTVELGTEVNEFACVVADAVIKTLQPVSELLTPLGIDLDEWSMATYYLFDESGEFKLASHMYCSFYPPDEDEEEGDCEEEEFEPSTQYEYGTEDDYQGKPLEFGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMELTPVVQTIEVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYDKLVSSFLEMKSEKQVEQKIAEIPKEEVKPFITESKPSVEQRKQDDKKIKACVEEVTTTLEETKFLTENLLLYIDINGNLHPDSATLVSDIDITFLKKDAPYIVGDVVQEGVLTAVVIPTKKAGGTTEMLAKALRKVPTDNYITTYPGQGLNGYTVEEAKTVLKKCKSAFYILPSIISNEKQEILGTVSWNLREMLAHAEETRKLMPVCVETKAIVSTIQRKYKGIKIQEGVVDYGARFYFYTSKTTVASLINTLNDLNETLVTMPLGYVTHGLNLEEAARYMRSLKVPATVSVSSPDAVTAYNGYLTSSSKTPEEHFIETISLAGSYKDWSYSGQSTQLGIEFLKRGDKSVYYTSNPTTFHLDGEVITFDNLKTLLSLREVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTYKLDGVVCTEIDPKLDNYYKKDNSYFTEQPIDLVPNQPYPNASFDNFKFVCDNIKFADDLNQLTGYKKPASRELKVTFFPDLNGDVVAIDYKHYTPSFKKGAKLLHKPIVWHVNNATNKATYKPNTWCIRCLWSTKPVETSNSFDVLKSEDAQGMDNLACEDLKPVSEEVVENPTIQKDVLECNVKTTEVVGDIILKPANNSLKITEEVGHTDLMAAYVDNSSLTIKKPNELSRVLGLKTLATHGLAAVNSVPWDTIANYAKPFLNKVVSTTTNIVTRCLNRVCTNYMPYFFTLLLQLCTFTRSTNSRIKASMPTTIAKNTVKSVGKFCLEASFNYLKSPNFSKLINIIIWFLLLSVCLGSLIYSTAALGVLMSNLGMPSYCTGYREGYLNSTNVTIATYCTGSIPCSVCLSGLDSLDTYPSLETIQITISSFKWDLTAFGLVAEWFLAYILFTRFFYVLGLAAIMQLFFSYFAVHFISNSWLMWLIINLVQMAPISAMVRMYIFFASFYYVWKSYVHVVDGCNSSTCMMCYKRNRATRVECTTIVNGVRRSFYVYANGGKGFCKLHNWNCVNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVTVKNGSIHLYFDKAGQKTYERHSLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESSAKSASVYYSQLMCQPILLLDQALVSDVGDSAEVAVKMFDAYVNTFSSTFNVPMEKLKTLVATAEAELAKNVSLDNVLSTFISAARQGFVDSDVETKDVVECLKLSHQSDIEVTGDSCNNYMLTYNKVENMTPRDLGACIDCSARHINAQVAKSHNIALIWNVKDFMSLSEQLRKQIRSAAKKNNLPF	.	Structure of Mpro from COVID-19 virus and discovery of its inhibitors. Nature. 2020 Apr 9.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTV1095	COVID-19 RNA-directed RNA polymerase (RdRp)	P0DTD1 (4393-5324)	R1AB_SARS2 (4393-5324)	Coronaviruses polyprotein 1ab family	COVID-19 Pol; COVID-19 nsp12	COVID-19 rep	Responsible for replication and transcription of the viral RNA genome.	EC 2.7.7.48	5R7Y; 5R7Z; 5R80; 5R81; 5R82	SADAQSFLNRVCGVSAARLTPCGTGTSTDVVYRAFDIYNDKVAGFAKFLKTNCCRFQEKDEDDNLIDSYFVVKRHTFSNYQHEETIYNLLKDCPAVAKHDFFKFRIDGDMVPHISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVENPDILRVYANLGERVRQALLKTVQFCDAMRNAGIVGVLTLDNQDLNGNWYDFGDFIQTTPGSGVPVVDSYYSLLMPILTLTRALTAESHVDTDLTKPYIKWDLLKYDFTEERLKLFDRYFKYWDQTYHPNCVNCLDDRCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGVVHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQTVKPGNFNKDFYDFAVSKGFFKEGSSVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGFPFNKWGKARLYYDSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTNRQFHQKLLKSIAATRGATVVIGTSKFYGGWHNMLKTVYSDVENPHLMGWDYPKCDRAMPNMLRIMASLVLARKHTTCCSLSHRFYRLANECAQVLSEMVMCGGSLYVKPGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLYECLYRNRDVDTDFVNEFYAYLRKHFSMMILSDDAVVCFNSTYASQGLVASIKNFKSVLYYQNNVFMSEAKCWTETDLTKGPHEFCSQHTMLVKQGDDYVYLPYPDPSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYIRKLHDELTGHMLDMYSVMLTNDNTSRYWEPEFYEAMYTPHTVLQ	.	"Comparative therapeutic efficacy of remdesivir and combination lopinavir, ritonavir, and interferon beta against MERS-CoV. Nat Commun. 2020 Jan 10;11(1):222."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZ3COY	COVID-19 spike glycoprotein (S)	P0DTC2	SPIKE_SARS2	Betacoronaviruses spike protein family	COVID-19 S glycoprotein; COVID-19 E2; COVID-19 Peplomer protein	COVID-19 S	"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."	.	6LVN; 6LXT; 6M0J; 6M17; 6VSB	.	.	Therapeutic options for the 2019 novel coronavirus (2019-nCoV). Nat Rev Drug Discov. 2020 Mar;19(3):149-150.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-9694322: Virion Assembly and Release; R-HSA-9694548: Maturation of spike protein; R-HSA-9694614: Attachment and Entry; R-HSA-9694635: Translation of Structural Proteins; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses	.	.
TT0F26C	Cytochrome c oxidase copper chaperone (COX17)	Q14061	COX17_HUMAN	.	Cytochrome c oxidase assembly protein COX17; COX17; CCO assembly protein COX17	COX17	Copper chaperone for cytochromec oxidase (COX). Binds two copper ions and deliver them to the Cu(A) site of COX.	.	2RNB; 2RN9; 2LGQ; 2L0Y	MPGLVDSNPAPPESQEKKPLKPCCACPETKKARDACIIEKGEEHCGHLIEAHKECMRALGFKI	Literature-reported	Identification of COX17 as a therapeutic target for non-small cell lung cancer. Cancer Res. 2003 Nov 1;63(21):7038-41.	.	.	.	.	.	.	.	.	.	.	.	hsa00190: Oxidative phosphorylation; hsa01100: Metabolic pathways; hsa04714: Thermogenesis	R-HSA-1268020: Mitochondrial protein import	.	Q14061
TT3LJ6G	Carboxypeptidase A1 (CPA1)	P15085	CBPA1_HUMAN	Peptidase	CPA	CPA1	"Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro."	EC 3.4.17.1	6I6Z; 5OM9; 4UF4; 4UEZ; 4UEF	MRGLLVLSVLLGAVFGKEDFVGHQVLRISVADEAQVQKVKELEDLEHLQLDFWRGPAHPGSPIDVRVPFPSIQAVKIFLESHGISYETMIEDVQSLLDEEQEQMFAFRSRARSTDTFNYATYHTLEEIYDFLDLLVAENPHLVSKIQIGNTYEGRPIYVLKFSTGGSKRPAIWIDTGIHSREWVTQASGVWFAKKITQDYGQDAAFTAILDTLDIFLEIVTNPDGFAFTHSTNRMWRKTRSHTAGSLCIGVDPNRNWDAGFGLSGASSNPCSETYHGKFANSEVEVKSIVDFVKDHGNIKAFISIHSYSQLLMYPYGYKTEPVPDQDELDQLSKAAVTALASLYGTKFNYGSIIKAIYQASGSTIDWTYSQGIKYSFTFELRDTGRYGFLLPASQIIPTAKETWLALLTIMEHTLNHPY	Literature-reported	A new type of five-membered heterocyclic inhibitors of basic metallocarboxypeptidases. Eur J Med Chem. 2009 Aug;44(8):3266-71.	0	.	.	.	.	.	.	.	.	.	.	hsa04972: Pancreatic secretion; hsa04974: Protein digestion and absorption	.	.	P15085
TT4UJX5	Carboxypeptidase B1 (CPB1)	P15086	CBPB1_HUMAN	Peptidase	Pancreas-specific protein; PASP; Carboxypeptidase B; CPB	CPB1	"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."	EC 3.4.17.2	1ZLI; 1KWM	MLALLVLVTVALASAHHGGEHFEGEKVFRVNVEDENHINIIRELASTTQIDFWKPDSVTQIKPHSTVDFRVKAEDTVTVENVLKQNELQYKVLISNLRNVVEAQFDSRVRATGHSYEKYNKWETIEAWTQQVATENPALISRSVIGTTFEGRAIYLLKVGKAGQNKPAIFMDCGFHAREWISPAFCQWFVREAVRTYGREIQVTELLDKLDFYVLPVLNIDGYIYTWTKSRFWRKTRSTHTGSSCIGTDPNRNFDAGWCEIGASRNPCDETYCGPAAESEKETKALADFIRNKLSSIKAYLTIHSYSQMMIYPYSYAYKLGENNAELNALAKATVKELASLHGTKYTYGPGATTIYPAAGGSDDWAYDQGIRYSFTFELRDTGRYGFLLPESQIRATCEETFLAIKYVASYVLEHLY	Patented-recorded	Synthesis and evaluation of imidazole acetic acid inhibitors of activated thrombin-activatable fibrinolysis inhibitor as novel antithrombotics. J Med Chem. 2003 Dec 4;46(25):5294-7.	0	.	.	.	.	.	.	.	.	.	.	hsa04972: Pancreatic secretion; hsa04974: Protein digestion and absorption	R-HSA-2022377: Metabolism of Angiotensinogen to Angiotensins	.	P15086
TTP18AY	Carboxypeptidase B2 (CPB2)	Q96IY4	CBPB2_HUMAN	Peptidase	Thrombin-activable fibrinolysis inhibitor; TAFI; Plasma carboxypeptidase B; Carboxypeptidase U; CPU; CPB2	CPB2	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.	EC 3.4.17.20	5HVH; 5HVG; 5HVF; 4P10; 3LMS	MKLCSLAVLVPIVLFCEQHVFAFQSGQVLAALPRTSRQVQVLQNLTTTYEIVLWQPVTADLIVKKKQVHFFVNASDVDNVKAHLNVSGIPCSVLLADVEDLIQQQISNDTVSPRASASYYEQYHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSGKEQAAKNAIWIDCGIHAREWISPAFCLWFIGHITQFYGIIGQYTNLLRLVDFYVMPVVNVDGYDYSWKKNRMWRKNRSFYANNHCIGTDLNRNFASKHWCEEGASSSSCSETYCGLYPESEPEVKAVASFLRRNINQIKAYISMHSYSQHIVFPYSYTRSKSKDHEELSLVASEAVRAIEKISKNTRYTHGHGSETLYLAPGGGDDWIYDLGIKYSFTIELRDTGTYGFLLPERYIKPTCREAFAAVSKIAWHVIRNV	Clinical trial	TAFIa inhibitors in the treatment of thrombosis. Curr Opin Drug Discov Devel. 2008 Jul;11(4):480-6.	17	.	.	.	.	.	.	.	.	.	.	hsa04610:Complement and coagulation cascades; hsa04972:Pancreatic secretion; hsa04974:Protein digestion and absorption	R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins	.	Q96IY4
TTXPWO6	Carboxypeptidase E (CPE)	P16870	CBPE_HUMAN	Peptidase	Prohormone processing carboxypeptidase; Enkephalin convertase; CPH; CPE	CPE	Removes residual C-terminal Arg or Lys remaining after initial endoprotease cleavage during prohormone processing. Processes proinsulin.	EC 3.4.17.10	.	MAGRGGSALLALCGALAACGWLLGAEAQEPGAPAAGMRRRRRLQQEDGISFEYHRYPELREALVSVWLQCTAISRIYTVGRSFEGRELLVIELSDNPGVHEPGEPEFKYIGNMHGNEAVGRELLIFLAQYLCNEYQKGNETIVNLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEGGPNNHLLKNMKKIVDQNTKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSGSAHEYSSSPDDAIFQSLARAYSSFNPAMSDPNRPPCRKNDDDSSFVDGTTNGGAWYSVPGGMQDFNYLSSNCFEITVELSCEKFPPEETLKTYWEDNKNSLISYLEQIHRGVKGFVRDLQGNPIANATISVEGIDHDVTSAKDGDYWRLLIPGNYKLTASAPGYLAITKKVAVPYSPAAGVDFELESFSERKEEEKEELMEWWKMMSETLNF	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	.	.	.	.	.	.	.	.	.	.	hsa04940: Type I diabetes mellitus	R-HSA-264876: Insulin processing	.	P16870
TTVOH2M	Carboxypeptidase M (CPM)	P14384	CBPM_HUMAN	Peptidase	Human carboxypeptidase M	CPM	"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."	EC 3.4.17.12	1UWY	MDFPCLWLGLLLPLVAALDFNYHRQEGMEAFLKTVAQNYSSVTHLHSIGKSVKGRNLWVLVVGRFPKEHRIGIPEFKYVANMHGDETVGRELLLHLIDYLVTSDGKDPEITNLINSTRIHIMPSMNPDGFEAVKKPDCYYSIGRENYNQYDLNRNFPDAFEYNNVSRQPETVAVMKWLKTETFVLSANLHGGALVASYPFDNGVQATGALYSRSLTPDDDVFQYLAHTYASRNPNMKKGDECKNKMNFPNGVTNGYSWYPLQGGMQDYNYIWAQCFEITLELSCCKYPREEKLPSFWNNNKASLIEYIKQVHLGVKGQVFDQNGNPLPNVIVEVQDRKHICPYRTNKYGEYYLLLLPGSYIINVTVPGHDPHITKVIIPEKSQNFSALKKDILLPFQGQLDSIPVSNPSCPMIPLYRNLPDHSAATKPSLFLFLVSLLHIFFK	Literature-reported	Synthesis and evaluation of imidazole acetic acid inhibitors of activated thrombin-activatable fibrinolysis inhibitor as novel antithrombotics. J Med Chem. 2003 Dec 4;46(25):5294-7.	0	EC:3.4	.	peptidase M14 family.	3.4.17.12 	Acting on peptide bonds (peptidases)	Zinc carboxypeptidase	PF00246	PF00246; Peptidase_M14	.	.	.	R-HSA-163125: Post-translational modification: synthesis of GPI-anchored proteins	.	P14384
TT8V2KD	Arginine carboxypeptidase (CPN1)	P15169	CBPN_HUMAN	.	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	CPN1	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.	EC 3.4.17.3	2NSM	MSDLLSVFLHLLLLFKLVAPVTFRHHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLCEEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYIYYNEKYGGPNHHLPLPDNWKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHRVRGVRRTASTPTPDDKLFQKLAKVYSYAHGWMFQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQVHQGIKGMVLDENYNNLANAVISVSGINHDVTSGDHGDYFRLLLPGIYTVSATAPGYDPETVTVTVGPAEPTLVNFHLKRSIPQVSPVRRAPSRRHGVRAKVQPQARKKEMEMRQLQRGPA	Literature-reported	Synthesis and evaluation of imidazole acetic acid inhibitors of activated thrombin-activatable fibrinolysis inhibitor as novel antithrombotics. J Med Chem. 2003 Dec 4;46(25):5294-7.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-977606: Regulation of Complement cascade	.	P15169
TT42M75	Carbamoyl-phosphate synthetase I (CPS1)	P31327	CPSM_HUMAN	Carbon-nitrogen ligase	"Carbamoyl-phosphate synthase [ammonia], mitochondrial; CPSase I; CPS1"	CPS1	Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell.	EC 6.3.4.16	5OJO; 5DOU; 5DOT; 4UUB; 4UUA	MTRILTAFKVVRTLKTGFGFTNVTAHQKWKFSRPGIRLLSVKAQTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTALDELGLSKYLESNGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVDFVDPNKQNLIAEVSTKDVKVYGKGNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTKMEYDGILIAGGPGNPALAEPLIQNVRKILESDRKEPLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDNTLPAGWKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKKGKATTITSVLPKPALVASRVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEVGLKQADTVYFLPITPQFVTEVIKAEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAMTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIEGFTPRLPMNKEWPSNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNSESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDVNFDDHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGCIISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAGVHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDEKHLPTLDHPIIPADYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRRTAVDSGIPLLTNFQVTKLFAEAVQKSRKVDSKSLFHYRQYSAGKAA	Successful	Mullard A: 2010 FDA drug approvals. Nat Rev Drug Discov. 2011 Feb;10(2):82-5.	34	.	.	.	.	.	.	.	.	.	.	"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"	R-HSA-70635: Urea cycle	MetaCyc:HS00415-MON	P31327
TTDL0NY	Carnitine O-palmitoyltransferase I (CPT1B)	Q92523	CPT1B_HUMAN	Acyltransferase	"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"	CPT1B	"mitochondrial outer membrane, mitochondrion, carnitine O-palmitoyltransferase activity, carnitine metabolic process, carnitine shuttle, fatty acid beta-oxidation, long-chain fatty acid transport."	EC 2.3.1.21	.	MAEAHQAVAFQFTVTPDGVDFRLSREALKHVYLSGINSWKKRLIRIKNGILRGVYPGSPTSWLVVIMATVGSSFCNVDISLGLVSCIQRCLPQGCGPYQTPQTRALLSMAIFSTGVWVTGIFFFRQTLKLLLCYHGWMFEMHGKTSNLTRIWAMCIRLLSSRHPMLYSFQTSLPKLPVPRVSATIQRYLESVRPLLDDEEYYRMELLAKEFQDKTAPRLQKYLVLKSWWASNYVSDWWEEYIYLRGRSPLMVNSNYYVMDLVLIKNTDVQAARLGNIIHAMIMYRRKLDREEIKPVMALGIVPMCSYQMERMFNTTRIPGKDTDVLQHLSDSRHVAVYHKGRFFKLWLYEGARLLKPQDLEMQFQRILDDPSPPQPGEEKLAALTAGGRVEWAQARQAFFSSGKNKAALEAIERAAFFVALDEESYSYDPEDEASLSLYGKALLHGNCYNRWFDKSFTLISFKNGQLGLNAEHAWADAPIIGHLWEFVLGTDSFHLGYTETGHCLGKPNPALAPPTRLQWDIPKQCQAVIESSYQVAKALADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDRGKFCLTYEASMTRMFREGRTETVRSCTSESTAFVQAMMEGSHTKADLRDLFQKAAKKHQNMYRLAMTGAGIDRHLFCLYLVSKYLGVSSPFLAEVLSEPWRLSTSQIPQSQIRMFDPEQHPNHLGAGGGFGPVADDGYGVSYMIAGENTIFFHISSKFSSSETNAQRFGNHIRKALLDIADLFQVPKAYS	Successful	Perhexiline. Cardiovasc Drug Rev. 2007 Spring;25(1):76-97.	34	EC:2.3	Acyltransferase	carnitine/choline acetyltransferase family.	2.3.1.21	Acyltransferases	Choline/Carnitine o-acyltransferase; Carnitine O-palmitoyltransferase N-terminus	PF00755; PF16484	PF00755; Carn_acyltransf; PF16484; CPT_N	.	.	hsa00071:Fatty acid degradation; hsa01212:Fatty acid metabolism; hsa03320:PPAR signaling pathway; hsa04152:AMPK signaling pathway; hsa04920:Adipocytokine signaling pathway; hsa04922:Glucagon signaling pathway	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	MetaCyc:MON66-34409	Q92523
TTEA8OW	Complement receptor type 1 (CR1)	P17927	CR1_HUMAN	Receptor of complement activation	CR1; CD35 antigen; C3b/C4b receptor	CR1	Mediates cellular binding of particles and immunecomplexes that have activated complement.	.	5FO9; 2Q7Z; 2MCZ; 2MCY; 1PPQ	MGASSPRSPEPVGPPAPGLPFCCGGSLLAVVVLLALPVAWGQCNAPEWLPFARPTNLTDEFEFPIGTYLNYECRPGYSGRPFSIICLKNSVWTGAKDRCRRKSCRNPPDPVNGMVHVIKGIQFGSQIKYSCTKGYRLIGSSSATCIISGDTVIWDNETPICDRIPCGLPPTITNGDFISTNRENFHYGSVVTYRCNPGSGGRKVFELVGEPSIYCTSNDDQVGIWSGPAPQCIIPNKCTPPNVENGILVSDNRSLFSLNEVVEFRCQPGFVMKGPRRVKCQALNKWEPELPSCSRVCQPPPDVLHAERTQRDKDNFSPGQEVFYSCEPGYDLRGAASMRCTPQGDWSPAAPTCEVKSCDDFMGQLLNGRVLFPVNLQLGAKVDFVCDEGFQLKGSSASYCVLAGMESLWNSSVPVCEQIFCPSPPVIPNGRHTGKPLEVFPFGKTVNYTCDPHPDRGTSFDLIGESTIRCTSDPQGNGVWSSPAPRCGILGHCQAPDHFLFAKLKTQTNASDFPIGTSLKYECRPEYYGRPFSITCLDNLVWSSPKDVCKRKSCKTPPDPVNGMVHVITDIQVGSRINYSCTTGHRLIGHSSAECILSGNAAHWSTKPPICQRIPCGLPPTIANGDFISTNRENFHYGSVVTYRCNPGSGGRKVFELVGEPSIYCTSNDDQVGIWSGPAPQCIIPNKCTPPNVENGILVSDNRSLFSLNEVVEFRCQPGFVMKGPRRVKCQALNKWEPELPSCSRVCQPPPDVLHAERTQRDKDNFSPGQEVFYSCEPGYDLRGAASMRCTPQGDWSPAAPTCEVKSCDDFMGQLLNGRVLFPVNLQLGAKVDFVCDEGFQLKGSSASYCVLAGMESLWNSSVPVCEQIFCPSPPVIPNGRHTGKPLEVFPFGKAVNYTCDPHPDRGTSFDLIGESTIRCTSDPQGNGVWSSPAPRCGILGHCQAPDHFLFAKLKTQTNASDFPIGTSLKYECRPEYYGRPFSITCLDNLVWSSPKDVCKRKSCKTPPDPVNGMVHVITDIQVGSRINYSCTTGHRLIGHSSAECILSGNTAHWSTKPPICQRIPCGLPPTIANGDFISTNRENFHYGSVVTYRCNLGSRGRKVFELVGEPSIYCTSNDDQVGIWSGPAPQCIIPNKCTPPNVENGILVSDNRSLFSLNEVVEFRCQPGFVMKGPRRVKCQALNKWEPELPSCSRVCQPPPEILHGEHTPSHQDNFSPGQEVFYSCEPGYDLRGAASLHCTPQGDWSPEAPRCAVKSCDDFLGQLPHGRVLFPLNLQLGAKVSFVCDEGFRLKGSSVSHCVLVGMRSLWNNSVPVCEHIFCPNPPAILNGRHTGTPSGDIPYGKEISYTCDPHPDRGMTFNLIGESTIRCTSDPHGNGVWSSPAPRCELSVRAGHCKTPEQFPFASPTIPINDFEFPVGTSLNYECRPGYFGKMFSISCLENLVWSSVEDNCRRKSCGPPPEPFNGMVHINTDTQFGSTVNYSCNEGFRLIGSPSTTCLVSGNNVTWDKKAPICEIISCEPPPTISNGDFYSNNRTSFHNGTVVTYQCHTGPDGEQLFELVGERSIYCTSKDDQVGVWSSPPPRCISTNKCTAPEVENAIRVPGNRSFFSLTEIIRFRCQPGFVMVGSHTVQCQTNGRWGPKLPHCSRVCQPPPEILHGEHTLSHQDNFSPGQEVFYSCEPSYDLRGAASLHCTPQGDWSPEAPRCTVKSCDDFLGQLPHGRVLLPLNLQLGAKVSFVCDEGFRLKGRSASHCVLAGMKALWNSSVPVCEQIFCPNPPAILNGRHTGTPFGDIPYGKEISYACDTHPDRGMTFNLIGESSIRCTSDPQGNGVWSSPAPRCELSVPAACPHPPKIQNGHYIGGHVSLYLPGMTISYICDPGYLLVGKGFIFCTDQGIWSQLDHYCKEVNCSFPLFMNGISKELEMKKVYHYGDYVTLKCEDGYTLEGSPWSQCQADDRWDPPLAKCTSRTHDALIVGTLSGTIFFILLIIFLSWIILKHRKGNNAHENPKEVAIHLHSQGGSSVHPRTLQTNEENSRVLP	Clinical trial	Complement activation is critical for placental ischemia-induced hypertension in the rat. Mol Immunol. 2013 Nov;56(1-2):91-7.	17	.	.	.	.	.	.	.	.	.	.	hsa04610:Complement and coagulation cascades; hsa04640:Hematopoietic cell lineage; hsa05134:Legionellosis; hsa05140:Leishmaniasis; hsa05144:Malaria; hsa05152:Tuberculosis	R-HSA-977606:Regulation of Complement cascade	.	P17927
TT0HUN7	Complement receptor type 2 (CD21)	P20023	CR2_HUMAN	.	EpsteinBarr virus receptor; Epstein-Barr virus receptor; EBV receptor; Cr2; Complement C3d receptor; C3DR	CR2	"Participates in B lymphocytes activation. Receptor for complement C3, for the Epstein-Barr virus on human B-cells and T-cells and for HNRNPU."	.	3OED; 2GSX; 2ATY; 1W2S; 1W2R	MGAAGLLGVFLALVAPGVLGISCGSPPPILNGRISYYSTPIAVGTVIRYSCSGTFRLIGEKSLLCITKDKVDGTWDKPAPKCEYFNKYSSCPEPIVPGGYKIRGSTPYRHGDSVTFACKTNFSMNGNKSVWCQANNMWGPTRLPTCVSVFPLECPALPMIHNGHHTSENVGSIAPGLSVTYSCESGYLLVGEKIINCLSSGKWSAVPPTCEEARCKSLGRFPNGKVKEPPILRVGVTANFFCDEGYRLQGPPSSRCVIAGQGVAWTKMPVCEEIFCPSPPPILNGRHIGNSLANVSYGSIVTYTCDPDPEEGVNFILIGESTLRCTVDSQKTGTWSGPAPRCELSTSAVQCPHPQILRGRMVSGQKDRYTYNDTVIFACMFGFTLKGSKQIRCNAQGTWEPSAPVCEKECQAPPNILNGQKEDRHMVRFDPGTSIKYSCNPGYVLVGEESIQCTSEGVWTPPVPQCKVAACEATGRQLLTKPQHQFVRPDVNSSCGEGYKLSGSVYQECQGTIPWFMEIRLCKEITCPPPPVIYNGAHTGSSLEDFPYGTTVTYTCNPGPERGVEFSLIGESTIRCTSNDQERGTWSGPAPLCKLSLLAVQCSHVHIANGYKISGKEAPYFYNDTVTFKCYSGFTLKGSSQIRCKADNTWDPEIPVCEKETCQHVRQSLQELPAGSRVELVNTSCQDGYQLTGHAYQMCQDAENGIWFKKIPLCKVIHCHPPPVIVNGKHTGMMAENFLYGNEVSYECDQGFYLLGEKKLQCRSDSKGHGSWSGPSPQCLRSPPVTRCPNPEVKHGYKLNKTHSAYSHNDIVYVDCNPGFIMNGSRVIRCHTDNTWVPGVPTCIKKAFIGCPPPPKTPNGNHTGGNIARFSPGMSILYSCDQGYLLVGEALLLCTHEGTWSQPAPHCKEVNCSSPADMDGIQKGLEPRKMYQYGAVVTLECEDGYMLEGSPQSQCQSDHQWNPPLAVCRSRSLAPVLCGIAAGLILLTFLIVITLYVISKHRARNYYTDTSQKEAFHLEAREVYSVDPYNPAS	Clinical trial	The complement receptor 2/factor H fusion protein TT30 protects paroxysmal nocturnal hemoglobinuria erythrocytes from complement-mediated hemolysis and C3 fragment. Blood. 2012 Jun 28;119(26):6307-16.	17	.	.	receptors of complement activation (RCA) family.	.	.	Sushi repeat (SCR repeat)	PF00084	PF00084; Sushi	.	.	hsa04610:Complement and coagulation cascades; hsa04640:Hematopoietic cell lineage; hsa04662:B cell receptor signaling pathway; hsa05169:Epstein-Barr virus infection	R-HSA-977606: Regulation of Complement cascade	.	P20023
TTC8M31	Carnitine acyltransferase (CRAT)	P43155	CACP_HUMAN	Acyltransferase	Carnitine acetylase; Carnitine O-acetyltransferase; CRAT	CRAT	"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."	EC 2.3.1.7	1S5O; 1NM8	MLAFAARTVVKPLGFLKPFSLMKASSRFKAHQDALPRLPVPPLQQSLDHYLKALQPIVSEEEWAHTKQLVDEFQASGGVGERLQKGLERRARKTENWLSEWWLKTAYLQYRQPVVIYSSPGVMLPKQDFVDLQGQLRFAAKLIEGVLDFKVMIDNETLPVEYLGGKPLCMNQYYQILSSCRVPGPKQDTVSNFSKTKKPPTHITVVHNYQFFELDVYHSDGTPLTADQIFVQLEKIWNSSLQTNKEPVGILTSNHRNSWAKAYNTLIKDKVNRDSVRSIQKSIFTVCLDATMPRVSEDVYRSHVAGQMLHGGGSRLNSGNRWFDKTLQFIVAEDGSCGLVYEHAAAEGPPIVTLLDYVIEYTKKPELVRSPLVPLPMPKKLRFNITPEIKSDIEKAKQNLSIMIQDLDITVMVFHHFGKDFPKSEKLSPDAFIQMALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASMDSLTFVKAMDDSSVTEHQKVELLRKAVQAHRGYTDRAIRGEAFDRHLLGLKLQAIEDLVSMPDIFMDTSYAIAMHFHLSTSQVPAKTDCVMFFGPVVPDGYGVCYNPMEAHINFSLSAYNSCAETNAARLAHYLEKALLDMRALLQSHPRAKL	Discontinued	Selective Reversible Inhibition of Liver Carnitine Palmitoyl-Transferase 1 by Teglicar Reduces Gluconeogenesis and Improves Glucose Homeostasis. Diabetes. 2011 February; 60(2): 644-651.	5	.	.	.	.	.	.	.	.	.	.	.	R-HSA-389887: Beta-oxidation of pristanoyl-CoA; R-HSA-9033241: Peroxisomal protein import	MetaCyc:HS01816-MON	P43155
TTDKGTC	Protein cereblon (CRBN)	Q96SW2	CRBN_HUMAN	.	Protein cereblon	CRBN	"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."	.	6H0G; 6H0F; 6BOY; 6BNB; 6BN9	MAGEGDQQDAAHNMGNHLPLLPAESEEEDEMEVEDQDSKEAKKPNIINFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQDFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQKRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDKVILCL	Clinical trial	"CC-122, a pleiotropic pathway modifier, mimics an interferon response and has antitumor activity in DLBCL. Blood. 2015 Aug 6;126(6):779-89."	17	.	.	.	.	.	.	.	.	.	.	.	R-HSA-9679191: Potential therapeutics for SARS	.	Q96SW2
TTH4AN3	Cyclic AMP-responsive element-binding protein (CREB1)	P16220	CREB1_HUMAN	Basic leucine zipper bZIP	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	CREB1	"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."	.	5ZKO; 5ZK1; 2LXT	MTMESGAENQQSGDAAVTEAENQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD	Literature-reported	cAMP-responsive element-binding protein (CREB) and cAMP co-regulate activator protein 1 (AP1)-dependent regeneration-associated gene expression and... J Biol Chem. 2014 Nov 21;289(47):32914-25.	.	bZIP	.	bZIP family.	.	.	bZIP transcription factor; pKID domain	PF00170; PF02173	PF00170; bZIP_1; PF02173; pKID	.	.	"hsa04022: cGMP-PKG signaling pathway; hsa04024: cAMP signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04152: AMPK signaling pathway; hsa04211: Longevity regulating pathway; hsa04261: Adrenergic signaling in cardiomyocytes; hsa04380: Osteoclast differentiation; hsa04612: Antigen processing and presentation; hsa04668: TNF signaling pathway; hsa04710: Circadian rhythm; hsa04713: Circadian entrainment; hsa04714: Thermogenesis; hsa04725: Cholinergic synapse; hsa04728: Dopaminergic synapse; hsa04911: Insulin secretion; hsa04915: Estrogen signaling pathway; hsa04916: Melanogenesis; hsa04918: Thyroid hormone synthesis; hsa04922: Glucagon signaling pathway; hsa04924: Renin secretion; hsa04925: Aldosterone synthesis and secretion; hsa04926: Relaxin signaling pathway; hsa04927: Cortisol synthesis and secretion; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04931: Insulin resistance; hsa04934: Cushing syndrome; hsa04935: Growth hormone synthesis, secretion and action; hsa04962: Vasopressin-regulated water reabsorption; hsa05016: Huntington disease; hsa05020: Prion disease; hsa05030: Cocaine addiction; hsa05031: Amphetamine addiction; hsa05034: Alcoholism; hsa05152: Tuberculosis; 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; hsa05203: Viral carcinogenesis; hsa05207: Chemical carcinogenesis - receptor activation; hsa05215: Prostate cancer"	R-HSA-111931: PKA-mediated phosphorylation of CREB; R-HSA-111932: CaMK IV-mediated phosphorylation of CREB; R-HSA-198693: AKT phosphorylates targets in the nucleus; R-HSA-199920: CREB phosphorylation; R-HSA-2151201: Transcriptional activation of mitochondrial biogenesis; R-HSA-2197563: NOTCH2 intracellular domain regulates transcription; R-HSA-375165: NCAM signaling for neurite out-growth; R-HSA-400253: Circadian Clock; R-HSA-442720: CREB1 phosphorylation through the activation of Adenylate Cyclase; R-HSA-442729: CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde; R-HSA-442742: CREB1 phosphorylation through NMDA receptor-mediated activation of RAS signaling; R-HSA-5674400: Constitutive Signaling by AKT1 E17K in Cancer; R-HSA-881907: Gastrin-CREB signalling pathway via PKC and MAPK; R-HSA-9022692: Regulation of MECP2 expression and activity; R-HSA-9022699: MECP2 regulates neuronal receptors and channels; R-HSA-9022702: MECP2 regulates transcription of neuronal ligands; R-HSA-9022707: MECP2 regulates transcription factors; R-HSA-9031628: NGF-stimulated transcription; R-HSA-9609690: HCMV Early Events; R-HSA-9616222: Transcriptional regulation of granulopoiesis; R-HSA-9634638: Estrogen-dependent nuclear events downstream of ESR-membrane signaling; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production; R-HSA-9664323: FCGR3A-mediated IL10 synthesis; R-HSA-9707616: Heme signaling	.	P16220
TTFRCTK	CREB-binding protein (CREBBP)	Q92793	CBP_HUMAN	Acyltransferase	CREBbinding protein; CBP	CREBBP	"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."	EC 2.3.1.48	6FRF; 6FR0; 6FQU; 6FQT; 6FQO	MAENLLDGPPNPKRAKLSSPGFSANDSTDFGSLFDLENDLPDELIPNGGELGLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSANMASLSAMGKSPLSQGDSSAPSLPKQAASTSGPTPAASQALNPQAQKQVGLATSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLINQASQGQAQVMNGSLGAAGRGRGAGMPYPTPAMQGASSSVLAETLTQVSPQMTGHAGLNTAQAGGMAKMGITGNTSPFGQPFSQAGGQPMGATGVNPQLASKQSMVNSLPTFPTDIKNTSVTNVPNMSQMQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGTGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPQTHQQMRTLNPLGNNPMNIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGTLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPLNMLGPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSEMMEEDLQGASQVKEETDIAEQKSEPMEVDEKKPEVKVEVKEEEESSSNGTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDCPPPNTRRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIIHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETTEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVINTLPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVSMSPAGFPSVARTQPPTTVSTGKPTSQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRVNINNSMPPGRTGMGTPGSQMAPVSLNVPRPNQVSGPVMPSMPPGQWQQAPLPQQQPMPGLPRPVISMQAQAAVAGPRMPSVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPQQQAMGGLNPQGQALNIMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQHLPLQGSSMGQMAAQMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSIDQGHLGNPEQSAMLPQLNTPSRSALSSELSLVGDTTGDTLEKFVEGL	Clinical trial	Inhibition of Wnt/beta-catenin/CREB binding protein (CBP) signaling reverses pulmonary fibrosis. Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14309-14.	19	EC:2.3	Acyltransferase	.	2.3.1.48 	Acyltransferases	"Bromodomain; Creb binding; Domain of Unknown Function (DUF902); Histone acetylation protein; KIX domain; TAZ zinc finger; Zinc finger, ZZ type"	PF00439; PF09030; PF06001; PF08214; PF02172; PF02135; PF00569	PF00439; Bromodomain; PF09030; Creb_binding; PF06001; DUF902; PF08214; HAT_KAT11; PF02172; KIX; PF02135; zf-TAZ; PF00569; ZZ	.	.	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	"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"	.	Q92793
TTA7YIZ	Corticoliberin (CRH)	P06850	CRF_HUMAN	.	Corticotropin-releasing hormone; Corticotropin-releasing factor; Corticotropin releasing hormone; Corticotropin; CRF; Adrenocorticotropic hormone	CRH	"Induces NLRP6 in intestinal epithelial cells, hence may influence gut microbiota profile. Hormone regulating the release of corticotropin from pituitary gland."	.	3EHU; 3EHT; 1GOE; 1GO9	MRLPLLVSAGVLLVALLPCPPCRALLSRGPVPGARQAPQHPQPLDFFQPPPQSEQPQQPQARPVLLRMGEEYFLRLGNLNKSPAAPLSPASSLLAGGSGSRPSPEQATANFFRVLLQQLLLPRRSLDSPAALAERGARNALGGHQEAPERERRSEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEIIGK	Literature-reported	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	0	.	.	sauvagine/corticotropin-releasing factor/urotensin I family.	.	.	Corticotropin-releasing factor family	PF00473	PF00473; CRF	.	.	hsa04730:Long-term depression; hsa05034:Alcoholism	R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-418555:G alpha (s) signalling events	.	P06850
TT3PKZE	Corticotropin-releasing factor binding protein (CRHBP)	P24387	CRHBP_HUMAN	.	Corticotropin-releasing hormone-binding protein; Corticotropin-releasing factor-binding protein; CRH-BP; CRFBP; CRF-binding protein; CRF-BP	CRHBP	May prevent inappropriate pituitary-adrenal stimulation in pregnancy. Binds CRF and inactivates it.	.	.	MSPNFKLQCHFILIFLTALRGESRYLELREAADYDPFLLFSANLKRELAGEQPYRRALRCLDMLSLQGQFTFTADRPQLHCAAFFISEPEEFITIHYDQVSIDCQGGDFLKVFDGWILKGEKFPSSQDHPLPSAERYIDFCESGLSRRSIRSSQNVAMIFFRVHEPGNGFTLTIKTDPNLFPCNVISQTPNGKFTLVVPHQHRNCSFSIIYPVVIKISDLTLGHVNGLQLKKSSAGCEGIGDFVELLGGTGLDPSKMTPLADLCYPFHGPAQMKVGCDNTVVRMVSSGKHVNRVTFEYRQLEPYELENPNGNSIGEFCLSGL	Literature-reported	Corticotropin-releasing factor-binding protein ligand inhibitor blunts excessive weight gain in genetically obese Zucker rats and rats during nicot... Proc Natl Acad Sci U S A. 1996 Dec 24;93(26):15475-80.	.	.	CRF-binding protein family	CRF-binding protein family.	.	.	Corticotropin-releasing factor binding protein (CRF-BP)	PF05428	PF05428; CRF-BP	.	.	.	R-HSA-373080: Class B/2 (Secretin family receptors)	.	P24387
TT7EFHR	Corticotropin-releasing factor receptor 1 (CRHR1)	P34998	CRFR1_HUMAN	GPCR secretin	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	CRHR1	"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."	.	4Z9G; 4K5Y; 3EHU; 3EHT; 3EHS	MGGHPQLRLVKALLLLGLNPVSASLQDQHCESLSLASNISGLQCNASVDLIGTCWPRSPAGQLVVRPCPAFFYGVRYNTTNNGYRECLANGSWAARVNYSECQEILNEEKKSKVHYHVAVIINYLGHCISLVALLVAFVLFLRLRPGCTHWGDQADGALEVGAPWSGAPFQVRRSIRCLRNIIHWNLISAFILRNATWFVVQLTMSPEVHQSNVGWCRLVTAAYNYFHVTNFFWMFGEGCYLHTAIVLTYSTDRLRKWMFICIGWGVPFPIIVAWAIGKLYYDNEKCWFGKRPGVYTDYIYQGPMILVLLINFIFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDEVSRVVFIYFNSFLESFQGFFVSVFYCFLNSEVRSAIRKRWHRWQDKHSIRARVARAMSIPTSPTRVSFHSIKQSTAV	Successful	A review of drug options in age-related macular degeneration therapy and potential new agents. Expert Opin Pharmacother. 2006 Dec;7(17):2355-68.	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04730:Long-term depression	R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-418555:G alpha (s) signalling events	.	P34998
TTIY658	Corticotropin-releasing factor receptor 2 (CRHR2)	Q13324	CRFR2_HUMAN	GPCR secretin	Corticotropin-releasinghormone receptor 2; CRHR2; CRH2 receptor; CRH-R 2; CRF2; CRF-R 2	CRHR2	"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."	.	3N96; 3N95; 3N93	MDAALLHSLLEANCSLALAEELLLDGWGPPLDPEGPYSYCNTTLDQIGTCWPRSAAGALVERPCPEYFNGVKYNTTRNAYRECLENGTWASKINYSQCEPILDDKQRKYDLHYRIALVVNYLGHCVSVAALVAAFLLFLALRSIRCLRNVIHWNLITTFILRNVMWFLLQLVDHEVHESNEVWCRCITTIFNYFVVTNFFWMFVEGCYLHTAIVMTYSTERLRKCLFLFIGWCIPFPIIVAWAIGKLYYENEQCWFGKEPGDLVDYIYQGPIILVLLINFVFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDDLSQIMFIYFNSFLQSFQGFFVSVFYCFFNGEVRSAVRKRWHRWQDHHSLRVPMARAMSIPTSPTRISFHSIKQTAAV	Clinical trial	Evolution of complementary peptide systems: teneurin C-terminal-associated peptides and corticotropin-releasing factor superfamilies. Ann N Y Acad Sci. 2009 Apr;1163:215-20.	21	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-418555:G alpha (s) signalling events	.	Q13324
TTDCO2A	Crithidia Tryparedoxin (Crithi TryX)	O96438	O96438_CRIFA	.	Tryparedoxin I	Crithi TryX	Mediates the flux of reduction equivalents from the unique redox metabolite trypanothione	.	1QK8; 1OKD; 1O8X; 1O8W; 1O85	MSGLDKYLPGIEKLRRGDGEVEVKSLAGKLVFFYFSASWCPPCRGFTPQLIEFYDKFHESKNFEVVFCTWDEEEDGFAGYFAKMPWLAVPFAQSEAVQKLSKHFNVESIPTLIGVDADSGDVVTTRARATLVKDPEGEQFPWKDAP	Literature-reported	Catalytic characteristics of tryparedoxin. Eur J Biochem. 1997 Sep 15;248(3):913-8.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTFEUYR	Proto-oncogene c-Crk (c-Crk)	P46108	CRK_HUMAN	.	P38; Adapter molecule crk	CRK	"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."	.	6ATV; 5UL6; 2MS4; 2EYZ; 2EYY	MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGDQEFDSLPALLEFYKIHYLDTTTLIEPVSRSRQGSGVILRQEEAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYRPASASVSALIGGNQEGSHPQPLGGPEPGPYAQPSVNTPLPNLQNGPIYARVIQKRVPNAYDKTALALEVGELVKVTKINVSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS	Literature-reported	NCBI GEO: archive for functional genomics data sets--update. Nucleic Acids Res. 2013 Jan;41(Database issue):D991-5.	.	.	Transmembrane protein	CRK family.	.	.	SH2 domain; SH3 domain; Variant SH3 domain	PF00017; PF00018; PF07653	PF00017; SH2; PF00018; SH3_1; PF07653; SH3_2	.	.	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	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	.	P46108
TT6YF5K	Cytokine receptor-like factor 1 (CRLF1)	O75462	CRLF1_HUMAN	Type I cytokine receptor family. Type 3 subfamily	ZcytoR5; Cytokine-like factor 1; CLF-1	CRLF1	"Cytokine receptor subunit, possibly playing a regulatory role in the immune system and during fetal development. May be involved in nervous system development."	.	.	MPAGRRGPAAQSARRPPPLLPLLLLLCVLGAPRAGSGAHTAVISPQDPTLLIGSSLLATCSVHGDPPGATAEGLYWTLNGRRLPPELSRVLNASTLALALANLNGSRQRSGDNLVCHARDGSILAGSCLYVGLPPEKPVNISCWSKNMKDLTCRWTPGAHGETFLHTNYSLKYKLRWYGQDNTCEEYHTVGPHSCHIPKDLALFTPYEIWVEATNRLGSARSDVLTLDILDVVTTDPPPDVHVSRVGGLEDQLSVRWVSPPALKDFLFQAKYQIRYRVEDSVDWKVVDDVSNQTSCRLAGLKPGTVYFVQVRCNPFGIYGSKKAGIWSEWSHPTAASTPRSERPGPGGGACEPRGGEPSSGPVRRELKQFLGWLKKHAYCSNLSFRLYDQWRAWMQKSHKTRNQDEGILPSGRRGTARGPAR	Literature-reported	Role of cytokine receptor-like factor 1 in hepatic stellate cells and fibrosis. World J Hepatol. 2012 Dec 27;4(12):356-64.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-6788467: IL-6-type cytokine receptor ligand interactions; R-HSA-9020956: Interleukin-27 signaling	.	O75462
TTRMZ0N	Thymic stromal lymphoprotein receptor (CRLF2)	Q9HC73	CRLF2_HUMAN	Cytokine receptor	Thymic stromal lymphopoietin protein receptor; TSLP receptor; ILXR; Cytokine receptorlike factor 2; Cytokine receptorlike 2; CRLF2	CRLF2	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.	.	5J12; 5J11	MGRLVLLWGAAVFLLGGWMALGQGGAAEGVQIQIIYFNLETVQVTWNASKYSRTNLTFHYRFNGDEAYDQCTNYLLQEGHTSGCLLDAEQRDDILYFSIRNGTHPVFTASRWMVYYLKPSSPKHVRFSWHQDAVTVTCSDLSYGDLLYEVQYRSPFDTEWQSKQENTCNVTIEGLDAEKCYSFWVRVKAMEDVYGPDTYPSDWSEVTCWQRGEIRDACAETPTPPKPKLSKFILISSLAILLMVSLLLLSLWKLWRVKKFLIPSVPDPKSIFPGLFEIHQGNFQEWITDTQNVAHLHKMAGAEQESGPEEPLVVQLAKTEAESPRMLDPQTEEKEASGGSLQLPHQPLQGGDVVTIGGFTFVMNDRSYVAL	Literature-reported	CRLF2 expression associates with ICN1 stabilization in T-cell acute lymphoblastic leukemia. Genes Chromosomes Cancer. 2019 Jun;58(6):396-401.	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04630: JAK-STAT signaling pathway	R-HSA-1266695: Interleukin-7 signaling	.	Q9HC73
TTWRN6M	CRP messenger RNA (CRP mRNA)	P02741	CRP_HUMAN	mRNA target	PTX1 (mRNA); C-reactive protein (mRNA)	CRP	"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."	.	3PVO; 3PVN; 3L2Y; 1LJ7; 1GNH	MEKLLCFLVLTSLSHAFGQTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFYTELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGSEILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKSLKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVNMWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFTKPQLWP	Clinical trial	"Antisense oligonucleotides on neurobehavior, respiratory, and cardiovascular function, and hERG channel current studies. J Pharmacol Toxicol Methods. 2014 Jan-Feb;69(1):49-60."	21	mRNA	mRNA target	.	.	.	Pentaxin family	PF00354	PF00354; Pentaxin	.	.	.	R-HSA-173623: Classical antibody-mediated complement activation	.	P02741
TTG01U6	HUMAN c-reactive protein (CRP)	P02741	CRP_HUMAN	Pentraxin family	C reactive protein	CRP	"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."	.	1B09; 1GNH; 1LJ7; 3L2Y; 3PVN	MEKLLCFLVLTSLSHAFGQTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFYTELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGSEILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKSLKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVNMWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFTKPQLWP	.	Biomarkers heavily used as diagnostic tools in COVID-19 trials. News Report.14 Apr 2020	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-173623: Classical antibody-mediated complement activation	.	P02741
TT4GO0F	CREB-regulated transcription coactivator 1 (TORC1)	Q6UUV9	CRTC1_HUMAN	.	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	CRTC1	"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."	.	.	MATSNNPRKFSEKIALHNQKQAEETAAFEEVMKDLSLTRAARLQLQKSQYLQLGPSRGQYYGGSLPNVNQIGSGTMDLPFQTPFQSSGLDTSRTTRHHGLVDRVYRERGRLGSPHRRPLSVDKHGRQADSCPYGTMYLSPPADTSWRRTNSDSALHQSTMTPTQPESFSSGSQDVHQKRVLLLTVPGMEETTSEADKNLSKQAWDTKKTGSRPKSCEVPGINIFPSADQENTTALIPATHNTGGSLPDLTNIHFPSPLPTPLDPEEPTFPALSSSSSTGNLAANLTHLGIGGAGQGMSTPGSSPQHRPAGVSPLSLSTEARRQQASPTLSPLSPITQAVAMDALSLEQQLPYAFFTQAGSQQPPPQPQPPPPPPPASQQPPPPPPPQAPVRLPPGGPLLPSASLTRGPQPPPLAVTVPSSLPQSPPENPGQPSMGIDIASAPALQQYRTSAGSPANQSPTSPVSNQGFSPGSSPQHTSTLGSVFGDAYYEQQMAARQANALSHQLEQFNMMENAISSSSLYSPGSTLNYSQAAMMGLTGSHGSLPDSQQLGYASHSGIPNIILTVTGESPPSLSKELTSSLAGVGDVSFDSDSQFPLDELKIDPLTLDGLHMLNDPDMVLADPATEDTFRMDRL	Clinical trial	"Palomid 529, a novel small-molecule drug, is a TORC1/TORC2 inhibitor that reduces tumor growth, tumor angiogenesis, and vascular permeability. Cancer Res. 2008 Nov 15;68(22):9551-7."	.	.	Transducer of regulated CREB	TORC family.	.	.	"Transducer of regulated CREB activity, C terminus; Transducer of regulated CREB activity middle domain; Transducer of regulated CREB activity, N terminus"	PF12886; PF12885; PF12884	PF12886; TORC_C; PF12885; TORC_M; PF12884; TORC_N	.	.	hsa05166: Human T-cell leukemia virus 1 infection	R-HSA-2151201: Transcriptional activation of mitochondrial biogenesis; R-HSA-400253: Circadian Clock; R-HSA-9707616: Heme signaling	.	Q6UUV9
TTFWETR	CREB-regulated transcription coactivator 2 (TORC2)	Q53ET0	CRTC2_HUMAN	Transducer of regulated CREB	Transducer of regulated cAMP response elementbinding protein 2; Transducer of CREB protein 2; CRTC2; CREBregulated transcription coactivator 2	CRTC2	"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)."	.	4HTM	MATSGANGPGSATASASNPRKFSEKIALQKQRQAEETAAFEEVMMDIGSTRLQAQKLRLAYTRSSHYGGSLPNVNQIGSGLAEFQSPLHSPLDSSRSTRHHGLVERVQRDPRRMVSPLRRYTRHIDSSPYSPAYLSPPPESSWRRTMAWGNFPAEKGQLFRLPSALNRTSSDSALHTSVMNPSPQDTYPGPTPPSILPSRRGGILDGEMDPKVPAIEENLLDDKHLLKPWDAKKLSSSSSRPRSCEVPGINIFPSPDQPANVPVLPPAMNTGGSLPDLTNLHFPPPLPTPLDPEETAYPSLSGGNSTSNLTHTMTHLGISRGMGLGPGYDAPGLHSPLSHPSLQSSLSNPNLQASLSSPQPQLQGSHSHPSLPASSLARHVLPTTSLGHPSLSAPALSSSSSSSSTSSPVLGAPSYPASTPGASPHHRRVPLSPLSLLAGPADARRSQQQLPKQFSPTMSPTLSSITQGVPLDTSKLSTDQRLPPYPYSSPSLVLPTQPHTPKSLQQPGLPSQSCSVQSSGGQPPGRQSHYGTPYPPGPSGHGQQSYHRPMSDFNLGNLEQFSMESPSASLVLDPPGFSEGPGFLGGEGPMGGPQDPHTFNHQNLTHCSRHGSGPNIILTGDSSPGFSKEIAAALAGVPGFEVSAAGLELGLGLEDELRMEPLGLEGLNMLSDPCALLPDPAVEESFRSDRLQ	Literature-reported	"Palomid 529, a novel small-molecule drug, is a TORC1/TORC2 inhibitor that reduces tumor growth, tumor angiogenesis, and vascular permeability. Cancer Res. 2008 Nov 15;68(22):9551-7."	.	.	.	.	.	.	.	.	.	.	.	hsa04151: PI3K-Akt signaling pathway; hsa04152: AMPK signaling pathway; hsa04922: Glucagon signaling pathway; hsa04931: Insulin resistance; hsa05166: Human T-cell leukemia virus 1 infection	R-HSA-2151201: Transcriptional activation of mitochondrial biogenesis; R-HSA-400253: Circadian Clock; R-HSA-9707616: Heme signaling	.	Q53ET0
TT5MLZR	Cryptochrome circadian clock 1 (CRY1)	Q16526	CRY1_HUMAN	.	PHLL1; Cryptochrome-1	CRY1	"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."	.	.	MGVNAVHWFRKGLRLHDNPALKECIQGADTIRCVYILDPWFAGSSNVGINRWRFLLQCLEDLDANLRKLNSRLFVIRGQPADVFPRLFKEWNITKLSIEYDSEPFGKERDAAIKKLATEAGVEVIVRISHTLYDLDKIIELNGGQPPLTYKRFQTLISKMEPLEIPVETITSEVIEKCTTPLSDDHDEKYGVPSLEELGFDTDGLSSAVWPGGETEALTRLERHLERKAWVANFERPRMNANSLLASPTGLSPYLRFGCLSCRLFYFKLTDLYKKVKKNSSPPLSLYGQLLWREFFYTAATNNPRFDKMEGNPICVQIPWDKNPEALAKWAEGRTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWISWEEGMKVFEELLLDADWSINAGSWMWLSCSSFFQQFFHCYCPVGFGRRTDPNGDYIRRYLPVLRGFPAKYIYDPWNAPEGIQKVAKCLIGVNYPKPMVNHAEASRLNIERMKQIYQQLSRYRGLGLLASVPSNPNGNGGFMGYSAENIPGCSSSGSCSQGSGILHYAHGDSQQTHLLKQGRSSMGTGLSGGKRPSQEEDTQSIGPKVQRQSTN	Preclinical	Development of Small-Molecule Cryptochrome Stabilizer Derivatives as Modulators of the Circadian Clock. ChemMedChem. 2015 Sep;10(9):1489-97.	0	.	.	DNA photolyase class-1 family.	.	.	DNA photolyase; FAD binding domain of DNA photolyase	PF00875; PF03441	PF00875; DNA_photolyase; PF03441; FAD_binding_7	.	.	hsa04710: Circadian rhythm	R-HSA-400253: Circadian Clock	.	Q16526
TTAO58M	Cryptochrome-2 (CRY2)	Q49AN0	CRY2_HUMAN	.	.	CRY2	"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)."	.	.	MAATVATAAAVAPAPAPGTDSASSVHWFRKGLRLHDNPALLAAVRGARCVRCVYILDPWFAASSSVGINRWRFLLQSLEDLDTSLRKLNSRLFVVRGQPADVFPRLFKEWGVTRLTFEYDSEPFGKERDAAIMKMAKEAGVEVVTENSHTLYDLDRIIELNGQKPPLTYKRFQAIISRMELPKKPVGLVTSQQMESCRAEIQENHDETYGVPSLEELGFPTEGLGPAVWQGGETEALARLDKHLERKAWVANYERPRMNANSLLASPTGLSPYLRFGCLSCRLFYYRLWDLYKKVKRNSTPPLSLFGQLLWREFFYTAATNNPRFDRMEGNPICIQIPWDRNPEALAKWAEGKTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWVSWESGVRVFDELLLDADFSVNAGSWMWLSCSAFFQQFFHCYCPVGFGRRTDPSGDYIRRYLPKLKAFPSRYIYEPWNAPESIQKAAKCIIGVDYPRPIVNHAETSRLNIERMKQIYQQLSRYRGLCLLASVPSCVEDLSHPVAEPSSSQAGSMSSAGPRPLPSGPASPKRKLEAAEEPPGEELSKRARVAELPTPELPSKDA	Preclinical	Circadian rhythm as a therapeutic target. Nat Rev Drug Discov. 2021 Apr;20(4):287-307.	.	.	.	.	.	.	.	.	.	.	.	hsa04710: Circadian rhythm	R-HSA-400253: Circadian Clock	.	Q49AN0
TT8CWJG	Alpha-crystallin A chain (CRYAA)	P02489	CRYAA_HUMAN	Heat shock protein	HspB4; Heat shock protein beta-4; CRYA1	CRYAA	"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."	.	.	MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFCGPKIQTGLDATHAERAIPVSREEKPTSAPSS	Literature-reported	Identification of the HSPB4/TLR2/NF-B axis in macrophage as a therapeutic target for sterile inflammation of the cornea. EMBO Mol Med. 2012 May;4(5):435-48.	.	Heat shock protein	Heat shock protein	small heat shock protein (HSP20) family.	.	.	"Alpha crystallin A chain, N terminal; Hsp20/alpha crystallin family"	PF00525; PF00011	PF00525; Crystallin; PF00011; HSP20	.	.	hsa04141: Protein processing in endoplasmic reticulum	.	.	P02489
TT7RUHB	Alpha(B)-crystallin	.	CRYAB_HUMAN	Single Protein	Renal carcinoma antigen NY-REN-27; Alpha-crystallin B chain; Rosenthal fiber component; Heat shock protein beta-5; HspB5	CRYAB	"May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions."	.	.	MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P02511
TTDS503	Beta-crystallin B1 (CRYBB1)	P53674	CRBB1_HUMAN	.	CRYBB1; Beta B1-crystallin	CRYBB1	Crystallins are the dominant structural components of the vertebrate eye lens.	.	1OKI	MSQAAKASASATVAVNPGPDTKGKGAPPAGTSPSPGTTLAPTTVPITSAKAAELPPGNYRLVVFELENFQGRRAEFSGECSNLADRGFDRVRSIIVSAGPWVAFEQSNFRGEMFILEKGEYPRWNTWSSSYRSDRLMSFRPIKMDAQEHKISLFEGANFKGNTIEIQGDDAPSLWVYGFSDRVGSVKVSSGTWVGYQYPGYRGYQYLLEPGDFRHWNEWGAFQPQMQSLRRLRDKQWHLEGSFPVLATEPPK	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P53674
TT0F5P8	Cryptosporidium Pyruvate:ferredoxin oxidoreductase (Crypto CpPNO)	Q968X7	PNO_CRYPV	Aldehyde/oxo donor oxidoreductase	Pyruvate:NADP+ oxidoreductase; PFOR; CpPNO	Crypto CpPNO	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.	EC 1.2.1.51	.	MGEKEIVDGCVAACHIAYACSEVAFTYPITPSSTISEVADSWMSRGRRNIFDQVVSVVEMQSEMGSAGALHGSLSVGCSTTTFTASQGLLLMIPNMYKIAGELWPCVFHVTARAIATSSLSIFGDHNDIMAARQTGWAFLGAMTVQEVMDLALVSHVSTFECSVPFVNFFDGFRTSHELQKIDMISYETIKKIFPYEKLKEFRERALNPTHPTLRGTATSSDVYFQLAEARNKYYESTPDIVQSVMDRLAKLIGRSYHLFDYYGHPDAEFLIVVMGSGGLTIEEMIDYLMEKSNEKVGMIKVRLFRPWSIDAFVKKIPKTTKRITVLERCKESGSLGEPLCLDVSTSIMRSELSSNNILVLGGRYGLASKEFTPGMALAVWENMISENPINNFSVGIDDDVTFKSLFVRQPRLDLLTSETKQCLFWGLGSDGTVSANKNAIKIIGESTDLQVQGYFAYDAKKAGGATMSHLRFGPKPIKSAYLLQRCDYVAVHHPSYVHKFDVLENIKQGGCFVLNCPWSTLEELNHELPSKIKHQIASRDVKFYVIDAQRIAQESNLGRRINNILMVVFFSLTNIIPLDLAIKLVKEAIKKTYGKKGDAVVNSNWKAVDLTLESLIQISYDKSQWISKDKCGEKSLPATAVETGNKDQEITKSTVLKQKPEHDVNQFVKDILGPVNALKGDELPVSMFEPTGTVPLGTTAYEKRGIAMSIPIVDMNKCTQCNYCSIVCPHAAIRPFLLDEAEFKNAPETMHIPKAKGGQEFSSYYYRIQVTPLDCTGCELCVHACPDDALHMEGLQKMEAVEKTHWDYLIGLPNKAEKFDRTTVKGSQFQQPLLEFSAACEGCGETPYVKLLTQLFGERMVIANATGCSSIWGASYPSVPYTKNQKGYGPAWGNSLFEDNAEYGLGMVVGYRQRRDRFRELVSNEILKDITEEEEFLKDDNASVQGRNEIITKYDHLKDYLRSWLKNIRNGEACQSLFEEISKLLEDNLINSNNFAQVLKKDRIELLEKLYDSRDLIPKISHWIVGGDGWAYDIGYAGLDHVLSFGEDVNIIILDTEVYSNTGGQASKSTPFGAIAKFAQSGNLRQKKDIGSIAMEYGSVYVASVALGANYSQTIKSLLEAEKYPGTSLIVAYSTCIEHGYTKYNLQQESVKLAVESGYWPLYRYNPELVRTEVVDNLTTIVSSGFTLDSKKVKVDIENFLKRENRFLQLIRSNPELASMAKDKLKAHSDKRFQKMKDMSENVTVTALKDQIKKLKDQLISIQNASKTGELAASGLINADLFIEQEMHVLYGTETGNSEEVAQYIQSQLVSRGYSSSSLNLDDLDIDEFLNPDKFSTVIIVTSTSGQGEFPGSSGILYEALLKKHLENQDDKFCSFMRFGIFGLGDSNYVFFNEAAKKWDKLLLDCGAVRIGAVGMGDDQSEEKYETELIEWLPDYLQLINAPEPKHDEKSEIPKATTFKVTILDSCRNDILNESTGTLCEKLDENNNIGNSHYKPIIPPNSVLLPVIENKRITNQDYDKDVRHIVFKLIGDGGDTPSLSYCLGDSLALYGQNPVNEAIKAIEMFGYNPYSLLRLSINEENEANNTNKVNQRYSSLFGYDITVLQLFVECLDLWGKPNRKFFQEFYRYCSNPEEKIQAKKWAQNEGKKLIEEFSSKTGTYLDVFKMFESARPTLAQLLDIVPFIKSRSYSIASCNKFVNGEKIELCVGIVDWKLESGEIRYGQCTGFLNRLPILDSESKIDSIPRLPSNIKASAFNLPFDYRSPVIMACMGTGIAPFRAFVQNKKYIRDVLKEEIGPVILYFGCRYYDNDYLYREELENYVKEGVITSLNIAFSRDPKGYKTSNCENIRYAQKMYVQHLMLENSQEIYENMIEKCGYFYLCGTKQVPIDIRKAIIQIIIKHSSTTEQVTSEEDANSILNSIQIMGRYNVEAWS	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	Q968X7
TTP6UO8	Quinone oxidoreductase (CRYZ)	Q08257	QOR_HUMAN	.	Zeta-crystallin; NADPH:quinone reductase; CRYZ	CRYZ	"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."	EC 1.6.5.5	1YB5	MATGQKLMRAVRVFEFGGPEVLKLRSDIAVPIPKDHQVLIKVHACGVNPVETYIRSGTYSRKPLLPYTPGSDVAGVIEAVGDNASAFKKGDRVFTSSTISGGYAEYALAADHTVYKLPEKLDFKQGAAIGIPYFTAYRALIHSACVKAGESVLVHGASGGVGLAACQIARAYGLKILGTAGTEEGQKIVLQNGAHEVFNHREVNYIDKIKKYVGEKGIDIIIEMLANVNLSKDLSLLSHGGRVIVVGSRGTIEINPRDTMAKESSIIGVTLFSSTKEEFQQYAAALQAGMEIGWLKPVIGSQYPLEKVAEAHENIIHGSGATGKMILLL	Literature-reported	NADPH/quinone oxidoreductase is a priority target of glioblastoma chemotherapy. Int J Oncol. 2000 Feb;16(2):295-303.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q08257
TTZA6B3	Citrate synthase (CS)	O75390	CISY_HUMAN	Acyltransferase	"Citrate synthase, mitochondrial; Citrate (Si)-synthase"	CS	"extracellular exosome, mitochondrial matrix, mitochondrion, nucleus, citrate (Si)-synthase activity, RNA binding, carbohydrate metabolic process, tricarboxylic acid cycle."	EC 2.3.3.1	5UZR; 5UZQ; 5UZP	MALLTAAARLLGTKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGEEPLPEGLFWLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAQGISRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNFTNMLGYTDHQFTELTRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSKSG	Literature-reported	STAT3 Regulation of Citrate Synthase Is Essential during the Initiation of Lymphocyte Cell Growth. Cell Rep. 2017 May 2;19(5):910-918.	.	EC:2.3	Acyltransferase	citrate synthase family.	2.3.3.1	Acyltransferases	"Citrate synthase, C-terminal domain"	PF00285	PF00285; Citrate_synt	.	.	hsa00020: Citrate cycle (TCA cycle); hsa00630: Glyoxylate and dicarboxylate metabolism; hsa01100: Metabolic pathways; hsa01200: Carbon metabolism; hsa01210: 2-Oxocarboxylic acid metabolism; hsa01230: Biosynthesis of amino acids	R-HSA-1268020: Mitochondrial protein import; R-HSA-71403: Citric acid cycle (TCA cycle)	MetaCyc:ENSG00000062485-MON	O75390
TTTRULD	Exportin-2 (CSE1L)	P55060	XPO2_HUMAN	.	Importin-alpha re-exporter; Exp2; Chromosome segregation 1-like protein; Cellular apoptosis susceptibility protein; CSE1L	CSE1L	"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. ."	.	.	MELSDANLQTLTEYLKKTLDPDPAIRRPAEKFLESVEGNQNYPLLLLTLLEKSQDNVIKVCASVTFKNYIKRNWRIVEDEPNKICEADRVAIKANIVHLMLSSPEQIQKQLSDAISIIGREDFPQKWPDLLTEMVNRFQSGDFHVINGVLRTAHSLFKRYRHEFKSNELWTEIKLVLDAFALPLTNLFKATIELCSTHANDASALRILFSSLILISKLFYSLNFQDLPEFFEDNMETWMNNFHTLLTLDNKLLQTDDEEEAGLLELLKSQICDNAALYAQKYDEEFQRYLPRFVTAIWNLLVTTGQEVKYDLLVSNAIQFLASVCERPHYKNLFEDQNTLTSICEKVIVPNMEFRAADEEAFEDNSEEYIRRDLEGSDIDTRRRAACDLVRGLCKFFEGPVTGIFSGYVNSMLQEYAKNPSVNWKHKDAAIYLVTSLASKAQTQKHGITQANELVNLTEFFVNHILPDLKSANVNEFPVLKADGIKYIMIFRNQVPKEHLLVSIPLLINHLQAESIVVHTYAAHALERLFTMRGPNNATLFTAAEIAPFVEILLTNLFKALTLPGSSENEYIMKAIMRSFSLLQEAIIPYIPTLITQLTQKLLAVSKNPSKPHFNHYMFEAICLSIRITCKANPAAVVNFEEALFLVFTEILQNDVQEFIPYVFQVMSLLLETHKNDIPSSYMALFPHLLQPVLWERTGNIPALVRLLQAFLERGSNTIASAAADKIPGLLGVFQKLIASKANDHQGFYLLNSIIEHMPPESVDQYRKQIFILLFQRLQNSKTTKFIKSFLVFINLYCIKYGALALQEIFDGIQPKMFGMVLEKIIIPEIQKVSGNVEKKICAVGITKLLTECPPMMDTEYTKLWTPLLQSLIGLFELPEDDTIPDEEHFIDIEDTPGYQTAFSQLAFAGKKEHDPVGQMVNNPKIHLAQSLHKLSTACPGRVPSMVSTSLNAEALQYLQGYLQAASVTLL	Literature-reported	Highly-purified exosomes and shed microvesicles isolated from the human colon cancer cell line LIM1863 by sequential centrifugal ultrafiltration ar... Methods. 2015 Oct 1;87:11-25.	.	.	.	.	.	.	.	.	.	.	.	hsa03013: Nucleocytoplasmic transport; hsa05132: Salmonella infection	.	.	P55060
TT0IQER	Macrophage colony-stimulating factor 1 (CSF1)	P09603	CSF1_HUMAN	.	Processed macrophagecolony-stimulating factor 1; MCSF; M-CSF; Lanimostim; CSF-1	CSF1	"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."	.	5LXF; 4WRM; 4WRL; 4FA8; 4ADF	MTAPGAAGRCPPTTWLGSLLLLVCLLASRSITEEVSEYCSHMIGSGHLQSLQRLIDSQMETSCQITFEFVDQEQLKDPVCYLKKAFLLVQDIMEDTMRFRDNTPNAIAIVQLQELSLRLKSCFTKDYEEHDKACVRTFYETPLQLLEKVKNVFNETKNLLDKDWNIFSKNCNNSFAECSSQDVVTKPDCNCLYPKAIPSSDPASVSPHQPLAPSMAPVAGLTWEDSEGTEGSSLLPGEQPLHTVDPGSAKQRPPRSTCQSFEPPETPVVKDSTIGGSPQPRPSVGAFNPGMEDILDSAMGTNWVPEEASGEASEIPVPQGTELSPSRPGGGSMQTEPARPSNFLSASSPLPASAKGQQPADVTGTALPRVGPVRPTGQDWNHTPQKTDHPSALLRDPPEPGSPRISSLRPQGLSNPSTLSAQPQLSRSHSSGSVLPLGELEGRRSTRDRRSPAEPEGGPASEGAARPLPRFNSVPLTDTGHERQSEGSFSPQLQESVFHLLVPSVILVLLAVGGLLFYRWRRRSHQEPQRADSPLEQPEGSPLTQDDRQVELPV	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	Macrophage colony stimulating factor-1 (CSF-1)	PF05337	PF05337; CSF-1	.	.	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	R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-449836: Other interleukin signaling; R-HSA-6783783: Interleukin-10 signaling; R-HSA-8957275: Post-translational protein phosphorylation	.	P09603
TT7MRDV	Macrophage colony-stimulating factor 1 receptor (CSF1R)	P07333	CSF1R_HUMAN	Kinase	Proto-oncogene c-Fms; M-CSF-R; FMS; CSF-1R; CSF-1-R; CSF-1 receptor; CD115	CSF1R	"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."	EC 2.7.10.1	4WRM; 4WRL; 4R7I; 4R7H; 4LIQ	MGPGVLLLLLVATAWHGQGIPVIEPSVPELVVKPGATVTLRCVGNGSVEWDGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAQEVVVFEDQDALLPCLLTDPVLEAGVSLVRVRGRPLMRHTNYSFSPWHGFTIHRAKFIQSQDYQCSALMGGRKVMSISIRLKVQKVIPGPPALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDHQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGRYSFLARNPGGWRALTFELTLRYPPEVSVIWTFINGSGTLLCAASGYPQPNVTWLQCSGHTDRCDEAQVLQVWDDPYPEVLSQEPFHKVTVQSLLTVETLEHNQTYECRAHNSVGSGSWAFIPISAGAHTHPPDEFLFTPVVVACMSIMALLLLLLLLLLYKYKQKPKYQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDPEGGVDYKNIHLEKKYVRRDSGFSSQGVDTYVEMRPVSTSSNDSFSEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQAQEDRRERDYTNLPSSSRSGGSGSSSSELEEESSSEHLTCCEQGDIAQPLLQPNNYQFC	Successful	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	EC:2.7	Protein kinase superfamily. Tyr protein kinase family	protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Immunoglobulin domain; Protein tyrosine kinase	PF00047; PF07714	PF00047; ig; PF07714; Pkinase_Tyr	.	.	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	R-HSA-449836: Other interleukin signaling; R-HSA-8853884: Transcriptional Regulation by VENTX	.	P07333
TTVW6QL	CSF1R messenger RNA (CSF1R mRNA)	P07333	CSF1R_HUMAN	mRNA target	Proto-oncogene c-Fms (mRNA); M-CSF-R (mRNA); FMS (mRNA); CSF-1R (mRNA); CSF-1-R (mRNA); CSF-1 receptor (mRNA); CD115 (mRNA)	CSF1R	"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."	EC 2.7.10.1	4WRM; 4WRL; 4R7I; 4R7H; 4LIQ	MGPGVLLLLLVATAWHGQGIPVIEPSVPELVVKPGATVTLRCVGNGSVEWDGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAQEVVVFEDQDALLPCLLTDPVLEAGVSLVRVRGRPLMRHTNYSFSPWHGFTIHRAKFIQSQDYQCSALMGGRKVMSISIRLKVQKVIPGPPALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDHQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGRYSFLARNPGGWRALTFELTLRYPPEVSVIWTFINGSGTLLCAASGYPQPNVTWLQCSGHTDRCDEAQVLQVWDDPYPEVLSQEPFHKVTVQSLLTVETLEHNQTYECRAHNSVGSGSWAFIPISAGAHTHPPDEFLFTPVVVACMSIMALLLLLLLLLLYKYKQKPKYQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDPEGGVDYKNIHLEKKYVRRDSGFSSQGVDTYVEMRPVSTSSNDSFSEQDLDKEDGRPLELRDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGLNPYPGILVNSKFYKLVKDGYQMAQPAFAPKNIYSIMQACWALEPTHRPTFQQICSFLQEQAQEDRRERDYTNLPSSSRSGGSGSSSSELEEESSSEHLTCCEQGDIAQPLLQPNNYQFC	Literature-reported	Inhibition of colony-stimulating-factor-1 signaling in vivo with the orally bioavailable cFMS kinase inhibitor GW2580. Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):16078-83.	0	mRNA	mRNA target	.	.	.	Immunoglobulin domain; Protein tyrosine kinase	PF00047; PF07714	PF00047; ig; PF07714; Pkinase_Tyr	.	.	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	R-HSA-449836: Other interleukin signaling; R-HSA-8853884: Transcriptional Regulation by VENTX	.	P07333
TT731LW	Colony stimulating factor-1 receptor (CSF-1R)	E9PEK4	E9PEK4_HUMAN	.	Macrophage colony-stimulating factor 1 receptor	CSF1R	"A cytokine which controls the production, differentiation, and function of macrophages."	.	.	MGPGVLLLLLVATAWHGQGIPVIEPSVPELVVKPGATVTLRCVGNGSVEWDGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAQEVVVFEDQDALLPCLLTDPVLEAGVSLVRVRGRPLMRHTNYSFSPWHGFTIHRAKFIQSQDYQCSALMGGRKVMSISIRLKVQKVIPGPPALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLNLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDHQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGRYSFLARNPGGWRALTFELTLRYPPEVSVIWTFINGSGTLLCAASGYPQPNVTWLQCSGHTDRCDEAQVLQVWDDPYPEVLSQEPFHKVTVQSLLTVETLEHNQTYECRAHNSVGSGSWAFIPISAGAHTHPPDEFLFTPVVVACMSIMALLLLLLLLLLYKYKQKPKYQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGTVASPARVWTPMWR	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	21	.	.	.	.	.	Immunoglobulin domain; Protein tyrosine kinase	PF00047; PF07714	PF00047; ig; PF07714; Pkinase_Tyr	.	.	.	.	.	.
TTNYZG2	Granulocyte-macrophage colony-stimulating factor (CSF2)	P04141	CSF2_HUMAN	Growth factor	Sargramostim; Molgramostin; GM-CSF; Colony-stimulating factor; CSF2; CSF	CSF2	"Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes."	.	6BFS; 6BFQ; 5D72; 5D71; 5D70	MWLQSLLLLGTVACSISAPARSPSPSTQPWEHVNAIQEARRLLNLSRDTAAEMNETVEVISEMFDLQEPTCLQTRLELYKQGLRGSLTKLKGPLTMMASHYKQHCPPTPETSCATQIITFESFKENLKDFLLVIPFDCWEPVQE	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	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	"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"	.	P04141
TTPZGYX	HUMAN colony-stimulating factor (GM-CSF)	P04141	CSF2_HUMAN	Growth factor	Sargramostim; Molgramostin; GM-CSF; Colony-stimulating factor; CSF2; CSF	CSF2	"Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes."	.	6BFS; 6BFQ; 5D72; 5D71; 5D70	MWLQSLLLLGTVACSISAPARSPSPSTQPWEHVNAIQEARRLLNLSRDTAAEMNETVEVISEMFDLQEPTCLQTRLELYKQGLRGSLTKLKGPLTMMASHYKQHCPPTPETSCATQIITFESFKENLKDFLLVIPFDCWEPVQE	.	The anti-viral facet of anti-rheumatic drugs: Lessons from COVID-19. J Autoimmun. 2020 Apr 17:102468.	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04630: JAK-STAT signaling pathway; hsa04640: Hematopoietic cell lineage; hsa04650: Natural killer cell mediated cytotoxicity; hsa04657: IL-17 signaling pathway; hsa04660: T cell receptor signaling pathway; hsa04664: Fc epsilon RI signaling pathway; hsa04668: TNF signaling pathway; hsa05131: Shigellosis; hsa05146: Amoebiasis; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05171: Coronavirus disease - COVID-19; hsa05202: Transcriptional misregulation in cancer; hsa05221: Acute myeloid leukemia; hsa05323: Rheumatoid arthritis	"R-HSA-512988: Interleukin-3, Interleukin-5 and GM-CSF signaling; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6783783: Interleukin-10 signaling; R-HSA-8939246: RUNX1 regulates transcription of genes involved in differentiation of myeloid cells; R-HSA-912526: Interleukin receptor SHC signaling"	.	P04141
TT6MP2Z	GMCSFR-alpha (CSF2RA)	P15509	CSF2R_HUMAN	Type I cytokine receptor family	GMR; GM-CSFR; GM-CSF-R-alpha; CSF2RA; CDw116; CD116 antigen	CSF2RA	"Low affinity receptor for granulocyte-macrophage colony- stimulating factor. Transduces a signal that results in the proliferation, differentiation, and functional activation of hematopoietic cells."	.	4RS1; 4NKQ	MLLLVTSLLLCELPHPAFLLIPEKSDLRTVAPASSLNVRFDSRTMNLSWDCQENTTFSKCFLTDKKNRVVEPRLSNNECSCTFREICLHEGVTFEVHVNTSQRGFQQKLLYPNSGREGTAAQNFSCFIYNADLMNCTWARGPTAPRDVQYFLYIRNSKRRREIRCPYYIQDSGTHVGCHLDNLSGLTSRNYFLVNGTSREIGIQFFDSLLDTKKIERFNPPSNVTVRCNTTHCLVRWKQPRTYQKLSYLDFQYQLDVHRKNTQPGTENLLINVSGDLENRYNFPSSEPRAKHSVKIRAADVRILNWSSWSEAIEFGSDDGNLGSVYIYVLLIVGTLVCGIVLGFLFKRFLRIQRLFPPVPQIKDKLNDNHEVEDEIIWEEFTPEEGKGYREEVLTVKEIT	Successful	Stem cell transplantation and hematopoietic growth factors. Curr Hematol Rep. 2002 Nov;1(2):103-9.	34	.	.	.	.	.	.	.	.	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa05200:Pathways in cancer	"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"	.	P15509
TTPYS82	Interleukin 3 receptor (CSF2RB)	P32927	IL3RB_HUMAN	Cytokine receptor	IL5RB; IL3RB; IL-5R; GM-CSF/IL-3/IL-5 receptor common beta subunit; Cytokine receptor common subunit beta; CDw131; CD131	CSF2RB	"High affinity receptor for interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor."	.	5DWU; 4NKQ; 2NA9; 2NA8; 2GYS	MVLAQGLLSMALLALCWERSLAGAEETIPLQTLRCYNDYTSHITCRWADTQDAQRLVNVTLIRRVNEDLLEPVSCDLSDDMPWSACPHPRCVPRRCVIPCQSFVVTDVDYFSFQPDRPLGTRLTVTLTQHVQPPEPRDLQISTDQDHFLLTWSVALGSPQSHWLSPGDLEFEVVYKRLQDSWEDAAILLSNTSQATLGPEHLMPSSTYVARVRTRLAPGSRLSGRPSKWSPEVCWDSQPGDEAQPQNLECFFDGAAVLSCSWEVRKEVASSVSFGLFYKPSPDAGEEECSPVLREGLGSLHTRHHCQIPVPDPATHGQYIVSVQPRRAEKHIKSSVNIQMAPPSLNVTKDGDSYSLRWETMKMRYEHIDHTFEIQYRKDTATWKDSKTETLQNAHSMALPALEPSTRYWARVRVRTSRTGYNGIWSEWSEARSWDTESVLPMWVLALIVIFLTIAVLLALRFCGIYGYRLRRKWEEKIPNPSKSHLFQNGSAELWPPGSMSAFTSGSPPHQGPWGSRFPELEGVFPVGFGDSEVSPLTIEDPKHVCDPPSGPDTTPAASDLPTEQPPSPQPGPPAASHTPEKQASSFDFNGPYLGPPHSRSLPDILGQPEPPQEGGSQKSPPPGSLEYLCLPAGGQVQLVPLAQAMGPGQAVEVERRPSQGAAGSPSLESGGGPAPPALGPRVGGQDQKDSPVAIPMSSGDTEDPGVASGYVSSADLVFTPNSGASSVSLVPSLGLPSDQTPSLCPGLASGPPGAPGPVKSGFEGYVELPPIEGRSPRSPRNNPVPPEAKSPVLNPGERPADVSPTSPQPEGLLVLQQVGDYCFLPGLGPGPLSLRSKPSSPGPGPEIKNLDQAFQVKKPPGQAVPQVPVIQLFKALKQQDYLSLPPWEVNKPGEVC	Clinical trial	"Leridistim, a chimeric dual G-CSF and IL-3 receptor agonist, enhances multilineage hematopoietic recovery in a nonhuman primate model of radiation-induced myelosuppression: effect of schedule, dose, and route of administration. Stem Cells. 2001;19(6):522-33."	21	Cytokine receptor	Type I cytokine receptor	type I cytokine receptor family. Type 4 subfamily.	.	.	"Interleukin-6 receptor alpha chain, binding; Interferon-alpha/beta receptor, fibronectin type III"	PF09240; PF09294	PF09240; IL6Ra-bind; PF09294; Interfer-bind	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage	"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"	.	P32927
TTTFS8O	GM-CSFR/IL-3R/IL-5R common beta messenger RNA (CSF2RB mRNA)	P32927	IL3RB_HUMAN	mRNA target	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)	CSF2RB	"High affinity receptor for interleukin-3, interleukin-5 and granulocyte-macrophage colony-stimulating factor."	.	5DWU; 4NKQ; 2NA9; 2NA8; 2GYS	MVLAQGLLSMALLALCWERSLAGAEETIPLQTLRCYNDYTSHITCRWADTQDAQRLVNVTLIRRVNEDLLEPVSCDLSDDMPWSACPHPRCVPRRCVIPCQSFVVTDVDYFSFQPDRPLGTRLTVTLTQHVQPPEPRDLQISTDQDHFLLTWSVALGSPQSHWLSPGDLEFEVVYKRLQDSWEDAAILLSNTSQATLGPEHLMPSSTYVARVRTRLAPGSRLSGRPSKWSPEVCWDSQPGDEAQPQNLECFFDGAAVLSCSWEVRKEVASSVSFGLFYKPSPDAGEEECSPVLREGLGSLHTRHHCQIPVPDPATHGQYIVSVQPRRAEKHIKSSVNIQMAPPSLNVTKDGDSYSLRWETMKMRYEHIDHTFEIQYRKDTATWKDSKTETLQNAHSMALPALEPSTRYWARVRVRTSRTGYNGIWSEWSEARSWDTESVLPMWVLALIVIFLTIAVLLALRFCGIYGYRLRRKWEEKIPNPSKSHLFQNGSAELWPPGSMSAFTSGSPPHQGPWGSRFPELEGVFPVGFGDSEVSPLTIEDPKHVCDPPSGPDTTPAASDLPTEQPPSPQPGPPAASHTPEKQASSFDFNGPYLGPPHSRSLPDILGQPEPPQEGGSQKSPPPGSLEYLCLPAGGQVQLVPLAQAMGPGQAVEVERRPSQGAAGSPSLESGGGPAPPALGPRVGGQDQKDSPVAIPMSSGDTEDPGVASGYVSSADLVFTPNSGASSVSLVPSLGLPSDQTPSLCPGLASGPPGAPGPVKSGFEGYVELPPIEGRSPRSPRNNPVPPEAKSPVLNPGERPADVSPTSPQPEGLLVLQQVGDYCFLPGLGPGPLSLRSKPSSPGPGPEIKNLDQAFQVKKPPGQAVPQVPVIQLFKALKQQDYLSLPPWEVNKPGEVC	Literature-reported	NCBI GEO: archive for functional genomics data sets--update. Nucleic Acids Res. 2013 Jan;41(Database issue):D991-5.	.	mRNA	mRNA target	.	.	.	"Interleukin-6 receptor alpha chain, binding; Interferon-alpha/beta receptor, fibronectin type III"	PF09240; PF09294	PF09240; IL6Ra-bind; PF09294; Interfer-bind	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04210: Apoptosis; hsa04630: JAK-STAT signaling pathway; hsa05200: Pathways in cancer	"R-HSA-512988: Interleukin-3, Interleukin-5 and GM-CSF signaling; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-5683826: Surfactant metabolism; R-HSA-5688849: Defective CSF2RB causes SMDP5; R-HSA-5688890: Defective CSF2RA causes SMDP4; R-HSA-912526: Interleukin receptor SHC signaling"	.	P32927
TT5TQ2W	Granulocyte colony-stimulating factor (CSF3)	P09919	CSF3_HUMAN	Cytokine: interleukin	Pluripoietin; Lenograstim; G-CSF; CSF3	CSF3	"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."	.	5ZO6; 5GW9; 2D9Q; 1RHG; 1PGR	MAGPATQSPMKLMALQLLLWHSALWTVQEATPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLVSECATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP	Successful	Interleukin 3: from colony-stimulating factor to pluripotent immunoregulatory cytokine. Int J Immunopharmacol. 1992 Apr;14(3):421-30.	34	.	.	.	.	.	.	.	.	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa05144:Malaria	R-HSA-449836: Other interleukin signaling; R-HSA-6783783: Interleukin-10 signaling; R-HSA-9674555: Signaling by CSF3 (G-CSF); R-HSA-9705462: Inactivation of CSF3 (G-CSF) signaling	.	P09919
TTC70AJ	Granulocyte colony-stimulating factor receptor (G-CSF-R)	Q99062	CSF3R_HUMAN	Cytokine receptor	c-fms; GCSFR; GCSF receptor; G-CSF receptor; Fms proto-oncogene; CD114	CSF3R	"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."	.	2D9Q; 1AZ7	MARLGNCSLTWAALIILLLPGSLEECGHISVSAPIVHLGDPITASCIIKQNCSHLDPEPQILWRLGAELQPGGRQQRLSDGTQESIITLPHLNHTQAFLSCCLNWGNSLQILDQVELRAGYPPAIPHNLSCLMNLTTSSLICQWEPGPETHLPTSFTLKSFKSRGNCQTQGDSILDCVPKDGQSHCCIPRKHLLLYQNMGIWVQAENALGTSMSPQLCLDPMDVVKLEPPMLRTMDPSPEAAPPQAGCLQLCWEPWQPGLHINQKCELRHKPQRGEASWALVGPLPLEALQYELCGLLPATAYTLQIRCIRWPLPGHWSDWSPSLELRTTERAPTVRLDTWWRQRQLDPRTVQLFWKPVPLEEDSGRIQGYVVSWRPSGQAGAILPLCNTTELSCTFHLPSEAQEVALVAYNSAGTSRPTPVVFSESRGPALTRLHAMARDPHSLWVGWEPPNPWPQGYVIEWGLGPPSASNSNKTWRMEQNGRATGFLLKENIRPFQLYEIIVTPLYQDTMGPSQHVYAYSQEMAPSHAPELHLKHIGKTWAQLEWVPEPPELGKSPLTHYTIFWTNAQNQSFSAILNASSRGFVLHGLEPASLYHIHLMAASQAGATNSTVLTLMTLTPEGSELHIILGLFGLLLLLTCLCGTAWLCCSPNRKNPLWPSVPDPAHSSLGSWVPTIMEEDAFQLPGLGTPPITKLTVLEEDEKKPVPWESHNSSETCGLPTLVQTYVLQGDPRAVSTQPQSQSGTSDQVLYGQLLGSPTSPGPGHYLRCDSTQPLLAGLTPSPKSYENLWFQASPLGTLVTPAPSQEDDCVFGPLLNFPLLQGIRVHGMEALGSF	Successful	Evidence that the granulocyte colony-stimulating factor (G-CSF) receptor plays a role in the pharmacokinetics of G-CSF and PegG-CSF using a G-CSF-R KO model. Pharmacol Res. 2004 Jul;50(1):55-8.	34	Cytokine receptor	Cytokine receptor	type I cytokine receptor family. Type 2 subfamily.	.	.	Fibronectin type III domain; Ig-like C2-type domain	PF00041; PF06328	PF00041; fn3; PF06328; Lep_receptor_Ig	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa05200:Pathways in cancer	R-HSA-449836: Other interleukin signaling; R-HSA-9616222: Transcriptional regulation of granulopoiesis; R-HSA-9674555: Signaling by CSF3 (G-CSF); R-HSA-9705462: Inactivation of CSF3 (G-CSF) signaling	.	Q99062
TTX6F0Q	Tyrosine-protein kinase CSK (CSK)	P41240	CSK_HUMAN	Kinase	Protein-tyrosine kinase CYL; C-Src kinase	CSK	"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."	EC 2.7.10.2	3EAZ; 3EAC; 3D7U; 3D7T; 1CSK	MSAIQAAWPSGTECIAKYNFHGTAEQDLPFCKGDVLTIVAVTKDPNWYKAKNKVGREGIIPANYVQKREGVKAGTKLSLMPWFHGKITREQAERLLYPPETGLFLVRESTNYPGDYTLCVSCDGKVEHYRIMYHASKLSIDEEVYFENLMQLVEHYTSDADGLCTRLIKPKVMEGTVAAQDEFYRSGWALNMKELKLLQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKGGLYIVTEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYEVMKNCWHLDAAMRPSFLQLREQLEHIKTHELHL	Patented-recorded	Discovery of type II inhibitors of TGFbeta-activated kinase 1 (TAK1) and mitogen-activated protein kinase kinase kinase kinase 2 (MAP4K2). J Med Chem. 2015 Jan 8;58(1):183-96.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. CSK subfamily.	2.7.10.2 	Transferring phosphorus-containing groups	Protein tyrosine kinase; SH2 domain; SH3 domain	PF07714; PF00017; PF00018	PF07714; Pkinase_Tyr; PF00017; SH2; PF00018; SH3_1	.	.	hsa05120: Epithelial cell signaling in Helicobacter pylori infection	R-HSA-180292: GAB1 signalosome; R-HSA-202427: Phosphorylation of CD3 and TCR zeta chains; R-HSA-354192: Integrin signaling; R-HSA-389948: PD-1 signaling; R-HSA-5674135: MAP2K and MAPK activation; R-HSA-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-9013407: RHOH GTPase cycle; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants; R-HSA-9706369: Negative regulation of FLT3	.	P41240
TTFQEMX	Casein kinase I alpha (CSNK1A1)	P48729	KC1A_HUMAN	Kinase	Casein kinase I isoform alpha; CKI-alpha; CK1	CSNK1A1	"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."	EC 2.7.11.1	6GZD; 5FQD	MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGKQTDKTKSNMKGF	Clinical trial	Crystal structure of a conformation-selective casein kinase-1 inhibitor. J Biol Chem. 2000 Jun 30;275(26):20052-60.	0	EC:2.7	.	protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04310: Wnt signaling pathway; hsa04340: Hedgehog signaling pathway; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05165: Human papillomavirus infection; hsa05224: Breast cancer; hsa05225: Hepatocellular carcinoma; hsa05226: Gastric cancer	R-HSA-195253: Degradation of beta-catenin by the destruction complex; R-HSA-196299: Beta-catenin phosphorylation cascade; R-HSA-4641262: Disassembly of the destruction complex and recruitment of AXIN to the membrane; R-HSA-5339716: Signaling by GSK3beta mutants; R-HSA-5358747: CTNNB1 S33 mutants aren't phosphorylated; R-HSA-5358749: CTNNB1 S37 mutants aren't phosphorylated; R-HSA-5358751: CTNNB1 S45 mutants aren't phosphorylated; R-HSA-5358752: CTNNB1 T41 mutants aren't phosphorylated; R-HSA-5467337: APC truncation mutants have impaired AXIN binding; R-HSA-5467340: AXIN missense mutants destabilize the destruction complex; R-HSA-5467348: Truncations of AMER1 destabilize the destruction complex; R-HSA-5610783: Degradation of GLI2 by the proteasome; R-HSA-5610785: GLI3 is processed to GLI3R by the proteasome; R-HSA-5635838: Activation of SMO; R-HSA-9694631: Maturation of nucleoprotein	.	P48729
TTH30UI	Casein kinase I delta (CSNK1D)	P48730	KC1D_HUMAN	Kinase	Tau-protein kinase CSNK1D; HCKID; Casein kinase I isoform delta; CKId; CKI-delta	CSNK1D	"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."	EC 2.7.11.1	6GZM; 6F26; 6F1W; 5W4W; 5OKT	MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRNPATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNISSSDLTGRQDTSRMSTSQIPGRVASSGLQSVVHR	Preclinical	Crystal structure of a conformation-selective casein kinase-1 inhibitor. J Biol Chem. 2000 Jun 30;275(26):20052-60.	0	EC:2.7	.	protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04340: Hedgehog signaling pathway; hsa04390: Hippo signaling pathway; hsa04540: Gap junction; hsa04710: Circadian rhythm	R-HSA-204005: COPII-mediated vesicle transport; 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-380320: Recruitment of NuMA to mitotic centrosomes; R-HSA-400253: Circadian Clock; R-HSA-5620912: Anchoring of the basal body to the plasma membrane; R-HSA-6791226: Major pathway of rRNA processing in the nucleolus and cytosol; R-HSA-8854518: AURKA Activation by TPX2	.	P48730
TTA8PLI	Casein kinase I epsilon (CSNK1E)	P49674	KC1E_HUMAN	Kinase	Casein kinase I isoform epsilon; CKIe; CKI-epsilon	CSNK1E	"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."	EC 2.7.11.1	4HOK; 4HNI	MELRVGNKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGAARNPEDVDRERREHEREERMGQLRGSATRALPPGPPTGATANRLRSAAEPVASTPASRIQPAGNTSPRAISRVDRERKVSMRLHRGAPANVSSSDLTGRQEVSRIPASQTSVPFDHLGK	Successful	Crystal structure of a conformation-selective casein kinase-1 inhibitor. J Biol Chem. 2000 Jun 30;275(26):20052-60.	0	EC:2.7	.	protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04068: FoxO signaling pathway; hsa04310: Wnt signaling pathway; hsa04340: Hedgehog signaling pathway; hsa04390: Hippo signaling pathway; hsa04392: Hippo signaling pathway - multiple species; hsa04710: Circadian rhythm; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases	R-HSA-201688: WNT mediated activation of DVL; 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-380320: Recruitment of NuMA to mitotic centrosomes; R-HSA-400253: Circadian Clock; R-HSA-5620912: Anchoring of the basal body to the plasma membrane; R-HSA-6791226: Major pathway of rRNA processing in the nucleolus and cytosol; R-HSA-8854518: AURKA Activation by TPX2	.	P49674
TTQR5YD	Casein kinase I gamma-1 (CSNK1G1)	Q9HCP0	KC1G1_HUMAN	.	Casein kinase I isoform gamma-1; CKI-gamma 1	CSNK1G1	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.	EC 2.7.11.1	2CMW	MDHPSREKDERQRTTKPMAQRSAHCSRPSGSSSSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPIKSRAPQLHLEYRFYKQLGSAGEGLPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFTLKTVLMIAIQLLSRMEYVHSKNLIYRDVKPENFLIGRQGNKKEHVIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRNTPIEALCENFPEEMATYLRYVRRLDFFEKPDYEYLRTLFTDLFEKKGYTFDYAYDWVGRPIPTPVGSVHVDSGASAITRESHTHRDRPSQQQPLRNQVVSSTNGELNVDDPTGAHSNAPITAHAEVEVVEEAKCCCFFKRKRKKTAQRHK	Literature-reported	Identification and SAR of squarate inhibitors of mitogen activated protein kinase-activated protein kinase 2 (MK-2). Bioorg Med Chem. 2009 May 1;17(9):3342-51.	0	.	.	.	.	.	.	.	.	.	.	hsa04340: Hedgehog signaling pathway	.	.	Q9HCP0
TT0UZJ9	Casein kinase I gamma-2 (CSNK1G2)	P78368	KC1G2_HUMAN	Kinase	Casein kinase I isoform gamma-2; CKI-gamma 2; CK1G2	CSNK1G2	"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."	EC 2.7.11.1	2C47	MDFDKKGGKGETEEGRRMSKAGGGRSSHGIRSSGTSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPIKSRAPQLHLEYRFYKQLSATEGVPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFTLKTVLMIAIQLITRMEYVHTKSLIYRDVKPENFLVGRPGTKRQHAIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPEEMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRSGFVFDYEYDWAGKPLPTPIGTVHTDLPSQPQLRDKTQPHSKNQALNSTNGELNADDPTAGHSNAPITAPAEVEVADETKCCCFFKRRKRKSLQRHK	Literature-reported	Structure-Based Design of Potent and Selective CK1gamma Inhibitors. ACS Med Chem Lett. 2012 Oct 18;3(12):1059-64.	0	EC:2.7	.	protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Casein kinase 1 gamma C terminal; Protein kinase domain	PF12605; PF00069	PF12605; CK1gamma_C; PF00069; Pkinase	.	.	hsa04340: Hedgehog signaling pathway	R-HSA-1660661: Sphingolipid de novo biosynthesis; R-HSA-4641262: Disassembly of the destruction complex and recruitment of AXIN to the membrane	.	P78368
TT34L5N	Casein kinase I gamma-3 (CSNK1G3)	Q9Y6M4	KC1G3_HUMAN	.	Casein kinase I isoform gamma-3; CKI-gamma 3	CSNK1G3	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).	EC 2.7.11.1	6GRO; 4HGS; 4HGL; 4G17; 4G16	MENKKKDKDKSDDRMARPSGRSGHNTRGTGSSSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQVIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPEMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKGYMFDYEYDWIGKQLPTPVGAVQQDPALSSNREAHQHRDKMQQSKNQSADHRAAWDSQQANPHHLRAHLAADRHGGSVQVVSSTNGELNTDDPTAGRSNAPITAPTEVEVMDETKCCCFFKRRKRKTIQRHK	Literature-reported	"7-(4H-1,2,4-Triazol-3-yl)benzo[c][2,6]naphthyridines: a novel class of Pim kinase inhibitors with potent cell antiproliferative activity. Bioorg Med Chem Lett. 2011 Nov 15;21(22):6687-92."	0	.	.	.	.	.	.	.	.	.	.	hsa04340: Hedgehog signaling pathway	.	.	Q9Y6M4
TTER6YH	Casein kinase II alpha (CSNK2A1)	P68400	CSK21_HUMAN	Kinase	Protein kinase CK2; Casein kinase II subunit alpha; CK2A1; CK II alpha; CK II	CSNK2A1	"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."	EC 2.7.11.1	6Q4Q; 6Q38; 6HME; 6HBN; 6GMD	MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMGSSSMPGGSTPVSSANMMSGISSVPTPSPLGPLAGSPVIAAANPLGMPVPAAAGAQQ	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	19	EC:2.7	Kinase	protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	R-HSA-2514853:Condensation of Prometaphase Chromosomes	.	P68400
TT7GR5W	HUMAN casein kinase II alpha prime (CSNK2A2)	P19784	CSK22_HUMAN	Kinase	Casein kinase II subunit alpha'; CK2A2; CK II alpha'	CSNK2A2	"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."	EC 2.7.11.1	6QY9; 6HMQ; 6HMD; 6HMC; 6HMB	MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRREPFFHGQDNYDQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCADNAVLSSGLTAAR	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa03008: Ribosome biogenesis in eukaryotes; hsa04064: NF-kappa B signaling pathway; hsa04137: Mitophagy - animal; hsa04310: Wnt signaling pathway; hsa04520: Adherens junction; hsa05010: Alzheimer disease; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05162: Measles; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer	R-HSA-1483191: Synthesis of PC; R-HSA-201688: WNT mediated activation of DVL; R-HSA-2514853: Condensation of Prometaphase Chromosomes; R-HSA-445144: Signal transduction by L1; R-HSA-6804756: Regulation of TP53 Activity through Phosphorylation; R-HSA-6814122: Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding; R-HSA-8934903: Receptor Mediated Mitophagy; R-HSA-8939243: RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known; R-HSA-8948751: Regulation of PTEN stability and activity; R-HSA-9755511: KEAP1-NFE2L2 pathway	.	P19784
TTR93NU	Casein kinase II alpha prime (CSNK2A2)	P19784	CSK22_HUMAN	Kinase	Casein kinase II subunit alpha'; CK2A2; CK II alpha'	CSNK2A2	"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."	EC 2.7.11.1	6QY9; 6HMQ; 6HMD; 6HMC; 6HMB	MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRREPFFHGQDNYDQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCADNAVLSSGLTAAR	Patented-recorded	"CK2alpha and CK2alpha' subunits differ in their sensitivity to 4,5,6,7-tetrabromo- and 4,5,6,7-tetraiodo-1H-benzimidazole derivatives. Eur J Med Chem. 2012 Jan;47(1):345-50."	0	EC:2.7	.	protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa03008: Ribosome biogenesis in eukaryotes; hsa04064: NF-kappa B signaling pathway; hsa04137: Mitophagy - animal; hsa04310: Wnt signaling pathway; hsa04520: Adherens junction; hsa05010: Alzheimer disease; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05162: Measles; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer	R-HSA-1483191: Synthesis of PC; R-HSA-201688: WNT mediated activation of DVL; R-HSA-2514853: Condensation of Prometaphase Chromosomes; R-HSA-445144: Signal transduction by L1; R-HSA-6804756: Regulation of TP53 Activity through Phosphorylation; R-HSA-6814122: Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding; R-HSA-8934903: Receptor Mediated Mitophagy; R-HSA-8939243: RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known; R-HSA-8948751: Regulation of PTEN stability and activity; R-HSA-9755511: KEAP1-NFE2L2 pathway	.	P19784
TT7MYXI	Chondroitin sulfate proteoglycan 4 (CSPG4)	Q6UVK1	CSPG4_HUMAN	.	Melanoma-associated chondroitin sulfate proteoglycan; Melanoma chondroitin sulfate proteoglycan; MCSP; Chondroitin sulfate proteoglycan NG2	CSPG4	"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."	.	.	MQSGPRPPLPAPGLALALTLTMLARLASAASFFGENHLEVPVATALTDIDLQLQFSTSQPEALLLLAAGPADHLLLQLYSGRLQVRLVLGQEELRLQTPAETLLSDSIPHTVVLTVVEGWATLSVDGFLNASSAVPGAPLEVPYGLFVGGTGTLGLPYLRGTSRPLRGCLHAATLNGRSLLRPLTPDVHEGCAEEFSASDDVALGFSGPHSLAAFPAWGTQDEGTLEFTLTTQSRQAPLAFQAGGRRGDFIYVDIFEGHLRAVVEKGQGTVLLHNSVPVADGQPHEVSVHINAHRLEISVDQYPTHTSNRGVLSYLEPRGSLLLGGLDAEASRHLQEHRLGLTPEATNASLLGCMEDLSVNGQRRGLREALLTRNMAAGCRLEEEEYEDDAYGHYEAFSTLAPEAWPAMELPEPCVPEPGLPPVFANFTQLLTISPLVVAEGGTAWLEWRHVQPTLDLMEAELRKSQVLFSVTRGARHGELELDIPGAQARKMFTLLDVVNRKARFIHDGSEDTSDQLVLEVSVTARVPMPSCLRRGQTYLLPIQVNPVNDPPHIIFPHGSLMVILEHTQKPLGPEVFQAYDPDSACEGLTFQVLGTSSGLPVERRDQPGEPATEFSCRELEAGSLVYVHRGGPAQDLTFRVSDGLQASPPATLKVVAIRPAIQIHRSTGLRLAQGSAMPILPANLSVETNAVGQDVSVLFRVTGALQFGELQKQGAGGVEGAEWWATQAFHQRDVEQGRVRYLSTDPQHHAYDTVENLALEVQVGQEILSNLSFPVTIQRATVWMLRLEPLHTQNTQQETLTTAHLEATLEEAGPSPPTFHYEVVQAPRKGNLQLQGTRLSDGQGFTQDDIQAGRVTYGATARASEAVEDTFRFRVTAPPYFSPLYTFPIHIGGDPDAPVLTNVLLVVPEGGEGVLSADHLFVKSLNSASYLYEVMERPRHGRLAWRGTQDKTTMVTSFTNEDLLRGRLVYQHDDSETTEDDIPFVATRQGESSGDMAWEEVRGVFRVAIQPVNDHAPVQTISRIFHVARGGRRLLTTDDVAFSDADSGFADAQLVLTRKDLLFGSIVAVDEPTRPIYRFTQEDLRKRRVLFVHSGADRGWIQLQVSDGQHQATALLEVQASEPYLRVANGSSLVVPQGGQGTIDTAVLHLDTNLDIRSGDEVHYHVTAGPRWGQLVRAGQPATAFSQQDLLDGAVLYSHNGSLSPRDTMAFSVEAGPVHTDATLQVTIALEGPLAPLKLVRHKKIYVFQGEAAEIRRDQLEAAQEAVPPADIVFSVKSPPSAGYLVMVSRGALADEPPSLDPVQSFSQEAVDTGRVLYLHSRPEAWSDAFSLDVASGLGAPLEGVLVELEVLPAAIPLEAQNFSVPEGGSLTLAPPLLRVSGPYFPTLLGLSLQVLEPPQHGALQKEDGPQARTLSAFSWRMVEEQLIRYVHDGSETLTDSFVLMANASEMDRQSHPVAFTVTVLPVNDQPPILTTNTGLQMWEGATAPIPAEALRSTDGDSGSEDLVYTIEQPSNGRVVLRGAPGTEVRSFTQAQLDGGLVLFSHRGTLDGGFRFRLSDGEHTSPGHFFRVTAQKQVLLSLKGSQTLTVCPGSVQPLSSQTLRASSSAGTDPQLLLYRVVRGPQLGRLFHAQQDSTGEALVNFTQAEVYAGNILYEHEMPPEPFWEAHDTLELQLSSPPARDVAATLAVAVSFEAACPQRPSHLWKNKGLWVPEGQRARITVAALDASNLLASVPSPQRSEHDVLFQVTQFPSRGQLLVSEEPLHAGQPHFLQSQLAAGQLVYAHGGGGTQQDGFHFRAHLQGPAGASVAGPQTSEAFAITVRDVNERPPQPQASVPLRLTRGSRAPISRAQLSVVDPDSAPGEIEYEVQRAPHNGFLSLVGGGLGPVTRFTQADVDSGRLAFVANGSSVAGIFQLSMSDGASPPLPMSLAVDILPSAIEVQLRAPLEVPQALGRSSLSQQQLRVVSDREEPEAAYRLIQGPQYGHLLVGGRPTSAFSQFQIDQGEVVFAFTNFSSSHDHFRVLALARGVNASAVVNVTVRALLHVWAGGPWPQGATLRLDPTVLDAGELANRTGSVPRFRLLEGPRHGRVVRVPRARTEPGGSQLVEQFTQQDLEDGRLGLEVGRPEGRAPGPAGDSLTLELWAQGVPPAVASLDFATEPYNAARPYSVALLSVPEAARTEAGKPESSTPTGEPGPMASSPEPAVAKGGFLSFLEANMFSVIIPMCLVLLLLALILPLLFYLRKRNKTGKHDVQVLTAKPRNGLAGDTETFRKVEPGQAIPLTAVPGQGPPPGGQPDPELLQFCRTPNPALKNGQYWV	Literature-reported	CSPG4 protein as a new target for the antibody-based immunotherapy of triple-negative breast cancer. J Natl Cancer Inst. 2010 Oct 6;102(19):1496-512.	.	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-1971475: A tetrasaccharide linker sequence is required for GAG synthesis; R-HSA-2022870: Chondroitin sulfate biosynthesis; R-HSA-2022923: Dermatan sulfate biosynthesis; R-HSA-2024101: CS/DS degradation; R-HSA-3560783: Defective B4GALT7 causes EDS, progeroid type; R-HSA-3560801: Defective B3GAT3 causes JDSSDHD; R-HSA-3595172: Defective CHST3 causes SEDCJD; R-HSA-3595174: Defective CHST14 causes EDS, musculocontractural type; R-HSA-3595177: Defective CHSY1 causes TPBS; R-HSA-4420332: Defective B3GALT6 causes EDSP2 and SEMDJL1"	.	Q6UVK1
TTE5ITK	Cancer/testis antigen 1 (NY-ESO-1)	P78358	CTG1B_HUMAN	.	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	CTAG1A	"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."	.	6AVG; 6AVF; 6AT5; 3KLA; 3HAE	MQAEGRGTGGSTGDADGPGGPGIPDGPGGNAGGPGEAGATGGRGPRGAGAARASGPGGGAPRGPHGGAASGLNGCCRCGARGPESRLLEFYLAMPFATPMEAELARRSLAQDAPPLPVPGVLLKEFTVSGNILTIRLTAADHRQLQLSISSCLQQLSLLMWITQCFLPVFLAQPPSGQRR	Clinical trial	National Cancer Institute Drug Dictionary (drug id 651880).	21	.	.	CTAG/PCC1 family.	.	.	Transcription factor Pcc1	PF09341	PF09341; Pcc1	.	.	.	.	.	P78358
TTY0RZT	BORIS messenger RNA (CTCFL mRNA)	Q8NI51	CTCFL_HUMAN	mRNA target	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)	CTCFL	"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."	.	.	MAATEISVLSEQFTKIKELELMPEKGLKEEEKDGVCREKDHRSPSELEAERTSGAFQDSVLEEEVELVLAPSEESEKYILTLQTVHFTSEAVELQDMSLLSIQQQEGVQVVVQQPGPGLLWLEEGPRQSLQQCVAISIQQELYSPQEMEVLQFHALEENVMVASEDSKLAVSLAETTGLIKLEEEQEKNQLLAERTKEQLFFVETMSGDERSDEIVLTVSNSNVEEQEDQPTAGQADAEKAKSTKNQRKTKGAKGTFHCDVCMFTSSRMSSFNRHMKTHTSEKPHLCHLCLKTFRTVTLLRNHVNTHTGTRPYKCNDCNMAFVTSGELVRHRRYKHTHEKPFKCSMCKYASVEASKLKRHVRSHTGERPFQCCQCSYASRDTYKLKRHMRTHSGEKPYECHICHTRFTQSGTMKIHILQKHGENVPKYQCPHCATIIARKSDLRVHMRNLHAYSAAELKCRYCSAVFHERYALIQHQKTHKNEKRFKCKHCSYACKQERHMTAHIRTHTGEKPFTCLSCNKCFRQKQLLNAHFRKYHDANFIPTVYKCSKCGKGFSRWINLHRHSEKCGSGEAKSAASGKGRRTRKRKQTILKEATKGQKEAAKGWKEAANGDEAAAEEASTTKGEQFPGEMFPVACRETTARVKEEVDEGVTCEMLLNTMDK	Literature-reported	BORIS/CTCFL mRNA isoform expression and epigenetic regulation in epithelial ovarian cancer. Cancer Immun. 2013;13:6.	.	mRNA	mRNA target	.	.	.	"Zinc finger, C2H2 type"	PF00096	PF00096; zf-C2H2	.	.	.	.	.	Q8NI51
TTY85FG	Transcriptional repressor CTCFL (CTCFL)	Q8NI51	CTCFL_HUMAN	.	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	CTCFL	"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."	.	.	MAATEISVLSEQFTKIKELELMPEKGLKEEEKDGVCREKDHRSPSELEAERTSGAFQDSVLEEEVELVLAPSEESEKYILTLQTVHFTSEAVELQDMSLLSIQQQEGVQVVVQQPGPGLLWLEEGPRQSLQQCVAISIQQELYSPQEMEVLQFHALEENVMVASEDSKLAVSLAETTGLIKLEEEQEKNQLLAERTKEQLFFVETMSGDERSDEIVLTVSNSNVEEQEDQPTAGQADAEKAKSTKNQRKTKGAKGTFHCDVCMFTSSRMSSFNRHMKTHTSEKPHLCHLCLKTFRTVTLLRNHVNTHTGTRPYKCNDCNMAFVTSGELVRHRRYKHTHEKPFKCSMCKYASVEASKLKRHVRSHTGERPFQCCQCSYASRDTYKLKRHMRTHSGEKPYECHICHTRFTQSGTMKIHILQKHGENVPKYQCPHCATIIARKSDLRVHMRNLHAYSAAELKCRYCSAVFHERYALIQHQKTHKNEKRFKCKHCSYACKQERHMTAHIRTHTGEKPFTCLSCNKCFRQKQLLNAHFRKYHDANFIPTVYKCSKCGKGFSRWINLHRHSEKCGSGEAKSAASGKGRRTRKRKQTILKEATKGQKEAAKGWKEAANGDEAAAEEASTTKGEQFPGEMFPVACRETTARVKEEVDEGVTCEMLLNTMDK	Literature-reported	Targeting CTCFL/BORIS for the immunotherapy of cancer. Cancer Immunol Immunother. 2018 Dec;67(12):1955-1965.	.	.	CTCF zinc-finger protein family	CTCF zinc-finger protein family.	.	.	"Zinc finger, C2H2 type"	PF00096	PF00096; zf-C2H2	.	.	.	.	.	Q8NI51
TTHZAF0	Small CTD phosphatase 1	.	CTDS1_HUMAN	Single Protein	Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1; Nuclear LIM interactor-interacting factor 3; SCP1; Small C-terminal domain phosphatase 1; NLI-IF; NLI-interacting factor 3	CTDSP1	"Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells."	.	.	MDSSAVITQISKEEARGPLRGKGDQKSAASQKPRSRGILHSLFCCVCRDDGEALPAHSGAPLLVEENGAIPKQTPVQYLLPEAKAQDSDKICVVIDLDETLVHSSFKPVNNADFIIPVEIDGVVHQVYVLKRPHVDEFLQRMGELFECVLFTASLAKYADPVADLLDKWGAFRARLFRESCVFHRGNYVKDLSRLGRDLRRVLILDNSPASYVFHPDNAVPVASWFDNMSDTELHDLLPFFEQLSRVDDVYSVLRQPRPGS	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9GZU7
TTXGTZU	Cardiotrophin-1 (CTF1)	Q16619	CTF1_HUMAN	Cytokine: interleukin	CTF1; CT-1	CTF1	Induces cardiac myocyte hypertrophy in vitro. Binds to and activates the ILST/gp130 receptor.	.	.	MSRREGSLEDPQTDSSVSLLPHLEAKIRQTHSLAHLLTKYAEQLLQEYVQLQGDPFGLPSFSPPRLPVAGLSAPAPSHAGLPVHERLRLDAAALAALPPLLDAVCRRQAELNPRAPRLLRRLEDAARQARALGAAVEALLAALGAANRGPRAEPPAATASAASATGVFPAKVLGLRVCGLYREWLSRTEGDLGQLLPGGSA	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	17	.	.	.	.	.	.	.	.	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway	R-HSA-6788467: IL-6-type cytokine receptor ligand interactions	.	Q16619
TTCJVNE	CTGF messenger RNA (CTGF mRNA)	P29279	CTGF_HUMAN	mRNA target	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)	CTGF	"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."	.	.	MTAASMGPVRVAFVVLLALCSRPAVGQNCSGPCRCPDEPAPRCPAGVSLVLDGCGCCRVCAKQLGELCTERDPCDPHKGLFCHFGSPANRKIGVCTAKDGAPCIFGGTVYRSGESFQSSCKYQCTCLDGAVGCMPLCSMDVRLPSPDCPFPRRVKLPGKCCEEWVCDEPKDQTVVGPALAAYRLEDTFGPDPTMIRANCLVQTTEWSACSKTCGMGISTRVTNDNASCRLEKQSRLCMVRPCEADLEENIKKGKKCIRTPKISKPIKFELSGCTSMKTYRAKFCGVCTDGRCCTPHRTTTLPVEFKCPDGEVMKKNMMFIKTCACHYNCPGDNDIFESLYYRKMYGDMA	Clinical trial	"Clinical pipeline report, company report or official report of ISIS Pharmaceuticals (2011)."	21	mRNA	mRNA target	.	.	.	Cystine-knot domain; Insulin-like growth factor binding protein; Thrombospondin type 1 domain; von Willebrand factor type C domain	PF00007; PF00219; PF00090; PF00093	PF00007; Cys_knot; PF00219; IGFBP; PF00090; TSP_1; PF00093; VWC	.	.	hsa04390:Hippo signaling pathway	R-HSA-1989781:PPARA activates gene expression; R-HSA-2032785:YAP1- and WWTR1 (TAZ)-stimulated gene expression	.	.
TTSECX1	Connective tissue growth factor (CTGF)	P29279	CTGF_HUMAN	.	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	CTGF	"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."	.	.	MTAASMGPVRVAFVVLLALCSRPAVGQNCSGPCRCPDEPAPRCPAGVSLVLDGCGCCRVCAKQLGELCTERDPCDPHKGLFCHFGSPANRKIGVCTAKDGAPCIFGGTVYRSGESFQSSCKYQCTCLDGAVGCMPLCSMDVRLPSPDCPFPRRVKLPGKCCEEWVCDEPKDQTVVGPALAAYRLEDTFGPDPTMIRANCLVQTTEWSACSKTCGMGISTRVTNDNASCRLEKQSRLCMVRPCEADLEENIKKGKKCIRTPKISKPIKFELSGCTSMKTYRAKFCGVCTDGRCCTPHRTTTLPVEFKCPDGEVMKKNMMFIKTCACHYNCPGDNDIFESLYYRKMYGDMA	Clinical trial	Cyr61/CTGF/Nov family proteins in gastric carcinogenesis. World J Gastroenterol. 2014 February 21; 20(7): 1694-1700.	21	.	CCN intercellular signaling protein	CCN family.	.	.	Cystine-knot domain; Insulin-like growth factor binding protein; Thrombospondin type 1 domain; von Willebrand factor type C domain	PF00007; PF00219; PF00090; PF00093	PF00007; Cys_knot; PF00219; IGFBP; PF00090; TSP_1; PF00093; VWC	.	.	hsa04390:Hippo signaling pathway	R-HSA-1989781:PPARA activates gene expression; R-HSA-2032785:YAP1- and WWTR1 (TAZ)-stimulated gene expression	.	.
TTLQUZS	Cystathionine gamma-lyase (CTH)	P32929	CGL_HUMAN	.	Gamma-cystathionase; Cysteine-protein sulfhydrase	CTH	"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."	EC 4.4.1.1	5TT2; 5TSU; 5EIG; 3ELP; 3COG	MQEKDASSQGFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGAPGQHSGFEYSRSGNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYGGTNRYFRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQKVIDIEGCAHIVHKHGDIILVVDNTFMSPYFQRPLALGADISMYSATKYMNGHSDVVMGLVSVNCESLHNRLRFLQNSLGAVPSPIDCYLCNRGLKTLHVRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQHELVKRQCTGCTGMVTFYIKGTLQHAEIFLKNLKLFTLAESLGGFESLAELPAIMTHASVLKNDRDVLGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPPSGSHS	Patented-recorded	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1444).	0	.	.	.	.	.	.	.	.	.	.	"hsa00260: Glycine, serine and threonine metabolism; hsa00270: Cysteine and methionine metabolism; hsa00450: Selenocompound metabolism; hsa01100: Metabolic pathways; hsa01230: Biosynthesis of amino acids"	"R-HSA-1614558: Degradation of cysteine and homocysteine; R-HSA-1614603: Cysteine formation from homocysteine; R-HSA-2408508: Metabolism of ingested SeMet, Sec, MeSec into H2Se"	MetaCyc:HS04050-MON	P32929
TTI2S1D	Cytotoxic T-lymphocyte protein 4 (CTLA-4)	P16410	CTLA4_HUMAN	Immunoglobulin	Cytotoxic T-lymphocyte-associated antigen 4; CTLA-4; CD152	CTLA4	"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."	.	5XJ3; 5TRU; 5GGV; 3OSK; 3BX7	MACLGFQRHKAQLNLATRTWPCTLLFFLLFIPVFCKAMHVAQPAVVLASSRGIASFVCEYASPGKATEVRVTVLRQADSQVTEVCAATYMMGNELTFLDDSICTGTSSGNQVNLTIQGLRAMDTGLYICKVELMYPPPYYLGIGNGTQIYVIDPEPCPDSDFLLWILAAVSSGLFFYSFLLTAVSLSKMLKKRSPLTTGVYVKMPPTEPECEKQFQPYFIPIN	Successful	Mullard A: 2010 FDA drug approvals. Nat Rev Drug Discov. 2011 Feb;10(2):82-5.	34	Immunoglobulin	Immunoglobulin	.	.	.	Immunoglobulin V-set domain	PF07686	PF07686; V-set	.	.	hsa04514:Cell adhesion molecules (CAMs); hsa04660:T cell receptor signaling pathway; hsa05320:Autoimmune thyroid disease; hsa05323:Rheumatoid arthritis	R-HSA-389513:CTLA4 inhibitory signaling	.	P16410
TTRPKQG	Beta-catenin (CTNNB1)	P35222	CTNB1_HUMAN	Beta-catenin	Wnt/beta-catenin signaling pathway; PRO2286; OK/SW-cl.35; Catenin beta-1; CTNNB	CTNNB1	"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."	.	6M94; 6M93; 6M92; 6M91; 6M90	MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL	Successful	"Endostar, a modified recombinant human endostatin, suppresses angiogenesis through inhibition of Wnt/beta-catenin signaling pathway. PLoS One. 2014 Sep 18;9(9):e107463."	34	Beta-catenin	.	beta-catenin family.	.	.	Armadillo/beta-catenin-like repeat	PF00514	PF00514; Arm	.	.	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)	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	.	P35222
TT1W2ZS	Cystinosin (CTNS)	O60931	CTNS_HUMAN	.	.	CTNS	"Cystine/H(+) symporter that mediates export of cystine, the oxidized dimer of cysteine, from lysosomes (PubMed:11689434, PubMed:18337546, PubMed:22232659, PubMed:29467429, PubMed:33208952, PubMed:15128704). Plays an important role in melanin synthesis by catalyzing cystine export from melanosomes, possibly by inhibiting pheomelanin synthesis (PubMed:22649030). In addition to cystine export, also acts as a positive regulator of mTORC1 signaling in kidney proximal tubular cells, via interactions with components of the v-ATPase and Ragulator complexes (By similarity). Also involved in small GTPase-regulated vesicle trafficking and lysosomal localization of LAMP2A, independently of cystine transporter activity (By similarity). {ECO:0000250|UniProtKB:P57757, ECO:0000269|PubMed:11689434, ECO:0000269|PubMed:15128704, ECO:0000269|PubMed:18337546, ECO:0000269|PubMed:22232659, ECO:0000269|PubMed:22649030, ECO:0000269|PubMed:29467429, ECO:0000269|PubMed:33208952}."	.	8DKE;8DKI;8DKM;8DKW;8DKX;8DYP	MIRNWLTIFILFPLKLVEKCESSVSLTVPPVVKLENGSSTNVSLTLRPPLNATLVITFEITFRSKNITILELPDEVVVPPGVTNSSFQVTSQNVGQLTVYLHGNHSNQTGPRIRFLVIRSSAISIINQVIGWIYFVAWSISFYPQVIMNWRRKSVIGLSFDFVALNLTGFVAYSVFNIGLLWVPYIKEQFLLKYPNGVNPVNSNDVFFSLHAVVLTLIIIVQCCLYERGGQRVSWPAIGFLVLAWLFAFVTMIVAAVGVTTWLQFLFCFSYIKLAVTLVKYFPQAYMNFYYKSTEGWSIGNVLLDFTGGSFSLLQMFLQSYNNDQWTLIFGDPTKFGLGVFSIVFDVVFFIQHFCLYRKRPGYDQLN	Clinical trial	ClinicalTrials.gov (NCT05146830) A Long-Term Follow-Up Study of Participants With Cystinosis Who Previously Received CTNS-RD-04. U.S.National Institutes of Health.	.	.	.	.	.	.	.	.	.	.	.	hsa:1497	R-HSA-425393;R-HSA-5223345;	.	O60931;
TTN12BZ	CTP synthase (CTPS1)	P17812	PYRG1_HUMAN	Carbon-nitrogen ligase	Uridine triphosphate aminase; UTP:ammonia ligase (ADP-forming); UTP--ammonia ligase; Cytidine triphosphate synthetase; Cytidine 5'-triphosphate synthetase; CTPS1; CTP synthetase	CTPS1	"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."	EC 6.3.4.2	5U03; 2VO1	MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFVLDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDAIQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHVSLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQVICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCSIALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQKLCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDANSTEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRHRFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPYFGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD	Clinical trial	Molecular approaches for the treatment of hemorrhagic fever virus infections. Antiviral Res. 1993 Sep;22(1):45-75.	17	.	.	.	.	.	.	.	.	.	.	hsa00240:Pyrimidine metabolism; hsa01100:Metabolic pathways	R-HSA-499943: Interconversion of nucleotide di- and triphosphates	MetaCyc:HS10382-MON	P17812
TT3RMNA	Chymotrypsin-C (CLCR)	Q99895	CTRC_HUMAN	.	Caldecrin; CLCR	CTRC	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.	EC 3.4.21.2	4H4F	MLGITVLAALLACASSCGVPSFPPNLSARVVGGEDARPHSWPWQISLQYLKNDTWRHTCGGTLIASNFVLTAAHCISNTRTYRVAVGKNNLEVEDEEGSLFVGVDTIHVHKRWNALLLRNDIALIKLAEHVELSDTIQVACLPEKDSLLPKDYPCYVTGWGRLWTNGPIADKLQQGLQPVVDHATCSRIDWWGFRVKKTMVCAGGDGVISACNGDSGGPLNCQLENGSWEVFGIVSFGSRRGCNTRKKPVVYTRVSAYIDWINEKMQL	Patented-recorded	P1 Phenethyl peptide boronic acid inhibitors of HCV NS3 protease. Bioorg Med Chem Lett. 2002 Nov 4;12(21):3199-202.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q99895
TT5NILS	Cathepsin A (CTSA)	P10619	PPGB_HUMAN	Peptidase	Protective protein for betagalactosidase; Protective protein cathepsin A; PPCA; Lysosomal protective protein 20 kDa chain; Lysosomal protective protein; Carboxypeptidase L; Carboxypeptidase C; CTSA	CTSA	"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."	EC 3.4.16.5	4MWT; 4MWS; 4CIB; 4CIA; 4CI9	MIRAAPPPLFLLLLLLLLLVSWASRGEAAPDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGVTLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVGNSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLRSGDKVRMDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMNSQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHMVPTDKPLAAFTMFSRFLNKQPY	Clinical trial	"Tolerability, safety and pharmacokinetics of the novel Cathepsin A inhibitor SAR164653 in healthy subjects.Clinical Pharmacology in Drug Development 05/2015."	17	.	.	.	.	.	.	.	.	.	.	hsa04142:Lysosome; hsa04614:Renin-angiotensin system	R-HSA-1660662:Glycosphingolipid metabolism; R-HSA-2132295:MHC class II antigen presentation; R-HSA-4085001:Sialic acid metabolism	.	P10619
TTF2LRI	Cathepsin B (CTSB)	P07858	CATB_HUMAN	Peptidase	Ctsb; Cathepsins B; Cathepsin-B; Cathepsin B1; CPSB; APPS; APP secretase	CTSB	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.	EC 3.4.22.1	6AY2; 5MBM; 5MBL; 3PBH; 3K9M	MWQLWASLCCLLVLANARSRPSFHPLSDELVNYVNKRNTTWQAGHNFYNVDMSYLKRLCGTFLGGPKPPQRVMFTEDLKLPASFDAREQWPQCPTIKEIRDQGSCGSCWAFGAVEAISDRICIHTNAHVSVEVSAEDLLTCCGSMCGDGCNGGYPAEAWNFWTRKGLVSGGLYESHVGCRPYSIPPCEHHVNGSRPPCTGEGDTPKCSKICEPGYSPTYKQDKHYGYNSYSVSNSEKDIMAEIYKNGPVEGAFSVYSDFLLYKSGVYQHVTGEMMGGHAIRILGWGVENGTPYWLVANSWNTDWGDNGFFKILRGQDHCGIESEVVAGIPRTDQYWEKI	Preclinical	Cathepsin B and L inhibitors: a patent review (2010 - present).Expert Opin Ther Pat. 2017 Jun;27(6):643-656.	15.5	EC:3.4	Peptidase	.	3.4.22.1 	Acting on peptide bonds (peptidases)	Papain family cysteine protease; Peptidase family C1 propeptide	PF00112; PF08127	PF00112; Peptidase_C1; PF08127; Propeptide_C1	.	.	hsa04142:Lysosome; hsa04612:Antigen processing and presentation	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	.	P07858
TT4H0V2	Dipeptidyl peptidase I (CTSC)	P53634	CATC_HUMAN	Peptidase	Dipeptidyl transferase; Dipeptidyl peptidase 1; DPPI; DPP-I; Cysteine protease dipeptidyl peptidase I; Cathepsin J; Cathepsin C; CPPI	CTSC	"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."	EC 3.4.14.1	4OEM; 4OEL; 4CDF; 4CDE; 4CDD	MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNIAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGGFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYHHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGENGYFRIRRGTDECAIESIAVAATPIPKL	Clinical trial	"ClinicalTrials.gov (NCT02058407) A Study to Evaluate the Safety, Tolerability, Pharmacokinetics (PK), Pharmacodynamics (PD) and Food Effect of Single or Repeat Doses of GSK2793660 in Healthy Subjects. U.S. National Institutes of Health."	17	EC:3.4	Peptidase	.	3.4.14.1	Acting on peptide bonds (peptidases)	Cathepsin C exclusion domain; Papain family cysteine protease	PF08773; PF00112	PF08773; CathepsinC_exc; PF00112; Peptidase_C1	.	.	hsa04142:Lysosome	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	MetaCyc:HS03265-MON	P53634
TTQ9J6R	HUMAN dipeptidyl peptidase 1 (CTSC)	P53634	CATC_HUMAN	Peptidase	Dipeptidyl transferase; Dipeptidyl peptidase 1; DPPI; DPP-I; Cysteine protease dipeptidyl peptidase I; Cathepsin J; Cathepsin C; CPPI	CTSC	"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."	EC 3.4.14.1	4OEM; 4OEL; 4CDF; 4CDE; 4CDD	MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNIAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGGFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYHHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGENGYFRIRRGTDECAIESIAVAATPIPKL	.	"Brensocatib (Formerly INS1007) to be Studied in Patients with Severe COVID-19 in Investigator-Initiated Trial. Apr 23, 2020."	.	.	.	.	.	.	.	.	.	.	.	hsa04142: Lysosome; hsa04210: Apoptosis	R-HSA-204005: COPII-mediated vesicle transport; R-HSA-2132295: MHC class II antigen presentation; R-HSA-5694530: Cargo concentration in the ER; R-HSA-6798695: Neutrophil degranulation	MetaCyc:HS03265-MON	P53634
TTPT2QI	Cathepsin D (CTSD)	P07339	CATD_HUMAN	Peptidase	CPSD; CD	CTSD	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.	EC 3.4.23.5	4OD9; 4OC6; 4OBZ; 1LYW; 1LYB	MQPSSLLPLALCLLAAPASALVRIPLHKFTSIRRTMSEVGGSVEDLIAKGPVSKYSQAVPAVTEGPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCQSASSASALGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGRYYTVFDRDNNRVGFAEAARL	Clinical trial	Synthesis and structure activity relationships of novel small molecule cathepsin D inhibitors. Bioorg Med Chem Lett. 1999 Sep 6;9(17):2531-6.	16	EC:3.4	Peptidase	peptidase A1 family.	3.4.23.5	Acting on peptide bonds (peptidases)	A1 Propeptide ; Eukaryotic aspartyl protease	PF07966; PF00026	PF07966; A1_Propeptide; PF00026; Asp	.	.	hsa04071:Sphingolipid signaling pathway; hsa04142:Lysosome; hsa05152:Tuberculosis	R-HSA-1442490:Collagen degradation; R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins; R-HSA-2132295:MHC class II antigen presentation	MetaCyc:HS04183-MON	P07339
TTLXC4Q	Cathepsin E (CTSE)	P14091	CATE_HUMAN	Peptidase	Cathepsin E	CTSE	"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."	EC 3.4.23.34	1TZS; 1LCG	MKTLLLLLLVLLELGEAQGSLHRVPLRRHPSLKKKLRARSQLSEFWKSHNLDMIQFTESCSMDQSAKEPLINYLDMEYFGTISIGSPPQNFTVIFDTGSSNLWVPSVYCTSPACKTHSRFQPSQSSTYSQPGQSFSIQYGTGSLSGIIGADQVSVEGLTVVGQQFGESVTEPGQTFVDAEFDGILGLGYPSLAVGGVTPVFDNMMAQNLVDLPMFSVYMSSNPEGGAGSELIFGGYDHSHFSGSLNWVPVTKQAYWQIALDNIQVGGTVMFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGAAPVDGEYAVECANLNVMPDVTFTINGVPYTLSPTAYTLLDFVDGMQFCSSGFQGLDIHPPAGPLWILGDVFIRQFYSVFDRGNNRVGLAPAVP	Literature-reported	Specificity in the binding of inhibitors to the active site of human/primate aspartic proteinases: analysis of P2-P1-P1'-P2' variation. J Med Chem. 1993 Sep 3;36(18):2614-20.	0	.	.	.	.	.	.	.	.	.	.	hsa04142: Lysosome	R-HSA-2132295: MHC class II antigen presentation	.	P14091
TTJOKD1	Cathepsin F (CTSF)	Q9UBX1	CATF_HUMAN	Peptidase	CATSF	CTSF	Has also been implicated in tumor invasion and metastasis. Thiol protease which is believed to participate in intracellular degradation and turnover of proteins.	EC 3.4.22.41	1M6D; 1D5U	MAPWLQLLSLLGLLPGAVAAPAQPRAASFQAWGPPSPELLAPTRFALEMFNRGRAAGTRAVLGLVRGRVRRAGQGSLYSLEATLEEPPCNDPMVCRLPVSKKTLLCSFQVLDELGRHVLLRKDCGPVDTKVPGAGEPKSAFTQGSAMISSLSQNHPDNRNETFSSVISLLNEDPLSQDLPVKMASIFKNFVITYNRTYESKEEARWRLSVFVNNMVRAQKIQALDRGTAQYGVTKFSDLTEEEFRTIYLNTLLRKEPGNKMKQAKSVGDLAPPEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKMDKACMGGLPSNAYSAIKNLGGLETEDDYSYQGHMQSCNFSAEKAKVYINDSVELSQNEQKLAAWLAKRGPISVAINAFGMQFYRHGISRPLRPLCSPWLIDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGSGACGVNTMASSAVVD	Patented-recorded	Cathepsin B and L inhibitors: a patent review (2010 - present).Expert Opin Ther Pat. 2017 Jun;27(6):643-656.	15.5	EC:3.4	Peptidase	.	3.4.22.41	Acting on peptide bonds (peptidases)	Cathepsin propeptide inhibitor domain (I29); Papain family cysteine protease	PF08246; PF00112	PF08246; Inhibitor_I29; PF00112; Peptidase_C1	.	.	hsa04142:Lysosome	R-HSA-2132295:MHC class II antigen presentation	.	Q9UBX1
TTQAJF1	Cathepsin G (CTSG)	P08311	CATG_HUMAN	Peptidase	CG	CTSG	"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."	EC 3.4.21.20	1T32; 1KYN; 1CGH; 1AU8	MQPLLLLLAFLLPTGAEAGEIIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQRRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGDSGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMRSFKLLDQMETPL	Clinical trial	"Discovery of potent, selective, orally active, nonpeptide inhibitors of human mast cell chymase. J Med Chem. 2007 Apr 19;50(8):1727-30."	21	EC:3.4	Peptidase	peptidase S1 family.	3.4.21.20	Acting on peptide bonds (peptidases)	Trypsin	PF00089	PF00089; Trypsin	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04142:Lysosome; hsa04614:Renin-angiotensin system; hsa05146:Amoebiasis; hsa05322:Systemic lupus erythematosus	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)	.	P08311
TT3G406	Cathepsin H (CTSH)	P09668	CATH_HUMAN	Peptidase	Pro-cathepsin H	CTSH	Important for the overall degradation of proteins in lysosomes.	.	6CZS; 6CZK; 1BZN	MWATLPLLCAGAWLLGVPVCGAAELCVNSLEKFHFKSWMSKHRKTYSTEEYHHRLQTFASNWRKINAHNNGNHTFKMALNQFSDMSFAEIKHKYLWSEPQNCSATKSNYLRGTGPYPPSVDWRKKGNFVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCAQDFNNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQGKDGYCKFQPGKAIGFVKDVANITIYDEEAMVEAVALYNPVSFAFEVTQDFMMYRTGIYSSTSCHKTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGLAACASYPIPLV	Literature-reported	"Semicarbazone-based inhibitors of cathepsin K, are they prodrugs for aldehyde inhibitors Bioorg Med Chem Lett. 2006 Feb 15;16(4):978-83."	0	.	.	.	.	.	.	.	.	.	.	hsa04142: Lysosome; hsa04210: Apoptosis	R-HSA-2132295: MHC class II antigen presentation; R-HSA-5683826: Surfactant metabolism; R-HSA-6798695: Neutrophil degranulation	.	P09668
TTDZN01	Cathepsin K (CTSK)	P43235	CATK_HUMAN	Peptidase	Cathepsin X; Cathepsin O2; Cathepsin O; CTSO2; CTSO	CTSK	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.	EC 3.4.22.38	7PCK; 6QBS; 6ASH; 5Z5O; 5TUN	MWGLKVLLLPVVSFALYPEEILDTHWELWKKTHRKQYNNKVDEISRRLIWEKNLKYISIHNLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLKVPLSHSRSNDTLYIPEWEGRAPDSVDYRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENDGCGGGYMTNAFQYVQKNRGIDSEDAYPYVGQEESCMYNPTGKAAKCRGYREIPEGNEKALKRAVARVGPVSVAIDASLTSFQFYSKGVYYDESCNSDNLNHAVLAVGYGIQKGNKHWIIKNSWGENWGNKGYILMARNKNNACGIANLASFPKM	Clinical trial	"A novel c-Met inhibitor, MK8033, synergizes with carboplatin plus paclitaxel to inhibit ovarian cancer cell growth. Oncol Rep. 2013 May;29(5):2011-8."	17	EC:3.4	Peptidase	.	3.4.22.38	Acting on peptide bonds (peptidases)	Cathepsin propeptide inhibitor domain (I29); Papain family cysteine protease	PF08246; PF00112	PF08246; Inhibitor_I29; PF00112; Peptidase_C1	.	.	hsa04142:Lysosome; hsa04380:Osteoclast differentiation; hsa04620:Toll-like receptor signaling pathway; hsa05323:Rheumatoid arthritis	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	.	P43235
TT36ETB	Cathepsin L (CTSL)	P07711	CATL1_HUMAN	Peptidase	Major excreted protein; MEP; Cathepsin L1; CTSL1	CTSL	Important for the overall degradation of proteins in lysosomes.	EC 3.4.22.15	6F06; 6EZX; 6EZP; 5MQY; 5MAJ	MNPTLILAAFCLGIASATLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPTV	Clinical trial	"Functionalized benzophenone, thiophene, pyridine, and fluorene thiosemicarbazone derivatives as inhibitors of cathepsin L. Bioorg Med Chem Lett. 2010 Nov 15;20(22):6610-5."	16	EC:3.4	Peptidase	.	3.4.22.15	Acting on peptide bonds (peptidases)	Cathepsin propeptide inhibitor domain (I29); Papain family cysteine protease	PF08246; PF00112	PF08246; Inhibitor_I29; PF00112; Peptidase_C1	.	.	hsa04142:Lysosome; hsa04145:Phagosome; hsa04612:Antigen processing and presentation; hsa05205:Proteoglycans in cancer; hsa05323:Rheumatoid arthritis	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	.	P07711
TTS586L	HUMAN cathepsin L (CTSL)	P07711	CATL1_HUMAN	Peptidase	Major excreted protein; MEP; Cathepsin L1; CTSL1	CTSL	Important for the overall degradation of proteins in lysosomes.	EC 3.4.22.15	6F06; 6EZX; 6EZP; 5MQY; 5MAJ	MNPTLILAAFCLGIASATLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPTV	.	Coronaviruses - drug discovery and therapeutic options. Nat Rev Drug Discov. 2016 May;15(5):327-47.	16	EC:3.4	Peptidase	.	3.4.22.15	Acting on peptide bonds (peptidases)	Cathepsin propeptide inhibitor domain (I29); Papain family cysteine protease	PF08246; PF00112	PF08246; Inhibitor_I29; PF00112; Peptidase_C1	.	.	hsa04140: Autophagy - animal; hsa04142: Lysosome; hsa04145: Phagosome; hsa04210: Apoptosis; hsa04612: Antigen processing and presentation; hsa05205: Proteoglycans in cancer; hsa05323: Rheumatoid arthritis; hsa05418: Fluid shear stress and atherosclerosis	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; R-HSA-8939242: RUNX1 regulates transcription of genes involved in differentiation of keratinocytes; R-HSA-9678110: Attachment and Entry; R-HSA-9694614: Attachment and Entry	.	P07711
TTUMQVO	Cathepsin S (CTSS)	P25774	CATS_HUMAN	Peptidase	Cysteine protease cathepsin S	CTSS	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.	EC 3.4.22.27	5QCJ; 5QCI; 5QCH; 5QCG; 5QCF	MKRLVCVLLVCSSAVAQLHKDPTLDHHWHLWKKTYGKQYKEKNEEAVRRLIWEKNLKFVMLHNLEHSMGMHSYDLGMNHLGDMTSEEVMSLMSSLRVPSQWQRNITYKSNPNRILPDSVDWREKGCVTEVKYQGSCGACWAFSAVGALEAQLKLKTGKLVSLSAQNLVDCSTEKYGNKGCNGGFMTTAFQYIIDNKGIDSDASYPYKAMDQKCQYDSKYRAATCSKYTELPYGREDVLKEAVANKGPVSVGVDARHPSFFLYRSGVYYEPSCTQNVNHGVLVVGYGDLNGKEYWLVKNSWGHNFGEEGYIRMARNKGNHCGIASFPSYPEI	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	EC:3.4	Peptidase	.	3.4.22.27	Acting on peptide bonds (peptidases)	Cathepsin propeptide inhibitor domain (I29); Papain family cysteine protease	PF08246; PF00112	PF08246; Inhibitor_I29; PF00112; Peptidase_C1	.	.	hsa04142:Lysosome; hsa04145:Phagosome; hsa04612:Antigen processing and presentation; hsa05152:Tuberculosis	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	.	P25774
TTSD9T1	Cathepsin V (CTSV)	O60911	CATL2_HUMAN	Peptidase	UNQ268/PRO305; Cathepsin U; Cathepsin L2; CTSU; CTSL2; CATL2	CTSV	May have an important role in corneal physiology. Cysteine protease.	EC 3.4.22.43	3KFQ; 3H6S; 1FH0	MNLSLVLAAFCLGIASAVPKFDQNLDTKWYQWKATHRRLYGANEEGWRRAVWEKNMKMIELHNGEYSQGKHGFTMAMNAFGDMTNEEFRQMMGCFRNQKFRKGKVFREPLFLDLPKSVDWRKKGYVTPVKNQKQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDCSRPQGNQGCNGGFMARAFQYVKENGGLDSEESYPYVAVDEICKYRPENSVANDTGFTVVAPGKEKALMKAVATVGPISVAMDAGHSSFQFYKSGIYFEPDCSSKNLDHGVLVVGYGFEGANSNNSKYWLVKNSWGPEWGSNGYVKIAKDKNNHCGIATAASYPNV	Patented-recorded	Cathepsin B and L inhibitors: a patent review (2010 - present).Expert Opin Ther Pat. 2017 Jun;27(6):643-656.	15.5	EC:3.4	Peptidase	.	3.4.22.43	Acting on peptide bonds (peptidases)	Cathepsin propeptide inhibitor domain (I29); Papain family cysteine protease	PF08246; PF00112	PF08246; Inhibitor_I29; PF00112; Peptidase_C1	.	.	hsa04142:Lysosome	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	.	O60911
TT9YLCR	Intrinsic factor-B12 receptor (CUBN)	O60494	CUBN_HUMAN	Growth factor	Intrinsic factor-vitamin B12 receptor; Cubilin; CUBN	CUBN	"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."	.	6GJE; 3KQ4	MMNMSLPFLWSLLTLLIFAEVNGEAGELELQRQKRSINLQQPRMATERGNLVFLTGSAQNIEFRTGSLGKIKLNDEDLSECLHQIQKNKEDIIELKGSAIGLPQNISSQIYQLNSKLVDLERKFQGLQQTVDKKVCSSNPCQNGGTCLNLHDSFFCICPPQWKGPLCSADVNECEIYSGTPLSCQNGGTCVNTMGSYSCHCPPETYGPQCASKYDDCEGGSVARCVHGICEDLMREQAGEPKYSCVCDAGWMFSPNSPACTLDRDECSFQPGPCSTLVQCFNTQGSFYCGACPTGWQGNGYICEDINECEINNGGCSVAPPVECVNTPGSSHCQACPPGYQGDGRVCTLTDICSVSNGGCHPDASCSSTLGSLPLCTCLPGYTGNGYGPNGCVQLSNICLSHPCLNGQCIDTVSGYFCKCDSGWTGVNCTENINECLSNPCLNGGTCVDGVDSFSCECTRLWTGALCQVPQQVCGESLSGINGSFSYRSPDVGYVHDVNCFWVIKTEMGKVLRITFTFFRLESMDNCPHEFLQVYDGDSSSAFQLGRFCGSSLPHELLSSDNALYFHLYSEHLRNGRGFTVRWETQQPECGGILTGPYGSIKSPGYPGNYPPGRDCVWIVVTSPDLLVTFTFGTLSLEHHDDCNKDYLEIRDGPLYQDPLLGKFCTTFSVPPLQTTGPFARIHFHSDSQISDQGFHITYLTSPSDLRCGGNYTDPEGELFLPELSGPFTHTRQCVYMMKQPQGEQIQINFTHVELQCQSDSSQNYIEVRDGETLLGKVCGNGTISHIKSITNSVWIRFKIDASVEKASFRAVYQVACGDELTGEGVIRSPFFPNVYPGERTCRWTIHQPQSQVILLNFTVFEIGSSAHCETDYVEIGSSSILGSPENKKYCGTDIPSFITSVYNFLYVTFVKSSSTENHGFMAKFSAEDLACGEILTESTGTIQSPGHPNVYPHGINCTWHILVQPNHLIHLMFETFHLEFHYNCTNDYLEVYDTDSETSLGRYCGKSIPPSLTSSGNSLMLVFVTDSDLAYEGFLINYEAISAATACLQDYTDDLGTFTSPNFPNNYPNNWECIYRITVRTGQLIAVHFTNFSLEEAIGNYYTDFLEIRDGGYEKSPLLGIFYGSNLPPTIISHSNKLWLKFKSDQIDTRSGFSAYWDGSSTGCGGNLTTSSGTFISPNYPMPYYHSSECYWWLKSSHGSAFELEFKDFHLEHHPNCTLDYLAVYDGPSSNSHLLTQLCGDEKPPLIRSSGDSMFIKLRTDEGQQGRGFKAEYRQTCENVVIVNQTYGILESIGYPNPYSENQHCNWTIRATTGNTVNYTFLAFDLEHHINCSTDYLELYDGPRQMGRYCGVDLPPPGSTTSSKLQVLLLTDGVGRREKGFQMQWFVYGCGGELSGATGSFSSPGFPNRYPPNKECIWYIRTDPGSSIQLTIHDFDVEYHSRCNFDVLEIYGGPDFHSPRIAQLCTQRSPENPMQVSSTGNELAIRFKTDLSINGRGFNASWQAVTGGCGGIFQAPSGEIHSPNYPSPYRSNTDCSWVIRVDRNHRVLLNFTDFDLEPQDSCIMAYDGLSSTMSRLARTCGREQLANPIVSSGNSLFLRFQSGPSRQNRGFRAQFRQACGGHILTSSFDTVSSPRFPANYPNNQNCSWIIQAQPPLNHITLSFTHFELERSTTCARDFVEILDGGHEDAPLRGRYCGTDMPHPITSFSSALTLRFVSDSSISAGGFHTTVTASVSACGGTFYMAEGIFNSPGYPDIYPPNVECVWNIVSSPGNRLQLSFISFQLEDSQDCSRDFVEIREGNATGHLVGRYCGNSFPLNYSSIVGHTLWVRFISDGSGSGTGFQATFMKIFGNDNIVGTHGKVASPFWPENYPHNSNYQWTVNVNASHVVHGRILEMDIEEIQNCYYDKLRIYDGPSIHARLIGAYCGTQTESFSSTGNSLTFHFYSDSSISGKGFLLEWFAVDAPDGVLPTIAPGACGGFLRTGDAPVFLFSPGWPDSYSNRVDCTWLIQAPDSTVELNILSLDIESHRTCAYDSLVIRDGDNNLAQQLAVLCGREIPGPIRSTGEYMFIRFTSDSSVTRAGFNASFHKSCGGYLHADRGIITSPKYPETYPSNLNCSWHVLVQSGLTIAVHFEQPFQIPNGDSSCNQGDYLVLRNGPDICSPPLGPPGGNGHFCGSHASSTLFTSDNQMFVQFISDHSNEGQGFKIKYEAKSLACGGNVYIHDADSAGYVTSPNHPHNYPPHADCIWILAAPPETRIQLQFEDRFDIEVTPNCTSNYLELRDGVDSDAPILSKFCGTSLPSSQWSSGEVMYLRFRSDNSPTHVGFKAKYSIAQCGGRVPGQSGVVESIGHPTLPYRDNLFCEWHLQGLSGHYLTISFEDFNLQNSSGCEKDFVEIWDNHTSGNILGRYCGNTIPDSIDTSSNTAVVRFVTDGSVTASGFRLRFESSMEECGGDLQGSIGTFTSPNYPNPNPHGRICEWRITAPEGRRITLMFNNLRLATHPSCNNEHVIVFNGIRSNSPQLEKLCSSVNVSNEIKSSGNTMKVIFFTDGSRPYGGFTASYTSSEDAVCGGSLPNTPEGNFTSPGYDGVRNYSRNLNCEWTLSNPNQGNSSISIHFEDFYLESHQDCQFDVLEFRVGDADGPLMWRLCGPSKPTLPLVIPYSQVWIHFVTNERVEHIGFHAKYSFTDCGGIQIGDSGVITSPNYPNAYDSLTHCSSLLEAPQGHTITLTFSDFDIEPHTTCAWDSVTVRNGGSPESPIIGQYCGNSNPRTIQSGSNQLVVTFNSDHSLQGGGFYATWNTQTLGCGGIFHSDNGTIRSPHWPQNFPENSRCSWTAITHKSKHLEISFDNNFLIPSGDGQCQNSFVKVWAGTEEVDKALLATGCGNVAPGPVITPSNTFTAVFQSQEAPAQGFSASFVSRCGSNFTGPSGYIISPNYPKQYDNNMNCTYVIEANPLSVVLLTFVSFHLEARSAVTGSCVNDGVHIIRGYSVMSTPFATVCGDEMPAPLTIAGPVLLNFYSNEQITDFGFKFSYRIISCGGVFNFSSGIITSPAYSYADYPNDMHCLYTITVSDDKVIELKFSDFDVVPSTSCSHDYLAIYDGANTSDPLLGKFCGSKRPPNVKSSNNSMLLVFKTDSFQTAKGWKMSFRQTLGPQQGCGGYLTGSNNTFASPDSDSNGMYDKNLNCVWIIIAPVNKVIHLTFNTFALEAASTRQRCLYDYVKLYDGDSENANLAGTFCGSTVPAPFISSGNFLTVQFISDLTLEREGFNATYTIMDMPCGGTYNATWTPQNISSPNSSDPDVPFSICTWVIDSPPHQQVKITVWALQLTSQDCTQNYLQLQDSPQGHGNSRFQFCGRNASAVPVFYSSMSTAMVIFKSGVVNRNSRMSFTYQIADCNRDYHKAFGNLRSPGWPDNYDNDKDCTVTLTAPQNHTISLFFHSLGIENSVECRNDFLEVRNGSNSNSPLLGKYCGTLLPNPVFSQNNELYLRFKSDSVTSDRGYEIIWTSSPSGCGGTLYGDRGSFTSPGYPGTYPNNTYCEWVLVAPAGRLVTINFYFISIDDPGDCVQNYLTLYDGPNASSPSSGPYCGGDTSIAPFVASSNQVFIKFHADYARRPSAFRLTWDS	Literature-reported	Sodium reabsorption in aldosterone-sensitive distal nephron: news and contributions from genetically engineered animals. Curr Opin Nephrol Hypertens. 2001 Jan;10(1):39-47.	.	.	.	.	.	.	.	.	.	.	.	hsa04977: Vitamin digestion and absorption	R-HSA-196791: Vitamin D (calciferol) metabolism; R-HSA-3359462: Defective AMN causes MGA1; R-HSA-3359463: Defective CUBN causes MGA1; R-HSA-8964011: HDL clearance; R-HSA-9758881: Uptake of dietary cobalamins into enterocytes	.	.
TTPCU0Q	Cullin-3 (CUL-3)	Q13618	CUL3_HUMAN	.	KIAA0617; Cullin3	CUL3	"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."	.	6I2M; 5NLB; 4HXI; 4EOZ; 4APF	MSNLSKGTGSRKDTKMRIRAFPMTMDEKYVNSIWDLLKNAIQEIQRKNNSGLSFEELYRNAYTMVLHKHGEKLYTGLREVVTEHLINKVREDVLNSLNNNFLQTLNQAWNDHQTAMVMIRDILMYMDRVYVQQNNVENVYNLGLIIFRDQVVRYGCIRDHLRQTLLDMIARERKGEVVDRGAIRNACQMLMILGLEGRSVYEEDFEAPFLEMSAEFFQMESQKFLAENSASVYIKKVEARINEEIERVMHCLDKSTEEPIVKVVERELISKHMKTIVEMENSGLVHMLKNGKTEDLGCMYKLFSRVPNGLKTMCECMSSYLREQGKALVSEEGEGKNPVDYIQGLLDLKSRFDRFLLESFNNDRLFKQTIAGDFEYFLNLNSRSPEYLSLFIDDKLKKGVKGLTEQEVETILDKAMVLFRFMQEKDVFERYYKQHLARRLLTNKSVSDDSEKNMISKLKTECGCQFTSKLEGMFRDMSISNTTMDEFRQHLQATGVSLGGVDLTVRVLTTGYWPTQSATPKCNIPPAPRHAFEIFRRFYLAKHSGRQLTLQHHMGSADLNATFYGPVKKEDGSEVGVGGAQVTGSNTRKHILQVSTFQMTILMLFNNREKYTFEEIQQETDIPERELVRALQSLACGKPTQRVLTKEPKSKEIENGHIFTVNDQFTSKLHRVKIQTVAAKQGESDPERKETRQKVDDDRKHEIEAAIVRIMKSRKKMQHNVLVAEVTQQLKARFLPSPVVIKKRIEGLIEREYLARTPEDRKVYTYVA	Literature-reported	Functional analysis of Cullin 3 E3 ligases in tumorigenesis. Biochim Biophys Acta Rev Cancer. 2018 Jan;1869(1):11-28.	.	.	Cullin family	.	.	.	Cullin family; Cullin protein neddylation domain	PF00888; PF10557	PF00888; Cullin; PF10557; Cullin_Nedd8	.	.	hsa04120: Ubiquitin mediated proteolysis; hsa04340: Hedgehog signaling pathway	R-HSA-4641258: Degradation of DVL; R-HSA-5632684: Hedgehog 'on' state; R-HSA-5658442: Regulation of RAS by GAPs; R-HSA-8951664: Neddylation; R-HSA-9013418: RHOBTB2 GTPase cycle; R-HSA-9013422: RHOBTB1 GTPase cycle; R-HSA-9679191: Potential therapeutics for SARS; R-HSA-9706019: RHOBTB3 ATPase cycle; R-HSA-9755511: KEAP1-NFE2L2 pathway; R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	Q13618
TTEZQ39	Cerebron E3 ubiquitin ligase complex (CRL4-CRBN E3 ubiquitin ligase)	Q13619/Q13620-Q16531-Q96SW2	CUL4A_HUMAN/CUL4B_HUMAN-DDB1_HUMAN-CRBN_HUMAN	.	.	CUL4A/CUL4B-DDB1-CRBN	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of Kangpu Biopharmaceuticals."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q13619
TTI8R0P	Cullin-7 (CUL-7)	Q14999	CUL7_HUMAN	.	KIAA0076	CUL7	"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."	.	2JNG	MVGELRYREFRVPLGPGLHAYPDELIRQRVGHDGHPEYQIRWLILRRGDEGDGGSGQVDCKAEHILLWMSKDEIYANCHKMLGEDGQVIGPSQESAGEVGALDKSVLEEMETDVKSLIQRALRQLEECVGTIPPAPLLHTVHVLSAYASIEPLTGVFKDPRVLDLLMHMLSSPDYQIRWSAGRMIQALSSHDAGTRTQILLSLSQQEAIEKHLDFDSRCALLALFAQATLSEHPMSFEGIQLPQVPGRVLFSLVKRYLHVTSLLDQLNDSAAEPGAQNTSAPEELSGERGQLELEFSMAMGTLISELVQAMRWDQASDRPRSSARSPGSIFQPQLADVSPGLPAAQAQPSFRRSRRFRPRSEFASGNTYALYVRDTLQPGMRVRMLDDYEEISAGDEGEFRQSNNGVPPVQVFWESTGRTYWVHWHMLEILGFEEDIEDMVEADEYQGAVASRVLGRALPAWRWRPMTELYAVPYVLPEDEDTEECEHLTLAEWWELLFFIKKLDGPDHQEVLQILQENLDGEILDDEILAELAVPIELAQDLLLTLPQRLNDSALRDLINCHVYKKYGPEALAGNQAYPSLLEAQEDVLLLDAQAQAKDSEDAAKVEAKEPPSQSPNTPLQRLVEGYGPAGKILLDLEQALSSEGTQENKVKPLLLQLQRQPQPFLALMQSLDTPETNRTLHLTVLRILKQLVDFPEALLLPWHEAVDACMACLRSPNTDREVLQELIFFLHRLTSVSRDYAVVLNQLGARDAISKALEKHLGKLELAQELRDMVFKCEKHAHLYRKLITNILGGCIQMVLGQIEDHRRTHQPINIPFFDVFLRYLCQGSSVEVKEDKCWEKVEVSSNPHRASKLTDHNPKTYWESNGSAGSHYITLHMRRGILIRQLTLLVASEDSSYMPARVVVCGGDSTSSLHTELNSVNVMPSASRVILLENLTRFWPIIQIRIKRCQQGGIDTRIRGLEILGPKPTFWPVFREQLCRHTRLFYMVRAQAWSQDMAEDRRSLLHLSSRLNGALRQEQNFADRFLPDDEAAQALGKTCWEALVSPVVQNITSPDEDGISPLGWLLDQYLECQEAVFNPQSRGPAFFSRVRRLTHLLVHVEPCEAPPPVVATPRPKGRNRSHDWSSLATRGLPSSIMRNLTRCWRAVVEKQVNNFLTSSWRDDDFVPRYCEHFNILQNSSSELFGPRAAFLLALQNGCAGALLKLPFLKAAHVSEQFARHIDQQIQGSRIGGAQEMERLAQLQQCLQAVLIFSGLEIATTFEHYYQHYMADRLLGVVSSWLEGAVLEQIGPCFPNRLPQQMLQSLSTSKELQRQFHVYQLQQLDQELLKLEDTEKKIQVGLGASGKEHKSEKEEEAGAAAVVDVAEGEEEEEENEDLYYEGAMPEVSVLVLSRHSWPVASICHTLNPRTCLPSYLRGTLNRYSNFYNKSQSHPALERGSQRRLQWTWLGWAELQFGNQTLHVSTVQMWLLLYLNDLKAVSVESLLAFSGLSADMLNQAIGPLTSSRGPLDLHEQKDIPGGVLKIRDGSKEPRSRWDIVRLIPPQTYLQAEGEDGQNLEKRRNLLNCLIVRILKAHGDEGLHIDQLVCLVLEAWQKGPCPPRGLVSSLGKGSACSSTDVLSCILHLLGKGTLRRHDDRPQVLSYAVPVTVMEPHTESLNPGSSGPNPPLTFHTLQIRSRGVPYASCTATQSFSTFR	Literature-reported	Cullin 7 is a predictor of poor prognosis in breast cancer patients and is involved in the proliferation and invasion of breast cancer cells by reg... Oncol Rep. 2018 Feb;39(2):603-610.	.	.	Cullin family	cullin family.	.	.	"Anaphase-promoting complex, subunit 10 (APC10); Mouse development and cellular proliferation protein Cullin-7; Cullin family"	PF03256; PF11515; PF00888	PF03256; ANAPC10; PF11515; Cul7; PF00888; Cullin	.	.	hsa04120: Ubiquitin mediated proteolysis	R-HSA-381038: XBP1(S) activates chaperone genes; R-HSA-8951664: Neddylation; R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	Q14999
TTCU5EN	HUMAN cullin-2 (CUL2)	Q13617	CUL2_HUMAN	Cullin family	cullin 2; CUL-2	cullin 2	"Human protein cullin 2 interacts with SARS-CoV-2 Orf10 protein with high significance, which indicates CUL2 as a potential therapeutic target."	.	4WQO; 5N4W; 6R6H; 6R7F; 6R7H	MSLKPRVVDFDETWNKLLTTIKAVVMLEYVERATWNDRFSDIYALCVAYPEPLGERLYTETKIFLENHVRHLHKRVLESEEQVLVMYHRYWEEYSKGADYMDCLYRYLNTQFIKKNKLTEADLQYGYGGVDMNEPLMEIGELALDMWRKLMVEPLQAILIRMLLREIKNDRGGEDPNQKVIHGVINSFVHVEQYKKKFPLKFYQEIFESPFLTETGEYYKQEASNLLQESNCSQYMEKVLGRLKDEEIRCRKYLHPSSYTKVIHECQQRMVADHLQFLHAECHNIIRQEKKNDMANMYVLLRAVSTGLPHMIQELQNHIHDEGLRATSNLTQENMPTLFVESVLEVHGKFVQLINTVLNGDQHFMSALDKALTSVVNYREPKSVCKAPELLAKYCDNLLKKSAKGMTENEVEDRLTSFITVFKYIDDKDVFQKFYARMLAKRLIHGLSMSMDSEEAMINKLKQACGYEFTSKLHRMYTDMSVSADLNNKFNNFIKNQDTVIDLGISFQIYVLQAGAWPLTQAPSSTFAIPQELEKSVQMFELFYSQHFSGRKLTWLHYLCTGEVKMNYLGKPYVAMVTTYQMAVLLAFNNSETVSYKELQDSTQMNEKELTKTIKSLLDVKMINHDSEKEDIDAESSFSLNMNFSSKRTKFKITTSMQKDTPQEMEQTRSAVDEDRKMYLQAAIVRIMKARKVLRHNALIQEVISQSRARFNPSISMIKKCIEVLIDKQYIERSQASADEYSYVA	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa04066: HIF-1 signaling pathway; hsa04120: Ubiquitin mediated proteolysis; hsa05200: Pathways in cancer; hsa05211: Renal cell carcinoma	R-HSA-1234176: Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha; R-HSA-8951664: Neddylation; R-HSA-9010553: Regulation of expression of SLITs and ROBOs; R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	Q13617
TT1OFBQ	Fractalkine (CX3CL1)	P78423	X3CL1_HUMAN	.	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	CX3CL1	"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."	.	5WB2; 4XT3; 4XT1; 3ONA; 1F2L	MAPISLSWLLRLATFCHLTVLLAGQHHGVTKCNITCSKMTSKIPVALLIHYQQNQASCGKRAIILETRQHRLFCADPKEQWVKDAMQHLDRQAAALTRNGGTFEKQIGEVKPRTTPAAGGMDESVVLEPEATGESSSLEPTPSSQEAQRALGTSPELPTGVTGSSGTRLPPTPKAQDGGPVGTELFRVPPVSTAATWQSSAPHQPGPSLWAEAKTSEAPSTQDPSTQASTASSPAPEENAPSEGQRVWGQGQSPRPENSLEREEMGPVPAHTDAFQDWGPGSMAHVSVVPVSSEGTPSREPVASGSWTPKAEEPIHATMDPQRLGVLITPVPDAQAATRRQAVGLLAFLGLLFCLGVAMFTYQSLQGCPRKMAGEMAEGLRYIPRSCGSNSYVLVPV	Literature-reported	Analysis of fractalkine receptor CX(3)CR1 function by targeted deletion and green fluorescent protein reporter gene insertion. Mol Cell Biol. 2000 Jun;20(11):4106-14.	.	.	Transmembrane protein	intercrine delta family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway; hsa04668: TNF signaling pathway; hsa05163: Human cytomegalovirus infection	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-418594: G alpha (i) signalling events	.	P78423
TT2T98G	C-X3-C chemokine receptor 1 (CX3CR1)	P49238	CX3C1_HUMAN	GPCR rhodopsin	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	CX3CR1	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.	.	.	MDQFPESVTENFEYDDLAEACYIGDIVVFGTVFLSIFYSVIFAIGLVGNLLVVFALTNSKKPKSVTDIYLLNLALSDLLFVATLPFWTHYLINEKGLHNAMCKFTTAFFFIGFFGSIFFITVISIDRYLAIVLAANSMNNRTVQHGVTISLGVWAAAILVAAPQFMFTKQKENECLGDYPEVLQEIWPVLRNVETNFLGFLLPLLIMSYCYFRIIQTLFSCKNHKKAKAIKLILLVVIVFFLFWTPYNVMIFLETLKLYDFFPSCDMRKDLRLALSVTETVAFSHCCLNPLIYAFAGEKFRRYLYHLYGKCLAVLCGRSVHVDFSSSESQRSRHGSVLSSNFTYHTSDGDALLLL	Literature-reported	Prevention of crescentic glomerulonephritis by immunoneutralization of the fractalkine receptor CX3CR1 rapid communication. Kidney Int. 1999 Aug;56(2):612-20.	.	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-418594: G alpha (i) signalling events	.	P49238
TTLK1RW	C-X-C motif chemokine 1 (CXCL1)	P09341	GROA_HUMAN	Cytokine: CXC chemokine	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	CXCL1	"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."	.	1ROD; 1MSH; 1MSG; 1MGS	MARAALSAAPSNPRLLRVALLLLLLVAAGRRAAGASVATELRCQCLQTLQGIHPKNIQSVNVKSPGPHCAQTEVIATLKNGRKACLNPASPIVKKIIEKMLNSDKSN	Literature-reported	Potential biomarkers for early detection of acute graft-versus-host disease. Proteomics Clin Appl. 2012 Aug;6(7-8):351-63. 	.	Cytokine	Intercrine-alpha family	intercrine alpha (chemokine CxC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway; hsa04064: NF-kappa B signaling pathway; hsa04621: NOD-like receptor signaling pathway; hsa04657: IL-17 signaling pathway; hsa04668: TNF signaling pathway; hsa04936: Alcoholic liver disease; hsa05120: Epithelial cell signaling in Helicobacter pylori infection; hsa05134: Legionellosis; hsa05146: Amoebiasis; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05323: Rheumatoid arthritis; hsa05417: Lipid and atherosclerosis	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-418594: G alpha (i) signalling events; R-HSA-6783783: Interleukin-10 signaling; R-HSA-6798695: Neutrophil degranulation	.	P09341
TTQOVYA	C-X-C motif chemokine 10 (CXCL10)	P02778	CXL10_HUMAN	Cytokine: CXC chemokine	Small-inducible cytokine B10; SCYB10; IP-10; INP10; Gamma-IP10; 10 kDa interferon gamma-induced protein	CXCL10	"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)."	.	1O80; 1O7Z; 1O7Y; 1LV9	MNQTAILICCLIFLTLSGIQGVPLSRTVRCTCISISNQPVNPRSLEKLEIIPASQFCPRVEIIATMKKKGEKRCLNPESKAIKNLLKAVSKERSKRSP	Clinical trial	Anti-IP-10 antibody (BMS-936557) for ulcerative colitis: a phase II randomised study. Gut. 2014 Mar;63(3):442-50.	21	Cytokine	Cytokine: CXC chemokine	intercrine alpha (chemokine CxC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	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	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P02778
TTWG0RE	C-X-C motif chemokine 11 (CXCL11)	O14625	CXL11_HUMAN	Cytokine: CXC chemokine	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	CXCL11	"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."	.	1RJT	MSVKGMAIALAVILCATVVQGFPMFKRGRCLCIGPGVKAVKVADIEKASIMYPSNNCDKIEVIITLKENKGQRCLNPKSKQARLIIKKVERKNF	Literature-reported	Chemokine (C-X-C motif) ligand 11 levels predict survival in cirrhotic patients with transjugular intrahepatic portosystemic shunt. Liver Int. 2016 Mar;36(3):386-94.	.	Cytokine	.	intercrine alpha (chemokine CxC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway; hsa04620: Toll-like receptor signaling pathway	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-418594: G alpha (i) signalling events	.	O14625
TT4UGTF	Stromal cell-derived factor 1 (CXCL12)	P48061	SDF1_HUMAN	Cytokine: CXC chemokine	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	CXCL12	"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."	.	4UAI; 4LMQ; 3HP3; 3GV3; 2SDF	MNAKVVVVLVLVLTALCLSDGKPVSLSYRCPCRFFESHVARANVKHLKILNTPNCALQIVARLKNNNRQVCIDPKLKWIQEYLEKALNKRFKM	Clinical trial	Stromal cell-derived factor-1 (SDF-1): homing factor for engineered regenerative medicine. Expert Opin Biol Ther. 2011 Feb;11(2):189-97.	25	Cytokine	Cytokine: CXC chemokine	intercrine alpha (chemokine CxC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	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	R-HSA-1251985:Nuclear signaling by ERBB4; R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P48061
TT0NIZ1	C-X-C motif chemokine 13 (CXCL13)	O43927	CXL13_HUMAN	Cytokine: CXC chemokine	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	CXCL13	"Does not induce calcium release in B-lymphocytes. Binds to BLR1/CXCR5. Chemotactic for B-lymphocytes but not for T-lymphocytes, monocytes and neutrophils."	.	5CBE; 5CBA; 4ZAI	MKFISTSLLLMLLVSSLSPVQGVLEVYYTSLRCRCVQESSVFIPRRFIDRIQILPRGNGCPRKEIIVWKKNKSIVCVDPQAEWIQRMMEVLRKRSSSTLPVPVFKRKIP	Literature-reported	Chemokine (C-X-C motif) ligand 13 promotes intrahepatic chemokine (C-X-C motif) receptor 5+ lymphocyte homing and aberrant B-cell immune responses ... Hepatology. 2015 Jun;61(6):1998-2007.	.	Cytokine	.	intercrine alpha (chemokine CxC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-418594: G alpha (i) signalling events	.	O43927
TTZF0K2	C-X-C motif chemokine 2 (CXCL2)	P19875	CXCL2_HUMAN	Cytokine: CXC chemokine	SCYB2; Macrophage inflammatory protein 2-alpha; MIP2A; MIP2-alpha; Growth-regulated protein beta; Growth regulatedprotein beta; Gro-beta; GROB; GRO2	CXCL2	"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."	.	5OB5; 1QNK	MARATLSAAPSNPRLLRVALLLLLLVAASRRAAGAPLATELRCQCLQTLQGIHLKNIQSVKVKSPGPHCAQTEVIATLKNGQKACLNPASPMVKKIIEKMLKNGKSN	Clinical trial	Multiple sclerosis: current and future treatment options. Endocr Metab Immune Disord Drug Targets. 2007 Dec;7(4):292-9.	25	Cytokine	Intercrine-alpha family	intercrine alpha (chemokine CxC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	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	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P19875
TTCTE1G	Interleukin-8 (IL8)	P10145	IL8_HUMAN	Cytokine: interleukin	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	CXCL8	"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."	.	5WDZ; 5D14; 4XDX; 3IL8; 2IL8	MTSKLAVALLAAFLISAALCEGAVLPRSAKELRCQCIKTYSKPFHPKFIKELRVIESGPHCANTEIIVKLSDGRELCLDPKENWVQRVVEKFLKRAENS	Successful	Structure-Activity Relationship of novel phenylacetic CXCR1 inhibitors. Bioorg Med Chem Lett. 2009 Aug 1;19(15):4026-30.	34	Cytokine	Intercrine-alpha family	intercrine alpha (chemokine CxC) family.	.	.	"Small cytokines (intecrine/chemokine), interleukin-8 like"	PF00048	PF00048; IL8	.	.	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	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	.	P10145
TT3JF7X	HUMAN interleukin 8 (IL8)	P10145	IL8_HUMAN	Cytokine: interleukin	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	CXCL8	"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."	.	5WDZ; 5D14; 4XDX; 3IL8; 2IL8	MTSKLAVALLAAFLISAALCEGAVLPRSAKELRCQCIKTYSKPFHPKFIKELRVIESGPHCANTEIIVKLSDGRELCLDPKENWVQRVVEKFLKRAENS	.	ClinicalTrials.gov (NCT04347226) Anti-Interleukin-8 (Anti-IL-8) for Patients With COVID-19. U.S. National Institutes of Health.	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway; hsa04064: NF-kappa B signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04218: Cellular senescence; hsa04620: Toll-like receptor signaling pathway; hsa04621: NOD-like receptor signaling pathway; hsa04622: RIG-I-like receptor signaling pathway; hsa04657: IL-17 signaling pathway; hsa04932: Non-alcoholic fatty liver disease; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04936: Alcoholic liver disease; hsa05120: Epithelial cell signaling in Helicobacter pylori infection; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05133: Pertussis; hsa05134: Legionellosis; hsa05135: Yersinia infection; hsa05142: Chagas disease; hsa05144: Malaria; hsa05146: Amoebiasis; hsa05161: Hepatitis B; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05202: Transcriptional misregulation in cancer; hsa05219: Bladder cancer; hsa05323: Rheumatoid arthritis; hsa05417: Lipid and atherosclerosis	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 in response to endoplasmic reticulum stress; R-HSA-418594: G alpha (i) signalling events; R-HSA-6783783: Interleukin-10 signaling; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling	.	P10145
TTWE5PB	C-X-C motif chemokine 9 (CXCL9)	Q07325	CXCL9_HUMAN	.	Gamma-interferon-induced monokine; Monokine induced by interferon-gamma; HuMIG; MIG; Small-inducible cytokine B9	CXCL9	"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."	.	.	MKKSGVLFLLGIILLVLIGVQGTPVVRKGRCSCISTNQGTIHLQSLKDLKQFAPSPSCEKIEIIATLKNGVQTCLNPDSADVKELIKKWEKQVSQKKKQKNGKKHQKKKVLKVRKSQRSRQKKTT	Clinical trial	"Clinical pipeline report, company report or official report of PsiOxus Therapeutics."	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway; hsa04620: Toll-like receptor signaling pathway	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-418594: G alpha (i) signalling events	.	Q07325
TTMWT8Z	C-X-C chemokine receptor type 1 (CXCR1)	P25024	CXCR1_HUMAN	GPCR rhodopsin	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	CXCR1	"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."	.	2LNL; 1ILQ; 1ILP	MSNITDPQMWDFDDLNFTGMPPADEDYSPCMLETETLNKYVVIIAYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRHLVKFVCLGCWGLSMNLSLPFFLFRQAYHPNNSSPVCYEVLGNDTAKWRMVLRILPHTFGFIVPLFVMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQESCERRNNIGRALDATEILGFLHSCLNPIIYAFIGQNFRHGFLKILAMHGLVSKEFLARHRVTSYTSSSVNVSSNL	Successful	2-Arylpropionic CXC chemokine receptor 1 (CXCR1) ligands as novel noncompetitive CXCL8 inhibitors. J Med Chem. 2005 Jun 30;48(13):4312-31.	34	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04144:Endocytosis; hsa05120:Epithelial cell signaling in Helicobacter pylori infection	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P25024
TT4PH9E	Interleukin 8 receptor (IL8R)	P25024; P25025	CXCR1_HUMAN; CXCR2_HUMAN	Cytokine receptor	IL8R; IL-8R; IL-8 receptor; High affinity interleukin-8 receptor; CXCR; CXC-R; CDw128	CXCR1	"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."	.	.	MSNITDPQMWDFDDLNFTGMPPADEDYSPCMLETETLNKYVVIIAYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRHLVKFVCLGCWGLSMNLSLPFFLFRQAYHPNNSSPVCYEVLGNDTAKWRMVLRILPHTFGFIVPLFVMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQESCERRNNIGRALDATEILGFLHSCLNPIIYAFIGQNFRHGFLKILAMHGLVSKEFLARHRVTSYTSSSVNVSSNL	Literature-reported	"Synthesis and structure-activity relationship of 2-amino-3-heteroaryl-quinoxalines as non-peptide, small-molecule antagonists for interleukin-8 rec... Bioorg Med Chem. 2003 Aug 15;11(17):3777-90."	0	Cytokine receptor	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04144: Endocytosis; hsa05120: Epithelial cell signaling in Helicobacter pylori infection	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-418594: G alpha (i) signalling events; R-HSA-6798695: Neutrophil degranulation	.	P25024
TT30C9G	C-X-C chemokine receptor type 2 (CXCR2)	P25025	CXCR2_HUMAN	GPCR rhodopsin	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	CXCR2	"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."	.	5TYT; 4Q3H	MEDFNMESDSFEDFWKGEDLSNYSYSSTLPPFLLDAAPCEPESLEINKYFVVIIYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRYLVKFICLSIWGLSLLLALPVLLFRRTVYSSNVSPACYEDMGNNTANWRMLLRILPQSFGFIVPLLIMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQETCERRNHIDRALDATEILGILHSCLNPLIYAFIGQKFRHGLLKILAIHGLISKDSLPKDSRPSFVGSSSGHTSTTL	Successful	2-Arylpropionic CXC chemokine receptor 1 (CXCR1) ligands as novel noncompetitive CXCL8 inhibitors. J Med Chem. 2005 Jun 30;48(13):4312-31.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway; hsa04144:Endocytosis; hsa05120:Epithelial cell signaling in Helicobacter pylori infection	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P25025
TT1UCIJ	C-X-C chemokine receptor type 3 (CXCR3)	P49682	CXCR3_HUMAN	GPCR rhodopsin	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	CXCR3	"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."	.	.	MVLEVSDHQVLNDAEVAALLENFSSSYDYGENESDSCCTSPPCPQDFSLNFDRAFLPALYSLLFLLGLLGNGAVAAVLLSRRTALSSTDTFLLHLAVADTLLVLTLPLWAVDAAVQWVFGSGLCKVAGALFNINFYAGALLLACISFDRYLNIVHATQLYRRGPPARVTLTCLAVWGLCLLFALPDFIFLSAHHDERLNATHCQYNFPQVGRTALRVLQLVAGFLLPLLVMAYCYAHILAVLLVSRGQRRLRAMRLVVVVVVAFALCWTPYHLVVLVDILMDLGALARNCGRESRVDVAKSVTSGLGYMHCCLNPLLYAFVGVKFRERMWMLLLRLGCPNQRGLQRQPSSSRRDSSWSETSEASYSGL	Preclinical	Pharmacological characterization of CXC chemokine receptor 3 ligands and a small molecule antagonist. J Pharmacol Exp Ther. 2005 Jun;313(3):1263-71.	5	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P49682
TTBID49	C-X-C chemokine receptor type 4 (CXCR4)	P61073	CXCR4_HUMAN	GPCR rhodopsin	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	CXCR4	"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."	.	4RWS; 3OE9; 3OE8; 3OE6; 3OE0	MEGISIYTSDNYTEEMGSGDYDSMKEPCFREENANFNKIFLPTIYSIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAVANWYFGNFLCKAVHVIYTVNLYSSVLILAFISLDRYLAIVHATNSQRPRKLLAEKVVYVGVWIPALLLTIPDFIFANVSEADDRYICDRFYPNDLWVVVFQFQHIMVGLILPGIVILSCYCIIISKLSHSKGHQKRKALKTTVILILAFFACWLPYYIGISIDSFILLEIIKQGCEFENTVHKWISITEALAFFHCCLNPILYAFLGAKFKTSAQHALTSVSRGSSLKILSKGKRGGHSSVSTESESSSFHSS	Successful	Emerging therapies for multiple myeloma. Expert Opin Emerg Drugs. 2009 Mar;14(1):99-127.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family); CXCR4 Chemokine receptor N terminal	PF00001; PF12109	PF00001; 7tm_1; PF12109; CXCR4_N	9.A.14.13.17	The G-protein-coupled receptor (GPCR) Family	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	R-HSA-173107:Binding and entry of HIV virion; R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	P61073
TTIW59R	C-X-C chemokine receptor type 5 (CXCR5)	P32302	CXCR5_HUMAN	GPCR rhodopsin	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	CXCR5	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).	.	.	MNYPLTLEMDLENLEDLFWELDRLDNYNDTSLVENHLCPATEGPLMASFKAVFVPVAYSLIFLLGVIGNVLVLVILERHRQTRSSTETFLFHLAVADLLLVFILPFAVAEGSVGWVLGTFLCKTVIALHKVNFYCSSLLLACIAVDRYLAIVHAVHAYRHRRLLSIHITCGTIWLVGFLLALPEILFAKVSQGHHNNSLPRCTFSQENQAETHAWFTSRFLYHVAGFLLPMLVMGWCYVGVVHRLRQAQRRPQRQKAVRVAILVTSIFFLCWSPYHIVIFLDTLARLKAVDNTCKLNGSLPVAITMCEFLGLAHCCLNPMLYTFAGVKFRSDLSRLLTKLGCTGPASLCQLFPSWRRSSLSESENATSLTTF	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	17	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04062: Chemokine signaling pathway	R-HSA-380108: Chemokine receptors bind chemokines; R-HSA-418594: G alpha (i) signalling events	.	P32302
TT2BVUA	C-X-C chemokine receptor type 6 (CXCR6)	O00574	CXCR6_HUMAN	GPCR rhodopsin	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	CXCR6	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.	.	.	MAEHDYHEDYGFSSFNDSSQEEHQDFLQFSKVFLPCMYLVVFVCGLVGNSLVLVISIFYHKLQSLTDVFLVNLPLADLVFVCTLPFWAYAGIHEWVFGQVMCKSLLGIYTINFYTSMLILTCITVDRFIVVVKATKAYNQQAKRMTWGKVTSLLIWVISLLVSLPQIIYGNVFNLDKLICGYHDEAISTVVLATQMTLGFFLPLLTMIVCYSVIIKTLLHAGGFQKHRSLKIIFLVMAVFLLTQMPFNLMKFIRSTHWEYYAMTSFHYTIMVTEAIAYLRACLNPVLYAFVSLKFRKNFWKLVKDIGCLPYLGVSHQWKSSEDNSKTFSASHNVEATSMFQL	Literature-reported	Opportunities and challenges in targeting HIV entry. Curr Opin Pharmacol. 2002 Oct;2(5):529-33.	0	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway	R-HSA-380108:Chemokine receptors bind chemokines; R-HSA-418594:G alpha (i) signalling events	.	O00574
TTVS4C3	Retinoid-inducible nuclear factor (CXXC5)	Q7LFL8	CXXC5_HUMAN	.	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	CXXC5	"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."	.	5W9S	MSSLGGGSQDAGGSSSSSTNGSGGSGSSGPKAGAADKSAVVAAAAPASVADDTPPPERRNKSGIISEPLNKSLRRSRPLSHYSSFGSSGGSGGGSMMGGESADKATAAAAAASLLANGHDLAAAMAVDKSNPTSKHKSGAVASLLSKAERATELAAEGQLTLQQFAQSTEMLKRVVQEHLPLMSEAGAGLPDMEAVAGAEALNGQSDFPYLGAFPINPGLFIMTPAGVFLAESALHMAGLAEYPMQGELASAISSGKKKRKRCGMCAPCRRRINCEQCSSCRNRKTGHQICKFRKCEELKKKPSAALEKVMLPTGAAFRWFQ	Literature-reported	CXXC5 suppresses hepatocellular carcinoma by promoting TGF--induced cell cycle arrest and apoptosis. J Mol Cell Biol. 2018 Feb 1;10(1):48-59.	.	.	.	.	.	.	CXXC zinc finger domain	PF02008	PF02008; zf-CXXC	.	.	.	R-HSA-9018519: Estrogen-dependent gene expression	.	Q7LFL8
TT5T8MR	NADPH oxidase 2 (CYBB)	P04839	CY24B_HUMAN	Phagocyte NADPH oxidase	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	CYBB	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.	EC 1.-.-.-	3A1F	MGNWAVNEGLSIFVILVWLGLNVFLFVWYYRVYDIPPKFFYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRVRRQLDRNLTFHKMVAWMIALHSAIHTIAHLFNVEWCVNARVNNSDPYSVALSELGDRQNESYLNFARKRIKNPEGGLYLAVTLLAGITGVVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERIVRGQTAESLAVHNITVCEQKISEWGKIKECPIPQFAGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYCNNATNLKLKKIYFYWLCRDTHAFEWFADLLQLLESQMQERNNAGFLSYNIYLTGWDESQANHFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASQHPNTRIGVFLCGPEALAETLSKQSISNSESGPRGVHFIFNKENF	Literature-reported	NADPH Oxidase 2 Regulates NLRP3 Inflammasome Activation in the Brain after Traumatic Brain Injury. Oxid Med Cell Longev. 2017;2017:6057609.	.	TC=5.B.1	.	.	1.-.-.-	Oxidoreductases	FAD-binding domain; Ferric reductase like transmembrane component; Ferric reductase NAD binding domain	PF08022; PF01794; PF08030	PF08022; FAD_binding_8; PF01794; Ferric_reduct; PF08030; NAD_binding_6	5.B.1.1.1	The Phagocyte (gp91<sup>phox</sup>) NADPH Oxidase Family	hsa04066: HIF-1 signaling pathway; hsa04145: Phagosome; hsa04216: Ferroptosis; hsa04217: Necroptosis; hsa04613: Neutrophil extracellular trap formation; hsa04621: NOD-like receptor signaling pathway; hsa04670: Leukocyte transendothelial migration; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa05010: Alzheimer disease; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05140: Leishmaniasis; hsa05171: Coronavirus disease - COVID-19; hsa05415: Diabetic cardiomyopathy; hsa05417: Lipid and atherosclerosis	R-HSA-1222556: ROS and RNS production in phagocytes; R-HSA-1236973: Cross-presentation of particulate exogenous antigens (phagosomes); R-HSA-3299685: Detoxification of Reactive Oxygen Species; R-HSA-4420097: VEGFA-VEGFR2 Pathway; R-HSA-5668599: RHO GTPases Activate NADPH Oxidases; R-HSA-6798695: Neutrophil degranulation; R-HSA-9013149: RAC1 GTPase cycle; R-HSA-9013404: RAC2 GTPase cycle; R-HSA-9013423: RAC3 GTPase cycle	.	P04839
TTB8JQ7	Electron transport complex III (Complex III)	P08574-P00156	CY1_HUMAN-CYB_HUMAN	.	Cytochrome bc1 complex; CoQH2-cytochrome c reductase	CYC1-MT-CYB	Produces a transmembrane proton electrochemical gradient as a result of the redox reactions	.	.	MTPMRKTNPLMKLINHSFIDLPTPSNISAWWNFGSLLGACLILQITTGLFLAMHYSPDASTAFSSIAHITRDVNYGWIIRYLHANGASMFFICLFLHIGRGLYYGSFLYSETWNIGIILLLATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGYSVDSPTLTRFFTFHFILPFIIAALATLHLLFLHETGSNNPLGITSHSDKITFHPYYTIKDALGLLLFLLSLMTLTLFSPDLLGDPDNYTLANPLNTPPHIKPEWYFLFAYTILRSVPNKLGGVLALLLSILILAMIPILHMSKQQSMMFRPLSQSLYWLLAADLLILTWIGGQPVSYPFTIIGQVASVLYFTTILILMPTISLIENKMLKWAMAAAAASLRGVVLGPRGAGLPGARARGLLCSARPGQLPLRTPQAVALSSKSGLSRGRKVMLSALGMLAAGGAGLAMALHSAVSASDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCASCHSMDFVAYRHLVGVCYTEDEAKELAAEVEVQDGPNEDGEMFMRPGKLFDYFPKPYPNSEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQAIAMAPPIYTDVLEFDDGTPATMSQIAKDVCTFLRWASEPEHDHRKRMGLKMLMMMALLVPLVYTIKRHKWSVLKSRKLAYRPPK	Successful	Tafenoquine: First Global Approval.Drugs. 2018 Sep;78(14):1517-1523. 	34	.	.	.	.	.	.	.	.	.	.	.	.	.	P08574
TTSYVO6	Cholesterol desmolase (CYP11A1)	P05108	CP11A_HUMAN	Paired donor oxygen oxidoreductase	"P450(scc); Cytochrome P450(scc); Cytochrome P450 11A1; Cholesterol side-chain cleavage enzyme, mitochondrial; CYPXIA1; CYP11A"	CYP11A1	"Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone, the precursor of most steroid hormones."	EC 1.14.15.6	3NA1; 3NA0; 3N9Z; 3N9Y	MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNEIPSPGDNGWLNLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVYVIDPEDVALLFKSEGPNPERFLIPPWVAYHQYYQRPIGVLLKKSAAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVSVLHRRIKKAGSGNYSGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQMFHTSVPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRGILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMARNLKVQDMLRAEVLAARHQAQGDMATMLQLVPLLKASIKETLRLHPISVTLQRYLVNDLVLRDYMIPAKTLVQVAIYALGREPTFFFDPENFDPTRWLSKDKNITYFRNLGFGWGVRQCLGRRIAELEMTIFLINMLENFRVEIQHLSDVGTTFNLILMPEKPISFTFWPFNQEATQQ	Successful	Breakdown of Th cell immune responses and steroidogenic CYP11A1 expression in CD4+ T cells in a murine model implanted with B16 melanoma. Cell Immunol. 2000 Nov 25;206(1):7-15.	34	EC:1.14	Paired donor oxidoreductase	cytochrome P450 family.	1.14.15.6	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	Cytochrome P450	PF00067	PF00067; p450	.	.	hsa00140:Steroid hormone biosynthesis; hsa01100:Metabolic pathways; hsa04913:Ovarian steroidogenesis	R-HSA-211976:Endogenous sterols	MetaCyc:HS06719-MON	P05108
TTIQUX7	Steroid 11-beta-hydroxylase (CYP11B1)	P15538	C11B1_HUMAN	Paired donor oxygen oxidoreductase	S11BH; P450C11; P-450c11; CYPXIB1; CYP11B1	CYP11B1	"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."	EC 1.14.15.4	6M7X	MALRAKAEVCMAVPWLSLQRAQALGTRAARVPRTVLPFEAMPRRPGNRWLRLLQIWREQGYEDLHLEVHQTFQELGPIFRYDLGGAGMVCVMLPEDVEKLQQVDSLHPHRMSLEPWVAYRQHRGHKCGVFLLNGPEWRFNRLRLNPEVLSPNAVQRFLPMVDAVARDFSQALKKKVLQNARGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFMPRSLSRWTSPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFSRPQQYTSIVAELLLNAELSPDAIKANSMELTAGSVDTTVFPLLMTLFELARNPNVQQALRQESLAAAASISEHPQKATTELPLLRAALKETLRLYPVGLFLERVASSDLVLQNYHIPAGTLVRVFLYSLGRNPALFPRPERYNPQRWLDIRGSGRNFYHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHLQVETLTQEDIKMVYSFILRPSMFPLLTFRAIN	Successful	Effects of 3-MeSO2-DDE and some CYP inhibitors on glucocorticoid steroidogenesis in the H295R human adrenocortical carcinoma cell line. Toxicol In Vitro. 2002 Apr;16(2):113-21.	34	.	.	.	.	.	.	.	.	.	.	hsa00140:Steroid hormone biosynthesis; hsa01100:Metabolic pathways	R-HSA-194002:Glucocorticoid biosynthesis; R-HSA-211976:Endogenous sterols	MetaCyc:HS08547-MON	P15538
TT9MNE2	Aldosterone synthase (CYP11B2)	P19099	C11B2_HUMAN	Paired donor oxygen oxidoreductase	"Steroid 18hydroxylase; Cytochrome P450C18; Cytochrome P450Aldo; Cytochrome P450 11B2, mitochondrial; CYPXIB2; CYP11B2; Aldosteronesynthesizing enzyme; ALDOS"	CYP11B2	Preferentially catalyzes the conversion of 11- deoxycorticosterone to aldosterone via corticosterone and 18- hydroxycorticosterone.	EC 1.14.15.4	4ZGX; 4FDH; 4DVQ	MALRAKAEVCVAAPWLSLQRARALGTRAARAPRTVLPFEAMPQHPGNRWLRLLQIWREQGYEHLHLEMHQTFQELGPIFRYNLGGPRMVCVMLPEDVEKLQQVDSLHPCRMILEPWVAYRQHRGHKCGVFLLNGPEWRFNRLRLNPDVLSPKAVQRFLPMVDAVARDFSQALKKKVLQNARGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFMPRSLSRWISPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFNRPQHYTGIVAELLLKAELSLEAIKANSMELTAGSVDTTAFPLLMTLFELARNPDVQQILRQESLAAAASISEHPQKATTELPLLRAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVQVFLYSLGRNAALFPRPERYNPQRWLDIRGSGRNFHHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHFLVETLTQEDIKMVYSFILRPGTSPLLTFRAIN	Literature-reported	Medical management of Cushing's disease: what is the future . Pituitary. 2012 September; 15(3): 330-341.	25	.	.	.	.	.	.	.	.	.	.	hsa00140:Steroid hormone biosynthesis; hsa01100:Metabolic pathways	R-HSA-194002:Glucocorticoid biosynthesis; R-HSA-211976:Endogenous sterols	MetaCyc:HS11355-MON	P19099
TTRA5BZ	Steroid 17-alpha-monooxygenase (S17AH)	P05093	CP17A_HUMAN	Paired donor oxygen oxidoreductase	"Steroid 17-alpha-hydroxylase/17,20 lyase; P450c17; P450-C17; P450 17; CYPXVII; CYP17A1; CYP 17; 17 alpha-Hydroxylase/C17-20-lyase"	CYP17A1	"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."	EC 1.14.14.19	6CIZ; 6CIR; 6CHI; 5UYS; 5IRV	MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKYGPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVISLICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRNDLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIFGAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREVLRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNPAGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIPKVVFLIDSFKVKIKVRQAWREAQAEGST	Successful	2011 FDA drug approvals. Nat Rev Drug Discov. 2012 Feb 1;11(2):91-4.	34	.	.	.	.	.	.	.	.	.	.	hsa00140:Steroid hormone biosynthesis; hsa01100:Metabolic pathways; hsa04913:Ovarian steroidogenesis; hsa04917:Prolactin signaling pathway	R-HSA-193048:Androgen biosynthesis; R-HSA-194002:Glucocorticoid biosynthesis; R-HSA-211976:Endogenous sterols	MetaCyc:HS07560-MON	P05093
TTSZLWK	Aromatase (CYP19A1)	P11511	CP19A_HUMAN	Paired donor oxygen oxidoreductase	P-450AROM; Estrogen synthetase; Estrogen synthase; Cytochrome P450 19A1; Cytochrome P-450AROM; CYPXIX; CYP19; CYAR; ARO1	CYP19A1	Catalyzes the formation of aromatic C18 estrogens from C19 androgens.	EC 1.14.14.14	5JL9; 5JL7; 5JL6; 5JKW; 5JKV	MVLEMLNPIHYNITSIVPEAMPAATMPVLLLTGLFLLVWNYEGTSSIPGPGYCMGIGPLISHGRFLWMGIGSACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKLGLQCIGMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEFFPKPNEFTLENFAKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLHPDETKNMLEMIFTPRNSDRCLEH	Successful	Aminoglutethimide-induced protein free radical formation on myeloperoxidase: a potential mechanism of agranulocytosis. Chem Res Toxicol. 2007 Jul;20(7):1038-45.	34	EC:1.14	Oxidoreductases acting on paired donors	cytochrome P450 family.	1.14.14.14 	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	Cytochrome P450	PF00067	PF00067; p450	.	.	hsa00140:Steroid hormone biosynthesis; hsa01100:Metabolic pathways; hsa04913:Ovarian steroidogenesis	R-HSA-211976:Endogenous sterols	MetaCyc:HS06413-MON	P11511
TTS1DTU	Cholesterol 25-hydroxylase	.	CP1A2_HUMAN	Single Protein	Cytochrome P450 1A2; Cytochrome P(3)450; Cytochrome P450 4; Cytochrome P450-P3; Cytochrome P-448; Hydroperoxy icosatetraenoate dehydratase; CYPIA2; Cytochrome P-450d; Cytochrome P450-D; Cytochrome P450-P3	CYP1A2	"A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens."	.	.	MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKNPHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDGQSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELMAGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFPILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGNLIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLSDRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPELWEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLEFSVPPGVKVDLTPIYGLTMKHARCEHVQARLRFSIN	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P05177
TTI84H7	Cytochrome P450 1B1 (CYP1B1)	Q16678	CP1B1_HUMAN	Paired donor oxygen oxidoreductase	CYPIB1	CYP1B1	"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."	EC 1.14.14.-	6IQ5; 3PM0	MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLIGNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAFASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVALLVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSLVDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSAEKKAAGDSHGGGARLDLENVPATITDIFGASQDTLSTALQWLLLLFTRYPDVQTRVQAELDQVVGRDRLPCMGDQPNLPYVLAFLYEAMRFSSFVPVTIPHATTANTSVLGYHIPKDTVVFVNQWSVNHDPLKWPNPENFDPARFLDKDGLINKDLTSRVMIFSVGKRRCIGEELSKMQLFLFISILAHQCDFRANPNEPAKMNFSYGLTIKPKSFKVNVTLRESMELLDSAVQNLQAKETCQ	Clinical trial	Selective inhibition of methoxyflavonoids on human CYP1B1 activity. Bioorg Med Chem. 2010 Sep 1;18(17):6310-5.	21	EC:1.14	Oxidoreductases acting on paired donors	cytochrome P450 family.	1.14.14.1 	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	Cytochrome P450	PF00067	PF00067; p450	.	.	hsa00140:Steroid hormone biosynthesis; hsa00380:Tryptophan metabolism; hsa00980:Metabolism of xenobiotics by cytochrome P450; hsa04913:Ovarian steroidogenesis; hsa05204:Chemical carcinogenesis; hsa05206:MicroRNAs in cancer	R-HSA-211976:Endogenous sterols	MetaCyc:HS06443-MON	Q16678
TTP4GLG	Steroid 21-hydroxylase (CYP21A2)	P08686	CP21A_HUMAN	Cytochrome P450 family	21-OHase; Cytochrome P-450c21; Cytochrome P450 21; Cytochrome P450 XXI; Cytochrome P450-C21; Cytochrome P450-C21B	CYP21A2	"A cytochrome P450 monooxygenase that plays a major role in adrenal steroidogenesis. Catalyzes the hydroxylation at C-21 of progesterone and 17alpha-hydroxyprogesterone to respectively form 11-deoxycorticosterone and 11-deoxycortisol, intermediate metabolites in the biosynthetic pathway of mineralocorticoids and glucocorticoids (PubMed:25855791, PubMed:10602386, PubMed:16984992, PubMed:22014889, PubMed:27721825). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:25855791). {ECO:0000269|PubMed:10602386, ECO:0000269|PubMed:16984992, ECO:0000269|PubMed:22014889, ECO:0000269|PubMed:25855791, ECO:0000269|PubMed:27721825}."	EC 1.14.14.16	4Y8W	MLLLGLLLLPLLAGARLLWNWWKLRSLHLPPLAPGFLHLLQPDLPIYLLGLTQKFGPIYRLHLGLQDVVVLNSKRTIEEAMVKKWADFAGRPEPLTYKLVSKNYPDLSLGDYSLLWKAHKKLTRSALLLGIRDSMEPVVEQLTQEFCERMRAQPGTPVAIEEEFSLLTCSIICYLTFGDKIKDDNLMPAYYKCIQEVLKTWSHWSIQIVDVIPFLRFFPNPGLRRLKQAIEKRDHIVEMQLRQHKESLVAGQWRDMMDYMLQGVAQPSMEEGSGQLLEGHVHMAAVDLLIGGTETTANTLSWAVVFLLHHPEIQQRLQEELDHELGPGASSSRVPYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTRPSSISGYDIPEGTVIIPNLQGAHLDETVWERPHEFWPDRFLEPGKNSRALAFGCGARVCLGEPLARLELFVVLTRLLQAFTLLPSGDALPSLQPLPHCSVILKMQPFQVRLQPRGMGAHSPGQNQ	Clinical trial	"Clinical pipeline report, company report or official report of Adrenas Therapeutics"	.	.	.	.	.	.	.	.	.	.	.	hsa:1589	R-HSA-193993;R-HSA-194002;R-HSA-211976;R-HSA-5579021;	MetaCyc:HS09769-MONOMER;	P08686;
TT82UI1	Cytochrome P450 24 (CYP24A1)	Q07973	CP24A_HUMAN	Paired donor oxygen oxidoreductase	"Vitamin D(3) 24hydroxylase; Cytochrome P450CC24; CYP24A1; 24OHase; 1,25dihydroxyvitamin D(3) 24hydroxylase, mitochondrial"	CYP24A1	"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."	EC 1.14.15.16	.	MSSPISKSRSLAAFLQQLRSPRQPPRLVTSTAYTSPQPREVPVCPLTAGGETQNAAALPGPTSWPLLGSLLQILWKGGLKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPGEVMKLDNKINEVLADFMGRIDELCDERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMSTFGRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSADFLCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKGTVLMLNTQVLGSSEDNFEDSSQFRPERWLQEKEKINPFAHLPFGVGKRMCIGRRLAELQLHLALCWIVRKYDIQATDNEPVEMLHSGTLVPSRELPIAFCQR	Clinical trial	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800022679)"	21	.	.	.	.	.	.	.	.	.	.	hsa00100:Steroid biosynthesis; hsa01100:Metabolic pathways; hsa05206:MicroRNAs in cancer	R-HSA-196791:Vitamin D (calciferol) metabolism	MetaCyc:HS00395-MON	Q07973
TTD7Q0R	Cytochrome P450 26 (CYP26A1)	O43174	CP26A_HUMAN	Paired donor oxygen oxidoreductase	Retinoic acid-metabolizing cytochrome; Retinoic acid inducible enzyme; Retinoic acid 4-hydroxylase; P450RAI; P450 retinoic acid-inactivating 1; HP450RAI; Cytochrome P450RAI; CYP26A1	CYP26A1	"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."	EC 1.14.13.-	.	MGLPALLASALCTFVLPLLLFLAAIKLWDLYCVSGRDRSCALPLPPGTMGFPFFGETLQMVLQRRKFLQMKRRKYGFIYKTHLFGRPTVRVMGADNVRRILLGEHRLVSVHWPASVRTILGSGCLSNLHDSSHKQRKKVIMRAFSREALECYVPVITEEVGSSLEQWLSCGERGLLVYPEVKRLMFRIAMRILLGCEPQLAGDGDSEQQLVEAFEEMTRNLFSLPIDVPFSGLYRGMKARNLIHARIEQNIRAKICGLRASEAGQGCKDALQLLIEHSWERGERLDMQALKQSSTELLFGGHETTASAATSLITYLGLYPHVLQKVREELKSKGLLCKSNQDNKLDMEILEQLKYIGCVIKETLRLNPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVAEIFTNKEEFNPDRFMLPHPEDASRFSFIPFGGGLRSCVGKEFAKILLKIFTVELARHCDWQLLNGPPTMKTSPTVYPVDNLPARFTHFHGEI	Clinical trial	Novel azolyl-(phenylmethyl)]aryl/heteroarylamines: potent CYP26 inhibitors and enhancers of all-trans retinoic acid activity in neuroblastoma cells. Bioorg Med Chem. 2008 Sep 1;16(17):8301-13.	24	.	.	.	.	.	.	.	.	.	.	hsa00830:Retinol metabolism; hsa01100:Metabolic pathways	R-HSA-211916: Vitamins; R-HSA-5365859: RA biosynthesis pathway	.	O43174
TT7N01U	Cytochrome P450 2A5 (CYP2A5)	P20853	CP2A7_HUMAN	Paired donor oxygen oxidoreductase	Cytochrome P450-IIA3.2; Cytochrome P450-15-COH; Cyp2a5; Cyp2a-5; CYPIIA5	Cyp2a5	Exhibits a high coumarin 7-hydroxylase activity.	EC 1.14.14.1	.	MLASGLLLVALLACLTVMVLMSVWQQRKSRGKLPPGPTPLPFIGNYLQLNTEHICDSIMKFSECYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVAFSNGERAKQLLRFAIATLRDFGVGKRGIEERIQEESGFLIEAIRSTHGANIDPTFFLSRTVSNVISSIVFGDRFDYEDKEFLSLLSMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFKLLQGLEDFIAKKVEHNQRTLDPNSPQDFIDSFLIHMQEEEKNPNTEFYLKNLMMSTLNLFIAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRTKMPYMEAVIHEIQRFGDVIPMSLARRVKKDTKFRDFFLPKGTEVFPMLGSVLRDPSFFSNPQDFNPQHFLDDKGQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVVFATIPRNYTMSFLPR	Literature-reported	"DrugBank: a knowledgebase for drugs, drug actions and drug targets. Nucleic Acids Res. 2008 Jan;36(Database issue):D901-6."	.	.	.	.	.	.	.	.	.	.	.	hsa00232: Caffeine metabolism; hsa00830: Retinol metabolism; hsa00980: Metabolism of xenobiotics by cytochrome P450; hsa00982: Drug metabolism - cytochrome P450; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa05204: Chemical carcinogenesis - DNA adducts; hsa05417: Lipid and atherosclerosis	R-HSA-211935: Fatty acids; R-HSA-211981: Xenobiotics; R-HSA-211999: CYP2E1 reactions	.	P20853
TTAQ6ZW	Cytochrome P450 2A6 (CYP2A6)	P11509	CP2A6_HUMAN	Paired donor oxygen oxidoreductase	Cytochrome P450(I); Cytochrome P450 IIA3; Coumarin 7-hydroxylase; CYPIIA6; CYP2A6; CYP2A3	CYP2A6	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.	EC 1.14.13.-	4RUI; 4EJJ; 3T3R; 3T3Q; 3EBS	MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMKISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSNGERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDALRGTGGANIDPTFFLSRTVSNVISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQLLQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFIGGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYMEAVIHEIQRFGDVIPMSLARRVKKDTKFRDFFLPKGTEVYPMLGSVLRDPSFFSNPQDFNPQHFLNEKGQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVGFATIPRNYTMSFLPR	Successful	"DrugBank: a knowledgebase for drugs, drug actions and drug targets. Nucleic Acids Res. 2008 Jan;36(Database issue):D901-6."	.	.	.	.	.	.	.	.	.	.	.	hsa00232: Caffeine metabolism; hsa00830: Retinol metabolism; hsa00980: Metabolism of xenobiotics by cytochrome P450; hsa00982: Drug metabolism - cytochrome P450; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa05204: Chemical carcinogenesis - DNA adducts; hsa05417: Lipid and atherosclerosis	R-HSA-211981: Xenobiotics; R-HSA-211999: CYP2E1 reactions	MetaCyc:HS10343-MON	P11509
TTMH124	Cytochrome P450 2B6 (CYP2B6)	P20813	CP2B6_HUMAN	Paired donor oxygen oxidoreductase	"Cytochrome P450 IIB1; CYPIIB6; 1,4-cineole 2-exo-monooxygenase"	CYP2B6	"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."	EC 1.14.13.-	5WBG; 5UFG; 5UEC; 5UDA; 5UAP	MELSVLLFLALLTGLLLLLVQRHPNTHDRLPPGPRPLPLLGNLLQMDRRGLLKSFLRFREKYGDVFTVHLGPRPVVMLCGVEAIREALVDKAEAFSGRGKIAMVDPFFRGYGVIFANGNRWKVLRRFSVTTMRDFGMGKRSVEERIQEEAQCLIEELRKSKGALMDPTFLFQSITANIICSIVFGKRFHYQDQEFLKMLNLFYQTFSLISSVFGQLFELFSGFLKYFPGAHRQVYKNLQEINAYIGHSVEKHRETLDPSAPKDLIDTYLLHMEKEKSNAHSEFSHQNLNLNTLSLFFAGTETTSTTLRYGFLLMLKYPHVAERVYREIEQVIGPHRPPELHDRAKMPYTEAVIYEIQRFSDLLPMGVPHIVTQHTSFRGYIIPKDTEVFLILSTALHDPHYFEKPDAFNPDHFLDANGALKKTEAFIPFSLGKRICLGEGIARAELFLFFTTILQNFSMASPVAPEDIDLTPQECGVGKIPPTYQIRFLPR	Literature-reported	"DrugBank: a knowledgebase for drugs, drug actions and drug targets. Nucleic Acids Res. 2008 Jan;36(Database issue):D901-6."	.	EC:1.14	Oxidoreductases acting on paired donors	cytochrome P450 family.	1.14.13.-	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	Cytochrome P450	PF00067	PF00067; p450	.	.	hsa00590: Arachidonic acid metabolism; hsa00830: Retinol metabolism; hsa00980: Metabolism of xenobiotics by cytochrome P450; hsa00982: Drug metabolism - cytochrome P450; hsa01100: Metabolic pathways; hsa05207: Chemical carcinogenesis - receptor activation; hsa05417: Lipid and atherosclerosis	R-HSA-211935: Fatty acids; R-HSA-211981: Xenobiotics; R-HSA-211999: CYP2E1 reactions	MetaCyc:HS09587-MON	P20813
TTZ58XG	Mephenytoin 4-hydroxylase	.	CP2CJ_HUMAN	Single Protein	Cytochrome P450 2C19; (R)-limonene 6-monooxygenase; (S)-limonene 6-monooxygenase; (S)-limonene 7-monooxygenase; CYPIIC17; CYPIIC19; Cytochrome P450-11A; Cytochrome P450-254C; Fenbendazole monooxygenase (4'-hydroxylating)	CYP2C19	"A cytochrome P450 monooxygenase involved in the metabolism of polyunsaturated fatty acids (PUFA). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates PUFA specifically at the omega-1 position. Catalyzes the epoxidation of double bonds of PUFA. Also metabolizes plant monoterpenes."	.	.	MDPFVVLVLCLSCLLLLSIWRQSSGRGKLPPGPTPLPVIGNILQIDIKDVSKSLTNLSKIYGPVFTLYFGLERMVVLHGYEVVKEALIDLGEEFSGRGHFPLAERANRGFGIVFSNGKRWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFQKRFDYKDQQFLNLMEKLNENIRIVSTPWIQICNNFPTIIDYFPGTHNKLLKNLAFMESDILEKVKEHQESMDINNPRDFIDCFLIKMEKEKQNQQSEFTIENLVITAADLLGAGTETTSTTLRYALLLLLKHPEVTAKVQEEIERVVGRNRSPCMQDRGHMPYTDAVVHEVQRYIDLIPTSLPHAVTCDVKFRNYLIPKGTTILTSLTSVLHDNKEFPNPEMFDPRHFLDEGGNFKKSNYFMPFSAGKRICVGEGLARMELFLFLTFILQNFNLKSLIDPKDLDTTPVVNGFASVPPFYQLCFIPV	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P33261
TTR40YJ	S-mephenytoin 4-hydroxylase (CYP2C9)	P11712	CP2C9_HUMAN	Paired donor oxygen oxidoreductase	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	CYP2C9	"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."	EC 1.14.14.-	5XXI; 5X24; 5X23; 5W0C; 5K7K	MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKVYGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFMKSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTETTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYIDLLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFKKSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVPPFYQLCFIPV	Successful	Identification of amino acid substitutions that confer a high affinity for sulfaphenazole binding and a high catalytic efficiency for warfarin meta... Biochemistry. 1998 Nov 17;37(46):16270-9.	34	EC:1.14	.	cytochrome P450 family.	1.14.14.- 	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	Cytochrome P450	PF00067	PF00067; p450	.	.	hsa00590: Arachidonic acid metabolism; hsa00591: Linoleic acid metabolism; hsa00830: Retinol metabolism; hsa00980: Metabolism of xenobiotics by cytochrome P450; hsa00982: Drug metabolism - cytochrome P450; hsa01100: Metabolic pathways; hsa04726: Serotonergic synapse; hsa05204: Chemical carcinogenesis - DNA adducts; hsa05417: Lipid and atherosclerosis	R-HSA-211981: Xenobiotics; R-HSA-211999: CYP2E1 reactions; R-HSA-2142670: Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET); R-HSA-2142816: Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE); R-HSA-9027307: Biosynthesis of maresin-like SPMs; R-HSA-9749641: Aspirin ADME	MetaCyc:HS06458-MON	P11712
TTVG215	Debrisoquine 4-hydroxylase (CYP2D6)	P10635	CP2D6_HUMAN	Paired donor oxygen oxidoreductase	P450-DB1; Cytochrome P450-DB1; Cytochrome P450 2D6; CYPIID6; CYP2DL1	CYP2D6	"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."	EC 1.14.14.-	6CSD; 6CSB; 5TFU; 5TFT; 4XRZ	MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGVFAFLVSPSPYELCAVPR	Successful	A study of the effects of large doses of glutethimide that were used for self-poisoning during pregnancy on human fetuses. Toxicol Ind Health. 2008 Feb-Mar;24(1-2):69-78.	34	EC:1.14	Oxidoreductases acting on paired donors	cytochrome P450 family.	1.14.14.1 	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	Cytochrome P450	PF00067	PF00067; p450	.	.	hsa00980:Metabolism of xenobiotics by cytochrome P450; hsa00982:Drug metabolism - cytochrome P450; hsa04726:Serotonergic synapse	R-HSA-211981:Xenobiotics	MetaCyc:HS01997-MON	P10635
TTWVHQ5	Cytochrome P450 2E1	.	CP2E1_HUMAN	Single Protein	Cytochrome P450-J; 4-nitrophenol 2-hydroxylase; CYPIIE1	CYP2E1	"A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids."	.	.	MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRLAQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGPTWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVIADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVAEVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAGTETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRFITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGKFKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGCIPPRYKLCVIPRS	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P05181
TTNE1C7	Cytochrome P450 2J2	.	CP2J2_HUMAN	Single Protein	Albendazole monooxygenase (hydroxylating); Albendazole monooxygenase (sulfoxide-forming); Arachidonic acid epoxygenase; CYPIIJ2; Hydroperoxy icosatetraenoate isomerase	CYP2J2	"A cytochrome P450 monooxygenase involved in the metabolism of polyunsaturated fatty acids (PUFA) in the cardiovascular system. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of PUFA. Converts arachidonic acid to four regioisomeric epoxyeicosatrienoic acids (EpETrE)."	.	.	MLAAMGSLAAALWAVVHPRTLLLGTVAFLLAADFLKRRRPKNYPPGPWRLPFLGNFFLVDFEQSHLEVQLFVKKYGNLFSLELGDISAVLITGLPLIKEALIHMDQNFGNRPVTPMREHIFKKNGLIMSSGQAWKEQRRFTLTALRNFGLGKKSLEERIQEEAQHLTEAIKEENGQPFDPHFKINNAVSNIICSITFGERFEYQDSWFQQLLKLLDEVTYLEASKTCQLYNVFPWIMKFLPGPHQTLFSNWKKLKLFVSHMIDKHRKDWNPAETRDFIDAYLKEMSKHTGNPTSSFHEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQGQQPSTAARESMPYTNAVIHEVQRMGNIIPLNVPREVTVDTTLAGYHLPKGTMILTNLTALHRDPTEWATPDTFNPDHFLENGQFKKREAFMPFSIGKRACLGEQLARTELFIFFTSLMQKFTFRPPNNEKLSLKFRMGITISPVSHRLCAVPQV	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P51589
TTWP7HQ	CYP3A4 messenger RNA (CYP3A4 mRNA)	P08684	CP3A4_HUMAN	mRNA target	"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)"	CYP3A4	"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."	EC 1.14.14.-	6BDM; 6BDK; 6BDI; 6BDH; 6BD8	MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTVSGA	Clinical trial	Phosphorodiamidate morpholino antisense oligomers inhibit expression of human cytochrome P450 3A4 and alter selected drug metabolism. Drug Metab Dispos. 2002 Jul;30(7):757-62.	21	mRNA	mRNA target	.	.	.	Cytochrome P450	PF00067	PF00067; p450	.	.	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	R-HSA-211981:Xenobiotics; R-HSA-5423646:Aflatoxin activation and detoxification	MetaCyc:HS08544-MON	P08684
TTXV4FI	Albendazole monooxygenase (CYP3A4)	P08684	CP3A4_HUMAN	Paired donor oxygen oxidoreductase	"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"	CYP3A4	"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."	EC 1.14.14.-	6BDM; 6BDK; 6BDI; 6BDH; 6BD8	MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTVSGA	Clinical trial	Structure-activity relationships for the inhibition of recombinant human cytochromes P450 by curcumin analogues. Eur J Med Chem. 2008 Aug;43(8):1621-31.	25	EC:1.14	Paired donor oxidoreductase	cytochrome P450 family.	1.14.14.-	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	Cytochrome P450	PF00067	PF00067; p450	.	.	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	R-HSA-211981:Xenobiotics; R-HSA-5423646:Aflatoxin activation and detoxification	MetaCyc:HS08544-MON	P08684
TTHS0OK	Cytochrome P450 3A5	.	CP3A5_HUMAN	Single Protein	Cytochrome P450-PCN3; Cytochrome P450 CYP3A5; CYPIIIA5	CYP3A5	"A cytochrome P450 monooxygenase involved in the metabolism of steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of catechol estrogens from 17beta-estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2."	.	.	MDLIPNLAVETWLLLAVSLVLLYLYGTRTHGLFKRLGIPGPTPLPLLGNVLSYRQGLWKFDTECYKKYGKMWGTYEGQLPVLAITDPDVIRTVLVKECYSVFTNRRSLGPVGFMKSAISLAEDEEWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVRNLRREAEKGKPVTLKDIFGAYSMDVITGTSFGVNIDSLNNPQDPFVESTKKFLKFGFLDPLFLSIILFPFLTPVFEALNVSLFPKDTINFLSKSVNRMKKSRLNDKQKHRLDFLQLMIDSQNSKETESHKALSDLELAAQSIIFIFAGYETTSSVLSFTLYELATHPDVQQKLQKEIDAVLPNKAPPTYDAVVQMEYLDMVVNETLRLFPVAIRLERTCKKDVEINGVFIPKGSMVVIPTYALHHDPKYWTEPEEFRPERFSKKKDSIDPYIYTPFGTGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLDTQGLLQPEKPIVLKVDSRDGTLSGE	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P20815
TT4EB85	Cholesterol 24-hydroxylase (CYP46A1)	Q9Y6A2	CP46A_HUMAN	Paired donor oxygen oxidoreductase	Cytochrome P450 46A1; CYP46; Cholesterol 24S-hydroxylase; Cholesterol 24-monooxygenase; CH24H	CYP46A1	"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."	EC 1.14.14.25	4J14; 4FIA; 4ENH; 3MDV; 3MDT	MSPGLLLLGSAVLLAFGLCCTFVHRARSRYEHIPGPPRPSFLLGHLPCFWKKDEVGGRVLQDVFLDWAKKYGPVVRVNVFHKTSVIVTSPESVKKFLMSTKYNKDSKMYRALQTVFGERLFGQGLVSECNYERWHKQRRVIDLAFSRSSLVSLMETFNEKAEQLVEILEAKADGQTPVSMQDMLTYTAMDILAKAAFGMETSMLLGAQKPLSQAVKLMLEGITASRNTLAKFLPGKRKQLREVRESIRFLRQVGRDWVQRRREALKRGEEVPADILTQILKAEEGAQDDEGLLDNFVTFFIAGHETSANHLAFTVMELSRQPEIVARLQAEVDEVIGSKRYLDFEDLGRLQYLSQVLKESLRLYPPAWGTFRLLEEETLIDGVRVPGNTPLLFSTYVMGRMDTYFEDPLTFNPDRFGPGAPKPRFTYFPFSLGHRSCIGQQFAQMEVKVVMAKLLQRLEFRLVPGQRFGLQEQATLKPLDPVLCTLRPRGWQPAPPPPPC	Clinical trial	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800040983)"	21	EC:1.14	Oxidoreductases acting on paired donors	cytochrome P450 family.	1.14.14.25 	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	Cytochrome P450	PF00067	PF00067; p450	.	.	hsa00120:Primary bile acid biosynthesis	R-HSA-211976:Endogenous sterols	.	Q9Y6A2
TTTHCPF	Cholesterol 24-monooxygenase (CYP46A1)	Q9Y6A2	CP46A_HUMAN	.	Cytochrome P450 46A1; Cholesterol 24S-hydroxylase; CYP46; CH24H	CYP46A1	"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."	EC 1.14.14.25	4J14; 4FIA; 4ENH; 3MDV; 3MDT	MSPGLLLLGSAVLLAFGLCCTFVHRARSRYEHIPGPPRPSFLLGHLPCFWKKDEVGGRVLQDVFLDWAKKYGPVVRVNVFHKTSVIVTSPESVKKFLMSTKYNKDSKMYRALQTVFGERLFGQGLVSECNYERWHKQRRVIDLAFSRSSLVSLMETFNEKAEQLVEILEAKADGQTPVSMQDMLTYTAMDILAKAAFGMETSMLLGAQKPLSQAVKLMLEGITASRNTLAKFLPGKRKQLREVRESIRFLRQVGRDWVQRRREALKRGEEVPADILTQILKAEEGAQDDEGLLDNFVTFFIAGHETSANHLAFTVMELSRQPEIVARLQAEVDEVIGSKRYLDFEDLGRLQYLSQVLKESLRLYPPAWGTFRLLEEETLIDGVRVPGNTPLLFSTYVMGRMDTYFEDPLTFNPDRFGPGAPKPRFTYFPFSLGHRSCIGQQFAQMEVKVVMAKLLQRLEFRLVPGQRFGLQEQATLKPLDPVLCTLRPRGWQPAPPPPPC	Discontinued	"Clinical pipeline report, company report or official report of Boston Millennia Partners."	3	.	.	.	.	.	.	.	.	.	.	hsa00120: Primary bile acid biosynthesis	R-HSA-193775: Synthesis of bile acids and bile salts via 24-hydroxycholesterol; R-HSA-211976: Endogenous sterols	.	Q9Y6A2
TTXLYW2	Cytochrome P450 4f (P450-4F)	P78329; Q08477	CP4F2_HUMAN; CP4F3_HUMAN	Paired donor oxygen oxidoreductase	Leukotriene-B(4) omega-hydroxylase; Leukotriene-B(4) 20-monooxygenase; Cytochrome P450-LTB-omega; CYPIVF; 20-hydroxyeicosatetraenoic acid synthase; 20-HETE synthase	CYP4F2	"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."	.	.	MSQLSLSWLGLWPVAASPWLLLLLVGASWLLAHVLAWTYAFYDNCRRLRCFPQPPRRNWFWGHQGMVNPTEEGMRVLTQLVATYPQGFKVWMGPISPLLSLCHPDIIRSVINASAAIAPKDKFFYSFLEPWLGDGLLLSAGDKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQLLASEGSACLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVSKRHHEILLHIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFIDVLLLSKDEDGKKLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQERCRQEVQELLKDREPKEIEWDDLAHLPFLTMCMKESLRLHPPVPVISRHVTQDIVLPDGRVIPKGIICLISVFGTHHNPAVWPDPEVYDPFRFDPENIKERSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALTLLRFRVLPDHTEPRRKPELVLRAEGGLWLRVEPLS	Literature-reported	"Cytochrome P4504f, a potential therapeutic target limiting neuroinflammation. Biochem Pharmacol. 2011 Jul 1;82(1):53-64."	.	.	.	.	.	.	.	.	.	.	.	hsa00590: Arachidonic acid metabolism; hsa01100: Metabolic pathways	R-HSA-211935: Fatty acids; R-HSA-211958: Miscellaneous substrates; R-HSA-211979: Eicosanoids; R-HSA-2142691: Synthesis of Leukotrienes (LT) and Eoxins (EX); R-HSA-2142816: Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE)	MetaCyc:HS02675-MON	P78329
TT67TDP	Lanosterol 14-alpha demethylase (CYP51A1)	Q16850	CP51A_HUMAN	Cytochrome P450 family	Cytochrome P450LI; Cytochrome P45014DM; Cytochrome P450-14DM; Cytochrome P450 51A1	CYP51A1	"Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol."	EC 1.14.14.154	4UHL; 4UHI; 3LD6; 3JUV; 3JUS	MLLLGLLQAGGSVLGQAMEKVTGGNLLSMLLIACAFTLSLVYLIRLAAGHLVQLPAGVKSPPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNSKNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSIIEKETKEYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWLLPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGRPLTDDEVAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTYDQLKDLNLLDRCIKETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWVERLDFNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFPTVNYTTMIHTPENPVIRYKRRSK	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	hsa00100:Steroid biosynthesis; hsa01100:Metabolic pathways	R-HSA-191273: Cholesterol biosynthesis; R-HSA-211976: Endogenous sterols; R-HSA-2426168: Activation of gene expression by SREBF (SREBP); R-HSA-9619665: EGR2 and SOX10-mediated initiation of Schwann cell myelination	MetaCyc:HS00076-MON	Q16850
TTQ7W6D	Cysteine-rich angiogenic inducer 61 (CYR61)	O00622	CYR61_HUMAN	.	CCN1	CYR61	"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."	.	4D11; 4D0Z	MSSRIARALALVVTLLHLTRLALSTCPAACHCPLEAPKCAPGVGLVRDGCGCCKVCAKQLNEDCSKTQPCDHTKGLECNFGASSTALKGICRAQSEGRPCEYNSRIYQNGESFQPNCKHQCTCIDGAVGCIPLCPQELSLPNLGCPNPRLVKVTGQCCEEWVCDEDSIKDPMEDQDGLLGKELGFDASEVELTRNNELIAVGKGSSLKRLPVFGMEPRILYNPLQGQKCIVQTTSWSQCSKTCGTGISTRVTNDNPECRLVKETRICEVRPCGQPVYSSLKKGKKCSKTKKSPEPVRFTYAGCLSVKKYRPKYCGSCVDGRCCTPQLTRTVKMRFRCEDGETFSKNVMMIQSCKCNYNCPHANEAAFPFYRLFNDIHKFRD	Literature-reported	Acute Kidney Injury (AKI) biomarker. Acta Med Indones. 2012 Jul;44(3):246-55.	.	.	.	CCN family.	.	.	Cystine-knot domain; Insulin-like growth factor binding protein; von Willebrand factor type C domain	PF00007; PF00219; PF00093	PF00007; Cys_knot; PF00219; IGFBP; PF00093; VWC	.	.	.	R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation	.	.
TTGKOY9	Leukotriene CysLT1 receptor (CYSLTR1)	Q9Y271	CLTR1_HUMAN	GPCR rhodopsin	Leukotriene D4-receptor; LTD4 receptor; HMTMF81; HG55; G-protein coupled receptor HG55; Cysteinyl leukotriene receptor 1; Cysteinyl leukotriene D4 receptor; CysLTR1; CYSLT1	CYSLTR1	"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."	.	.	MDETGNLTVSSATCHDTIDDFRNQVYSTLYSMISVVGFFGNGFVLYVLIKTYHKKSAFQVYMINLAVADLLCVCTLPLRVVYYVHKGIWLFGDFLCRLSTYALYVNLYCSIFFMTAMSFFRCIAIVFPVQNINLVTQKKARFVCVGIWIFVILTSSPFLMAKPQKDEKNNTKCFEPPQDNQTKNHVLVLHYVSLFVGFIIPFVIIIVCYTMIILTLLKKSMKKNLSSHKKAIGMIMVVTAAFLVSFMPYHIQRTIHLHFLHNETKPCDSVLRMQKSVVITLSLAASNCCFDPLLYFFSGGNFRKRLSTFRKHSLSSVTYVPRKKASLPEKGEEICKV	Successful	Protective potential of montelukast against hepatic ischemia/reperfusion injury in rats. J Surg Res. 2010 Mar;159(1):588-94.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.13.2	The G-protein-coupled receptor (GPCR) Family	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction	R-HSA-391906:Leukotriene receptors; R-HSA-416476:G alpha (q) signalling events	.	Q9Y271
TTSB6CA	HUMAN cysteinyl leukotriene receptor (CysLTR)	Q9Y271; Q9NS75	CLTR1_HUMAN; CLTR2_HUMAN	G-protein coupled receptor 1 family	.	CYSLTR1	"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."	.	.	MDETGNLTVSSATCHDTIDDFRNQVYSTLYSMISVVGFFGNGFVLYVLIKTYHKKSAFQVYMINLAVADLLCVCTLPLRVVYYVHKGIWLFGDFLCRLSTYALYVNLYCSIFFMTAMSFFRCIAIVFPVQNINLVTQKKARFVCVGIWIFVILTSSPFLMAKPQKDEKNNTKCFEPPQDNQTKNHVLVLHYVSLFVGFIIPFVIIIVCYTMIILTLLKKSMKKNLSSHKKAIGMIMVVTAAFLVSFMPYHIQRTIHLHFLHNETKPCDSVLRMQKSVVITLSLAASNCCFDPLLYFFSGGNFRKRLSTFRKHSLSSVTYVPRKKASLPEKGEEICKV	.	As a potential treatment of COVID-19: Montelukast. Med Hypotheses. 2020 May 11;142:109828.	.	.	.	.	.	.	.	.	.	.	.	hsa04020: Calcium signaling pathway; hsa04080: Neuroactive ligand-receptor interaction	R-HSA-391906: Leukotriene receptors; R-HSA-416476: G alpha (q) signalling events; R-HSA-9664535: LTC4-CYSLTR mediated IL4 production; R-HSA-9679191: Potential therapeutics for SARS	.	Q9Y271
TT0PZR5	Leukotriene CysLT2 receptor (CYSLTR2)	Q9NS75	CLTR2_HUMAN	GPCR rhodopsin	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	CYSLTR2	"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."	.	.	MERKFMSLQPSISVSEMEPNGTFSNNNSRNCTIENFKREFFPIVYLIIFFWGVLGNGLSIYVFLQPYKKSTSVNVFMLNLAISDLLFISTLPFRADYYLRGSNWIFGDLACRIMSYSLYVNMYSSIYFLTVLSVVRFLAMVHPFRLLHVTSIRSAWILCGIIWILIMASSIMLLDSGSEQNGSVTSCLELNLYKIAKLQTMNYIALVVGCLLPFFTLSICYLLIIRVLLKVEVPESGLRVSHRKALTTIIITLIIFFLCFLPYHTLRTVHLTTWKVGLCKDRLHKALVITLALAAANACFNPLLYYFAGENFKDRLKSALRKGHPQKAKTKCVFPVSVWLRKETRV	Clinical trial	"The effect of a novel leukotriene C4/D4 antagonist, BAY-x-7195, on experimental allergic reactions. Prostaglandins. 1995 Nov-Dec;50(5-6):269-85."	21	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction	R-HSA-391906:Leukotriene receptors; R-HSA-416476:G alpha (q) signalling events	.	Q9NS75
TTOM97J	Cytohesin-2 messenger RNA (CYTH2 mRNA)	Q99418	CYH2_HUMAN	mRNA target	"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)"	CYTH2	"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)."	.	4Z21; 4L5M; 4JXH; 4JWL; 4JMO	MEDGVYEPPDLTPEERMELENIRRRKQELLVEIQRLREELSEAMSEVEGLEANEGSKTLQRNRKMAMGRKKFNMDPKKGIQFLVENELLQNTPEEIARFLYKGEGLNKTAIGDYLGEREELNLAVLHAFVDLHEFTDLNLVQALRQFLWSFRLPGEAQKIDRMMEAFAQRYCLCNPGVFQSTDTCYVLSFAVIMLNTSLHNPNVRDKPGLERFVAMNRGINEGGDLPEELLRNLYDSIRNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVDDPRKPNCFELYIPNNKGQLIKACKTEADGRVVEGNHMVYRISAPTQEEKDEWIKSIQAAVSVDPFYEMLAARKKRISVKKKQEQP	Literature-reported	"US patent application no. 6,271,029, Antisense inhibition of cytohesin-2 expression."	0	mRNA	mRNA target	.	.	.	PH domain; Sec7 domain	PF00169; PF01369	PF00169; PH; PF01369; Sec7	.	.	hsa04144:Endocytosis	R-HSA-6811438: Intra-Golgi traffic	.	Q99418
TTN0Z6H	Disheveled-associated activator of morphogenesis 2 (DAAM2)	Q86T65	DAAM2_HUMAN	.	KIAA0381; Disheveledassociated activator of morphogenesis 2	DAAM2	"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."	.	.	MAPRKRSHHGLGFLCCFGGSDIPEINLRDNHPLQFMEFSSPIPNAEELNIRFAELVDELDLTDKNREAMFALPPEKKWQIYCSKKKEQEDPNKLATSWPDYYIDRINSMAAMQSLYAFDEEETEMRNQVVEDLKTALRTQPMRFVTRFIELEGLTCLLNFLRSMDHATCESRIHTSLIGCIKALMNNSQGRAHVLAQPEAISTIAQSLRTENSKTKVAVLEILGAVCLVPGGHKKVLQAMLHYQVYAAERTRFQTLLNELDRSLGRYRDEVNLKTAIMSFINAVLNAGAGEDNLEFRLHLRYEFLMLGIQPVIDKLRQHENAILDKHLDFFEMVRNEDDLELARRFDMVHIDTKSASQMFELIHKKLKYTEAYPCLLSVLHHCLQMPYKRNGGYFQQWQLLDRILQQIVLQDERGVDPDLAPLENFNVKNIVNMLINENEVKQWRDQAEKFRKEHMELVSRLERKERECETKTLEKEEMMRTLNKMKDKLARESQELRQARGQVAELVAQLSELSTGPVSSPPPPGGPLTLSSSMTTNDLPPPPPPLPFACCPPPPPPPLPPGGPPTPPGAPPCLGMGLPLPQDPYPSSDVPLRKKRVPQPSHPLKSFNWVKLNEERVPGTVWNEIDDMQVFRILDLEDFEKMFSAYQRHQKELGSTEDIYLASRKVKELSVIDGRRAQNCIILLSKLKLSNEEIRQAILKMDEQEDLAKDMLEQLLKFIPEKSDIDLLEEHKHEIERMARADRFLYEMSRIDHYQQRLQALFFKKKFQERLAEAKPKVEAILLASRELVRSKRLRQMLEVILAIGNFMNKGQRGGAYGFRVASLNKIADTKSSIDRNISLLHYLIMILEKHFPDILNMPSELQHLPEAAKVNLAELEKEVGNLRRGLRAVEVELEYQRRQVREPSDKFVPVMSDFITVSSFSFSELEDQLNEARDKFAKALMHFGEHDSKMQPDEFFGIFDTFLQAFSEARQDLEAMRRRKEEEERRARMEAMLKEQRERERWQRQRKVLAAGSSLEEGGEFDDLVSALRSGEVFDKDLCKLKRSRKRSGSQALEVTRERAINRLNY	Literature-reported	Daam2 driven degradation of VHL promotes gliomagenesis. Elife. 2017 Oct 20;6. pii: e31926.	.	.	Formin homology family	formin homology family.	.	.	Diaphanous FH3 Domain; Diaphanous GTPase-binding Domain; Formin Homology 2 Domain	PF06367; PF06371; PF02181	PF06367; Drf_FH3; PF06371; Drf_GBD; PF02181; FH2	.	.	hsa04310: Wnt signaling pathway	.	.	Q86T65
TT4X7PG	Dystroglycan (DAG1)	Q14118	DAG1_HUMAN	Dystroglycan protein	Dystrophin-associated glycoprotein 1; Alpha-dystroglycan	DAG1	"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."	.	5LLK; 5GGP; 2MK7; 1EG4	MRMSVGLSLLLPLSGRTFLLLLSVVMAQSHWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEGLPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVRTASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIHGVEAPAREGAMSAQLGYPVVGWHIANKKPPLPKRVRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPGQIRPTMTIPGYVEPTAVATPPTTTTKKPRVSTPKPATPSTDSTTTTTRRPTKKPRTPRPVPRVTTKVSITRLETASPPTRIRTTTSGVPRGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDHEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHRRPQGDRAPARFKAKFVGDPALVLNDIHKKIALVKKLAFAFGDRNCSTITLQNITRGSIVVEWTNNTLPLEPCPKEQIAGLSRRIAEDDGKPRPAFSNALEPDFKATSITVTGSGSCRHLQFIPVVPPRRVPSEAPPTEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQDTMGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP	Literature-reported	Deficiency of alpha-dystroglycan in muscle-eye-brain disease. Biochem Biophys Res Commun. 2002 Mar 15;291(5):1283-6.	.	TC=9.B.277	Transmembrane protein	.	.	.	Alpha-Dystroglycan N-terminal domain 2; Dystroglycan (Dystrophin-associated glycoprotein 1)	PF18424; PF05454	PF18424; a_DG1_N2; PF05454; DAG1	9.B.277.1.1	The Dystroglycan (DG) Family	hsa04512: ECM-receptor interaction; hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy; hsa05416: Viral myocarditis	"R-HSA-3000171: Non-integrin membrane-ECM interactions; R-HSA-3000178: ECM proteoglycans; R-HSA-5083628: Defective POMGNT1 causes MDDGA3, MDDGB3 and MDDGC3; R-HSA-5083629: Defective POMT2 causes MDDGA2, MDDGB2 and MDDGC2; R-HSA-5083633: Defective POMT1 causes MDDGA1, MDDGB1 and MDDGC1; R-HSA-5173105: O-linked glycosylation; R-HSA-9010553: Regulation of expression of SLITs and ROBOs; R-HSA-9619665: EGR2 and SOX10-mediated initiation of Schwann cell myelination"	.	Q14118
TTRQ6UD	Diacylglycerol lipase alpha (DAGLA)	Q9Y4D2	DGLA_HUMAN	Carboxylic ester hydrolase	Sn1-specific diacylglycerol lipase alpha; Neural stem cell-derived dendrite regulator; NSDDR; KIAA0659; DGL-alpha; C11orf11	DAGLA	"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."	EC 3.1.1.-	.	MPGIVVFRRRWSVGSDDLVLPAIFLFLLHTTWFVILSVVLFGLVYNPHEACSLNLVDHGRGYLGILLSCMIAEMAIIWLSMRGGILYTEPRDSMQYVLYVRLAILVIEFIYAIVGIVWLTQYYTSCNDLTAKNVTLGMVVCNWVVILSVCITVLCVFDPTGRTFVKLRATKRRQRNLRTYNLRHRLEEGQATSWSRRLKVFLCCTRTKDSQSDAYSEIAYLFAEFFRDLDIVPSDIIAGLVLLRQRQRAKRNAVLDEANNDILAFLSGMPVTRNTKYLDLKNSQEMLRYKEVCYYMLFALAAYGWPMYLMRKPACGLCQLARSCSCCLCPARPRFAPGVTIEEDNCCGCNAIAIRRHFLDENMTAVDIVYTSCHDAVYETPFYVAVDHDKKKVVISIRGTLSPKDALTDLTGDAERLPVEGHHGTWLGHKGMVLSAEYIKKKLEQEMVLSQAFGRDLGRGTKHYGLIVVGHSLGAGTAAILSFLLRPQYPTLKCFAYSPPGGLLSEDAMEYSKEFVTAVVLGKDLVPRIGLSQLEGFRRQLLDVLQRSTKPKWRIIVGATKCIPKSELPEEVEVTTLASTRLWTHPSDLTIALSASTPLYPPGRIIHVVHNHPAEQCCCCEQEEPTYFAIWGDNKAFNEVIISPAMLHEHLPYVVMEGLNKVLENYNKGKTALLSAAKVMVSPTEVDLTPELIFQQQPLPTGPPMPTGLALELPTADHRNSSVRSKSQSEMSLEGFSEGRLLSPVVAAAARQDPVELLLLSTQERLAAELQARRAPLATMESLSDTESLYSFDSRRSSGFRSIRGSPSLHAVLERDEGHLFYIDPAIPEENPSLSSRTELLAADSLSKHSQDTQPLEAALGSGGVTPERPPSAAANDEEEEVGGGGGGPASRGELALHNGRLGDSPSPQVLEFAEFIDSLFNLDSKSSSFQDLYCMVVPESPTSDYAEGPKSPSQQEILLRAQFEPNLVPKPPRLFAGSADPSSGISLSPSFPLSSSGELMDLTPTGLSSQECLAADKIRTSTPTGHGASPAKQDELVISAR	Patented-recorded	A patent review of Monoacylglycerol Lipase (MAGL) inhibitors (2013-2017).Expert Opin Ther Pat. 2017 Dec;27(12):1341-1351.	15.5	EC:3.1.1	AB hydrolase superfamily	AB hydrolase superfamily. Lipase family.	3.1.1.-	Acting on ester bonds	Lipase (class 3)	PF01764	PF01764; Lipase_3	.	.	hsa04723: Retrograde endocannabinoid signaling; hsa04925: Aldosterone synthesis and secretion	R-HSA-426048: Arachidonate production from DAG	MetaCyc:ENSG00000134780-MON	Q9Y4D2
TTXZDEN	Diacylglycerol lipase beta (DAGLB)	Q8NCG7	DGLB_HUMAN	.	Sn1-specific diacylglycerol lipase beta; KCCR13L; DGL-beta	DAGLB	"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."	EC 3.1.1.-	.	MPGMVLFGRRWAIASDDLVFPGFFELVVRVLWWIGILTLYLMHRGKLDCAGGALLSSYLIVLMILLAVVICTVSAIMCVSMRGTICNPGPRKSMSKLLYIRLALFFPEMVWASLGAAWVADGVQCDRTVVNGIIATVVVSWIIIAATVVSIIIVFDPLGGKMAPYSSAGPSHLDSHDSSQLLNGLKTAATSVWETRIKLLCCCIGKDDHTRVAFSSTAELFSTYFSDTDLVPSDIAAGLALLHQQQDNIRNNQEPAQVVCHAPGSSQEADLDAELENCHHYMQFAAAAYGWPLYIYRNPLTGLCRIGGDCCRSRTTDYDLVGGDQLNCHFGSILHTTGLQYRDFIHVSFHDKVYELPFLVALDHRKESVVVAVRGTMSLQDVLTDLSAESEVLDVECEVQDRLAHKGISQAARYVYQRLINDGILSQAFSIAPEYRLVIVGHSLGGGAAALLATMLRAAYPQVRCYAFSPPRGLWSKALQEYSQSFIVSLVLGKDVIPRLSVTNLEDLKRRILRVVAHCNKPKYKILLHGLWYELFGGNPNNLPTELDGGDQEVLTQPLLGEQSLLTRWSPAYSFSSDSPLDSSPKYPPLYPPGRIIHLQEEGASGRFGCCSAAHYSAKWSHEAEFSKILIGPKMLTDHMPDILMRALDSVVSDRAACVSCPAQGVSSVDVA	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1397).	0	.	.	.	.	.	.	.	.	.	.	hsa04723: Retrograde endocannabinoid signaling; hsa04925: Aldosterone synthesis and secretion	R-HSA-426048: Arachidonate production from DAG	MetaCyc:ENSG00000164535-MON	Q8NCG7
TT7Y3EJ	D-amino acid oxidase (DAO)	P14920	OXDA_HUMAN	CH-NH(2) donor oxidoreductase	Daminoacid oxidase; DAMOX; DAAO	DAO	"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."	EC 1.4.3.3	5ZJA; 5ZJ9; 4QFD; 4QFC; 3ZNQ	MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPNNPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPRELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVNCTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGGIFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGPSNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	"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"	R-HSA-389661: Glyoxylate metabolism and glycine degradation; R-HSA-9033241: Peroxisomal protein import	MetaCyc:HS03351-MON	P14920
TTERVQN	Death-associated protein kinase 3 (DAPK3)	O43293	DAPK3_HUMAN	Kinase	Zipper-interacting protein kinase; ZIPK; ZIP-kinase; MYPT1 kinase; DAP-like kinase; DAP kinase 3	DAPK3	"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."	EC 2.7.11.1	5VJA; 5A6O; 5A6N; 3BQR; 3BHY	MSTFRQEDVEDHYEMGEELGSGQFAIVRKCRQKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVNILREIRHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAHKIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKAIRRRNVRGEDSGRKPERRRLKTTRLKEYTIKSHSSLPPNNSYADFERFSKVLEEAAAAEEGLRELQRSRRLCHEDVEALAAIYEEKEAWYREESDSLGQDLRRLRQELLKTEALKRQAQEEAKGALLGTSGLKRRFSRLENRYEALAKQVASEMRFVQDLVRALEQEKLQGVECGLR	Literature-reported	"Discovery, synthesis, and characterization of an orally bioavailable, brain penetrant inhibitor of mixed lineage kinase 3. J Med Chem. 2013 Oct 24;56(20):8032-48."	0	EC:2.7	.	protein kinase superfamily. CAMK Ser/Thr protein kinase family. DAP kinase subfamily.	2.7.11.1 	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04140: Autophagy - animal; hsa05200: Pathways in cancer; hsa05219: Bladder cancer	R-HSA-418889: Caspase activation via Dependence Receptors in the absence of ligand	.	O43293
TTYIP79	Dopamine beta hydroxylase (DBH)	P09172	DOPO_HUMAN	Paired donor oxygen oxidoreductase	Soluble dopamine betahydroxylase; Dopamine betamonooxygenase; Dopamine betahydroxylase; Dopamine beta-monooxygenase; Dopamine beta-hydroxylase	DBH	Conversion of dopamine to noradrenaline.	EC 1.14.17.1	4ZEL	MPALSRWASLPGPSMREAAFMYSTAVAIFLVILVAALQGSAPRESPLPYHIPLDPEGSLELSWNVSYTQEAIHFQLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSDQKGQIHLDPQQDYQLLQVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQMGLQRVQLLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVTKGNEALVHHMEVFQCAPEMDSVPHFSGPCDSKMKPDRLNYCRHVLAAWALGAKAFYYPEEAGLAFGGPGSSRYLRLEVHYHNPLVIEGRNDSSGIRLYYTAKLRRFNAGIMELGLVYTPVMAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIVNQDNHYSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHYYPQTQLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQFTSVPWNSFNRDVLKALYSFAPISMHCNKSSAVRFQGEWNLQPLPKVISTLEEPTPQCPTSQGRSPAGPTVVSIGGGKG	Clinical trial	"Safety, tolerability, and pharmacokinetics of etamicastat, a novel dopamine-beta-hydroxylase inhibitor, in a rising multiple-dose study in young healthy subjects. Drugs R D. 2010;10(4):225-42."	21	EC:1.14	Oxidoreductases acting on paired donors	copper type II ascorbate-dependent monooxygenase family.	1.14.17.1 	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	"Copper type II ascorbate-dependent monooxygenase, C-terminal domain; Copper type II ascorbate-dependent monooxygenase, N-terminal domain; DOMON domain"	PF03712; PF01082; PF03351	PF03712; Cu2_monoox_C; PF01082; Cu2_monooxygen; PF03351; DOMON	.	.	hsa00350:Tyrosine metabolism; hsa01100:Metabolic pathways	R-HSA-209905: Catecholamine biosynthesis	MetaCyc:MON66-381	P09172
TTJOCE4	Deoxycytidine kinase (DCK)	P27707	DCK_HUMAN	Kinase	dCK	DCK	"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."	EC 2.7.1.74	5MQT; 5MQL; 5MQJ; 4Q1F; 4Q1E	MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCNVQSTQDEFEELTMSQKNGGNVLQMMYEKPERWSFTFQTYACLSRIRAQLASLNGKLKDAEKPVLFFERSVYSDRYIFASNLYESECMNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQATPETCLHRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFDYLQEVPILTLDVNEDFKDKYESLVEKVKEFLSTL	Literature-reported	236th ACS National Meeting	0	.	.	.	.	.	.	.	.	.	.	hsa00230: Purine metabolism; hsa00240: Pyrimidine metabolism; hsa01100: Metabolic pathways; hsa01232: Nucleotide metabolism	R-HSA-73614: Pyrimidine salvage; R-HSA-74217: Purine salvage	MetaCyc:HS08100-MON	P27707
TTOHTCY	Doublecortin-like kinase 1 (DCLK1)	O15075	DCLK1_HUMAN	Kinase	Serine/threonine-protein kinase DCLK1; KIAA0369; Doublecortin-like and CAM kinase-like 1; Doublecortin domain-containing protein 3A; DCDC3A; DCAMKL1	DCLK1	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.	EC 2.7.11.1	5JZN; 5JZJ; 1UF0; 1MG4; 1MFW	MSFGRDMELEHFDERDKAQRYSRGSRVNGLPSPTHSAHCSFYRTRTLQTLSSEKKAKKVRFYRNGDRYFKGIVYAISPDRFRSFEALLADLTRTLSDNVNLPQGVRTIYTIDGLKKISSLDQLVEGESYVCGSIEPFKKLEYTKNVNPNWSVNVKTTSASRAVSSLATAKGSPSEVRENKDFIRPKLVTIIRSGVKPRKAVRILLNKKTAHSFEQVLTDITDAIKLDSGVVKRLYTLDGKQVMCLQDFFGDDDIFIACGPEKFRYQDDFLLDESECRVVKSTSYTKIASSSRRSTTKSPGPSRRSKSPASTSSVNGTPGSQLSTPRSGKSPSPSPTSPGSLRKQRSSQHGGSSTSLASTKVCSSMDENDGPGEEVSEEGFQIPATITERYKVGRTIGDGNFAVVKECVERSTAREYALKIIKKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDVPTELYLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATIVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQVDFPSPYWDNVSDSAKELITMMLLVDVDQRFSAVQVLEHPWVNDDGLPENEHQLSVAGKIKKHFNTGPKPNSTAAGVSVIATTALDKERQVFRRRRNQDVRSRYKAQPAPPELNSESEDYSPSSSETVRSPNSPF	Literature-reported	"Synthesis and structure-activity relationships of 1,2,3,4-tetrahydropyrido[2,3-b]pyrazines as potent and selective inhibitors of the anaplastic lymphoma kinase. Bioorg Med Chem. 2010 Jun 15;18(12):4351-62."	0	EC:2.7	.	protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Doublecortin; Protein kinase domain	PF03607; PF00069	PF03607; DCX; PF00069; Pkinase	.	.	.	.	.	O15075
TTHK3MO	Doublecortin-like kinase 2 (DCLK2)	Q8N568	DCLK2_HUMAN	Kinase	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	DCLK2	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.	EC 2.7.11.1	.	MASTRSIELEHFEERDKRPRPGSRRGAPSSSGGSSSSGPKGNGLIPSPAHSAHCSFYRTRTLQALSSEKKAKKARFYRNGDRYFKGLVFAISSDRFRSFDALLIELTRSLSDNVNLPQGVRTIYTIDGSRKVTSLDELLEGESYVCASNEPFRKVDYTKNINPNWSVNIKGGTSRALAAASSVKSEVKESKDFIKPKLVTVIRSGVKPRKAVRILLNKKTAHSFEQVLTDITEAIKLDSGVVKRLCTLDGKQVTCLQDFFGDDDVFIACGPEKFRYAQDDFVLDHSECRVLKSSYSRSSAVKYSGSKSPGPSRRSKSPASVNGTPSSQLSTPKSTKSSSSSPTSPGSFRGLKQISAHGRSSSNVNGGPELDRCISPEGVNGNRCSESSTLLEKYKIGKVIGDGNFAVVKECIDRSTGKEFALKIIDKAKCCGKEHLIENEVSILRRVKHPNIIMLVEEMETATELFLVMELVKGGDLFDAITSSTKYTERDGSAMVYNLANALRYLHGLSIVHRDIKPENLLVCEYPDGTKSLKLGDFGLATVVEGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFDQILAGKLEFPAPYWDNITDSAKELISQMLQVNVEARCTAGQILSHPWVSDDASQENNMQAEVTGKLKQHFNNALPKQNSTTTGVSVIMNTALDKEGQIFCSKHCQDSGRPGMEPISPVPPSVEEIPVPGEAVPAPTPPESPTPHPPPAAPGGERAGTWRRHRD	Literature-reported	Pharmacological inhibition of BMK1 suppresses tumor growth through promyelocytic leukemia protein. Cancer Cell. 2010 Sep 14;18(3):258-67.	0	EC:2.7	.	protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Doublecortin; Protein kinase domain	PF03607; PF00069	PF03607; DCX; PF00069; Pkinase	.	.	.	.	.	Q8N568
TTMYK4Z	Doublecortin-like kinase 3 (DCLK3)	Q9C098	DCLK3_HUMAN	Kinase	Serine/threonine-protein kinase DCLK3; KIAA1765; Doublecortin-like and CAM kinase-like 3; Doublecortin domain-containing protein 3C; DCDC3C; DCAMKL3	DCLK3	"Protein kinase activity, peptidyl-serine phosphorylation."	EC 2.7.11.1	.	MGKEPLTLKSIQVAVEELYPNKARALTLAQHSRAPSPRLRSRLFSKALKGDHRCGETETPKSCSEVAGCKAAMRHQGKIPEELSLDDRARTQKKWGRGKWEPEPSSKPPREATLEERHARGEKHLGVEIEKTSGEIIRCEKCKRERELQQSLERERLSLGTSELDMGKGPMYDVEKLVRTRSCRRSPEANPASGEEGWKGDSHRSSPRNPTQELRRPSKSMDKKEDRGPEDQESHAQGAAKAKKDLVEVLPVTEEGLREVKKDTRPMSRSKHGGWLLREHQAGFEKLRRTRGEEKEAEKEKKPCMSGGRRMTLRDDQPAKLEKEPKTRPEENKPERPSGRKPRPMGIIAANVEKHYETGRVIGDGNFAVVKECRHRETRQAYAMKIIDKSRLKGKEDMVDSEILIIQSLSHPNIVKLHEVYETDMEIYLILEYVQGGDLFDAIIESVKFPEPDAALMIMDLCKALVHMHDKSIVHRDLKPENLLVQRNEDKSTTLKLADFGLAKHVVRPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERDQDELFNIIQLGHFEFLPPYWDNISDAAKDLVSRLLVVDPKKRYTAHQVLQHPWIETAGKTNTVKRQKQVSPSSEGHFRSQHKRVVEQVS	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2007).	0	EC:2.7	.	protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	.	Q9C098
TTB3XAN	Decorin (DCN)	P07585	PGS2_HUMAN	.	SLRR1B; PGS2; PG40; PG-S2; Bone proteoglycan II	DCN	May affect the rate of fibrils formation.	.	.	MKATIILLLLAQVSWAGPFQQRGLFDFMLEDEASGIGPEVPDDRDFEPSLGPVCPFRCQCHLRVVQCSDLGLDKVPKDLPPDTTLLDLQNNKITEIKDGDFKNLKNLHALILVNNKISKVSPGAFTPLVKLERLYLSKNQLKELPEKMPKTLQELRAHENEITKVRKVTFNGLNQMIVIELGTNPLKSSGIENGAFQGMKKLSYIRIADTNITSIPQGLPPSLTELHLDGNKISRVDAASLKGLNNLAKLGLSFNSISAVDNGSLANTPHLRELHLDNNKLTRVPGGLAEHKYIQVVYLHNNNISVVGSSDFCPPGHNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRSAIQLGNYK	Literature-reported	Decorin over-expression by decidual cells in preeclampsia: a potential blood biomarker. Am J Obstet Gynecol. 2016 Sep;215(3):361.e1-361.e15.	.	.	.	small leucine-rich proteoglycan (SLRP) family. SLRP class I subfamily.	.	.	Leucine rich repeat; Leucine rich repeat N-terminal domain	PF13855; PF01462	PF13855; LRR_8; PF01462; LRRNT	.	.	hsa04350: TGF-beta signaling pathway; hsa05205: Proteoglycans in cancer	"R-HSA-1474228: Degradation of the extracellular matrix; R-HSA-1971475: A tetrasaccharide linker sequence is required for GAG synthesis; R-HSA-2022870: Chondroitin sulfate biosynthesis; R-HSA-2022923: Dermatan sulfate biosynthesis; R-HSA-2024101: CS/DS degradation; R-HSA-3000178: ECM proteoglycans; R-HSA-3560783: Defective B4GALT7 causes EDS, progeroid type; R-HSA-3560801: Defective B3GAT3 causes JDSSDHD; R-HSA-3595172: Defective CHST3 causes SEDCJD; R-HSA-3595174: Defective CHST14 causes EDS, musculocontractural type; R-HSA-3595177: Defective CHSY1 causes TPBS; R-HSA-4420332: Defective B3GALT6 causes EDSP2 and SEMDJL1"	.	P07585
TTLSW9V	Scavenger decapping enzyme DcpS (DCPS)	Q96C86	DCPS_HUMAN	Acid anhydrides hydrolase	Scavenger mRNA-decapping enzyme DcpS; Histidine triad protein member5; Hint-related 7meGMP-directed hydrolase; HINT-5; DCS-1; DCPS	DCPS	"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."	EC 3.6.1.59	5OSY; 4QEB; 4QDV; 4QDE; 3BLA	MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS	Clinical trial	2011 Pipeline of Repligen.	17	.	.	.	.	.	.	.	.	.	.	hsa03018:RNA degradation	R-HSA-429958: mRNA decay by 3' to 5' exoribonuclease	.	Q96C86
TTZ1YIS	HUMAN dCTP pyrophosphatase 1	Q9H773	DCTP1_HUMAN	.	XTP3-transactivated gene A protein ; RS21C6 ; Deoxycytidine-triphosphatase 1; dCTPase 1	DCTPP1	"Human protein dCTP pyrophosphatase 1 interacts with SARS-CoV-2 Orf9b protein with high significance, which indicates DCTPP1 as a potential therapeutic target."	EC 3.6.1.12	.	MSVAGGEIRGDTGGEDTAAPGRFSFSPEPTLEDIRRLHAEFAAERDWEQFHQPRNLLLALVGEVGELAELFQWKTDGEPGPQGWSPRERAALQEELSDVLIYLVALAARCRVDLPLAVLSKMDINRRRYPAHLARSSSRKYTELPHGAISEDQAVGPADIPCDSTGQTST	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa00240: Pyrimidine metabolism; hsa01100: Metabolic pathways; hsa01232: Nucleotide metabolism	R-HSA-499943: Interconversion of nucleotide di- and triphosphates	.	Q9H773
TTN451K	Aromatic-L-amino-acid decarboxylase (DDC)	P20711	DDC_HUMAN	Carbon-carbon lyase	DOPA decarboxylase; AADC	DDC	"Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine."	EC 4.1.1.28	3RCH; 3RBL; 3RBF	MNASEFRRRGKEMVDYMANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDVEKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIMEKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMVATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVNEALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE	Successful	Functional COMT variant predicts response to high dose pyridoxine in Parkinson's disease. Am J Med Genet B Neuropsychiatr Genet. 2005 Aug 5;137B(1):1-4.	34	EC:4.1	Carbon carbon lyase	group II decarboxylase family.	4.1.1.28	Carbon-carbon lyases	Pyridoxal-dependent decarboxylase conserved domain	PF00282	PF00282; Pyridoxal_deC	.	.	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	R-HSA-209905: Catecholamine biosynthesis; R-HSA-209931: Serotonin and melatonin biosynthesis	MetaCyc:HS05635-MON	P20711
TTVEOY6	RTP801 messenger RNA (RTP801 mRNA)	Q9NX09	DDIT4_HUMAN	mRNA target	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)	DDIT4	"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)."	.	3LQ9	MPSLWDRFSSSSTSSSPSSLPRTPTPDRPPRSAWGSATREEGFDRSTSLESSDCESLDSSNSGFGPEEDTAYLDGVSLPDFELLSDPEDEHLCANLMQLLQESLAQARLGSRRPARLLMPSQLVSQVGKELLRLAYSEPCGLRGALLDVCVEQGKSCHSVGQLALDPSLVPTFQLTLVLRLDSRLWPKIQGLFSSANSPFLPGFSQSLTLSTGFRVIKKKLYSSEQLLIEEC	Clinical trial	DNA-damage-inducible transcript 4 (DDIT4; RTP801). SciBX 3(20); doi:10.1038/scibx.2010.629. May 20 2010	21	mRNA	mRNA target	.	.	.	RTP801 C-terminal region	PF07809	PF07809; RTP801_C	.	.	hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa05206:MicroRNAs in cancer	R-HSA-5628897:TP53 Regulates Metabolic Genes	.	Q9NX09
TT0AWFK	HIF-1 responsive protein RTP801 (DDIT4)	Q9NX09	DDIT4_HUMAN	.	RTP801; REDD1; REDD-1; Protein regulated in development and DNA damage response 1; DNA damage-inducible transcript 4 protein	DDIT4	"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."	.	3LQ9	MPSLWDRFSSSSTSSSPSSLPRTPTPDRPPRSAWGSATREEGFDRSTSLESSDCESLDSSNSGFGPEEDTAYLDGVSLPDFELLSDPEDEHLCANLMQLLQESLAQARLGSRRPARLLMPSQLVSQVGKELLRLAYSEPCGLRGALLDVCVEQGKSCHSVGQLALDPSLVPTFQLTLVLRLDSRLWPKIQGLFSSANSPFLPGFSQSLTLSTGFRVIKKKLYSSEQLLIEEC	Clinical trial	Teaming up to tackle RNAi delivery challenge. Nat Rev Drug Discov. 2009 Jul;8(7):525-6.	21	.	.	.	.	.	.	.	.	.	.	hsa04140: Autophagy - animal; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa05206: MicroRNAs in cancer	R-HSA-5628897: TP53 Regulates Metabolic Genes	.	Q9NX09
TTI1FPZ	Epithelial discoidin domain receptor 1 (DDR1)	Q08345	DDR1_HUMAN	Kinase	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	DDR1	"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."	EC 2.7.10.1	6HP9; 6GWR; 6FIQ; 6FIO; 6FIN	MGPEALSSLLLLLLVASGDADMKGHFDPAKCRYALGMQDRTIPDSDISASSSWSDSTAARHSRLESSDGDGAWCPAGSVFPKEEEYLQVDLQRLHLVALVGTQGRHAGGLGKEFSRSYRLRYSRDGRRWMGWKDRWGQEVISGNEDPEGVVLKDLGPPMVARLVRFYPRADRVMSVCLRVELYGCLWRDGLLSYTAPVGQTMYLSEAVYLNDSTYDGHTVGGLQYGGLGQLADGVVGLDDFRKSQELRVWPGYDYVGWSNHSFSSGYVEMEFEFDRLRAFQAMQVHCNNMHTLGARLPGGVECRFRRGPAMAWEGEPMRHNLGGNLGDPRARAVSVPLGGRVARFLQCRFLFAGPWLLFSEISFISDVVNNSSPALGGTFPPAPWWPPGPPPTNFSSLELEPRGQQPVAKAEGSPTAILIGCLVAIILLLLLIIALMLWRLHWRRLLSKAERRVLEEELTVHLSVPGDTILINNRPGPREPPPYQEPRPRGNPPHSAPCVPNGSALLLSNPAYRLLLATYARPPRGPGPPTPAWAKPTNTQAYSGDYMEPEKPGAPLLPPPPQNSVPHYAEADIVTLQGVTGGNTYAVPALPPGAVGDGPPRVDFPRSRLRFKEKLGEGQFGEVHLCEVDSPQDLVSLDFPLNVRKGHPLLVAVKILRPDATKNARNDFLKEVKIMSRLKDPNIIRLLGVCVQDDPLCMITDYMENGDLNQFLSAHQLEDKAAEGAPGDGQAAQGPTISYPMLLHVAAQIASGMRYLATLNFVHRDLATRNCLVGENFTIKIADFGMSRNLYAGDYYRVQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEVLMLCRAQPFGQLTDEQVIENAGEFFRDQGRQVYLSRPPACPQGLYELMLRCWSRESEQRPPFSQLHRFLAEDALNTV	Patented-recorded	"Discovery and optimization of 3-(2-(Pyrazolo[1,5-a]pyrimidin-6-yl)ethynyl)benzamides as novel selective and orally bioavailable discoidin domain receptor 1 (DDR1) inhibitors. J Med Chem. 2013 Apr 25;56(8):3281-95."	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	F5/8 type C domain; Protein tyrosine kinase	PF00754; PF07714	PF00754; F5_F8_type_C; PF07714; Pkinase_Tyr	.	.	.	R-HSA-3000171: Non-integrin membrane-ECM interactions	.	Q08345
TTU98HG	Discoidin domain-containing receptor 2 (DDR2)	Q16832	DDR2_HUMAN	Kinase	"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"	DDR2	"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."	EC 2.7.10.1	6FER; 2Z4F; 2WUH	MILIPRMLLVLFLLLPILSSAKAQVNPAICRYPLGMSGGQIPDEDITASSQWSESTAAKYGRLDSEEGDGAWCPEIPVEPDDLKEFLQIDLHTLHFITLVGTQGRHAGGHGIEFAPMYKINYSRDGTRWISWRNRHGKQVLDGNSNPYDIFLKDLEPPIVARFVRFIPVTDHSMNVCMRVELYGCVWLDGLVSYNAPAGQQFVLPGGSIIYLNDSVYDGAVGYSMTEGLGQLTDGVSGLDDFTQTHEYHVWPGYDYVGWRNESATNGYIEIMFEFDRIRNFTTMKVHCNNMFAKGVKIFKEVQCYFRSEASEWEPNAISFPLVLDDVNPSARFVTVPLHHRMASAIKCQYHFADTWMMFSEITFQSDAAMYNNSEALPTSPMAPTTYDPMLKVDDSNTRILIGCLVAIIFILLAIIVIILWRQFWQKMLEKASRRMLDDEMTVSLSLPSDSSMFNNNRSSSPSEQGSNSTYDRIFPLRPDYQEPSRLIRKLPEFAPGEEESGCSGVVKPVQPSGPEGVPHYAEADIVNLQGVTGGNTYSVPAVTMDLLSGKDVAVEEFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYSQLSDEQVIENTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQQGDE	Patented-recorded	Mutational Landscape of DDR2 Gene in Lung Squamous Cell Carcinoma Using Next-generation Sequencing. Clin Lung Cancer. 2018 Mar;19(2):163-169.e4.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-3000171: Non-integrin membrane-ECM interactions	.	Q16832
TTZKPVC	Phosphorylated p68 RNA helicase (pDDX5)	P17844 (phosphorylated)	DDX5_HUMAN	.	RNA helicase p68 (phosphorylated); Probable ATP-dependent RNA helicase DDX5 (phosphorylated); HLR1 (phosphorylated); HELR (phosphorylated); G17P1 (phosphorylated); DEAD box protein 5 (phosphorylated)	DDX5	"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."	EC 3.6.4.13	4A4D; 3FE2	MSGYSSDRDRGRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSSLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQTSFRTGNPTGTYQNGYDSTQQYGSNVPNMHNGMNQQAYAYPATAAAPMIGYPMPTGYSQ	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	.	.	.	P17844
TTOTSW1	ATP-dependent RNA helicase DDX5 (DDX5)	P17844	DDX5_HUMAN	.	RNA helicase p68; Probable ATP-dependent RNA helicase DDX5; HLR1; HELR; G17P1; DEAD box protein 5	DDX5	"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."	EC 3.6.4.13	4A4D; 3FE2	MSGYSSDRDRGRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSSLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQTSFRTGNPTGTYQNGYDSTQQYGSNVPNMHNGMNQQAYAYPATAAAPMIGYPMPTGYSQ	Clinical trial	Company report (Rexahn)	21	.	.	DEAD box helicase family. DDX5/DBP2 subfamily.	.	.	DEAD/DEAH box helicase; Helicase conserved C-terminal domain; P68HR (NUC004) repeat	PF00270; PF00271; PF08061	PF00270; DEAD; PF00271; Helicase_C; PF08061; P68HR	.	.	hsa03040: Spliceosome; hsa05202: Transcriptional misregulation in cancer; hsa05205: Proteoglycans in cancer	R-HSA-3899300: SUMOylation of transcription cofactors; R-HSA-72163: mRNA Splicing - Major Pathway; R-HSA-9018519: Estrogen-dependent gene expression; R-HSA-9682706: Replication of the SARS-CoV-1 genome; R-HSA-9694686: Replication of the SARS-CoV-2 genome	.	P17844
TTVB0O3	Retinoic acid-inducible gene-1 (RIG-1)	O95786	DDX58_HUMAN	Acid anhydride hydrolase	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	DDX58	"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."	EC 3.6.4.13	6GPG; 5F9H; 5F9F; 5F98; 5E3H	MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAGYSGLYEAIESWDFKKIEKLEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKERNKFSELWIVEKGIKDVETEDLEDKMETSDIQIFYQEDPECQNLSENSCPPSEVSDTNLYSPFKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGSSGPLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATVKHNLEELEQVVYKPQKFFRKVESRISDKFKYIIAQLMRDTESLAKRICKDLENLSQIQNREFGTQKYEQWIVTVQKACMVFQMPDKDEESRICKALFLYTSHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESVSRDPSNENPKLEDLCFILQEEYHLNPETITILFVKTRALVDALKNWIEGNPKLSFLKPGILTGRGKTNQNTGMTLPAQKCILDAFKASGDHNILIATSVADEGIDIAQCNLVILYEYVGNVIKMIQTRGRGRARGSKCFLLTSNAGVIEKEQINMYKEKMMNDSILRLQTWDEAVFREKILHIQTHEKFIRDSQEKPKPVPDKENKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPKPKQFSSFEKRAKIFCARQNCSHDWGIHVKYKTFEIPVIKIESFVVEDIATGVQTLYSKWKDFHFEKIPFDPAEMSK	Clinical trial	Company reprot (Spring Bank Pharmaceuticals) (drug: SB 9200)	17	EC:3.6	Acid anhydrides hydrolase	helicase family. RLR subfamily.	3.6.4.13	Acting on acid anhydrides	Caspase recruitment domain; DEAD/DEAH box helicase; Helicase conserved C-terminal domain; RIG-I receptor C-terminal domain; C-terminal domain of RIG-I	PF16739; PF00270; PF00271; PF18119; PF11648	PF16739; CARD_2; PF00270; DEAD; PF00271; Helicase_C; PF18119; RIG-I_C; PF11648; RIG-I_C-RD	.	.	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	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	.	O95786
TTIVY12	Beta-defensin 4A (DEFB4A)	O15263	DFB4A_HUMAN	.	"hBD2; Skinantimicrobial peptide 1; SAP1; Defensin, beta 2; DEFB4B; DEFB4A; Betadefensin 4A; Betadefensin 2; BD2"	DEFB4A	Has antibacterial activity.	.	6CS9; 1FQQ; 1FD4; 1FD3; 1E4Q	MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP	Literature-reported	Bioactive coating of titanium surfaces with recombinant human -defensin-2 (rHuD2) may prevent bacterial colonization in orthopaedic surgery.J Bone Joint Surg Am.2011 May 4;93(9):840-6.	0	.	.	.	.	.	.	.	.	.	.	hsa04621: NOD-like receptor signaling pathway; hsa04657: IL-17 signaling pathway; hsa05150: Staphylococcus aureus infection	R-HSA-1461957: Beta defensins; R-HSA-1461973: Defensins	.	O15263
TT1NMGV	DEK protein (DEK)	P35659	DEK_HUMAN	.	Protein DEK	DEK	Involved in chromatin organization.	.	2JX3; 1Q1V	MSASAPAAEGEGTPTQPASEKEPEMPGPREESEEEEDEDDEEEEEEEKEKSLIVEGKREKKKVERLTMQVSSLQREPFTIAQGKGQKLCEIERIHFFLSKKKTDELRNLHKLLYNRPGTVSSLKKNVGQFSGFPFEKGSVQYKKKEEMLKKFRNAMLKSICEVLDLERSGVNSELVKRILNFLMHPKPSGKPLPKSKKTCSKGSKKERNSSGMARKAKRTKCPEILSDESSSDEDEKKNKEESSDDEDKESEEEPPKKTAKREKPKQKATSKSKKSVKSANVKKADSSTTKKNQNSSKKESESEDSSDDEPLIKKLKKPPTDEELKETIKKLLASANLEEVTMKQICKKVYENYPTYDLTERKDFIKTTVKELIS	Literature-reported	DEK-targeting DNA aptamers as therapeutics for inflammatory arthritis. Nat Commun. 2017 Feb 6;8:14252.	.	.	.	.	.	.	DEK C terminal domain	PF08766	PF08766; DEK_C	.	.	.	R-HSA-5250924: B-WICH complex positively regulates rRNA expression; R-HSA-8864260: Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors; R-HSA-9616222: Transcriptional regulation of granulopoiesis	.	P35659
TTMYZNX	Dengue virus Envelope (DENV E)	P17763 (281-775)	POLG_DEN1W (281-775)	.	.	DENV E	.	.	.	.	Preclinical	"Neutralization of antibody-enhanced dengue infection by VIS513, a pan serotype reactive monoclonal antibody targeting domain III of the dengue E protein. PLoS Negl Trop Dis. 2018 Feb 9;12(2):e0006209."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNEYST	Dengue virus NS2B/NS3 protease (DENV NS2B/NS3)	P29990	POLG_DEN26	.	Genome polyprotein	DENV NS2B/NS3	"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."	.	4O6B; 2R69	MNDQRKKAKNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLYMALVAFLRFLTIPPTAGILKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRRSAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTEDGVNMCTLMAMDLGELCEDTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTCTTMGEHRRQKRSVALVPHVGMGLETRTETWMSSEGAWKHVQRIETWILRHPGFTMMAAILAYTIGTTHFQRALIFILLTAVTPSMTMRCIGMSNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFRCKKNMEGKVVQPENLEYTIVITPHSGEEHAVGNDTGKHGKEIKITPQSSTTEAELTGYGTVTMECSPRTGLDFNEMVLLQMENKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVFGAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVTLVLVGIVTLYLGVMVQADSGCVVSWKNKELKCGSGIFITDNVHTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITPELNHILSENEVKLTIMTGDIKGIMQAGKRSLRPQPTELKYSWKTWGKAKMLSTESHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLKLKEKQDVFCDSKLMSAAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKNCHWPKSHTLWSNGVLESEMIIPKNLAGPVSQHNYRPGYHTQITGPWHLGKLEMDFDFCDGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENLVNSLVTAGHGQVDNFSLGVLGMALFLEEMLRTRVGTKHAILLVAVSFVTLIIGNMSFRDLGRVMVMVGATMTDDIGMGVTYLALLAAFKVRPTFAAGLLLRKLTSKALMMTTIGIVLSSQSTTPETILELTDALALGMMVLKMVRNMEKYQLAVTIMAILCVPNAVILQNAWKVSCTILAVVSVSPLFLTSSQQKTDWIPLALTIKGLNPTAIFLTTLSRTSKKRSWPLNEAIMAVGMVSILASSLLKNDIPMTGPLVAGGPLTVCYVLTGRSADLELERAADVKWEDQAEISGSSPILSITISEDGSMSIKNEEEEQTLTILIRTGLLVISGLFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPMGKAELEDGAYRIKQKGILGYSQIGAGVYKEGTFHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFKTNAGTIGAVSLDFSPGTSGSPIIDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRRLTIMDLHPGAGKTKRYLPAIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEAHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIIDEEREIPERSWNSGHEWVTDFKGKTVWFVPSIKAGNDIAACLSKNGKKVIQLSRKTFDSEYAKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAGPMPVTHSSAAQRRGRIGRNPKNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRLRGEARTTFVDLMRRGDLPVWLAYRVAAEGINYADRRWCFDGVKNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPLALKEFKEFAAGRKSLTLNLITEMGRLPTFMTQKARDALDNLAVLHTAEAGGRAYNHALSELPETLETLLLLTLLATVTGGILLFLMSGRGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVVIAILTVVAATMANEMGFLEKTKKDLGLGSIATQQPESNILDIDLRPASAWTLYAVATTFVTPMLRHSIENSSVNVSLTAIANQATVLMGLGKGWPLSKMDIGVPLLAIGCYSQVNPTTLTAALFLLVAHYAIIGPALQAKASREAQKRAAAGIMKNPTVDGITVIDLDPIPYDPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEVLTLATGPISTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLFSIMKNTTNARRGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERNMVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFIPPEKCDTLLCDIGESSPNPTVEAGRTLRVLNLVENWLNNNTQFCIKVLNPYMPSVIEKMEALQRKYGGALVRNPLSRNSTHEMYWVSNASGNIVSSVNMISRMLINRFTMRYKKATYEPDVDLGSGTRNIGIESEIPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSYETKQTGSASSMVNGVFRLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKKTPRMCTREEFTRKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDKERNLHLEGKCETCVYNIMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILRDVSKKEGGAMYADDTAGWDTRITLEDLKNEAMVTNHMEGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGVFKSIQHLTITEEIAVQNWLARVGRERLSRMAISGDDCVVKPLDDRLPSALTALNDTGKIRKDIQQWEPSRGWNDWTQVPFCSHHFHELIMKDGRVLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYDQMWSLMYFHRRDLRLAANAICSAVPSHWVPTSRTTWSIHAKHEWMTTEDMLTVWNRVWIQENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQAAINQVRSLIGNEEYTDYMPSMKRFRREEEEAGVLW	Literature-reported	Novel dengue virus NS2B/NS3 protease inhibitors. Antimicrob Agents Chemother. 2015 Feb;59(2):1100-9.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8S9CM	DEP domain-containing protein 1A (DEPDC1)	Q5TB30	DEP1A_HUMAN	.	DEPDC1A	DEPDC1	"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."	.	2YSR	MESQGVPPGPYRATKLWNEVTTSFRAGMPLRKHRQHFKKYGNCFTAGEAVDWLYDLLRNNSNFGPEVTRQQTIQLLRKFLKNHVIEDIKGRWGSENVDDNNQLFRFPATSPLKTLPRRYPELRKNNIENFSKDKDSIFKLRNLSRRTPKRHGLHLSQENGEKIKHEIINEDQENAIDNRELSQEDVEEVWRYVILIYLQTILGVPSLEEVINPKQVIPQYIMYNMANTSKRGVVILQNKSDDLPHWVLSAMKCLANWPRSNDMNNPTYVGFERDVFRTIADYFLDLPEPLLTFEYYELFVNILVVCGYITVSDRSSGIHKIQDDPQSSKFLHLNNLNSFKSTECLLLSLLHREKNKEESDSTERLQISNPGFQERCAKKMQLVNLRNRRVSANDIMGGSCHNLIGLSNMHDLSSNSKPRCCSLEGIVDVPGNSSKEASSVFHQSFPNIEGQNNKLFLESKPKQEFLLNLHSEENIQKPFSAGFKRTSTLTVQDQEELCNGKCKSKQLCRSQSLLLRSSTRRNSYINTPVAEIIMKPNVGQGSTSVQTAMESELGESSATINKRLCKSTIELSENSLLPASSMLTGTQSLLQPHLERVAIDALQLCCLLLPPPNRRKLQLLMRMISRMSQNVDMPKLHDAMGTRSLMIHTFSRCVLCCAEEVDLDELLAGRLVSFLMDHHQEILQVPSYLQTAVEKHLDYLKKGHIENPGDGLFAPLPTYSYCKQISAQEFDEQKVSTSQAAIAELLENIIKNRSLPLKEKRKKLKQFQKEYPLIYQKRFPTTESEAALFGDKPTIKQPMLILRKPKFRSLR	Literature-reported	Cell-permeable peptide DEPDC1-ZNF224 interferes with transcriptional repression and oncogenicity in bladder cancer cells. Cancer Res. 2010 Jul 15;70(14):5829-39.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q5TB30
TTLYP6D	DEP domain-containing protein 6 (DEPTOR)	Q8TB45	DPTOR_HUMAN	.	DEPDC6	DEPTOR	Negative regulator of the mTORC1 and mTORC2 signaling pathways. Inhibits the kinase activity of both complexes.	.	.	MEEGGSTGSAGSDSSTSGSGGAQQRELERMAEVLVTGEQLRLRLHEEKVIKDRRHHLKTYPNCFVAKELIDWLIEHKEASDRETAIKLMQKLADRGIIHHVCDEHKEFKDVKLFYRFRKDDGTFPLDNEVKAFMRGQRLYEKLMSPENTLLQPREEEGVKYERTFMASEFLDWLVQEGEATTRKEAEQLCHRLMEHGIIQHVSNKHPFVDSNLLYQFRMNFRRRRRLMELLNEKSPSSQETHDSPFCLRKQSHDNRKSTSFMSVSPSKEIKIVSAVRRSSMSSCGSSGYFSSSPTLSSSPPVLCNPKSVLKRPVTSEELLTPGAPYARKTFTIVGDAVGWGFVVRGSKPCHIQAVDPSGPAAAAGMKVCQFVVSVNGLNVLHVDYRTVSNLILTGPRTIVMEVMEELEC	Literature-reported	DEP domain-containing mTOR-interacting protein suppresses lipogenesis and ameliorates hepatic steatosis and acute-on-chronic liver injury in alcoho... Hepatology. 2018 Aug;68(2):496-514.	.	.	.	.	.	.	.	.	.	.	.	hsa04140:Autophagy - animal; hsa04150:mTOR signaling pathway	.	.	Q8TB45
TTYVQ9C	DNA fragmentation factor alpha (DFFA)	O00273	DFFA_HUMAN	.	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	DFFA	Inhibitor of the caspase-activated DNase (DFF40).	.	1KOY; 1IYR; 1IBX	MEVTGDAGVPESGEIRTLKPCLLRRNYSREQHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLPSNTKFVALASNEKWAYNNSDGGTAWISQESFDVDETDSGAGLKWKNVARQLKEDLSSIILLSEEDLQMLVDAPCSDLAQELRQSCATVQRLQHTLQQVLDQREEVRQSKQLLQLYLQALEKEGSLLSKQEESKAAFGEEVDAVDTGISRETSSDVALASHILTALREKQAPELSLSSQDLELVTKEDPKALAVALNWDIKKTETVQEACERELALRLQQTQSLHSLRSISASKASPPGDLQNPKRARQDPT	Literature-reported	Growth phase-dependent expression of ICAD-L/DFF45 modulates the pattern of apoptosis in human colonic cancer cells. Cancer Res. 2002 Apr 1;62(7):2169-74.	.	.	.	.	.	.	"CIDE-N domain; DNA Fragmentation factor 45kDa, C terminal domain"	PF02017; PF09033	PF02017; CIDE-N; PF09033; DFF-C	.	.	hsa04210: Apoptosis	R-HSA-140342: Apoptosis induced DNA fragmentation	.	O00273
TT2SRE0	Caspase-activated deoxyribonuclease (DFFB)	O76075	DFFB_HUMAN	.	DFFB; DFF-40; Caspase-activated nuclease; Caspase-activated DNase; CPAN	DFFB	Nuclease that induces DNA fragmentation andchromatin condensation during apoptosis. Degrades naked DNA and induces apoptotic morphology.	EC 3.-.-.-	1IBX	MLQKPKSVKLRALRSPRKFGVAGRSCQEVLRKGCLRFQLPERGSRLCLYEDGTELTEDYFPSVPDNAELVLLTLGQAWQGYVSDIRRFLSAFHEPQVGLIQAAQQLLCDEQAPQRQRLLADLLHNVSQNIAAETRAEDPPWFEGLESRFQSKSGYLRYSCESRIRSYLREVSSYPSTVGAEAQEEFLRVLGSMCQRLRSMQYNGSYFDRGAKGGSRLCTPEGWFSCQGPFDMDSCLSRHSINPYSNRESRILFSTWNLDHIIEKKRTIIPTLVEAIKEQDGREVDWEYFYGLLFTSENLKLVHIVCHKKTTHKLNCDPSRIYKPQTRLKRKQPVRKRQ	Literature-reported	Growth phase-dependent expression of ICAD-L/DFF45 modulates the pattern of apoptosis in human colonic cancer cells. Cancer Res. 2002 Apr 1;62(7):2169-74.	.	.	.	.	.	.	.	.	.	.	.	hsa04210: Apoptosis	R-HSA-140342: Apoptosis induced DNA fragmentation	.	O76075
TT0GV3R	DGAT1 messenger RNA (DGAT1 mRNA)	O75907	DGAT1_HUMAN	mRNA target	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)	DGAT1	"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."	EC 2.3.1.20	.	MGDRGSSRRRRTGSRPSSHGGGGPAAAEEEVRDAAAGPDVGAAGDAPAPAPNKDGDAGVGSGHWELRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQVVSLFLKDPYSWPAPCLVIAANVFAVAAFQVEKRLAVGALTEQAGLLLHVANLATILCFPAAVVLLVESITPVGSLLALMAHTILFLKLFSYRDVNSWCRRARAKAASAGKKASSAAAPHTVSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWMVPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREFYRDWWNSESVTYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWMARTGVFLASAFFHEYLVSVPLRMFRLWAFTGMMAQIPLAWFVGRFFQGNYGNAAVWLSLIIGQPIAVLMYVHDYYVLNYEAPAAEA	Literature-reported	"Discovery of a potent, selective, and orally efficacious pyrimidinooxazinyl bicyclooctaneacetic acid diacylglycerol acyltransferase-1 inhibitor. J Med Chem. 2009 Mar 26;52(6):1558-68."	15.5	mRNA	mRNA target	.	.	.	"MBOAT, membrane-bound O-acyltransferase family"	PF03062	PF03062; MBOAT	.	.	hsa00561:Glycerolipid metabolism; hsa00830:Retinol metabolism; hsa01100:Metabolic pathways; hsa04975:Fat digestion and absorption	R-HSA-1482883:Acyl chain remodeling of DAG and TAG; R-HSA-75109:Triglyceride Biosynthesis	.	O75907
TTF8P9I	Diacylglycerol acyltransferase 1 (DGAT1)	O75907	DGAT1_HUMAN	Acyltransferase	Retinol O-fatty-acyltransferase; Diglyceride acyltransferase; Diacylglycerol O-acyltransferase 1; DGAT; Acyl-CoA retinol O-fatty-acyltransferase; ARAT; AGRP1; ACAT-related gene product 1	DGAT1	"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."	EC 2.3.1.20	.	MGDRGSSRRRRTGSRPSSHGGGGPAAAEEEVRDAAAGPDVGAAGDAPAPAPNKDGDAGVGSGHWELRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQVVSLFLKDPYSWPAPCLVIAANVFAVAAFQVEKRLAVGALTEQAGLLLHVANLATILCFPAAVVLLVESITPVGSLLALMAHTILFLKLFSYRDVNSWCRRARAKAASAGKKASSAAAPHTVSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWMVPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREFYRDWWNSESVTYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWMARTGVFLASAFFHEYLVSVPLRMFRLWAFTGMMAQIPLAWFVGRFFQGNYGNAAVWLSLIIGQPIAVLMYVHDYYVLNYEAPAAEA	Successful	In vitro inhibition of diacylglycerol acyltransferase by prenylflavonoids from Sophora flavescens. Planta Med. 2004 Mar;70(3):258-60.	34	EC:2.3	Acyltransferase	membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.	2.3.1.20 	Acyltransferases	"MBOAT, membrane-bound O-acyltransferase family"	PF03062	PF03062; MBOAT	.	.	hsa00561:Glycerolipid metabolism; hsa00830:Retinol metabolism; hsa01100:Metabolic pathways; hsa04975:Fat digestion and absorption	R-HSA-1482883:Acyl chain remodeling of DAG and TAG; R-HSA-75109:Triglyceride Biosynthesis	.	O75907
TTRHEQ4	Diacylglycerol O-acyltransferase 2 (DGAT2)	Q96PD7	DGAT2_HUMAN	Acyltransferase	UNQ738/PRO1433; HMFN1045; Diglyceride acyltransferase 2	DGAT2	"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."	EC 2.3.1.20	.	MKTLIAAYSGVLRGERQAEADRSQRSHGGPALSREGSGRWGTGSSILSALQDLFSVTWLNRSKVEKQLQVISVLQWVLSFLVLGVACSAILMYIFCTDCWLIAVLYFTWLVFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVSRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPIYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPKLEHPTQQDIDLYHTMYMEALVKLFDKHKTKFGLPETEVLEVN	Successful	"Hakozaki T, Minwalla L, Zhuang J, Chhoa M, Matsubara A, Miyamoto K, Greatens A, Hillebrand GG, Bissett DL, Boissy RE: The effect of niacinamide on reducing cutaneous pigmentation and suppression of melanosome transfer. Br J Dermatol. 2002 Jul;147(1):20-31."	34	EC:2.3	Acyltransferase	diacylglycerol acyltransferase family.	2.3.1.20 	Acyltransferases	Diacylglycerol acyltransferase 	PF03982	PF03982; DAGAT	.	.	hsa00561:Glycerolipid metabolism; hsa01100:Metabolic pathways; hsa04975:Fat digestion and absorption	R-HSA-1482883:Acyl chain remodeling of DAG and TAG; R-HSA-75109:Triglyceride Biosynthesis	.	Q96PD7
TT8N5V1	DGAT2 messenger RNA (DGAT2 mRNA)	Q96PD7	DGAT2_HUMAN	.	Acyl-CoA retinol O-fatty-acyltransferase; ARAT; Retinol O-fatty-acyltransferase; Diglyceride acyltransferase 2	DGAT2	"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)."	EC 2.3.1.20	.	MKTLIAAYSGVLRGERQAEADRSQRSHGGPALSREGSGRWGTGSSILSALQDLFSVTWLNRSKVEKQLQVISVLQWVLSFLVLGVACSAILMYIFCTDCWLIAVLYFTWLVFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVSRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPIYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPKLEHPTQQDIDLYHTMYMEALVKLFDKHKTKFGLPETEVLEVN	Clinical trial	"Clinical pipeline report, company report or official report of Ionis Pharmaceuticals."	.	.	.	.	.	.	.	.	.	.	.	hsa00561: Glycerolipid metabolism; hsa01100: Metabolic pathways; hsa04975: Fat digestion and absorption	R-HSA-1482883: Acyl chain remodeling of DAG and TAG; R-HSA-75109: Triglyceride biosynthesis	.	Q96PD7
TTGL8F0	Diacylglycerol kinase alpha	.	DGKA_HUMAN	Single Protein	DAG kinase alpha; DGK-alpha; Diglyceride kinase alpha; 80 kDa diacylglycerol kinase	DGKA	"Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Also plays an important role in the biosynthesis of complex lipids. Can also phosphorylate 1-alkyl-2-acylglycerol in vitro as efficiently as diacylglycerol provided it contains an arachidonoyl group."	.	.	MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIYLEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFKLYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEWVRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKYTVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNLSTSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRLFKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQNLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVLNIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLEGAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTIKITHKNQMPMLMGPPPRSTNFFGFLS	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P23743
TTSBBXL	Diacylglycerol kinase zeta (DGKZ)	Q13574	DGKZ_HUMAN	Kinase	DAG kinase zeta; Diglyceride kinase zeta; DGK-zeta	DGKZ	"Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:9159104, PubMed:15544348, PubMed:18004883, PubMed:19744926, PubMed:22108654, PubMed:22627129, PubMed:23949095). Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (PubMed:9159104, PubMed:15544348, PubMed:18004883, PubMed:19744926, PubMed:22108654, PubMed:22627129, PubMed:23949095). Also plays an important role in the biosynthesis of complex lipids (Probable). Does not exhibit an acyl chain-dependent substrate specificity among diacylglycerol species (PubMed:9159104, PubMed:19744926, PubMed:22108654). Can also phosphorylate 1-alkyl-2-acylglycerol in vitro but less efficiently and with a preference for alkylacylglycerols containing an arachidonoyl group (PubMed:15544348, PubMed:19744926, PubMed:22627129). The biological processes it is involved in include T cell activation since it negatively regulates T-cell receptor signaling which is in part mediated by diacylglycerol (By similarity). By generating phosphatidic acid, stimulates PIP5KIA activity which regulates actin polymerization (PubMed:15157668). Through the same mechanism could also positively regulate insulin-induced translocation of SLC2A4 to the cell membrane (By similarity). {ECO:0000250|UniProtKB:Q80UP3, ECO:0000269|PubMed:15157668, ECO:0000269|PubMed:15544348, ECO:0000269|PubMed:18004883, ECO:0000269|PubMed:19744926, ECO:0000269|PubMed:22108654, ECO:0000269|PubMed:22627129, ECO:0000269|PubMed:23949095, ECO:0000269|PubMed:9159104, ECO:0000305|PubMed:8626588}.; [Isoform 1]: Regulates RASGRP1 activity. {ECO:0000269|PubMed:11257115}.; [Isoform 2]: Does not regulate RASGRP1 activity. {ECO:0000269|PubMed:11257115}."	EC 2.7.1.107	5ELQ	MEPRDGSPEARSSDSESASASSSGSERDAGPEPDKAPRRLNKRRFPGLRLFGHRKAITKSGLQHLAPPPPTPGAPCSESERQIRSTVDWSESATYGEHIWFETNVSGDFCYVGEQYCVARMLKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESGSRNVREPTFVRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRKSSKKGPEEGRWRPFIIRPTPSPLMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHNLRILACGGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDRWDLHAEPNPEAGPEDRDEGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCVVFLNIPRYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVVLTTSKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSAAPLHSDQQPVPEQLRIQVSRVSMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPTCQKLSPKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLPTSPCSPTPRSLQGDAAPPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV	Clinical trial	Manipulation of diacylglycerol and ERK-mediated signaling differentially controls CD8(+) T cell responses during chronic viral infection. Front Immunol. 2022 Nov 24;13:1032113.	.	.	.	.	.	.	.	.	.	.	.	hsa:8525	R-HSA-114508;	.	Q13574;
TTTK0NH	Delta(24)-sterol reductase (DHCR24)	Q15392	DHC24_HUMAN	CH-CH donor oxidoreductase	Seladin-1; Diminuto/dwarf1 homolog; DHCR24	DHCR24	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.	EC 1.3.1.72	.	MEPAVSLAVCALLFLLWVRLKGLEFVLIHQRWVFVCLFLLPLSLIFDIYYYVRAWVVFKLSSAPRLHEQRVRDIQKQVREWKEQGSKTFMCTGRPGWLTVSLRVGKYKKTHKNIMINLMDILEVDTKKQIVRVEPLVTMGQVTALLTSIGWTLPVLPELDDLTVGGLIMGTGIESSSHKYGLFQHICTAYELVLADGSFVRCTPSENSDLFYAVPWSCGTLGFLVAAEIRIIPAKKYVKLRFEPVRGLEAICAKFTHESQRQENHFVEGLLYSLDEAVIMTGVMTDEAEPSKLNSIGNYYKPWFFKHVENYLKTNREGLEYIPLRHYYHRHTRSIFWELQDIIPFGNNPIFRYLFGWMVPPKISLLKLTQGETLRKLYEQHHVVQDMLVPMKCLQQALHTFQNDIHVYPIWLCPFILPSQPGLVHPKGNEAELYIDIGAYGEPRVKHFEARSCMRQLEKFVRSVHGFQMLYADCYMNREEFWEMFDGSLYHKLREKLGCQDAFPEVYDKICKAARH	Literature-reported	Antilipemic drug-induced skin manifestations. Hautarzt. 1995 Feb;46(2):76-80.	2.1	.	.	.	.	.	.	.	.	.	.	hsa00100:Steroid biosynthesis; hsa01100:Metabolic pathways	R-HSA-191273:Cholesterol biosynthesis	.	Q15392
TTYZVDJ	Dihydrofolate reductase (DHFR)	P00374	DYR_HUMAN	CH-NH donor oxidoreductase	DYR; DHFRP1	DHFR	"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."	EC 1.5.1.3	6DE4; 6DAV; 6A7E; 6A7C; 5HVE	MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKND	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	EC:1.5	Oxidoreductases acting on CH-NH group of donors	dihydrofolate reductase family.	1.5.1.3	Acting on the CH-NH group of donors	Dihydrofolate reductase	PF00186	PF00186; DHFR_1	.	.	hsa00670:One carbon pool by folate; hsa00790:Folate biosynthesis; hsa01100:Metabolic pathways	"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"	MetaCyc:HS09699-MON	P00374
TTLVP78	Dihydroorotate dehydrogenase (DHODH)	Q02127	PYRD_HUMAN	CH-CH donor oxidoreductase	"Dihydroorotate oxidase; Dihydroorotate dehydrogenase (quinone), mitochondrial; DHOdehase; DHODH"	DHODH	Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.	EC 1.3.5.2	6FMD; 6ET4; 6CJG; 6CJF; 5ZFB	MAWRHLKKRAQDAVIILGGGGLLFASYLMATGDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVNLGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTDAIGADHRR	Successful	Nat Rev Drug Discov. 2013 Feb;12(2):87-90.	34	.	.	.	.	.	.	.	.	.	.	hsa00240:Pyrimidine metabolism; hsa01100:Metabolic pathways	R-HSA-500753:Pyrimidine biosynthesis	.	Q02127
TT3UY29	HUMAN dihydroorotate dehydrogenase (DHODH)	Q02127	PYRD_HUMAN	CH-CH donor oxidoreductase	"Dihydroorotate oxidase; Dihydroorotate dehydrogenase (quinone), mitochondrial; DHOdehase; DHODH"	DHODH	Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.	EC 1.3.5.2	6FMD; 6ET4; 6CJG; 6CJF; 5ZFB	MAWRHLKKRAQDAVIILGGGGLLFASYLMATGDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVNLGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTDAIGADHRR	.	Broad-spectrum inhibition of common respiratory RNA viruses by a pyrimidine synthesis inhibitor with involvement of the host antiviral response. J Gen Virol. 2017 May;98(5):946-954.	34	.	.	.	.	.	.	.	.	.	.	hsa00240: Pyrimidine metabolism; hsa01100: Metabolic pathways; hsa01240: Biosynthesis of cofactors	R-HSA-500753: Pyrimidine biosynthesis	.	Q02127
TTBO2A9	Deoxyhypusine synthase (DHPS)	P49366	DHYS_HUMAN	Alkyl aryl transferase	DHS	DHPS	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.	EC 2.5.1.46	1RQD; 1ROZ; 1RLZ; 1DHS	MEGSLEREAPAGALAAVLKHSSTLPPESTQVRGYDFNRGVNYRALLEAFGTTGFQATNFGRAVQQVNAMIEKKLEPLSQDEDQHADLTQSRRPLTSCTIFLGYTSNLISSGIRETIRYLVQHNMVDVLVTTAGGVEEDLIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNENYCKFEDWLMPILDQMVMEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVFSPALTDGSLGDMIFFHSYKNPGLVLDIVEDLRLINTQAIFAKCTGMIILGGGVVKHHIANANLMRNGADYAVYINTAQEFDGSDSGARPDEAVSWGKIRVDAQPVKVYADASLVFPLLVAETFAQKMDAFMHEKNED	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-204626: Hypusine synthesis from eIF5A-lysine	MetaCyc:HS01810-MON	P49366
TTN74LE	Direct IAP-binding protein with low pI (DIABLO)	Q9NR28	DBLOH_HUMAN	.	"Smac protein; Smac; Second mitochondria-derived activator of caspase; Direct IAP binding protein with low pI; Diablo homolog, mitochondrial"	DIABLO	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.	.	4TX5; 3UIJ; 3UIH; 3D9U; 1XB1	MAALKSWLSRSVTSFFRYRQCLCVPVVANFKKRCFSELIRPWHKTVTIGFGVTLCAVPIAQKSEPHSLSSEALMRRAVSLVTDSTSTFLSQTTYALIEAITEYTKAVYTLTSLYRQYTSLLGKMNSEEEDEVWQVIIGARAEMTSKHQEYLKLETTWMTAVGLSEMAAEAAYQTGADQASITARNHIQLVKLQVEEVHQLSRKAETKLAEAQIEELRQKTQEEGEERAESEQEAYLRED	Literature-reported	Smac induces cytochrome c release and apoptosis independently from Bax/Bcl-x(L) in a strictly caspase-3-dependent manner in human carcinoma cells. Oncogene. 2004 Jun 3;23(26):4523-35.	.	.	.	.	.	.	Second Mitochondria-derived Activator of Caspases	PF09057	PF09057; Smac_DIABLO	.	.	hsa04210: Apoptosis; hsa04215: Apoptosis - multiple species	"R-HSA-111457: Release of apoptotic factors from the mitochondria; R-HSA-111463: SMAC (DIABLO) binds to IAPs; R-HSA-111464: SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes; R-HSA-111469: SMAC, XIAP-regulated apoptotic response; R-HSA-9627069: Regulation of the apoptosome activity"	.	Q9NR28
TTTEOPU	Helicase-moi messenger RNA (DICER1 mRNA)	Q9UPY3	DICER_HUMAN	mRNA target	KIAA0928 (mRNA); Helicase with RNase motif (mRNA); Helicase MOI (mRNA); HERNA (mRNA); Endoribonuclease Dicer (mRNA); DICER (mRNA)	DICER1	"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."	EC 3.1.26.3	5ZAM; 5ZAL; 5ZAK; 4WYQ; 4NHA	MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELSYQIRGDFSRNGKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKERWNQEFTKHQVLIMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLCENCPSCPRILGLTASILNGKCDPEELEEKIQKLEKILKSNAETATDLVVLDRYTSQPCEIVVDCGPFTDRSGLYERLLMELEEALNFINDCNISVHSKERDSTLISKQILSDCRAVLVVLGPWCADKVAGMMVRELQKYIKHEQEELHRKFLLFTDTFLRKIHALCEEHFSPASLDLKFVTPKVIKLLEILRKYKPYERQQFESVEWYNNRNQDNYVSWSDSEDDDEDEEIEEKEKPETNFPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFITGHGIGKNQPRNKQMEAEFRKQEEVLRKFRAHETNLLIATSIVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRARAPISNYIMLADTDKIKSFEEDLKTYKAIEKILRNKCSKSVDTGETDIDPVMDDDDVFPPYVLRPDDGGPRVTINTAIGHINRYCARLPSDPFTHLAPKCRTRELPDGTFYSTLYLPINSPLRASIVGPPMSCVRLAERVVALICCEKLHKIGELDDHLMPVGKETVKYEEELDLHDEEETSVPGRPGSTKRRQCYPKAIPECLRDSYPRPDQPCYLYVIGMVLTTPLPDELNFRRRKLYPPEDTTRCFGILTAKPIPQIPHFPVYTRSGEVTISIELKKSGFMLSLQMLELITRLHQYIFSHILRLEKPALEFKPTDADSAYCVLPLNVVNDSSTLDIDFKFMEDIEKSEARIGIPSTKYTKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKFPSPEYETFAEYYKTKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQILVPELCAIHPIPASLWRKAVCLPSILYRLHCLLTAEELRAQTASDAGVGVRSLPADFRYPNLDFGWKKSIDSKSFISISNSSSAENDNYCKHSTIVPENAAHQGANRTSSLENHDQMSVNCRTLLSESPGKLHVEVSADLTAINGLSYNQNLANGSYDLANRDFCQGNQLNYYKQEIPVQPTTSYSIQNLYSYENQPQPSDECTLLSNKYLDGNANKSTSDGSPVMAVMPGTTDTIQVLKGRMDSEQSPSIGYSSRTLGPNPGLILQALTLSNASDGFNLERLEMLGDSFLKHAITTYLFCTYPDAHEGRLSYMRSKKVSNCNLYRLGKKKGLPSRMVVSIFDPPVNWLPPGYVVNQDKSNTDKWEKDEMTKDCMLANGKLDEDYEEEDEEEESLMWRAPKEEADYEDDFLEYDQEHIRFIDNMLMGSGAFVKKISLSPFSTTDSAYEWKMPKKSSLGSMPFSSDFEDFDYSSWDAMCYLDPSKAVEEDDFVVGFWNPSEENCGVDTGKQSISYDLHTEQCIADKSIADCVEALLGCYLTSCGERAAQLFLCSLGLKVLPVIKRTDREKALCPTRENFNSQQKNLSVSCAAASVASSRSSVLKDSEYGCLKIPPRCMFDHPDADKTLNHLISGFENFEKKINYRFKNKAYLLQAFTHASYHYNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYDYHKYFKAVSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLETVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPQVPNS	Literature-reported	"US patent application no. 7,427,470, Antisense modulation of helicase-moi expression."	0	mRNA	mRNA target	.	.	.	"Dicer dimerisation domain; Helicase conserved C-terminal domain; PAZ domain; Type III restriction enzyme, res subunit; Ribonuclease III domain"	PF03368; PF00271; PF02170; PF04851; PF00636	PF03368; Dicer_dimer; PF00271; Helicase_C; PF02170; PAZ; PF04851; ResIII; PF00636; Ribonuclease_3	.	.	hsa05206:MicroRNAs in cancer	"R-HSA-203927: MicroRNA (miRNA) biogenesis; R-HSA-426486: Small interfering RNA (siRNA) biogenesis; R-HSA-9708296: tRNA-derived small RNA (tsRNA or tRNA-related fragment, tRF) biogenesis"	.	Q9UPY3
TTU3X26	Iodothyronine deiodinase type I (DIO1)	P49895	IOD1_HUMAN	.	Type-I 5'-deiodinase; Type I iodothyronine deiodinase; Type 1 DI; TXDI1; ITDI1; DIOI; 5DI	DIO1	"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)."	EC 1.21.99.4	.	MGLPQPGLWLKRLWVLLEVAVHVVVGKVLLILFPDRVKRNILAMGEKTGMTRNPHFSHDNWIPTFFSTQYFWFVLKVRWQRLEDTTELGGLAPNCPVVRLSGQRCNIWEFMQGNRPLVLNFGSCTUPSFMFKFDQFKRLIEDFSSIADFLVIYIEEAHASDGWAFKNNMDIRNHQNLQDRLQAAHLLLARSPQCPVVVDTMQNQSSQLYAALPERLYIIQEGRILYKGKSGPWNYNPEEVRAVLEKLHS	Successful	Type 1 iodothyronine deiodinase is the major source of circulating T3 in hyperthyroidism: implications for therapy. Nat Clin Pract Endocrinol Metab. 2007 Nov;3(11):740-1.	34	.	.	iodothyronine deiodinase family.	1.21.99.4	Catalysing the reaction X-H + Y-H = X-Y	Iodothyronine deiodinase	PF00837	PF00837; T4_deiodinase	.	.	hsa04919:Thyroid hormone signaling pathway	R-HSA-350864: Regulation of thyroid hormone activity	.	.
TTE3RAC	Dickkopf-related protein 1 (DKK1)	O94907	DKK1_HUMAN	Dickkopf protein	hDkk1; hDkk-1; UNQ492/PRO1008; Dkk1; Dkk-1; Dickkopfrelated protein 1; Dickkopf1; Dickkopf-1	DKK1	"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."	.	5GJE; 5FWW; 3SOQ; 3S8V; 3S2K	MMALGAAGATRVFVAMVAAALGGHPLLGVSATLNSVLNSNAIKNLPPPLGGAAGHPGSAVSAAPGILYPGGNKYQTIDNYQPYPCAEDEECGTDEYCASPTRGGDAGVQICLACRKRRKRCMRHAMCCPGNYCKNGICVSSDQNHFRGEIEETITESFGNDHSTLDGYSRRTTLSSKMYHTKGQEGSVCLRSSDCASGLCCARHFWSKICKPVLKEGQVCTKHRRKGSHGLEIFQRCYCGEGLSCRIQKDHHQASNSSRLHTCQRH	Clinical trial	Biological therapy for osteoporosis. Clin Calcium. 2014 Jun;24(6):919-25.	21	Dickkopf	Dickkopf family	dickkopf family.	.	.	Dickkopf N-terminal cysteine-rich region	PF04706	PF04706; Dickkopf_N	.	.	hsa04310:Wnt signaling pathway	R-HSA-201681:TCF dependent signaling in response to WNT; R-HSA-3772470:Negative regulation of TCF-dependent signaling by WNT ligand antagonists	.	O94907
TTST5KX	Dickkopf-related protein 2 (DKK2)	Q9UBU2	DKK2_HUMAN	Dickkopf protein	hDkk2; hDkk-2; UNQ682/PRO1316; Dkk2; Dkk-2; Dickkopfrelated protein 2; Dickkopf2; Dickkopf-2	DKK2	"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."	.	.	MAALMRSKDSSCCLLLLAAVLMVESSQIGSSRAKLNSIKSSLGGETPGQAANRSAGMYQGLAFGGSKKGKNLGQAYPCSSDKECEVGRYCHSPHQGSSACMVCRRKKKRCHRDGMCCPSTRCNNGICIPVTESILTPHIPALDGTRHRDRNHGHYSNHDLGWQNLGRPHTKMSHIKGHEGDPCLRSSDCIEGFCCARHFWTKICKPVLHQGEVCTKQRKKGSHGLEIFQRCDCAKGLSCKVWKDATYSSKARLHVCQKI	Literature-reported	Prognostic value of DKK2 from the Dickkopf family in human breast cancer. Int J Oncol. 2018 Dec;53(6):2555-2565.	.	Dickkopf	Dickkopf family	dickkopf family.	.	.	Dickkopf N-terminal cysteine-rich region	PF04706	PF04706; Dickkopf_N	.	.	hsa04310: Wnt signaling pathway; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases	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-5339717: Signaling by LRP5 mutants	.	Q9UBU2
TTY2ZV6	Dickkopf-related protein 3 (DKK3)	Q9UBP4	DKK3_HUMAN	Dickkopf protein	hDkk-3; UNQ258/PRO295; REIC; Dkk-3; Dickkopf-3	DKK3	"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."	.	.	MQRLGATLLCLLLAAAVPTAPAPAPTATSAPVKPGPALSYPQEEATLNEMFREVEELMEDTQHKLRSAVEEMEAEEAAAKASSEVNLANLPPSYHNETNTDTKVGNNTIHVHREIHKITNNQTGQMVFSETVITSVGDEEGRRSHECIIDEDCGPSMYCQFASFQYTCQPCRGQRMLCTRDSECCGDQLCVWGHCTKMATRGSNGTICDNQRDCQPGLCCAFQRGLLFPVCTPLPVEGELCHDPASRLLDLITWELEPDGALDRCPCASGLLCQPHSHSLVYVCKPTFVGSRDQDGEILLPREVPDEYEVGSFMEEVRQELEDLERSLTEEMALREPAAAAAALLGGEEI	Clinical trial	Potential of adenovirus-mediated REIC/Dkk-3 gene therapy for use in the treatment of pancreatic cancer. J Gastroenterol Hepatol. 2014 May;29(5):973-83.	19	Dickkopf	.	dickkopf family.	.	.	Dickkopf N-terminal cysteine-rich region	PF04706	PF04706; Dickkopf_N	.	.	.	.	.	Q9UBP4
TT9PB26	Presynaptic density protein 95 (DLG4)	P78352	DLG4_HUMAN	Ezrin/radixin/moesin-binding phosphoprotein 50	"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"	DLG4	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.	.	6QJN; 6QJL; 6QJK; 6QJJ; 6QJI	MDCLCIVTTKKYRYQDEDTPPLEHSPAHLPNQANSPPVIVNTDTLEAPGYELQVNGTEGEMEYEEITLERGNSGLGFSIAGGTDNPHIGDDPSIFITKIIPGGAAAQDGRLRVNDSILFVNEVDVREVTHSAAVEALKEAGSIVRLYVMRRKPPAEKVMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGRLQIGDKILAVNSVGLEDVMHEDAVAALKNTYDVVYLKVAKPSNAYLSDSYAPPDITTSYSQHLDNEISHSSYLGTDYPTAMTPTSPRRYSPVAKDLLGEEDIPREPRRIVIHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDQILSVNGVDLRNASHEQAAIALKNAGQTVTIIAQYKPEEYSRFEAKIHDLREQLMNSSLGSGTASLRSNPKRGFYIRALFDYDKTKDCGFLSQALSFRFGDVLHVIDASDEEWWQARRVHSDSETDDIGFIPSKRRVERREWSRLKAKDWGSSSGSQGREDSVLSYETVTQMEVHYARPIIILGPTKDRANDDLLSEFPDKFGSCVPHTTRPKREYEIDGRDYHFVSSREKMEKDIQAHKFIEAGQYNSHLYGTSVQSVREVAEQGKHCILDVSANAVRRLQAAHLHPIAIFIRPRSLENVLEINKRITEEQARKAFDRATKLEQEFTECFSAIVEGDSFEEIYHKVKRVIEDLSGPYIWVPARERL	Clinical trial	Treatment of stroke with a PSD-95 inhibitor in the gyrencephalic primate brain. Nature. 2012 Feb 29;483(7388):213-7.	25	TC=8.A.24	.	MAGUK family.	.	.	Guanylate kinase; Polyubiquitination (PEST) N-terminal domain of MAGUK; PDZ domain; PDZ-associated domain of NMDA receptors; SH3 domain	PF00625; PF10608; PF00595; PF10600; PF00018	PF00625; Guanylate_kin; PF10608; MAGUK_N_PEST; PF00595; PDZ; PF10600; PDZ_assoc; PF00018; SH3_1	8.A.24.1.3	The Ezrin/Radixin/Moesin-binding Phosphoprotein 50 (EBP50) Family	hsa04390:Hippo signaling pathway; hsa04724:Glutamatergic synapse; hsa05016:Huntington's disease; hsa05030:Cocaine addiction	"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"	.	P78352
TTMADVT	PSD95-nNOS interaction (PSD95-nNOS PPI)	P78352-P29475	DLG4_HUMAN-NOS1_HUMAN	.	Disks large homolog 4-Constitutive NOS interaction	DLG4-NOS1	Functions as a novel molecular target to modulate conditioned fear: relevance to PTSD.	.	.	MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQAGDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTIRVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAPRPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQVDRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPSKCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLFPLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHVWKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCEIFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQEERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANNSLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGVISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEYEEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSREPDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSSMDCLCIVTTKKYRYQDEDTPPLEHSPAHLPNQANSPPVIVNTDTLEAPGYELQVNGTEGEMEYEEITLERGNSGLGFSIAGGTDNPHIGDDPSIFITKIIPGGAAAQDGRLRVNDSILFVNEVDVREVTHSAAVEALKEAGSIVRLYVMRRKPPAEKVMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGRLQIGDKILAVNSVGLEDVMHEDAVAALKNTYDVVYLKVAKPSNAYLSDSYAPPDITTSYSQHLDNEISHSSYLGTDYPTAMTPTSPRRYSPVAKDLLGEEDIPREPRRIVIHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDQILSVNGVDLRNASHEQAAIALKNAGQTVTIIAQYKPEEYSRFEAKIHDLREQLMNSSLGSGTASLRSNPKRGFYIRALFDYDKTKDCGFLSQALSFRFGDVLHVIDASDEEWWQARRVHSDSETDDIGFIPSKRRVERREWSRLKAKDWGSSSGSQGREDSVLSYETVTQMEVHYARPIIILGPTKDRANDDLLSEFPDKFGSCVPHTTRPKREYEIDGRDYHFVSSREKMEKDIQAHKFIEAGQYNSHLYGTSVQSVREVAEQGKHCILDVSANAVRRLQAAHLHPIAIFIRPRSLENVLEINKRITEEQARKAFDRATKLEQEFTECFSAIVEGDSFEEIYHKVKRVIEDLSGPYIWVPARERL	Literature-reported	PSD95 and nNOS interaction as a novel molecular target to modulate conditioned fear: relevance to PTSD.Transl Psychiatry. 2018 Aug 14;8(1):155.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P78352
TTF4AVB	Protein delta homolog 1 (DLK1)	P80370	DLK1_HUMAN	.	pG2; DLK-1	DLK1	May have a role in neuroendocrine differentiation.	.	.	MTATEALLRVLLLLLAFGHSTYGAECFPACNPQNGFCEDDNVCRCQPGWQGPLCDQCVTSPGCLHGLCGEPGQCICTDGWDGELCDRDVRACSSAPCANNRTCVSLDDGLYECSCAPGYSGKDCQKKDGPCVINGSPCQHGGTCVDDEGRASHASCLCPPGFSGNFCEIVANSCTPNPCENDGVCTDIGGDFRCRCPAGFIDKTCSRPVTNCASSPCQNGGTCLQHTQVSYECLCKPEFTGLTCVKKRALSPQQVTRLPSGYGLAYRLTPGVHELPVQQPEHRILKVSMKELNKKTPLLTEGQAICFTILGVLTSLVVLGTVGIVFLNKCETWVSNLRYNHMLRKKKNLLLQYNSGEDLAVNIIFPEKIDMTTFSKEAGDEEI	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	EGF-like domain	PF00008	PF00008; EGF	.	.	.	R-HSA-2122948: Activated NOTCH1 Transmits Signal to the Nucleus	.	P80370
TT9CFQD	Delta-like protein 1 (DLL1)	O00548	DLL1_HUMAN	.	H-Delta-1; Drosophila Delta homolog 1; Delta1	DLL1	"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)."	.	4XBM	MGSRCALALAVLSALLCQVWSSGVFELKLQEFVNKKGLLGNRNCCRGGAGPPPCACRTFFRVCLKHYQASVSPEPPCTYGSAVTPVLGVDSFSLPDGGGADSAFSNPIRFPFGFTWPGTFSLIIEALHTDSPDDLATENPERLISRLATQRHLTVGEEWSQDLHSSGRTDLKYSYRFVCDEHYYGEGCSVFCRPRDDAFGHFTCGERGEKVCNPGWKGPYCTEPICLPGCDEQHGFCDKPGECKCRVGWQGRYCDECIRYPGCLHGTCQQPWQCNCQEGWGGLFCNQDLNYCTHHKPCKNGATCTNTGQGSYTCSCRPGYTGATCELGIDECDPSPCKNGGSCTDLENSYSCTCPPGFYGKICELSAMTCADGPCFNGGRCSDSPDGGYSCRCPVGYSGFNCEKKIDYCSSSPCSNGAKCVDLGDAYLCRCQAGFSGRHCDDNVDDCASSPCANGGTCRDGVNDFSCTCPPGYTGRNCSAPVSRCEHAPCHNGATCHERGHRYVCECARGYGGPNCQFLLPELPPGPAVVDLTEKLEGQGGPFPWVAVCAGVILVLMLLLGCAAVVVCVRLRLQKHRPPADPCRGETETMNNLANCQREKDISVSIIGATQIKNTNKKADFHGDHSADKNGFKARYPAVDYNLVQDLKGDDTAVRDAHSKRDTKCQPQGSSGEEKGTPTTLRGGEASERKRPDSGCSTSKDTKYQSVYVISEEKDECVIATEV	Literature-reported	Notch ligand Delta-like 1 as a novel molecular target in childhood neuroblastoma. BMC Cancer. 2017 May 19;17(1):352.	.	.	.	.	.	.	.	.	.	.	.	hsa01522: Endocrine resistance; hsa04330: Notch signaling pathway; hsa04658: Th1 and Th2 cell differentiation; hsa05200: Pathways in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05224: Breast cancer	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-9013507: NOTCH3 Activation and Transmission of Signal to the Nucleus; R-HSA-9022702: MECP2 regulates transcription of neuronal ligands	.	O00548
TT1C9K6	Delta-like protein 3 (DLL3)	Q9NYJ7	DLL3_HUMAN	.	pudgy; pu; delta like canonical Notch ligand 3; SCDO1; Drosophila Delta homolog 3; Delta3	DLL3	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.	.	.	MVSPRMSGLLSQTVILALIFLPQTRPAGVFELQIHSFGPGPGPGAPRSPCSARLPCRLFFRVCLKPGLSEEAAESPCALGAALSARGPVYTEQPGAPAPDLPLPDGLLQVPFRDAWPGTFSFIIETWREELGDQIGGPAWSLLARVAGRRRLAAGGPWARDIQRAGAWELRFSYRARCEPPAVGTACTRLCRPRSAPSRCGPGLRPCAPLEDECEAPLVCRAGCSPEHGFCEQPGECRCLEGWTGPLCTVPVSTSSCLSPRGPSSATTGCLVPGPGPCDGNPCANGGSCSETPRSFECTCPRGFYGLRCEVSGVTCADGPCFNGGLCVGGADPDSAYICHCPPGFQGSNCEKRVDRCSLQPCRNGGLCLDLGHALRCRCRAGFAGPRCEHDLDDCAGRACANGGTCVEGGGAHRCSCALGFGGRDCRERADPCAARPCAHGGRCYAHFSGLVCACAPGYMGARCEFPVHPDGASALPAAPPGLRPGDPQRYLLPPALGLLVAAGVAGAALLLVHVRRRGHSQDAGSRLLAGTPEPSVHALPDALNNLRTQEGSGDGPSSSVDWNRPEDVDPQGIYVISAPSIYAREVATPLFPPLHTGRAGQRQHLLFPYPSSILSVK	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	.	.	.	.	.	EGF-like domain; Human growth factor-like EGF	PF00008; PF12661	PF00008; EGF; PF12661; hEGF	.	.	hsa01522:Endocrine resistance; hsa04330:Notch signaling pathway; hsa04658:Th1 and Th2 cell differentiation; hsa05200:Pathways in cancer; hsa05224:Breast cancer	.	.	Q9NYJ7
TTV23LH	Delta-like protein 4 (DLL4)	Q9NR61	DLL4_HUMAN	.	UNQ1895/PRO4341; Drosophila Delta homolog 4; Deltalike protein 4; Delta4	DLL4	"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."	.	5MVX	MAAASRSASGWALLLLVALWQQRAAGSGVFQLQLQEFINERGVLASGRPCEPGCRTFFRVCLKHFQAVVSPGPCTFGTVSTPVLGTNSFAVRDDSSGGGRNPLQLPFNFTWPGTFSLIIEAWHAPGDDLRPEALPPDALISKIAIQGSLAVGQNWLLDEQTSTLTRLRYSYRVICSDNYYGDNCSRLCKKRNDHFGHYVCQPDGNLSCLPGWTGEYCQQPICLSGCHEQNGYCSKPAECLCRPGWQGRLCNECIPHNGCRHGTCSTPWQCTCDEGWGGLFCDQDLNYCTHHSPCKNGATCSNSGQRSYTCTCRPGYTGVDCELELSECDSNPCRNGGSCKDQEDGYHCLCPPGYYGLHCEHSTLSCADSPCFNGGSCRERNQGANYACECPPNFTGSNCEKKVDRCTSNPCANGGQCLNRGPSRMCRCRPGFTGTYCELHVSDCARNPCAHGGTCHDLENGLMCTCPAGFSGRRCEVRTSIDACASSPCFNRATCYTDLSTDTFVCNCPYGFVGSRCEFPVGLPPSFPWVAVSLGVGLAVLLVLLGMVAVAVRQLRLRRPDDGSREAMNNLSDFQKDNLIPAAQLKNTNQKKELEVDCGLDKSNCGKQQNHTLDYNLAPGPLGRGTMPGKFPHSDKSLGEKAPLRLHSEKPECRISAICSPRDSMYQSVCLISEERNECVIATEV	Clinical trial	"J Clin Oncol 31, 2013 (suppl; abstr 2502)."	17	.	Delta serrate	.	.	.	Delta serrate ligand; EGF-like domain; N terminus of Notch ligand	PF01414; PF00008; PF07657	PF01414; DSL; PF00008; EGF; PF07657; MNNL	.	.	hsa04330:Notch signaling pathway	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	.	Q9NR61
TTWLFXU	Dystrophin messenger RNA (DMD mRNA)	P11532	DMD_HUMAN	mRNA target	Dystrophin mRNA	DMD	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.	.	3UUN; 1EG4; 1EG3; 1DXX	MLWWEEVEDCYEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNVMKNIMAGLQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDPEDVDTTYPDKKSILMYITSLFQVLPQQVSIEAIQEVEMLPRPPKVTKEEHFQLHHQMHYSQQITVSLAQGYERTSSPKPRFKSYAYTQAAYVTTSDPTRSPFPSQHLEAPEDKSFGSSLMESEVNLDRYQTALEEVLSWLLSAEDTLQAQGEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIGTGKLSEDEETEVQEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQNQKLKELNDWLTKTEERTRKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDILLKWQRLTEEQCLFSAWLSEKEDAVNKIHTTGFKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSVTQKTEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLTQTTVMETVTTVTTREQILVKHAQEELPPPPPQKKRQITVDSEIRKRLDVDITELHSWITRSEAVLQSPEFAIFRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEGVNADSIKQASEQLNSRWIEFCQLLSERLNWLEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSEPTAIKSQLKICKDEVNRLSDLQPQIERLKIQSIALKEKGQGPMFLDADFVAFTNHFKQVFSDVQAREKELQTIFDTLPPMRYQETMSAIRTWVQQSETKLSIPQLSVTDYEIMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEWPALGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEFASRLETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANKWLNEVEFKLKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGGVMDELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVEPQISELNHRFAAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQIHTVREETMMVMTEDMPLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRSVEKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKTDASILQEKLGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQPVVTKETAISKLEMPSSLMLEVPALADFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDATRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKLYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLQELQEATDELDLKLRQAEVIKGSWQPVGDLLIDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLSTLEDLNTRWKLLQVAVEDRVRQLHEAHRDFGPASQHFLSTSVQGPWERAISPNKVPYYINHETQTTCWDHPKMTELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQSMVWLPVLHRVAAAETAKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEYCTPTTSGEDVRDFAKVLKNKFRTKRYFAKHPRMGYLPVQTVLEGDNMETPVTLINFWPVDSAPASSPQLSHDDTHSRIEHYASRLAEMENSNGSYLNDSISPNESIDDEHLLIQHYCQSLNQDSPLSQPRSPAQILISLESEERGELERILADLEEENRNLQAEYDRLKQQHEHKGLSPLPSPPEMMPTSPQSPRDAELIAEAKLLRQHKGRLEARMQILEDHNKQLESQLHRLRQLLEQPQAEAKVNGTTVSSPSTSLQRSDSSQPMLLRVVGSQTSDSMGEEDLLSPPQDTSTGLEEVMEQLNNSFPSSRGRNTPGKPMREDTM	Clinical trial	"PRO-051, an antisense oligonucleotide for the potential treatment of Duchenne muscular dystrophy. Curr Opin Mol Ther. 2010 Aug;12(4):478-86."	25	mRNA	mRNA target	.	.	.	"Calponin homology (CH) domain; EF hand; EF-hand; Spectrin repeat; WW domain; Zinc finger, ZZ type"	PF00307; PF09068; PF09069; PF00435; PF00397; PF00569	PF00307; CH; PF09068; EF-hand_2; PF09069; EF-hand_3; PF00435; Spectrin; PF00397; WW; PF00569; ZZ	.	.	hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy; hsa05416:Viral myocarditis	R-HSA-3000171:Non-integrin membrane-ECM interactions; R-HSA-390522:Striated Muscle Contraction	.	.
TT48MP6	Dystrophin (DMD)	P11532	DMD_HUMAN	Dystrophin protein	Dystrophin	DMD	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.	.	3UUN; 1EG4; 1EG3; 1DXX	MLWWEEVEDCYEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNVMKNIMAGLQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDPEDVDTTYPDKKSILMYITSLFQVLPQQVSIEAIQEVEMLPRPPKVTKEEHFQLHHQMHYSQQITVSLAQGYERTSSPKPRFKSYAYTQAAYVTTSDPTRSPFPSQHLEAPEDKSFGSSLMESEVNLDRYQTALEEVLSWLLSAEDTLQAQGEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIGTGKLSEDEETEVQEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQNQKLKELNDWLTKTEERTRKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDILLKWQRLTEEQCLFSAWLSEKEDAVNKIHTTGFKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSVTQKTEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLTQTTVMETVTTVTTREQILVKHAQEELPPPPPQKKRQITVDSEIRKRLDVDITELHSWITRSEAVLQSPEFAIFRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEGVNADSIKQASEQLNSRWIEFCQLLSERLNWLEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSEPTAIKSQLKICKDEVNRLSDLQPQIERLKIQSIALKEKGQGPMFLDADFVAFTNHFKQVFSDVQAREKELQTIFDTLPPMRYQETMSAIRTWVQQSETKLSIPQLSVTDYEIMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEWPALGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEFASRLETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANKWLNEVEFKLKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGGVMDELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVEPQISELNHRFAAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQIHTVREETMMVMTEDMPLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRSVEKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKTDASILQEKLGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQPVVTKETAISKLEMPSSLMLEVPALADFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDATRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKLYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLQELQEATDELDLKLRQAEVIKGSWQPVGDLLIDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLSTLEDLNTRWKLLQVAVEDRVRQLHEAHRDFGPASQHFLSTSVQGPWERAISPNKVPYYINHETQTTCWDHPKMTELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQSMVWLPVLHRVAAAETAKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEYCTPTTSGEDVRDFAKVLKNKFRTKRYFAKHPRMGYLPVQTVLEGDNMETPVTLINFWPVDSAPASSPQLSHDDTHSRIEHYASRLAEMENSNGSYLNDSISPNESIDDEHLLIQHYCQSLNQDSPLSQPRSPAQILISLESEERGELERILADLEEENRNLQAEYDRLKQQHEHKGLSPLPSPPEMMPTSPQSPRDAELIAEAKLLRQHKGRLEARMQILEDHNKQLESQLHRLRQLLEQPQAEAKVNGTTVSSPSTSLQRSDSSQPMLLRVVGSQTSDSMGEEDLLSPPQDTSTGLEEVMEQLNNSFPSSRGRNTPGKPMREDTM	Clinical trial	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800009280)"	17	TC=8.A.66	Zinc-finger	.	.	.	"Calponin homology (CH) domain; EF hand; EF-hand; Spectrin repeat; WW domain; Zinc finger, ZZ type"	PF00307; PF09068; PF09069; PF00435; PF00397; PF00569	PF00307; CH; PF09068; EF-hand_2; PF09069; EF-hand_3; PF00435; Spectrin; PF00397; WW; PF00569; ZZ	8.A.66.1.2	The Dystrophin (Dystrophin) Family	hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC); hsa05414:Dilated cardiomyopathy; hsa05416:Viral myocarditis	R-HSA-3000171:Non-integrin membrane-ECM interactions; R-HSA-390522:Striated Muscle Contraction	.	.
TT2TNRM	Dystrophin nonsense mutant (DMD)	P11532	DMD_HUMAN	.	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	DMD	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.	.	3UUN; 1EG4; 1EG3; 1DXX	MLWWEEVEDCYEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQKLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQVKNVMKNIMAGLQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDLFDWNSVVCQQSATQRLEHAFNIARYQLGIEKLLDPEDVDTTYPDKKSILMYITSLFQVLPQQVSIEAIQEVEMLPRPPKVTKEEHFQLHHQMHYSQQITVSLAQGYERTSSPKPRFKSYAYTQAAYVTTSDPTRSPFPSQHLEAPEDKSFGSSLMESEVNLDRYQTALEEVLSWLLSAEDTLQAQGEISNDVEVVKDQFHTHEGYMMDLTAHQGRVGNILQLGSKLIGTGKLSEDEETEVQEQMNLLNSRWECLRVASMEKQSNLHRVLMDLQNQKLKELNDWLTKTEERTRKMEEEPLGPDLEDLKRQVQQHKVLQEDLEQEQVRVNSLTHMVVVVDESSGDHATAALEEQLKVLGDRWANICRWTEDRWVLLQDILLKWQRLTEEQCLFSAWLSEKEDAVNKIHTTGFKDQNEMLSSLQKLAVLKADLEKKKQSMGKLYSLKQDLLSTLKNKSVTQKTEAWLDNFARCWDNLVQKLEKSTAQISQAVTTTQPSLTQTTVMETVTTVTTREQILVKHAQEELPPPPPQKKRQITVDSEIRKRLDVDITELHSWITRSEAVLQSPEFAIFRKEGNFSDLKEKVNAIEREKAEKFRKLQDASRSAQALVEQMVNEGVNADSIKQASEQLNSRWIEFCQLLSERLNWLEYQNNIIAFYNQLQQLEQMTTTAENWLKIQPTTPSEPTAIKSQLKICKDEVNRLSDLQPQIERLKIQSIALKEKGQGPMFLDADFVAFTNHFKQVFSDVQAREKELQTIFDTLPPMRYQETMSAIRTWVQQSETKLSIPQLSVTDYEIMEQRLGELQALQSSLQEQQSGLYYLSTTVKEMSKKAPSEISRKYQSEFEEIEGRWKKLSSQLVEHCQKLEEQMNKLRKIQNHIQTLKKWMAEVDVFLKEEWPALGDSEILKKQLKQCRLLVSDIQTIQPSLNSVNEGGQKIKNEAEPEFASRLETELKELNTQWDHMCQQVYARKEALKGGLEKTVSLQKDLSEMHEWMTQAEEEYLERDFEYKTPDELQKAVEEMKRAKEEAQQKEAKVKLLTESVNSVIAQAPPVAQEALKKELETLTTNYQWLCTRLNGKCKTLEEVWACWHELLSYLEKANKWLNEVEFKLKTTENIPGGAEEISEVLDSLENLMRHSEDNPNQIRILAQTLTDGGVMDELINEELETFNSRWRELHEEAVRRQKLLEQSIQSAQETEKSLHLIQESLTFIDKQLAAYIADKVDAAQMPQEAQKIQSDLTSHEISLEEMKKHNQGKEAAQRVLSQIDVAQKKLQDVSMKFRLFQKPANFEQRLQESKMILDEVKMHLPALETKSVEQEVVQSQLNHCVNLYKSLSEVKSEVEMVIKTGRQIVQKKQTENPKELDERVTALKLHYNELGAKVTERKQQLEKCLKLSRKMRKEMNVLTEWLAATDMELTKRSAVEGMPSNLDSEVAWGKATQKEIEKQKVHLKSITEVGEALKTVLGKKETLVEDKLSLLNSNWIAVTSRAEEWLNLLLEYQKHMETFDQNVDHITKWIIQADTLLDESEKKKPQQKEDVLKRLKAELNDIRPKVDSTRDQAANLMANRGDHCRKLVEPQISELNHRFAAISHRIKTGKASIPLKELEQFNSDIQKLLEPLEAEIQQGVNLKEEDFNKDMNEDNEGTVKELLQRGDNLQQRITDERKREEIKIKQQLLQTKHNALKDLRSQRRKKALEISHQWYQYKRQADDLLKCLDDIEKKLASLPEPRDERKIKEIDRELQKKKEELNAVRRQAEGLSEDGAAMAVEPTQIQLSKRWREIESKFAQFRRLNFAQIHTVREETMMVMTEDMPLEISYVPSTYLTEITHVSQALLEVEQLLNAPDLCAKDFEDLFKQEESLKNIKDSLQQSSGRIDIIHSKKTAALQSATPVERVKLQEALSQLDFQWEKVNKMYKDRQGRFDRSVEKWRRFHYDIKIFNQWLTEAEQFLRKTQIPENWEHAKYKWYLKELQDGIGQRQTVVRTLNATGEEIIQQSSKTDASILQEKLGSLNLRWQEVCKQLSDRKKRLEEQKNILSEFQRDLNEFVLWLEEADNIASIPLEPGKEQQLKEKLEQVKLLVEELPLRQGILKQLNETGGPVLVSAPISPEEQDKLENKLKQTNLQWIKVSRALPEKQGEIEAQIKDLGQLEKKLEDLEEQLNHLLLWLSPIRNQLEIYNQPNQEGPFDVKETEIAVQAKQPDVEEILSKGQHLYKEKPATQPVKRKLEDLSSEWKAVNRLLQELRAKQPDLAPGLTTIGASPTQTVTLVTQPVVTKETAISKLEMPSSLMLEVPALADFNRAWTELTDWLSLLDQVIKSQRVMVGDLEDINEMIIKQKATMQDLEQRRPQLEELITAAQNLKNKTSNQEARTIITDRIERIQNQWDEVQEHLQNRRQQLNEMLKDSTQWLEAKEEAEQVLGQARAKLESWKEGPYTVDAIQKKITETKQLAKDLRQWQTNVDVANDLALKLLRDYSADDTRKVHMITENINASWRSIHKRVSEREAALEETHRLLQQFPLDLEKFLAWLTEAETTANVLQDATRKERLLEDSKGVKELMKQWQDLQGEIEAHTDVYHNLDENSQKILRSLEGSDDAVLLQRRLDNMNFKWSELRKKSLNIRSHLEASSDQWKRLHLSLQELLVWLQLKDDELSRQAPIGGDFPAVQKQNDVHRAFKRELKTKEPVIMSTLETVRIFLTEQPLEGLEKLYQEPRELPPEERAQNVTRLLRKQAEEVNTEWEKLNLHSADWQRKIDETLERLQELQEATDELDLKLRQAEVIKGSWQPVGDLLIDSLQDHLEKVKALRGEIAPLKENVSHVNDLARQLTTLGIQLSPYNLSTLEDLNTRWKLLQVAVEDRVRQLHEAHRDFGPASQHFLSTSVQGPWERAISPNKVPYYINHETQTTCWDHPKMTELYQSLADLNNVRFSAYRTAMKLRRLQKALCLDLLSLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEHNNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWMRLEPQSMVWLPVLHRVAAAETAKHQAKCNICKECPIIGFRYRSLKHFNYDICQSCFFSGRVAKGHKMHYPMVEYCTPTTSGEDVRDFAKVLKNKFRTKRYFAKHPRMGYLPVQTVLEGDNMETPVTLINFWPVDSAPASSPQLSHDDTHSRIEHYASRLAEMENSNGSYLNDSISPNESIDDEHLLIQHYCQSLNQDSPLSQPRSPAQILISLESEERGELERILADLEEENRNLQAEYDRLKQQHEHKGLSPLPSPPEMMPTSPQSPRDAELIAEAKLLRQHKGRLEARMQILEDHNKQLESQLHRLRQLLEQPQAEAKVNGTTVSSPSTSLQRSDSSQPMLLRVVGSQTSDSMGEEDLLSPPQDTSTGLEEVMEQLNNSFPSSRGRNTPGKPMREDTM	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Ligand id: 7341).	25	.	.	.	.	.	"Calponin homology (CH) domain; EF hand; EF-hand; Spectrin repeat; WW domain; Zinc finger, ZZ type"	PF00307; PF09068; PF09069; PF00435; PF00397; PF00569	PF00307; CH; PF09068; EF-hand_2; PF09069; EF-hand_3; PF00435; Spectrin; PF00397; WW; PF00569; ZZ	.	.	hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy; hsa05416: Viral myocarditis	R-HSA-3000171: Non-integrin membrane-ECM interactions; R-HSA-390522: Striated Muscle Contraction	.	.
TTZQTY2	DMPK messenger RNA (DMPK mRNA)	Q09013	DMPK_HUMAN	mRNA target	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)	DMPK	"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."	EC 2.7.11.1	2VD5; 1WT6	MSAEVRLRRLQQLVLDPGFLGLEPLLDLLLGVHQELGASELAQDKYVADFLQWAEPIVVRLKEVRLQRDDFEILKVIGRGAFSEVAVVKMKQTGQVYAMKIMNKWDMLKRGEVSCFREERDVLVNGDRRWITQLHFAFQDENYLYLVMEYYVGGDLLTLLSKFGERIPAEMARFYLAEIVMAIDSVHRLGYVHRDIKPDNILLDRCGHIRLADFGSCLKLRADGTVRSLVAVGTPDYLSPEILQAVGGGPGTGSYGPECDWWALGVFAYEMFYGQTPFYADSTAETYGKIVHYKEHLSLPLVDEGVPEEARDFIQRLLCPPETRLGRGGAGDFRTHPFFFGLDWDGLRDSVPPFTPDFEGATDTCNFDLVEDGLTAMVSGGGETLSDIREGAPLGVHLPFVGYSYSCMALRDSEVPGPTPMELEAEQLLEPHVQAPSLEPSVSPQDETAEVAVPAAVPAAEAEAEVTLRELQEALEEEVLTRQSLSREMEAIRTDNQNFASQLREAEARNRDLEAHVRQLQERMELLQAEGATAVTGVPSPRATDPPSHLDGPPAVAVGQCPLVGPGPMHRRHLLLPARVPRPGLSEALSLLLFAVVLSRAAALGCIGLVAHAGQLTAVWRRPGAARAP	Clinical trial	"Clinical pipeline report, company report or official report of ISIS Pharmaceuticals."	19	mRNA	mRNA target	.	.	.	DMPK coiled coil domain like; Protein kinase domain	PF08826; PF00069	PF08826; DMPK_coil; PF00069; Pkinase	.	.	.	R-HSA-5578775: Ion homeostasis	.	Q09013
TTPXAWS	Heat shock protein 40 (HSP40)	P25685	DNJB1_HUMAN	Heat shock protein	Heat shock 40 kDa protein 1; HSP40; HDJ-1; DnaJ protein homolog 1; DnaJ homolog subfamily B member 1; DNAJB1	DNAJB1	Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP.	.	6BYR; 4WB7; 3AGZ; 3AGY; 3AGX	MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSGGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKKGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLIIEFEVIFPERIPQTSRTVLEQVLPI	Literature-reported	Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular a... Hum Mol Genet. 2002 Mar 1;11(5):515-23.	.	.	.	.	.	.	.	.	.	.	.	hsa04141: Protein processing in endoplasmic reticulum; hsa05164: Influenza A	R-HSA-3371453: Regulation of HSF1-mediated heat shock response; R-HSA-3371497: HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand; R-HSA-3371568: Attenuation phase; R-HSA-3371571: HSF1-dependent transactivation; R-HSA-5687128: MAPK6/MAPK4 signaling	.	P25685
TTYWGOJ	Deoxyribonuclease I (DNASE1)	P24855	DNAS1_HUMAN	Endodeoxyribonucleases	Herpesvirus alkaline deoxyribonuclease; Herpesvirus alkaline DNase; Dornase alfa; DNase I; DNASE1; Alkaline deoxyribonuclease	DNASE1	"Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization."	EC 3.1.21.1	4AWN	MRGMKLLGALLALAALLQGAVSLKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVMLK	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P24855
TT7KNZQ	Thymidine kinase 2 (Mt-TK2)	O00142	KITM_HUMAN	Kinase	dnk; Multispecific deoxynucleoside kinase; Dm-Dnk; Deoxyribonucleoside kinase	dnk	"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."	EC 2.7.1.21	.	MLLWPLRGWAARALRCFGPGSRGSPASGPGPRRVQRRAWPPDKEQEKEKKSVICVEGNIASGKTTCLEFFSNATDVEVLTEPVSKWRNVRGHNPLGLMYHDASRWGLTLQTYVQLTMLDRHTRPQVSSVRLMERSIHSARYIFVENLYRSGKMPEVDYVVLSEWFDWILRNMDVSVDLIVYLRTNPETCYQRLKKRCREEEKVIPLEYLEAIHHLHEEWLIKGSLFPMAAPVLVIEADHHMERMLELFEQNRDRILTPENRKHCP	Clinical trial	N1-substituted thymine derivatives as mitochondrial thymidine kinase (TK-2) inhibitors. J Med Chem. 2006 Dec 28;49(26):7766-73.	0	.	.	.	.	.	.	.	.	.	.	hsa00240: Pyrimidine metabolism; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa01232: Nucleotide metabolism	R-HSA-73614: Pyrimidine salvage	MetaCyc:HS09420-MON	O00142
TTE3JW9	Dynamin-1	.	DYN1_HUMAN	Single Protein	Dynamin 1 type; Dynamin type 1; DNM1; Dynamin 1	DNM1	Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.	.	.	MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVEEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRSGQASPSRPESPRPPFDL	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q05193
TTVRA5G	DNM2 messenger RNA (DNM2 mRNA)	P50570	DYN2_HUMAN	.	.	DNM2	"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)."	EC 3.6.5.5	.	MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEHAEFLHCKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLPALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTSKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQRSTQLNKKRAIPNQGEILVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWLQSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFANSDLFPAPPQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSLLD	Clinical trial	"Clinical pipeline report, company report or official report of Ionis Pharmaceuticals."	.	.	.	.	.	.	.	.	.	.	.	hsa04072: Phospholipase D signaling pathway; hsa04144: Endocytosis; hsa04666: Fc gamma R-mediated phagocytosis; hsa04721: Synaptic vesicle cycle; hsa04961: Endocrine and other factor-regulated calcium reabsorption; hsa05100: Bacterial invasion of epithelial cells; hsa05132: Salmonella infection	R-HSA-166016: Toll Like Receptor 4 (TLR4) Cascade; R-HSA-177504: Retrograde neurotrophin signalling; R-HSA-190873: Gap junction degradation; R-HSA-196025: Formation of annular gap junctions; R-HSA-203641: NOSTRIN mediated eNOS trafficking; R-HSA-2132295: MHC class II antigen presentation; R-HSA-432720: Lysosome Vesicle Biogenesis; R-HSA-432722: Golgi Associated Vesicle Biogenesis; R-HSA-437239: Recycling pathway of L1; R-HSA-8856828: Clathrin-mediated endocytosis; R-HSA-9031628: NGF-stimulated transcription	.	P50570
TT6S2FE	DNA [cytosine-5]-methyltransferase 1 (DNMT1)	P26358	DNMT1_HUMAN	Methyltransferase	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	DNMT1	"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."	EC 2.1.1.37	5YDR; 5WVO; 4Z97; 4Z96; 4YOC	MPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKECVKEKLNLLHEFLQTEIKNQLCDLETKLRKEELSEEGYLAKVKSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRVGMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKEEERDEKEEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPEEKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYLDDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEGGVNGKNLGPINEWWITGFDGGEKALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSNSDSTYEDLINKIETTVPPSGLNLNRFTEDSLLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRDLIKLAGVTLGQRRAQARRQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENAFKRRRCGVCEVCQQPECGKCKACKDMVKFGGSGRSKQACQERRCPNMAMKEADDDEEVDDNIPEMPSPKKMHQGKKKKQNKNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKAPSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCARLAEMRQKEIPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKRPRKEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLRTLDVFSGCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLVMAGETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVRNGASALEISYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRDLPNIEVRLSDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKARESASAKIKEEEAAKD	Clinical trial	"S110, a 5-Aza-2'-deoxycytidine-containing dinucleotide, is an effective DNA methylation inhibitor in vivo and can reduce tumor growth. Mol Cancer Ther. 2010 May;9(5):1443-50."	25	EC:2.1	Methyltransferase superfamily	class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.	2.1.1.37	Transferring one-carbon groups	BAH domain; DMAP1-binding Domain; C-5 cytosine-specific DNA methylase; Cytosine specific DNA methyltransferase replication foci domain; CXXC zinc finger domain	PF01426; PF06464; PF00145; PF12047; PF02008	PF01426; BAH; PF06464; DMAP_binding; PF00145; DNA_methylase; PF12047; DNMT1-RFD; PF02008; zf-CXXC	.	.	hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways; hsa05206:MicroRNAs in cancer	R-HSA-212300:PRC2 methylates histones and DNA; R-HSA-427413:NoRC negatively regulates rRNA expression; R-HSA-5334118:DNA methylation	.	P26358
TTOX4TW	HUMAN DNA [cytosine-5]-methyltransferase 1 (DNMT1)	P26358	DNMT1_HUMAN	Methyltransferase	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	DNMT1	"Human protein DNA methyltransferase 1 interacts with SARS-CoV-2 Orf8 protein with high significance, which indicates DNMT1 as a potential therapeutic target."	EC 2.1.1.37	5YDR; 5WVO; 4Z97; 4Z96; 4YOC	MPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKECVKEKLNLLHEFLQTEIKNQLCDLETKLRKEELSEEGYLAKVKSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRVGMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKEEERDEKEEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPEEKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYLDDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEGGVNGKNLGPINEWWITGFDGGEKALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSNSDSTYEDLINKIETTVPPSGLNLNRFTEDSLLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRDLIKLAGVTLGQRRAQARRQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENAFKRRRCGVCEVCQQPECGKCKACKDMVKFGGSGRSKQACQERRCPNMAMKEADDDEEVDDNIPEMPSPKKMHQGKKKKQNKNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKAPSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCARLAEMRQKEIPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKRPRKEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLRTLDVFSGCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLVMAGETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVRNGASALEISYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRDLPNIEVRLSDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKARESASAKIKEEEAAKD	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa00270: Cysteine and methionine metabolism; hsa01100: Metabolic pathways; hsa05206: MicroRNAs in cancer	R-HSA-212300: PRC2 methylates histones and DNA; R-HSA-427413: NoRC negatively regulates rRNA expression; R-HSA-4655427: SUMOylation of DNA methylation proteins; R-HSA-5334118: DNA methylation; R-HSA-9710421: Defective pyroptosis	.	P26358
TTJUALD	DNA [cytosine-5]-methyltransferase 3A (DNMT3A)	Q9Y6K1	DNM3A_HUMAN	Methyltransferase	M.HsaIIIA; Dnmt3a; DNA methyltransferase HsaIIIA; DNA MTase HsaIIIA; DNA (cytosine-5)-methyltransferase 3A	DNMT3A	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.	EC 2.1.1.37	6F57; 6BRR; 5YX2; 4U7T; 4U7P	MPAMPSSGPGDTSSSAAEREEDRKDGEEQEEPRGKEERQEPSTTARKVGRPGRKRKHPPVESGDTPKDPAVISKSPSMAQDSGASELLPNGDLEKRSEPQPEEGSPAGGQKGGAPAEGEGAAETLPEASRAVENGCCTPKEGRGAPAEAGKEQKETNIESMKMEGSRGRLRGGLGWESSLRQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAGMNAVEENQGPGESQKVEEASPPAVQQPTDPASPTVATTPEPVGSDAGDKNATKAGDDEPEYEDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIYEVLQVASSRAGKLFPVCHDSDESDTAKAVEVQNKPMIEWALGGFQPSGPKGLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTAEKPKVKEIIDERTRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKEYFACV	Patented-recorded	DNA methyltransferase inhibitors: an updated patent review (2012-2015).Expert Opin Ther Pat. 2016 Sep;26(9):1017-30.	15.5	EC:2.1	Class I-like SAM-binding methyltransferase superfamily	class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.	2.1.1.37	Transferring one-carbon groups	Cysteine rich ADD domain in DNMT3; C-5 cytosine-specific DNA methylase; PWWP domain	PF17980; PF00145; PF00855	PF17980; ADD_DNMT3; PF00145; DNA_methylase; PF00855; PWWP	.	.	hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways; hsa05206:MicroRNAs in cancer	R-HSA-212300: PRC2 methylates histones and DNA; R-HSA-3214858: RMTs methylate histone arginines; R-HSA-4655427: SUMOylation of DNA methylation proteins; R-HSA-5334118: DNA methylation; R-HSA-9710421: Defective pyroptosis	.	Q9Y6K1
TT6VZ78	DNA [cytosine-5]-methyltransferase 3B (DNMT3B)	Q9UBC3	DNM3B_HUMAN	Methyltransferase	M.HsaIIIB; Dnmt3b; DNA methyltransferase HsaIIIB; DNA methyltransferase 3B; DNA MTase HsaIIIB; DNA (cytosine-5)-methyltransferase 3B	DNMT3B	"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."	EC 2.1.1.37	5NVO; 5NV7; 5NV2; 5NV0; 5NRV	MKGDTRHLNGEEDAGGREDSILVNGACSDQSSDSPPILEAIRTPEIRGRRSSSRLSKREVSSLLSYTQDLTGDGDGEDGDGSDTPVMPKLFRETRTRSESPAVRTRNNNSVSSRERHRPSPRSTRGRQGRNHVDESPVEFPATRSLRRRATASAGTPWPSPPSSYLTIDLTDDTEDTHGTPQSSSTPYARLAQDSQQGGMESPQVEADSGDGDSSEYQDGKEFGIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVSYRKAMYHALEKARVRAGKTFPSSPGDSLEDQLKPMLEWAHGGFKPTGIEGLKPNNTQPVVNKSKVRRAGSRKLESRKYENKTRRRTADDSATSDYCPAPKRLKTNCYNNGKDRGDEDQSREQMASDVANNKSSLEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGTGTAAEAKLQEPWSCYMCLPQRCHGVLRRRKDWNVRLQAFFTSDTGLEYEAPKLYPAIPAARRRPIRVLSLFDGIATGYLVLKELGIKVGKYVASEVCEESIAVGTVKHEGNIKYVNDVRNITKKNIEEWGPFDLVIGGSPCNDLSNVNPARKGLYEGTGRLFFEFYHLLNYSRPKEGDDRPFFWMFENVVAMKVGDKRDISRFLECNPVMIDAIKVSAAHRARYFWGNLPGMNRPVIASKNDKLELQDCLEYNRIAKLKKVQTITTKSNSIKQGKNQLFPVVMNGKEDVLWCTELERIFGFPVHYTDVSNMGRGARQKLLGRSWSVPVIRHLFAPLKDYFACE	Clinical trial	Novel and selective DNA methyltransferase inhibitors: Docking-based virtual screening and experimental evaluation. Bioorg Med Chem. 2010 Jan 15;18(2):822-9.	25	EC:2.1	Methyltransferase superfamily	class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.	2.1.1.37	Transferring one-carbon groups	Cysteine rich ADD domain in DNMT3; C-5 cytosine-specific DNA methylase; PWWP domain	PF17980; PF00145; PF00855	PF17980; ADD_DNMT3; PF00145; DNA_methylase; PF00855; PWWP	.	.	hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways; hsa05206:MicroRNAs in cancer	R-HSA-212300:PRC2 methylates histones and DNA; R-HSA-427413:NoRC negatively regulates rRNA expression; R-HSA-5334118:DNA methylation	.	Q9UBC3
TT3FDAV	DNA [cytosine-5]-methyltransferase 3-like (DNMT3L)	Q9UJW3	DNM3L_HUMAN	.	DNA (cytosine-5)-methyltransferase 3-like	DNMT3L	"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."	.	6F57; 6BRR; 5YX2; 4U7T; 4U7P	MAAIPALDPEAEPSMDVILVGSSELSSSVSPGTGRDLIAYEVKANQRNIEDICICCGSLQVHTQHPLFEGGICAPCKDKFLDALFLYDDDGYQSYCSICCSGETLLICGNPDCTRCYCFECVDSLVGPGTSGKVHAMSNWVCYLCLPSSRSGLLQRRRKWRSQLKAFYDRESENPLEMFETVPVWRRQPVRVLSLFEDIKKELTSLGFLESGSDPGQLKHVVDVTDTVRKDVEEWGPFDLVYGATPPLGHTCDRPPSWYLFQFHRLLQYARPKPGSPRPFFWMFVDNLVLNKEDLDVASRFLEMEPVTIPDVHGGSLQNAVRVWSNIPAIRSRHWALVSEEELSLLAQNKQSSKLAAKWPTKLVKNCFLPLREYFKYFSTELTSSL	Patented-recorded	DNA methyltransferase inhibitors: an updated patent review (2012-2015).Expert Opin Ther Pat. 2016 Sep;26(9):1017-30.	15.5	.	.	.	.	.	Cysteine rich ADD domain in DNMT3	PF17980	PF17980; ADD_DNMT3	.	.	.	R-HSA-5334118: DNA methylation	.	Q9UJW3
TTGMFY7	Aspartyl aminopeptidase (DNPEP)	Q9ULA0	DNPEP_HUMAN	Peptidase	DAP; ASPEP	DNPEP	Likely to play an important role in intracellular protein and peptide metabolism. Aminopeptidase with specificity towards an acidic amino acid at the N-terminus.	EC 3.4.11.21	4DYO	MSGHSPTRGAMQVAMNGKARKEAVQTAAKELLKFVNRSPSPFHAVAECRNRLLQAGFSELKETEKWNIKPESKYFMTRNSSTIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRRSRRSQVGFQQVGVETYGGGIWSTWFDRDLTLAGRVIVKCPTSGRLEQQLVHVERPILRIPHLAIHLQRNINENFGPNTEMHLVPILATAIQEELEKGTPEPGPLNAVDERHHSVLMSLLCAHLGLSPKDIVEMELCLADTQPAVLGGAYDEFIFAPRLDNLHSCFCALQALIDSCAGPGSLATEPHVRMVTLYDNEEVGSESAQGAQSLLTELVLRRISASCQHPTAFEEAIPKSFMISADMAHAVHPNYLDKHEENHRPLFHKGPVIKVNSKQRYASNAVSEALIREVANKVKVPLQDLMVRNDTPCGTTIGPILASRLGLRVLDLGSPQLAMHSIREMACTTGVLQTLTLFKGFFELFPSLSHNLLVD	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	EC:3.4	.	peptidase M18 family.	3.4.11.21	Acting on peptide bonds (peptidases)	Aminopeptidase I zinc metalloprotease (M18)	PF02127	PF02127; Peptidase_M18	.	.	.	.	.	Q9ULA0
TTSZ8T1	Histone-lysine N-methyltransferase (HLNM)	Q8TEK3	DOT1L_HUMAN	Methyltransferase	"Lysine N-methyltransferase 4; KMT4; KIAA1814; Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone H3-K79 methyltransferase; H3-K79-HMTase; DOT1-like protein"	DOT1L	Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA.	EC 2.1.1.43	6O96; 6NQA; 6NOG; 6NN6; 6NJ9	MGEKLELRLKSPVGAEPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLAMENYVLIDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSTGLLRHILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTIDRTILENYFSSLKNPKLREEQEAARRRQQRESKSNAATPTKGPEGKVAGPADAPMDSGAEEEKAGAATVKKPSPSKARKKKLNKKGRKMAGRKRGRPKKMNTANPERKPKKNQTALDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSVQRHSPNPLLVAPTPPALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKARCEELQLDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKSCVPPDDALSLHLRGKGALGRELEPDASRLHLELDCTKFSLPHLSSMSPELSMNGQAAGYELCGVLSRPSSKQNTPQYLASPLDQEVVPCTPSHVGRPRLEKLSGLAAPDYTRLSPAKIVLRRHLSQDHTVPGRPAASELHSRAEHTKENGLPYQSPSVPGSMKLSPQDPRPLSPGALQLAGEKSSEKGLRERAYGSSGELITSLPISIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVLQPRDPSSTLEKQIGANAHGAGSRSLALAPAGFSYAGSVAISGALAGSPASLTPGAEPATLDESSSSGSLFATVGSRSSTPQHPLLLAQPRNSLPASPAHQLSSSPRLGGAAQGPLPEASKGDLPSDSGFSDPESEAKRRIVFTITTGAGSAKQSPSSKHSPLTASARGDCVPSHGQDSRRRGRRKRASAGTPSLSAGVSPKRRALPSVAGLFTQPSGSPLNLNSMVSNINQPLEITAISSPETSLKSSPVPYQDHDQPPVLKKERPLSQTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLAGRKPAPAGEPVNSSKWKSTFSPISDIGLAKSADSPLQASSALSQNSLFTFRPALEEPSADAKLAAHPRKGFPGSLSGADGLSPGTNPANGCTFGGGLAADLSLHSFSDGASLPHKGPEAAGLSSPLSFPSQRGKEGSDANPFLSKRQLDGLAGLKGEGSRGKEAGEGGLPLCGPTDKTPLLSGKAAKARDREVDLKNGHNLFISAAAVPPGSLLSGPGLAPAASSAGGAASSAQTHRSFLGPFPPGPQFALGPMSLQANLGSVAGSSVLQSLFSSVPAAAGLVHVSSAATRLTNSHAMGSFSGVAGGTVGGN	Clinical trial	Potent inhibition of DOT1L as treatment of MLL-fusion leukemia. Blood. 2013 August 8; 122(6): 1017-1025.	17	EC:2.1	Methyltransferase superfamily	class I-like SAM-binding methyltransferase superfamily. DOT1 family.	2.1.1.43 	Transferring one-carbon groups	Histone methylation protein DOT1 	PF08123	PF08123; DOT1	.	.	hsa00310:Lysine degradation; hsa05202:Transcriptional misregulation in cancer	R-HSA-3214841:PKMTs methylate histone lysines	MetaCyc:HS02643-MON	Q8TEK3
TTYUENF	Dehydropeptidase I (DPEP1)	P16444	DPEP1_HUMAN	Peptidase	hRDP; Renal dipeptidase; RDP; Microsomal dipeptidase; MDP; Dipeptidase 1; Dehydropeptidase-I	DPEP1	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.	EC 3.4.13.19	1ITU; 1ITQ	MWSGWWLWPLVAVCTADFFRDEAERIMRDSPVIDGHNDLPWQLLDMFNNRLQDERANLTTLAGTHTNIPKLRAGFVGGQFWSVYTPCDTQNKDAVRRTLEQMDVVHRMCRMYPETFLYVTSSAGIRQAFREGKVASLIGVEGGHSIDSSLGVLRALYQLGMRYLTLTHSCNTPWADNWLVDTGDSEPQSQGLSPFGQRVVKELNRLGVLIDLAHVSVATMKATLQLSRAPVIFSHSSAYSVCASRRNVPDDVLRLVKQTDSLVMVNFYNNYISCTNKANLSQVADHLDHIKEVAGARAVGFGGDFDGVPRVPEGLEDVSKYPDLIAELLRRNWTEAEVKGALADNLLRVFEAVEQASNLTQAPEEEPIPLDQLGGSCRTHYGYSSGASSLHRHWGLLLASLAPLVLCLSLL	Successful	Pharmacokinetic study of pleural fluid penetration of carbapenem antibiotic agents in chemical pleurisy. Respir Med. 2006 Feb;100(2):324-31.	34	EC:3.4	Peptidase	metallo-dependent hydrolases superfamily. Peptidase M19 family.	3.4.13.19	Acting on peptide bonds (peptidases)	Membrane dipeptidase (Peptidase family M19)	PF01244	PF01244; Peptidase_M19	.	.	.	R-HSA-5423646:Aflatoxin activation and detoxification	MetaCyc:HS00367-MON	P16444
TTV6BQU	Dolichol phosphate mannose synthase (DPMS)	O60762; O94777; Q9P2X0	DPM1_HUMAN; DPM2_HUMAN; DPM3_HUMAN	.	Mannose-P-dolichol synthase; MPD synthase; Dolichyl-phosphate beta-D-mannosyltransferase; Dolichol-phosphate mannosyltransferase; Dolichol-phosphate mannose synthase; DPM synthase	DPM1	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. 	.	.	MASLEVSRSPRRSRRELEVRSPRQNKYSVLLPTYNERENLPLIVWLLVKSFSESGINYEIIIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAYIHGMKHATGNYIIIMDADLSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGASDLTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT	Literature-reported	"Dolichol-phosphate mannose synthase: structure, function and regulation. Biochim Biophys Acta. 2008 Jun;1780(6):861-8."	.	.	.	.	.	.	.	.	.	.	.	hsa00510: N-Glycan biosynthesis; hsa01100: Metabolic pathways	R-HSA-162699: Synthesis of dolichyl-phosphate mannose; R-HSA-4717374: Defective DPM1 causes DPM1-CDG; R-HSA-4719360: Defective DPM3 causes DPM3-CDG; R-HSA-4719377: Defective DPM2 causes DPM2-CDG	MetaCyc:ENSG00000000419-MON	O60762
TTOVUPC	Similar to dipeptidyl aminopeptidase-like protein (DPP10)	Q8N608	DPP10_HUMAN	Prolyl oligopeptidase family	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	DPP10	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.	.	4WJL	MNQTASVSHHIKCQPSKTIKELGSNSPPQRNWKGIAIALLVILVVCSLITMSVILLTPDELTNSSETRLSLEDLFRKDFVLHDPEARWINDTDVVYKSENGHVIKLNIETNATTLLLENTTFVTFKASRHSVSPDLKYVLLAYDVKQIFHYSYTASYVIYNIHTREVWELNPPEVEDSVLQYAAWGVQGQQLIYIFENNIYYQPDIKSSSLRLTSSGKEEIIFNGIADWLYEEELLHSHIAHWWSPDGERLAFLMINDSLVPTMVIPRFTGALYPKGKQYPYPKAGQVNPTIKLYVVNLYGPTHTLELMPPDSFKSREYYITMVKWVSNTKTVVRWLNRAQNISILTVCETTTGACSKKYEMTSDTWLSQQNEEPVFSRDGSKFFMTVPVKQGGRGEFHHVAMFLIQSKSEQITVRHLTSGNWEVIKILAYDETTQKIYFLSTESSPRGRQLYSASTEGLLNRQCISCNFMKEQCTYFDASFSPMNQHFLLFCEGPRVPVVSLHSTDNPAKYFILESNSMLKEAILKKKIGKPEIKILHIDDYELPLQLSLPKDFMDRNQYALLLIMDEEPGGQLVTDKFHIDWDSVLIDMDNVIVARFDGRGSGFQGLKILQEIHRRLGSVEVKDQITAVKFLLKLPYIDSKRLSIFGKGYGGYIASMILKSDEKLFKCGSVVAPITDLKLYASAFSERYLGMPSKEESTYQAASVLHNVHGLKEENILIIHGTADTKVHFQHSAELIKHLIKAGVNYTMQVYPDEGHNVSEKSKYHLYSTILKFFSDCLKEEISVLPQEPEEDE	Literature-reported	Positional cloning of a novel gene influencing asthma from chromosome 2q14. Nat Genet. 2003 Nov;35(3):258-63.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q8N608
TTDIGC1	Dipeptidyl peptidase 4 (DPP-4)	P27487	DPP4_HUMAN	Peptidase	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	DPP4	"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."	EC 3.4.14.5	6B1O; 6B1E; 5ZID; 5Y7K; 5Y7J	MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP	Successful	"Clinical pipeline report, company report or official report of Takeda (2009)."	34	EC:3.4	Peptidase	peptidase S9B family. DPPIV subfamily.	3.4.14.5 	Acting on peptide bonds (peptidases)	Dipeptidyl peptidase IV (DPP IV) N-terminal region; Prolyl oligopeptidase family	PF00930; PF00326	PF00930; DPPIV_N; PF00326; Peptidase_S9	.	.	hsa04974:Protein digestion and absorption	"R-HSA-381771: Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1); R-HSA-400511: Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP)"	.	P27487
TTF928K	HUMAN dipeptidyl peptidase 4 (DPP-4)	P27487	DPP4_HUMAN	Peptidase	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	DPP4	"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."	EC 3.4.14.5	6B1O; 6B1E; 5ZID; 5Y7K; 5Y7J	MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP	.	In-vitro renal epithelial cell infection reveals a viral kidney tropism as a potential mechanism for acute renal failure during Middle East Respira... Virol J. 2013 Dec 23;10:359.	34	EC:3.4	Peptidase	peptidase S9B family. DPPIV subfamily.	3.4.14.5 	Acting on peptide bonds (peptidases)	Dipeptidyl peptidase IV (DPP IV) N-terminal region; Prolyl oligopeptidase family	PF00930; PF00326	PF00930; DPPIV_N; PF00326; Peptidase_S9	.	.	hsa04974: Protein digestion and absorption	"R-HSA-381771: Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1); R-HSA-400511: Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP)"	.	P27487
TTOYT5L	Dipeptidyl-peptidase 7 (DPP7)	Q9UHL4	DPP2_HUMAN	.	Quiescent cell proline dipeptidase; QPP; Dipeptidyl peptidase II; Dipeptidyl peptidase 7; Dipeptidyl peptidase 2; Dipeptidyl aminopeptidase II; DPP2; DPP II	DPP7	Plays an important role in the degradation of some oligopeptides.	EC 3.4.14.2	4EBB; 3N0T; 3JYH	MGSAPWAPVLLLALGLRGLQAGARRAPDPGFQERFFQQRLDHFNFERFGNKTFPQRFLVSDRFWVRGEGPIFFYTGNEGDVWAFANNSAFVAELAAERGALLVFAEHRYYGKSLPFGAQSTQRGHTELLTVEQALADFAELLRALRRDLGAQDAPAIAFGGSYGGMLSAYLRMKYPHLVAGALAASAPVLAVAGLGDSNQFFRDVTADFEGQSPKCTQGVREAFRQIKDLFLQGAYDTVRWEFGTCQPLSDEKDLTQLFMFARNAFTVLAMMDYPYPTDFLGPLPANPVKVGCDRLLSEAQRITGLRALAGLVYNASGSEHCYDIYRLYHSCADPTGCGTGPDARAWDYQACTEINLTFASNNVTDMFPDLPFTDELRQRYCLDTWGVWPRPDWLLTSFWGGDLRAASNIIFSNGNLDPWAGGGIRRNLSASVIAVTIQGGAHHLDLRASHPEDPASVVEARKLEATIIGEWVKAARREQQPALRGGPRLSL	Patented-recorded	Dipeptidyl peptidase II and leukocyte cell death. Biochem Pharmacol. 2006 Jun 28;72(1):70-9.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-6798695: Neutrophil degranulation	.	Q9UHL4
TTJGLZF	Dipeptidyl peptidase 8 (DPP-8)	Q6V1X1	DPP8_HUMAN	Peptidase	Prolyl dipeptidase DPP8; MSTP141; MSTP135; MSTP097; Dipeptidyl peptidase VIII; Dipeptidyl peptidase IV-related protein 1; DPRP1; DPRP-1; DPP VIII; DP8	DPP8	Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2.	EC 3.4.14.5	6EOT; 6EOS; 6EOP; 6EOO	MWKRSEQMKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHSDRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIGTVGIASYDYHQGSGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPNIRMDPKLCPADPDWIAFIHSNDIWISNIVTREERRLTYVHNELANMEEDARSAGVATFVLQEEFDRYSGYWWCPKAETTPSGGKILRILYEENDESEVEIIHVTSPMLETRRADSFRYPKTGTANPKVTFKMSEIMIDAEGRIIDVIDKELIQPFEILFEGVEYIARAGWTPEGKYAWSILLDRSQTRLQIVLISPELFIPVEDDVMERQRLIESVPDSVTPLIIYEETTDIWINIHDIFHVFPQSHEEEIEFIFASECKTGFRHLYKITSILKESKYKRSSGGLPAPSDFKCPIKEEIAITSGEWEVLGRHGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDRGYSHSCCISQHCDFFISKYSNQKNPHCVSLYKLSSPEDDPTCKTKEFWATILDSAGPLPDYTPPEIFSFESTTGFTLYGMLYKPHDLQPGKKYPTVLFIYGGPQVQLVNNRFKGVKYFRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTGYTERYMGHPDQNEQGYYLGSVAMQAEKFPSEPNRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSRIAALKVI	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	EC:3.4	.	peptidase S9B family. DPPIV subfamily.	3.4.14.5 	Acting on peptide bonds (peptidases)	Dipeptidyl peptidase IV (DPP IV) N-terminal region; Prolyl oligopeptidase family	PF00930; PF00326	PF00930; DPPIV_N; PF00326; Peptidase_S9	.	.	.	.	.	Q6V1X1
TTNDUL7	Dipeptidyl peptidase 9 (DPP-9)	Q86TI2	DPP9_HUMAN	Peptidase	Dipeptidyl peptidase-like protein 9; Dipeptidyl peptidase IX; Dipeptidyl peptidase IV-related protein 2; DPRP2; DPRP-2; DPP IX; DPLP9; DP9	DPP9	Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2.	EC 3.4.14.5	6EOR; 6EOQ	MATTGTPTADRGDAAATDDPAARFQVQKHSWDGLRSIIHGSRKYSGLIVNKAPHDFQFVQKTDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLLSWKQMLDHFQATPHHGVYSREEELLRERKRLGVFGITSYDFHSESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIKTQCSGPRMDPKICPADPAFFSFINNSDLWVANIETGEERRLTFCHQGLSNVLDDPKSAGVATFVIQEEFDRFTGYWWCPTASWEGSEGLKTLRILYEEVDESEVEVIHVPSPALEERKTDSYRYPRTGSKNPKIALKLAEFQTDSQGKIVSTQEKELVQPFSSLFPKVEYIARAGWTRDGKYAWAMFLDRPQQWLQLVLLPPALFIPSTENEEQRLASARAVPRNVQPYVVYEEVTNVWINVHDIFYPFPQSEGEDELCFLRANECKTGFCHLYKVTAVLKSQGYDWSEPFSPGEDEFKCPIKEEIALTSGEWEVLARHGSKIWVNEETKLVYFQGTKDTPLEHHLYVVSYEAAGEIVRLTTPGFSHSCSMSQNFDMFVSHYSSVSTPPCVHVYKLSGPDDDPLHKQPRFWASMMEAASCPPDYVPPEIFHFHTRSDVRLYGMIYKPHALQPGKKHPTVLFVYGGPQVQLVNNSFKGIKYLRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKYGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTGYTERYMDVPENNQHGYEAGSVALHVEKLPNEPNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHSIRCPESGEHYEVTLLHFLQEYL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	EC:3.4	.	peptidase S9B family. DPPIV subfamily.	3.4.14.5 	Acting on peptide bonds (peptidases)	Dipeptidyl peptidase IV (DPP IV) N-terminal region; Prolyl oligopeptidase family	PF00930; PF00326	PF00930; DPPIV_N; PF00326; Peptidase_S9	.	.	.	.	.	Q86TI2
TTZPS91	Dihydrothymine dehydrogenase (DPYD)	Q12882	DPYD_HUMAN	CH/CH donor oxidoreductase	Dihydrouracil dehydrogenase; Dihydropyrimidine dehydrogenase [NADP(+)]; Dihydropyrimidine dehydrogenase; DPD; DHPDHase	DPYD	Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil. Involved in pyrimidine base degradation.	EC 1.3.1.2	.	MAPVLSKDSADIESILALNPRTQTHATLCSTSAKKLDKKHWKRNPDKNCFNCEKLENNFDDIKHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCNLYATEEGPINIGGLQQFATEVFKAMSIPQIRNPSLPPPEKMSEAYSAKIALFGAGPASISCASFLARLGYSDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNEMTLSTLKEKGYKAAFIGIGLPEPNKDAIFQGLTQDQGFYTSKDFLPLVAKGSKAGMCACHSPLPSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQDETGKWNEDEDQMVHLKADVVISAFGSVLSDPKVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQSQYGASVSAKPELPLFYTPIDLVDISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPMYGPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLMGLKSDGTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTSIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELQDWDGQSPATVSHQKGKPVPRIAELMDKKLPSFGPYLEQRKKIIAENKIRLKEQNVAFSPLKRNCFIPKRPIPTIKDVIGKALQYLGTFGELSNVEQVVAMIDEEMCINCGKCYMTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPIVDCIKMVSRTTPYEPKRGVPLSVNPVC	Successful	"Enhancement of the antitumour activity of 5-fluorouracil (5-FU) by inhibiting dihydropyrimidine dehydrogenase activity (DPD) using 5-chloro-2,4-dihydroxypyridine (CDHP) in human tumour cells. Eur J Cancer. 2002 Jun;38(9):1271-7."	34	EC:1.3	Dihydropyrimidine dehydrogenase	dihydropyrimidine dehydrogenase family.	1.3.1.2	Acting on the CH-CH group of donors	"Dihydroorotate dehydrogenase; Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Pyridine nucleotide-disulphide oxidoreductase"	PF01180; PF14691; PF07992	PF01180; DHO_dh; PF14691; Fer4_20; PF07992; Pyr_redox_2	.	.	hsa00240:Pyrimidine metabolism; hsa00410:beta-Alanine metabolism; hsa00770:Pantothenate and CoA biosynthesis; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways	R-HSA-73621: Pyrimidine catabolism	MetaCyc:HS06975-MON	Q12882
TTZCW3T	Dihydropyrimidinase related protein 2 (DPYSL2)	Q16555	DPYL2_HUMAN	.	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	DPYSL2	"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."	.	5YZB; 5YZA; 5YZ5; 5X1D; 5X1C	MSYQGKKNIPRITSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLAELRGVPRGLYDGPVCEVSVTPKTVTPASSAKTSPAKQQAPPVRNLHQSGFSLSGAQIDDNIPRRTTQRIVAPPGGRANITSLG	Successful	2008 FDA drug approvals. Nat Rev Drug Discov. 2009 Feb;8(2):93-6.	34	.	.	metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family.	.	.	Amidohydrolase family	PF01979	PF01979; Amidohydro_1	.	.	hsa04360: Axon guidance	R-HSA-399956: CRMPs in Sema3A signaling; R-HSA-437239: Recycling pathway of L1	.	Q16555
TTZFYLI	Dopamine D1 receptor (D1R)	P21728	DRD1_HUMAN	GPCR rhodopsin	D(1A) dopamine receptor	DRD1	Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.	.	1OZ5	MRTLNTSAMDGTGLVVERDFSVRILTACFLSLLILSTLLGNTLVCAAVIRFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVAEIAGFWPFGSFCNIWVAFDIMCSTASILNLCVISVDRYWAISSPFRYERKMTPKAAFILISVAWTLSVLISFIPVQLSWHKAKPTSPSDGNATSLAETIDNCDSSLSRTYAISSSVISFYIPVAIMIVTYTRIYRIAQKQIRRIAALERAAVHAKNCQTTTGNGKPVECSQPESSFKMSFKRETKVLKTLSVIMGVFVCCWLPFFILNCILPFCGSGETQPFCIDSNTFDVFVWFGWANSSLNPIIYAFNADFRKAFSTLLGCYRLCPATNNAIETVSINNNGAAMFSSHHEPRGSISKECNLVYLIPHAVGSSEDLKKEEAAGIARPLEKLSPALSVILDYDTDVSLEKIQPITQNGQHPT	Successful	Etiology of iodinated radiocontrast nephrotoxicity and its attenuation by beraprost. Yakugaku Zasshi. 2008 Jul;128(7):1023-9.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	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	R-HSA-390651:Dopamine receptors; R-HSA-418555:G alpha (s) signalling events	.	P21728
TTEX248	Dopamine D2 receptor (D2R)	P14416	DRD2_HUMAN	GPCR rhodopsin	Dopamine receptor 2; D(2) dopamine receptor	DRD2	Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase.	.	6CM4; 5AER; 1I15	MDPLNLSWYDDDLERQNWSRPFNGSDGKADRPHYNYYATLLTLLIAVIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMISIVWVLSFTISCPLLFGLNNADQNECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRRRRKRVNTKRSSRAFRAHLRAPLKGNCTHPEDMKLCTVIMKSNGSFPVNRRRVEAARRAQELEMEMLSSTSPPERTRYSPIPPSHHQLTLPDPSHHGLHSTPDSPAKPEKNGHAKDHPKIAKIFEIQTMPNGKTRTSLKTMSRRKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNIHCDCNIPPVLYSAFTWLGYVNSAVNPIIYTTFNIEFRKAFLKILHC	Successful	"Silymarin BIO-C, an extract from Silybum marianum fruits, induces hyperprolactinemia in intact female rats. Phytomedicine. 2009 Sep;16(9):839-44."	34	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.3.10	The G-protein-coupled receptor (GPCR) Family	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	R-HSA-390651:Dopamine receptors; R-HSA-418594:G alpha (i) signalling events	.	P14416
TT4C8EA	Dopamine D3 receptor (D3R)	P35462	DRD3_HUMAN	GPCR rhodopsin	D(3) dopamine receptor	DRD3	Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation.	.	3PBL	MASLSQLSSHLNYTCGAENSTGASQARPHAYYALSYCALILAIVFGNGLVCMAVLKERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPTVCSISNPDFVIYSSVVSFYLPFGVTVLVYARIYVVLKQRRRKRILTRQNSQCNSVRPGFPQQTLSPDPAHLELKRYYSICQDTALGGPGFQERGGELKREEKTRNSLSPTIAPKLSLEVRKLSNGRLSTSLKLGPLQPRGVPLREKKATQMVAIVLGAFIVCWLPFFLTHVLNTHCQTCHVSPELYSATTWLGYVNSALNPVIYTTFNIEFRKAFLKILSC	Successful	Radium 223 dichloride for prostate cancer treatment. Drug Des Devel Ther. 2017 Sep 6;11:2643-2651.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.3.9	The G-protein-coupled receptor (GPCR) Family	hsa04080:Neuroactive ligand-receptor interaction; hsa04728:Dopaminergic synapse	R-HSA-390651:Dopamine receptors; R-HSA-418594:G alpha (i) signalling events	.	P35462
TTE0A2F	Dopamine D4 receptor (D4R)	P21917	DRD4_HUMAN	GPCR rhodopsin	DRD4; D(2C)D(4) dopamine receptor dopamine receptor	DRD4	"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."	.	5WIV; 5WIU	MGNRSTADADGLLAGRGPAAGASAGASAGLAGQGAAALVGGVLLIGAVLAGNSLVCVSVATERALQTPTNSFIVSLAAADLLLALLVLPLFVYSEVQGGAWLLSPRLCDALMAMDVMLCTASIFNLCAISVDRFVAVAVPLRYNRQGGSRRQLLLIGATWLLSAAVAAPVLCGLNDVRGRDPAVCRLEDRDYVVYSSVCSFFLPCPLMLLLYWATFRGLQRWEVARRAKLHGRAPRRPSGPGPPSPTPPAPRLPQDPCGPDCAPPAPGLPRGPCGPDCAPAAPSLPQDPCGPDCAPPAPGLPPDPCGSNCAPPDAVRAAALPPQTPPQTRRRRRAKITGRERKAMRVLPVVVGAFLLCWTPFFVVHITQALCPACSVPPRLVSAVTWLGYVNSALNPVIYTVFNAEFRNVFRKALRACC	Successful	Dopamine/serotonin receptor ligands. 9. Oxygen-containing midsized heterocyclic ring systems and nonrigidized analogues. A step toward dopamine D5 ... J Med Chem. 2004 Aug 12;47(17):4155-8.	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04728:Dopaminergic synapse	R-HSA-390651:Dopamine receptors; R-HSA-418594:G alpha (i) signalling events	.	P21917
TTS2PH3	Dopamine D5 receptor (D5R)	P21918	DRD5_HUMAN	GPCR rhodopsin	Dopamine receptor 5; DRD5; D1beta dopamine receptor; D(5)D(1B) dopamine receptor dopamine receptor; D(5) dopamine receptor	DRD5	Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.	.	.	MLPPGSNGTAYPGQFALYQQLAQGNAVGGSAGAPPLGPSQVVTACLLTLLIIWTLLGNVLVCAAIVRSRHLRANMTNVFIVSLAVSDLFVALLVMPWKAVAEVAGYWPFGAFCDVWVAFDIMCSTASILNLCVISVDRYWAISRPFRYKRKMTQRMALVMVGLAWTLSILISFIPVQLNWHRDQAASWGGLDLPNNLANWTPWEEDFWEPDVNAENCDSSLNRTYAISSSLISFYIPVAIMIVTYTRIYRIAQVQIRRISSLERAAEHAQSCRSSAACAPDTSLRASIKKETKVLKTLSVIMGVFVCCWLPFFILNCMVPFCSGHPEGPPAGFPCVSETTFDVFVWFGWANSSLNPVIYAFNADFQKVFAQLLGCSHFCSRTPVETVNISNELISYNQDIVFHKEIAAAYIHMMPNAVTPGNREVDNDEEEGPFDRMFQIYQTSPDGDPVAESVWELDCEGEISLDKITPFTPNGFH	Successful	Dopamine/serotonin receptor ligands. 9. Oxygen-containing midsized heterocyclic ring systems and nonrigidized analogues. A step toward dopamine D5 ... J Med Chem. 2004 Aug 12;47(17):4155-8.	34	.	.	.	.	.	.	.	.	.	.	hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04728:Dopaminergic synapse	R-HSA-390651:Dopamine receptors; R-HSA-418555:G alpha (s) signalling events	.	P21918
TTEO4P8	Desmoglein-3 (DSG3)	P32926	DSG3_HUMAN	.	PVA; DSG3; Cadherin family member 6; 130 kDa pemphigus vulgaris antigen	DSG3	Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.	.	5EQX	MMGLFPRTTGALAIFVVVILVHGELRIETKGQYDEEEMTMQQAKRRQKREWVKFAKPCREGEDNSKRNPIAKITSDYQATQKITYRISGVGIDQPPFGIFVVDKNTGDINITAIVDREETPSFLITCRALNAQGLDVEKPLILTVKILDINDNPPVFSQQIFMGEIEENSASNSLVMILNATDADEPNHLNSKIAFKIVSQEPAGTPMFLLSRNTGEVRTLTNSLDREQASSYRLVVSGADKDGEGLSTQCECNIKVKDVNDNFPMFRDSQYSARIEENILSSELLRFQVTDLDEEYTDNWLAVYFFTSGNEGNWFEIQTDPRTNEGILKVVKALDYEQLQSVKLSIAVKNKAEFHQSVISRYRVQSTPVTIQVINVREGIAFRPASKTFTVQKGISSKKLVDYILGTYQAIDEDTNKAASNVKYVMGRNDGGYLMIDSKTAEIKFVKNMNRDSTFIVNKTITAEVLAIDEYTGKTSTGTVYVRVPDFNDNCPTAVLEKDAVCSSSPSVVVSARTLNNRYTGPYTFALEDQPVKLPAVWSITTLNATSALLRAQEQIPPGVYHISLVLTDSQNNRCEMPRSLTLEVCQCDNRGICGTSYPTTSPGTRYGRPHSGRLGPAAIGLLLLGLLLLLLAPLLLLTCDCGAGSTGGVTGGFIPVPDGSEGTIHQWGIEGAHPEDKEITNICVPPVTANGADFMESSEVCTNTYARGTAVEGTSGMEMTTKLGAATESGGAAGFATGTVSGAASGFGAATGVGICSSGQSGTMRTRHSTGGTNKDYADGAISMNFLDSYFSQKAFACAEEDDGQEANDCLLIYDNEGADATGSPVGSVGCCSFIADDLDDSFLDSLGPKFKKLAEISLGVDGEGKEVQPPSKDSGYGIESCGHPIEVQQTGFVKCQTLSGSQGASALSTSGSVQPAVSIPDPLQHGNYLVTETYSASGSLVQPSTAGFDPLLTQNVIVTERVICPISSVPGNLAGPTQLRGSHTMLCTEDPCSRLI	Literature-reported	Desmoglein 3: a help or a hindrance in cancer progression Cancers (Basel). 2015 Jan 26;7(1):266-86.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-351906: Apoptotic cleavage of cell adhesion proteins; R-HSA-6805567: Keratinization; R-HSA-6809371: Formation of the cornified envelope	.	P32926
TT8396I	DDB1- and CUL4-associated factor 2 (DTL)	Q9NZJ0	DTL_HUMAN	.	Retinoic acid-regulated nuclear matrix-associated protein; RAMP; Lethal(2) denticleless protein homolog; L2DTL; Denticleless protein homolog; DCAF2; CDW1; CDT2	DTL	"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."	.	6QC0	MLFNSVLRQPQLGVLRNGWSSQYPLQSLLTGYQCSGNDEHTSYGETGVPVPPFGCTFSSAPNMEHVLAVANEEGFVRLYNTESQSFRKKCFKEWMAHWNAVFDLAWVPGELKLVTAAGDQTAKFWDVKAGELIGTCKGHQCSLKSVAFSKFEKAVFCTGGRDGNIMVWDTRCNKKDGFYRQVNQISGAHNTSDKQTPSKPKKKQNSKGLAPSVDFQQSVTVVLFQDENTLVSAGAVDGIIKVWDLRKNYTAYRQEPIASKSFLYPGSSTRKLGYSSLILDSTGSTLFANCTDDNIYMFNMTGLKTSPVAIFNGHQNSTFYVKSSLSPDDQFLVSGSSDEAAYIWKVSTPWQPPTVLLGHSQEVTSVCWCPSDFTKIATCSDDNTLKIWRLNRGLEEKPGGDKLSTVGWASQKKKESRPGLVTVTSSQSTPAKAPRAKCNPSNSSPSSAACAPSCAGDLPLPSNTPTFSIKTSPAKARSPINRRGSVSSVSPKPPSSFKMSIRNWVTRTPSSSPPITPPASETKIMSPRKALIPVSQKSSQAEACSESRNRVKRRLDSSCLESVKQKCVKSCNCVTELDGQVENLHLDLCCLAGNQEDLSKDSLGPTKSSKIEGAGTSISEPPSPISPYASESCGTLPLPLRPCGEGSEMVGKENSSPENKNWLLAMAAKRKAENPSPRSPSSQTPNSRRQSGKKLPSPVTITPSSMRKICTYFHRKSQEDFCGPEHSTEL	Literature-reported	CRL4DCAF2 is required for mature T-cell expansion via Aurora B-regulated proteasome activity. J Autoimmun. 2019 Jan;96:74-85.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-110314: Recognition of DNA damage by PCNA-containing replication complex; R-HSA-8951664: Neddylation	.	Q9NZJ0
TTG8HIM	Dual specificity protein phosphatase 1 (DUSP1)	P28562	DUS1_HUMAN	Phosphoric monoester hydrolase	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	DUSP1	"Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle."	EC 3.1.3.16	6D67; 6D66; 6D65; 6APX	MVMEVGTLDAGGLRALLGERAAQCLLLDCRSFFAFNAGHIAGSVNVRFSTIVRRRAKGAMGLEHIVPNAELRGRLLAGAYHAVVLLDERSAALDGAKRDGTLALAAGALCREARAAQVFFLKGGYEAFSASCPELCSKQSTPMGLSLPLSTSVPDSAESGCSSCSTPLYDQGGPVEILPFLYLGSAYHASRKDMLDALGITALINVSANCPNHFEGHYQYKSIPVEDNHKADISSWFNEAIDFIDSIKNAGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQVLAPHCSAEAGSPAMAVLDRGTSTTTVFNFPVSIPVHSTNSALSYLQSPITTSPSC	Clinical trial	"Bioactivities of simplified adociaquinone B and naphthoquinone derivatives against Cdc25B, MKP-1, and MKP-3 phosphatases. Bioorg Med Chem. 2009 Mar 15;17(6):2276-81."	25	EC:3.1.3	Phosphoric monoester hydrolases	protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.	3.1.3.16 	Acting on ester bonds	"Dual specificity phosphatase, catalytic domain; Rhodanese-like domain"	PF00782; PF00581	PF00782; DSPc; PF00581; Rhodanese	.	.	hsa04010:MAPK signaling pathway; hsa04726:Serotonergic synapse	R-HSA-112409:RAF-independent MAPK1/3 activation; R-HSA-5675221:Negative regulation of MAPK pathway	.	P28562
TTF3RJ0	Dual specificity protein phosphatase 10 (DUSP10)	Q9Y6W6	DUS10_HUMAN	Phosphoric monoester hydrolase	Mitogen-activated protein kinase phosphatase 5; MKP5; MKP-5; MAP kinase phosphatase 5	DUSP10	Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38. Protein phosphatase involved in the inactivation of MAP kinases.	EC 3.1.3.16	3TG1; 2OUD; 2OUC; 1ZZW	MPPSPLDDRVVVALSRPVRPQDLNLCLDSSYLGSANPGSNSHPPVIATTVVSLKAANLTYMPSSSGSARSLNCGCSSASCCTVATYDKDNQAQTQAIAAGTTTTAIGTSTTCPANQMVNNNENTGSLSPSSGVGSPVSGTPKQLASIKIIYPNDLAKKMTKCSKSHLPSQGPVIIDCRPFMEYNKSHIQGAVHINCADKISRRRLQQGKITVLDLISCREGKDSFKRIFSKEIIVYDENTNEPSRVMPSQPLHIVLESLKREGKEPLVLKGGLSSFKQNHENLCDNSLQLQECREVGGGASAASSLLPQPIPTTPDIENAELTPILPFLFLGNEQDAQDLDTMQRLNIGYVINVTTHLPLYHYEKGLFNYKRLPATDSNKQNLRQYFEEAFEFIEEAHQCGKGLLIHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKGKRPIISPNLNFMGQLLEFEEDLNNGVTPRILTPKLMGVETVV	Literature-reported	DUSP10 regulates intestinal epithelial cell growth and colorectal tumorigenesis. Oncogene. 2016 Jan 14;35(2):206-17.	.	EC:3.1.3	Phosphoric monoester hydrolases	protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.	3.1.3.16 	Acting on ester bonds	"Dual specificity phosphatase, catalytic domain; Rhodanese-like domain"	PF00782; PF00581	PF00782; DSPc; PF00581; Rhodanese	.	.	hsa04010: MAPK signaling pathway	R-HSA-112409: RAF-independent MAPK1/3 activation; R-HSA-5675221: Negative regulation of MAPK pathway; R-HSA-9652817: Signaling by MAPK mutants	.	Q9Y6W6
TTIFAYS	Vaccinia H1 phosphatase	.	DUS3_HUMAN	Single Protein	Dual specificity protein phosphatase VHR; VHR; Vaccinia H1-related phosphatase; Dual specificity protein phosphatase 3; DUSP3	DUSP3	"Shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. Specifically dephosphorylates and inactivates ERK1 and ERK2."	.	.	MSGSFELSVQDLNDLLSDGSGCYSLPSQPCNEVTPRIYVGNASVAQDIPKLQKLGITHVLNAAEGRSFMHVNTNANFYKDSGITYLGIKANDTQEFNLSAYFERAADFIDQALAQKNGRVLVHCREGYSRSPTLVIAYLMMRQKMDVKSALSIVRQNREIGPNDGFLAQLCQLNDRLAKEGKLKP	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P51452
TTZN92A	DUSP5 messenger RNA (DUSP5 mRNA)	Q16690	DUS5_HUMAN	mRNA target	VH3 (mRNA); Dual specificity protein phosphatase hVH3 (mRNA); Dual specificity protein phosphatase 5 (mRNA)	DUSP5	"The highest relative activity is toward ERK1. Dual specificity protein phosphatase; active with phosphotyrosine, phosphoserine and phosphothreonine residues."	EC 3.1.3.16	2G6Z	MKVTSLDGRQLRKMLRKEAAARCVVLDCRPYLAFAASNVRGSLNVNLNSVVLRRARGGAVSARYVLPDEAARARLLQEGGGGVAAVVVLDQGSRHWQKLREESAARVVLTSLLACLPAGPRVYFLKGGYETFYSEYPECCVDVKPISQEKIESERALISQCGKPVVNVSYRPAYDQGGPVEILPFLYLGSAYHASKCEFLANLHITALLNVSRRTSEACATHLHYKWIPVEDSHTADISSHFQEAIDFIDCVREKGGKVLVHCEAGISRSPTICMAYLMKTKQFRLKEAFDYIKQRRSMVSPNFGFMGQLLQYESEILPSTPNPQPPSCQGEAAGSSLIGHLQTLSPDMQGAYCTFPASVLAPVPTHSTVSELSRSPVATATSC	Literature-reported	"US patent application no. 6,867,039, Antisense modulation of dual specific phosphatase 5 expression."	0	mRNA	mRNA target	.	.	.	"Dual specificity phosphatase, catalytic domain; Rhodanese-like domain"	PF00782; PF00581	PF00782; DSPc; PF00581; Rhodanese	.	.	hsa04010:MAPK signaling pathway	R-HSA-112409:RAF-independent MAPK1/3 activation; R-HSA-5675221:Negative regulation of MAPK pathway	.	Q16690
TTK0TF2	DUSP8 messenger RNA (DUSP8 mRNA)	Q13202	DUS8_HUMAN	mRNA target	VH5 (mRNA); Dual specificity protein phosphatase hVH-5 (mRNA); Dual specificity protein phosphatase 8 (mRNA); C11orf81 (mRNA)	DUSP8	"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."	EC 3.1.3.16	4JMK	MAGDRLPRKVMDAKKLASLLRGGPGGPLVIDSRSFVEYNSWHVLSSVNICCSKLVKRRLQQGKVTIAELIQPAARSQVEATEPQDVVVYDQSTRDASVLAADSFLSILLSKLDGCFDSVAILTGGFATFSSCFPGLCEGKPAALLPMSLSQPCLPVPSVGLTRILPHLYLGSQKDVLNKDLMTQNGISYVLNASNSCPKPDFICESRFMRVPINDNYCEKLLPWLDKSIEFIDKAKLSSCQVIVHCLAGISRSATIAIAYIMKTMGMSSDDAYRFVKDRRPSISPNFNFLGQLLEYERSLKLLAALQGDPGTPSGTPEPPPSPAAGAPLPRLPPPTSESAATGNAAAREGGLSAGGEPPAPPTPPATSALQQGLRGLHLSSDRLQDTNRLKRSFSLDIKSAYAPSRRPDGPGPPDPGEAPKLCKLDSPSGAALGLSSPSPDSPDAAPEARPRPRRRPRPPAGSPARSPAHSLGLNFGDAARQTPRHGLSALSAPGLPGPGQPAGPGAWAPPLDSPGTPSPDGPWCFSPEGAQGAGGVLFAPFGRAGAPGPGGGSDLRRREAARAEPRDARTGWPEEPAPETQFKRRSCQMEFEEGMVEGRARGEELAALGKQASFSGSVEVIEVS	Literature-reported	"US patent application no. 6,482,644, Antisense modulation of dual specific phosphatase 8 expression."	0	mRNA	mRNA target	.	.	.	"Dual specificity phosphatase, catalytic domain; Rhodanese-like domain"	PF00782; PF00581	PF00782; DSPc; PF00581; Rhodanese	.	.	hsa04010:MAPK signaling pathway	R-HSA-112409:RAF-independent MAPK1/3 activation; R-HSA-5675221:Negative regulation of MAPK pathway	.	Q13202
TT1GV6C	DUSP9 messenger RNA (DUSP9 mRNA)	Q99956	DUS9_HUMAN	mRNA target	Mitogen-activated protein kinase phosphatase 4 (mRNA); MKP4 (mRNA); MKP-4 (mRNA); MAP kinase phosphatase 4 (mRNA); Dual specificity protein phosphatase 9 (mRNA)	DUSP9	Has a specificity for the ERK family. Inactivates MAP kinases.	EC 3.1.3.16	3LJ8; 2HXP	MEGLGRSCLWLRRELSPPRPRLLLLDCRSRELYESARIGGALSVALPALLLRRLRRGSLSVRALLPGPPLQPPPPAPVLLYDQGGGRRRRGEAEAEAEEWEAESVLGTLLQKLREEGYLAYYLQGGFSRFQAECPHLCETSLAGRAGSSMAPVPGPVPVVGLGSLCLGSDCSDAESEADRDSMSCGLDSEGATPPPVGLRASFPVQILPNLYLGSARDSANLESLAKLGIRYILNVTPNLPNFFEKNGDFHYKQIPISDHWSQNLSRFFPEAIEFIDEALSQNCGVLVHCLAGVSRSVTVTVAYLMQKLHLSLNDAYDLVKRKKSNISPNFNFMGQLLDFERSLRLEERHSQEQGSGGQASAASNPPSFFTTPTSDGAFELAPT	Literature-reported	"US patent application no. 6,566,133, Antisense inhibition of dual specific phosphatase 9 expression."	0	mRNA	mRNA target	.	.	.	"Dual specificity phosphatase, catalytic domain; Rhodanese-like domain"	PF00782; PF00581	PF00782; DSPc; PF00581; Rhodanese	.	.	hsa04010:MAPK signaling pathway; hsa04550:Signaling pathways regulating pluripotency of stem cells	R-HSA-112409:RAF-independent MAPK1/3 activation; R-HSA-5675221:Negative regulation of MAPK pathway	.	Q99956
TTH6MBO	dUTP pyrophosphatase (DUT)	P33316	DUT_HUMAN	Acid anhydrides hydrolase	"Deoxyuridine 5' triphosphate nucleotidohydrolase, mitochondrial; DUT"	DUT	"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}."	EC 3.6.1.23	5H4J; 4MZ6; 4MZ5; 3EHW; 3ARN	MTPLCPRPALCYHFLTSLLRSAMQNARGARQRAEAAVLSGPGPPLGRAAQHGIPRPLSSAGRLSQGCRGASTVGAAGWKGELPKAGGSPAPGPETPAISPSKRARPAEVGGMQLRFARLSEHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDDTERGSGGFGSTGKN	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	hsa00240: Pyrimidine metabolism; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa01232: Nucleotide metabolism	R-HSA-499943: Interconversion of nucleotide di- and triphosphates	MetaCyc:HS05235-MON	P33316
TTCVQYE	Dynactin-associated protein (DYNAP)	Q8N1N2	DYNAP_HUMAN	.	Full; C18orf26	DYNAP	Plays a role in the regulation of cell proliferation. Promotes activation of the AKT1 signaling pathway. Promotes phosphorylation of AKT1 at 'Ser-473'.	.	.	MVADIKGNEQIEKYSWREACDTGSSRMDRKHGKYILNVEHSENQPPITHPNDQEAHSSICWCLPSNDITSDVSPNLTGVCVNPGILAHSRCLQSESCNTQVKEYCRNDWSMWKVFLACLLACVIMTAIGVLIICLVNNKGSANSSIVIQLSTNDGECVTVKPGTPSPACPPTMTTTSTVPASTATESTTSTATAATTSTEPITVAPTDHL	Literature-reported	"A novel human dynactin-associated protein, dynAP, promotes activation of Akt, and ergosterol-related compounds induce dynAP-dependent apoptosis of ... Mol Cancer Ther. 2010 Nov;9(11):2934-42."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q8N1N2
TTSBVFO	Dual-specificity tyrosine-phosphorylation regulated kinase 1A (DYRK1A)	Q13627	DYR1A_HUMAN	Kinase	hMNB; Protein kinase minibrain homolog; MNBH; MNB; HP86; Dual specificity tyrosine-phosphorylation-regulated kinase 1A; Dual specificity YAK1-related kinase; DYRK	DYRK1A	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).	EC 2.7.12.1	6EJ4; 6EIV; 6EIS; 6EIR; 6EIQ	MHTGGETSACKPSSVRLAPSFSFHAAGLQMAGQMPHSHQYSDRRQPNISDQQVSALSYSDQIQQPLTNQVMPDIVMLQRRMPQTFRDPATAPLRKLSVDLIKTYKHINEVYYAKKKRRHQQGQGDDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTSNSVSTSPAMEQSQSSGTTSSTSSSSGGSSGTSNSGRARSDPTHQHRHSGGHFTAAVQAMDCETHSPQVRQQFPAPLGWSGTEAPTQVTVETHPVQETTFHVAPQQNALHHHHGNSSHHHHHHHHHHHHHGQQALGNRTRPRVYNSPTNSSSTQDSMEVGHSHHSMTSLSSSTTSSSTSSSSTGNQGNQAYQNRPVAANTLDFGQNGAMDVNLTVYSNPRQETGIAGHPTYQFSANTGPAHYMTEGHLTMRQGADREESPMTGVCVQQSPVASS	Patented-recorded	Dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) inhibitors: a survey of recent patent literature.Expert Opin Ther Pat. 2017 Nov;27(11):1183-1199.	15.5	EC:2.7	.	protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily.	2.7.12.1 	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	R-HSA-1538133: G0 and Early G1	.	Q13627
TTYGQ8A	Dual-specificity tyrosine-phosphorylation regulated kinase 1B (DYRK1B)	Q9Y463	DYR1B_HUMAN	Kinase	Minibrain-related kinase; MIRK; Dual specificity tyrosine-phosphorylation-regulated kinase 1B	DYRK1B	"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."	EC 2.7.12.1	.	MAVPPGHGPFSGFPGPQEHTQVLPDVRLLPRRLPLAFRDATSAPLRKLSVDLIKTYKHINEVYYAKKKRRAQQAPPQDSSNKKEKKVLNHGYDDDNHDYIVRSGERWLERYEIDSLIGKGSFGQVVKAYDHQTQELVAIKIIKNKKAFLNQAQIELRLLELMNQHDTEMKYYIVHLKRHFMFRNHLCLVFELLSYNLYDLLRNTHFRGVSLNLTRKLAQQLCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGTPYDLAIDMWSLGCILVEMHTGEPLFSGSNEVDQMNRIVEVLGIPPAAMLDQAPKARKYFERLPGGGWTLRRTKELRKDYQGPGTRRLQEVLGVQTGGPGGRRAGEPGHSPADYLRFQDLVLRMLEYEPAARISPLGALQHGFFRRTADEATNTGPAGSSASTSPAPLDTCPSSSTASSISSSGGSSGSSSDNRTYRYSNRYCGGPGPPITDCEMNSPQVPPSQPLRPWAGGDVPHKTHQAPASASSLPGTGAQLPPQPRYLGRPPSPTSPPPPELMDVSLVGGPADCSPPHPAPAPQHPAASALRTRMTGGRPPLPPPDDPATLGPHLGLRGVPQSTAASS	Patented-recorded	Dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) inhibitors: a survey of recent patent literature.Expert Opin Ther Pat. 2017 Nov;27(11):1183-1199.	15.5	EC:2.7	.	protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily.	2.7.12.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	MetaCyc:HS02690-MON	Q9Y463
TT84OS6	Dual-specificity tyrosine-phosphorylation regulated kinase 2 (DYRK2)	Q92630	DYRK2_HUMAN	Kinase	Dual specificity tyrosine-phosphorylation-regulated kinase 2	DYRK2	"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."	EC 2.7.12.1	5ZTN; 5LXD; 5LXC; 4AZF; 3KVW	MLTRKPSAAAPAAYPTGRGGDSAVRQLQASPGLGAGATRSGVGTGPPSPIALPPLRASNAAAAAHTIGGSKHTMNDHLHVGSHAHGQIQVQQLFEDNSNKRTVLTTQPNGLTTVGKTGLPVVPERQLDSIHRRQGSSTSLKSMEGMGKVKATPMTPEQAMKQYMQKLTAFEHHEIFSYPEIYFLGLNAKKRQGMTGGPNNGGYDDDQGSYVQVPHDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPRYCTVTTLSDGSVVLNGGRSRRGKLRGPPESREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWLRRRLPKPPTGEKTSVKRITESTGAITSISKLPPPSSSASKLRTNLAQMTDANGNIQQRTVLPKLVS	Patented-recorded	Dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) inhibitors: a survey of recent patent literature.Expert Opin Ther Pat. 2017 Nov;27(11):1183-1199.	15.5	EC:2.7	.	protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily.	2.7.12.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	R-HSA-6804756: Regulation of TP53 Activity through Phosphorylation	.	Q92630
TTV4EX0	Dual-specificity tyrosine-phosphorylation regulated kinase 3 (DYRK3)	O43781	DYRK3_HUMAN	Kinase	Regulatory erythroid kinase; REDK; Dual specificity tyrosine-phosphorylation-regulated kinase 3	DYRK3	"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."	EC 2.7.12.1	5Y86	MGGTARGPGRKDAGPPGAGLPPQQRRLGDGVYDTFMMIDETKCPPCSNVLCNPSEPPPPRRLNMTTEQFTGDHTQHFLDGGEMKVEQLFQEFGNRKSNTIQSDGISDSEKCSPTVSQGKSSDCLNTVKSNSSSKAPKVVPLTPEQALKQYKHHLTAYEKLEIINYPEIYFVGPNAKKRHGVIGGPNNGGYDDADGAYIHVPRDHLAYRYEVLKIIGKGSFGQVARVYDHKLRQYVALKMVRNEKRFHRQAAEEIRILEHLKKQDKTGSMNVIHMLESFTFRNHVCMAFELLSIDLYELIKKNKFQGFSVQLVRKFAQSILQSLDALHKNKIIHCDLKPENILLKHHGRSSTKVIDFGSSCFEYQKLYTYIQSRFYRAPEIILGSRYSTPIDIWSFGCILAELLTGQPLFPGEDEGDQLACMMELLGMPPPKLLEQSKRAKYFINSKGIPRYCSVTTQADGRVVLVGGRSRRGKKRGPPGSKDWGTALKGCDDYLFIEFLKRCLHWDPSARLTPAQALRHPWISKSVPRPLTTIDKVSGKRVVNPASAFQGLGSKLPPVVGIANKLKANLMSETNGSIPLCSVLPKLIS	Patented-recorded	Dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) inhibitors: a survey of recent patent literature.Expert Opin Ther Pat. 2017 Nov;27(11):1183-1199.	15.5	EC:2.7	.	protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily.	2.7.12.1 	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	.	O43781
TTCLIHJ	Dual-specificity tyrosine-phosphorylation regulated kinase 4 (DYRK4)	Q9NR20	DYRK4_HUMAN	Kinase	Dual specificity tyrosine-phosphorylation-regulated kinase 4	DYRK4	Possible non-essential role in spermiogenesis.	EC 2.7.12.1	.	MPASELKASEIPFHPSIKTQDPKAEEKSPKKQKVTLTAAEALKLFKNQLSPYEQSEILGYAELWFLGLEAKKLDTAPEKFSKTSFDDEHGFYLKVLHDHIAYRYEVLETIGKGSFGQVAKCLDHKNNELVALKIIRNKKRFHQQALMELKILEALRKKDKDNTYNVVHMKDFFYFRNHFCITFELLGINLYELMKNNNFQGFSLSIVRRFTLSVLKCLQMLSVEKIIHCDLKPENIVLYQKGQASVKVIDFGSSCYEHQKVYTYIQSRFYRSPEVILGHPYDVAIDMWSLGCITAELYTGYPLFPGENEVEQLACIMEVLGLPPAGFIQTASRRQTFFDSKGFPKNITNNRGKKRYPDSKDLTMVLKTYDTSFLDFLRRCLVWEPSLRMTPDQALKHAWIHQSRNLKPQPRPQTLRKSNSFFPSETRKDKVQGCHHSSRKADEITKETTEKTKDSPTKHVQHSGDQQDCLQHGADTVQLPQLVDAPKKSEAAVGAEVSMTSPGQSKNFSLKNTNVLPPIV	Literature-reported	"Selectivity, cocrystal structures, and neuroprotective properties of leucettines, a family of protein kinase inhibitors derived from the marine sponge alkaloid leucettamine B. J Med Chem. 2012 Nov 8;55(21):9312-30."	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9NR20
TTA7MXQ	Dysferlin (DYSF)	O75923	DYSF_HUMAN	Synaptosomal vesicle fusion pore	Fer1like protein 1; Dystrophyassociated fer1like protein; DYSF	DYSF	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}.	.	4IQH; 4IHB; 4CAI; 4CAH	MLRVFILYAENVHTPDTDISDAYCSAVFAGVKKRTKVIKNSVNPVWNEGFEWDLKGIPLDQGSELHVVVKDHETMGRNRFLGEAKVPLREVLATPSLSASFNAPLLDTKKQPTGASLVLQVSYTPLPGAVPLFPPPTPLEPSPTLPDLDVVADTGGEEDTEDQGLTGDEAEPFLDQSGGPGAPTTPRKLPSRPPPHYPGIKRKRSAPTSRKLLSDKPQDFQIRVQVIEGRQLPGVNIKPVVKVTAAGQTKRTRIHKGNSPLFNETLFFNLFDSPGELFDEPIFITVVDSRSLRTDALLGEFRMDVGTIYREPRHAYLRKWLLLSDPDDFSAGARGYLKTSLCVLGPGDEAPLERKDPSEDKEDIESNLLRPTGVALRGAHFCLKVFRAEDLPQMDDAVMDNVKQIFGFESNKKNLVDPFVEVSFAGKMLCSKILEKTANPQWNQNITLPAMFPSMCEKMRIRIIDWDRLTHNDIVATTYLSMSKISAPGGEIEEEPAGAVKPSKASDLDDYLGFLPTFGPCYINLYGSPREFTGFPDPYTELNTGKGEGVAYRGRLLLSLETKLVEHSEQKVEDLPADDILRVEKYLRRRKYSLFAAFYSATMLQDVDDAIQFEVSIGNYGNKFDMTCLPLASTTQYSRAVFDGCHYYYLPWGNVKPVVVLSSYWEDISHRIETQNQLLGIADRLEAGLEQVHLALKAQCSTEDVDSLVAQLTDELIAGCSQPLGDIHETPSATHLDQYLYQLRTHHLSQITEAALALKLGHSELPAALEQAEDWLLRLRALAEEPQNSLPDIVIWMLQGDKRVAYQRVPAHQVLFSRRGANYCGKNCGKLQTIFLKYPMEKVPGARMPVQIRVKLWFGLSVDEKEFNQFAEGKLSVFAETYENETKLALVGNWGTTGLTYPKFSDVTGKIKLPKDSFRPSAGWTWAGDWFVCPEKTLLHDMDAGHLSFVEEVFENQTRLPGGQWIYMSDNYTDVNGEKVLPKDDIECPLGWKWEDEEWSTDLNRAVDEQGWEYSITIPPERKPKHWVPAEKMYYTHRRRRWVRLRRRDLSQMEALKRHRQAEAEGEGWEYASLFGWKFHLEYRKTDAFRRRRWRRRMEPLEKTGPAAVFALEGALGGVMDDKSEDSMSVSTLSFGVNRPTISCIFDYGNRYHLRCYMYQARDLAAMDKDSFSDPYAIVSFLHQSQKTVVVKNTLNPTWDQTLIFYEIEIFGEPATVAEQPPSIVVELYDHDTYGADEFMGRCICQPSLERMPRLAWFPLTRGSQPSGELLASFELIQREKPAIHHIPGFEVQETSRILDESEDTDLPYPPPQREANIYMVPQNIKPALQRTAIEILAWGLRNMKSYQLANISSPSLVVECGGQTVQSCVIRNLRKNPNFDICTLFMEVMLPREELYCPPITVKVIDNRQFGRRPVVGQCTIRSLESFLCDPYSAESPSPQGGPDDVSLLSPGEDVLIDIDDKEPLIPIQEEEFIDWWSKFFASIGEREKCGSYLEKDFDTLKVYDTQLENVEAFEGLSDFCNTFKLYRGKTQEETEDPSVIGEFKGLFKIYPLPEDPAIPMPPRQFHQLAAQGPQECLVRIYIVRAFGLQPKDPNGKCDPYIKISIGKKSVSDQDNYIPCTLEPVFGKMFELTCTLPLEKDLKITLYDYDLLSKDEKIGETVVDLENRLLSKFGARCGLPQTYCVSGPNQWRDQLRPSQLLHLFCQQHRVKAPVYRTDRVMFQDKEYSIEEIEAGRIPNPHLGPVEERLALHVLQQQGLVPEHVESRPLYSPLQPDIEQGKLQMWVDLFPKALGRPGPPFNITPRRARRFFLRCIIWNTRDVILDDLSLTGEKMSDIYVKGWMIGFEEHKQKTDVHYRSLGGEGNFNWRFIFPFDYLPAEQVCTIAKKDAFWRLDKTESKIPARVVFQIWDNDKFSFDDFLGSLQLDLNRMPKPAKTAKKCSLDQLDDAFHPEWFVSLFEQKTVKGWWPCVAEEGEKKILAGKLEMTLEIVAESEHEERPAGQGRDEPNMNPKLEDPRRPDTSFLWFTSPYKTMKFILWRRFRWAIILFIILFILLLFLAIFIYAFPNYAAMKLVKPFS	Literature-reported	Identification of Novel Antisense-Mediated Exon Skipping Targets in DYSF for Therapeutic Treatment of Dysferlinopathy. Mol Ther Nucleic Acids. 2018 Dec 7;13:596-604.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-445355: Smooth Muscle Contraction	.	O75923
TTASI04	E2F1 messenger RNA (E2F1 mRNA)	Q01094	E2F1_HUMAN	mRNA target	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)	E2F1	"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."	.	6G0P; 5M9O; 5M9N; 2AZE; 1O9K	MALAGAPAGGPCAPALEALLGAGALRLLDSSQIVIISAAQDASAPPAPTGPAAPAAGPCDPDLLLFATPQAPRPTPSAPRPALGRPPVKRRLDLETDHQYLAESSGPARGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTTVGVGGRLEGLTQDLRQLQESEQQLDHLMNICTTQLRLLSEDTDSQRLAYVTCQDLRSIADPAEQMVMVIKAPPETQLQAVDSSENFQISLKSKQGPIDVFLCPEETVGGISPGKTPSQEVTSEEENRATDSATIVSPPPSSPPSSLTTDPSQSLLSLEQEPLLSRMGSLRAPVDEDRLSPLVAADSLLEHVREDFSGLLPEEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF	Literature-reported	"US patent application no. 6,187,587, Antisense inhibition of e2f transcription factor 1 expression."	0	mRNA	mRNA target	.	.	.	E2F transcription factor CC-MB domain; E2F/DP family winged-helix DNA-binding domain	PF16421; PF02319	PF16421; E2F_CC-MB; PF02319; E2F_TDP	.	.	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	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	.	Q01094
TTVJDNB	E2F transcription factor 1 (E2F1)	Q01094	E2F1_HUMAN	.	pRB-binding protein E2F-1; Transcription factor E2F1; Retinoblastoma-binding protein 3; Retinoblastoma-associated protein 1; RBBP3; RBBP-3; RBAP-1; PBR3; E2F-1	E2F1	"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."	.	6G0P; 5M9O; 5M9N; 2AZE; 1O9K	MALAGAPAGGPCAPALEALLGAGALRLLDSSQIVIISAAQDASAPPAPTGPAAPAAGPCDPDLLLFATPQAPRPTPSAPRPALGRPPVKRRLDLETDHQYLAESSGPARGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTTVGVGGRLEGLTQDLRQLQESEQQLDHLMNICTTQLRLLSEDTDSQRLAYVTCQDLRSIADPAEQMVMVIKAPPETQLQAVDSSENFQISLKSKQGPIDVFLCPEETVGGISPGKTPSQEVTSEEENRATDSATIVSPPPSSPPSSLTTDPSQSLLSLEQEPLLSRMGSLRAPVDEDRLSPLVAADSLLEHVREDFSGLLPEEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF	Clinical trial	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800025396)"	17	.	.	E2F/DP family.	.	.	E2F transcription factor CC-MB domain; E2F/DP family winged-helix DNA-binding domain	PF16421; PF02319	PF16421; E2F_CC-MB; PF02319; E2F_TDP	.	.	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	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	.	Q01094
TT5FYX0	Transcription factor E2F2 (E2F2)	Q14209	E2F2_HUMAN	.	E2F-2	E2F2	"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."	.	1N4M	MLQGPRALASAAGQTPKVVPAMSPTELWPSGLSSPQLCPATATYYTPLYPQTAPPAAAPGTCLDATPHGPEGQVVRCLPAGRLPAKRKLDLEGIGRPVVPEFPTPKGKCIRVDGLPSPKTPKSPGEKTRYDTSLGLLTKKFIYLLSESEDGVLDLNWAAEVLDVQKRRIYDITNVLEGIQLIRKKAKNNIQWVGRGMFEDPTRPGKQQQLGQELKELMNTEQALDQLIQSCSLSFKHLTEDKANKRLAYVTYQDIRAVGNFKEQTVIAVKAPPQTRLEVPDRTEDNLQIYLKSTQGPIEVYLCPEEVQEPDSPSEEPLPSTSTLCPSPDSAQPSSSTDPSIMEPTASSVPAPAPTPQQAPPPPSLVPLEATDSLLELPHPLLQQTEDQFLSPTLACSSPLISFSPSLDQDDYLWGLEAGEGISDLFDSYDLGDLLIN	Literature-reported	Inhibition of cell proliferation and induction of apoptosis by novel tetravalent peptides inhibiting DNA binding of E2F. Oncogene. 2003 Aug 7;22(32):4943-52.	.	.	.	E2F/DP family.	.	.	E2F transcription factor CC-MB domain; E2F/DP family winged-helix DNA-binding domain	PF16421; PF02319	PF16421; E2F_CC-MB; PF02319; E2F_TDP	.	.	hsa01522: Endocrine resistance; hsa04110: Cell cycle; hsa04218: Cellular senescence; hsa04934: Cushing syndrome; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05163: Human cytomegalovirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05169: Epstein-Barr virus 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; hsa05224: Breast cancer; hsa05225: Hepatocellular carcinoma; hsa05226: Gastric cancer	"R-HSA-2559580: Oxidative Stress Induced Senescence; R-HSA-2559585: Oncogene Induced Senescence; R-HSA-69231: Cyclin D associated events in G1; R-HSA-9661069: Defective binding of RB1 mutants to E2F1,(E2F2, E2F3)"	.	Q14209
TTWIJYH	E2F3 messenger RNA (E2F3 mRNA)	O00716	E2F3_HUMAN	mRNA target	Transcription factor E2F3 (mRNA); KIAA0075 (mRNA); E2F-3 (mRNA)	E2F3	"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."	.	.	MRKGIQPALEQYLVTAGGGEGAAVVAAAAAASMDKRALLASPGFAAAAAAAAAPGAYIQILTTNTSTTSCSSSLQSGAVAAGPLLPSAPGAEQTAGSLLYTTPHGPSSRAGLLQQPPALGRGGSGGGGGPPAKRRLELGESGHQYLSDGLKTPKGKGRAALRSPDSPKTPKSPSEKTRYDTSLGLLTKKFIQLLSQSPDGVLDLNKAAEVLKVQKRRIYDITNVLEGIHLIKKKSKNNVQWMGCSLSEDGGMLAQCQGLSKEVTELSQEEKKLDELIQSCTLDLKLLTEDSENQRLAYVTYQDIRKISGLKDQTVIVVKAPPETRLEVPDSIESLQIHLASTQGPIEVYLCPEETETHSPMKTNNQDHNGNIPKPASKDLASTNSGHSDCSVSMGNLSPLASPANLLQQTEDQIPSNLEGPFVNLLPPLLQEDYLLSLGEEEGISDLFDAYDLEKLPLVEDFMCS	Literature-reported	"US patent application no. 6,165,791, Antisense inhibition of E2F transcription factor 3 expression."	0	mRNA	mRNA target	.	.	.	E2F transcription factor CC-MB domain; E2F/DP family winged-helix DNA-binding domain	PF16421; PF02319	PF16421; E2F_CC-MB; PF02319; E2F_TDP	.	.	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	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	.	O00716
TTJF68X	Interleukin-35 (IL35)	Q14213	IL27B_HUMAN	Cytokine: interleukin	Interleukin-27 subunit beta; IL27B; IL-27B; IL-27 subunit beta; Epstein-Barr virus-induced gene 3 protein; EBV-induced gene 3 protein	EBI3	"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."	.	.	MTPQLLLALVLWASCPPCSGRKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSFIATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVLNVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQVQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSFILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK	Literature-reported	Accumulation of EBI3 induced by virulent Mycobacterium tuberculosis inhibits apoptosis in murine macrophages. Pathog Dis. 2019 Feb 1;77(1). pii: ftz007.	.	Cytokine	.	type I cytokine receptor family. Type 3 subfamily.	.	.	Fibronectin type III domain	PF00041	PF00041; fn3	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04659: Th17 cell differentiation	R-HSA-8984722: Interleukin-35 Signalling; R-HSA-9020956: Interleukin-27 signaling	.	Q14213
TT4VQZX	Cholestenol delta-isomerase (EBP)	Q15125	EBP_HUMAN	Intramolecular oxidoreductases	"Emopamilbinding protein; EBP; Delta(8)Delta(7) sterol isomerase; D8D7 sterol isomerase; 3betahydroxysteroidDelta(8),Delta(7)isomerase"	EBP	Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers.	EC 5.3.3.5	.	MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIYGDVLYFLTEHRDGFQHGELGHPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN	Clinical trial	Both the immunosuppressant SR31747 and the antiestrogen tamoxifen bind to an emopamil-insensitive site of mammalian Delta8-Delta7 sterol isomerase. J Pharmacol Exp Ther. 1998 Jun;285(3):1296-302.	21	.	.	.	.	.	.	.	.	.	.	hsa00100:Steroid biosynthesis; hsa01100:Metabolic pathways	R-HSA-6807047: Cholesterol biosynthesis via desmosterol; R-HSA-6807062: Cholesterol biosynthesis via lathosterol	MetaCyc:ENSG00000147155-MON	Q15125
TT1JL7D	Epstein-Barr virus Envelope glycoprotein gp340 (EBV BLLF1)	P68344	VGP3_EBVP3	.	Membrane antigen; MA; Envelope glycoprotein GP340	EBV BLLF1	Responsible for EBV binding to the CR2 receptor on human B-cells.	.	.	MEAALLVCQYTIQSLIQLTRDDPGFFNVEILEFPFYPACNVCTADVNATINFDVGGKKHKLNLDFGLLTPHTKAVYQPRGAFGGSENATNLFLLELLGAGELALTMRSKKLPINITTGEEQQVSLESVDVYFQDVFGTMWCHHAEMQNPVYLIPETVPYIKWDNCNSTNITAVVRAQGLDVTLPLSLPTSAQDSNFSVKTEMLGNEIDIECIMEDGEISQVLPGDNKFNITCSGYESHVPSGGILTSTSPVATPIPGTGYAYSLRLTPRPVSRFLGNNSILYVFYSGNGPKASGGDYCIQSNIVFSDEIPASQDMPTNTTDITYVGDNATYSVPMVTSEDANSPNVTVTAFWAWPNNTETDFKCKWTLTSGTPSGCENISGAFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRFSNLSMLVLQWASLAVLTLLLLLVMADCAFRRNLSTSHTYTTPPYDDAETYV	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT0BI4Q	Epstein-Barr virus Latent membrane protein 1 (EBV LMP1)	P0C741	LMP1_EBVG	.	Protein p63; P63; Latent membrane protein 1; LMP1; LMP-1; BNLF1	EBV LMP1	"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."	.	.	MERDLERGPPGPPRPPLGPPLSSSIGLALLLLLLALLFWLYIVLSNWTGGALLVLYSFALMLIIIILIIFIFRRDLLCPLGGLGLLLLMVTLLLIALWNLHGQALYLGIVLFIFGCLLVLGLWIYFLEILWRLGATIWQLLAFILAFFLAIILLIIALYLQQNWWTLLVDLLWLLLFMAILIWMYFHGPRHTDEHHHDDSLPHPQQATDDSSHESDSNSNEGRHHLLVSGAGDGPPLCSQNLGAPGGGPDNGPQDPDNTDDNGPQDPDNTDDNGNTDDNGPQDPDNTDDNGPHDPLPHNPSDSAGNDGGPPNLTEEVENKGGDRGPPSMTDGGGGDPHLPTLLLGTSGSGGDDDDPHGPVQLSYYD	Clinical trial	ClinicalTrials.gov (NCT02980315) A New EBV Related Technologies of T Cells in Treating Malignant Tumors and Clinical Application	19	.	.	.	.	.	Herpesvirus latent membrane protein 1 (LMP1)	PF05297	PF05297; Herpes_LMP1	.	.	.	.	.	.
TTBK351	Epstein-Barr virus Latent membrane protein 2 (EBV LMP2)	P13285	LMP2_EBVB9	Herpesviridae LMP-2	Terminal protein; Latent membrane protein 2	EBV LMP2	Isoform LMP2B may be a negative regulator of isoform LMP2A.	.	5GSD; 5GRD; 3REW; 3BVN; 2JO9	MGSLEMVPMGAGPPSPGGDPDGYDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDPYWGNGDRHSDYQPLGTQDQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSMNPVCLPVIVAPYLFWLAAIAASCFTASVSTVVTATGLALSLLLLAAVASSYAAAQRKLLTPVTVLTAVVTFFAICLTWRIEDPPFNSLLFALLAAAGGLQGIYVLVMLVLLILAYRRRWRRLTVCGGIMFLACVLVLIVDAVLQLSPLLGAVTVVSMTLLLLAFVLWLSSPGGLGTLGAALLTLAAALALLASLILGTLNLTTMFLLMLLWTLVVLLICSSCSSCPLSKILLARLFLYALALLLLASALIAGGSILQTNFKSLSSTEFIPNLFCMLLLIVAGILFILAILTEWGSGNRTYGPVFMCLGGLLTMVAGAVWLTVMSNTLLSAWILTAGFLIFLIGFALFGVIRCCRYCCYYCLTLESEERPPTPYRNTV	Clinical trial	In vivo expansion of LMP 1- and 2-specific T-cells in a patient who received donor-derived EBV-specific T-cells after allogeneic stem cell transplantation. Leuk Lymphoma. 2006 May;47(5):837-42.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOJCQV	Epstein-Barr virus Latent membrane protein 2A (EBV LMP2A)	Q69133	Q69133_EBVG	.	Latent membrane protein 2A	EBV LMP2A	A virally encoded membrane protein that is expressed in EBV latent infection and in most of the tumors associated with EBV infection.	.	.	PMGAGPPSPGGDPDGDDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDLDWGNGDRHSDYQPLGNQDPSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSMNPVC	Literature-reported	Inhibition of host kinase activity altered by the LMP2A signalosome-a therapeutic target for Epstein-Barr virus latency and associated disease. Antiviral Res. 2002 Dec;56(3):219-31.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT0VZF7	Epstein-Barr virus Nuclear antigen gene (EBV NA)	Q69128	Q69128_EBVG	.	EBV Uncharacterized protein	EBV NA	"A multifunctional, dimeric viral protein associated with EpsteinBarr virus (EBV). The only EBV protein found in all EBV-related malignancies."	.	.	MSDEGPGTGPGNGLGEKGDTSGPEGSGGSGPQRRGGDNHGRGRGRGRGRGGGRPGAPG	Literature-reported	Epstein-barr virus nuclear antigen 1: from immunologically invisible to a promising T cell target. J Exp Med. 2004 May 17;199(10):1301-4.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQ9RYT	Endothelin-converting enzyme 1 (ECE1)	P42892	ECE1_HUMAN	Peptidase	ECE-1	ECE1	Converts big endothelin-1 to endothelin-1.	EC 3.4.24.71	3DWB	MRGVWPPPVSALLSALGMSTYKRATLDEEDLVDSLSEGDAYPNGLQVNFHSPRSGQRCWAARTQVEKRLVVLVVLLAAGLVACLAALGIQYQTRSPSVCLSEACVSVTSSILSSMDPTVDPCHDFFSYACGGWIKANPVPDGHSRWGTFSNLWEHNQAIIKHLLENSTASVSEAERKAQVYYRACMNETRIEELRAKPLMELIERLGGWNITGPWAKDNFQDTLQVVTAHYRTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGDEEAIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVVYDKEYLEQISTLINTTDRCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEVMYGTKKTCLPRWKFCVSDTENNLGFALGPMFVKATFAEDSKSIATEIILEIKKAFEESLSTLKWMDEETRKSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPKALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKRQTECMVEQYSNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEHSLPTLGLTNNQLFFLGFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSLSNSKEFSEHFRCPPGSPMNPPHKCEVW	Literature-reported	Phosphinic tripeptides as dual angiotensin-converting enzyme C-domain and endothelin-converting enzyme-1 inhibitors. J Med Chem. 2010 Jan 14;53(1):208-20.	2	EC:3.4	.	peptidase M13 family.	3.4.24.71	Acting on peptide bonds (peptidases)	Peptidase family M13; Peptidase family M13	PF01431; PF05649	PF01431; Peptidase_M13; PF05649; Peptidase_M13_N	.	.	.	R-HSA-375276: Peptide ligand-binding receptors	.	P42892
TT5U914	Endothelin-converting enzyme 2 (ECE2)	O60344	ECE2_HUMAN	.	UNQ403/PRO740; KIAA0604; ECE-2	ECE2	"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."	EC 3.4.24.71	.	MNVALQELGAGSNMVEYKRATLRDEDAPETPVEGGASPDAMEVGKGASPFSPGPSPGMTPGTPRSSGLFWRVTCPHLRSISGLCSRTMVGFQKGTRQLLGSRTQLELVLAGASLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAEQKTQRFYLSCLQVERIEELGAQPLRDLIEKIGGWNITGPWDQDNFMEVLKAVAGTYRATPFFTVYISADSKSSNSNVIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMEELGMLLGGRPTSTREQMQQVLELEIQLANITVPQDQRRDEEKIYHKMSISELQALAPSMDWLEFLSFLLSPLELSDSEPVVVYGMDYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDRRFESAQEKLLETLYGTKKSCVPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMISEIRTAFEEALGQLVWMDEKTRQAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEISEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYARNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLAAFRNHTACMEEQYNQYQVNGERLNGRQTLGENIADNGGLKAAYNAYKAWLRKHGEEQQLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW	Literature-reported	Homology modeling and site-directed mutagenesis to identify selective inhibitors of endothelin-converting enzyme-2. J Med Chem. 2008 Jun 26;51(12):3378-87.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P0DPD6
TTJR60Z	Endothelin-1 (EDN1)	P05305	EDN1_HUMAN	Endothelin/sarafotoxin	Preproendothelin-1; PPET1	EDN1	Endothelins are endothelium-derived vasoconstrictor peptides.	.	6DK5; 5GLH; 1V6R; 1T7H; 1EDP	MDYLLMIFSLLFVACQGAPETAVLGAELSAVGENGGEKPTPSPPWRLRRSKRCSCSSLMDKECVYFCHLDIIWVNTPEHVVPYGLGSPRSKRALENLLPTKATDRENRCQCASQKDKKCWNFCQAGKELRAEDIMEKDWNNHKKGKDCSKLGKKCIYQQLVRGRKIRRSSEEHLRQTRSETMRNSVKSSFHDPKLKGKPSRERYVTHNRAHW	Literature-reported	Predictive value of biomarkers in patients with heart failure. Curr Med Chem. 2012;19(16):2534-47.	.	Endothelin/sarafotoxin	Endothelin family	endothelin/sarafotoxin family.	.	.	Endothelin family	PF00322	PF00322; Endothelin	.	.	hsa04024: cAMP signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04080: Neuroactive ligand-receptor interaction; hsa04270: Vascular smooth muscle contraction; hsa04668: TNF signaling pathway; hsa04916: Melanogenesis; hsa04924: Renin secretion; hsa04926: Relaxin signaling pathway; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa05200: Pathways in cancer; hsa05410: Hypertrophic cardiomyopathy; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-416476: G alpha (q) signalling events	.	P05305
TTMR0OP	Endothelin (EDN)	P20800	EDN2_HUMAN	Endothelin/sarafotoxin	Preproendothelin-2; PPET2; Endothelin-2; ET-2	EDN2	Endothelins are endothelium-derived vasoconstrictor peptides.	.	.	MVSVPTTWCSVALALLVALHEGKGQAAATLEQPASSSHAQGTHLRLRRCSCSSWLDKECVYFCHLDIIWVNTPEQTAPYGLGNPPRRRRRSLPRRCQCSSARDPACATFCLRRPWTEAGAVPSRKSPADVFQTGKTGATTGELLQRLRDISTVKSLFAKRQQEAMREPRSTHSRWRKR	Literature-reported	Endothelin as a therapeutic target in the treatment of cardiovascular disease. Heart Dis. 2001 May-Jun;3(3):176-88.	.	Endothelin/sarafotoxin	.	endothelin/sarafotoxin family.	.	.	Endothelin family	PF00322	PF00322; Endothelin	.	.	hsa04024: cAMP signaling pathway; hsa04080: Neuroactive ligand-receptor interaction; hsa04270: Vascular smooth muscle contraction; hsa04924: Renin secretion	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-416476: G alpha (q) signalling events	.	P20800
TTKRD0G	Endothelin A receptor (EDNRA)	P25101	EDNRA_HUMAN	GPCR rhodopsin	HET-AR; Endothelin-1 receptor; Endothelin receptor type A; Endothelin receptor A; ETRA; ETA-R; ETA receptor; ETA; ET-A	EDNRA	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.	.	.	METLCLRASFWLALVGCVISDNPERYSTNLSNHVDDFTTFRGTELSFLVTTHQPTNLVLPSNGSMHNYCPQQTKITSAFKYINTVISCTIFIVGMVGNATLLRIIYQNKCMRNGPNALIASLALGDLIYVVIDLPINVFKLLAGRWPFDHNDFGVFLCKLFPFLQKSSVGITVLNLCALSVDRYRAVASWSRVQGIGIPLVTAIEIVSIWILSFILAIPEAIGFVMVPFEYRGEQHKTCMLNATSKFMEFYQDVKDWWLFGFYFCMPLVCTAIFYTLMTCEMLNRRNGSLRIALSEHLKQRREVAKTVFCLVVIFALCWFPLHLSRILKKTVYNEMDKNRCELLSFLLLMDYIGINLATMNSCINPIALYFVSKKFKNCFQSCLCCCCYQSKSLMTSVPMNGTSIQWKNHDQNNHNTDRSSHKDSMN	Successful	"Clinical pipeline report, company report or official report of GlaxoSmithKline (2009)."	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family. Endothelin receptor subfamily. EDNRA sub-subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	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	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events	.	P25101
TT3ZTGU	Endothelin B receptor (EDNRB)	P24530	EDNRB_HUMAN	GPCR rhodopsin	Endothelin receptor type B; Endothelin receptor Non-selective type; Endothelin receptor B; ETRB; ET-BR; ET-B	EDNRB	"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."	.	6IGL; 6IGK; 5XPR; 5X93; 5GLI	MQPPPSLCGRALVALVLACGLSRIWGEERGFPPDRATPLLQTAEIMTPPTKTLWPKGSNASLARSLAPAEVPKGDRTAGSPPRTISPPPCQGPIEIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIVIDIPINVYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAIGFDIITMDYKGSYLRICLLHPVQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTLYNQNDPNRCELLSFLLVLDYIGINMASLNSCINPIALYLVSKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS	Successful	Radium 223 dichloride for prostate cancer treatment. Drug Des Devel Ther. 2017 Sep 6;11:2643-2651.	34	PF00001	.	G-protein coupled receptor 1 family. Endothelin receptor subfamily. EDNRB sub-subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04020:Calcium signaling pathway; hsa04022:cGMP-PKG signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04916:Melanogenesis; hsa05200:Pathways in cancer	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events	.	P24530
TTFNJ4R	Embryonic ectoderm development protein (EED)	O75530	EED_HUMAN	.	hEED; WD protein associating with integrin cytoplasmic tails 1; WAIT-1	EED	"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."	.	6C24; 6C23; 6B3W; 5WUK; 5WP3	MSEREVSTAPAGTDMPAAKKQKLSSDENSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	19	.	.	.	.	.	.	.	.	.	.	.	R-HSA-212300: PRC2 methylates histones and DNA; R-HSA-2559580: Oxidative Stress Induced Senescence; R-HSA-3214841: PKMTs methylate histone lysines; R-HSA-5617472: Activation of anterior HOX genes in hindbrain development during early embryogenesis; R-HSA-8943724: Regulation of PTEN gene transcription; R-HSA-8953750: Transcriptional Regulation by E2F6; R-HSA-9609690: HCMV Early Events; R-HSA-9710421: Defective pyroptosis	.	O75530
TT8R0BZ	Elongation factor 1A (EF1A)	P68104; Q05639	EF1A1_HUMAN; EF1A2_HUMAN	.	eEF1A; Eukaryotic elongation factor 1 A; Elongation factor 1-alpha; Elongation factor; EF-1-alpha	EEF1A1	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.	.	.	MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK	Literature-reported	Targeting of eEF1A with Amaryllidaceae isocarbostyrils as a strategy to combat melanomas. FASEB J. 2010 Nov;24(11):4575-84.	0	.	.	.	.	.	.	.	.	.	.	hsa03013: Nucleocytoplasmic transport; hsa05134: Legionellosis; hsa05140: Leishmaniasis	R-HSA-156842: Eukaryotic Translation Elongation; R-HSA-156902: Peptide chain elongation; R-HSA-3371511: HSF1 activation; R-HSA-6798695: Neutrophil degranulation; R-HSA-8876725: Protein methylation; R-HSA-9613829: Chaperone Mediated Autophagy	.	P68104
TT1QFLA	Eukaryotic elongation factor 2 kinase (eEF-2K)	O00418	EF2K_HUMAN	Kinase	eEF-2K; eEF-2 kinase; Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase	EEF2K	"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."	EC 2.7.11.20	5KS5; 5J8H	MADEDLIFRLEGVDGGQSPRAGHDGDSDGDSDDEEGYFICPITDDPSSNQNVNSKVNKYYSNLTKSERYSSSGSPANSFHFKEAWKHAIQKAKHMPDPWAEFHLEDIATERATRHRYNAVTGEWLDDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRDVYFEDVRLQMEAKLWGEEYNRHKPPKQVDIMQMCIIELKDRPGKPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTETGTDFGDGNLGVRGMALFFYSHACNRICESMGLAPFDLSPRERDAVNQNTKLLQSAKTILRGTEEKCGSPQVRTLSGSRPPLLRPLSENSGDENMSDVTFDSLPSSPSSATPHSQKLDHLHWPVFSDLDNMASRDHDHLDNHRESENSGDSGYPSEKRGELDDPEPREHGHSYSNRKYESDEDSLGSSGRVCVEKWNLLNSSRLHLPRASAVALEVQRLNALDLEKKIGKSILGKVHLAMVRYHEGGRFCEKGEEWDQESAVFHLEHAANLGELEAIVGLGLMYSQLPHHILADVSLKETEENKTKGFDYLLKAAEAGDRQSMILVARAFDSGQNLSPDRCQDWLEALHWYNTALEMTDCDEGGEYDGMQDEPRYMMLAREAEMLFTGGYGLEKDPQRSGDLYTQAAEAAMEAMKGRLANQYYQKAEEAWAQMEE	Successful	Inhibition of eEF-2 kinase sensitizes human nasopharyngeal carcinoma cells to lapatinib-induced apoptosis through the Src and Erk pathways.BMC Cancer. 2016 Oct 19;16(1):813.	34	.	.	.	.	.	.	.	.	.	.	hsa04152:AMPK signaling pathway; hsa04921:Oxytocin signaling pathway	R-HSA-166208: mTORC1-mediated signalling	.	O00418
TTED8JB	Epidermal growth factor (EGF)	P01133	EGF_HUMAN	Growth factor	Proepidermal growth factor; Pro-epidermal growth factor	EGF	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.	.	3NJP; 2KV4; 1P9J; 1NQL; 1JL9	MLLTLIILLPVVSKFSFVSLSAPQHWSCPEGTLAGNGNSTCVGPAPFLIFSHGNSIFRIDTEGTNYEQLVVDAGVSVIMDFHYNEKRIYWVDLERQLLQRVFLNGSRQERVCNIEKNVSGMAINWINEEVIWSNQQEGIITVTDMKGNNSHILLSALKYPANVAVDPVERFIFWSSEVAGSLYRADLDGVGVKALLETSEKITAVSLDVLDKRLFWIQYNREGSNSLICSCDYDGGSVHISKHPTQHNLFAMSLFGDRIFYSTWKMKTIWIANKHTGKDMVRINLHSSFVPLGELKVVHPLAQPKAEDDTWEPEQKLCKLRKGNCSSTVCGQDLQSHLCMCAEGYALSRDRKYCEDVNECAFWNHGCTLGCKNTPGSYYCTCPVGFVLLPDGKRCHQLVSCPRNVSECSHDCVLTSEGPLCFCPEGSVLERDGKTCSGCSSPDNGGCSQLCVPLSPVSWECDCFPGYDLQLDEKSCAASGPQPFLLFANSQDIRHMHFDGTDYGTLLSQQMGMVYALDHDPVENKIYFAHTALKWIERANMDGSQRERLIEEGVDVPEGLAVDWIGRRFYWTDRGKSLIGRSDLNGKRSKIITKENISQPRGIAVHPMAKRLFWTDTGINPRIESSSLQGLGRLVIASSDLIWPSGITIDFLTDKLYWCDAKQSVIEMANLDGSKRRRLTQNDVGHPFAVAVFEDYVWFSDWAMPSVMRVNKRTGKDRVRLQGSMLKPSSLVVVHPLAKPGADPCLYQNGGCEHICKKRLGTAWCSCREGFMKASDGKTCLALDGHQLLAGGEVDLKNQVTPLDILSKTRVSEDNITESQHMLVAEIMVSDQDDCAPVGCSMYARCISEGEDATCQCLKGFAGDGKLCSDIDECEMGVPVCPPASSKCINTEGGYVCRCSEGYQGDGIHCLDIDECQLGEHSCGENASCTNTEGGYTCMCAGRLSEPGLICPDSTPPPHLREDDHHYSVRNSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELRHAGHGQQQKVIVVAVCVVVLVMLLLLSLWGAHYYRTQKLLSKNPKNPYEESSRDVRSRRPADTEDGMSSCPQPWFVVIKEHQDLKNGGQPVAGEDGQAADGSMQPTSWRQEPQLCGMGTEQGCWIPVSSDKGSCPQVMERSFHMPSYGTQTLEGGVEKPHSLLSANPLWQQRALDPPHQMELTQ	Successful	"Repurposing of the epidermal growth factor. Journal of Commercial Biotechnology (2011) 17, 45-52."	34	.	.	.	.	.	EGF-like domain; Calcium-binding EGF domain; Low-density lipoprotein receptor repeat class B	PF00008; PF07645; PF00058	PF00008; EGF; PF07645; EGF_CA; PF00058; Ldl_recept_b	.	.	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	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	.	P01133
TTXJGAR	Epidermal growth factor-like protein 6 (EGFL6)	Q8IUX8	EGFL6_HUMAN	Growth factor	MAM and EGF domains-containing gene protein; EGFL6; EGF-like protein 6	EGFL6	May bind integrin alpha-8/beta-1 and play a role in hair follicle morphogenesis. Promotes matrix assembly.	.	.	MPLPWSLALPLLLSWVAGGFGNAASARHHGLLASARQPGVCHYGTKLACCYGWRRNSKGVCEATCEPGCKFGECVGPNKCRCFPGYTGKTCSQDVNECGMKPRPCQHRCVNTHGSYKCFCLSGHMLMPDATCVNSRTCAMINCQYSCEDTEEGPQCLCPSSGLRLAPNGRDCLDIDECASGKVICPYNRRCVNTFGSYYCKCHIGFELQYISGRYDCIDINECTMDSHTCSHHANCFNTQGSFKCKCKQGYKGNGLRCSAIPENSVKEVLRAPGTIKDRIKKLLAHKNSMKKKAKIKNVTPEPTRTPTPKVNLQPFNYEEIVSRGGNSHGGKKGNEEKMKEGLEDEKREEKALKNDIEERSLRGDVFFPKVNEAGEFGLILVQRKALTSKLEHKDLNISVDCSFNHGICDWKQDREDDFDWNPADRDNAIGFYMAVPALAGHKKDIGRLKLLLPDLQPQSNFCLLFDYRLAGDKVGKLRVFVKNSNNALAWEKTTSEDEKWKTGKIQLYQGTDATKSIIFEAERGKGKTGEIAVDGVLLVSGLCPDSLLSVDD	Literature-reported	"EGFL6 Regulates the Asymmetric Division, Maintenance, and Metastasis of ALDH+ Ovarian Cancer Cells. Cancer Res. 2016 Nov 1;76(21):6396-6409."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q8IUX8
TT7WD0H	Epidermal growth factor-like protein 7 (EGFL7)	Q9UHF1	EGFL7_HUMAN	Growth factor	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	EGFL7	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.	.	.	MRGSQEVLLMWLLVLAVGGTEHAYRPGRRVCAVRAHGDPVSESFVQRVYQPFLTTCDGHRACSTYRTIYRTAYRRSPGLAPARPRYACCPGWKRTSGLPGACGAAICQPPCRNGGSCVQPGRCRCPAGWRGDTCQSDVDECSARRGGCPQRCVNTAGSYWCQCWEGHSLSADGTLCVPKGGPPRVAPNPTGVDSAMKEEVQRLQSRVDLLEEKLQLVLAPLHSLASQALEHGLPDPGSLLVHSFQQLGRIDSLSEQISFLEEQLGSCSCKKDS	Clinical trial	"A first-in-human phase Ia open-label dose-escalation study of the safety, pharmacokinetics (PK), and pharmacodynamics (PD) of the humanized monoclonal antibody (huMAb) anti-EGFL7 (MEGF0444A) administered intravenously in patients with advanced solid tumors. J Clin Oncol (Meeting Abstracts) May 2011 vol.29 no.15_suppl 2614."	21	Growth factor	Growth factor	.	.	.	EGF-like domain; Calcium-binding EGF domain; EMI domain	PF07974; PF07645; PF07546	PF07974; EGF_2; PF07645; EGF_CA; PF07546; EMI	.	.	.	.	.	Q9UHF1
TTGKNB4	Epidermal growth factor receptor (EGFR)	P00533	EGFR_HUMAN	Kinase	Receptor tyrosine-protein kinase erbB-1; Proto-oncogene c-ErbB-1; HER1; ERBB1; ERBB	EGFR	"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)."	EC 2.7.10.1	6D8E; 6B3S; 6ARU; 5ZWJ; 5YU9	MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA	Successful	Molecular inhibition of angiogenesis and metastatic potential in human squamous cell carcinomas after epidermal growth factor receptor blockade. Mol Cancer Ther. 2002 May;1(7):507-14.	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Furin-like cysteine rich region; Growth factor receptor domain IV; Protein tyrosine kinase; Receptor L domain	PF00757; PF14843; PF07714; PF01030	PF00757; Furin-like; PF14843; GF_recep_IV; PF07714; Pkinase_Tyr; PF01030; Recep_L_domain	.	.	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	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	.	P00533
TTG96HZ	EGFR messenger RNA (EGFR mRNA)	P00533	EGFR_HUMAN	mRNA target	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)	EGFR	"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."	EC 2.7.10.1	6D8E; 6B3S; 6ARU; 5ZWJ; 5YU9	MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA	Clinical trial	Antitumor Effects of EGFR Antisense Guanidine-Based Peptide Nucleic Acids in Cancer Models. ACS Chem Biol. 2013 February 15; 8(2): 345-352.	19	mRNA	mRNA target	.	.	.	Furin-like cysteine rich region; Growth factor receptor domain IV; Protein tyrosine kinase; Receptor L domain	PF00757; PF14843; PF07714; PF01030	PF00757; Furin-like; PF14843; GF_recep_IV; PF07714; Pkinase_Tyr; PF01030; Recep_L_domain	.	.	"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; hsa04020: Calcium signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04068: FoxO signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04144: Endocytosis; hsa04151: PI3K-Akt signaling pathway; hsa04510: Focal adhesion; hsa04520: Adherens junction; hsa04540: Gap junction; hsa04630: JAK-STAT signaling pathway; hsa04810: Regulation of actin cytoskeleton; hsa04912: GnRH signaling pathway; hsa04915: Estrogen signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04926: Relaxin signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04934: Cushing syndrome; hsa05120: Epithelial cell signaling in Helicobacter pylori infection; hsa05131: Shigellosis; hsa05160: Hepatitis C; hsa05163: Human cytomegalovirus infection; hsa05165: Human papillomavirus infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05206: MicroRNAs in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05210: Colorectal cancer; hsa05212: Pancreatic cancer; hsa05213: Endometrial cancer; hsa05214: Glioma; hsa05215: Prostate cancer; hsa05218: Melanoma; hsa05219: Bladder cancer; 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"	"R-HSA-1227986: Signaling by ERBB2; R-HSA-1236382: Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-1236394: Signaling by ERBB4; 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-177929: Signaling by EGFR; 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-212718: EGFR interacts with phospholipase C-gamma; R-HSA-2179392: EGFR Transactivation by Gastrin; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-445144: Signal transduction by L1; R-HSA-5637810: Constitutive Signaling by EGFRvIII; R-HSA-5638303: Inhibition of Signaling by Overexpressed EGFR; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6785631: ERBB2 Regulates Cell Motility; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-8847993: ERBB2 Activates PTK6 Signaling; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis; R-HSA-8857538: PTK6 promotes HIF1A stabilization; R-HSA-8863795: Downregulation of ERBB2 signaling; R-HSA-8866910: TFAP2 (AP-2) family regulates transcription of growth factors and their receptors; R-HSA-9009391: Extra-nuclear estrogen signaling; R-HSA-9013507: NOTCH3 Activation and Transmission of Signal to the Nucleus; R-HSA-9609690: HCMV Early Events; R-HSA-9634638: Estrogen-dependent nuclear events downstream of ESR-membrane signaling; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665348: Signaling by ERBB2 ECD mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants"	.	P00533
TT2M7YX	EGFR Exon20ins mutant (EGFR Exon20ins)	P00533	EGFR_HUMAN	.	.	EGFR	.	.	.	MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA	Clinical trial	Mobocertinib (TAK-788): A Targeted Inhibitor of EGFR Exon 20 Insertion Mutants in Non-Small Cell Lung Cancer. Cancer Discov. 2021 Feb 25;candisc.1683.2020.	.	.	.	.	.	.	.	.	.	.	.	"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; hsa04020: Calcium signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04068: FoxO signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04144: Endocytosis; hsa04151: PI3K-Akt signaling pathway; hsa04510: Focal adhesion; hsa04520: Adherens junction; hsa04540: Gap junction; hsa04630: JAK-STAT signaling pathway; hsa04810: Regulation of actin cytoskeleton; hsa04912: GnRH signaling pathway; hsa04915: Estrogen signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04926: Relaxin signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04934: Cushing syndrome; hsa05120: Epithelial cell signaling in Helicobacter pylori infection; hsa05131: Shigellosis; hsa05160: Hepatitis C; hsa05163: Human cytomegalovirus infection; hsa05165: Human papillomavirus infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05206: MicroRNAs in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05210: Colorectal cancer; hsa05212: Pancreatic cancer; hsa05213: Endometrial cancer; hsa05214: Glioma; hsa05215: Prostate cancer; hsa05218: Melanoma; hsa05219: Bladder cancer; 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"	"R-HSA-1227986: Signaling by ERBB2; R-HSA-1236382: Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-1236394: Signaling by ERBB4; 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-177929: Signaling by EGFR; 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-212718: EGFR interacts with phospholipase C-gamma; R-HSA-2179392: EGFR Transactivation by Gastrin; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-445144: Signal transduction by L1; R-HSA-5637810: Constitutive Signaling by EGFRvIII; R-HSA-5638303: Inhibition of Signaling by Overexpressed EGFR; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6785631: ERBB2 Regulates Cell Motility; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-8847993: ERBB2 Activates PTK6 Signaling; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis; R-HSA-8857538: PTK6 promotes HIF1A stabilization; R-HSA-8863795: Downregulation of ERBB2 signaling; R-HSA-8866910: TFAP2 (AP-2) family regulates transcription of growth factors and their receptors; R-HSA-9009391: Extra-nuclear estrogen signaling; R-HSA-9013507: NOTCH3 Activation and Transmission of Signal to the Nucleus; R-HSA-9609690: HCMV Early Events; R-HSA-9634638: Estrogen-dependent nuclear events downstream of ESR-membrane signaling; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665348: Signaling by ERBB2 ECD mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants"	.	P00533
TTZ04AF	EGFR T790M mutant (EGFR T790M)	P00533	EGFR_HUMAN	Kinase	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	EGFR	"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."	EC 2.7.10.1	6D8E; 6B3S; 6ARU; 5ZWJ; 5YU9	MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA	Patented-recorded	"Inhibitors of JAK-family kinases: an update on the patent literature 2013-2015, part 1.Expert Opin Ther Pat. 2017 Feb;27(2):127-143."	15.5	EC:2.7	Protein kinase superfamily. Tyr protein kinase family	.	.	.	Furin-like cysteine rich region; Growth factor receptor domain IV; Protein tyrosine kinase; Receptor L domain	PF00757; PF14843; PF07714; PF01030	PF00757; Furin-like; PF14843; GF_recep_IV; PF07714; Pkinase_Tyr; PF01030; Recep_L_domain	.	.	"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; hsa04020: Calcium signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04068: FoxO signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04144: Endocytosis; hsa04151: PI3K-Akt signaling pathway; hsa04510: Focal adhesion; hsa04520: Adherens junction; hsa04540: Gap junction; hsa04630: JAK-STAT signaling pathway; hsa04810: Regulation of actin cytoskeleton; hsa04912: GnRH signaling pathway; hsa04915: Estrogen signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04926: Relaxin signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04934: Cushing syndrome; hsa05120: Epithelial cell signaling in Helicobacter pylori infection; hsa05131: Shigellosis; hsa05160: Hepatitis C; hsa05163: Human cytomegalovirus infection; hsa05165: Human papillomavirus infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05206: MicroRNAs in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05210: Colorectal cancer; hsa05212: Pancreatic cancer; hsa05213: Endometrial cancer; hsa05214: Glioma; hsa05215: Prostate cancer; hsa05218: Melanoma; hsa05219: Bladder cancer; 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"	"R-HSA-1227986: Signaling by ERBB2; R-HSA-1236382: Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-1236394: Signaling by ERBB4; 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-177929: Signaling by EGFR; 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-212718: EGFR interacts with phospholipase C-gamma; R-HSA-2179392: EGFR Transactivation by Gastrin; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-445144: Signal transduction by L1; R-HSA-5637810: Constitutive Signaling by EGFRvIII; R-HSA-5638303: Inhibition of Signaling by Overexpressed EGFR; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6785631: ERBB2 Regulates Cell Motility; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-8847993: ERBB2 Activates PTK6 Signaling; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis; R-HSA-8857538: PTK6 promotes HIF1A stabilization; R-HSA-8863795: Downregulation of ERBB2 signaling; R-HSA-8866910: TFAP2 (AP-2) family regulates transcription of growth factors and their receptors; R-HSA-9009391: Extra-nuclear estrogen signaling; R-HSA-9013507: NOTCH3 Activation and Transmission of Signal to the Nucleus; R-HSA-9609690: HCMV Early Events; R-HSA-9634638: Estrogen-dependent nuclear events downstream of ESR-membrane signaling; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665348: Signaling by ERBB2 ECD mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants"	.	P00533
TTZ6B2I	Epidermal growth factor receptor variant III (EGFR vIII)	P00533	EGFR_HUMAN	Kinase	ERBB1 variant III; ERBB variant III	EGFR	"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)."	EC 2.7.10.1	6D8E; 6B3S; 6ARU; 5ZWJ; 5YU9	MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA	Clinical trial	ClinicalTrials.gov (NCT01454596) CAR T Cell Receptor Immunotherapy Targeting EGFRvIII for Patients With Malignant Gliomas Expressing EGFRvIII. U.S. National Institutes of Health.	21	.	.	.	.	.	Furin-like cysteine rich region; Growth factor receptor domain IV; Protein tyrosine kinase; Receptor L domain	PF00757; PF14843; PF07714; PF01030	PF00757; Furin-like; PF14843; GF_recep_IV; PF07714; Pkinase_Tyr; PF01030; Recep_L_domain	.	.	"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; hsa04020: Calcium signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04068: FoxO signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04144: Endocytosis; hsa04151: PI3K-Akt signaling pathway; hsa04510: Focal adhesion; hsa04520: Adherens junction; hsa04540: Gap junction; hsa04630: JAK-STAT signaling pathway; hsa04810: Regulation of actin cytoskeleton; hsa04912: GnRH signaling pathway; hsa04915: Estrogen signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04926: Relaxin signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04934: Cushing syndrome; hsa05120: Epithelial cell signaling in Helicobacter pylori infection; hsa05131: Shigellosis; hsa05160: Hepatitis C; hsa05163: Human cytomegalovirus infection; hsa05165: Human papillomavirus infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05206: MicroRNAs in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05210: Colorectal cancer; hsa05212: Pancreatic cancer; hsa05213: Endometrial cancer; hsa05214: Glioma; hsa05215: Prostate cancer; hsa05218: Melanoma; hsa05219: Bladder cancer; 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"	"R-HSA-1227986: Signaling by ERBB2; R-HSA-1236382: Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants; R-HSA-1236394: Signaling by ERBB4; 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-177929: Signaling by EGFR; 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-212718: EGFR interacts with phospholipase C-gamma; R-HSA-2179392: EGFR Transactivation by Gastrin; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-445144: Signal transduction by L1; R-HSA-5637810: Constitutive Signaling by EGFRvIII; R-HSA-5638303: Inhibition of Signaling by Overexpressed EGFR; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6785631: ERBB2 Regulates Cell Motility; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-8847993: ERBB2 Activates PTK6 Signaling; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis; R-HSA-8857538: PTK6 promotes HIF1A stabilization; R-HSA-8863795: Downregulation of ERBB2 signaling; R-HSA-8866910: TFAP2 (AP-2) family regulates transcription of growth factors and their receptors; R-HSA-9009391: Extra-nuclear estrogen signaling; R-HSA-9013507: NOTCH3 Activation and Transmission of Signal to the Nucleus; R-HSA-9609690: HCMV Early Events; R-HSA-9634638: Estrogen-dependent nuclear events downstream of ESR-membrane signaling; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665348: Signaling by ERBB2 ECD mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants"	.	P00533
TT9ISBX	HIF-prolyl hydroxylase 2 (HPH-2)	Q9GZT9	EGLN1_HUMAN	Paired donor oxygen oxidoreductase	SM-20; Prolyl hydroxylase domain-containing protein 2; PHD2; Hypoxia-inducible factor prolyl hydroxylase 2; HPH-2; HIF-PH2; Egl nine homolog 1; C1orf12	EGLN1	"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."	EC 1.14.11.29	6NMQ; 5V18; 5OX6; 5OX5; 5LBF	MANDSGGPGGPSPSERDRQYCELCGKMENLLRCSRCRSSFYCCKEHQRQDWKKHKLVCQGSEGALGHGVGPHQHSGPAPPAAVPPPRAGAREPRKAAARRDNASGDAAKGKVKAKPPADPAAAASPCRAAAGGQGSAVAAEAEPGKEEPPARSSLFQEKANLYPPSNTPGDALSPGGGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDSVGKDVF	Patented-recorded	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2833).	0	EC:1.14	Oxidoreductases acting on paired donors	.	1.14.11.29 	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	2OG-Fe(II) oxygenase superfamily; MYND finger	PF13640; PF01753	PF13640; 2OG-FeII_Oxy_3; PF01753; zf-MYND	.	.	hsa04066:HIF-1 signaling pathway; hsa05200:Pathways in cancer; hsa05211:Renal cell carcinoma	R-HSA-1234176:Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha	.	Q9GZT9
TTMHFRY	HIF-prolyl hydroxylase 1 (HPH-1)	Q96KS0	EGLN2_HUMAN	Paired donor oxygen oxidoreductase	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	EGLN2	"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."	EC 1.14.11.29	5V1B	MDSPCQPQPLSQALPQLPGSSSEPLEPEPGRARMGVESYLPCPLLPSYHCPGVPSEASAGSGTPRATATSTTASPLRDGFGGQDGGELRPLQSEGAAALVTKGCQRLAAQGARPEAPKRKWAEDGGDAPSPSKRPWARQENQEAEREGGMSCSCSSGSGEASAGLMEEALPSAPERLALDYIVPCMRYYGICVKDSFLGAALGGRVLAEVEALKRGGRLRDGQLVSQRAIPPRSIRGDQIAWVEGHEPGCRSIGALMAHVDAVIRHCAGRLGSYVINGRTKAMVACYPGNGLGYVRHVDNPHGDGRCITCIYYLNQNWDVKVHGGLLQIFPEGRPVVANIEPLFDRLLIFWSDRRNPHEVKPAYATRYAITVWYFDAKERAAAKDKYQLASGQKGVQVPVSQPPTPT	Clinical trial	The latest advances in kidney diseases and related disorders. Drug News Perspect. 2007 Dec;20(10):647-54.	25	EC:1.14	Oxidoreductases acting on paired donors	.	1.14.11.29 	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	2OG-Fe(II) oxygenase superfamily	PF13640	PF13640; 2OG-FeII_Oxy_3	.	.	hsa04066:HIF-1 signaling pathway; hsa05200:Pathways in cancer; hsa05211:Renal cell carcinoma	R-HSA-1234176:Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha	MetaCyc:ENSG00000171570-MON	Q96KS0
TTE8LGD	EGR1 messenger RNA (EGR1 mRNA)	P18146	EGR1_HUMAN	.	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	EGR1	"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)."	.	.	MAAAKAEMQLMSPLQISDPFGSFPHSPTMDNYPKLEEMMLLSNGAPQFLGAAGAPEGSGSNSSSSSSGGGGGGGGGSNSSSSSSTFNPQADTGEQPYEHLTAESFPDISLNNEKVLVETSYPSQTTRLPPITYTGRFSLEPAPNSGNTLWPEPLFSLVSGLVSMTNPPASSSSAPSPAASSASASQSPPLSCAVPSNDSSPIYSAAPTFPTPNTDIFPEPQSQAFPGSAGTALQYPPPAYPAAKGGFQVPMIPDYLFPQQQGDLGLGTPDQKPFQGLESRTQQPSLTPLSTIKAFATQSGSQDLKALNTSYQSQLIKPSRMRKYPNRPSKTPPHERPYACPVESCDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDERKRHTKIHLRQKDKKADKSVVASSATSSLSSYPSPVATSYPSPVTTSYPSPATTSYPSPVPTSFSSPGSSTYPSPVHSGFPSPSVATTYSSVPPAFPAQVSSFPSSAVTNSFSASTGLSDMTATFSPRTIEIC	Clinical trial	ClinicalTrials.gov (NCT04104919) Study to Evaluate a Preop Dose of Brivoligide Injection for Pain After Mastectomy in Patients With High PCS Scores. U.S. National Institutes of Health.	.	.	.	.	.	.	.	.	.	.	.	"hsa04371: Apelin signaling pathway; hsa04912: GnRH signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa05020: Prion disease; hsa05166: Human T-cell leukemia virus 1 infection"	R-HSA-8943724: Regulation of PTEN gene transcription; R-HSA-9031628: NGF-stimulated transcription; R-HSA-909733: Interferon alpha/beta signaling	.	P18146
TTUQREN	Early growth response protein 1 (EGR-1)	P18146	EGR1_HUMAN	EGR C2H2-type zinc-finger	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	EGR1	"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."	.	5N14; 4X9J; 4R2D; 4R2C; 4R2A	MAAAKAEMQLMSPLQISDPFGSFPHSPTMDNYPKLEEMMLLSNGAPQFLGAAGAPEGSGSNSSSSSSGGGGGGGGGSNSSSSSSTFNPQADTGEQPYEHLTAESFPDISLNNEKVLVETSYPSQTTRLPPITYTGRFSLEPAPNSGNTLWPEPLFSLVSGLVSMTNPPASSSSAPSPAASSASASQSPPLSCAVPSNDSSPIYSAAPTFPTPNTDIFPEPQSQAFPGSAGTALQYPPPAYPAAKGGFQVPMIPDYLFPQQQGDLGLGTPDQKPFQGLESRTQQPSLTPLSTIKAFATQSGSQDLKALNTSYQSQLIKPSRMRKYPNRPSKTPPHERPYACPVESCDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDERKRHTKIHLRQKDKKADKSVVASSATSSLSSYPSPVATSYPSPVTTSYPSPATTSYPSPVPTSFSSPGSSTYPSPVHSGFPSPSVATTYSSVPPAFPAQVSSFPSSAVTNSFSASTGLSDMTATFSPRTIEIC	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	EGR C2H2-type zinc-finger	EGR C2H2-type zinc-finger	EGR C2H2-type zinc-finger protein family.	.	.	"Domain of unknown function (DUF3432); Early growth response N-terminal domain; Zinc finger, C2H2 type"	PF11914; PF11928; PF00096	PF11914; DUF3432; PF11928; DUF3446; PF00096; zf-C2H2	.	.	"hsa04371: Apelin signaling pathway; hsa04912: GnRH signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa05020: Prion disease; hsa05166: Human T-cell leukemia virus 1 infection"	R-HSA-8943724: Regulation of PTEN gene transcription; R-HSA-9031628: NGF-stimulated transcription; R-HSA-909733: Interferon alpha/beta signaling	.	P18146
TTPXTVS	Entamoeba Cysteine proteinase CP4  (Eh CP4)	Q27641	Q27641_ENTDI	.	Entamoeba Cysteine proteinase CP4; Cysteine proteinase	Eh CP4	"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."	EC 3.4.22.35	.	FVAAATAIDFKSWAAKNNKHFTAVEALRRRAIFNMNAKFVAKFNKANSFELSVDGPFAAMTNEEYNHLLRVHETEAAADSVYDNTIITASSKDWRAEGKVTPVRDQGNCGSCYSFSSLAVLESRLLIAGSKYNQNNQDLSEQQIVDCSTANNGCNGGSLSATYLYVKNNGVTDEASYPYTATKGTCKAFTPKVQTTGLTHVTPNEDALTSALEQGPVAVCIDAGKASFQLYKSGVYDEPKCSKTVNHGVAAVGYGTQDGKDYYIVKNSWGTSWGDKGYILMSRNKNNQCAIASVAYFPNGAHDAN	Literature-reported	"A novel Entamoeba histolytica cysteine proteinase, EhCP4, is key for invasive amebiasis and a therapeutic target. J Biol Chem. 2010 Jun 11;285(24):18516-27."	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOFXD7	Euchromatic histone-lysine N-methyltransferase 1 (EHMT1)	Q9H9B1	EHMT1_HUMAN	.	EHMT1	EHMT1	"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."	EC 2.1.1.-	6MBP; 6MBO; 6BY9; 5VSF; 5VSD	MAAADAEAVPARGEPQQDCCVKTELLGEETPMAADEGSAEKQAGEAHMAADGETNGSCENSDASSHANAAKHTQDSARVNPQDGTNTLTRIAENGVSERDSEAAKQNHVTADDFVQTSVIGSNGYILNKPALQAQPLRTTSTLASSLPGHAAKTLPGGAGKGRTPSAFPQTPAAPPATLGEGSADTEDRKLPAPGADVKVHRARKTMPKSVVGLHAASKDPREVREARDHKEPKEEINKNISDFGRQQLLPPFPSLHQSLPQNQCYMATTKSQTACLPFVLAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGSKGEKDLGASSLHVNGESLEMDSDEDDSEELEEDDGHGAEQAAAFPTEDSRTSKESMSEADRAQKMDGESEEEQESVDTGEEEEGGDESDLSSESSIKKKFLKRKGKTDSPWIKPARKRRRRSRKKPSGALGSESYKSSAGSAEQTAPGDSTGYMEVSLDSLDLRVKGILSSQAEGLANGPDVLETDGLQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTNSVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESSKAKEVTIAKADTTSTVTPVPGQEKGSALEGRADTTTGSAAGPPLSEDDKLQGAASHVPEGFDPTGPAGLGRPTPGLSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVWSALQMSKALQDSAPDRPSPVERIVSRDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHSSAALAQRQASAAQEAQEDGLPDTSSAAAADPL	Literature-reported	A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells. Nat Chem Biol. 2011 Jul 10;7(8):566-74.	0	.	.	.	.	.	.	.	.	.	.	hsa00310: Lysine degradation; hsa01100: Metabolic pathways; hsa04211: Longevity regulating pathway	R-HSA-2559582: Senescence-Associated Secretory Phenotype (SASP); R-HSA-3214841: PKMTs methylate histone lysines; R-HSA-6804760: Regulation of TP53 Activity through Methylation; R-HSA-8853884: Transcriptional Regulation by VENTX; R-HSA-8953750: Transcriptional Regulation by E2F6	MetaCyc:HS17627-MON	Q9H9B1
TTS6RZT	Histone-lysine N-methyltransferase EHMT2 (EHMT2)	Q96KQ7	EHMT2_HUMAN	Methyltransferase	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	EHMT2	"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."	EC 2.1.1.-	5VSE; 5VSC; 5V9I; 5TUY; 5TTF	MAAAAGAAAAAAAEGEAPAEMGALLLEKETRGATERVHGSLGDTPRSEETLPKATPDSLEPAGPSSPASVTVTVGDEGADTPVGATPLIGDESENLEGDGDLRGGRILLGHATKSFPSSPSKGGSCPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAAAAGSEPPPATTSPEGQPKVHRARKTMSKPGNGQPPVPEKRPPEIQHFRMSDDVHSLGKVTSDLAKRRKLNSGGGLSEELGSARRSGEVTLTKGDPGSLEEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEALTEQLSEEEEEEEEEEEEEEEEEEEEEEEEDEESGNQSDRSGSSGRRKAKKKWRKDSPWVKPSRKRRKREPPRAKEPRGVNGVGSSGPSEYMEVPLGSLELPSEGTLSPNHAGVSNDTSSLETERGFEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELSGCNAAILKRETMRPSSRVALMVLCETHRARMVKHHCCPGCGYFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDASEAQEVTIPRGDGVTPPAGTAAPAPPPLSQDVPGRADTSQPSARMRGHGEPRRPPCDPLADTIDSSGPSLTLPNGGCLSAVGLPLGPGREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFALQLNRKLRLGVGNRAIRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLDPHPELLPELGSLPPVNT	Preclinical	"Protein lysine methyltransferase G9a inhibitors: design, synthesis, and structure activity relationships of 2,4-diamino-7-aminoalkoxy-quinazolines. J Med Chem. 2010 Aug 12;53(15):5844-57."	0	EC:2.1	.	class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.	2.1.1.-	Transferring one-carbon groups	Ankyrin repeats (3 copies); Pre-SET motif; SET domain	PF12796; PF05033; PF00856	PF12796; Ank_2; PF05033; Pre-SET; PF00856; SET	.	.	hsa00310: Lysine degradation; hsa01100: Metabolic pathways; hsa04211: Longevity regulating pathway	R-HSA-2559582: Senescence-Associated Secretory Phenotype (SASP); R-HSA-3214841: PKMTs methylate histone lysines; R-HSA-427389: ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression; R-HSA-6804760: Regulation of TP53 Activity through Methylation; R-HSA-73762: RNA Polymerase I Transcription Initiation; R-HSA-8853884: Transcriptional Regulation by VENTX; R-HSA-8953750: Transcriptional Regulation by E2F6	MetaCyc:HS06313-MON	Q96KQ7
TTRUJBV	Eukaryotic translation initiation factor 2-alpha kinase 1 (EIF2AK1)	Q9BQI3	E2AK1_HUMAN	.	PRO1362; KIAA1369; Hemin-sensitive initiation factor 2-alpha kinase; Heme-regulated inhibitor; Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase; HRI	EIF2AK1	"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)."	EC 2.7.11.1	.	MQGGNSGVRKREEEGDGAGAVAAPPAIDFPAEGPDPEYDESDVPAEIQVLKEPLQQPTFPFAVANQLLLVSLLEHLSHVHEPNPLRSRQVFKLLCQTFIKMGLLSSFTCSDEFSSLRLHHNRAITHLMRSAKERVRQDPCEDISRIQKIRSREVALEAQTSRYLNEFEELAILGKGGYGRVYKVRNKLDGQYYAIKKILIKGATKTVCMKVLREVKVLAGLQHPNIVGYHTAWIEHVHVIQPRADRAAIELPSLEVLSDQEEDREQCGVKNDESSSSSIIFAEPTPEKEKRFGESDTENQNNKSVKYTTNLVIRESGELESTLELQENGLAGLSASSIVEQQLPLRRNSHLEESFTSTEESSEENVNFLGQTEAQYHLMLHIQMQLCELSLWDWIVERNKRGREYVDESACPYVMANVATKIFQELVEGVFYIHNMGIVHRDLKPRNIFLHGPDQQVKIGDFGLACTDILQKNTDWTNRNGKRTPTHTSRVGTCLYASPEQLEGSEYDAKSDMYSLGVVLLELFQPFGTEMERAEVLTGLRTGQLPESLRKRCPVQAKYIQHLTRRNSSQRPSAIQLLQSELFQNSGNVNLTLQMKIIEQEKEIAELKKQLNLLSQDKGVRDDGKDGGVG	Literature-reported	Discovery of the first known small-molecule inhibitors of heme-regulated eukaryotic initiation factor 2alpha (HRI) kinase. Bioorg Med Chem Lett. 2009 Dec 1;19(23):6548-51.	0	.	.	.	.	.	.	.	.	.	.	hsa04141: Protein processing in endoplasmic reticulum; hsa05160: Hepatitis C; hsa05162: Measles; hsa05168: Herpes simplex virus 1 infection	R-HSA-9648895: Response of EIF2AK1 (HRI) to heme deficiency	.	Q9BQI3
TT5BYHP	Heme-controlled repressor (HCR)	Q9BQI3	E2AK1_HUMAN	.	HCR	EIF2AK1	"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)."	EC 2.7.11.1	.	MQGGNSGVRKREEEGDGAGAVAAPPAIDFPAEGPDPEYDESDVPAEIQVLKEPLQQPTFPFAVANQLLLVSLLEHLSHVHEPNPLRSRQVFKLLCQTFIKMGLLSSFTCSDEFSSLRLHHNRAITHLMRSAKERVRQDPCEDISRIQKIRSREVALEAQTSRYLNEFEELAILGKGGYGRVYKVRNKLDGQYYAIKKILIKGATKTVCMKVLREVKVLAGLQHPNIVGYHTAWIEHVHVIQPRADRAAIELPSLEVLSDQEEDREQCGVKNDESSSSSIIFAEPTPEKEKRFGESDTENQNNKSVKYTTNLVIRESGELESTLELQENGLAGLSASSIVEQQLPLRRNSHLEESFTSTEESSEENVNFLGQTEAQYHLMLHIQMQLCELSLWDWIVERNKRGREYVDESACPYVMANVATKIFQELVEGVFYIHNMGIVHRDLKPRNIFLHGPDQQVKIGDFGLACTDILQKNTDWTNRNGKRTPTHTSRVGTCLYASPEQLEGSEYDAKSDMYSLGVVLLELFQPFGTEMERAEVLTGLRTGQLPESLRKRCPVQAKYIQHLTRRNSSQRPSAIQLLQSELFQNSGNVNLTLQMKIIEQEKEIAELKKQLNLLSQDKGVRDDGKDGGVG	Literature-reported	DNA methylation signatures at endoplasmic reticulum stress genes are associated with adiposity and insulin resistance. Mol Genet Metab. 2018 Jan;123(1):50-58.	.	.	.	.	.	.	.	.	.	.	.	hsa04141: Protein processing in endoplasmic reticulum; hsa05160: Hepatitis C; hsa05162: Measles; hsa05168: Herpes simplex virus 1 infection	R-HSA-9648895: Response of EIF2AK1 (HRI) to heme deficiency	.	Q9BQI3
TTFYBZ3	EIF protein kinase messenger RNA (EIFK mRNA)	Q9BQI3; P19525; P19525; Q9P2K8	E2AK1_HUMAN; E2AK2_HUMAN; E2AK3_HUMAN; E2AK4_HUMAN	mRNA target	eIF-2A kinase; Eukaryotic translation initiation factor 2-alpha kinase	EIF2AK1	"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."	.	.	MQGGNSGVRKREEEGDGAGAVAAPPAIDFPAEGPDPEYDESDVPAEIQVLKEPLQQPTFPFAVANQLLLVSLLEHLSHVHEPNPLRSRQVFKLLCQTFIKMGLLSSFTCSDEFSSLRLHHNRAITHLMRSAKERVRQDPCEDISRIQKIRSREVALEAQTSRYLNEFEELAILGKGGYGRVYKVRNKLDGQYYAIKKILIKGATKTVCMKVLREVKVLAGLQHPNIVGYHTAWIEHVHVIQPRADRAAIELPSLEVLSDQEEDREQCGVKNDESSSSSIIFAEPTPEKEKRFGESDTENQNNKSVKYTTNLVIRESGELESTLELQENGLAGLSASSIVEQQLPLRRNSHLEESFTSTEESSEENVNFLGQTEAQYHLMLHIQMQLCELSLWDWIVERNKRGREYVDESACPYVMANVATKIFQELVEGVFYIHNMGIVHRDLKPRNIFLHGPDQQVKIGDFGLACTDILQKNTDWTNRNGKRTPTHTSRVGTCLYASPEQLEGSEYDAKSDMYSLGVVLLELFQPFGTEMERAEVLTGLRTGQLPESLRKRCPVQAKYIQHLTRRNSSQRPSAIQLLQSELFQNSGNVNLTLQMKIIEQEKEIAELKKQLNLLSQDKGVRDDGKDGGVG	Literature-reported	Kinases of eIF2a Switch Translation of mRNA Subset during Neuronal Plasticity. Int J Mol Sci. 2017 Oct 22;18(10). pii: E2213.	.	mRNA	mRNA target	.	.	.	.	.	.	.	.	hsa04141: Protein processing in endoplasmic reticulum; hsa05160: Hepatitis C; hsa05162: Measles; hsa05168: Herpes simplex virus 1 infection	R-HSA-9648895: Response of EIF2AK1 (HRI) to heme deficiency	.	Q9BQI3
TTXEZJ4	Tyrosine-protein kinase EIF2AK2 (p68)	P19525	E2AK2_HUMAN	Kinase	"p68 kinase; Proteinkinase RNA-activated; Interferon-inducible RNA-dependent protein kinase p68; Interferon-induced, double-stranded RNA-activated protein kinase p68"	EIF2AK2	"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."	EC 2.7.11.1	3UIU; 2A1A; 2A19; 1QU6	MAGDLSAGFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFQVIIDGREFPEGEGRSKKEAKNAAAKLAVEILNKEKKAVSPLLLTTTNSSEGLSMGNYIGLINRIAQKKRLTVNYEQCASGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQILSEETSVKSDYLSSGSFATTCESQSNSLVTSTLASESSSEGDFSADTSEINSNSDSLNSSSLLMNGLRNNQRKAKRSLAPRFDLPDMKETKYTVDKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGFDYDPETSDDSLESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIEKRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNERHTC	Patented-recorded	Identification of new inhibitors of protein kinase R guided by statistical modeling. Bioorg Med Chem Lett. 2011 Jul 1;21(13):4108-14.	0	EC:2.7	Kinase	protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Double-stranded RNA binding motif; Protein kinase domain	PF00035; PF00069	PF00035; dsrm; PF00069; Pkinase	.	.	hsa04141: Protein processing in endoplasmic reticulum; hsa04217: Necroptosis; hsa05010: Alzheimer disease; hsa05160: Hepatitis C; hsa05162: Measles; hsa05164: Influenza A; hsa05165: Human papillomavirus infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05171: Coronavirus disease - COVID-19; hsa05203: Viral carcinogenesis	R-HSA-1169408:ISG15 antiviral mechanism	.	P19525
TTF0OQ7	Protein kinase R (PKR)	P19525	E2AK2_HUMAN	.	"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"	EIF2AK2	"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."	EC 2.7.11.1	3UIU; 2A1A; 2A19; 1QU6	MAGDLSAGFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFQVIIDGREFPEGEGRSKKEAKNAAAKLAVEILNKEKKAVSPLLLTTTNSSEGLSMGNYIGLINRIAQKKRLTVNYEQCASGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQILSEETSVKSDYLSSGSFATTCESQSNSLVTSTLASESSSEGDFSADTSEINSNSDSLNSSSLLMNGLRNNQRKAKRSLAPRFDLPDMKETKYTVDKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGFDYDPETSDDSLESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIEKRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNERHTC	Literature-reported	Direct interaction between STAT3 and EIF2AK2 controls fatty acid-induced autophagy. Autophagy. 2013 Mar;9(3):415-7.	.	.	.	.	.	.	.	.	.	.	.	hsa04141: Protein processing in endoplasmic reticulum; hsa04217: Necroptosis; hsa05010: Alzheimer disease; hsa05160: Hepatitis C; hsa05162: Measles; hsa05164: Influenza A; hsa05165: Human papillomavirus infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05171: Coronavirus disease - COVID-19; hsa05203: Viral carcinogenesis	R-HSA-1169408: ISG15 antiviral mechanism; R-HSA-169131: Inhibition of PKR	.	P19525
TT79U1M	Pancreatic eIF2-alpha kinase (HsPEK)	Q9NZJ5	E2AK3_HUMAN	.	PERK; HsPEK; Eukaryotic translation initiation factor 2-alpha kinase 3	EIF2AK3	"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."	EC 2.7.11.1	5SV7; 4YZS; 4X7O; 4X7N; 4X7L	MERAISPGLLVRALLLLLLLLGLAARTVAAGRARGLPAPTAEAAFGLGAAAAPTSATRVPAAGAVAAAEVTVEDAEALPAAAGEQEPRGPEPDDETELRPRGRSLVIISTLDGRIAALDPENHGKKQWDLDVGSGSLVSSSLSKPEVFGNKMIIPSLDGALFQWDQDRESMETVPFTVESLLESSYKFGDDVVLVGGKSLTTYGLSAYSGKVRYICSALGCRQWDSDEMEQEEDILLLQRTQKTVRAVGPRSGNEKWNFSVGHFELRYIPDMETRAGFIESTFKPNENTEESKIISDVEEQEAAIMDIVIKVSVADWKVMAFSKKGGHLEWEYQFCTPIASAWLLKDGKVIPISLFDDTSYTSNDDVLEDEEDIVEAARGATENSVYLGMYRGQLYLQSSVRISEKFPSSPKALESVTNENAIIPLPTIKWKPLIHSPSRTPVLVGSDEFDKCLSNDKFSHEEYSNGALSILQYPYDNGYYLPYYKRERNKRSTQITVRFLDNPHYNKNIRKKDPVLLLHWWKEIVATILFCIIATTFIVRRLFHPHPHRQRKESETQCQTENKYDSVSGEANDSSWNDIKNSGYISRYLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAIKRIRLPNRELAREKVMREVKALAKLEHPGIVRYFNAWLEAPPEKWQEKMDEIWLKDESTDWPLSSPSPMDAPSVKIRRMDPFATKEHIEIIAPSPQRSRSFSVGISCDQTSSSESQFSPLEFSGMDHEDISESVDAAYNLQDSCLTDCDVEDGTMDGNDEGHSFELCPSEASPYVRSRERTSSSIVFEDSGCDNASSKEEPKTNRLHIGNHCANKLTAFKPTSSKSSSEATLSISPPRPTTLSLDLTKNTTEKLQPSSPKVYLYIQMQLCRKENLKDWMNGRCTIEERERSVCLHIFLQIAEAVEFLHSKGLMHRDLKPSNIFFTMDDVVKVGDFGLVTAMDQDEEEQTVLTPMPAYARHTGQVGTKLYMSPEQIHGNSYSHKVDIFSLGLILFELLYPFSTQMERVRTLTDVRNLKFPPLFTQKYPCEYVMVQDMLSPSPMERPEAINIIENAVFEDLDFPGKTVLRQRSRSLSSSGTKHSRQSNNSHSPLPSN	Literature-reported	Autophagy and protein kinase RNA-like endoplasmic reticulum kinase (PERK)/eukaryotic initiation factor 2 alpha kinase (eIF2) pathway protect ovari... Mol Carcinog. 2016 Apr;55(4):346-56.	.	.	.	.	.	.	.	.	.	.	.	hsa04137: Mitophagy - animal; hsa04140: Autophagy - animal; hsa04141: Protein processing in endoplasmic reticulum; hsa04210: Apoptosis; hsa04932: Non-alcoholic fatty liver disease; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05014: Amyotrophic lateral sclerosis; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05160: Hepatitis C; hsa05162: Measles; hsa05168: Herpes simplex virus 1 infection; hsa05417: Lipid and atherosclerosis	R-HSA-381042: PERK regulates gene expression; R-HSA-9700645: ALK mutants bind TKIs; R-HSA-9725370: Signaling by ALK fusions and activated point mutants	.	Q9NZJ5
TT5OU0D	PRKR-like endoplasmic reticulum kinase (PERK)	Q9NZJ5	E2AK3_HUMAN	Kinase	PEK	EIF2AK3	"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."	EC 2.7.11.1	5SV7; 4YZS; 4X7O; 4X7N; 4X7L	MERAISPGLLVRALLLLLLLLGLAARTVAAGRARGLPAPTAEAAFGLGAAAAPTSATRVPAAGAVAAAEVTVEDAEALPAAAGEQEPRGPEPDDETELRPRGRSLVIISTLDGRIAALDPENHGKKQWDLDVGSGSLVSSSLSKPEVFGNKMIIPSLDGALFQWDQDRESMETVPFTVESLLESSYKFGDDVVLVGGKSLTTYGLSAYSGKVRYICSALGCRQWDSDEMEQEEDILLLQRTQKTVRAVGPRSGNEKWNFSVGHFELRYIPDMETRAGFIESTFKPNENTEESKIISDVEEQEAAIMDIVIKVSVADWKVMAFSKKGGHLEWEYQFCTPIASAWLLKDGKVIPISLFDDTSYTSNDDVLEDEEDIVEAARGATENSVYLGMYRGQLYLQSSVRISEKFPSSPKALESVTNENAIIPLPTIKWKPLIHSPSRTPVLVGSDEFDKCLSNDKFSHEEYSNGALSILQYPYDNGYYLPYYKRERNKRSTQITVRFLDNPHYNKNIRKKDPVLLLHWWKEIVATILFCIIATTFIVRRLFHPHPHRQRKESETQCQTENKYDSVSGEANDSSWNDIKNSGYISRYLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAIKRIRLPNRELAREKVMREVKALAKLEHPGIVRYFNAWLEAPPEKWQEKMDEIWLKDESTDWPLSSPSPMDAPSVKIRRMDPFATKEHIEIIAPSPQRSRSFSVGISCDQTSSSESQFSPLEFSGMDHEDISESVDAAYNLQDSCLTDCDVEDGTMDGNDEGHSFELCPSEASPYVRSRERTSSSIVFEDSGCDNASSKEEPKTNRLHIGNHCANKLTAFKPTSSKSSSEATLSISPPRPTTLSLDLTKNTTEKLQPSSPKVYLYIQMQLCRKENLKDWMNGRCTIEERERSVCLHIFLQIAEAVEFLHSKGLMHRDLKPSNIFFTMDDVVKVGDFGLVTAMDQDEEEQTVLTPMPAYARHTGQVGTKLYMSPEQIHGNSYSHKVDIFSLGLILFELLYPFSTQMERVRTLTDVRNLKFPPLFTQKYPCEYVMVQDMLSPSPMERPEAINIIENAVFEDLDFPGKTVLRQRSRSLSSSGTKHSRQSNNSHSPLPSN	Patented-recorded	Protein kinase R(PKR)-like endoplasmic reticulum kinase (PERK) inhibitors: a patent review (2010-2015).Expert Opin Ther Pat. 2017 Jan;27(1):37-48.	15.5	EC:2.7	.	protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04137: Mitophagy - animal; hsa04140: Autophagy - animal; hsa04141: Protein processing in endoplasmic reticulum; hsa04210: Apoptosis; hsa04932: Non-alcoholic fatty liver disease; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05014: Amyotrophic lateral sclerosis; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05160: Hepatitis C; hsa05162: Measles; hsa05168: Herpes simplex virus 1 infection; hsa05417: Lipid and atherosclerosis	R-HSA-381042: PERK regulates gene expression; R-HSA-9700645: ALK mutants bind TKIs; R-HSA-9725370: Signaling by ALK fusions and activated point mutants	.	Q9NZJ5
TT9U4EP	Eukaryotic translation initiation factor 2-alpha kinase 4 (EIF2AK4)	Q9P2K8	E2AK4_HUMAN	.	eIF-2-alpha kinase GCN2; KIAA1338; GCN2-like protein; GCN2	EIF2AK4	"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)."	EC 2.7.11.1	.	MAGGRGAPGRGRDEPPESYPQRQDHELQALEAIYGADFQDLRPDACGPVKEPPEINLVLYPQGLTGEEVYVKVDLRVKCPPTYPDVVPEIELKNAKGLSNESVNLLKSRLEELAKKHCGEVMIFELAYHVQSFLSEHNKPPPKSFHEEMLERRAQEEQQRLLEAKRKEEQEQREILHEIQRRKEEIKEEKKRKEMAKQERLEIASLSNQDHTSKKDPGGHRTAAILHGGSPDFVGNGKHRANSSGRSRRERQYSVCNSEDSPGSCEILYFNMGSPDQLMVHKGKCIGSDEQLGKLVYNALETATGGFVLLYEWVLQWQKKMGPFLTSQEKEKIDKCKKQIQGTETEFNSLVKLSHPNVVRYLAMNLKEQDDSIVVDILVEHISGVSLAAHLSHSGPIPVHQLRRYTAQLLSGLDYLHSNSVVHKVLSASNVLVDAEGTVKITDYSISKRLADICKEDVFEQTRVRFSDNALPYKTGKKGDVWRLGLLLLSLSQGQECGEYPVTIPSDLPADFQDFLKKCVCLDDKERWSPQQLLKHSFINPQPKMPLVEQSPEDSEGQDYVETVIPSNRLPSAAFFSETQRQFSRYFIEFEELQLLGKGAFGAVIKVQNKLDGCCYAVKRIPINPASRQFRRIKGEVTLLSRLHHENIVRYYNAWIERHERPAGPGTPPPDSGPLAKDDRAARGQPASDTDGLDSVEAAAPPPILSSSVEWSTSGERSASARFPATGPGSSDDEDDDEDEHGGVFSQSFLPASDSESDIIFDNEDENSKSQNQDEDCNEKNGCHESEPSVTTEAVHYLYIQMEYCEKSTLRDTIDQGLYRDTVRLWRLFREILDGLAYIHEKGMIHRDLKPVNIFLDSDDHVKIGDFGLATDHLAFSADSKQDDQTGDLIKSDPSGHLTGMVGTALYVSPEVQGSTKSAYNQKVDLFSLGIIFFEMSYHPMVTASERIFVLNQLRDPTSPKFPEDFDDGEHAKQKSVISWLLNHDPAKRPTATELLKSELLPPPQMEESELHEVLHHTLTNVDGKAYRTMMAQIFSQRISPAIDYTYDSDILKGNFSIRTAKMQQHVCETIIRIFKRHGAVQLCTPLLLPRNRQIYEHNEAALFMDHSGMLVMLPFDLRIPFARYVARNNILNLKRYCIERVFRPRKLDRFHPKELLECAFDIVTSTTNSFLPTAEIIYTIYEIIQEFPALQERNYSIYLNHTMLLKAILLHCGIPEDKLSQVYIILYDAVTEKLTRREVEAKFCNLSLSSNSLCRLYKFIEQKGDLQDLMPTINSLIKQKTGIAQLVKYGLKDLEEVVGLLKKLGIKLQVLINLGLVYKVQQHNGIIFQFVAFIKRRQRAVPEILAAGGRYDLLIPQFRGPQALGPVPTAIGVSIAIDKISAAVLNMEESVTISSCDLLVVSVGQMSMSRAINLTQKLWTAGITAEIMYDWSQSQEELQEYCRHHEITYVALVSDKEGSHVKVKSFEKERQTEKRVLETELVDHVLQKLRTKVTDERNGREASDNLAVQNLKGSFSNASGLFEIHGATVVPIVSVLAPEKLSASTRRRYETQVQTRLQTSLANLHQKSSEIEILAVDLPKETILQFLSLEWDADEQAFNTTVKQLLSRLPKQRYLKLVCDEIYNIKVEKKVSVLFLYSYRDDYYRILF	Literature-reported	"Triazolo[4,5-d]pyrimidine Derivatives as Inhibitors of GCN2. ACS Med Chem Lett. 2014 Feb 12;5(4):282-3."	0	.	.	.	.	.	.	.	.	.	.	hsa04140: Autophagy - animal; hsa04141: Protein processing in endoplasmic reticulum; hsa05160: Hepatitis C; hsa05162: Measles; hsa05168: Herpes simplex virus 1 infection	R-HSA-9633012: Response of EIF2AK4 (GCN2) to amino acid deficiency	.	Q9P2K8
TTKIGZF	Guanine nucleotide exchange factor (GNEF)	Q14232; P49770	EI2BA_HUMAN; EI2BB_HUMAN	.	eIF-2B GDP-GTP exchange factor; Translation initiation factor eIF-2B; EIF2B	EIF2B1	Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.	.	.	MDDKELIEYFKSQMKEDPDMASAVAAIRTLLEFLKRDKGETIQGLRANLTSAIETLCGVDSSVAVSSGGELFLRFISLASLEYSDYSKCKKIMIERGELFLRRISLSRNKIADLCHTFIKDGATILTHAYSRVVLRVLEAAVAAKKRFSVYVTESQPDLSGKKMAKALCHLNVPVTVVLDAAVGYIMEKADLVIVGAEGVVENGGIINKIGTNQMAVCAKAQNKPFYVVAESFKFVRLFPLNQQDVPDKFKYKADTLKVAQTGQDLKEEHPWVDYTAPSLITLLFTDLGVLTPSAVSDELIKLYL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	.	.	.	.	.	.	.	.	.	.	hsa05168: Herpes simplex virus 1 infection	R-HSA-72731: Recycling of eIF2:GDP	.	Q14232
TTIGYVZ	HUMAN eukaryotic initiation factor-4A (eIF4A)	P60842; Q14240; P38919	IF4A1_HUMAN; IF4A2_HUMAN; IF4A3_HUMAN	eIF4A subfamily	eIF-4A; ATP-dependent RNA helicase Eif4a	EIF4A1	"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"	.	.	MSASQDSRSRDNGPDGMEPEGVIESNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEWKLDTLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI	.	Broad-spectrum antiviral activity of the eIF4A inhibitor silvestrol against corona- and picornaviruses. Antiviral Res. 2018 Feb;150:123-129.	.	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-1169408: ISG15 antiviral mechanism; R-HSA-156827: L13a-mediated translational silencing of Ceruloplasmin expression; R-HSA-429947: Deadenylation of mRNA; R-HSA-72649: Translation initiation complex formation; R-HSA-72662: Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S; R-HSA-72702: Ribosomal scanning and start codon recognition; R-HSA-72706: GTP hydrolysis and joining of the 60S ribosomal subunit"	.	P60842
TTZGCP6	EIF4E messenger RNA (EIF4E mRNA)	P06730	IF4E_HUMAN	mRNA target	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)	EIF4E	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.	.	5ZML; 5ZK9; 5ZK7; 5ZK5; 5ZJZ	MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	mRNA	mRNA target	.	.	.	Eukaryotic initiation factor 4E	PF01652	PF01652; IF4E	.	.	hsa03013:RNA transport; hsa04066:HIF-1 signaling pathway; hsa04150:mTOR signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04910:Insulin signaling pathway	R-HSA-1169408:ISG15 antiviral mechanism; R-HSA-166208:mTORC1-mediated signalling	.	P06730
TTUF10B	Eukaryotic initiation factor 4E (EIF4E)	P06730	IF4E_HUMAN	.	eIF4F 25 kDa subunit; eIF4E; eIF-4F 25 kDa subunit; eIF-4E; Eukaryotic translation initiation factor 4E; EIF4F; EIF4EL1	EIF4E	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.	.	5ZML; 5ZK9; 5ZK7; 5ZK5; 5ZJZ	MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV	Literature-reported	Signalling to eIF4E in cancer. Biochem Soc Trans. 2015 Oct;43(5):763-72.	.	.	.	eukaryotic initiation factor 4E family.	.	.	Eukaryotic initiation factor 4E	PF01652	PF01652; IF4E	.	.	hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa04066: HIF-1 signaling pathway; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04211: Longevity regulating pathway; hsa04910: Insulin signaling pathway	"R-HSA-1169408: ISG15 antiviral mechanism; R-HSA-156827: L13a-mediated translational silencing of Ceruloplasmin expression; R-HSA-159227: Transport of the SLBP independent Mature mRNA; R-HSA-159230: Transport of the SLBP Dependant Mature mRNA; R-HSA-159231: Transport of Mature mRNA Derived from an Intronless Transcript; R-HSA-166208: mTORC1-mediated signalling; R-HSA-429947: Deadenylation of mRNA; R-HSA-72649: Translation initiation complex formation; R-HSA-72662: Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S; R-HSA-72702: Ribosomal scanning and start codon recognition; R-HSA-72706: GTP hydrolysis and joining of the 60S ribosomal subunit"	.	P06730
TT2ZSKV	HUMAN eukaryotic translation initiation factor 4E family member 2 (EIF4E2)	Q53RG0	Q53RG0_HUMAN	Eukaryotic initiation factor 4E family	4EHP; IF4e; 4E-LP; h4EHP; EIF4EL3	EIF4E2	"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."	.	.	MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKAVVPGPAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPGRLGPQRLLFQNLWKPRLNVP	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa04066: HIF-1 signaling pathway; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04211: Longevity regulating pathway; hsa04910: Insulin signaling pathway	.	.	.
TTKGEBL	Eukaryotic translation initiation factor 4E-binding protein 1 (EIF4EBP1)	Q13541	4EBP1_HUMAN	.	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	EIF4EBP1	"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."	.	6BCX; 6BCU; 5WBJ; 5NVN; 5EKV	MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI	Literature-reported	EIF4EBP1 overexpression is associated with poor survival and disease progression in patients with hepatocellular carcinoma. PLoS One. 2015 Feb 6;10(2):e0117493.	.	.	.	eIF4E-binding protein family.	.	.	Eukaryotic translation initiation factor 4E binding protein (EIF4EBP)	PF05456	PF05456; eIF_4EBP	.	.	hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa04012: ErbB signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04152: AMPK signaling pathway; hsa04211: Longevity regulating pathway; hsa04218: Cellular senescence; hsa04910: Insulin signaling pathway; hsa05163: Human cytomegalovirus infection; hsa05165: Human papillomavirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05207: Chemical carcinogenesis - receptor activation; hsa05221: Acute myeloid leukemia; hsa05231: Choline metabolism in cancer	"R-HSA-166208: mTORC1-mediated signalling; R-HSA-72662: Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S"	.	Q13541
TTNBTCW	eIF4E-BP2 messenger RNA (eIF4E-BP2 mRNA)	Q13542	4EBP2_HUMAN	mRNA target	eIF4E-binding protein 2 (mRNA); Eukaryotic translation initiation factor 4E-binding protein 2 (mRNA); 4E-BP2 (mRNA)	EIF4EBP2	"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."	.	3AM7; 2MX4	MSSSAGSGHQPSQSRAIPTRTVAISDAAQLPHDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGTLIEDSKVEVNNLNNLNNHDRKHAVGDDAQFEMDI	Clinical trial	"Clinical pipeline report, company report or official report of ISIS Pharmaceuticals (2011)."	21	mRNA	mRNA target	.	.	.	Eukaryotic translation initiation factor 4E binding protein (EIF4EBP)	PF05456	PF05456; eIF_4EBP	.	.	hsa03013:RNA transport	.	.	Q13542
TTIVCNR	Eukaryotic translation initiation factor 5A-1 (EIF5A)	P63241	IF5A1_HUMAN	.	eIF-5A1; eIF-5A-1; eIF-5A; eIF-4D; Rev-binding factor; Eukaryotic initiation factor 5A isoform 1	EIF5A	"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."	.	5DLQ; 3CPF; 1FH4	MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDFQLIGIQDGYLSLLQDSGEVREDLRLPEGDLGKEIEQKYDCGEEILITVLSAMTEEAAVAIKAMAK	Literature-reported	Hypusine: a new target for therapeutic intervention in diabetic inflammation. Discov Med. 2010 Jul;10(50):18-23.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-204626: Hypusine synthesis from eIF5A-lysine	.	P63241
TTH53G9	Eukaryotic initiation factor 5A2 (EIF5A2)	Q9GZV4	IF5A2_HUMAN	Eukaryotic nuclear pore complex	eIF5A2; eIF-5A2; eIF-5A-2; Eukaryotic translation initiation factor 5A-2; Eukaryotic initiation factor 5A isoform 2	EIF5A2	"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."	.	.	MADEIDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAGEDVQVSVMCAMSEEYAVAIKPCK	Literature-reported	"Increased expression of EIF5A2, via hypoxia or gene amplification, contributes to metastasis and angiogenesis of esophageal squamous cell carcinoma. Gastroenterology. 2014 Jun;146(7):1701-13."	.	TC=1.I.1	.	eIF-5A family.	.	.	"Eukaryotic elongation factor 5A hypusine, DNA-binding OB fold"	PF01287	PF01287; eIF-5a	1.I.1.1.3	The Eukaryotic Nuclear Pore Complex (E-NPC) Family	.	R-HSA-204626: Hypusine synthesis from eIF5A-lysine	.	Q9GZV4
TTMJ862	Eimeria tenella Telomerase reverse transcriptase (EIMTE TERT)	D2Y0P7	D2Y0P7_EIMTE	.	EIMTE Telomerase reverse transcriptase; EIMTE Telomerase catalytic subunit	EIMTE TERT	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.	EC 2.7.7.49	.	MVLSKAGLVALKQMELVTGELYLEKQRKRIVKFEELGYNDSSGLERRLEELLITLDPSEPKAILEGFKLGRELLFNTSLDNLSDNGIDRKLRLINGEKLILWSSIELQNGYSSFPNQRSMSSSGRSRKNEYNTELSPTSFITDQIKNIIPDSEKDSLTYQVQDFELLLRKHFPRIRIFHSGSYSGLRTSFDTIKPKKYSFCNSTLYKFQNLHAWNTLLSKIGPIEILFLFVCCIIFRILGDHSEILIQQAGRMLTNDFLEELARLYETGPKTKNKFVSSSSVLTSPLTTIIEKEEVKPELDETERQVNKREPGGIIKSEDRLSKSIYILDIKPYLSTRFLCDHFYSRGGLPCKSLVRLLPPLLLGANRTLRFILQTDHIFIDHNRQSKLGLLGISEMTKYSRVFKKLASACMEEFQMNLLLIRNTNSPVNFLDQICPIEPKLIDDLSLQFNNKLPPCFEITSTRVVNFLSRYLIKVLPKNILLGTFKNFKTFINKKIPIIVNLHIRETFKIQHAMNGIEVSNWVNRLEIESYQFKIKSKNELNESINRSKKQPNNVTRSKSKKSLISLGIKYLATRENIYFLIYLVFPVILRRHYATEIEGFSKVRYFNRPVWIKIVHRQADKWYLESLKGIIQLKDSYMLNLSISQIISKELDKNISFSEENIPKIRWVPKSKGLRPLINSKLVSGQIGLVQNLQEDHTVREEKKCKGFCDICSVWCTNGDCLPTGSCINNNWYYNYYFSYNGNNNGIVNNHYNYGHIYNNGGGIKFTSFSNSQCTQIMTNPPGRGVGLGFGNLNIGIGYISGSSVPTNTPINVMRRPSSNRKIIDIRPSTNNRMLFYPSILRSFKLLRMGKNHTLASLVGQGDIYKFIIKNWIKNWRDKQQFRQMNEFYQNDKQGKMSHVIYIIKADLVNCKFENINKSKIFEFLDVISLPNIESLSLYLSRALKTTSIPPFDNMNRDSYIQDELRSCGITSKGKLNMIVIFEKDHDPEDQKVVKSKIKIIGPRDLDELWNLKLNSCLSKDLSINLGQKAEIFTFKLSRRVINNWLVKEIIKIHKLNTSFRLRTCSFKSLRLISKQLGNSKIKFGRFLSLFKQDFGIKPQGSSSYILCICLYYNFLDLNPEIQNLLGHSFSSSYFISSFLNPIKLQEVQLLDKPTEDLFSQHKDLEGLSRTYPEKENEIFNIYNTSSKTRRLEISEYNINAKSVKLLQPEEFNNNSINQNCQNIRANLSYDQESPKSSNKQQESLLRWVDDLFLLTSDLESFAKKFLKLYIQLLWGSNVKSKDKINSNPWIDHNNEIIFILEDDVLLSSPSSSECSSSCSSSSSSSSSSSSSSSSSSSFPPSTECSSPVTEKRNTNKISEKDCNEKEMINKQAKIASQFHKQVSWTGMKFKSSEYSYNCMVSLPWKNEFICVMLDTVTLTKHQFTTSNYNFHRFKSSTISENLQTKSNYWSVLGMIKLIRYDFRIKFNGLLYCKINSLFTDVSFYNSTNNTEIKN	Literature-reported	A novel telomerase-interacting OTU protein of Eimeria tenella and its telomerase-regulating activity. Acta Biochim Biophys Sin (Shanghai). 2017 Aug 1;49(8):744-745.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTPLTSQ	Neutrophil elastase (NE)	P08246	ELNE_HUMAN	Peptidase	PMN elastase; Medullasin; Human leukocyte elastase; HLE; Elastase-2; ELA2; Bone marrow serine protease	ELANE	"Inhibits C5a-dependent neutrophil enzyme release and chemotaxis. Modifies the functions of natural killer cells, monocytes and granulocytes."	EC 3.4.21.37	6F5M; 5ABW; 5A8Z; 5A8Y; 5A8X	MTLGRRLACLFLACVLPALLLGGTALASEIVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQRSEDNPCPHPRDPDPASRTH	Clinical trial	Emerging therapies for treatment of acute lung injury and acute respiratory distress syndrome. Expert Opin Emerg Drugs. 2007 Sep;12(3):461-77.	31	EC:3.4	Peptidase	peptidase S1 family. Elastase subfamily.	3.4.21.37	Acting on peptide bonds (peptidases)	Trypsin	PF00089	PF00089; Trypsin	.	.	hsa05202:Transcriptional misregulation in cancer; hsa05322:Systemic lupus erythematosus	R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases	.	P08246
TTPC9D0	ELAV-like protein 1 (ELAVL1)	Q15717	ELAV1_HUMAN	.	HuR; Hu-antigen R	ELAVL1	"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."	.	6GD3; 6GD2; 6GD1; 6GC5; 6G2K	MSNGYEDHMAEDCRGDIGRTNLIVNYLPQNMTQDELRSLFSSIGEVESAKLIRDKVAGHSLGYGFVNYVTAKDAERAINTLNGLRLQSKTIKVSYARPSSEVIKDANLYISGLPRTMTQKDVEDMFSRFGRIINSRVLVDQTTGLSRGVAFIRFDKRSEAEEAITSFNGHKPPGSSEPITVKFAANPNQNKNVALLSQLYHSPARRFGGPVHHQAQRFRFSPMGVDHMSGLSGVNVPGNASSGWCIFIYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAMAIASLNGYRLGDKILQVSFKTNKSHK	Literature-reported	"HuR, a novel target of anti-Hu antibodies, is expressed in non-neural tissues. J Neuroimmunol. 1998 Dec 1;92(1-2):152-9."	.	.	RNA recognition motif	RRM elav family.	.	.	"RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)"	PF00076	PF00076; RRM_1	.	.	hsa04152: AMPK signaling pathway; hsa04657: IL-17 signaling pathway	R-HSA-450520: HuR (ELAVL1) binds and stabilizes mRNA; R-HSA-72163: mRNA Splicing - Major Pathway	.	Q15717
TT0VH8G	Elegans Endoprotease bli-4 (Elegans bli-4)	P51559	BLI4_CAEEL	Peptidase	kpc-4; bli-4; K04F10.4; Endoprotease bli-4; Blistered cuticle protein 4; Blisterase	Elegans bli-4	"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."	EC 3.4.21.-	.	MRISIGRIAWQILAVLIAVAFTIEHDSICDESIGACGEPIHTVIRLAKRDDELARRIAADHDMHVKGDPFLDTHYFLYHSETTRTRRHKRAIVERLDSHPAVEWVEEQRPKKRVKRDYILLDNDVHHSNPFRRSVLNRDGTRRAQRQQPQSPREIPSLPFPDPLYKDQWYLHGGAVGGYDMNVRQAWLQGYAGRNVSVSILDDGIQRDHPDLAANYDPLASTDINDHDDDPTPQNNGDNKHGTRCAGEVAALAGNNQCGVGVAFKAKIGGVRMLDGAVSDSVEAASLSLNQDHIDIYSASWGPEDDGKTFDGPGPLAREAFYRGIKNGRGGKGNIFVWASGNGGSRQDSCSADGYTTSVYTLSISSATYDNHRPWYLEECPSSIATTYSSADFRQPAIVTVDVPGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTANWKPLENNPGWSRNGVGRMVSNKFGYGLIDGGALVNMAKTWKTVPEQHICTYEYRLANPNPRPIVGRFQLNFTLDVNGCESGTPVLYLEHVQVHATVRYLKRGDLKLTLFSPSGTRSVLLPPRPQDFNANGFHKWPFLSVQQWGEDPRGTWLLMVESVTTNPAATGTFHDWTLLLYGTADPAQSGDPVYSATPATSQGVLSRVHQLTSQVEESAPISFPDLTSAGNCHDECNGGCTESSSATSCFACKHLTQTLRNKGGSGFKCVQKCDDTYYLDGDKCKMCSSHCHTCTKAEVCETCPGSLLLIDVDNMPHYDHGKCVESCPPGLVADYESNLVQAKCIWRKDLCGDGYYINAVGKCDLCDSSCETCTAPGPMSCEKCSKGYGKGSIGYCRPCCPEGSTKSWQCEDCSKPDPTLLIDSNKSSGFGLMFWIVVSLIAACGICACKKCASETKSSNVEYAPLAQYNATNGAINLGAHTDDEDDDEDEVFVNPQIV	Literature-reported	Removal of the glycosylphosphatidylinositol anchor from PrP(Sc) by cathepsin D does not reduce prion infectivity. Biochem J. 2006 Apr 15;395(2):443-8.	0	EC:3.4	.	peptidase S8 family. Furin subfamily.	3.4.21.- 	Acting on peptide bonds (peptidases)	Proprotein convertase P-domain; Subtilase family; Peptidase S8 pro-domain	PF01483; PF00082; PF16470	PF01483; P_proprotein; PF00082; Peptidase_S8; PF16470; S8_pro-domain	.	.	.	R-CEL-1592389: Activation of Matrix Metalloproteinases; R-CEL-159782: Removal of aminoterminal propeptides from gamma-carboxylated proteins; R-CEL-186797: Signaling by PDGF	.	P51559
TT5OJMV	ETS domain-containing protein Elk-3 (ELK3)	P41970	ELK3_HUMAN	E26 transformation-specific ETS	Serum response factor accessory protein 2; SRF accessory protein 2; SAP2; SAP-2; ETS-related protein NET; ETS-related protein ERP	ELK3	"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."	.	.	MESAITLWQFLLQLLLDQKHEHLICWTSNDGEFKLLKAEEVAKLWGLRKNKTNMNYDKLSRALRYYYDKNIIKKVIGQKFVYKFVSFPEILKMDPHAVEISRESLLLQDSDCKASPEGREAHKHGLAALRSTSRNEYIHSGLYSSFTINSLQNPPDAFKAIKTEKLEEPPEDSPPVEEVRTVIRFVTNKTDKHVTRPVVSLPSTSEAAAASAFLASSVSAKISSLMLPNAASISSASPFSSRSPSLSPNSPLPSEHRSLFLEAACHDSDSLEPLNLSSGSKTKSPSLPPKAKKPKGLEISAPPLVLSGTDIGSIALNSPALPSGSLTPAFFTAQTPNGLLLTPSPLLSSIHFWSSLSPVAPLSPARLQGPSTLFQFPTLLNGHMPVPIPSLDRAASPVLLSSNSQKS	Literature-reported	"Evidence that members of the secretory aspartyl proteinase gene family, in particular SAP2, are virulence factors for Candida vaginitis. J Infect Dis. 1999 Jan;179(1):201-8."	.	ETS	.	ETS family.	.	.	Ets-domain	PF00178	PF00178; Ets	.	.	.	.	.	P41970
TT92GY4	Echinoderm microtubule-associated protein-like 4 (EMAP-4)	Q9HC35	EMAL4_HUMAN	.	Ropp 120; Restrictedly overexpressed proliferation-associated protein; EMAPL4; EMAP-4; C2orf2	EML4	"May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic."	.	4CGC	MDGFAGSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKKSVSSKGQPSPRAVIPMSCITNGSGANRKPSHTSAVSIAGKETLSSAAKSGTEKKKEKPQGQREKKEESHSNDQSPQIRASPSPQPSSQPLQIHRQTPESKNATPTKSIKRPSPAEKSHNSWENSDDSRNKLSKIPSTPKLIPKVTKTADKHKDVIINQEGEYIKMFMRGRPITMFIPSDVDNYDDIRTELPPEKLKLEWAYGYRGKDCRANVYLLPTGKIVYFIASVVVLFNYEERTQRHYLGHTDCVKCLAIHPDKIRIATGQIAGVDKDGRPLQPHVRVWDSVTLSTLQIIGLGTFERGVGCLDFSKADSGVHLCIIDDSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPTDANTIITCGKSHIFFWTWSGNSLTRKQGIFGKYEKPKFVQCLAFLGNGDVLTGDSGGVMLIWSKTTVEPTPGKGPKGVYQISKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNPEREIEVPDQYGTIRAVAEGKADQFLVGTSRNFILRGTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNSMEHRLEWTRLVDEPGHCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHDNFIYLYVVSENGRKYSRYGRCTGHSSYITHLDWSPDNKYIMSNSGDYEILYWDIPNGCKLIRNRSDCKDIDWTTYTCVLGFQVFGVWPEGSDGTDINALVRSHNRKVIAVADDFCKVHLFQYPCSKAKAPSHKYSAHSSHVTNVSFTHNDSHLISTGGKDMSIIQWKLVEKLSLPQNETVADTTLTKAPVSSTESVIQSNTPTPPPSQPLNETAEEESRISSSPTLLENSLEQTVEPSEDHSEEESEEGSGDLGEPLYEEPCNEISKEQAKATLLEDQQDPSPSS	Literature-reported	Systemic therapy for echinoderm microtubule-associated protein-like 4 anaplastic lymphoma kinase non-small cell lung cancer brain metastases. J Thorac Dis. 2016 Sep;8(9):E1028-E1031.	.	.	.	.	.	.	.	.	.	.	.	hsa05200: Pathways in cancer; hsa05223: Non-small cell lung cancer; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer	R-HSA-9648025: EML4 and NUDC in mitotic spindle formation; R-HSA-9700645: ALK mutants bind TKIs; R-HSA-9725370: Signaling by ALK fusions and activated point mutants; R-HSA-9725371: Nuclear events stimulated by ALK signaling in cancer	.	Q9HC35
TTY36UA	Protein enabled homolog MENA (ENAH)	Q8N8S7	ENAH_HUMAN	.	MENA	ENAH	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.	.	5NEG; 5NDU; 5ND0; 5NCP; 5NCG	MSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVLNSQETGPTLPRQNSQLPAQVQNGPSQEELEIQRRQLQEQQRQKELERERLERERMERERLERERLERERLERERLEQEQLERERQERERQERLERQERLERQERLERQERLDRERQERQERERLERLERERQERERQEQLEREQLEWERERRISSAAAPASVETPLNSVLGDSSASEPGLQAASQPAETPSQQGIVLGPLAPPPPPPLPPGPAQASVALPPPPGPPPPPPLPSTGPPPPPPPPPLPNQVPPPPPPPPAPPLPASGFFLASMSEDNRPLTGLAAAIAGAKLRKVSRMEDTSFPSGGNAIGVNSASSKTDTGRGNGPLPLGGSGLMEEMSALLARRRRIAEKGSTIETEQKEDKGEDSEPVTSKASSTSTPEPTRKPWERTNTMNGSKSPVISRRDSPRKNQIVFDNRSYDSLHRPKSTPLSQPSANGVQTEGLDYDRLKQDILDEMRKELTKLKEELIDAIRQELSKSNTA	Literature-reported	Mammalian-enabled (MENA) protein enhances oncogenic potential and cancer stem cell-like phenotype in hepatocellular carcinoma cells. FEBS Open Bio. 2017 Jun 22;7(8):1144-1153.	.	.	.	.	.	.	.	.	.	.	.	hsa04015:Rap1 signaling pathway; hsa04360:Axon guidance; hsa04810:Regulation of actin cytoskeleton	R-HSA-202433: Generation of second messenger molecules; R-HSA-376176: Signaling by ROBO receptors	.	Q8N8S7
TTB30LE	Endoglin CD105 (ENG)	P17813	EGLN_HUMAN	.	Endoglin; END; CD105	ENG	"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."	.	5I04; 5HZW; 5HZV	MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTYTTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVLSVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPITSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLEGVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLIDANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPLASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKELVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNILSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSEFLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPIPKTGTLSCTVALRPKTGSQDQEVHRTVFMRLNIISPDLSGCTSKGLVLPAVLGITFGAFLIGALLTAALWYIYSHTRSPSKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA	Clinical trial	An open-label phase Ib dose-escalation study of TRC105 (anti-endoglin antibody) with bevacizumab in patients with advanced cancer. Clin Cancer Res. 2014 Dec 1;20(23):5918-26.	21	.	.	.	.	.	Zona pellucida-like domain	PF00100	PF00100; Zona_pellucida	.	.	.	.	.	P17813
TTUJZRL	Tumor-associated hydroquinone oxidase (tNOX)	Q16206	ENOX2_HUMAN	.	Tumorassociated hydroquinone oxidase; Protein disulfidethiol oxidoreductase; EctoNOX disulfidethiol exchanger 2; Ecto-NOX disulfide-thiol exchanger 2; Cytosolic ovarian carcinoma antigen 1; COVA1; APK1 antigen	ENOX2	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.	.	.	MQRDFRWLWVYEIGYAADNSRTLNVDSTAMTLPMSDPTAWATAMNNLGMAPLGIAGQPILPDFDPALGMMTGIPPITPMMPGLGIVPPPIPPDMPVVKEIIHCKSCTLFPPNPNLPPPATRERPPGCKTVFVGGLPENGTEQIIVEVFEQCGEIIAIRKSKKNFCHIRFAEEYMVDKALYLSGYRIRLGSSTDKKDTGRLHVDFAQARDDLYEWECKQRMLAREERHRRRMEEERLRPPSPPPVVHYSDHECSIVAEKLKDDSKFSEAVQTLLTWIERGEVNRRSANNFYSMIQSANSHVRRLVNEKAAHEKDMEEAKEKFKQALSGILIQFEQIVAVYHSASKQKAWDHFTKAQRKNISVWCKQAEEIRNIHNDELMGIRREEEMEMSDDEIEEMTETKETEESALVSQAEALKEENDSLRWQLDAYRNEVELLKQEQGKVHREDDPNKEQQLKLLQQALQGMQQHLLKVQEEYKKKEAELEKLKDDKLQVEKMLENLKEKESCASRLCASNQDSEYPLEKTMNSSPIKSEREALLVGIISTFLHVHPFGASIEYICSYLHRLDNKICTSDVECLMGRLQHTFKQEMTGVGASLEKRWKFCGFEGLKLT	Literature-reported	Update on a tumor-associated NADH oxidase in gastric cancer cell growth. World J Gastroenterol. 2016 Mar 14;22(10):2900-5.	.	.	.	ENOX family.	1.-.-.-	Oxidoreductases	"RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)"	PF00076	PF00076; RRM_1	.	.	.	.	.	Q16206
TT9PBIL	Glutamyl aminopeptidase (ENPEP)	Q07075	AMPE_HUMAN	Peptidase	ENPEP; EAP; Differentiation antigen gp160; Aminopeptidase A; APA	ENPEP	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.	EC 3.4.11.7	4KXD; 4KXC; 4KXB; 4KXA; 4KX9	MNFAEREGSKRYCIQTKHVAILCAVVVGVGLIVGLAVGLTRSCDSSGDGGPGTAPAPSHLPSSTASPSGPPAQDQDICPASEDESGQWKNFRLPDFVNPVHYDLHVKPLLEEDTYTGTVSISINLSAPTRYLWLHLRETRITRLPELKRPSGDQVQVRRCFEYKKQEYVVVEAEEELTPSSGDGLYLLTMEFAGWLNGSLVGFYRTTYTENGQVKSIVATDHEPTDARKSFPCFDEPNKKATYTISITHPKEYGALSNMPVAKEESVDDKWTRTTFEKSVPMSTYLVCFAVHQFDSVKRISNSGKPLTIYVQPEQKHTAEYAANITKSVFDYFEEYFAMNYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYDPKESASSNQQRVATVVAHELVHQWFGNIVTMDWWEDLWLNEGFASFFEFLGVNHAETDWQMRDQMLLEDVLPVQEDDSLMSSHPIIVTVTTPDEITSVFDGISYSKGSSILRMLEDWIKPENFQKGCQMYLEKYQFKNAKTSDFWAALEEASRLPVKEVMDTWTRQMGYPVLNVNGVKNITQKRFLLDPRANPSQPPSDLGYTWNIPVKWTEDNITSSVLFNRSEKEGITLNSSNPSGNAFLKINPDHIGFYRVNYEVATWDSIATALSLNHKTFSSADRASLIDDAFALARAQLLDYKVALNLTKYLKREENFLPWQRVISAVTYIISMFEDDKELYPMIEEYFQGQVKPIADSLGWNDAGDHVTKLLRSSVLGFACKMGDREALNNASSLFEQWLNGTVSLPVNLRLLVYRYGMQNSGNEISWNYTLEQYQKTSLAQEKEKLLYGLASVKNVTLLSRYLDLLKDTNLIKTQDVFTVIRYISYNSYGKNMAWNWIQLNWDYLVNRYTLNNRNLGRIVTIAEPFNTELQLWQMESFFAKYPQAGAGEKPREQVLETVKNNIEWLKQHRNTIREWFFNLLESG	Clinical trial	"Clinical pipeline report, company report or official report of Quantum Genomics."	21	.	.	.	.	.	.	.	.	.	.	hsa04614:Renin-angiotensin system	R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins	.	Q07075
TTZTIWS	Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 (ENPP1)	P22413	ENPP1_HUMAN	.	E-NPP 1; Membrane component chromosome 6 surface marker 1; Phosphodiesterase I/nucleotide pyrophosphatase 1; Plasma-cell membrane glycoprotein PC-1	ENPP1	"Nucleotide pyrophosphatase that generates diphosphate (PPi) and functions in bone mineralization and soft tissue calcification by regulating pyrophosphate levels (By similarity). PPi inhibits bone mineralization and soft tissue calcification by binding to nascent hydroxyapatite crystals, thereby preventing further growth of these crystals (PubMed:11004006). Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP and UTP to their corresponding monophosphates with release of pyrophosphate, as well as diadenosine polyphosphates, and also 3',5'-cAMP to AMP (PubMed:27467858, PubMed:8001561, PubMed:25344812, PubMed:28011303, PubMed:35147247). May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling (PubMed:27467858, PubMed:8001561). Inhibits ectopic joint calcification and maintains articular chondrocytes by repressing hedgehog signaling; it is however unclear whether hedgehog inhibition is direct or indirect (By similarity). Appears to modulate insulin sensitivity and function (PubMed:10615944). Also involved in melanogenesis (PubMed:28964717). Also able to hydrolyze 2',3'-cGAMP (cyclic GMP-AMP), a second messenger that activates TMEM173/STING and triggers type-I interferon production (PubMed:25344812). 2',3'-cGAMP degradation takes place in the lumen or extracellular space, and not in the cytosol where it is produced; the role of 2',3'-cGAMP hydrolysis is therefore unclear (PubMed:25344812). Not able to hydrolyze the 2',3'-cGAMP linkage isomer 3'-3'-cGAMP (PubMed:25344812). {ECO:0000250|UniProtKB:P06802, ECO:0000269|PubMed:10615944, ECO:0000269|PubMed:25344812, ECO:0000269|PubMed:27467858, ECO:0000269|PubMed:28011303, ECO:0000269|PubMed:28964717, ECO:0000269|PubMed:35147247, ECO:0000269|PubMed:8001561, ECO:0000305|PubMed:11004006}."	EC 3.1.4.1; EC 3.6.1.9	2YS0;6WET;6WEU;6WEV;6WEW;6WFJ	MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPLEKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNCRCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINYSSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKKCGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEWYKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLPKDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLILISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSCREPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNVFSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVYTPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYGRPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPLSPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTLLRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKDTSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSFYQQRKEPVSDILKLKTHLPTFSQED	Clinical trial	"Clinical pipeline report, company report or official report of Inozyme pharma"	.	.	.	.	.	.	.	.	.	.	.	hsa:5167	R-HSA-196843;R-HSA-199220;	.	P22413;
TTSCIM2	Extracellular lysophospholipase D (E-NPP2)	Q13822	ENPP2_HUMAN	Phosphoric diester hydrolase	LysoPLD; Ectonucleotide pyrophosphatase/phosphodiesterase family member 2; E-NPP 2; Autotaxin; ATX	ENPP2	"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."	EC 3.1.4.39	5MHP; 5M7M; 5KXA; 4ZGA; 4ZG9	MARRSSFQSCQIISLFTFAVGVNICLGFTAHRIKRAEGWEEGPPTVLSDSPWTNISGSCKGRCFELQEAGPPDCRCDNLCKSYTSCCHDFDELCLKTARGWECTKDRCGEVRNEENACHCSEDCLARGDCCTNYQVVCKGESHWVDDDCEEIKAAECPAGFVRPPLIIFSVDGFRASYMKKGSKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDATFHLRGREKFNHRWWGGQPLWITATKQGVKAGTFFWSVVIPHERRILTILQWLTLPDHERPSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDHGMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRSKFSNNAKYDPKAIIANLTCKKPDQHFKPYLKQHLPKRLHYANNRRIEDIHLLVERRWHVARKPLDVYKKPSGKCFFQGDHGFDNKVNSMQTVFVGYGSTFKYKTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTFRPTMPEEVTRPNYPGIMYLQSDFDLGCTCDDKVEPKNKLDELNKRLHTKGSTEERHLLYGRPAVLYRTRYDILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDHLTSCVRPDVRVSPSFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWNYFQRVLVKKYASERNGVNVISGPIFDYDYDGLHDTEDKIKQYVEGSSIPVPTHYYSIITSCLDFTQPADKCDGPLSVSSFILPHRPDNEESCNSSEDESKWVEELMKMHTARVRDIEHLTSLDFFRKTSRSYPEILTLKTYLHTYESEI	Patented-recorded	Autotaxin inhibitors: a patent review (2012-2016).Expert Opin Ther Pat. 2017 Jul;27(7):815-829.	15.5	EC:3.1.4	Nucleotide pyrophosphatase/phosphodiesterase family	nucleotide pyrophosphatase/phosphodiesterase family.	3.1.4.39 	Acting on ester bonds	DNA/RNA non-specific endonuclease; Type I phosphodiesterase / nucleotide pyrophosphatase; Somatomedin B domain	PF01223; PF01663; PF01033	PF01223; Endonuclease_NS; PF01663; Phosphodiest; PF01033; Somatomedin_B	.	.	hsa00565:Ether lipid metabolism	R-HSA-199220: Vitamin B5 (pantothenate) metabolism	MetaCyc:HS06258-MON	Q13822
TTD4TKP	Phosphodiesterase I beta (ENPP3)	O14638	ENPP3_HUMAN	Phosphoric diester hydrolase	Phosphodiesterase I/nucleotide pyrophosphatase 3; PDNP3; PD-Ibeta; NPP3; Ectonucleotide pyrophosphatase/phosphodiesterase family member 3; E-NPP 3; CD203c	ENPP3	"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."	.	6C02; 6C01	MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFDASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCLQRKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTLMPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLSSKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERISTLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRNLHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNSEEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGGGNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLNHLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEITATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPTVPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEEFRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHYFVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVRDVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	EC:3.1.4	.	nucleotide pyrophosphatase/phosphodiesterase family.	3.1.4.1 	Acting on ester bonds	DNA/RNA non-specific endonuclease; Type I phosphodiesterase / nucleotide pyrophosphatase; Somatomedin B domain	PF01223; PF01663; PF01033	PF01223; Endonuclease_NS; PF01663; Phosphodiest; PF01033; Somatomedin_B	.	.	hsa00230: Purine metabolism; hsa00240: Pyrimidine metabolism; hsa00500: Starch and sucrose metabolism; hsa00740: Riboflavin metabolism; hsa00760: Nicotinate and nicotinamide metabolism; hsa00770: Pantothenate and CoA biosynthesis; hsa01100: Metabolic pathways; hsa01232: Nucleotide metabolism	R-HSA-199220: Vitamin B5 (pantothenate) metabolism	.	O14638
TTQD0YT	Alpha-endosulfine (ENSA)	O43768	ENSA_HUMAN	Endosulfine family	ENSA; ARPP19e	ENSA	"Endogenous ligand for sulfonylurea receptor. By inhibitingsulfonylurea from binding to the receptor, it reduces k(atp) channel currents and thereby stimulates insulin secretion."	.	.	MSQKQEEENPAEETGEEKQDTQEKEGILPERAEEAKLKAKYPSLGQKPGGSDFLMKRLQKGQKYFDSGDYNMAKAKMKNKQLPSAGPDKNLVTGDHIPTPQDLPQRKSSLVTSKLAGGQVE	Literature-reported	Brain alpha-endosulfine is manifold decreased in brains from patients with Alzheimer's disease: a tentative marker and drug target Neurosci Lett. 2001 Sep 14;310(2-3):77-80.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2465910: MASTL Facilitates Mitotic Progression	.	O43768
TTJS7O4	Entamoeba Alcohol dehydrogenase 2 (Entamo ADH2)	Q24803	ADH2_ENTHI	CH-OH donor oxidoreductase	Aldehydealcohol dehydrogenase 2; Aldehyde-alcohol dehydrogenase 2; Alcohol dehydrogenase; ADH; ACDH	Entamo ADH2	May be a critical enzyme in the fermentative pathway. This enzyme has two NAD(+)-dependent activities: ADH and ACDH.	.	.	MSTQQTMTVDEHINQLVRKAQVALKEYLKPEYTQEKIDYIVKKASVAALDQHCALAAAAVEETGRGIFEDKATKNIFACEHVTHEMRHAKTVGIINVDPLYGITEIAEPVGVVCGVTPVTNPTSTAIFKSLISIKTRNPIVFSFHPSALKCSIMAAKIVRDAAIAAGAPENCIQWIEFGGIEASNKLMNHPGVATILATGGNAMVKAAYSSGKPALGVGAGNVPTYIEKTCNIKQAANDVVMSKSFDNGMICASEQAAIIDKEIYDQVVEEMKTLGAYFINEEEKAKLEKFMFGVNAYSADVNNARLNPKCPGMSPQWFAEQVGIKVPEDCNIICAVCKEVGPNEPLTREKLSPVLAILKAENTQDGIDKAEAMVEFNGRGHSAAIHSNDKAVVEKYALTMKACRILHNTPSSQGGIGSIYNYIWPSFTLGCGSYGGNSVSANVTYHNLLNIKRLADRRNNLQWFRVPPKIFFEPHSIRYLAELKELSKIFIVSDRMMYKLGYVDRVMDVLKRRSNEVEIEIFIDVEPDPSIQTVQKGLAVMNTFGPDNIIAIGGGSAMDAAKIMWLLYEHPEADFFAMKQKFIDLRKRAFKFPTMGKKARLICIPTTSGTGSEVTPFAVISDHETGKKYPLADYSLTPSVAIVDPMFTMSLPKRAIADTGLDVLVHATEAYVSVMANEYTDGLAREAVKLVFENLLKSYNGDLEAREKMHNAATIAGMAFASAFLGMDHSMAHKVGAAFHLPHGRCVAVLLPHVIRYNGQKPRKLAMWPKYNFYKADQRYMELAQMVGLKCNTPAEGVEAFAKACEELMKATETITGFKKANIDEAAWMSKVPEMALLAFEDQCSPANPRVPMVKDMEKILKAAYYPIA	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	EC:1.1	Short-chain dehydrogenases reductases	.	1.1.1.1 	Acting on the CH-OH group of donors	Aldehyde dehydrogenase family; Iron-containing alcohol dehydrogenase 	PF00171; PF00465	PF00171; Aldedh; PF00465; Fe-ADH	.	.	hsa00010:Glycolysis / Gluconeogenesis; hsa00040:Pentose and glucuronate interconversions; hsa00561:Glycerolipid metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01220:Degradation of aromatic compounds	.	.	Q24803
TTRV7FQ	Enterobacteria Shiga-like toxin 2B (EntBac stxB2)	P09386	STXB_BP933	Shiga-like toxin beta	stxB2; Verotoxin 2 subunit B; Verocytotoxin 2 subunit B; Shiga-like toxin 2 subunit B; SLT-IIb; SLT-2b; SLT-2 B subunit	EntBac stxB2	"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."	.	6FE4; 2GA4; 1R4P	MKKMFMAVLFALASVNAMAADCAKGKIEFSKYNEDDTFTVKVDGKEYWTSRWNLQPLLQSAQLTGMTVTIKSSTCESGSGFAEVQFNND	Discontinued	"Safety and pharmacokinetics of urtoxazumab, a humanized monoclonal antibody, against Shiga-like toxin 2 in healthy adults and in pediatric patients infected with Shiga-like toxin-producing Escherichia coli. Antimicrob Agents Chemother. 2010 Jan;54(1):239-43."	5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZXI0P	Enterococcus fsrC (Ente-cocc fsrC)	C3VD18	C3VD18_ENTFC	.	.	Ente-cocc fsrC	.	.	.	MILSLLATNVLLVSSFIVFVFLRVTLIKIECKIPLLSLLIVINLCSFAALMLGYSWLIYALTVVVFTGFLLIHKKRFSIFKAIFLSVFTLLMVSFINYTEQTILSVFFQQIYQNKLLWIASNVLLLLINIWIALKIPNSVFLRLNRVLENSRIFFGCLLLLLILLLLFVFLISPEISPDFMRGFVTVNSSKLELLISVGLFLILIGLVIEAYLEEQRINTQLLNNLTIYTEKIESINEELAMFRHDYKNLLYSLQIAISYEDILEIKRIYEETIAPTKKIIDNEEFELMKLNRLKNMELKALISMKINTAKQAKLKVIVDVPEVFILDTSIDLVVVIRLLAILLDNAIENSAKSELKMFAISIFNKNETQEFVITNSVQAEFDFKVMKKTKFSSKSNPEEHGWGLLYVKEIVDFSDQFDLQTSFNEGAVTQHLIIEKNHNSKKVVNE	Preclinical	Different drugs for bad bugs: antivirulence strategies in the age of antibiotic resistance. Nat Rev Drug Discov. 2017 Jul;16(7):457-471.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYM8DJ	Ectonucleoside triphosphate diphosphohydrolase 1 (CD39)	P49961	ENTP1_HUMAN	Acid anhydride hydrolase	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	ENTPD1	"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."	EC 3.6.1.5	.	MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHTSLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQHQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWITINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFRLYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTPCTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAFSAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYILSLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFLMVLFSLVLFTVAIIGLLIFHKPSYFWKDMV	Clinical trial	Selective nucleoside triphosphate diphosphohydrolase-2 (NTPDase2) inhibitors: nucleotide mimetics derived from uridine-5'-carboxamide. J Med Chem. 2008 Aug 14;51(15):4518-28.	0	EC:3.6	Acid anhydrides hydrolase	GDA1/CD39 NTPase family.	3.6.1.5	Acting on acid anhydrides	GDA1/CD39 (nucleoside phosphatase) family	PF01150	PF01150; GDA1_CD39	.	.	hsa00230:Purine metabolism; hsa00240:Pyrimidine metabolism; hsa05169:Epstein-Barr virus infection	R-HSA-8850843: Phosphate bond hydrolysis by NTPDase proteins; R-HSA-9660826: Purinergic signaling in leishmaniasis infection	MetaCyc:HS06471-MON	P49961
TT7ES5I	Ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3)	O75355	ENTP3_HUMAN	.	NTPDase 3; CD39 antigen-like 3; Ecto-ATP diphosphohydrolase 3; Ecto-ATPDase 3; Ecto-ATPase 3; Ecto-apyrase 3; HB6	ENTPD3	"Has a threefold preference for the hydrolysis of ATP over ADP. {ECO:0000269|PubMed:10231536, ECO:0000269|PubMed:11300774}."	EC 3.6.1.5	.	MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIVLDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKVKGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQEEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTSDIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTMGHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQPKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARSYCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRLPIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD	Clinical trial	"Clinical pipeline report, company report or official report of AstraZeneca"	.	.	.	.	.	.	.	.	.	.	.	hsa:956	R-HSA-8850843;	.	O75355;
TTGH73N	Histone acetyltransferase p300 (EP300)	Q09472	EP300_HUMAN	Acyltransferase	p300 HAT; Protein propionyltransferase p300; P300; Histone crotonyltransferase p300; Histone butyryltransferase p300; E1Aassociated protein p300; E1A-associated protein p300	EP300	"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."	EC 2.3.1.48	6GYT; 6GYR; 6FGS; 6FGN; 6DS6	MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDINQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMPNMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQMPTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQNPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSMAQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTPTPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPSLPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSSTEVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELKTEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHLEPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNSDLNSNLSQSTLDIH	Clinical trial	"Tumour suppressor EP300, a modulator of paclitaxel resistance and stemness, is downregulated in metaplastic breast cancer. Breast Cancer Res Treat. 2017 Jun;163(3):461-474."	.	EC:2.3	Acyltransferase	.	2.3.1.48 	Acyltransferases	"Bromodomain; Creb binding; Domain of Unknown Function (DUF902); Histone acetylation protein; KIX domain; TAZ zinc finger; Zinc finger, ZZ type"	PF00439; PF09030; PF06001; PF08214; PF02172; PF02135; PF00569	PF00439; Bromodomain; PF09030; Creb_binding; PF06001; DUF902; PF08214; HAT_KAT11; PF02172; KIX; PF02135; zf-TAZ; PF00569; ZZ	.	.	"hsa03250: Viral life cycle - HIV-1; 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; hsa04935: Growth hormone synthesis, secretion and action; hsa05016: Huntington disease; hsa05152: Tuberculosis; hsa05161: Hepatitis B; hsa05164: Influenza A; hsa05165: Human papillomavirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05200: Pathways in cancer; hsa05203: Viral carcinogenesis; hsa05206: MicroRNAs in cancer; hsa05211: Renal cell carcinoma; hsa05215: Prostate cancer"	R-HSA-1234158: Regulation of gene expression by Hypoxia-inducible Factor; R-HSA-1368082: RORA activates 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-210744: Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells; R-HSA-2122947: NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2197563: NOTCH2 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-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-3899300: SUMOylation of transcription cofactors; R-HSA-400253: Circadian Clock; R-HSA-5250924: B-WICH complex positively regulates rRNA expression; R-HSA-5617472: Activation of anterior HOX genes in hindbrain development during early embryogenesis; R-HSA-5621575: CD209 (DC-SIGN) signaling; R-HSA-5689901: Metalloprotease DUBs; R-HSA-6781823: Formation of TC-NER Pre-Incision Complex; R-HSA-6781827: Transcription-Coupled Nucleotide Excision Repair (TC-NER); R-HSA-6782135: Dual incision in TC-NER; R-HSA-6782210: Gap-filling DNA repair synthesis and ligation in TC-NER; R-HSA-6804114: TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest; R-HSA-6804758: Regulation of TP53 Activity through Acetylation; R-HSA-6804760: Regulation of TP53 Activity through Methylation; R-HSA-6811555: PI5P Regulates TP53 Acetylation; R-HSA-8866907: Activation of the TFAP2 (AP-2) family of transcription factors; R-HSA-8936459: RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function; R-HSA-8939243: RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known; R-HSA-8941856: RUNX3 regulates NOTCH signaling; R-HSA-8941858: Regulation of RUNX3 expression and activity; R-HSA-8951936: RUNX3 regulates p14-ARF; R-HSA-9013508: NOTCH3 Intracellular Domain Regulates Transcription; R-HSA-9013695: NOTCH4 Intracellular Domain Regulates Transcription; R-HSA-9018519: Estrogen-dependent gene expression; R-HSA-9029569: NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux; R-HSA-9031628: NGF-stimulated transcription; R-HSA-918233: TRAF3-dependent IRF activation pathway; R-HSA-933541: TRAF6 mediated IRF7 activation; R-HSA-9614657: FOXO-mediated transcription of cell death genes; R-HSA-9616222: Transcriptional regulation of granulopoiesis; R-HSA-9617629: Regulation of FOXO transcriptional activity by acetylation; R-HSA-9701898: STAT3 nuclear events downstream of ALK signaling; R-HSA-9707616: Heme signaling; R-HSA-9759194: Nuclear events mediated by NFE2L2	.	Q09472
TTWPA54	HIF2-alpha messenger RNA (EPAS1 mRNA)	Q99814	EPAS1_HUMAN	mRNA target	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	EPAS1	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).	.	6D0C; 6D0B; 6D09; 6CZW; 6BVB	MTADKEKKRSSSERRKEKSRDAARCRRSKETEVFYELAHELPLPHSVSSHLDKASIMRLAISFLRTHKLLSSVCSENESEAEADQQMDNLYLKALEGFIAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENLSLKNGSGFGKKSKDMSTERDFFMRMKCTVTNRGRTVNLKSATWKVLHCTGQVKVYNNCPPHNSLCGYKEPLLSCLIIMCEPIQHPSHMDIPLDSKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLETQGTVIYNPRNLQPQCIMCVNYVLSEIEKNDVVFSMDQTESLFKPHLMAMNSIFDSSGKGAVSEKSNFLFTKLKEEPEELAQLAPTPGDAIISLDFGNQNFEESSAYGKAILPPSQPWATELRSHSTQSEAGSLPAFTVPQAAAPGSTTPSATSSSSSCSTPNSPEDYYTSLDNDLKIEVIEKLFAMDTEAKDQCSTQTDFNELDLETLAPYIPMDGEDFQLSPICPEERLLAENPQSTPQHCFSAMTNIFQPLAPVAPHSPFLLDKFQQQLESKKTEPEHRPMSSIFFDAGSKASLPPCCGQASTPLSSMGGRSNTQWPPDPPLHFGPTKWAVGDQRTEFLGAAPLGPPVSPPHVSTFKTRSAKGFGARGPDVLSPAMVALSNKLKLKRQLEYEEQAFQDLSGGDPPGGSTSHLMWKRMKNLRGGSCPLMPDKPLSANVPNDKFTQNPMRGLGHPLRHLPLPQPPSAISPGENSKSRFPPQCYATQYQDYSLSSAHKVSGMASRLLGPSFESYLLPELTRYDCEVNVPVLGSSTLLQGGDLLRALDQAT	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	mRNA	mRNA target	.	.	.	Hypoxia-inducible factor-1; HIF-1 alpha C terminal transactivation domain; PAS fold; PAS fold	PF11413; PF08778; PF00989; PF08447	PF11413; HIF-1; PF08778; HIF-1a_CTAD; PF00989; PAS; PF08447; PAS_3	.	.	hsa05200:Pathways in cancer; hsa05211:Renal cell carcinoma	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	.	Q99814
TTDMLNT	Hypoxia-inducible factor 2 alpha (HIF-2A)	Q99814	EPAS1_HUMAN	.	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	EPAS1	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.	.	6D0C; 6D0B; 6D09; 6CZW; 6BVB	MTADKEKKRSSSERRKEKSRDAARCRRSKETEVFYELAHELPLPHSVSSHLDKASIMRLAISFLRTHKLLSSVCSENESEAEADQQMDNLYLKALEGFIAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENLSLKNGSGFGKKSKDMSTERDFFMRMKCTVTNRGRTVNLKSATWKVLHCTGQVKVYNNCPPHNSLCGYKEPLLSCLIIMCEPIQHPSHMDIPLDSKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLETQGTVIYNPRNLQPQCIMCVNYVLSEIEKNDVVFSMDQTESLFKPHLMAMNSIFDSSGKGAVSEKSNFLFTKLKEEPEELAQLAPTPGDAIISLDFGNQNFEESSAYGKAILPPSQPWATELRSHSTQSEAGSLPAFTVPQAAAPGSTTPSATSSSSSCSTPNSPEDYYTSLDNDLKIEVIEKLFAMDTEAKDQCSTQTDFNELDLETLAPYIPMDGEDFQLSPICPEERLLAENPQSTPQHCFSAMTNIFQPLAPVAPHSPFLLDKFQQQLESKKTEPEHRPMSSIFFDAGSKASLPPCCGQASTPLSSMGGRSNTQWPPDPPLHFGPTKWAVGDQRTEFLGAAPLGPPVSPPHVSTFKTRSAKGFGARGPDVLSPAMVALSNKLKLKRQLEYEEQAFQDLSGGDPPGGSTSHLMWKRMKNLRGGSCPLMPDKPLSANVPNDKFTQNPMRGLGHPLRHLPLPQPPSAISPGENSKSRFPPQCYATQYQDYSLSSAHKVSGMASRLLGPSFESYLLPELTRYDCEVNVPVLGSSTLLQGGDLLRALDQAT	Clinical trial	Hypoxia-inducible factor 2: a novel target in gliomas.Future Med Chem. 2018 Sep 1;10(18):2227-2236. 	21	.	.	.	.	.	Hypoxia-inducible factor-1; HIF-1 alpha C terminal transactivation domain; PAS fold; PAS fold	PF11413; PF08778; PF00989; PF08447	PF11413; HIF-1; PF08778; HIF-1a_CTAD; PF00989; PAS; PF08447; PAS_3	.	.	hsa05200:Pathways in cancer; hsa05211:Renal cell carcinoma	R-HSA-1234158: Regulation of gene expression by Hypoxia-inducible Factor; R-HSA-1234174: Cellular response to hypoxia; R-HSA-1234176: Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha; R-HSA-452723: Transcriptional regulation of pluripotent stem cells; R-HSA-8849473: PTK6 Expression; R-HSA-8951664: Neddylation; R-HSA-9664873: Pexophagy	.	Q99814
TTZ8WH4	Tumor-associated calcium signal transducer 1 (EPCAM)	P16422	EPCAM_HUMAN	.	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	EPCAM	"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."	.	6I07; 4MZV	MAPPQVLAFGLLLAAATATFAAAQEECVCENYKLAVNCFVNNNRQCQCTSVGAQNTVICSKLAAKCLVMKAEMNGSKLGRRAKPEGALQNNDGLYDPDCDESGLFKAKQCNGTSMCWCVNTAGVRRTDKDTEITCSERVRTYWIIIELKHKAREKPYDSKSLRTALQKEITTRYQLDPKFITSILYENNVITIDLVQNSSQKTQNDVDIADVAYYFEKDVKGESLFHSKKMDLTVNGEQLDLDPGQTLIYYVDEKAPEFSMQGLKAGVIAVIVVVVIAVVAGIVVLVISRKKRMAKYEKAEIKEMGEMHRELNA	Clinical trial	A bispecific EpCAM/CD133 targeted toxin is effective against carcinoma. Target Oncol. 2014 September; 9(3): 239-249.	24	.	.	EPCAM family.	.	.	Epithelial cell adhesion molecule N-terminal domain; Thyroglobulin type-1 repeat	PF18635; PF00086	PF18635; EpCAM_N; PF00086; Thyroglobulin_1	.	.	.	R-HSA-202733: Cell surface interactions at the vascular wall	.	P16422
TTLFZVU	Ephrin type-A receptor 1 (EPHA1)	P21709	EPHA1_HUMAN	Kinase	hEpha1; Tyrosine-protein kinase receptor EPH; Erythropoietin-producing hepatoma receptor; EPHT1; EPHT; EPH tyrosine kinase 1; EPH tyrosine kinase; EPH	EPHA1	"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."	EC 2.7.10.1	3KKA; 3HIL; 2K1L; 2K1K	MERRWPLGLGLVLLLCAPLPPGARAKEVTLMDTSKAQGELGWLLDPPKDGWSEQQQILNGTPLYMYQDCPMQGRRDTDHWLRSNWIYRGEEASRVHVELQFTVRDCKSFPGGAGPLGCKETFNLLYMESDQDVGIQLRRPLFQKVTTVAADQSFTIRDLVSGSVKLNVERCSLGRLTRRGLYLAFHNPGACVALVSVRVFYQRCPETLNGLAQFPDTLPGPAGLVEVAGTCLPHARASPRPSGAPRMHCSPDGEWLVPVGRCHCEPGYEEGGSGEACVACPSGSYRMDMDTPHCLTCPQQSTAESEGATICTCESGHYRAPGEGPQVACTGPPSAPRNLSFSASGTQLSLRWEPPADTGGRQDVRYSVRCSQCQGTAQDGGPCQPCGVGVHFSPGARGLTTPAVHVNGLEPYANYTFNVEAQNGVSGLGSSGHASTSVSISMGHAESLSGLSLRLVKKEPRQLELTWAGSRPRSPGANLTYELHVLNQDEERYQMVLEPRVLLTELQPDTTYIVRVRMLTPLGPGPFSPDHEFRTSPPVSRGLTGGEIVAVIFGLLLGAALLLGILVFRSRRAQRQRQQRQRDRATDVDREDKLWLKPYVDLQAYEDPAQGALDFTRELDPAWLMVDTVIGEGEFGEVYRGTLRLPSQDCKTVAIKTLKDTSPGGQWWNFLREATIMGQFSHPHILHLEGVVTKRKPIMIITEFMENGALDAFLREREDQLVPGQLVAMLQGIASGMNYLSNHNYVHRDLAARNILVNQNLCCKVSDFGLTRLLDDFDGTYETQGGKIPIRWTAPEAIAHRIFTTASDVWSFGIVMWEVLSFGDKPYGEMSNQEVMKSIEDGYRLPPPVDCPAPLYELMKNCWAYDRARRPHFQKLQAHLEQLLANPHSLRTIANFDPRMTLRLPSLSGSDGIPYRTVSEWLESIRMKRYILHFHSAGLDTMECVLELTAEDLTQMGITLPGHQKRILCSIQGFKD	Literature-reported	Structure-based optimization of potent and selective inhibitors of the tyrosine kinase erythropoietin producing human hepatocellular carcinoma receptor B4 (EphB4). J Med Chem. 2009 Oct 22;52(20):6433-46.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Ephrin type-A receptor 2 transmembrane domain; Ephrin receptor ligand binding domain; Fibronectin type III domain; Protein tyrosine kinase; SAM domain (Sterile alpha motif)	PF14575; PF01404; PF00041; PF07714; PF00536	PF14575; EphA2_TM; PF01404; Ephrin_lbd; PF00041; fn3; PF07714; Pkinase_Tyr; PF00536; SAM_1	.	.	hsa04360: Axon guidance	"R-HSA-2682334: EPH-Ephrin signaling; R-HSA-2892247: POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation; R-HSA-3928663: EPHA-mediated growth cone collapse; R-HSA-3928665: EPH-ephrin mediated repulsion of cells"	.	P21709
TTRJB2G	Ephrin type-A receptor 2 (EPHA2)	P29317	EPHA2_HUMAN	Kinase	Tyrosine-protein kinase receptor ECK; Epithelial cell kinase; EphA2receptor; ECK	EPHA2	"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."	EC 2.7.10.1	6NKP; 6NK2; 6NK1; 6NK0; 6NJZ	MELQAARACFALLWGCALAAAAAAQGKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNIMNDMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPPGGEEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTLPSPEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGREDIVYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGVSGLVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGDSNSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGNLAVIGGVAVGVVLLLVLAGVGFFIHRRRKNQRARQSPEDVYFSKSEQLKPLKTYVDPHTYEDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSGSEGVPFRTVSEWLESIKMQQYTEHFMAAGYTAIEKVVQMTNDDIKRIGVRLPGHQKRIAYSLLGLKDQVNTVGIPI	Clinical trial	ClinicalTrials.gov (NCT02575261) CAR-T Cell Immunotherapy for EphA2 Positive Malignant Glioma Patients	19	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Ephrin type-A receptor 2 transmembrane domain; Ephrin receptor ligand binding domain; Fibronectin type III domain; Protein tyrosine kinase; SAM domain (Sterile alpha motif)	PF14575; PF01404; PF00041; PF07714; PF00536	PF14575; EphA2_TM; PF01404; Ephrin_lbd; PF00041; fn3; PF07714; Pkinase_Tyr; PF00536; SAM_1	.	.	hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04360:Axon guidance	R-HSA-2682334:EPH-Ephrin signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-3928665:EPH-ephrin mediated repulsion of cells	.	P29317
TTHS2LR	Ephrin type-A receptor 3 (EPHA3)	P29320	EPHA3_HUMAN	Kinase	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	EPHA3	"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."	EC 2.7.10.1	4TWO; 4TWN; 4P5Z; 4P5Q; 4P4C	MDCQLSILLLLSCSVLDSFGELIPQPSNEVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGACVALVSVRVYFKKCPFTVKNLAMFPDTVPMDSQSLVEVRGSCVNNSKEEDPPRMYCSTEGEWLVPIGKCSCNAGYEERGFMCQACRPGFYKALDGNMKCAKCPPHSSTQEDGSMNCRCENNYFRADKDPPSMACTRPPSSPRNVISNINETSVILDWSWPLDTGGRKDVTFNIICKKCGWNIKQCEPCSPNVRFLPRQFGLTNTTVTVTDLLAHTNYTFEIDAVNGVSELSSPPRQFAAVSITTNQAAPSPVLTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRARGTNVTISSLKPDTIYVFQIRARTAAGYGTNSRKFEFETSPDSFSISGESSQVVMIAISAAVAIILLTVVIYVLIGRFCGYKSKHGADEKRLHFGNGHLKLPGLRTYVDPHTYEDPTQAVHEFAKELDATNISIDKVVGAGEFGEVCSGRLKLPSKKEISVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIRLEGVVTKSKPVMIVTEYMENGSLDSFLRKHDAQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTSPEAIAYRKFTSASDVWSYGIVLWEVMSYGERPYWEMSNQDVIKAVDEGYRLPPPMDCPAALYQLMLDCWQKDRNNRPKFEQIVSILDKLIRNPGSLKIITSAAARPSNLLLDQSNVDITTFRTTGDWLNGVWTAHCKEIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIISSIKALETQSKNGPVPV	Clinical trial	"Clinical pipeline report, company report or official report of Kalobios."	19	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Ephrin type-A receptor 2 transmembrane domain; Ephrin receptor ligand binding domain; Putative ephrin-receptor like ; Fibronectin type III domain; Protein tyrosine kinase; SAM domain (Sterile alpha motif)	PF14575; PF01404; PF07699; PF00041; PF07714; PF07647	PF14575; EphA2_TM; PF01404; Ephrin_lbd; PF07699; Ephrin_rec_like; PF00041; fn3; PF07714; Pkinase_Tyr; PF07647; SAM_2	.	.	hsa04360:Axon guidance	R-HSA-2682334:EPH-Ephrin signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-3928665:EPH-ephrin mediated repulsion of cells	.	P29320
TTG84D3	Ephrin type-A receptor 4 (EPHA4)	P54764	EPHA4_HUMAN	Kinase	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	EPHA4	"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."	EC 2.7.10.1	5JR2; 4W50; 4W4Z; 4M4R; 4M4P	MAGIFYFALFSCLFGICDAVTGSRVYPANEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKCPLTVRNLAQFPDTITGADTSSLVEVRGSCVNNSEEKDVPKMYCGADGEWLVPIGNCLCNAGHEERSGECQACKIGYYKALSTDATCAKCPPHSYSVWEGATSCTCDRGFFRADNDAASMPCTRPPSAPLNLISNVNETSVNLEWSSPQNTGGRQDISYNVVCKKCGAGDPSKCRPCGSGVHYTPQQNGLKTTKVSITDLLAHTNYTFEIWAVNGVSKYNPNPDQSVSVTVTTNQAAPSSIALVQAKEVTRYSVALAWLEPDRPNGVILEYEVKYYEKDQNERSYRIVRTAARNTDIKGLNPLTSYVFHVRARTAAGYGDFSEPLEVTTNTVPSRIIGDGANSTVLLVSVSGSVVLVVILIAAFVISRRRSKYSKAKQEADEEKHLNQGVRTYVDPFTYEDPNQAVREFAKEIDASCIKIEKVIGVGEFGEVCSGRLKVPGKREICVAIKTLKAGYTDKQRRDFLSEASIMGQFDHPNIIHLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFTVIQLVGMLRGIGSGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPPPMDCPIALHQLMLDCWQKERSDRPKFGQIVNMLDKLIRNPNSLKRTGTESSRPNTALLDPSSPEFSAVVSVGDWLQAIKMDRYKDNFTAAGYTTLEAVVHVNQEDLARIGITAITHQNKILSSVQAMRTQMQQMHGRMVPV	Literature-reported	"Product Pipeline Review of MedImmune, LLC in 2012."	2	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Ephrin type-A receptor 2 transmembrane domain; Ephrin receptor ligand binding domain; Fibronectin type III domain; Protein tyrosine kinase; SAM domain (Sterile alpha motif)	PF14575; PF01404; PF00041; PF07714; PF07647	PF14575; EphA2_TM; PF01404; Ephrin_lbd; PF00041; fn3; PF07714; Pkinase_Tyr; PF07647; SAM_2	.	.	hsa04360:Axon guidance	R-HSA-2682334:EPH-Ephrin signaling; R-HSA-3928663:EPHA-mediated growth cone collapse; R-HSA-3928665:EPH-ephrin mediated repulsion of cells	.	P54764
TTV9KOD	Ephrin type-A receptor 5 (EPHA5)	P54756	EPHA5_HUMAN	Kinase	hEK7; EPH-like kinase 7; EPH homology kinase 1; EK7; EHK1; EHK-1; Brain-specific kinase; BSK	EPHA5	"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."	EC 2.7.10.1	4ET7; 2R2P	MRGSGPRGAGRRRPPSGGGDTPITPASLAGCYSAPRRAPLWTCLLLCAALRTLLASPSNEVNLLDSRTVMGDLGWIAFPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWISNEGASRIFIELKFTLRDCNSLPGGLGTCKETFNMYYFESDDQNGRNIKENQYIKIDTIAADESFTELDLGDRVMKLNTEVRDVGPLSKKGFYLAFQDVGACIALVSVRVYYKKCPSVVRHLAVFPDTITGADSSQLLEVSGSCVNHSVTDEPPKMHCSAEGEWLVPIGKCMCKAGYEEKNGTCQVCRPGFFKASPHIQSCGKCPPHSYTHEEASTSCVCEKDYFRRESDPPTMACTRPPSAPRNAISNVNETSVFLEWIPPADTGGRKDVSYYIACKKCNSHAGVCEECGGHVRYLPRQSGLKNTSVMMVDLLAHTNYTFEIEAVNGVSDLSPGARQYVSVNVTTNQAAPSPVTNVKKGKIAKNSISLSWQEPDRPNGIILEYEIKYFEKDQETSYTIIKSKETTITAEGLKPASVYVFQIRARTAAGYGVFSRRFEFETTPVFAASSDQSQIPVIAVSVTVGVILLAVVIGVLLSGSCCECGCGRASSLCAVAHPSLIWRCGYSKAKQDPEEEKMHFHNGHIKLPGVRTYIDPHTYEDPNQAVHEFAKEIEASCITIERVIGAGEFGEVCSGRLKLPGKRELPVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIHLEGVVTKSKPVMIVTEYMENGSLDTFLKKNDGQFTVIQLVGMLRGISAGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAFRKFTSASDVWSYGIVMWEVVSYGERPYWEMTNQDVIKAVEEGYRLPSPMDCPAALYQLMLDCWQKERNSRPKFDEIVNMLDKLIRNPSSLKTLVNASCRVSNLLAEHSPLGSGAYRSVGEWLEAIKMGRYTEIFMENGYSSMDAVAQVTLEDLRRLGVTLVGHQKKIMNSLQEMKVQLVNGMVPL	Literature-reported	Structure-based optimization of potent and selective inhibitors of the tyrosine kinase erythropoietin producing human hepatocellular carcinoma receptor B4 (EphB4). J Med Chem. 2009 Oct 22;52(20):6433-46.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Ephrin type-A receptor 2 transmembrane domain; Ephrin receptor ligand binding domain; Fibronectin type III domain; Protein tyrosine kinase; SAM domain (Sterile alpha motif)	PF14575; PF01404; PF00041; PF07714; PF00536	PF14575; EphA2_TM; PF01404; Ephrin_lbd; PF00041; fn3; PF07714; Pkinase_Tyr; PF00536; SAM_1	.	.	hsa04360: Axon guidance	R-HSA-2682334: EPH-Ephrin signaling; R-HSA-3928663: EPHA-mediated growth cone collapse; R-HSA-3928665: EPH-ephrin mediated repulsion of cells	.	P54756
TTFAHWI	Ephrin type-A receptor 6 (EPHA6)	Q9UF33	EPHA6_HUMAN	Kinase	HEK12; EPH-like kinase 12; EPH homology kinase 2; EK12; EHK2; EHK-2	EPHA6	"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."	EC 2.7.10.1	.	MGGCEVREFLLQFGFFLPLLTAWPGDCSHVSNNQVVLLDTTTVLGELGWKTYPLNGWDAITEMDEHNRPIHTYQVCNVMEPNQNNWLRTNWISRDAAQKIYVEMKFTLRDCNSIPWVLGTCKETFNLFYMESDESHGIKFKPNQYTKIDTIAADESFTQMDLGDRILKLNTEIREVGPIERKGFYLAFQDIGACIALVSVRVFYKKCPFTVRNLAMFPDTIPRVDSSSLVEVRGSCVKSAEERDTPKLYCGADGDWLVPLGRCICSTGYEEIEGSCHACRPGFYKAFAGNTKCSKCPPHSLTYMEATSVCQCEKGYFRAEKDPPSMACTRPPSAPRNVVFNINETALILEWSPPSDTGGRKDLTYSVICKKCGLDTSQCEDCGGGLRFIPRHTGLINNSVIVLDFVSHVNYTFEIEAMNGVSELSFSPKPFTAITVTTDQDAPSLIGVVRKDWASQNSIALSWQAPAFSNGAILDYEIKYYEKEHEQLTYSSTRSKAPSVIITGLKPATKYVFHIRVRTATGYSGYSQKFEFETGDETSDMAAEQGQILVIATAAVGGFTLLVILTLFFLITGRCQWYIKAKMKSEEKRRNHLQNGHLRFPGIKTYIDPDTYEDPSLAVHEFAKEIDPSRIRIERVIGAGEFGEVCSGRLKTPGKREIPVAIKTLKGGHMDRQRRDFLREASIMGQFDHPNIIRLEGVVTKRSFPAIGVEAFCPSFLRAGFLNSIQAPHPVPGGGSLPPRIPAGRPVMIVVEYMENGSLDSFLRKHDGHFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEAAYTTTGGKIPIRWTAPEAIAYRKFSSASDAWSYGIVMWEVMSYGERPYWEMSNQDVILSIEEGYRLPAPMGCPASLHQLMLHCWQKERNHRPKFTDIVSFLDKLIRNPSALHTLVEDILVMPESPGEVPEYPLFVTVGDWLDSIKMGQYKNNFVAAGFTTFDLISRMSIDDIRRIGVILIGHQRRIVSSIQTLRLHMMHIQEKGFHV	Literature-reported	Amino acid conjugates of lithocholic acid as antagonists of the EphA2 receptor. J Med Chem. 2013 Apr 11;56(7):2936-47.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Ephrin type-A receptor 2 transmembrane domain; Ephrin receptor ligand binding domain; Fibronectin type III domain; Protein tyrosine kinase; SAM domain (Sterile alpha motif)	PF14575; PF01404; PF00041; PF07714; PF00536	PF14575; EphA2_TM; PF01404; Ephrin_lbd; PF00041; fn3; PF07714; Pkinase_Tyr; PF00536; SAM_1	.	.	hsa04360: Axon guidance	R-HSA-2682334: EPH-Ephrin signaling; R-HSA-3928663: EPHA-mediated growth cone collapse; R-HSA-3928665: EPH-ephrin mediated repulsion of cells	.	Q9UF33
TTAHTVG	Ephrin type-A receptor 7 (EPHA7)	Q15375	EPHA7_HUMAN	Kinase	hEK11; EPH-like kinase 11; EPH homology kinase 3; EK11; EHK3; EHK-3	EPHA7	"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."	EC 2.7.10.1	3NRU; 3H8M; 3DKO; 2REI	MVFQTRYPSWIILCYIWLLRFAHTGEAQAAKEVLLLDSKAQQTELEWISSPPNGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNSLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGACIALVSVKVYYKKCWSIIENLAIFPDTVTGSEFSSLVEVRGTCVSSAEEEAENAPRMHCSAEGEWLVPIGKCICKAGYQQKGDTCEPCGRGFYKSSSQDLQCSRCPTHSFSDKEGSSRCECEDGYYRAPSDPPYVACTRPPSAPQNLIFNINQTTVSLEWSPPADNGGRNDVTYRILCKRCSWEQGECVPCGSNIGYMPQQTGLEDNYVTVMDLLAHANYTFEVEAVNGVSDLSRSQRLFAAVSITTGQAAPSQVSGVMKERVLQRSVELSWQEPEHPNGVITEYEIKYYEKDQRERTYSTVKTKSTSASINNLKPGTVYVFQIRAFTAAGYGNYSPRLDVATLEEATGKMFEATAVSSEQNPVIIIAVVAVAGTIILVFMVFGFIIGRRHCGYSKADQEGDEELYFHFKFPGTKTYIDPETYEDPNRAVHQFAKELDASCIKIERVIGAGEFGEVCSGRLKLPGKRDVAVAIKTLKVGYTEKQRRDFLCEASIMGQFDHPNVVHLEGVVTRGKPVMIVIEFMENGALDAFLRKHDGQFTVIQLVGMLRGIAAGMRYLADMGYVHRDLAARNILVNSNLVCKVSDFGLSRVIEDDPEAVYTTTGGKIPVRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPAPMDCPAGLHQLMLDCWQKERAERPKFEQIVGILDKMIRNPNSLKTPLGTCSRPISPLLDQNTPDFTTFCSVGEWLQAIKMERYKDNFTAAGYNSLESVARMTIEDVMSLGITLVGHQKKIMSSIQTMRAQMLHLHGTGIQV	Literature-reported	Structure-based optimization of potent and selective inhibitors of the tyrosine kinase erythropoietin producing human hepatocellular carcinoma receptor B4 (EphB4). J Med Chem. 2009 Oct 22;52(20):6433-46.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Ephrin type-A receptor 2 transmembrane domain; Ephrin receptor ligand binding domain; Putative ephrin-receptor like ; Fibronectin type III domain; Protein tyrosine kinase; SAM domain (Sterile alpha motif)	PF14575; PF01404; PF07699; PF00041; PF07714; PF00536	PF14575; EphA2_TM; PF01404; Ephrin_lbd; PF07699; Ephrin_rec_like; PF00041; fn3; PF07714; Pkinase_Tyr; PF00536; SAM_1	.	.	hsa04360: Axon guidance	R-HSA-2682334: EPH-Ephrin signaling; R-HSA-3928663: EPHA-mediated growth cone collapse; R-HSA-3928665: EPH-ephrin mediated repulsion of cells	.	Q15375
TTHZ2LW	Ephrin type-A receptor 8 (EPHA8)	P29322	EPHA8_HUMAN	Kinase	hEK3; Tyrosine-protein kinase receptor EEK; KIAA1459; EPH-like kinase 3; EPH- and ELK-related kinase; EK3; EEK	EPHA8	"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."	EC 2.7.10.1	3KUL; 1X5L; 1UCV	MAPARGRLPPALWVVTAAAAAATCVSAARGEVNLLDTSTIHGDWGWLTYPAHGWDSINEVDESFQPIHTYQVCNVMSPNQNNWLRTSWVPRDGARRVYAEIKFTLRDCNSMPGVLGTCKETFNLYYLESDRDLGASTQESQFLKIDTIAADESFTGADLGVRRLKLNTEVRSVGPLSKRGFYLAFQDIGACLAILSLRIYYKKCPAMVRNLAAFSEAVTGADSSSLVEVRGQCVRHSEERDTPKMYCSAEGEWLVPIGKCVCSAGYEERRDACVACELGFYKSAPGDQLCARCPPHSHSAAPAAQACHCDLSYYRAALDPPSSACTRPPSAPVNLISSVNGTSVTLEWAPPLDPGGRSDITYNAVCRRCPWALSRCEACGSGTRFVPQQTSLVQASLLVANLLAHMNYSFWIEAVNGVSDLSPEPRRAAVVNITTNQAAPSQVVVIRQERAGQTSVSLLWQEPEQPNGIILEYEIKYYEKDKEMQSYSTLKAVTTRATVSGLKPGTRYVFQVRARTSAGCGRFSQAMEVETGKPRPRYDTRTIVWICLTLITGLVVLLLLLICKKRHCGYSKAFQDSDEEKMHYQNGQAPPPVFLPLHHPPGKLPEPQFYAEPHTYEEPGRAGRSFTREIEASRIHIEKIIGSGDSGEVCYGRLRVPGQRDVPVAIKALKAGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTRGRLAMIVTEYMENGSLDTFLRTHDGQFTIMQLVGMLRGVGAGMRYLSDLGYVHRDLAARNVLVDSNLVCKVSDFGLSRVLEDDPDAAYTTTGGKIPIRWTAPEAIAFRTFSSASDVWSFGVVMWEVLAYGERPYWNMTNRDVISSVEEGYRLPAPMGCPHALHQLMLDCWHKDRAQRPRFSQIVSVLDALIRSPESLRATATVSRCPPPAFVRSCFDLRGGSGGGGGLTVGDWLDSIRMGRYRDHFAAGGYSSLGMVLRMNAQDVRALGITLMGHQKKILGSIQTMRAQLTSTQGPRRHL	Literature-reported	Structure-based optimization of potent and selective inhibitors of the tyrosine kinase erythropoietin producing human hepatocellular carcinoma receptor B4 (EphB4). J Med Chem. 2009 Oct 22;52(20):6433-46.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Ephrin type-A receptor 2 transmembrane domain; Ephrin receptor ligand binding domain; Fibronectin type III domain; Protein tyrosine kinase; SAM domain (Sterile alpha motif)	PF14575; PF01404; PF00041; PF07714; PF00536	PF14575; EphA2_TM; PF01404; Ephrin_lbd; PF00041; fn3; PF07714; Pkinase_Tyr; PF00536; SAM_1	.	.	hsa04360: Axon guidance	R-HSA-2682334: EPH-Ephrin signaling; R-HSA-3928663: EPHA-mediated growth cone collapse; R-HSA-3928665: EPH-ephrin mediated repulsion of cells	.	P29322
TT8MDAC	Ephrin type-B receptor 1 (EPHB1)	P54762	EPHB1_HUMAN	Kinase	hEK6; Tyrosine-protein kinase receptor EPH-2; Neuronally-expressed EPH-related tyrosine kinase; EPHT2; EPH-like kinase 6; EPH tyrosine kinase 2; ELK; EK6	EPHB1	"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."	EC 2.7.10.1	5MJB; 5MJA; 3ZFX; 2EAO; 2DJS	MALDYLLLLLLASAVAAMEETLMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPNVPGSCKETFNLYYYETDSVIATKKSAFWSEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYGACMSLLSVRVFFKKCPSIVQNFAVFPETMTGAESTSLVIARGTCIPNAEEVDVPIKLYCNGDGEWMVPIGRCTCKPGYEPENSVACKACPAGTFKASQEAEGCSHCPSNSRSPAEASPICTCRTGYYRADFDPPEVACTSVPSGPRNVISIVNETSIILEWHPPRETGGRDDVTYNIICKKCRADRRSCSRCDDNVEFVPRQLGLTECRVSISSLWAHTPYTFDIQAINGVSSKSPFPPQHVSVNITTNQAAPSTVPIMHQVSATMRSITLSWPQPEQPNGIILDYEIRYYEKEHNEFNSSMARSQTNTARIDGLRPGMVYVVQVRARTVAGYGKFSGKMCFQTLTDDDYKSELREQLPLIAGSAAAGVVFVVSLVAISIVCSRKRAYSKEAVYSDKLQHYSTGRGSPGMKIYIDPFTYEDPNEAVREFAKEIDVSFVKIEEVIGAGEFGEVYKGRLKLPGKREIYVAIKTLKAGYSEKQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLAEMNYVHRDLAARNILVNSNLVCKVSDFGLSRYLQDDTSDPTYTSSLGGKIPVRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPMDCPAALHQLMLDCWQKDRNSRPRFAEIVNTLDKMIRNPASLKTVATITAVPSQPLLDRSIPDFTAFTTVDDWLSAIKMVQYRDSFLTAGFTSLQLVTQMTSEDLLRIGITLAGHQKKILNSIHSMRVQISQSPTAMA	Literature-reported	Structure-based optimization of potent and selective inhibitors of the tyrosine kinase erythropoietin producing human hepatocellular carcinoma receptor B4 (EphB4). J Med Chem. 2009 Oct 22;52(20):6433-46.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Ephrin type-A receptor 2 transmembrane domain; Ephrin receptor ligand binding domain; Fibronectin type III domain; Protein tyrosine kinase; SAM domain (Sterile alpha motif)	PF14575; PF01404; PF00041; PF07714; PF00536	PF14575; EphA2_TM; PF01404; Ephrin_lbd; PF00041; fn3; PF07714; Pkinase_Tyr; PF00536; SAM_1	.	.	hsa04360: Axon guidance	R-HSA-2682334: EPH-Ephrin signaling; R-HSA-3928662: EPHB-mediated forward signaling; R-HSA-3928664: Ephrin signaling; R-HSA-3928665: EPH-ephrin mediated repulsion of cells	.	P54762
TTKPV6O	Ephrin type-B receptor 2 (EPHB2)	P29323	EPHB2_HUMAN	Kinase	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	EPHB2	"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."	EC 2.7.10.1	3ZFM; 2QBX; 1F0M; 1B4F	MALRRLGAALLLLPLLAAVEETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKFIRRRGAHRIHVEMKFSVRDCSSIPSVPGSCKETFNLYYYEADFDSATKTFPNWMENPWVKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRSGFYLAFQDYGGCMSLIAVRVFYRKCPRIIQNGAIFQETLSGAESTSLVAARGSCIANAEEVDVPIKLYCNGDGEWLVPIGRCMCKAGFEAVENGTVCRGCPSGTFKANQGDEACTHCPINSRTTSEGATNCVCRNGYYRADLDPLDMPCTTIPSAPQAVISSVNETSLMLEWTPPRDSGGREDLVYNIICKSCGSGRGACTRCGDNVQYAPRQLGLTEPRIYISDLLAHTQYTFEIQAVNGVTDQSPFSPQFASVNITTNQAAPSAVSIMHQVSRTVDSITLSWSQPDQPNGVILDYELQYYEKELSEYNATAIKSPTNTVTVQGLKAGAIYVFQVRARTVAGYGRYSGKMYFQTMTEAEYQTSIQEKLPLIIGSSAAGLVFLIAVVVIAIVCNRRGFERADSEYTDKLQHYTSGHMTPGMKIYIDPFTYEDPNEAVREFAKEIDISCVKIEQVIGAGEFGEVCSGHLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNVIHLEGVVTKSTPVMIITEFMENGSLDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLADMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSDPTYTSALGGKIPIRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMTNQDVINAIEQDYRLPPPMDCPSALHQLMLDCWQKDRNHRPKFGQIVNTLDKMIRNPNSLKAMAPLSSGINLPLLDRTIPDYTSFNTVDEWLEAIKMGQYKESFANAGFTSFDVVSQMMMEDILRVGVTLAGHQKKILNSIQVMRAQMNQIQSVEGQPLARRPRATGRTKRCQPRDVTKKTCNSNDGKKKGMGKKKTDPGRGREIQGIFFKEDSHKESNDCSCGG	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	19	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Ephrin type-A receptor 2 transmembrane domain; Ephrin receptor ligand binding domain; Putative ephrin-receptor like ; Fibronectin type III domain; Protein tyrosine kinase; SAM domain (Sterile alpha motif)	PF14575; PF01404; PF07699; PF00041; PF07714; PF00536	PF14575; EphA2_TM; PF01404; Ephrin_lbd; PF07699; Ephrin_rec_like; PF00041; fn3; PF07714; Pkinase_Tyr; PF00536; SAM_1	.	.	hsa04360:Axon guidance	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	.	P29323
TT5LM7U	Ephrin type-B receptor 3 (EPHB3)	P54753	EPHB3_HUMAN	Kinase	hEK2; Tyrosine-protein kinase TYRO6; TYRO6; Embryonic kinase 2; ETK2; EPH-like tyrosine kinase 2; EPH-like kinase 2; EK2	EPHB3	"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."	EC 2.7.10.1	5L6P; 5L6O; 3ZFY; 3P1I	MARARPPPPPSPPPGLLPLLPPLLLLPLLLLPAGCRALEETLMDTKWVTSELAWTSHPESGWEEVSGYDEAMNPIRTYQVCNVRESSQNNWLRTGFIWRRDVQRVYVELKFTVRDCNSIPNIPGSCKETFNLFYYEADSDVASASSPFWMENPYVKVDTIAPDESFSRLDAGRVNTKVRSFGPLSKAGFYLAFQDQGACMSLISVRAFYKKCASTTAGFALFPETLTGAEPTSLVIAPGTCIPNAVEVSVPLKLYCNGDGEWMVPVGACTCATGHEPAAKESQCRPCPPGSYKAKQGEGPCLPCPPNSRTTSPAASICTCHNNFYRADSDSADSACTTVPSPPRGVISNVNETSLILEWSEPRDLGGRDDLLYNVICKKCHGAGGASACSRCDDNVEFVPRQLGLTERRVHISHLLAHTRYTFEVQAVNGVSGKSPLPPRYAAVNITTNQAAPSEVPTLRLHSSSGSSLTLSWAPPERPNGVILDYEMKYFEKSEGIASTVTSQMNSVQLDGLRPDARYVVQVRARTVAGYGQYSRPAEFETTSERGSGAQQLQEQLPLIVGSATAGLVFVVAVVVIAIVCLRKQRHGSDSEYTEKLQQYIAPGMKVYIDPFTYEDPNEAVREFAKEIDVSCVKIEEVIGAGEFGEVCRGRLKQPGRREVFVAIKTLKVGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMILTEFMENCALDSFLRLNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDPSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAVEQDYRLPPPMDCPTALHQLMLDCWVRDRNLRPKFSQIVNTLDKLIRNAASLKVIASAQSGMSQPLLDRTVPDYTTFTTVGDWLDAIKMGRYKESFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMRLQMNQTLPVQV	Literature-reported	Structure-based optimization of potent and selective inhibitors of the tyrosine kinase erythropoietin producing human hepatocellular carcinoma receptor B4 (EphB4). J Med Chem. 2009 Oct 22;52(20):6433-46.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Ephrin type-A receptor 2 transmembrane domain; Ephrin receptor ligand binding domain; Putative ephrin-receptor like ; Fibronectin type III domain; Protein tyrosine kinase; SAM domain (Sterile alpha motif)	PF14575; PF01404; PF07699; PF00041; PF07714; PF00536	PF14575; EphA2_TM; PF01404; Ephrin_lbd; PF07699; Ephrin_rec_like; PF00041; fn3; PF07714; Pkinase_Tyr; PF00536; SAM_1	.	.	hsa04360: Axon guidance	R-HSA-2682334: EPH-Ephrin signaling; R-HSA-3928662: EPHB-mediated forward signaling; R-HSA-3928664: Ephrin signaling; R-HSA-3928665: EPH-ephrin mediated repulsion of cells	.	P54753
TTI4ZX2	Ephrin type-B receptor 4 (EPHB4)	P54760	EPHB4_HUMAN	Kinase	Tyrosine-protein kinase TYRO11; TYRO11; MYK1; Hepatoma transmembrane kinase; HTK	EPHB4	"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."	EC 2.7.10.1	6FNM; 6FNL; 6FNK; 6FNJ; 6FNI	MELRVLLCWASLAAALEETLLNTKLETADLKWVTFPQVDGQWEELSGLDEEQHSVRTYEVCDVQRAPGQAHWLRTGWVPRRGAVHVYATLRFTMLECLSLPRAGRSCKETFTVFYYESDADTATALTPAWMENPYIKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAGFYLAFQDQGACMALLSLHLFYKKCAQLTVNLTRFPETVPRELVVPVAGSCVVDAVPAPGPSPSLYCREDGQWAEQPVTGCSCAPGFEAAEGNTKCRACAQGTFKPLSGEGSCQPCPANSHSNTIGSAVCQCRVGYFRARTDPRGAPCTTPPSAPRSVVSRLNGSSLHLEWSAPLESGGREDLTYALRCRECRPGGSCAPCGGDLTFDPGPRDLVEPWVVVRGLRPDFTYTFEVTALNGVSSLATGPVPFEPVNVTTDREVPPAVSDIRVTRSSPSSLSLAWAVPRAPSGAVLDYEVKYHEKGAEGPSSVRFLKTSENRAELRGLKRGASYLVQVRARSEAGYGPFGQEHHSQTQLDESEGWREQLALIAGTAVVGVVLVLVVIVVAVLCLRKQSNGREAEYSDKHGQYLIGHGTKVYIDPFTYEDPNEAVREFAKEIDVSYVKIEEVIGAGEFGEVCRGRLKAPGKKESCVAIKTLKGGYTERQRREFLSEASIMGQFEHPNIIRLEGVVTNSMPVMILTEFMENGALDSFLRLNDGQFTVIQLVGMLRGIASGMRYLAEMSYVHRDLAARNILVNSNLVCKVSDFGLSRFLEENSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTSASDAWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPPDCPTSLHQLMLDCWQKDRNARPRFPQVVSALDKMIRNPASLKIVARENGGASHPLLDQRQPHYSAFGSVGEWLRAIKMGRYEESFAAAGFGSFELVSQISAEDLLRIGVTLAGHQKKILASVQHMKSQAKPGTPGGTGGPAPQY	Clinical trial	XL647--a multitargeted tyrosine kinase inhibitor: results of a phase II study in subjects with non-small cell lung cancer who have progressed after responding to treatment with either gefitinib or erlotinib. J Thorac Oncol. 2012 Jan;7(1):219-26.	25	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Ephrin type-A receptor 2 transmembrane domain; Ephrin receptor ligand binding domain; Putative ephrin-receptor like ; Fibronectin type III domain; Protein tyrosine kinase; SAM domain (Sterile alpha motif)	PF14575; PF01404; PF07699; PF00041; PF07714; PF00536	PF14575; EphA2_TM; PF01404; Ephrin_lbd; PF07699; Ephrin_rec_like; PF00041; fn3; PF07714; Pkinase_Tyr; PF00536; SAM_1	8.A.23.1.15	The Basigin (Basigin) Family	hsa04360:Axon guidance	R-HSA-2682334:EPH-Ephrin signaling; R-HSA-3928662:EPHB-mediated forward signaling; R-HSA-3928665:EPH-ephrin mediated repulsion of cells	.	P54760
TTZEMUY	Ephrin type-B receptor 6 (EPHB6)	O15197	EPHB6_HUMAN	Kinase	Tyrosine-protein kinase-defective receptor EPH-6; HEP	EPHB6	"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."	.	.	MATEGAAQLGNRVAGMVCSLWVLLLVSSVLALEEVLLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEACHVAGAPPGTGQDNWLQTHFVERRGAQRAHIRLHFSVRACSSLGVSGGTCRETFTLYYRQAEEPDSPDSVSSWHLKRWTKVDTIAADESFPSSSSSSSSSSSAAWAVGPHGAGQRAGLQLNVKERSFGPLTQRGFYVAFQDTGACLALVAVRLFSYTCPAVLRSFASFPETQASGAGGASLVAAVGTCVAHAEPEEDGVGGQAGGSPPRLHCNGEGKWMVAVGGCRCQPGYQPARGDKACQACPRGLYKSSAGNAPCSPCPARSHAPNPAAPVCPCLEGFYRASSDPPEAPCTGPPSAPQELWFEVQGSALMLHWRLPRELGGRGDLLFNVVCKECEGRQEPASGGGGTCHRCRDEVHFDPRQRGLTESRVLVGGLRAHVPYILEVQAVNGVSELSPDPPQAAAINVSTSHEVPSAVPVVHQVSRASNSITVSWPQPDQTNGNILDYQLRYYDQAEDESHSFTLTSETNTATVTQLSPGHIYGFQVRARTAAGHGPYGGKVYFQTLPQGELSSQLPERLSLVIGSILGALAFLLLAAITVLAVVFQRKRRGTGYTEQLQQYSSPGLGVKYYIDPSTYEDPCQAIRELAREVDPAYIKIEEVIGTGSFGEVRQGRLQPRGRREQTVAIQALWAGGAESLQMTFLGRAAVLGQFQHPNILRLEGVVTKSRPLMVLTEFMELGPLDSFLRQREGQFSSLQLVAMQRGVAAAMQYLSSFAFVHRSLSAHSVLVNSHLVCKVARLGHSPQGPSCLLRWAAPEVIAHGKHTTSSDVWSFGILMWEVMSYGERPYWDMSEQEVLNAIEQEFRLPPPPGCPPGLHLLMLDTWQKDRARRPHFDQLVAAFDKMIRKPDTLQAGGDPGERPSQALLTPVALDFPCLDSPQAWLSAIGLECYQDNFSKFGLCTFSDVAQLSLEDLPALGITLAGHQKKLLHHIQLLQQHLRQQGSVEV	Literature-reported	Amino acid conjugates of lithocholic acid as antagonists of the EphA2 receptor. J Med Chem. 2013 Apr 11;56(7):2936-47.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.	.	.	Ephrin type-A receptor 2 transmembrane domain; Ephrin receptor ligand binding domain; Putative ephrin-receptor like ; Fibronectin type III domain; Protein tyrosine kinase; SAM domain (Sterile alpha motif)	PF14575; PF01404; PF07699; PF00041; PF07714; PF07647	PF14575; EphA2_TM; PF01404; Ephrin_lbd; PF07699; Ephrin_rec_like; PF00041; fn3; PF07714; Pkinase_Tyr; PF07647; SAM_2	.	.	hsa04360: Axon guidance	R-HSA-2682334: EPH-Ephrin signaling; R-HSA-3928662: EPHB-mediated forward signaling; R-HSA-3928664: Ephrin signaling; R-HSA-3928665: EPH-ephrin mediated repulsion of cells	.	O15197
TT7WVHI	Soluble epoxide hydrolase (EPHX2)	P34913	HYES_HUMAN	Ether bond hydrolase	Bifunctional epoxide hydrolase 2	EPHX2	"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."	.	6AUM; 5MWA; 5FP0; 5AM5; 5AM4	MTLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATTRLMKGEITLSQWIPLMEENCRKCSETAKVCLPKNFSIKEIFDKAISARKINRPMLQAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDARNPPVVSKM	Clinical trial	Orally bioavailable potent soluble epoxide hydrolase inhibitors. J Med Chem. 2007 Aug 9;50(16):3825-40.	21	EC:3.3	Ether hydrolase	AB hydrolase superfamily. Epoxide hydrolase family.	3.3.2.10 	Acting on ether bonds	alpha/beta hydrolase fold; Haloacid dehalogenase-like hydrolase	PF00561; PF13419	PF00561; Abhydrolase_1; PF13419; HAD_2	.	.	hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways; hsa04146:Peroxisome	R-HSA-2142670: Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET); R-HSA-9018682: Biosynthesis of maresins; R-HSA-9033241: Peroxisomal protein import	.	P34913
TTQG4NR	Erythropoietin (EPO)	P01588	EPO_HUMAN	.	Epoetin	EPO	"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."	.	1EER; 1CN4; 1BUY	MGVHECPAWLWLLLSLLSLPLGLPVLGAPPRLICDSRVLERYLLEAKEAENITTGCAEHCSLNENITVPDTKVNFYAWKRMEVGQQAVEVWQGLALLSEAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDR	Clinical trial	Merck ditches biogeneric. Nat Biotechnol. 2010 Jul;28(7):636.	21	.	.	EPO/TPO family.	.	.	Erythropoietin/thrombopoietin	PF00758	PF00758; EPO_TPO	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04066:HIF-1 signaling pathway; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage	R-HSA-1234158:Regulation of gene expression by Hypoxia-inducible Factor	.	P01588
TTAUX24	Erythropoietin Receptor (EPOR)	P19235	EPOR_HUMAN	Cytokine receptor	Full-length form; EPO-R	EPOR	"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."	.	6E2Q; 4Y5Y; 4Y5X; 4Y5V; 2MV6	MDHLGASLWPQVGSLCLLLAGAAWAPPPNLPDPKFESKAALLAARGPEELLCFTERLEDLVCFWEEAASAGVGPGNYSFSYQLEDEPWKLCRLHQAPTARGAVRFWCSLPTADTSSFVPLELRVTAASGAPRYHRVIHINEVVLLDAPVGLVARLADESGHVVLRWLPPPETPMTSHIRYEVDVSAGNGAGSVQRVEILEGRTECVLSNLRGRTRYTFAVRARMAEPSFGGFWSAWSEPVSLLTPSDLDPLILTLSLILVVILVLLTVLALLSHRRALKQKIWPGIPSPESEFEGLFTTHKGNFQLWLYQNDGCLWWSPCTPFTEDPPASLEVLSERCWGTMQAVEPGTDDEGPLLEPVGSEHAQDTYLVLDKWLLPRNPPSEDLPGPGGSVDIVAMDEGSEASSCSSALASKPSPEGASAASFEYTILDPSSQLLRPWTLCPELPPTPPHLKYLYLVVSDSGISTDYSSGDSQGAQGGLSDGPYSNPYENSLIPAAEPLPPSYVACS	Successful	"2007 Standards, Options, and Recommendations: use of erythropoiesis-stimulating agents (ESA: epoetin alfa, epoetin beta, and darbepoetin) for the management of anemia in children with cancer. PediatrBlood Cancer. 2009 Jul;53(1):7-12."	34	Cytokine receptor	Type I cytokine receptor	type I cytokine receptor family. Type 1 subfamily.	.	.	"Erythropoietin receptor, ligand binding; Fibronectin type III domain"	PF09067; PF00041	PF09067; EpoR_lig-bind; PF00041; fn3	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage	R-HSA-9006335: Signaling by Erythropoietin; R-HSA-9027276: Erythropoietin activates Phosphoinositide-3-kinase (PI3K); R-HSA-9027277: Erythropoietin activates Phospholipase C gamma (PLCG); R-HSA-9027283: Erythropoietin activates STAT5; R-HSA-9027284: Erythropoietin activates RAS	.	P19235
TTXYCDZ	Bifunctional aminoacyl-tRNA synthetase (EPRS)	P07814	SYEP_HUMAN	Carbon-oxygen ligase	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	EPRS	"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."	.	5Y6L; 5VAD; 5V58; 5BMU; 5A5H	MATLSLTVNSGDPPLGALLAVEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLARVATTAGLYGSNLMEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEKKQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFIEGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKLNLENKDYKKTTKVTWLAETTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTKVEATKNETSAPFKERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPEAKVLFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAEDKDKKKKEKENKSEKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDKEALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY	Clinical trial	Halofuginone and other febrifugine derivatives inhibit prolyl-tRNA synthetase. Nat Chem Biol. 2012 Feb 12;8(3):311-7.	21	EC:6.1	Carbon oxygen ligase	.	6.1.1.17	Forming carbon-oxygen bonds	"Glutathione S-transferase, C-terminal domain; Anticodon binding domain; Prolyl-tRNA synthetase, C-terminal; tRNA synthetases class I (E and Q), catalytic domain; tRNA synthetases class I (E and Q), anti-codon binding domain; tRNA synthetase class II core domain (G, H, P, S and T); WHEP-TRS domain"	PF00043; PF03129; PF09180; PF00749; PF03950; PF00587; PF00458	PF00043; GST_C; PF03129; HGTP_anticodon; PF09180; ProRS-C_1; PF00749; tRNA-synt_1c; PF03950; tRNA-synt_1c_C; PF00587; tRNA-synt_2b; PF00458; WHEP-TRS	.	.	hsa00860:Porphyrin and chlorophyll metabolism; hsa00970:Aminoacyl-tRNA biosynthesis; hsa01100:Metabolic pathways	R-HSA-2408522: Selenoamino acid metabolism; R-HSA-379716: Cytosolic tRNA aminoacylation; R-HSA-6782315: tRNA modification in the nucleus and cytosol	.	P07814
TTCIO0M	Eosinophil peroxidase (EPX)	P11678	PERE_HUMAN	Peroxidases	EPX	EPX	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.	EC 1.11.1.7	.	MHLLPALAGVLATLVLAQPCEGTDPASPGAVETSVLRDCIAEAKLLVDAAYNWTQKSIKQRLRSGSASPMDLLSYFKQPVAATRTVVRAADYMHVALGLLEEKLQPQRSGPFNVTDVLTEPQLRLLSQASGCALRDQAERCSDKYRTITGRCNNKRRPLLGASNQALARWLPAEYEDGLSLPFGWTPSRRRNGFLLPLVRAVSNQIVRFPNERLTSDRGRALMFMQWGQFIDHDLDFSPESPARVAFTAGVDCERTCAQLPPCFPIKIPPNDPRIKNQRDCIPFFRSAPSCPQNKNRVRNQINALTSFVDASMVYGSEVSLSLRLRNRTNYLGLLAINQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSTETPKLAAMHTLFMREHNRLATELRRLNPRWNGDKLYNEARKIMGAMVQIITYRDFLPLVLGKARARRTLGHYRGYCSNVDPRVANVFTLAFRFGHTMLQPFMFRLDSQYRASAPNSHVPLSSAFFASWRIVYEGGIDPILRGLMATPAKLNRQDAMLVDELRDRLFRQVRRIGLDLAALNMQRSRDHGLPGYNAWRRFCGLSQPRNLAQLSRVLKNQDLARKFLNLYGTPDNIDIWIGAIAEPLLPGARVGPLLACLFENQFRRARDGDRFWWQKRGVFTKRQRKALSRISLSRIICDNTGITTVSRDIFRANIYPRGFVNCSRIPRLNLSAWRGT	Literature-reported	Biomarkers of eosinophil involvement in allergic and eosinophilic diseases: review of phenotypic and serum markers including a novel assay to quantify levels of soluble Siglec-8. J Immunol Methods. 2012 Sep 28;383(1-2):39-46. 	.	.	.	.	.	.	.	.	.	.	.	hsa05310: Asthma	R-HSA-6798695: Neutrophil degranulation	.	P11678
TT60XFL	Adipocyte-derived leucine aminopeptidase (ERAP1)	Q9NZ08	ERAP1_HUMAN	Peptidase	Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator; Puromycin-insensitive leucyl-specific aminopeptidase; PILS-AP; ERAP1; Aminopeptidase PILS; ARTS-1; ALAP; A-LAP	ERAP1	"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."	EC 3.4.11.-	6Q4R; 5J5E; 3RJO; 3QNF; 3MDJ	MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASICPTDGVKGMDGFCSRSQHSSSSSHWHQEGVDVKTMMNTWTLQKGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWHVPLTFITSKSDMVHRFLLKTKTDVLILPEEVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLKHETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQRAEGYFRKWKESNGNLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQEFPQILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQLRCVQQTIETIEENIGWMDKNFDKIRVWLQSEKLERM	Literature-reported	Novel selective inhibitors of aminopeptidases that generate antigenic peptides. Bioorg Med Chem Lett. 2013 Sep 1;23(17):4832-6.	0	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-983170: Antigen Presentation: Folding, assembly and peptide loading of class I MHC"	.	Q9NZ08
TTVGS1C	Endoplasmic reticulum aminopeptidase 2 (ERAP2)	Q6P179	ERAP2_HUMAN	Peptidase	Leukocyte-derived arginine aminopeptidase; LRAP; L-RAP	ERAP2	"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."	EC 3.4.11.-	5K1V; 5J6S; 5CU5; 5AB2; 5AB0	MFHSSAMVNSHRKPMFNIHRGFYCLTAILPQICICSQFSVPSSYHFTEDPGAFPVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSNATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVPEKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKLLDFYEKYFDIYYPLSKLDLIAIPDFAPGAMENWGLITYRETSLLFDPKTSSASDKLWVTRVIAHELAHQWFGNLVTMEWWNDIWLKEGFAKYMELIAVNATYPELQFDDYFLNVCFEVITKDSLNSSRPISKPAETPTQIQEMFDEVSYNKGACILNMLKDFLGEEKFQKGIIQYLKKFSYRNAKNDDLWSSLSNSCLESDFTSGGVCHSDPKMTSNMLAFLGENAEVKEMMTTWTLQKGIPLLVVKQDGCSLRLQQERFLQGVFQEDPEWRALQERYLWHIPLTYSTSSSNVIHRHILKSKTDTLDLPEKTSWVKFNVDSNGYYIVHYEGHGWDQLITQLNQNHTLLRPKDRVGLIHDVFQLVGAGRLTLDKALDMTYYLQHETSSPALLEGLSYLESFYHMMDRRNISDISENLKRYLLQYFKPVIDRQSWSDKGSVWDRMLRSALLKLACDLNHAPCIQKAAELFSQWMESSGKLNIPTDVLKIVYSVGAQTTAGWNYLLEQYELSMSSAEQNKILYALSTSKHQEKLLKLIELGMEGKVIKTQNLAALLHAIARRPKGQQLAWDFVRENWTHLLKKFDLGSYDIRMIISGTTAHFSSKDKLQEVKLFFESLEAQGSHLDIFQTVLETITKNIKWLEKNLPTLRTWLMVNT	Literature-reported	Novel selective inhibitors of aminopeptidases that generate antigenic peptides. Bioorg Med Chem Lett. 2013 Sep 1;23(17):4832-6.	0	EC:3.4	.	peptidase M1 family.	3.4.11.-	Acting on peptide bonds (peptidases)	ERAP1-like C-terminal domain; Peptidase family M1 domain	PF11838; PF01433	PF11838; ERAP1_C; PF01433; Peptidase_M1	.	.	.	"R-HSA-983170: Antigen Presentation: Folding, assembly and peptide loading of class I MHC"	.	Q6P179
TTR5TV4	ERBB2 messenger RNA (HER2 mRNA)	P04626	ERBB2_HUMAN	mRNA target	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)	ERBB2	"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."	EC 2.7.10.1	6OGE; 6J71; 6BGT; 6ATT; 5TQS	MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV	Clinical trial	Identification of genotype-correlated sensitivity to selective kinase inhibitors by using high-throughput tumor cell line profiling. Proc Natl Acad Sci U S A. 2007 Dec 11;104(50):19936-41.	25	mRNA	mRNA target	.	.	.	Furin-like cysteine rich region; Growth factor receptor domain IV; Protein tyrosine kinase; Receptor L domain	PF00757; PF14843; PF07714; PF01030	PF00757; Furin-like; PF14843; GF_recep_IV; PF07714; Pkinase_Tyr; PF01030; Recep_L_domain	.	.	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	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	.	P04626
TT6EO5L	Erbb2 tyrosine kinase receptor (HER2)	P04626	ERBB2_HUMAN	Kinase	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	ERBB2	"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."	EC 2.7.10.1	6OGE; 6J71; 6BGT; 6ATT; 5TQS	MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV	Successful	Her2/neu is not a commonly expressed therapeutic target in melanoma -- a large cohort tissue microarray study. Melanoma Res. 2004 Jun;14(3):207-10.	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Furin-like cysteine rich region; Growth factor receptor domain IV; Protein tyrosine kinase; Receptor L domain	PF00757; PF14843; PF07714; PF01030	PF00757; Furin-like; PF14843; GF_recep_IV; PF07714; Pkinase_Tyr; PF01030; Recep_L_domain	.	.	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	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	.	P04626
TTSINU2	ERBB3 messenger RNA (ERBB3 mRNA)	P21860	ERBB3_HUMAN	mRNA target	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)	ERBB3	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.	EC 2.7.10.1	5O7P; 5O4O; 5CUS; 4RIY; 4RIX	MRANDALQVLGLLFSLARGSEVGNSQAVCPGTLNGLSVTGDAENQYQTLYKLYERCEVVMGNLEIVLTGHNADLSFLQWIREVTGYVLVAMNEFSTLPLPNLRVVRGTQVYDGKFAIFVMLNYNTNSSHALRQLRLTQLTEILSGGVYIEKNDKLCHMDTIDWRDIVRDRDAEIVVKDNGRSCPPCHEVCKGRCWGPGSEDCQTLTKTICAPQCNGHCFGPNPNQCCHDECAGGCSGPQDTDCFACRHFNDSGACVPRCPQPLVYNKLTFQLEPNPHTKYQYGGVCVASCPHNFVVDQTSCVRACPPDKMEVDKNGLKMCEPCGGLCPKACEGTGSGSRFQTVDSSNIDGFVNCTKILGNLDFLITGLNGDPWHKIPALDPEKLNVFRTVREITGYLNIQSWPPHMHNFSVFSNLTTIGGRSLYNRGFSLLIMKNLNVTSLGFRSLKEISAGRIYISANRQLCYHHSLNWTKVLRGPTEERLDIKHNRPRRDCVAEGKVCDPLCSSGGCWGPGPGQCLSCRNYSRGGVCVTHCNFLNGEPREFAHEAECFSCHPECQPMEGTATCNGSGSDTCAQCAHFRDGPHCVSSCPHGVLGAKGPIYKYPDVQNECRPCHENCTQGCKGPELQDCLGQTLVLIGKTHLTMALTVIAGLVVIFMMLGGTFLYWRGRRIQNKRAMRRYLERGESIEPLDPSEKANKVLARIFKETELRKLKVLGSGVFGTVHKGVWIPEGESIKIPVCIKVIEDKSGRQSFQAVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVRQHRGALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQVQVADFGVADLLPPDDKQLLYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAEPYAGLRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYLVIKRESGPGIAPGPEPHGLTNKKLEEVELEPELDLDLDLEAEEDNLATTTLGSALSLPVGTLNRPRGSQSLLSPSSGYMPMNQGNLGESCQESAVSGSSERCPRPVSLHPMPRGCLASESSEGHVTGSEAELQEKVSMCRSRSRSRSPRPRGDSAYHSQRHSLLTPVTPLSPPGLEEEDVNGYVMPDTHLKGTPSSREGTLSSVGLSSVLGTEEEDEDEEYEYMNRRRRHSPPHPPRPSSLEELGYEYMDVGSDLSASLGSTQSCPLHPVPIMPTAGTTPDEDYEYMNRQRDGGGPGGDYAAMGACPASEQGYEEMRAFQGPGHQAPHVHYARLKTLRSLEATDSAFDNPDYWHSRLFPKANAQRT	Literature-reported	"Downregulation of HER3 by a novel antisense oligonucleotide, EZN-3920, improves the antitumor activity of EGFR and HER2 tyrosine kinase inhibitors in animal models. Mol Cancer Ther. 2013 Apr;12(4):427-37."	0	mRNA	mRNA target	.	.	.	Furin-like cysteine rich region; Growth factor receptor domain IV; Protein tyrosine kinase; Receptor L domain	PF00757; PF14843; PF07714; PF01030	PF00757; Furin-like; PF14843; GF_recep_IV; PF07714; Pkinase_Tyr; PF01030; Recep_L_domain	.	.	hsa04012:ErbB signaling pathway; hsa04020:Calcium signaling pathway; hsa04144:Endocytosis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer	"R-HSA-1227986: Signaling by ERBB2; R-HSA-1236394: Signaling by ERBB4; R-HSA-1250196: SHC1 events in ERBB2 signaling; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1306955: GRB7 events in ERBB2 signaling; R-HSA-1358803: Downregulation of ERBB2:ERBB3 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; R-HSA-6785631: ERBB2 Regulates Cell Motility; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-8847993: ERBB2 Activates PTK6 Signaling; R-HSA-8863795: Downregulation of ERBB2 signaling; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants"	.	P21860
TTDC8N2	Erbb3 tyrosine kinase receptor (Erbb-3)	P21860	ERBB3_HUMAN	Kinase	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	ERBB3	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.	EC 2.7.10.1	5O7P; 5O4O; 5CUS; 4RIY; 4RIX	MRANDALQVLGLLFSLARGSEVGNSQAVCPGTLNGLSVTGDAENQYQTLYKLYERCEVVMGNLEIVLTGHNADLSFLQWIREVTGYVLVAMNEFSTLPLPNLRVVRGTQVYDGKFAIFVMLNYNTNSSHALRQLRLTQLTEILSGGVYIEKNDKLCHMDTIDWRDIVRDRDAEIVVKDNGRSCPPCHEVCKGRCWGPGSEDCQTLTKTICAPQCNGHCFGPNPNQCCHDECAGGCSGPQDTDCFACRHFNDSGACVPRCPQPLVYNKLTFQLEPNPHTKYQYGGVCVASCPHNFVVDQTSCVRACPPDKMEVDKNGLKMCEPCGGLCPKACEGTGSGSRFQTVDSSNIDGFVNCTKILGNLDFLITGLNGDPWHKIPALDPEKLNVFRTVREITGYLNIQSWPPHMHNFSVFSNLTTIGGRSLYNRGFSLLIMKNLNVTSLGFRSLKEISAGRIYISANRQLCYHHSLNWTKVLRGPTEERLDIKHNRPRRDCVAEGKVCDPLCSSGGCWGPGPGQCLSCRNYSRGGVCVTHCNFLNGEPREFAHEAECFSCHPECQPMEGTATCNGSGSDTCAQCAHFRDGPHCVSSCPHGVLGAKGPIYKYPDVQNECRPCHENCTQGCKGPELQDCLGQTLVLIGKTHLTMALTVIAGLVVIFMMLGGTFLYWRGRRIQNKRAMRRYLERGESIEPLDPSEKANKVLARIFKETELRKLKVLGSGVFGTVHKGVWIPEGESIKIPVCIKVIEDKSGRQSFQAVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVRQHRGALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQVQVADFGVADLLPPDDKQLLYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAEPYAGLRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYLVIKRESGPGIAPGPEPHGLTNKKLEEVELEPELDLDLDLEAEEDNLATTTLGSALSLPVGTLNRPRGSQSLLSPSSGYMPMNQGNLGESCQESAVSGSSERCPRPVSLHPMPRGCLASESSEGHVTGSEAELQEKVSMCRSRSRSRSPRPRGDSAYHSQRHSLLTPVTPLSPPGLEEEDVNGYVMPDTHLKGTPSSREGTLSSVGLSSVLGTEEEDEDEEYEYMNRRRRHSPPHPPRPSSLEELGYEYMDVGSDLSASLGSTQSCPLHPVPIMPTAGTTPDEDYEYMNRQRDGGGPGGDYAAMGACPASEQGYEEMRAFQGPGHQAPHVHYARLKTLRSLEATDSAFDNPDYWHSRLFPKANAQRT	Clinical trial	Molecular pharmacodynamics of PM02734 (elisidepsin) as single agent and in combination with erlotinib; synergistic activity in human non-small cell lung cancer cell lines and xenograft models. Eur J Cancer. 2009 Jul;45(10):1855-64.	21	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Furin-like cysteine rich region; Growth factor receptor domain IV; Protein tyrosine kinase; Receptor L domain	PF00757; PF14843; PF07714; PF01030	PF00757; Furin-like; PF14843; GF_recep_IV; PF07714; Pkinase_Tyr; PF01030; Recep_L_domain	.	.	hsa04012:ErbB signaling pathway; hsa04020:Calcium signaling pathway; hsa04144:Endocytosis; hsa05205:Proteoglycans in cancer; hsa05206:MicroRNAs in cancer	"R-HSA-1227986: Signaling by ERBB2; R-HSA-1236394: Signaling by ERBB4; R-HSA-1250196: SHC1 events in ERBB2 signaling; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1306955: GRB7 events in ERBB2 signaling; R-HSA-1358803: Downregulation of ERBB2:ERBB3 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; R-HSA-6785631: ERBB2 Regulates Cell Motility; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-8847993: ERBB2 Activates PTK6 Signaling; R-HSA-8863795: Downregulation of ERBB2 signaling; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants"	.	P21860
TTWALCO	HER4 messenger RNA (ERBB4 mRNA)	Q15303	ERBB4_HUMAN	mRNA target	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)	ERBB4	"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."	EC 2.7.10.1	3U9U; 3U7U; 3U2P; 3BCE; 3BBW	MKPATGLWVWVSLLVAAGTVQPSDSQSVCAGTENKLSSLSDLEQQYRALRKYYENCEVVMGNLEITSIEHNRDLSFLRSVREVTGYVLVALNQFRYLPLENLRIIRGTKLYEDRYALAIFLNYRKDGNFGLQELGLKNLTEILNGGVYVDQNKFLCYADTIHWQDIVRNPWPSNLTLVSTNGSSGCGRCHKSCTGRCWGPTENHCQTLTRTVCAEQCDGRCYGPYVSDCCHRECAGGCSGPKDTDCFACMNFNDSGACVTQCPQTFVYNPTTFQLEHNFNAKYTYGAFCVKKCPHNFVVDSSSCVRACPSSKMEVEENGIKMCKPCTDICPKACDGIGTGSLMSAQTVDSSNIDKFINCTKINGNLIFLVTGIHGDPYNAIEAIDPEKLNVFRTVREITGFLNIQSWPPNMTDFSVFSNLVTIGGRVLYSGLSLLILKQQGITSLQFQSLKEISAGNIYITDNSNLCYYHTINWTTLFSTINQRIVIRDNRKAENCTAEGMVCNHLCSSDGCWGPGPDQCLSCRRFSRGRICIESCNLYDGEFREFENGSICVECDPQCEKMEDGLLTCHGPGPDNCTKCSHFKDGPNCVEKCPDGLQGANSFIFKYADPDRECHPCHPNCTQGCNGPTSHDCIYYPWTGHSTLPQHARTPLIAAGVIGGLFILVIVGLTFAVYVRRKSIKKKRALRRFLETELVEPLTPSGTAPNQAQLRILKETELKRVKVLGSGAFGTVYKGIWVPEGETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQLVTQLMPHGCLLEYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQRYLVIQGDDRMKLPSPNDSKFFQNLLDEEDLEDMMDAEEYLVPQAFNIPPPIYTSRARIDSNRSEIGHSPPPAYTPMSGNQFVYRDGGFAAEQGVSVPYRAPTSTIPEAPVAQGATAEIFDDSCCNGTLRKPVAPHVQEDSSTQRYSADPTVFAPERSPRGELDEEGYMTPMRDKPKQEYLNPVEENPFVSRRKNGDLQALDNPEYHNASNGPPKAEDEYVNEPLYLNTFANTLGKAEYLKNNILSMPEKAKKAFDNPDYWNHSLPPRSTLQHPDYLQEYSTKYFYKQNGRIRPIVAENPEYLSEFSLKPGTVLPPPPYRHRNTVV	Literature-reported	"US patent application no. 6,255,111, Antisense modulation of Her-4 expression."	0	mRNA	mRNA target	.	.	.	Furin-like cysteine rich region; Growth factor receptor domain IV; Protein tyrosine kinase; Receptor L domain	PF00757; PF14843; PF07714; PF01030	PF00757; Furin-like; PF14843; GF_recep_IV; PF07714; Pkinase_Tyr; PF01030; Recep_L_domain	.	.	hsa04012:ErbB signaling pathway; hsa04020:Calcium signaling pathway; hsa04144:Endocytosis; hsa05205:Proteoglycans in cancer	"R-HSA-1227986: Signaling by ERBB2; R-HSA-1236394: Signaling by ERBB4; 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-1253288: Downregulation of ERBB4 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-5673001: RAF/MAP kinase cascade; R-HSA-6785631: ERBB2 Regulates Cell Motility; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-8847993: ERBB2 Activates PTK6 Signaling; R-HSA-8863795: Downregulation of ERBB2 signaling; R-HSA-9018519: Estrogen-dependent gene expression; R-HSA-9620244: Long-term potentiation; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants"	.	Q15303
TT0JESD	Erbb4 tyrosine kinase receptor (Erbb-4)	Q15303	ERBB4_HUMAN	Kinase	Tyrosine kinase-type cell surface receptor HER4; Receptor tyrosine-protein kinase erbB-4; Proto-oncogene-like protein c-ErbB-4; P180erbB4; HER4	ERBB4	"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."	EC 2.7.10.1	3U9U; 3U7U; 3U2P; 3BCE; 3BBW	MKPATGLWVWVSLLVAAGTVQPSDSQSVCAGTENKLSSLSDLEQQYRALRKYYENCEVVMGNLEITSIEHNRDLSFLRSVREVTGYVLVALNQFRYLPLENLRIIRGTKLYEDRYALAIFLNYRKDGNFGLQELGLKNLTEILNGGVYVDQNKFLCYADTIHWQDIVRNPWPSNLTLVSTNGSSGCGRCHKSCTGRCWGPTENHCQTLTRTVCAEQCDGRCYGPYVSDCCHRECAGGCSGPKDTDCFACMNFNDSGACVTQCPQTFVYNPTTFQLEHNFNAKYTYGAFCVKKCPHNFVVDSSSCVRACPSSKMEVEENGIKMCKPCTDICPKACDGIGTGSLMSAQTVDSSNIDKFINCTKINGNLIFLVTGIHGDPYNAIEAIDPEKLNVFRTVREITGFLNIQSWPPNMTDFSVFSNLVTIGGRVLYSGLSLLILKQQGITSLQFQSLKEISAGNIYITDNSNLCYYHTINWTTLFSTINQRIVIRDNRKAENCTAEGMVCNHLCSSDGCWGPGPDQCLSCRRFSRGRICIESCNLYDGEFREFENGSICVECDPQCEKMEDGLLTCHGPGPDNCTKCSHFKDGPNCVEKCPDGLQGANSFIFKYADPDRECHPCHPNCTQGCNGPTSHDCIYYPWTGHSTLPQHARTPLIAAGVIGGLFILVIVGLTFAVYVRRKSIKKKRALRRFLETELVEPLTPSGTAPNQAQLRILKETELKRVKVLGSGAFGTVYKGIWVPEGETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQLVTQLMPHGCLLEYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQRYLVIQGDDRMKLPSPNDSKFFQNLLDEEDLEDMMDAEEYLVPQAFNIPPPIYTSRARIDSNRSEIGHSPPPAYTPMSGNQFVYRDGGFAAEQGVSVPYRAPTSTIPEAPVAQGATAEIFDDSCCNGTLRKPVAPHVQEDSSTQRYSADPTVFAPERSPRGELDEEGYMTPMRDKPKQEYLNPVEENPFVSRRKNGDLQALDNPEYHNASNGPPKAEDEYVNEPLYLNTFANTLGKAEYLKNNILSMPEKAKKAFDNPDYWNHSLPPRSTLQHPDYLQEYSTKYFYKQNGRIRPIVAENPEYLSEFSLKPGTVLPPPPYRHRNTVV	Successful	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Ligand id: 7422).	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Furin-like cysteine rich region; Growth factor receptor domain IV; Protein tyrosine kinase; Receptor L domain	PF00757; PF14843; PF07714; PF01030	PF00757; Furin-like; PF14843; GF_recep_IV; PF07714; Pkinase_Tyr; PF01030; Recep_L_domain	8.A.23.1.17	The Basigin (Basigin) Family	hsa04012:ErbB signaling pathway; hsa04020:Calcium signaling pathway; hsa04144:Endocytosis; hsa05205:Proteoglycans in cancer	"R-HSA-1227986: Signaling by ERBB2; R-HSA-1236394: Signaling by ERBB4; 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-1253288: Downregulation of ERBB4 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-5673001: RAF/MAP kinase cascade; R-HSA-6785631: ERBB2 Regulates Cell Motility; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-8847993: ERBB2 Activates PTK6 Signaling; R-HSA-8863795: Downregulation of ERBB2 signaling; R-HSA-9018519: Estrogen-dependent gene expression; R-HSA-9620244: Long-term potentiation; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants"	.	Q15303
TTYSB89	Epiregulin (EREG)	O14944	EREG_HUMAN	Growth factor	l=Epiregulin; Proepiregulin; EPR	EREG	"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."	.	5WB7; 5E8D; 1K37; 1K36	MTAGRRMEMLCAGRVPALLLCLGFHLLQAVLSTTVIPSCIPGESSDNCTALVQTEDNPRVAQVSITKCSSDMNGYCLHGQCIYLVDMSQNYCRCEVGYTGVRCEHFFLTVHQPLSKEYVALTVILIILFLITVVGSTYYFCRWYRNRKSKEPKKEYERVTSGDPELPQV	Clinical trial	Generation and activity of a humanized monoclonal antibody that selectively neutralizes the epidermal growth factor receptor ligands transforming growth factor-alpha and epiregulin. J Pharmacol Exp Ther. 2014 May;349(2):330-43.	19	Growth factor	Growth factor	.	.	.	.	.	.	.	.	hsa04012:ErbB signaling pathway	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	.	O14944
TTGXULC	ETS-domain transcription factor ERF (ERF)	P50548	ERF_HUMAN	E26 transformation-specific ETS	Transcription factor Ets2; PE-2; Ets2 repressor factor; ETS domain-containing transcription factor ERF	ERF	"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."	.	.	MKTPADTGFAFPDWAYKPESSPGSRQIQLWHFILELLRKEEYQGVIAWQGDYGEFVIKDPDEVARLWGVRKCKPQMNYDKLSRALRYYYNKRILHKTKGKRFTYKFNFNKLVLVNYPFIDVGLAGGAVPQSAPPVPSGGSHFRFPPSTPSEVLSPTEDPRSPPACSSSSSSLFSAVVARRLGRGSVSDCSDGTSELEEPLGEDPRARPPGPPDLGAFRGPPLARLPHDPGVFRVYPRPRGGPEPLSPFPVSPLAGPGSLLPPQLSPALPMTPTHLAYTPSPTLSPMYPSGGGGPSGSGGGSHFSFSPEDMKRYLQAHTQSVYNYHLSPRAFLHYPGLVVPQPQRPDKCPLPPMAPETPPVPSSASSSSSSSSSPFKFKLQPPPLGRRQRAAGEKAVAGADKSGGSAGGLAEGAGALAPPPPPPQIKVEPISEGESEEVEVTDISDEDEEDGEVFKTPRAPPAPPKPEPGEAPGASQCMPLKLRFKRRWSEDCRLEGGGGPAGGFEDEGEDKKVRGEGPGEAGGPLTPRRVSSDLQHATAQLSLEHRDS	Literature-reported	Selective inhibition of transcription of the Ets2 gene in prostate cancer cells by a triplex-forming oligonucleotide. Nucleic Acids Res. 2003 Feb 1;31(3):833-43.	.	ETS	.	ETS family.	.	.	Ets-domain	PF00178	PF00178; Ets	.	.	.	R-HSA-2559585: Oncogene Induced Senescence	.	P50548
TTKIAT3	Inositol-requiring protein 1 (IRE1a)	O75460	ERN1_HUMAN	.	hIRE1p; Serine/threonine-protein kinase/endoribonuclease IRE1; Ire1-alpha; IRE1a; IRE1; Endoplasmic reticulum-to-nucleus signaling 1	ERN1	"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."	.	6HX1; 6HV0; 5HGI; 4Z7H; 4Z7G	MPARRLLLLLTLLLPGLGIFGSTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGSKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQREGLRKVMHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDVKFDPGLKSKNKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKKSFEEVINLVDQTSENAPTTVSRDVEEKPAHAPARPEAPVDSMLKDMATIILSTFLLIGWVAFIITYPLSMHQQQQLQHQQFQKELEKIQLLQQQQQQLPFHPPGDTAQDGELLDTSGPYSESSGTSSPSTSPRASNHSLCSGSSASKAGSSPSLEQDDGDEETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFHEPPEPQPPVTPDAL	Literature-reported	IRE1 signaling exacerbates Alzheimer's disease pathogenesis. Acta Neuropathol. 2017 Sep;134(3):489-506.	.	.	.	.	.	.	.	.	.	.	.	hsa04140: Autophagy - animal; hsa04141: Protein processing in endoplasmic reticulum; hsa04210: Apoptosis; hsa04932: Non-alcoholic fatty liver disease; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05014: Amyotrophic lateral sclerosis; hsa05016: Huntington disease; hsa05017: Spinocerebellar ataxia; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05417: Lipid and atherosclerosis	R-HSA-381070: IRE1alpha activates chaperones	.	O75460
TTOJ9QL	Endoplasmic reticulum to nucleus signaling 1 (ERN1)	O75460	ERN1_HUMAN	Kinase	Serine/threonine-protein kinase/endoribonuclease IRE1; Ire1-alpha; IRE1a; IRE1; Inositol-requiring protein 1; hIRE1p; Endoplasmic reticulum-to-nucleus signaling 1	ERN1	"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)."	.	6HX1; 6HV0; 5HGI; 4Z7H; 4Z7G	MPARRLLLLLTLLLPGLGIFGSTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGSKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQREGLRKVMHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDVKFDPGLKSKNKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKKSFEEVINLVDQTSENAPTTVSRDVEEKPAHAPARPEAPVDSMLKDMATIILSTFLLIGWVAFIITYPLSMHQQQQLQHQQFQKELEKIQLLQQQQQQLPFHPPGDTAQDGELLDTSGPYSESSGTSSPSTSPRASNHSLCSGSSASKAGSSPSLEQDDGDEETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFHEPPEPQPPVTPDAL	Clinical trial	Synthesis of novel tricyclic chromenone-based inhibitors of IRE-1 RNase activity. J Med Chem. 2014 May 22;57(10):4289-301.	0	EC:2.7	.	protein kinase superfamily. Ser/Thr protein kinase family.	2.7.11.1 	Transferring phosphorus-containing groups	Protein kinase domain; Ribonuclease 2-5A	PF00069; PF06479	PF00069; Pkinase; PF06479; Ribonuc_2-5A	.	.	hsa04140: Autophagy - animal; hsa04141: Protein processing in endoplasmic reticulum; hsa04210: Apoptosis; hsa04932: Non-alcoholic fatty liver disease; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05014: Amyotrophic lateral sclerosis; hsa05016: Huntington disease; hsa05017: Spinocerebellar ataxia; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05417: Lipid and atherosclerosis	R-HSA-381070: IRE1alpha activates chaperones	.	O75460
TTQMNEJ	Endogenous retrovirus group K Env polyprotein (ENK)	Q9HDB8; Q69384	ENK5_HUMAN; ENK6_HUMAN	.	HERV-envelope protein; HERV-K provirus ancestral Env polyprotein; HERV-K envelope protein; Envelope polyprotein; Endogenous retrovirus group K member  Env polyprotein; ERVK	ERVK-5	"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."	.	.	MVTPVTWMDNPIEVYVNDSVWVPGPTDDRCPAKPEEEGMMINISIVYRYPPICLGRAPGCLMPAVQNWLVEVPTVSPNSRFTYHMVSGMSLRPRVNYLQDFSYQRSLKFRPKGKPCPKEIPKESKNTEVLVWEECVANSAVILQNNEFGTIIDWAPRGQFYHNCSGQTQSCPSAQVSPAVDSDLTESLDKHKHKKLQSFYPWEWGEKGISTPRPEIISPVSGPEHPELWRLWPDTTLEFGLEIKL	Literature-reported	Infectious Entry Pathway Mediated by the Human Endogenous Retrovirus K Envelope Protein. J Virol. 2016 Jan 20;90(7):3640-9.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9HDB8
TTZAYWL	Estrogen receptor (ESR)	P03372	ESR1_HUMAN	Nuclear hormone receptor	Nuclear receptor subfamily 3 group A member 1; NR3A1; Estradiol receptor; ESR; ER-alpha; ER	ESR1	"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."	.	6IAR; 6HMU; 6HKF; 6HKB; 6HHP	MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKRSKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV	Successful	Beta3-tubulin is induced by estradiol in human breast carcinoma cells through an estrogen-receptor dependent pathway. Cell Motil Cytoskeleton. 2009 Jul;66(7):378-88.	34	Nuclear hormone receptor	Zinc finger	nuclear hormone receptor family. NR3 subfamily.	.	.	"Oestrogen-type nuclear receptor final C-terminal ; Ligand-binding domain of nuclear hormone receptor; Oestrogen receptor; Zinc finger, C4 type (two domains)"	PF12743; PF00104; PF02159; PF00105	PF12743; ESR1_C; PF00104; Hormone_recep; PF02159; Oest_recep; PF00105; zf-C4	.	.	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	R-HSA-1251985:Nuclear signaling by ERBB4; R-HSA-383280:Nuclear Receptor transcription pathway	.	P03372
TTAHMI6	HUMAN estrogen receptor (ESR1)	P03372	ESR1_HUMAN	Nuclear hormone receptor	Nuclear receptor subfamily 3 group A member 1; NR3A1; Estradiol receptor; ESR; ER-alpha; ER	ESR1	"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."	.	6IAR; 6HMU; 6HKF; 6HKB; 6HHP	MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKRSKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV	.	Prevention and therapy of COVID-19 via exogenous estrogen treatment for both male and female patients. J Pharm Pharm Sci. 2020;23(1):75-85.	.	.	.	.	.	.	.	.	.	.	.	hsa01522: Endocrine resistance; hsa04915: Estrogen signaling pathway; hsa04917: Prolactin signaling pathway; hsa04919: Thyroid hormone signaling pathway; hsa04961: Endocrine and other factor-regulated calcium reabsorption; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05224: Breast cancer	"R-HSA-1251985: Nuclear signaling by ERBB4; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-383280: Nuclear Receptor transcription pathway; R-HSA-4090294: SUMOylation of intracellular receptors; R-HSA-5689896: Ovarian tumor domain proteases; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-8866910: TFAP2 (AP-2) family regulates transcription of growth factors and their receptors; R-HSA-8931987: RUNX1 regulates estrogen receptor mediated transcription; R-HSA-8939211: ESR-mediated signaling; R-HSA-8939256: RUNX1 regulates transcription of genes involved in WNT signaling; R-HSA-8939902: Regulation of RUNX2 expression and activity; R-HSA-9009391: Extra-nuclear estrogen signaling; R-HSA-9018519: Estrogen-dependent gene expression"	.	P03372
TTOM3J0	Estrogen receptor beta (ESR2)	Q92731	ESR2_HUMAN	Nuclear hormone receptor	Oestrogen receptor beta; Nuclear receptor subfamily 3 group A member 2; NR3A2; Erbeta; ESTRB; ER-beta; Beta-1	ESR2	"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."	.	5TOA; 4ZI1; 4J26; 4J24; 3OMQ	MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPSNVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQKSPWCEARSLEHTLPVNRETLKRKVSGNRCASPVTGPGSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRLVRRQRSADEQLHCAGKAKRSGGHAPRVRELLLDALSPEQLVLTLLEAEPPHVLISRPSAPFTEASMMMSLTKLADKELVHMISWAKKIPGFVELSLFDQVRLLESCWMEVLMMGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPLVTATQDADSSRKLAHLLNAVTDALVWVIAKSGISSQQQSMRLANLLMLLSHVRHASNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKSKEGSQNPQSQ	Successful	Differential biochemical and cellular actions of Premarin estrogens: distinct pharmacology of bazedoxifene-conjugated estrogens combination. Mol Endocrinol. 2009 Jan;23(1):74-85.	34	Nuclear hormone receptor	Nuclear hormone receptor	nuclear hormone receptor family. NR3 subfamily.	.	.	"Estrogen receptor beta; Ligand-binding domain of nuclear hormone receptor; Zinc finger, C4 type (two domains)"	PF12497; PF00104; PF00105	PF12497; ERbeta_N; PF00104; Hormone_recep; PF00105; zf-C4	.	.	hsa04915:Estrogen signaling pathway; hsa04917:Prolactin signaling pathway	R-HSA-383280:Nuclear Receptor transcription pathway	.	Q92731
TTPNQAC	Estrogen-related receptor-alpha (ESRRA)	P11474	ERR1_HUMAN	Nuclear hormone receptor	"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"	ESRRA	"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'."	.	3K6P; 3D24; 2PJL; 1XB7	MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVALAPGPAPTRCLPGHKEEEDGEGAGPGEQGGGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGPFPAGPLAVAGGPRKTAAPVNALVSHLLVVEPEKLYAMPDPAGPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGELGAALLQLVRRLQALRLEREEYVLLKALALANSDSVHIEDAEAVEQLREALHEALLEYEAGRAGPGGGAERRRAGRLLLTLPLLRQTAGKVLAHFYGVKLEGKVPMHKLFLEMLEAMMD	Successful	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 622).	34	Nuclear hormone receptor	Nuclear hormone receptor	nuclear hormone receptor family. NR3 subfamily.	.	.	"Ligand-binding domain of nuclear hormone receptor; Zinc finger, C4 type (two domains)"	PF00104; PF00105	PF00104; Hormone_recep; PF00105; zf-C4	.	.	.	R-HSA-1989781:PPARA activates gene expression; R-HSA-2151201:Transcriptional activation of mitochondrial biogenesis; R-HSA-383280:Nuclear Receptor transcription pathway	.	P11474
TTP3UTW	Steroid hormone receptor ERR (ESRR)	P11474; O95718; P62508	ERR1_HUMAN; ERR2_HUMAN; ERR3_HUMAN	Nuclear hormone receptor	Nuclear receptor subfamily 3 group B; NR3B; ERR	ESRRA	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	.	.	MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVALAPGPAPTRCLPGHKEEEDGEGAGPGEQGGGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGPFPAGPLAVAGGPRKTAAPVNALVSHLLVVEPEKLYAMPDPAGPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGELGAALLQLVRRLQALRLEREEYVLLKALALANSDSVHIEDAEAVEQLREALHEALLEYEAGRAGPGGGAERRRAGRLLLTLPLLRQTAGKVLAHFYGVKLEGKVPMHKLFLEMLEAMMD	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1989781: PPARA activates gene expression; R-HSA-2151201: Transcriptional activation of mitochondrial biogenesis; R-HSA-383280: Nuclear Receptor transcription pathway; R-HSA-8939902: Regulation of RUNX2 expression and activity	.	P11474
TTKF0XS	Estrogen-related receptor-beta (ESRRB)	O95718	ERR2_HUMAN	Nuclear hormone receptor	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	ESRRB	"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)."	.	1LO1	MSSDDRHLGSSCGSFIKTEPSSPSSGIDALSHHSPSGSSDASGGFGLALGTHANGLDSPPMFAGAGLGGTPCRKSYEDCASGIMEDSAIKCEYMLNAIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRLDSESSPYLSLQISPPAKKPLTKIVSYLLVAEPDKLYAMPPPGMPEGDIKALTTLCDLADRELVVIIGWAKHIPGFSSLSLGDQMSLLQSAWMEILILGIVYRSLPYDDKLVYAEDYIMDEEHSRLAGLLELYRAILQLVRRYKKLKVEKEEFVTLKALALANSDSMYIEDLEAVQKLQDLLHEALQDYELSQRHEEPWRTGKLLLTLPLLRQTAAKAVQHFYSVKLQGKVPMHKLFLEMLEAKV	Literature-reported	Identification of an agonist ligand for estrogen-related receptors ERRbeta/gamma. Bioorg Med Chem Lett. 2005 Mar 1;15(5):1311-3.	0	.	.	.	.	.	.	.	.	.	.	hsa04550: Signaling pathways regulating pluripotency of stem cells	R-HSA-383280: Nuclear Receptor transcription pathway	.	O95718
TT9ZRHB	Estrogen-related receptor-gamma (ESRRG)	P62508	ERR3_HUMAN	Nuclear hormone receptor	Nuclear receptor subfamily 3 group B member 3; NR3B3; KIAA0832; Estrogen-related receptor gamma; Estrogen receptor-related protein 3; ERRG2; ERR3; ERR gamma-2	ESRRG	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.	.	6A6K; 5YSO; 2ZKC; 2ZBS; 2ZAS	MDSVELCLPESFSLHYEEELLCRMSNKDRHIDSSCSSFIKTEPSSPASLTDSVNHHSPGGSSDASGSYSSTMNGHQNGLDSPPLYPSAPILGGSGPVRKLYDDCSSTIVEDPQTKCEYMLNSMPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRIDAENSPYLNPQLVQPAKKPYNKIVSHLLVAEPEKIYAMPDPTVPDSDIKALTTLCDLADRELVVIIGWAKHIPGFSTLSLADQMSLLQSAWMEILILGVVYRSLSFEDELVYADDYIMDEDQSKLAGLLDLNNAILQLVKKYKSMKLEKEEFVTLKAIALANSDSMHIEDVEAVQKLQDVLHEALQDYEAGQHMEDPRRAGKMLMTLPLLRQTSTKAVQHFYNIKLEGKVPMHKLFLEMLEAKV	Literature-reported	Flavone and isoflavone phytoestrogens are agonists of estrogen-related receptors. Mol Cancer Res. 2003 Nov;1(13):981-91.	0	Nuclear hormone receptor	.	nuclear hormone receptor family. NR3 subfamily.	.	.	"Ligand-binding domain of nuclear hormone receptor; Zinc finger, C4 type (two domains)"	PF00104; PF00105	PF00104; Hormone_recep; PF00105; zf-C4	.	.	.	R-HSA-383280: Nuclear Receptor transcription pathway	.	P62508
TTTGPSD	Protein C-ets-1 (ETS1)	P14921	ETS1_HUMAN	E26 transformation-specific ETS	P54; EWSR2	ETS1	"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."	.	5ZMC; 4LG0; 4L18; 4L0Z; 4L0Y	MKAAVDLKPTLTIIKTEKVDLELFPSPDMECADVPLLTPSSKEMMSQALKATFSGFTKEQQRLGIPKDPRQWTETHVRDWVMWAVNEFSLKGVDFQKFCMNGAALCALGKDCFLELAPDFVGDILWEHLEILQKEDVKPYQVNGVNPAYPESRYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILRDPLQTDTLQNDYFAIKQEVVTPDNMCMGRTSRGKLGGQDSFESIESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDSEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVIPAAALAGYTGSGPIQLWQFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDADE	Literature-reported	Differential regulation of the response to DNA damage in Ewing's sarcoma cells by ETS1 and EWS/FLI-1. Oncogene. 2002 Apr 25;21(18):2890-5.	.	ETS	.	ETS family.	.	.	Ets-domain; Sterile alpha motif (SAM)/Pointed domain	PF00178; PF02198	PF00178; Ets; PF02198; SAM_PNT	.	.	hsa04014: Ras signaling pathway; hsa04218: Cellular senescence; hsa05166: Human T-cell leukemia virus 1 infection; hsa05200: Pathways in cancer; hsa05211: Renal cell carcinoma	R-HSA-2559585: Oncogene Induced Senescence	.	P14921
TT9AH0M	Protein C-ets-2 (ETS2)	P15036	ETS2_HUMAN	E26 transformation-specific ETS	"ETS2IT1; ETS proto-oncogene 2, transcription factor"	ETS2	Binds specifically the DNA GGAA/T core motif (Ets-binding site or EBS) in gene promoters and stimulates transcription. Transcription factor activating transcription.	.	4MHV; 4BQA	MNDFGIKNMDQVAPVANSYRGTLKRQPAFDTFDGSLFAVFPSLNEEQTLQEVPTGLDSISHDSANCELPLLTPCSKAVMSQALKATFSGFKKEQRRLGIPKNPWLWSEQQVCQWLLWATNEFSLVNVNLQRFGMNGQMLCNLGKERFLELAPDFVGDILWEHLEQMIKENQEKTEDQYEENSHLTSVPHWINSNTLGFGTEQAPYGMQTQNYPKGGLLDSMCPASTPSVLSSEQEFQMFPKSRLSSVSVTYCSVSQDFPGSNLNLLTNNSGTPKDHDSPENGADSFESSDSLLQSWNSQSSLLDVQRVPSFESFEDDCSQSLCLNKPTMSFKDYIQERSDPVEQGKPVIPAAVLAGFTGSGPIQLWQFLLELLSDKSCQSFISWTGDGWEFKLADPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTSGKRYVYRFVCDLQNLLGFTPEELHAILGVQPDTED	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	ETS	.	ETS family.	.	.	Ets-domain; Sterile alpha motif (SAM)/Pointed domain	PF00178; PF02198	PF00178; Ets; PF02198; SAM_PNT	.	.	hsa04014: Ras signaling pathway; hsa05166: Human T-cell leukemia virus 1 infection	R-HSA-2559585: Oncogene Induced Senescence	.	P15036
TT2F0AU	Ebola virus Envelope glycoprotein (EV GP)	Q05320	VGP_EBOZM	.	"GP1,2; GP"	EV GP	"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."	.	.	MGVTGILQLPRDRFKRTSFFLWVIILFQRTFSIPLGVIHNSTLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNETEYLFEVDNLTYVQLESRFTPQFLLQLNETIYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKNLTRKIRSEELSFTVVSNGAKNISGQSPARTSSDPGTNTTTEDHKIMASENSSAMVQVHSQGREAAVSHLTTLATISTSPQSLTTKPGPDNSTHNTPVYKLDISEATQVEQHHRRTDNDSTASDTPSATTAAGPPKAENTNTSKSTDFLDPATTTSPQNHSETAGNNNTHHQDTGEESASSGKLGLITNTIAGVAGLITGGRRTRREAIVNAQPKCNPNLHYWTTQDEGAAIGLAWIPYFGPAAEGIYIEGLMHNQDGLICGLRQLANETTQALQLFLRATTELRTFSILNRKAIDFLLQRWGGTCHILGPDCCIEPHDWTKNITDKIDQIIHDFVDKTLPDQGDNDNWWTGWRQWIPAGIGVTGVIIAVIALFCICKFVF	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health  Human Services. 2020	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTDJLWQ	Ebola virus VP24 messenger RNA (EV VP24 mRNA)	Q5XX02	VP24_EBOSU	mRNA target	rVP24 (mRNA); VP24 (mRNA); Reston VP24 (mRNA); Membrane-associated protein VP24 (mRNA)	EV VP24 mRNA	"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."	.	3VNF; 3VNE	MAKATGRYNLVTPKRELEQGVVFSDLCNFLVTPTVQGWKVYWAGLEFDVNQKGITLLNRLKVNDFAPAWAMTRNLFPHLFKNQQSEVQTPIWALRVILAAGILDQLMDHSLIEPLSGALNLIADWLLTTSTNHFNMRTQRVKDQLSMRMLSLIRSNIINFINKLETLHVVNYKGLLSSVEIGTPSYAIIITRTNMGYLVEVQEPDKSAMDIRHPGPVKFSLLHESTLKPVATPKPSSITSLIMEFNSSLAI	Clinical trial	Discovery and Early Development of AVI-7537 and AVI-7288 for the Treatment of Ebola Virus and Marburg Virus Infections. Viruses. 2012 November; 4(11): 2806-2830.	17	mRNA	mRNA target	.	.	.	Filovirus membrane-associated protein VP24	PF06389	PF06389; Filo_VP24	.	.	.	.	.	.
TTS6VPR	Ebola virus VP30-NP interaction (EV VP30-NP PPI)	Q05323-P18272	VP30_EBOZM-NCAP_EBOZM	.	Ebola VP30-Nucleocapsid protein interaction	EV VP30-NP PPI	Plays both essential and inhibitory roles in Ebola virus RNA synthesis.	.	.	MEASYERGRPRAARQHSRDGHDHHVRARSSSRENYRGEYRQSRSASQVRVPTVFHKKRVEPLTVPPAPKDICPTLKKGFLCDSSFCKKDHQLESLTDRELLLLIARKTCGSVEQQLNITAPKDSRLANPTADDFQQEEGPKITLLTLIKTAEHWARQDIRTIEDSKLRALLTLCAVMTRKFSKSQLSLLCETHLRREGLGQDQAEPVLEVYQRLHSDKGGSFEAALWQQWDRQSLIMFITAFLNIALQLPCESSAVVVSGLRTLVPQSDNEEASTNPGTCSWSDEGTPMDSRPQKIWMAPSLTESDMDYHKILTAGLSVQQGIVRQRVIPVYQVNNLEEICQLIIQAFEAGVDFQESADSFLLMLCLHHAYQGDYKLFLESGAVKYLEGHGFRFEVKKRDGVKRLEELLPAVSSGKNIKRTLAAMPEEETTEANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHAEQGLIQYPTAWQSVGHMMVIFRLMRTNFLIKFLLIHQGMHMVAGHDANDAVISNSVAQARFSGLLIVKTVLDHILQKTERGVRLHPLARTAKVKNEVNSFKAALSSLAKHGEYAPFARLLNLSGVNNLEHGLFPQLSAIALGVATAHGSTLAGVNVGEQYQQLREAATEAEKQLQQYAESRELDHLGLDDQEKKILMNFHQKKNEISFQQTNAMVTLRKERLAKLTEAITAASLPKTSGHYDDDDDIPFPGPINDDDNPGHQDDDPTDSQDTTIPDVVVDPDDGSYGEYQSYSENGMNAPDDLVLFDLDEDDEDTKPVPNRSTKGGQQKNSQKGQHIEGRQTQSRPIQNVPGPHRTIHHASAPLTDNDRRNEPSGSTSPRMLTPINEEADPLDDADDETSSLPPLESDDEEQDRDGTSNRTPTVAPPAPVYRDHSEKKELPQDEQQDQDHTQEARNQDSDNTQSEHSFEEMYRHILRSQGPFDAVLYYHMMKDEPVVFSTSDGKEYTYPDSLEEEYPPWLTEKEAMNEENRFVTLDGQQFYWPVMNHKNKFMAILQHHQ	Literature-reported	Ebola virus VP30 and nucleoprotein interactions modulate viral RNA synthesis. Nat Commun. 2017 Jun 8;8:15576.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3Z102	Ebola virus VP35 messenger RNA (EV VP35 mRNA)	Q5XX07	VP35_EBOSU	mRNA target	VP35 (mRNA); Polymerase cofactor VP35 (mRNA)	EV VP35 mRNA	"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."	.	.	MQQDRTYRHHGPEVSGWFSEQLMTGKIPLTEVFVDVENKPSPAPITIISKNPKTTRKSDKQVQTDDASSLLTEEVKAAINSVISAVRRQTNAIESLEGRVTTLEASLKPVQDMAKTISSLNRSCAEMVAKYDLLVMTTGRATATAAATEAYWNEHGQAPPGPSLYEDDAIKAKLKDPNGKVPESVKQAYINLDSTSALNEENFGRPYISAKDLKEIIYDHLPGFGTAFHQLVQVICKIGKDNNILDIIHAEFQASLAEGDSPQCALIQITKRIPAFQDASPPIVHIKSRGDIPKACQKSLRPVPPSPKIDRGWVCIFQFQDGKALGLKI	Clinical trial	Discovery and Early Development of AVI-7537 and AVI-7288 for the Treatment of Ebola Virus and Marburg Virus Infections. Viruses. 2012 November; 4(11): 2806-2830.	17	mRNA	mRNA target	.	.	.	Filoviridae VP35	PF02097	PF02097; Filo_VP35	.	.	.	.	.	.
TTHOM2S	EWS-FLI1 fusion gene mRNA (EWS-FLI1 mRNA)	Q01844-Q01543	EWS_HUMAN-FLI1_HUMAN	.	.	EWS-FLI1	.	.	.	.	Clinical trial	National Cancer Institute Drug Dictionary (drug id 780967).	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q01844
TTUY9C6	Eyes absent homolog 2	.	EYA2_HUMAN	Single Protein	EYA transcriptional coactivator and phosphatase 2; EAB1; EYA2	EYA2	"Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5. Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress."	.	.	MVELVISPSLTVNSDCLDKLKFNRADAAVWTLSDRQGITKSAPLRVSQLFSRSCPRVLPRQPSTAMAAYGQTQYSAGIQQATPYTAYPPPAQAYGIPSYSIKTEDSLNHSPGQSGFLSYGSSFSTSPTGQSPYTYQMHGTTGFYQGGNGLGNAAGFGSVHQDYPSYPGFPQSQYPQYYGSSYNPPYVPASSICPSPLSTSTYVLQEASHNVPNQSSESLAGEYNTHNGPSTPAKEGDTDRPHRASDGKLRGRSKRSSDPSPAGDNEIERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLSTYNFSADGFHSSAPGANLCLGSGVHGGVDWMRKLAFRYRRVKEMYNTYKNNVGGLIGTPKRETWLQLRAELEALTDLWLTHSLKALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQRFGRKAVYVVIGDGVEEEQGAKKHNMPFWRISCHADLEALRHALELEYL	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	O00167
TTNJA0C	Enhancer of zeste homolog 1 (EZH1)	Q92800	EZH1_HUMAN	Methyltransferase	KIAA0388; Histone-lysine N-methyltransferase EZH1; ENX-2	EZH1	"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."	EC 2.1.1.43	.	MEIPNPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEWKKLRVQPVQSMKPVSGHPFLKKCTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQNFMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMIPGSVLISDAVFLELVDALNQYSDEEEEGHNDTSDGKQDDSKEDLPVTRKRKRHAIEGNKKSSKKQFPNDMIFSAIASMFPENGVPDDMKERYRELTEMSDPNALPPQCTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNVYKRKNKEIKIEPEPCGTDCFLLLEGAKEYAMLHNPRSKCSGRRRRRHHIVSASCSNASASAVAETKEGDSDRDTGNDWASSSSEANSRCQTPTKQKASPAPPQLCVVEAPSEPVEWTGAEESLFRVFHGTYFNNFCSIARLLGTKTCKQVFQFAVKESLILKLPTDELMNPSQKKKRKHRLWAAHCRKIQLKKDNSSTQVYNYQPCDHPDRPCDSTCPCIMTQNFCEKFCQCNPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIERETDVL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	EC:2.1	.	class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily.	2.1.1.43	Transferring one-carbon groups	WD repeat binding protein EZH2; Polycomb repressive complex 2 tri-helical domain; CXC domain; SET domain	PF11616; PF18118; PF18264; PF00856	PF11616; EZH2_WD-Binding; PF18118; PRC2_HTH_1; PF18264; preSET_CXC; PF00856; SET	.	.	hsa00310: Lysine degradation; hsa01100: Metabolic pathways	.	MetaCyc:HS03158-MON	Q92800
TT9MZCQ	Enhancer of zeste homolog 2 (EZH2)	Q15910	EZH2_HUMAN	Methyltransferase	Lysine Nmethyltransferase 6; Lysine N-methyltransferase 6; KMT6; Histonelysine Nmethyltransferase EZH2; Histone-lysine N-methyltransferase EZH2; EZH2; ENX1; ENX-1	EZH2	"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."	EC 2.1.1.43	6C24; 6C23; 5WUK; 5WG6; 5U62	MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP	Successful	Selective inhibition of EZH2 by EPZ-6438 leads to potent antitumor activity in EZH2-mutant non-Hodgkin lymphoma. Mol Cancer Ther. 2014 Apr;13(4):842-54.	21	EC:2.1	Methyltransferase superfamily	class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily.	2.1.1.43 	Transferring one-carbon groups	WD repeat binding protein EZH2; Polycomb repressive complex 2 tri-helical domain; CXC domain; SET domain	PF11616; PF18118; PF18264; PF00856	PF11616; EZH2_WD-Binding; PF18118; PRC2_HTH_1; PF18264; preSET_CXC; PF00856; SET	.	.	hsa05206:MicroRNAs in cancer	R-HSA-212300:PRC2 methylates histones and DNA; R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-3214841:PKMTs methylate histone lysines	MetaCyc:HS02911-MON	Q15910
TTJBYRU	EZH2 Y641F mutant (EZH2 Y641F)	Q15910	EZH2_HUMAN	.	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	EZH2	"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."	EC 2.1.1.43	6C24; 6C23; 5WUK; 5WG6; 5U62	MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP	Patented-recorded	EZH2 inhibitors: a patent review (2014-2016).Expert Opin Ther Pat. 2017 Jul;27(7):797-813.	15.5	.	Class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily.	.	.	.	WD repeat binding protein EZH2; Polycomb repressive complex 2 tri-helical domain; CXC domain; SET domain	PF11616; PF18118; PF18264; PF00856	PF11616; EZH2_WD-Binding; PF18118; PRC2_HTH_1; PF18264; preSET_CXC; PF00856; SET	.	.	hsa00310: Lysine degradation; hsa01100: Metabolic pathways; hsa05206: MicroRNAs in cancer	R-HSA-212300: PRC2 methylates histones and DNA; R-HSA-2559580: Oxidative Stress Induced Senescence; R-HSA-3214841: PKMTs methylate histone lysines; R-HSA-5617472: Activation of anterior HOX genes in hindbrain development during early embryogenesis; R-HSA-8943724: Regulation of PTEN gene transcription; R-HSA-8953750: Transcriptional Regulation by E2F6; R-HSA-9609690: HCMV Early Events; R-HSA-9710421: Defective pyroptosis	MetaCyc:HS02911-MON	Q15910
TTJW2UQ	EZH2 Y641N mutant (EZH2 Y641N)	Q15910	EZH2_HUMAN	.	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	EZH2	"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."	EC 2.1.1.43	6C24; 6C23; 5WUK; 5WG6; 5U62	MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP	Patented-recorded	EZH2 inhibitors: a patent review (2014-2016).Expert Opin Ther Pat. 2017 Jul;27(7):797-813.	15.5	.	Class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily.	.	.	.	WD repeat binding protein EZH2; Polycomb repressive complex 2 tri-helical domain; CXC domain; SET domain	PF11616; PF18118; PF18264; PF00856	PF11616; EZH2_WD-Binding; PF18118; PRC2_HTH_1; PF18264; preSET_CXC; PF00856; SET	.	.	hsa00310: Lysine degradation; hsa01100: Metabolic pathways; hsa05206: MicroRNAs in cancer	R-HSA-212300: PRC2 methylates histones and DNA; R-HSA-2559580: Oxidative Stress Induced Senescence; R-HSA-3214841: PKMTs methylate histone lysines; R-HSA-5617472: Activation of anterior HOX genes in hindbrain development during early embryogenesis; R-HSA-8943724: Regulation of PTEN gene transcription; R-HSA-8953750: Transcriptional Regulation by E2F6; R-HSA-9609690: HCMV Early Events; R-HSA-9710421: Defective pyroptosis	MetaCyc:HS02911-MON	Q15910
TTE47YC	Cytovillin (EZR)	P15311	EZRI_HUMAN	.	p81; Villin-2; VIL2	EZR	"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."	.	4RMA; 4RM9; 4RM8; 1NI2	MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPEDVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL	Literature-reported	Expression of Ezrin and Estrogen Receptors During Cervical Carcinogenesis. Reprod Sci. 2017 May;24(5):706-712.	.	.	.	.	.	.	.	.	.	.	.	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	R-HSA-373752: Netrin-1 signaling; R-HSA-437239: Recycling pathway of L1; R-HSA-9662360: Sensory processing of sound by inner hair cells of the cochlea; R-HSA-9662361: Sensory processing of sound by outer hair cells of the cochlea	.	P15311
TTCIHJA	Coagulation factor Xa (F10)	P00742	FA10_HUMAN	Peptidase	Fxa; Factor Xa; F10; Activated coagulation factor X	F10	"Factor Xa is avitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting."	EC 3.4.21.6	6RK9; 5VOF; 5VOE; 5K0H; 5JZU	MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK	Successful	Pfizer. Product Development Pipeline. March 31 2009.	34	.	.	.	.	.	.	.	.	.	.	hsa04610:Complement and coagulation cascades	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	MetaCyc:HS05000-MON	P00742
TTDM4ZU	Factor XI messenger RNA (F11 mRNA)	P03951	FA11_HUMAN	mRNA target	Plasma thromboplastin antecedent (mRNA); PTA (mRNA); FXI (mRNA); Coagulation factor XI (mRNA)	F11	Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX.	EC 3.4.21.27	6R8X; 6I58; 6C0S; 6AOD; 5WB6	MIFLYQVVHFILFTSVSGECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDPTRWFTCVLKDSVTETLPRVNRTAAISGYSFKQCSHQISACNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPSLEHRNICLLKHTQTGTPTRITKLDKVVSGFSLKSCALSNLACIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESQRNLCLLKTSESGLPSTRIKKSKALSGFSLQSCRHSIPVFCHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNEGKGKCYLKLSSNGSPTKILHGRGGISGYTLRLCKMDNECTTKIKPRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSGILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAV	Clinical trial	"Clinical pipeline report, company report or official report of ISIS Pharmaceuticals (2011)."	17	mRNA	mRNA target	.	.	.	PAN domain; Trypsin	PF00024; PF00089	PF00024; PAN_1; PF00089; Trypsin	.	.	hsa04610:Complement and coagulation cascades	R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation	.	P03951
TTJCPUT	Coagulation factor XI (F11)	P03951	FA11_HUMAN	Peptidase	Plasma thromboplastin antecedent; PTA; FXI	F11	Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX.	EC 3.4.21.27	6R8X; 6I58; 6C0S; 6AOD; 5WB6	MIFLYQVVHFILFTSVSGECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDPTRWFTCVLKDSVTETLPRVNRTAAISGYSFKQCSHQISACNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPSLEHRNICLLKHTQTGTPTRITKLDKVVSGFSLKSCALSNLACIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESQRNLCLLKTSESGLPSTRIKKSKALSGFSLQSCRHSIPVFCHSSFYHDTDFLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNEGKGKCYLKLSSNGSPTKILHGRGGISGYTLRLCKMDNECTTKIKPRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSGILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAV	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	hsa04610: Complement and coagulation cascades	R-HSA-140837: Intrinsic Pathway of Fibrin Clot Formation; R-HSA-9673221: Defective F9 activation	.	P03951
TT3C8EG	Junctional adhesion molecule A (F11R)	Q9Y624	JAM1_HUMAN	Immunoglobulin	Platelet adhesion molecule 1; Platelet F11 receptor; PAM-1; Junctional adhesion molecule 1; JCAM; JAM1; JAM-A; JAM-1; CD321	F11R	"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."	.	4ODB; 3TSZ; 3EOY; 1NBQ	MGTKAQVERKLLCLFILAILLCSLALGSVTVHSSEPEVRIPENNPVKLSCAYSGFSSPRVEWKFDQGDTTRLVCYNNKITASYEDRVTFLPTGITFKSVTREDTGTYTCMVSEEGGNSYGEVKVKLIVLVPPSKPTVNIPSSATIGNRAVLTCSEQDGSPPSEYTWFKDGIVMPTNPKSTRAFSNSSYVLNPTTGELVFDPLSASDTGEYSCEARNGYGTPMTSNAVRMEAVERNVGVIVAAVLVTLILLGILVFGIWFAYSRGHFDRTKKGTSSKKVIYSQPSARSEGEFKQTSSFLV	Literature-reported	Junctional Adhesion Molecule-A in Head and Neck Squamous Cell Carcinoma. Adv Otorhinolaryngol. 2016;77:92-7.	.	Immunoglobulin	Immunoglobulin superfamily	immunoglobulin superfamily.	.	.	Immunoglobulin V-set domain	PF07686	PF07686; V-set	.	.	hsa04514: Cell adhesion molecules; hsa04530: Tight junction; hsa04670: Leukocyte transendothelial migration; hsa05120: Epithelial cell signaling in Helicobacter pylori infection	R-HSA-202733: Cell surface interactions at the vascular wall; R-HSA-216083: Integrin cell surface interactions; R-HSA-2173791: TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition); R-HSA-420029: Tight junction interactions	.	Q9Y624
TTRJSMV	Factor XII messenger RNA (FA12 mRNA)	P00748	FA12_HUMAN	mRNA target	Hageman factor (mRNA); HAF (mRNA); Coagulation factor XII (mRNA)	F12	"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."	EC 3.4.21.38	6B77; 6B74; 4XE4; 4XDE; 4BDX	MRALLLLGFLLVSLESTLSIPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCLCPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRTNPCLHGGRCLEVEGHRLCHCPVGYTGAFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQPWASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQAAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCGQRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAPEDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSPYVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGSSILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYTDVAYYLAWIREHTVS	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2361).	16	mRNA	mRNA target	.	.	.	EGF-like domain; Fibronectin type I domain; Fibronectin type II domain; Kringle domain; Trypsin	PF00008; PF00039; PF00040; PF00051; PF00089	PF00008; EGF; PF00039; fn1; PF00040; fn2; PF00051; Kringle; PF00089; Trypsin	.	.	hsa04610:Complement and coagulation cascades	R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation	.	P00748
TTMXD0O	Coagulation factor XII (F12)	P00748	FA12_HUMAN	.	Hageman factor; HAF	F12	.	EC 3.4.21.38	.	MRALLLLGFLLVSLESTLSIPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCLCPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRTNPCLHGGRCLEVEGHRLCHCPVGYTGAFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQPWASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQAAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCGQRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAPEDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSPYVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGSSILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYTDVAYYLAWIREHTVS	Clinical trial	"Clinical pipeline report, company report or official report of CSL Behring."	.	.	.	.	.	.	.	.	.	.	.	hsa04610: Complement and coagulation cascades	R-HSA-140837: Intrinsic Pathway of Fibrin Clot Formation; R-HSA-9657688: Defective factor XII causes hereditary angioedema; R-HSA-9657689: Defective SERPING1 causes hereditary angioedema	.	P00748
TTXI2RA	Coagulation factor XIIIA (F13A1)	P00488	F13A_HUMAN	Acyltransferase	Transglutaminase A chain; Protein-glutamine gamma-glutamyltransferase A chain; F13A; Coagulation factor XIII A chain	F13A1	"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."	EC 2.3.2.13	5MHO; 5MHN; 5MHM; 5MHL; 4KTY	MSETSRTAFGGRRAVPPNNSNAAEDDLPTVELQGVVPRGVNLQEFLNVTSVHLFKERWDTNKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPVPIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETDTYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCLYVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDILLEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGNVNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKHGHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITDTYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSRSNVDMDFEVENAVLGKDFKLSITFRNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLLEQASLHFFVTARINETRDVLAKQKSTVLTIPEIIIKVRGTQVVGSDMTVTVQFTNPLKETLRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYGELDVQIQRRPSM	Patented-recorded	Transglutaminase inhibitors: a patent review.Expert Opin Ther Pat. 2016;26(1):49-63.	15.5	EC:2.3	Transglutaminase superfamily	transglutaminase superfamily. Transglutaminase family.	2.3.2.13 	Acyltransferases	"Transglutaminase family, C-terminal ig like domain; Transglutaminase-like superfamily; Transglutaminase family"	PF00927; PF01841; PF00868	PF00927; Transglut_C; PF01841; Transglut_core; PF00868; Transglut_N	.	.	hsa04610:Complement and coagulation cascades	R-HSA-114608: Platelet degranulation; R-HSA-140875: Common Pathway of Fibrin Clot Formation; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling	.	P00488
TTAXGIP	Coagulation factor XIII (F13B)	P05160	F13B_HUMAN	Acyltransferase	F13B	F13B	"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."	.	.	MRLKNLTFIIILIISGELYAEEKPCGFPHVENGRIAQYYYTFKSFYFPMSIDKKLSFFCLAGYTTESGRQEEQTTCTTEGWSPEPRCFKKCTKPDLSNGYISDVKLLYKIQENMRYGCASGYKTTGGKDEEVVQCLSDGWSSQPTCRKEHETCLAPELYNGNYSTTQKTFKVKDKVQYECATGYYTAGGKKTEEVECLTYGWSLTPKCTKLKCSSLRLIENGYFHPVKQTYEEGDVVQFFCHENYYLSGSDLIQCYNFGWYPESPVCEGRRNRCPPPPLPINSKIQTHSTTYRHGEIVHIECELNFEIHGSAEIRCEDGKWTEPPKCIEGQEKVACEEPPFIENGAANLHSKIYYNGDKVTYACKSGYLLHGSNEITCNRGKWTLPPECVENNENCKHPPVVMNGAVADGILASYATGSSVEYRCNEYYLLRGSKISRCEQGKWSSPPVCLEPCTVNVDYMNRNNIEMKWKYEGKVLHGDLIDFVCKQGYDLSPLTPLSELSVQCNRGEVKYPLCTRKESKGMCTSPPLIKHGVIISSTVDTYENGSSVEYRCFDHHFLEGSREAYCLDGMWTTPPLCLEPCTLSFTEMEKNNLLLKWDFDNRPHILHGEYIEFICRGDTYPAELYITGSILRMQCDRGQLKYPRCIPRQSTLSYQEPLRT	Clinical trial	Catridecacog: a breakthrough in the treatment of congenital factor XIII A-subunit deficiency. J Blood Med. 2014 Jul 9;5:107-13.	25	.	.	.	.	.	.	.	.	.	.	hsa04610:Complement and coagulation cascades	R-HSA-140875:Common Pathway of Fibrin Clot Formation	.	P05160
TT6L509	Coagulation factor IIa (F2)	P00734	THRB_HUMAN	Peptidase	Prothrombin; Coagulation factor II	F2	"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."	EC 3.4.21.5	8KME; 7KME; 6EO9; 6EO8; 6EO7	MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE	Successful	Emerging drugs in peripheral arterial disease. Expert Opin Emerg Drugs. 2006 Mar;11(1):75-90.	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04610:Complement and coagulation cascades; hsa04810:Regulation of actin cytoskeleton	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)	.	P00734
TTL935N	Proteinase activated receptor 1 (F2R)	P25116	PAR1_HUMAN	GPCR rhodopsin	Thrombin receptor; Proteinase-activated receptor 1; Protease-activated receptor-1; Protease activated receptor 1; PAR1; PAR-1; Coagulation factor II receptor; CF2R	F2R	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.	.	3VW7; 3LU9; 3HKJ; 3HKI; 3BEF	MGPRRLLLVAACFSLCGPLLSARTRARRPESKATNATLDPRSFLLRNPNDKYEPFWEDEEKNESGLTEYRLVSINKSSPLQKQLPAFISEDASGYLTSSWLTLFVPSVYTGVFVVSLPLNIMAIVVFILKMKVKKPAVVYMLHLATADVLFVSVLPFKISYYFSGSDWQFGSELCRFVTAAFYCNMYASILLMTVISIDRFLAVVYPMQSLSWRTLGRASFTCLAIWALAIAGVVPLLLKEQTIQVPGLNITTCHDVLNETLLEGYYAYYFSAFSAVFFFVPLIISTVCYVSIIRCLSSSAVANRSKKSRALFLSAAVFCIFIICFGPTNVLLIAHYSFLSHTSTTEAAYFAYLLCVCVSSISCCIDPLIYYYASSECQRYVYSILCCKESSDPSSYNSSGQLMASKMDTCSSNLNNSIYKKLLT	Successful	In Process Citation. Pharm Unserer Zeit. 2009;38(4):320-8.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	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	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)	.	P25116
TTQR74A	Proteinase activated receptor 2 (PAR2)	P55085	PAR2_HUMAN	GPCR rhodopsin	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	F2RL1	"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."	.	5NJ6; 5NDZ; 5NDD	MRSPSAAWLLGAAILLAASLSCSGTIQGTNRSSKGRSLIGKVDGTSHVTGKGVTVETVFSVDEFSASVLTGKLTTVFLPIVYTIVFVVGLPSNGMALWVFLFRTKKKHPAVIYMANLALADLLSVIWFPLKIAYHIHGNNWIYGEALCNVLIGFFYGNMYCSILFMTCLSVQRYWVIVNPMGHSRKKANIAIGISLAIWLLILLVTIPLYVVKQTIFIPALNITTCHDVLPEQLLVGDMFNYFLSLAIGVFLFPAFLTASAYVLMIRMLRSSAMDENSEKKRKRAIKLIVTVLAMYLICFTPSNLLLVVHYFLIKSQGQSHVYALYIVALCLSTLNSCIDPFVYYFVSHDFRDHAKNALLCRSVRTVKQMQVSLTSKKHSRKSSSYSSSSTTVKTSY	Patented-recorded	Protease activated receptor 2 (PAR2) modulators: a patent review (2010-2015).Expert Opin Ther Pat. 2016;26(4):471-83.	15.5	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.13.12	The G-protein-coupled receptor (GPCR) Family	hsa04080:Neuroactive ligand-receptor interaction; hsa04750:Inflammatory mediator regulation of TRP channels; hsa05143:African trypanosomiasis	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events	.	P55085
TTD3TZ2	HUMAN proteinase activated receptor 2 (PAR2)	P55085	PAR2_HUMAN	GPCR rhodopsin	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	F2RL1	"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."	.	5NJ6; 5NDZ; 5NDD	MRSPSAAWLLGAAILLAASLSCSGTIQGTNRSSKGRSLIGKVDGTSHVTGKGVTVETVFSVDEFSASVLTGKLTTVFLPIVYTIVFVVGLPSNGMALWVFLFRTKKKHPAVIYMANLALADLLSVIWFPLKIAYHIHGNNWIYGEALCNVLIGFFYGNMYCSILFMTCLSVQRYWVIVNPMGHSRKKANIAIGISLAIWLLILLVTIPLYVVKQTIFIPALNITTCHDVLPEQLLVGDMFNYFLSLAIGVFLFPAFLTASAYVLMIRMLRSSAMDENSEKKRKRAIKLIVTVLAMYLICFTPSNLLLVVHYFLIKSQGQSHVYALYIVALCLSTLNSCIDPFVYYFVSHDFRDHAKNALLCRSVRTVKQMQVSLTSKKHSRKSSSYSSSSTTVKTSY	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04750: Inflammatory mediator regulation of TRP channels; hsa05143: African trypanosomiasis	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-416476: G alpha (q) signalling events	.	P55085
TTVSEBF	Proteinase activated receptor 3 (F2RL2)	O00254	PAR3_HUMAN	GPCR rhodopsin	Thrombin receptor-like 2; Protease activated receptor 3; PAR-3; F2RL2; Coagulation factor II receptor-like 2	F2RL2	Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis.	.	.	MKALIFAAAGLLLLLPTFCQSGMENDTNNLAKPTLPIKTFRGAPPNSFEEFPFSALEGWTGATITVKIKCPEESASHLHVKNATMGYLTSSLSTKLIPAIYLLVFVVGVPANAVTLWMLFFRTRSICTTVFYTNLAIADFLFCVTLPFKIAYHLNGNNWVFGEVLCRATTVIFYGNMYCSILLLACISINRYLAIVHPFTYRGLPKHTYALVTCGLVWATVFLYMLPFFILKQEYYLVQPDITTCHDVHNTCESSSPFQLYYFISLAFFGFLIPFVLIIYCYAAIIRTLNAYDHRWLWYVKASLLILVIFTICFAPSNIILIIHHANYYYNNTDGLYFIYLIALCLGSLNSCLDPFLYFLMSKTRNHSTAYLTK	Literature-reported	Protease-activated receptors: the role of cell-surface proteolysis in signalling. Essays Biochem. 2002;38:169-83.	.	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04610: Complement and coagulation cascades	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)	.	O00254
TTD0652	Proteinase activated receptor 4 (F2RL3)	Q96RI0	PAR4_HUMAN	GPCR rhodopsin	Thrombin receptor-like 3; Protease activated receptor 4; F2RL3; Coagulation factor II receptor-like3	F2RL3	Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation.	.	3QDZ; 2ZPK	MWGRLLLWPLVLGFSLSGGTQTPSVYDESGSTGGGDDSTPSILPAPRGYPGQVCANDSDTLELPDSSRALLLGWVPTRLVPALYGLVLVVGLPANGLALWVLATQAPRLPSTMLLMNLAAADLLLALALPPRIAYHLRGQRWPFGEAACRLATAALYGHMYGSVLLLAAVSLDRYLALVHPLRARALRGRRLALGLCMAAWLMAAALALPLTLQRQTFRLARSDRVLCHDALPLDAQASHWQPAFTCLALLGCFLPLLAMLLCYGATLHTLAASGRRYGHALRLTAVVLASAVAFFVPSNLLLLLHYSDPSPSAWGNLYGAYVPSLALSTLNSCVDPFIYYYVSAEFRDKVRAGLFQRSPGDTVASKASAEGGSRGMGTHSSLLQ	Literature-reported	Novel thiazole-based heterocycles as selective inhibitors of fibrinogen-mediated platelet aggregation. J Med Chem. 1995 Jan 6;38(1):34-41.	2	.	.	.	.	.	.	.	.	.	.	hsa04015:Rap1 signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04611:Platelet activation; hsa05200:Pathways in cancer	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)	.	Q96RI0
TT38MDJ	Tissue factor (F3)	P13726	TF_HUMAN	.	Thromboplastin; TF; F3; Coagulation factor III; CD142 antigen	F3	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.	.	5W06; 4ZMA; 4Z6A; 4YLQ; 4M7L	METPAWPRVPRPETAVARTLLLGWVFAQVAGASGTTNTVAAYNLTWKSTNFKTILEWEPKPVNQVYTVQISTKSGDWKSKCFYTTDTECDLTDEIVKDVKQTYLARVFSYPAGNVESTGSAGEPLYENSPEFTPYLETNLGQPTIQSFEQVGTKVNVTVEDERTLVRRNNTFLSLRDVFGKDLIYTLYYWKSSSSGKKTAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSPVECMGQEKGEFREIFYIIGAVVFVVIILVIILAISLHKCRKAGVGQSWKENSPLNVS	Clinical trial	TETIS study: evaluation of new topical hemostatic agent TT-173 in tooth extraction. Clin Oral Investig. 2016 Jun;20(5):1055-63.	21	.	.	.	.	.	.	.	.	.	.	hsa04610:Complement and coagulation cascades	R-HSA-140834:Extrinsic Pathway of Fibrin Clot Formation	.	P13726
TT1O264	Coagulation factor Va (F5)	P12259	FA5_HUMAN	.	Factor Va; F5	F5	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.	.	3S9C; 3P70; 3P6Z; 1Y61; 1FV4	MFPGCPRLWVLVVLGTSWVGWGSQGTEAAQLRQFYVAAQGISWSYRPEPTNSSLNLSVTSFKKIVYREYEPYFKKEKPQSTISGLLGPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYYSHENLIEDFNSGLIGPLLICKKGTLTEGGTQKTFDKQIVLLFAVFDESKSWSQSSSLMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNGQVLEQNHHKVSAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQAYIDIKNCPKKTRNLKKITREQRRHMKRWEYFIAAEEVIWDYAPVIPANMDKKYRSQHLDNFSNQIGKHYKKVMYTQYEDESFTKHTVNPNMKEDGILGPIIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDEVNSSFTSGRNNTMIRAVQPGETYTYKWNILEFDEPTENDAQCLTRPYYSDVDIMRDIASGLIGLLLICKSRSLDRRGIQRAADIEQQAVFAVFDENKSWYLEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNEILTIHFTGHSFIYGKRHEDTLTLFPMRGESVTVTMDNVGTWMLTSMNSSPRSKKLRLKFRDVKCIPDDDEDSYEIFEPPESTVMATRKMHDRLEPEDEESDADYDYQNRLAAALGIRSFRNSSLNQEEEEFNLTALALENGTEFVSSNTDIIVGSNYSSPSNISKFTVNNLAEPQKAPSHQQATTAGSPLRHLIGKNSVLNSSTAEHSSPYSEDPIEDPLQPDVTGIRLLSLGAGEFKSQEHAKHKGPKVERDQAAKHRFSWMKLLAHKVGRHLSQDTGSPSGMRPWEDLPSQDTGSPSRMRPWKDPPSDLLLLKQSNSSKILVGRWHLASEKGSYEIIQDTDEDTAVNNWLISPQNASRAWGESTPLANKPGKQSGHPKFPRVRHKSLQVRQDGGKSRLKKSQFLIKTRKKKKEKHTHHAPLSPRTFHPLRSEAYNTFSERRLKHSLVLHKSNETSLPTDLNQTLPSMDFGWIASLPDHNQNSSNDTGQASCPPGLYQTVPPEEHYQTFPIQDPDQMHSTSDPSHRSSSPELSEMLEYDRSHKSFPTDISQMSPSSEHEVWQTVISPDLSQVTLSPELSQTNLSPDLSHTTLSPELIQRNLSPALGQMPISPDLSHTTLSPDLSHTTLSLDLSQTNLSPELSQTNLSPALGQMPLSPDLSHTTLSLDFSQTNLSPELSHMTLSPELSQTNLSPALGQMPISPDLSHTTLSLDFSQTNLSPELSQTNLSPALGQMPLSPDPSHTTLSLDLSQTNLSPELSQTNLSPDLSEMPLFADLSQIPLTPDLDQMTLSPDLGETDLSPNFGQMSLSPDLSQVTLSPDISDTTLLPDLSQISPPPDLDQIFYPSESSQSLLLQEFNESFPYPDLGQMPSPSSPTLNDTFLSKEFNPLVIVGLSKDGTDYIEIIPKEEVQSSEDDYAEIDYVPYDDPYKTDVRTNINSSRDPDNIAAWYLRSNNGNRRNYYIAAEEISWDYSEFVQRETDIEDSDDIPEDTTYKKVVFRKYLDSTFTKRDPRGEYEEHLGILGPIIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTYVWHATERSGPESPGSACRAWAYYSAVNPEKDIHSGLIGPLLICQKGILHKDSNMPMDMREFVLLFMTFDEKKSWYYEKKSRSSWRLTSSEMKKSHEFHAINGMIYSLPGLKMYEQEWVRLHLLNIGGSQDIHVVHFHGQTLLENGNKQHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLIMDRDCRMPMGLSTGIISDSQIKASEFLGYWEPRLARLNNGGSYNAWSVEKLAAEFASKPWIQVDMQKEVIITGIQTQGAKHYLKSCYTTEFYVAYSSNQINWQIFKGNSTRNVMYFNGNSDASTIKENQFDPPIVARYIRISPTRAYNRPTLRLELQGCEVNGCSTPLGMENGKIENKQITASSFKKSWWGDYWEPFRARLNAQGRVNAWQAKANNNKQWLEIDLLKIKKITAIITQGCKSLSSEMYVKSYTIHYSEQGVEWKPYRLKSSMVDKIFEGNTNTKGHVKNFFNPPIISRFIRVIPKTWNQSIALRLELFGCDIY	Successful	Protein C in critical illness. Am J Health Syst Pharm. 2009 Jun 15;66(12):1089-96.	34	.	.	.	.	.	.	.	.	.	.	hsa04610:Complement and coagulation cascades	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	.	P12259
TTF0EGX	Coagulation factor VII (F7)	P08709	FA7_HUMAN	Peptidase	Serum prothrombin conversion accelerator; SPCA; Proconvertin; Eptacog alfa	F7	"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."	EC 3.4.21.21	5U6J; 5TQG; 5TQF; 5TQE; 5PB6	MVSQALRLLCLLLGLQGCLAAGGVAKASGGETRDMPWKPGPHRVFVTQEEAHGVLHRRRRANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP	Successful	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2363).	34	.	.	.	.	.	.	.	.	.	.	hsa04610:Complement and coagulation cascades	"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"	.	P08709
TT1290U	Coagulation factor VIII (F8)	P00451	FA8_HUMAN	.	Procoagulant component; F8C; Antihemophilic factor; AHF	F8	"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."	.	5K8D; 4XZU; 4PT6; 4KI5; 4BDV	MQIELSTCFFLCLLRFCFSATRRYYLGAVELSWDYMQSDLGELPVDARFPPRVPKSFPFNTSVVYKKTLFVEFTDHLFNIAKPRPPWMGLLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQREKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHVDLVKDLNSGLIGALLVCREGSLAKEKTQTLHKFILLFAVFDEGKSWHSETKNSLMQDRDAASARAWPKMHTVNGYVNRSLPGLIGCHRKSVYWHVIGMGTTPEVHSIFLEGHTFLVRNHRQASLEISPITFLTAQTLLMDLGQFLLFCHISSHQHDGMEAYVKVDSCPEEPQLRMKNNEEAEDYDDDLTDSEMDVVRFDDDNSPSFIQIRSVAKKHPKTWVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGITDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFVNMERDLASGLIGPLLICYKESVDQRGNQIMSDKRNVILFSVFDENRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILSIGAQTDFLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSCDKNTGDYYEDSYEDISAYLLSKNNAIEPRSFSQNSRHPSTRQKQFNATTIPENDIEKTDPWFAHRTPMPKIQNVSSSDLLMLLRQSPTPHGLSLSDLQEAKYETFSDDPSPGAIDSNNSLSEMTHFRPQLHHSGDMVFTPESGLQLRLNEKLGTTAATELKKLDFKVSSTSNNLISTIPSDNLAAGTDNTSSLGPPSMPVHYDSQLDTTLFGKKSSPLTESGGPLSLSEENNDSKLLESGLMNSQESSWGKNVSSTESGRLFKGKRAHGPALLTKDNALFKVSISLLKTNKTSNNSATNRKTHIDGPSLLIENSPSVWQNILESDTEFKKVTPLIHDRMLMDKNATALRLNHMSNKTTSSKNMEMVQQKKEGPIPPDAQNPDMSFFKMLFLPESARWIQRTHGKNSLNSGQGPSPKQLVSLGPEKSVEGQNFLSEKNKVVVGKGEFTKDVGLKEMVFPSSRNLFLTNLDNLHENNTHNQEKKIQEEIEKKETLIQENVVLPQIHTVTGTKNFMKNLFLLSTRQNVEGSYDGAYAPVLQDFRSLNDSTNRTKKHTAHFSKKGEEENLEGLGNQTKQIVEKYACTTRISPNTSQQNFVTQRSKRALKQFRLPLEETELEKRIIVDDTSTQWSKNMKHLTPSTLTQIDYNEKEKGAITQSPLSDCLTRSHSIPQANRSPLPIAKVSSFPSIRPIYLTRVLFQDNSSHLPAASYRKKDSGVQESSHFLQGAKKNNLSLAILTLEMTGDQREVGSLGTSATNSVTYKKVENTVLPKPDLPKTSGKVELLPKVHIYQKDLFPTETSNGSPGHLDLVEGSLLQGTEGAIKWNEANRPGKVPFLRVATESSAKTPSKLLDPLAWDNHYGTQIPKEEWKSQEKSPEKTAFKKKDTILSLNACESNHAIAAINEGQNKPEIEVTWAKQGRTERLCSQNPPVLKRHQREITRTTLQSDQEEIDYDDTISVEMKKEDFDIYDEDENQSPRSFQKKTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHTNTLNPAHGRQVTVQEFALFFTIFDETKSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITASGQYGQWAPKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQFIIMYSLDGKKWQTYRGNSTGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSKARLHLQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLY	Successful	Protein C in critical illness. Am J Health Syst Pharm. 2009 Jun 15;66(12):1089-96.	34	.	Multicopper oxidase	multicopper oxidase family.	.	.	Multicopper oxidase; Multicopper oxidase; Multicopper oxidase; F5/8 type C domain	PF00394; PF07731; PF07732; PF00754	PF00394; Cu-oxidase; PF07731; Cu-oxidase_2; PF07732; Cu-oxidase_3; PF00754; F5_F8_type_C	.	.	hsa04610:Complement and coagulation cascades	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	.	P00451
TTFEZ5Q	Coagulation factor IX (F9)	P00740	FA9_HUMAN	Peptidase	Plasma thromboplastin component; PTC protein; Factor IX; Christmas factor	F9	"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."	EC 3.4.21.22	6MV4; 5VYG; 5TNT; 5TNO; 5JBC	MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT	Successful	BAX326 (RIXUBIS): a novel recombinant factor IX for the control and prevention of bleeding episodes in adults and children with hemophilia B. Ther Adv Hematol. 2014 Oct;5(5):168-80.	34	EC:3.4	Peptidase	peptidase S1 family.	3.4.21.22 	Acting on peptide bonds (peptidases)	EGF-like domain; Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain; Trypsin	PF00008; PF00594; PF00089	PF00008; EGF; PF00594; Gla; PF00089; Trypsin	.	.	hsa04610:Complement and coagulation cascades	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	.	P00740
TTGX13H	Fatty-acid amide hydrolase 1 (FAAH1)	O08914	FAAH1_HUMAN	Carbon-nitrogen hydrolase	Oleamide hydrolase 1  of mouse; Oleamide hydrolase 1; FAAH; Anandamide amidohydrolase 1  of mouse; Anandamide amidohydrolase 1	FAAH1	"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."	EC 3.5.1.99	.	MVQYELWAALPGASGVALACCFVAAAVALRWSGRRTARGAVVRARQRQRAGLENMDRAAQRFRLQNPDLDSEALLALPLPQLVQKLHSRELAPEAVLFTYVGKAWEVNKGTNCVTSYLADCETQLSQAPRQGLLYGVPVSLKECFTYKGQDSTLGLSLNEGVPAECDSVVVHVLKLQGAVPFVHTNVPQSMFSYDCSNPLFGQTVNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSSFCGICGLKPTGNRLSKSGLKGCVYGQEAVRLSVGPMARDVESLALCLRALLCEDMFRLDPTVPPLPFREEVYTSSQPLRVGYYETDNYTMPSPAMRRAVLETKQSLEAAGHTLVPFLPSNIPHALETLSTGGLFSDGGHTFLQNFKGDFVDPCLGDLVSILKLPQWLKGLLAFLVKPLLPRLSAFLSNMKSRSAGKLWELQHEIEVYRKTVIAQWRALDLDVVLTPMLAPALDLNAPGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDEAQMEHYRGYFGDIWDKMLQKGMKKSVGLPVAVQCVALPWQEELCLRFMREVERLMTPEKQSS	Patented-recorded	Fatty acid amide hydrolase inhibitors: a patent review (2009-2014).Expert Opin Ther Pat. 2015;25(11):1247-66.	15.5	EC:3.5	Amidase family	amidase family.	3.5.1.99	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Amidase	PF01425	PF01425; Amidase	.	.	hsa04723:Retrograde endocannabinoid signaling	R-MMU-2142753: Arachidonic acid metabolism	.	O00519
TTWTES7	Fatty-acid amide hydrolase 2 (FAAH2)	Q6GMR7	FAAH2_HUMAN	Carbon-nitrogen hydrolase	Oleamide hydrolase 2; Anandamide amidohydrolase 2; Amidase domain-containing protein; AMDD	FAAH2	"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."	EC 3.5.1.99	.	MAPSFTARIQLFLLRALGFLIGLVGRAALVLGGPKFASKTPRPVTEPLLLLSGMQLAKLIRQRKVKCIDVVQAYINRIKDVNPMINGIVKYRFEEAMKEAHAVDQKLAEKQEDEATLENKWPFLGVPLTVKEAFQLQGMPNSSGLMNRRDAIAKTDATVVALLKGAGAIPLGITNCSELCMWYESSNKIYGRSNNPYDLQHIVGGSSGGEGCTLAAACSVIGVGSDIGGSIRMPAFFNGIFGHKPSPGVVPNKGQFPLAVGAQELFLCTGPMCRYAEDLAPMLKVMAGPGIKRLKLDTKVHLKDLKFYWMEHDGGSFLMSKVDQDLIMTQKKVVVHLETILGASVQHVKLKKMKYSFQLWIAMMSAKGHDGKEPVKFVDLLGDHGKHVSPLWELIKWCLGLSVYTIPSIGLALLEEKLRYSNEKYQKFKAVEESLRKELVDMLGDDGVFLYPSHPTVAPKHHVPLTRPFNFAYTGVFSALGLPVTQCPLGLNAKGLPLGIQVVAGPFNDHLTLAVAQYLEKTFGGWVCPGKF	Literature-reported	Expression and distribution of key proteins of the endocannabinoid system in the human seminal vesicles. Andrologia. 2018 Mar;50(2).	.	EC:3.5	.	amidase family.	3.5.1.99	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Amidase	PF01425	PF01425; Amidase	.	.	.	R-HSA-2142753: Arachidonic acid metabolism	MetaCyc:HS09254-MON	Q6GMR7
TTIV96N	Fatty acid-binding protein 1 (FABP1)	P07148	FABPL_HUMAN	.	L-FABP; FABP1; 14-kDa fatty-acid binding protein; 14 kDa selenium-binding protein	FABP1	"Binds free fatty acids andtheir coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport."	.	6DRG; 6DO7; 6DO6; 3VG7; 3VG6	MSFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKTVVQLEGDNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI	Successful	Characterization of the drug binding specificity of rat liver fatty acid binding protein. J Med Chem. 2008 Jul 10;51(13):3755-64.	34	.	.	.	.	.	.	.	.	.	.	hsa03320:PPAR signaling pathway; hsa04975:Fat digestion and absorption	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)	.	P07148
TTS4YLO	Intestinal lipid-binding protein	.	FABPI_HUMAN	Single Protein	"Fatty acid-binding protein 2; I-FABP; Intestinal-type fatty acid-binding protein; Fatty acid-binding protein, intestinal; FABP2"	FABP2	"FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor."	.	.	MAFDSTWKVDRSENYDKFMEKMGVNIVKRKLAAHDNLKLTITQEGNKFTVKESSAFRNIEVVFELGVTFNYNLADGTELRGTWSLEGNKLIGKFKRTDNGNELNTVREIIGDELVQTYVYEGVEAKRIFKKD	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P12104
TT3TGLR	Heart lipid-binding protein	.	FABPH_HUMAN	Single Protein	"Fatty acid-binding protein 3; H-FABP; Heart-type fatty acid-binding protein; M-FABP; MDGI; Mammary-derived growth inhibitor; Muscle fatty acid-binding protein; Fatty acid-binding protein, heart; FABP3"	FABP3	FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.	.	.	MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEKEA	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P05413
TTHWMFZ	Fatty acid-binding protein 4 (FABP4)	P15090	FABP4_HUMAN	Fatty acid binding protein	"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"	FABP4	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.	.	6AYL; 5Y13; 5Y12; 5Y0X; 5Y0G	MCDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKSTITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYERA	Patented-recorded	Fatty acid binding protein (FABP) inhibitors: a patent review (2012-2015).Expert Opin Ther Pat. 2016 Jul;26(7):767-76.	15.5	TC=8.A.33	Calycin family	calycin superfamily. Fatty-acid binding protein (FABP) family.	.	.	Lipocalin / cytosolic fatty-acid binding protein family	PF00061	PF00061; Lipocalin	.	.	hsa03320:PPAR signaling pathway	R-HSA-163560:Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation	.	P15090
TTNT2S6	Fatty acid-binding protein 5 (FABP5)	Q01469	FABP5_HUMAN	Fatty acid binding protein	"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"	FABP5	"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."	.	5UR9; 5HZ5; 4LKT; 4LKP; 4AZR	MATVQQLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKNLTIKTESTLKTTQFSCTLGEKFEETTADGRKTQTVCNFTDGALVQHQEWDGKESTITRKLKDGKLVVECVMNNVTCTRIYEKVE	Patented-recorded	Fatty acid binding protein (FABP) inhibitors: a patent review (2012-2015).Expert Opin Ther Pat. 2016 Jul;26(7):767-76.	15.5	TC=8.A.33	Fatty acid bindingprotein	calycin superfamily. Fatty-acid binding protein (FABP) family.	.	.	Lipocalin / cytosolic fatty-acid binding protein family	PF00061	PF00061; Lipocalin	8.A.33.1.1	The Fatty Acid Binding Protein (FABP) Family	hsa03320:PPAR signaling pathway	R-HSA-163560:Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis	.	Q01469
TTT2VDU	Fatty acid desaturase 2 (FADS2)	O95864	FADS2_HUMAN	Paired donor oxygen oxidoreductase	FADS2; Delta-6 desaturase; Delta(6) fatty acid desaturase; Delta(6) desaturase; D6D	FADS2	"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."	EC 1.14.19.3	.	MGKGGNQGEGAAEREVSVPTFSWEEIQKHNLRTDRWLVIDRKVYNITKWSIQHPGGQRVIGHYAGEDATDAFRAFHPDLEFVGKFLKPLLIGELAPEEPSQDHGKNSKITEDFRALRKTAEDMNLFKTNHVFFLLLLAHIIALESIAWFTVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVLGEWQPIEYGKKKLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIVHKNWVDLAWAVSYYIRFFITYIPFYGILGALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAYRDWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKKSGKLWLDAYLHK	Literature-reported	"Genetic polymorphisms of FADS1, FADS2, and FADS3 and fatty acid profiles in subjects received methadone maintenance therapy. Prostaglandins Leukot Essent Fatty Acids. 2018 Sep;136:117-121."	.	.	.	.	.	.	.	.	.	.	.	hsa00592: alpha-Linolenic acid metabolism; hsa01040: Biosynthesis of unsaturated fatty acids; hsa01100: Metabolic pathways; hsa01212: Fatty acid metabolism; hsa03320: PPAR signaling pathway	R-HSA-2046105: Linoleic acid (LA) metabolism; R-HSA-2046106: alpha-linolenic acid (ALA) metabolism	MetaCyc:HS05918-MON	O95864
TTSKL3G	FAS-associated factor 1 (FAF1)	Q9UNN5	FAF1_HUMAN	.	hFAF1; UBX domain-containing protein 12; UBX domain-containing protein 3A	FAF1	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).	.	.	MASNMDREMILADFQACTGIENIDEAITLLEQNNWDLVAAINGVIPQENGILQSEYGGETIPGPAFNPASHPASAPTSSSSSAFRPVMPSRQIVERQPRMLDFRVEYRDRNVDVVLEDTCTVGEIKQILENELQIPVSKMLLKGWKTGDVEDSTVLKSLHLPKNNSLYVLTPDLPPPSSSSHAGALQESLNQNFMLIITHREVQREYNLNFSGSSTIQEVKRNVYDLTSIPVRHQLWEGWPTSATDDSMCLAESGLSYPCHRLTVGRRSSPAQTREQSEEQITDVHMVSDSDGDDFEDATEFGVDDGEVFGMASSALRKSPMMPENAENEGDALLQFTAEFSSRYGDCHPVFFIGSLEAAFQEAFYVKARDRKLLAIYLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKDSNRARFLTMCNRHFGSVVAQTIRTQKTDQFPLFLIIMGKRSSNEVLNVIQGNTTVDELMMRLMAAMEIFTAQQQEDIKDEDEREARENVKREQDEAYRLSLEADRAKREAHEREMAEQFRLEQIRKEQEEEREAIRLSLEQALPPEPKEENAEPVSKLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDEYKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFLEAKE	Clinical trial	"A first-in-human study to investigate the safety, tolerability, pharmacokinetics, and pharmacodynamics of KM-819 (FAS-associated factor 1 inhibitor), a drug for Parkinson's disease, in healthy volunteers. Drug Des Devel Ther. 2019 Mar 29;13:1011-1022."	.	.	.	.	.	.	.	.	.	.	.	hsa04217: Necroptosis	.	.	Q9UNN5
TT1Q347	Protein FAM83B (FA83B)	Q5T0W9	FA83B_HUMAN	.	C6orf143	FAM83B	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.	.	5QHS; 5QHR; 5QHQ; 5QHP; 5QHO	METSSMLSSLNDECKSDNYIEPHYKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQKVAQSTAHGTDDSCDDTLSSGTYWPVESDVEAPNLDLGWPYVMPGLLGGTHIDLLFHPPRAHLLTIKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEASTRGVSVYILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSFEKAHLSMVQIITGQLVESFDEEFRTLYARSCVPSSFAQEESARVKHGKALWENGTYQHSVSSLASVSSQRNLFGRQDKIHKLDSSYFKNRGIYTLNEHDKYNIRSHGYKPHFVPNFNGPNAIRQFQPNQINENWKRHSYAGEQPETVPYLLLNRALNRTNNPPGNWKKPSDSLSVASSSREGYVSHHNTPAQSFANRLAQRKTTNLADRNSNVRRSFNGTDNHIRFLQQRMPTLEHTTKSFLRNWRIESYLNDHSEATPDSNGSALGDRFEGYDNPENLKANALYTHSRLRSSLVFKPTLPEQKEVNSCTTGSSNSTIIGSQGSETPKEVPDTPTNVQHLTDKPLPESIPKLPLQSEAPKMHTLQVPENHSVALNQTTNGHTESNNYIYKTLGVNKQTENLKNQQTENLLKRRSFPLFDNSKANLDPGNSKHYVYSTLTRNRVRQPEKPKEDLLKSSKSMHNVTHNLEEDEEEVTKRNSPSGTTTKSVSIAALLDVNKEESNKELASKKEVKGSPSFLKKGSQKLRSLLSLTPDKKENLSKNKAPAFYRLCSSSDTLVSEGEENQKPKKSDTKVDSSPRRKHSSSSNSQGSIHKSKEDVTVSPSQEINAPPDENKRTPSPGPVESKFLERAGDASAPRFNTEQIQYRDSREINAVVTPERRPTSSPRPTSSELLRSHSTDRRVYSRFEPFCKIESSIQPTSNMPNTSINRPEIKSATMGNSYGRSSPLLNYNTGVYRSYQPNENKFRGFMQKFGNFIHKNK	Literature-reported	FAM83A and FAM83B as Prognostic Biomarkers and Potential New Therapeutic Targets in NSCLC. Cancers (Basel). 2019 May 11;11(5). pii: E652.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-9696264: RND3 GTPase cycle; R-HSA-9696270: RND2 GTPase cycle; R-HSA-9696273: RND1 GTPase cycle	.	Q5T0W9
TTFIW7J	Spindle protein CHICA (FAM83D)	Q9H4H8	FA83D_HUMAN	.	Protein FAM83D; FAM83D	FAM83D	"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."	.	5E0M; 5E0L	MALLSEGLDEVPAACLSPCGPPNPTELFSESRRLALEELVAGGPEAFAAFLRRERLARFLNPDEVHAILRAAERPGEEGAAAAAAAEDSFGSSHDCSSGTYFPEQSDLEPPLLELGWPAFYQGAYRGATRVETHFQPRGAGEGGPYGCKDALRQQLRSAREVIAVVMDVFTDIDIFRDLQEICRKQGVAVYILLDQALLSQFLDMCMDLKVHPEQEKLMTVRTITGNIYYARSGTKIIGKVHEKFTLIDGIRVATGSYSFTWTDGKLNSSNLVILSGQVVEHFDLEFRILYAQSKPISPKLLSHFQSSNKFDHLTNRKPQSKELTLGNLLRMRLARLSSTPRKADLDPEMPAEGKAERKPHDCESSTVSEEDYFSSHRDELQSRKAIDAATQTEPGEEMPGLSVSEVGTQTSITTACAGTQTAVITRIASSQTTIWSRSTTTQTDMDENILFPRGTQSTEGSPVSKMSVSRSSSLKSSSSVSSQGSVASSTGSPASIRTTDFHNPGYPKYLGTPHLELYLSDSLRNLNKERQFHFAGIRSRLNHMLAMLSRRTLFTENHLGLHSGNFSRVNLLAVRDVALYPSYQ	Literature-reported	"FAM83D knockdown regulates proliferation, migration and invasion of colorectal cancer through inhibiting FBXW7/Notch-1 signalling pathway. Biomed Pharmacother. 2017 Jun;90:548-554."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9H4H8
TTV5HJS	Fanconi anemia group A protein (FANCA)	O15360	FANCA_HUMAN	.	Protein FACA	FANCA	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.	.	.	MSDSWVPNSASGQDPGGRRRAWAELLAGRVKREKYNPERAQKLKESAVRLLRSHQDLNALLLEVEGPLCKKLSLSKVIDCDSSEAYANHSSSFIGSALQDQASRLGVPVGILSAGMVASSVGQICTAPAETSHPVLLTVEQRKKLSSLLEFAQYLLAHSMFSRLSFCQELWKIQSSLLLEAVWHLHVQGIVSLQELLESHPDMHAVGSWLFRNLCCLCEQMEASCQHADVARAMLSDFVQMFVLRGFQKNSDLRRTVEPEKMPQVTVDVLQRMLIFALDALAAGVQEESSTHKIVRCWFGVFSGHTLGSVISTDPLKRFFSHTLTQILTHSPVLKASDAVQMQREWSFARTHPLLTSLYRRLFVMLSAEELVGHLQEVLETQEVHWQRVLSFVSALVVCFPEAQQLLEDWVARLMAQAFESCQLDSMVTAFLVVRQAALEGPSAFLSYADWFKASFGSTRGYHGCSKKALVFLFTFLSELVPFESPRYLQVHILHPPLVPGKYRSLLTDYISLAKTRLADLKVSIENMGLYEDLSSAGDITEPHSQALQDVEKAIMVFEHTGNIPVTVMEASIFRRPYYVSHFLPALLTPRVLPKVPDSRVAFIESLKRADKIPPSLYSTYCQACSAAEEKPEDAALGVRAEPNSAEEPLGQLTAALGELRASMTDPSQRDVISAQVAVISERLRAVLGHNEDDSSVEISKIQLSINTPRLEPREHMAVDLLLTSFCQNLMAASSVAPPERQGPWAALFVRTMCGRVLPAVLTRLCQLLRHQGPSLSAPHVLGLAALAVHLGESRSALPEVDVGPPAPGAGLPVPALFDSLLTCRTRDSLFFCLKFCTAAISYSLCKFSSQSRDTLCSCLSPGLIKKFQFLMFRLFSEARQPLSEEDVASLSWRPLHLPSADWQRAALSLWTHRTFREVLKEEDVHLTYQDWLHLELEIQPEADALSDTERQDFHQWAIHEHFLPESSASGGCDGDLQAACTILVNALMDFHQSSRSYDHSENSDLVFGGRTGNEDIISRLQEMVADLELQQDLIVPLGHTPSQEHFLFEIFRRRLQALTSGWSVAASLQRQRELLMYKRILLRLPSSVLCGSSFQAEQPITARCEQFFHLVNSEMRNFCSHGGALTQDITAHFFRGLLNACLRSRDPSLMVDFILAKCQTKCPLILTSALVWWPSLEPVLLCRWRRHCQSPLPRELQKLQEGRQFASDFLSPEAASPAPNPDWLSAAALHFAIQQVREENIRKQLKKLDCEREELLVFLFFFSLMGLLSSHLTSNSTTDLPKAFHVCAAILECLEKRKISWLALFQLTESDLRLGRLLLRVAPDQHTRLLPFAFYSLLSYFHEDAAIREEAFLHVAVDMYLKLVQLFVAGDTSTVSPPAGRSLELKGQGNPVELITKARLFLLQLIPRCPKKSFSHVAELLADRGDCDPEVSAALQSRQQAAPDADLSQEPHLF	Clinical trial	"Clinical pipeline report, company report or official report of Rocket Pharmaceuticals."	.	.	.	.	.	.	.	.	.	.	.	hsa03460: Fanconi anemia pathway	R-HSA-6783310: Fanconi Anemia Pathway	.	O15360
TTNZKFJ	Fanconi anemia group F protein (FANCF)	Q9NPI8	FANCF_HUMAN	.	Protein FACF	FANCF	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.	.	2IQC	MESLLQHLDRFSELLAVSSTTYVSTWDPATVRRALQWARYLRHIHRRFGRHGPIRTALERRLHNQWRQEGGFGRGPVPGLANFQALGHCDVLLSLRLLENRALGDAARYHLVQQLFPGPGVRDADEETLQESLARLARRRSAVHMLRFNGYRENPNLQEDSLMKTQAELLLERLQEVGKAEAERPARFLSSLWERLPQNNFLKVIAVALLQPPLSRRPQEELEPGIHKSPGEGSQVLVHWLLGNSEVFAAFCRALPAGLLTLVTSRHPALSPVYLGLLTDWGQRLHYDLQKGIWVGTESQDVPWEELHNRFQSLCQAPPPLKDKVLTALETCKAQDGDFEVPGLSIWTDLLLALRSGAFRKRQVLGLSAGLSSV	Literature-reported	Inactivation of the Fanconi anemia/BRCA pathway in lung and oral cancers: implications for treatment and survival. Oncogene. 2004 Jan 29;23(4):1000-4.	.	.	DNA repair	.	.	.	Fanconi anemia group F protein (FANCF)	PF11107	PF11107; FANCF	.	.	hsa03460: Fanconi anemia pathway	R-HSA-6783310: Fanconi Anemia Pathway	.	Q9NPI8
TTGPQ0F	Prolyl endopeptidase FAP (FAP)	Q12884	SEPR_HUMAN	Peptidase	Integral membrane serine protease; Fibroblast activation protein alpha; FAP; Antiplasmin-cleaving enzyme; APCE; 170-kDa melanoma membrane-bound gelatinase	FAP	"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."	EC 3.4.21.26	1Z68	MKTWVKIVFGVATSAVLALLVMCIVLRPSRVHNSEENTMRALTLKDILNGTFSYKTFFPNWISGQEYLHQSADNNIVLYNIETGQSYTILSNRTMKSVNASNYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLSNGEFVRGNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITFNGRENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTDIPVIAYSYYGDEQYPRTINIPYPKAGAKNPVVRIFIIDTTYPAYVGPQEVPVPAMIASSDYYFSWLTWVTDERVCLQWLKRVQNVSVLSICDFREDWQTWDCPKTQEHIEESRTGWAGGFFVSTPVFSYDAISYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEEYPGRRNIYRISIGSYPPSKKCVTCHLRKERCQYYTASFSDYAKYYALVCYGPGIPISTLHDGRTDQEIKILEENKELENALKNIQLPKEEIKKLEVDEITLWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASVYTERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGLSGLSTNHLYTHMTHFLKQCFSLSD	Clinical trial	Phase II trial of single agent Val-boroPro (Talabostat) inhibiting Fibroblast Activation Protein in patients with metastatic colorectal cancer. Cancer Biol Ther. 2007 Nov;6(11):1691-9.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	Q12884
TT7LTUJ	Fas messenger RNA (FAS mRNA)	P25445	TNR6_HUMAN	mRNA target	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)	FAS	"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."	.	3TJE; 3THM; 3EZQ; 3EWT; 2NA7	MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNLGWLCLLLLPIPLIVWVKRKEVQKTCRKHRKENQGSHESPTLNPETVAINLSDVDLSKYITTIAGVMTLSQVKGFVRKNGVNEAKIDEIKNDNVQDTAEQKVQLLRNWHQLHGKKEAYDTLIKDLKKANLCTLAEKIQTIILKDITSDSENSNFRNEIQSLV	Literature-reported	"US patent application no. 6,204,055, Antisense inhibition of Fas mediated signaling."	0	mRNA	mRNA target	.	.	.	Death domain; TNFR/NGFR cysteine-rich region	PF00531; PF00020	PF00531; Death; PF00020; TNFR_c6	.	.	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	R-HSA-75157:FasL/ CD95L signaling	.	P25445
TTF0RCZ	Apoptosis mediating surface antigen FAS (FAS)	P25445	TNR6_HUMAN	Cytokine receptor	Tumor necrosis factor receptor superfamily member 6; TNFRSF6; FASLG receptor; FAS1; CD95; Apoptosis-mediating surface antigen FAS; Apo-1 antigen; APT1	FAS	"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."	.	3TJE; 3THM; 3EZQ; 3EWT; 2NA7	MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNLGWLCLLLLPIPLIVWVKRKEVQKTCRKHRKENQGSHESPTLNPETVAINLSDVDLSKYITTIAGVMTLSQVKGFVRKNGVNEAKIDEIKNDNVQDTAEQKVQLLRNWHQLHGKKEAYDTLIKDLKKANLCTLAEKIQTIILKDITSDSENSNFRNEIQSLV	Clinical trial	"Phase I dose-escalation study of VB-111, an antiangiogenic virotherapy, in patients with advanced solid tumors.Clin Cancer Res.2013 Jul 15;19(14):3996-4007."	25	Cytokine receptor	Cytokine receptor	.	.	.	Death domain; TNFR/NGFR cysteine-rich region	PF00531; PF00020	PF00531; Death; PF00020; TNFR_c6	.	.	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	R-HSA-75157:FasL/ CD95L signaling	.	P25445
TTO7014	FasL messenger RNA (FASLG mRNA)	P48023	TNFL6_HUMAN	mRNA target	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)	FASLG	"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."	.	5L36; 5L19; 4MSV; 1BZI	MQQPFNYPYPQIYWVDSSASSPWAPPGTVLPCPTSVPRRPGQRRPPPPPPPPPLPPPPPPPPLPPLPLPPLKKRGNHSTGLCLLVMFFMVLVALVGLGLGMFQLFHLQKELAELRESTSQMHTASSLEKQIGHPSPPPEKKELRKVAHLTGKSNSRSMPLEWEDTYGIVLLSGVKYKKGGLVINETGLYFVYSKVYFRGQSCNNLPLSHKVYMRNSKYPQDLVMMEGKMMSYCTTGQMWARSSYLGAVFNLTSADHLYVNVSELSLVNFEESQTFFGLYKL	Literature-reported	"US patent application no. 6,204,055, Antisense inhibition of Fas mediated signaling."	0	mRNA	mRNA target	.	.	.	TNF(Tumour Necrosis Factor) family 	PF00229	PF00229; TNF	.	.	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	R-HSA-75157:FasL/ CD95L signaling	.	P48023
TTTNMUF	Apoptosis antigen ligand (CD178)	P48023	TNFL6_HUMAN	Cytokine: tumor necrosis factor	Tumor necrosis factor ligand superfamily member 6; TNFSF6; FasL; Fas ligand; FAS antigen ligand; CD95L; CD95-L; CD95 ligand; CD178 antigen; CD178; APTL; APT1LG1	FASLG	"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."	.	5L36; 5L19; 4MSV; 1BZI	MQQPFNYPYPQIYWVDSSASSPWAPPGTVLPCPTSVPRRPGQRRPPPPPPPPPLPPPPPPPPLPPLPLPPLKKRGNHSTGLCLLVMFFMVLVALVGLGLGMFQLFHLQKELAELRESTSQMHTASSLEKQIGHPSPPPEKKELRKVAHLTGKSNSRSMPLEWEDTYGIVLLSGVKYKKGGLVINETGLYFVYSKVYFRGQSCNNLPLSHKVYMRNSKYPQDLVMMEGKMMSYCTTGQMWARSSYLGAVFNLTSADHLYVNVSELSLVNFEESQTFFGLYKL	Literature-reported	Hypoxia stimulates release of the soluble form of fas ligand that inhibits endothelial cell apoptosis. Lab Invest. 2001 Feb;81(2):177-84.	.	Cytokine	Cytokine: tumor necrosis factor	tumor necrosis factor family.	.	.	TNF(Tumour Necrosis Factor) family 	PF00229	PF00229; TNF	.	.	hsa01524: Platinum drug resistance; hsa04010: MAPK signaling pathway; hsa04014: Ras signaling pathway; hsa04060: Cytokine-cytokine receptor interaction; hsa04068: FoxO signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04210: Apoptosis; hsa04217: Necroptosis; hsa04650: Natural killer cell mediated cytotoxicity; hsa04722: Neurotrophin signaling pathway; hsa04932: Non-alcoholic fatty liver disease; hsa04936: Alcoholic liver disease; hsa04940: Type I diabetes mellitus; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05130: Pathogenic Escherichia coli infection; hsa05142: Chagas disease; hsa05143: African trypanosomiasis; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05162: Measles; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; hsa05165: Human papillomavirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05320: Autoimmune thyroid disease; hsa05330: Allograft rejection; hsa05332: Graft-versus-host disease; hsa05417: Lipid and atherosclerosis	R-HSA-140534: Caspase activation via Death Receptors in the presence of ligand; R-HSA-3371378: Regulation by c-FLIP; R-HSA-5213460: RIPK1-mediated regulated necrosis; R-HSA-5218900: CASP8 activity is inhibited; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-69416: Dimerization of procaspase-8; R-HSA-75157: FasL/ CD95L signaling; R-HSA-8862803: Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models; R-HSA-9614657: FOXO-mediated transcription of cell death genes	.	P48023
TT7AOUD	Fatty acid synthase (FASN)	P49327	FAS_HUMAN	Acyltransferase	Yeast fatty acid synthase; Fatty-acyl-CoA synthase; Fatty acyl-CoA synthetase enzyme; FAS	FASN	"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."	EC 2.3.1.85	6NNA; 5C37; 4Z49; 4W9N; 4W82	MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRFDASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEALSRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLARRVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGPEVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEAQWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSLAWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLARALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQWDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRLLWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVVSRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQLCKGLVQALQTKVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQVLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLLSPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVAALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESLFSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRPVWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGDLVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPGAQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEEPEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLRSLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG	Successful	Inhibition of fatty acid biosynthesis prevents adipocyte lipotoxicity on human osteoblasts in vitro. J Cell Mol Med. 2010 Apr;14(4):982-91.	34	EC:2.3	Acyltransferase	.	2.3.1.85	Acyltransferases	"Acyl transferase domain; Zinc-binding dehydrogenase; Ketoacyl-synthetase C-terminal extension; Beta-ketoacyl synthase, N-terminal domain; Beta-ketoacyl synthase, C-terminal domain; KR domain; Methyltransferase domain; Phosphopantetheine attachment site; Polyketide synthase dehydratase; Thioesterase domain"	PF00698; PF00107; PF16197; PF00109; PF02801; PF08659; PF08242; PF00550; PF14765; PF00975	PF00698; Acyl_transf_1; PF00107; ADH_zinc_N; PF16197; KAsynt_C_assoc; PF00109; ketoacyl-synt; PF02801; Ketoacyl-synt_C; PF08659; KR; PF08242; Methyltransf_12; PF00550; PP-binding; PF14765; PS-DH; PF00975; Thioesterase	.	.	hsa00061:Fatty acid biosynthesis; hsa01100:Metabolic pathways; hsa01212:Fatty acid metabolism; hsa04152:AMPK signaling pathway; hsa04910:Insulin signaling pathway	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	MetaCyc:HS09992-MON	P49327
TTGUJYV	Protocadherin Fat 1 (FAT1)	Q14517	FAT1_HUMAN	.	"Protocadherin Fat 1, nuclear form; Protein fat homolog; Cadherin-related tumor suppressor homolog; Cadherin family member 7; CDHF7"	FAT1	"Plays an essential role for cellular polarization, directed cell migration and modulating cell-cell contact."	.	.	MGRHLALLLLLLLLFQHFGDSDGSQRLEQTPLQFTHLEYNVTVQENSAAKTYVGHPVKMGVYITHPAWEVRYKIVSGDSENLFKAEEYILGDFCFLRIRTKGGNTAILNREVKDHYTLIVKALEKNTNVEARTKVRVQVLDTNDLRPLFSPTSYSVSLPENTAIRTSIARVSATDADIGTNGEFYYSFKDRTDMFAIHPTSGVIVLTGRLDYLETKLYEMEILAADRGMKLYGSSGISSMAKLTVHIEQANECAPVITAVTLSPSELDRDPAYAIVTVDDCDQGANGDIASLSIVAGDLLQQFRTVRSFPGSKEYKVKAIGGIDWDSHPFGYNLTLQAKDKGTPPQFSSVKVIHVTSPQFKAGPVKFEKDVYRAEISEFAPPNTPVVMVKAIPAYSHLRYVFKSTPGKAKFSLNYNTGLISILEPVKRQQAAHFELEVTTSDRKASTKVLVKVLGANSNPPEFTQTAYKAAFDENVPIGTTVMSLSAVDPDEGENGYVTYSIANLNHVPFAIDHFTGAVSTSENLDYELMPRVYTLRIRASDWGLPYRREVEVLATITLNNLNDNTPLFEKINCEGTIPRDLGVGEQITTVSAIDADELQLVQYQIEAGNELDFFSLNPNSGVLSLKRSLMDGLGAKVSFHSLRITATDGENFATPLYINITVAASHKLVNLQCEETGVAKMLAEKLLQANKLHNQGEVEDIFFDSHSVNAHIPQFRSTLPTGIQVKENQPVGSSVIFMNSTDLDTGFNGKLVYAVSGGNEDSCFMIDMETGMLKILSPLDRETTDKYTLNITVYDLGIPQKAAWRLLHVVVVDANDNPPEFLQESYFVEVSEDKEVHSEIIQVEATDKDLGPNGHVTYSIVTDTDTFSIDSVTGVVNIARPLDRELQHEHSLKIEARDQAREEPQLFSTVVVKVSLEDVNDNPPTFIPPNYRVKVREDLPEGTVIMWLEAHDPDLGQSGQVRYSLLDHGEGNFDVDKLSGAVRIVQQLDFEKKQVYNLTVRAKDKGKPVSLSSTCYVEVEVVDVNENLHPPVFSSFVEKGTVKEDAPVGSLVMTVSAHDEDARRDGEIRYSIRDGSGVGVFKIGEETGVIETSDRLDRESTSHYWLTVFATDQGVVPLSSFIEIYIEVEDVNDNAPQTSEPVYYPEIMENSPKDVSVVQIEAFDPDSSSNDKLMYKITSGNPQGFFSIHPKTGLITTTSRKLDREQQDEHILEVTVTDNGSPPKSTIARVIVKILDENDNKPQFLQKFYKIRLPEREKPDRERNARREPLYHVIATDKDEGPNAEISYSIEDGNEHGKFFIEPKTGVVSSKRFSAAGEYDILSIKAVDNGRPQKSSTTRLHIEWISKPKPSLEPISFEESFFTFTVMESDPVAHMIGVISVEPPGIPLWFDITGGNYDSHFDVDKGTGTIIVAKPLDAEQKSNYNLTVEATDGTTTILTQVFIKVIDTNDHRPQFSTSKYEVVIPEDTAPETEILQISAVDQDEKNKLIYTLQSSRDPLSLKKFRLDPATGSLYTSEKLDHEAVHQHTLTVMVRDQDVPVKRNFARIVVNVSDTNDHAPWFTASSYKGRVYESAAVGSVVLQVTALDKDKGKNAEVLYSIESGNIGNSFMIDPVLGSIKTAKELDRSNQAEYDLMVKATDKGSPPMSEITSVRIFVTIADNASPKFTSKEYSVELSETVSIGSFVGMVTAHSQSSVVYEIKDGNTGDAFDINPHSGTIITQKALDFETLPIYTLIIQGTNMAGLSTNTTVLVHLQDENDNAPVFMQAEYTGLISESASINSVVLTDRNVPLVIRAADADKDSNALLVYHIVEPSVHTYFAIDSSTGAIHTVLSLDYEETSIFHFTVQVHDMGTPRLFAEYAANVTVHVIDINDCPPVFAKPLYEASLLLPTYKGVKVITVNATDADSSAFSQLIYSITEGNIGEKFSMDYKTGALTVQNTTQLRSRYELTVRASDGRFAGLTSVKINVKESKESHLKFTQDVYSAVVKENSTEAETLAVITAIGNPINEPLFYHILNPDRRFKISRTSGVLSTTGTPFDREQQEAFDVVVEVTEEHKPSAVAHVVVKVIVEDQNDNAPVFVNLPYYAVVKVDTEVGHVIRYVTAVDRDSGRNGEVHYYLKEHHEHFQIGPLGEISLKKQFELDTLNKEYLVTVVAKDGGNPAFSAEVIVPITVMNKAMPVFEKPFYSAEIAESIQVHSPVVHVQANSPEGLKVFYSITDGDPFSQFTINFNTGVINVIAPLDFEAHPAYKLSIRATDSLTGAHAEVFVDIIVDDINDNPPVFAQQSYAVTLSEASVIGTSVVQVRATDSDSEPNRGISYQMFGNHSKSHDHFHVDSSTGLISLLRTLDYEQSRQHTIFVRAVDGGMPTLSSDVIVTVDVTDLNDNPPLFEQQIYEARISEHAPHGHFVTCVKAYDADSSDIDKLQYSILSGNDHKHFVIDSATGIITLSNLHRHALKPFYSLNLSVSDGVFRSSTQVHVTVIGGNLHSPAFLQNEYEVELAENAPLHTLVMEVKTTDGDSGIYGHVTYHIVNDFAKDRFYINERGQIFTLEKLDRETPAEKVISVRLMAKDAGGKVAFCTVNVILTDDNDNAPQFRATKYEVNIGSSAAKGTSVVKVLASDADEGSNADITYAIEADSESVKENLEINKLSGVITTKESLIGLENEFFTFFVRAVDNGSPSKESVVLVYVKILPPEMQLPKFSEPFYTFTVSEDVPIGTEIDLIRAEHSGTVLYSLVKGNTPESNRDESFVIDRQSGRLKLEKSLDHETTKWYQFSILARCTQDDHEMVASVDVSIQVKDANDNSPVFESSPYEAFIVENLPGGSRVIQIRASDADSGTNGQVMYSLDQSQSVEVIESFAINMETGWITTLKELDHEKRDNYQIKVVASDHGEKIQLSSTAIVDVTVTDVNDSPPRFTAEIYKGTVSEDDPQGGVIAILSTTDADSEEINRQVTYFITGGDPLGQFAVETIQNEWKVYVKKPLDREKRDNYLLTITATDGTFSSKAIVEVKVLDANDNSPVCEKTLYSDTIPEDVLPGKLIMQISATDADIRSNAEITYTLLGSGAEKFKLNPDTGELKTSTPLDREEQAVYHLLVRATDGGGRFCQASIVLTLEDVNDNAPEFSADPYAITVFENTEPGTLLTRVQATDADAGLNRKILYSLIDSADGQFSINELSGIIQLEKPLDRELQAVYTLSLKAVDQGLPRRLTATGTVIVSVLDINDNPPVFEYREYGATVSEDILVGTEVLQVYAASRDIEANAEITYSIISGNEHGKFSIDSKTGAVFIIENLDYESSHEYYLTVEATDGGTPSLSDVATVNVNVTDINDNTPVFSQDTYTTVISEDAVLEQSVITVMADDADGPSNSHIHYSIIDGNQGSSFTIDPVRGEVKVTKLLDRETISGYTLTVQASDNGSPPRVNTTTVNIDVSDVNDNAPVFSRGNYSVIIQENKPVGFSVLQLVVTDEDSSHNGPPFFFTIVTGNDEKAFEVNPQGVLLTSSAIKRKEKDHYLLQVKVADNGKPQLSSLTYIDIRVIEESIYPPAILPLEIFITSSGEEYSGGVIGKIHATDQDVYDTLTYSLDPQMDNLFSVSSTGGKLIAHKKLDIGQYLLNVSVTDGKFTTVADITVHIRQVTQEMLNHTIAIRFANLTPEEFVGDYWRNFQRALRNILGVRRNDIQIVSLQSSEPHPHLDVLLFVEKPGSAQISTKQLLHKINSSVTDIEEIIGVRILNVFQKLCAGLDCPWKFCDEKVSVDESVMSTHSTARLSFVTPRHHRAAVCLCKEGRCPPVHHGCEDDPCPEGSECVSDPWEEKHTCVCPSGRFGQCPGSSSMTLTGNSYVKYRLTENENKLEMKLTMRLRTYSTHAVVMYARGTDYSILEIHHGRLQYKFDCGSGPGIVSVQSIQVNDGQWHAVALEVNGNYARLVLDQVHTASGTAPGTLKTLNLDNYVFFGGHIRQQGTRHGRSPQVGNGFRGCMDSIYLNGQELPLNSKPRSYAHIEESVDVSPGCFLTATEDCASNPCQNGGVCNPSPAGGYYCKCSALYIGTHCEISVNPCSSKPCLYGGTCVVDNGGFVCQCRGLYTGQRCQLSPYCKDEPCKNGGTCFDSLDGAVCQCDSGFRGERCQSDIDECSGNPCLHGALCENTHGSYHCNCSHEYRGRHCEDAAPNQYVSTPWNIGLAEGIGIVVFVAGIFLLVVVFVLCRKMISRKKKHQAEPKDKHLGPATAFLQRPYFDSKLNKNIYSDIPPQVPVRPISYTPSIPSDSRNNLDRNSFEGSAIPEHPEFSTFNPESVHGHRKAVAVCSVAPNLPPPPPSNSPSDSDSIQKPSWDFDYDTKVVDLDPCLSKKPLEEKPSQPYSARESLSEVQSLSSFQSESCDDNGYHWDTSDWMPSVPLPDIQEFPNYEVIDEQTPLYSADPNAIDTDYYPGGYDIESDFPPPPEDFPAADELPPLPPEFSNQFESIHPPRDMPAAGSLGSSSRNRQRFNLNQYLPNFYPLDMSEPQTKGTGENSTCREPHAPYPPGYQRHFEAPAVESMPMSVYASTASCSDVSACCEVESEVMMSDYESGDDGHFEEVTIPPLDSQQHTEV	Literature-reported	Protocadherin FAT1 binds Ena/VASP proteins and is necessary for actin dynamics and cell polarization. EMBO J. 2004 Oct 1;23(19):3769-79.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTWHDVK	"Fructose-1,6-bisphosphatase (FBP)"	P09467; O00757	F16P1_HUMAN; F16P2_HUMAN	Phosphoric monoester hydrolase	"FBPase; D-fructose-1,6-bisphosphate 1-phosphohydrolase"	FBP1	"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."	.	.	MADQAPFDTDVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHSAQ	Clinical trial	"MB06322 (CS-917): A potent and selective inhibitor of fructose 1,6-bisphosphatase for controlling gluconeogenesis in type 2 diabetes. Proc Natl Acad Sci U S A. 2005 May 31;102(22):7970-5."	21	.	.	.	.	.	.	.	.	.	.	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	R-HSA-70263:Gluconeogenesis	MetaCyc:HS09189-MON	P09467
TT6G10V	Vitiligo-associated protein 1 (FBXO11)	Q86XK2	FBX11_HUMAN	.	Vitiligoassociated protein 1; VIT1; VIT-1; UG063H01; Protein arginine N-methyltransferase 9; PRMT9; Fbox only protein 11; FBX11; F-box only protein 11	FBXO11	"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."	.	5VMD	MNSVRAANRRPRRVSRPRPVQQQQQQPPQQPPPQPPQQQPPQQQPPPPPQQQQQQQPPPPPPPPPPLPQERNNVGERDDDVPADMVAEESGPGAQNSPYQLRRKTLLPKRTACPTKNSMEGASTSTTENFGHRAKRARVSGKSQDLSAAPAEQYLQEKLPDEVVLKIFSYLLEQDLCRAACVCKRFSELANDPILWKRLYMEVFEYTRPMMHPEPGKFYQINPEEYEHPNPWKESFQQLYKGAHVKPGFAEHFYSNPARYKGRENMLYYDTIEDALGGVQEAHFDGLIFVHSGIYTDEWIYIESPITMIGAAPGKVADKVIIENTRDSTFVFMEGSEDAYVGYMTIRFNPDDKSAQHHNAHHCLEITVNCSPIIDHCIIRSTCTVGSAVCVSGQGACPTIKHCNISDCENVGLYITDHAQGIYEDNEISNNALAGIWVKNHGNPIIRRNHIHHGRDVGVFTFDHGMGYFESCNIHRNRIAGFEVKAYANPTVVRCEIHHGQTGGIYVHEKGRGQFIENKIYANNFAGVWITSNSDPTIRGNSIFNGNQGGVYIFGDGRGLIEGNDIYGNALAGIQIRTNSCPIVRHNKIHDGQHGGIYVHEKGQGVIEENEVYSNTLAGVWVTTGSTPVLRRNRIHSGKQVGVYFYDNGHGVLEDNDIYNHMYSGVQIRTGSNPKIRRNKIWGGQNGGILVYNSGLGCIEDNEIFDNAMAGVWIKTDSNPTLRRNKIHDGRDGGICIFNGGRGLLEENDIFRNAQAGVLISTNSHPILRKNRIFDGFAAGIEITNHATATLEGNQIFNNRFGGLFLASGVNVTMKDNKIMNNQDAIEKAVSRGQCLYKISSYTSYPMHDFYRCHTCNTTDRNAICVNCIKKCHQGHDVEFIRHDRFFCDCGAGTLSNPCTLAGEPTHDTDTLYDSAPPIESNTLQHN	Literature-reported	FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas. Nature. 2012 Jan 5;481(7379):90-3.	.	.	.	.	.	.	Right handed beta helix region; F-box-like; Periplasmic copper-binding protein (NosD); Putative zinc finger in N-recognin (UBR box)	PF13229; PF12937; PF05048; PF02207	PF13229; Beta_helix; PF12937; F-box-like; PF05048; NosD; PF02207; zf-UBR	.	.	.	R-HSA-8951664: Neddylation; R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	Q86XK2
TTUX14L	F-box only protein 3 (FBXO3)	Q9UK99	FBX3_HUMAN	.	.	FBXO3	"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."	.	.	MAAMETETAPLTLESLPTDPLLLILSFLDYRDLINCCYVSRRLSQLSSHDPLWRRHCKKYWLISEEEKTQKNQCWKSLFIDTYSDVGRYIDHYAAIKKAWDDLKKYLEPRCPRMVLSLKEGAREEDLDAVEAQIGCKLPDDYRCSYRIHNGQKLVVPGLLGSMALSNHYRSEDLLDVDTAAGGFQQRQGLKYCLPLTFCIHTGLSQYIAVEAAEGRNKNEVFYQCPDQMARNPAAIDMFIIGATFTDWFTSYVKNVVSGGFPIIRDQIFRYVHDPECVATTGDITVSVSTSFLPELSSVHPPHYFFTYRIRIEMSKDALPEKACQLDSRYWRITNAKGDVEEVQGPGVVGEFPIISPGRVYEYTSCTTFSTTSGYMEGYYTFHFLYFKDKIFNVAIPRFHMACPTFRVSIARLEMGPDEYEEMEEEEEEEEEEDEDDDSADMDESDEDDEEERRRRVFDVPIRRRRCSRLF	Preclinical	Targeting F box protein Fbxo3 to control cytokine-driven inflammation. J Immunol. 2013 Nov 15;191(10):5247-55.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9UK99
TT29KY7	F-box and WD-40 domain protein 7 (Fbxw7)	Q969H0	FBXW7_HUMAN	.	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	FBXW7	"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."	.	5V4B; 5IBK; 2OVR; 2OVQ; 2OVP	MNQELLSVGSKRRRTGGSLRGNPSSSQVDEEQMNRVVEEEQQQQLRQQEEEHTARNGEVVGVEPRPGGQNDSQQGQLEENNNRFISVDEDSSGNQEEQEEDEEHAGEQDEEDEEEEEMDQESDDFDQSDDSSREDEHTHTNSVTNSSSIVDLPVHQLSSPFYTKTTKMKRKLDHGSEVRSFSLGKKPCKVSEYTSTTGLVPCSATPTTFGDLRAANGQGQQRRRITSVQPPTGLQEWLKMFQSWSGPEKLLALDELIDSCEPTQVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKCKEEGIDEPLHIKRRKVIKPGFIHSPWKSAYIRQHRIDTNWRRGELKSPKVLKGHDDHVITCLQFCGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWSSQMRDNIIISGSTDRTLKVWNAETGECIHTLYGHTSTVRCMHLHEKRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQYDGRRVVSGAYDFMVKVWDPETETCLHTLQGHTNRVYSLQFDGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGMELKDNILVSGNADSTVKIWDIKTGQCLQTLQGPNKHQSAVTCLQFNKNFVITSSDDGTVKLWDLKTGEFIRNLVTLESGGSGGVVWRIRASNTKLVCAVGSRNGTEETKLLVLDFDVDMK	Literature-reported	"BRAF and FBXW7 (CDC4, FBW7, AGO, SEL10) mutations in distinct subsets of pancreatic cancer: potential therapeutic targets. Am J Pathol. 2003 Oct;163(4):1255-60."	.	.	.	.	.	.	"F-box-like; WD domain, G-beta repeat"	PF12937; PF00400	PF12937; F-box-like; PF00400; WD40	.	.	hsa04120: Ubiquitin mediated proteolysis	R-HSA-2122947: NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2644606: Constitutive Signaling by NOTCH1 PEST Domain Mutants; R-HSA-2644607: Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling; R-HSA-2894862: Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants; R-HSA-390471: Association of TriC/CCT with target proteins during biosynthesis; R-HSA-8939902: Regulation of RUNX2 expression and activity; R-HSA-8951664: Neddylation; R-HSA-9604323: Negative regulation of NOTCH4 signaling; R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	Q969H0
TTGUJAO	Immunoglobulin alpha Fc receptor (FCAR)	P24071	FCAR_HUMAN	.	IgA Fc receptor; FCAR; CD89 antigen; CD89	FCAR	Binds to the fc region of immunoglobulins alpha. Mediates several functions including cytokine production.	.	1UCT; 1OW0; 1OVZ	MDPKQTTLLCLVLCLGQRIQAQEGDFPMPFISAKSSPVIPLDGSVKIQCQAIREAYLTQLMIIKNSTYREIGRRLKFWNETDPEFVIDHMDANKAGRYQCQYRIGHYRFRYSDTLELVVTGLYGKPFLSADRGLVLMPGENISLTCSSAHIPFDRFSLAKEGELSLPQHQSGEHPANFSLGPVDLNVSGIYRCYGWYNRSPYLWSFPSNALELVVTDSIHQDYTTQNLIRMAVAGLVLVALLAILVENWHSHTALNKEASADVAEPSWSQQMCQPGLTFARTPSVCK	Discontinued	"A phase I, pharmacokinetic (PK) and pharmacodynamic (PD) study of MDX-214, a novel immune-mediated mechanism agent targeting the epithelial growth factor receptor (EGFR), in patients with advanced solid tumors. Journal of Clinical Oncology, Vol 24, No 18S (June 20 Supplement), 2006: 2523."	4	.	.	.	.	.	.	.	.	.	.	hsa04145:Phagosome; hsa05150:Staphylococcus aureus infection	R-HSA-6798695: Neutrophil degranulation	.	P24071
TTDGEC0	Immunoglobulin epsilon Fc receptor gamma (FCERG)	P30273	FCERG_HUMAN	Immunoglobulin	IgE Fc receptor subunit gamma; High affinity immunoglobulin epsilon receptor subunit gamma; FceRI gamma; FcRgamma; Fc receptor gamma-chain	FCER1G	"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."	.	.	MIPAVVLLLLLLVEQAAALGEPQLCYILDAILFLYGIVLTLLYCRLKIQVRKAAITSYEKSDGVYTGLSTRNQETYETLKHEKPPQ	Successful	Penicillin allergy: anti-penicillin IgE antibodies and immediate hypersensitivity skin reactions employing major and minor determinants of penicillin. Arch Dis Child. 1980 Nov;55(11):857-60.	34	.	.	CD3Z/FCER1G family.	.	.	Immunoreceptor tyrosine-based activation motif; T-cell surface glycoprotein CD3 zeta chain	PF02189; PF11628	PF02189; ITAM; PF11628; TCR_zetazeta	.	.	hsa04071:Sphingolipid signaling pathway; hsa04664:Fc epsilon RI signaling pathway; hsa05310:Asthma	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	.	P30273
TTCH6MU	Lymphocyte IgE receptor (CD23)	P06734	FCER2_HUMAN	Immunoglobulin	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	FCER2	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).	.	5LGK; 4KI1; 4J6Q; 4J6P; 4J6N	MEEGQYSEIEELPRRRCCRRGTQIVLLGLVTAALWAGLLTLLLLWHWDTTQSLKQLEERAARNVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLSSFKSQELNERNEASDLLERLREEVTKLRMELQVSSGFVCNTCPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVDYSNWAPGEPTSRSQGEDCVMMRGSGRWNDAFCDRKLGAWVCDRLATCTPPASEGSAESMGPDSRPDPDGRLPTPSAPLHS	Clinical trial	"Anti-CD23 monoclonal antibody, lumiliximab, inhibited allergen-induced responses in antigen-presenting cells and T cells from atopic subjects. J Allergy Clin Immunol. 2005 Oct;116(4):780-8."	21	.	.	.	.	.	.	.	.	.	.	hsa04640:Hematopoietic cell lineage; hsa05169:Epstein-Barr virus infection	R-HSA-2197563:NOTCH2 intracellular domain regulates transcription	.	P06734
TTZK4I3	Immunoglobulin gamma Fc receptor I (FCGR1)	P12314	FCGR1_HUMAN	Immunoglobulin	IgG Fc receptor I; FcRI; Fc-gamma RI; FCGR1A; CD64 antigen; CD64	FCGR1A	High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses.	.	4ZNE; 4X4M; 4W4O; 3RJD	MWFLTTLLLWVPVDGQVDTTKAVITLQPPWVSVFQEETVTLHCEVLHLPGSSSTQWFLNGTATQTSTPSYRITSASVNDSGEYRCQRGLSGRSDPIQLEIHRGWLLLQVSSRVFTEGEPLALRCHAWKDKLVYNVLYYRNGKAFKFFHWNSNLTILKTNISHNGTYHCSGMGKHRYTSAGISVTVKELFPAPVLNASVTSPLLEGNLVTLSCETKLLLQRPGLQLYFSFYMGSKTLRGRNTSSEYQILTARREDSGLYWCEAATEDGNVLKRSPELELQVLGLQLPTPVWFHVLFYLAVGIMFLVNTVLWVTIRKELKRKKKWDLEISLDSGHEKKVISSLQEDRHLEEELKCQEQKEEQLQEGVHRKEPQGAT	Literature-reported	Neutrophil Fc gamma RI as target for immunotherapy of invasive candidiasis. J Immunol. 2001 Jun 15;166(12):7019-22.	.	.	.	.	.	.	.	.	.	.	.	hsa04145: Phagosome; hsa04380: Osteoclast differentiation; hsa04613: Neutrophil extracellular trap formation; hsa04640: Hematopoietic cell lineage; hsa04666: Fc gamma R-mediated phagocytosis; hsa05140: Leishmaniasis; hsa05150: Staphylococcus aureus infection; hsa05152: Tuberculosis; hsa05202: Transcriptional misregulation in cancer; hsa05221: Acute myeloid leukemia; hsa05322: Systemic lupus erythematosus	R-HSA-1236978: Cross-presentation of soluble exogenous antigens (endosomes); R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; 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-877300: Interferon gamma signaling; R-HSA-9664323: FCGR3A-mediated IL10 synthesis	.	P12314
TTXT21W	Immunoglobulin gamma Fc receptor IIA (FCGR2A)	P12318	FCG2A_HUMAN	Immunoglobulin	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	FCGR2A	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.	.	3RY6; 3RY5; 3RY4; 3D5O; 1H9V	MTMETQMSQNVCPRNLWLLQPLTVLLLLASADSQAAAPPKAVLKLEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVTITVQVPSMGSSSPMGIIVAVVIATAVAAIVAAVVALIYCRKKRISANSTDPVKAAQFEPPGRQMIAIRKRQLEETNNDYETADGGYMTLNPRAPTDDDKNIYLTLPPNDHVNSNN	Successful	Emerging drugs for idiopathic thrombocytopenic purpura in adults. Expert Opin Emerg Drugs. 2008 Jun;13(2):237-54.	34	.	Transmembrane protein	.	.	.	Immunoglobulin domain	PF13895	PF13895; Ig_2	.	.	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	R-HSA-2029481:FCGR activation; R-HSA-2029482:Regulation of actin dynamics for phagocytic cup formation; R-HSA-2029485:Role of phospholipids in phagocytosis	.	P12318
TTST6IQ	Immunoglobulin gamma Fc receptor II (FCGR2)	P12318; P31994; P31995	FCG2A_HUMAN; FCG2B_HUMAN; FCG2C_HUMAN	Immunoglobulin	Low affinity immunoglobulin gamma Fc region receptor II; IgG Fc receptor II; IGFR2; FcRII; Fc-gamma-RII; Fc-gamma RII; FCG2; CDw32; CD32	FCGR2A	"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."	.	.	MTMETQMSQNVCPRNLWLLQPLTVLLLLASADSQAAAPPKAVLKLEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVTITVQVPSMGSSSPMGIIVAVVIATAVAAIVAAVVALIYCRKKRISANSTDPVKAAQFEPPGRQMIAIRKRQLEETNNDYETADGGYMTLNPRAPTDDDKNIYLTLPPNDHVNSNN	Literature-reported	Fc gamma receptor IIb participates in maternal IgG trafficking of human placental endothelial cells. Int J Mol Med. 2015 May;35(5):1273-89.	.	.	.	.	.	.	.	.	.	.	.	hsa04145: Phagosome; hsa04380: Osteoclast differentiation; hsa04611: Platelet activation; hsa04613: Neutrophil extracellular trap formation; hsa04666: Fc gamma R-mediated phagocytosis; hsa05130: Pathogenic Escherichia coli infection; hsa05135: Yersinia infection; hsa05140: Leishmaniasis; hsa05150: Staphylococcus aureus infection; hsa05152: Tuberculosis; hsa05171: Coronavirus disease - COVID-19; hsa05322: Systemic lupus erythematosus	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-6798695: Neutrophil degranulation; R-HSA-9664323: FCGR3A-mediated IL10 synthesis	.	P12318
TT5RWKQ	Immunoglobulin gamma Fc receptor IIB (FCGR2B)	P31994	FCG2B_HUMAN	Immunoglobulin	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	FCGR2B	"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."	.	5OCC; 3WJJ; 2FCB	MGILSFLPVLATESDWADCKSPQPWGHMLLWTAVLFLAPVAGTPAAPPKAVLKLEPQWINVLQEDSVTLTCRGTHSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIVLRCHSWKDKPLVKVTFFQNGKSKKFSRSDPNFSIPQANHSHSGDYHCTGNIGYTLYSSKPVTITVQAPSSSPMGIIVAVVTGIAVAAIVAAVVALIYCRKKRISALPGYPECREMGETLPEKPANPTNPDEADKVGAENTITYSLLMHPDALEEPDDQNRI	Clinical trial	CD19 as an attractive target for antibody-based therapy. MAbs. 2012 Sep-Oct;4(5):571-7.	21	.	.	.	.	.	Immunoglobulin domain	PF13895	PF13895; Ig_2	.	.	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	R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	P31994
TTIFOC0	Immunoglobulin gamma Fc receptor IIIA (FCGR3A)	P08637	FCG3A_HUMAN	Immunoglobulin	FCGR3A	FCGR3A	"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."	.	5YC5; 5XJF; 5XJE; 5VU0; 5MN2	MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTQWFHNESLISSQASSYFIDAATVDDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKGRKYFHHNSDFYIPKATLKDSGSYFCRGLFGSKNVSSETVNITITQGLAVSTISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKTNIRSSTRDWKDHKFKWRKDPQDK	Clinical trial	Bispecific antibodies rise again. Nat Rev Drug Discov. 2014 Nov;13(11):799-801. 	21	.	.	.	.	.	.	.	.	.	.	hsa04145: Phagosome; hsa04380: Osteoclast differentiation; hsa04613: Neutrophil extracellular trap formation; hsa04650: Natural killer cell mediated cytotoxicity; hsa04666: Fc gamma R-mediated phagocytosis; hsa05140: Leishmaniasis; hsa05150: Staphylococcus aureus infection; hsa05152: Tuberculosis; hsa05322: Systemic lupus erythematosus	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; 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-9664323: FCGR3A-mediated IL10 synthesis; R-HSA-9664422: FCGR3A-mediated phagocytosis	.	P08637
TT7KTSR	Immunoglobulin gamma Fc receptor III (FCGR3)	P08637; O75015	FCG3A_HUMAN; FCG3B_HUMAN	Immunoglobulin	Low affinity immunoglobulin gamma Fc region receptor III; IgG Fc receptor III; IGFR3; FcRIIIb; FcRIIIa; FcRIII; FcR-10; Fc-gamma RIII; FCGR3; FCG3; CD16	FCGR3A	"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."	.	.	MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTQWFHNESLISSQASSYFIDAATVDDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKGRKYFHHNSDFYIPKATLKDSGSYFCRGLFGSKNVSSETVNITITQGLAVSTISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKTNIRSSTRDWKDHKFKWRKDPQDK	Successful	Emerging drugs for idiopathic thrombocytopenic purpura in adults. Expert Opin Emerg Drugs. 2008 Jun;13(2):237-54.	34	.	.	.	.	.	.	.	.	.	.	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	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; 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-9664323: FCGR3A-mediated IL10 synthesis; R-HSA-9664422: FCGR3A-mediated phagocytosis	.	P08637
TTKLPHO	Neonatal Fc receptor (FCGRT)	P55899	FCGRN_HUMAN	Immunoglobulin	"Neonatal FcR; MHC class I family-like Fc receptor; IgG Fc fragment receptor transporter, alpha chain; FcRn; FCGRT"	FCGRT	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.	.	6ILM; 6FGB; 6C99; 6C98; 6C97	MGVPRPQPWALGLLLFLLPGSLGAESHLSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGEAEPCGAWVWENQVSWYWEKETTDLRIKEKLFLEAFKALGGKGPYTLQGLLGCELGPDNTSVPTAKFALNGEEFMNFDLKQGTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLREHLERGRGNLEWKEPPSMRLKARPSSPGFSVLTCSAFSFYPPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSLTVKSGDEHHYCCIVQHAGLAQPLRVELESPAKSSVLVVGIVIGVLLLTAAAVGGALLWRRMRSGLPAPWISLRGDDTGVLLPTPGEAQDADLKDVNVIPATA	Clinical trial	Structure-activity relationships of a peptide inhibitor of the human FcRn:human IgG interaction. Bioorg Med Chem. 2008 Jun 15;16(12):6394-405.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P55899
TTFQEO5	Squalene synthetase (FDFT1)	P37268	FDFT_HUMAN	Alkyl aryl transferase	Squalene synthase; SS; SQS; Farnesyl-diphosphate farnesyltransferase; FPP:FPP farnesyltransferase	FDFT1	"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."	EC 2.5.1.21	3WSA; 3WEK; 3WEJ; 3WEI; 3WEH	MEFVKCLGHPEEFYNLVRFRIGGKRKVMPKMDQDSLSSSLKTCYKYLNQTSRSFAAVIQALDGEMRNAVCIFYLVLRALDTLEDDMTISVEKKVPLLHNFHSFLYQPDWRFMESKEKDRQVLEDFPTISLEFRNLAEKYQTVIADICRRMGIGMAEFLDKHVTSEQEWDKYCHYVAGLVGIGLSRLFSASEFEDPLVGEDTERANSMGLFLQKTNIIRDYLEDQQGGREFWPQEVWSRYVKKLGDFAKPENIDLAVQCLNELITNALHHIPDVITYLSRLRNQSVFNFCAIPQVMAIATLAACYNNQQVFKGAVKIRKGQAVTLMMDATNMPAVKAIIYQYMEEIYHRIPDSDPSSSKTRQIISTIRTQNLPNCQLISRSHYSPIYLSFVMLLAALSWQYLTTLSQVTEDYVQTGEH	Discontinued	"Lapaquistat acetate, a squalene synthase inhibitor, changes macrophage/lipid-rich coronary plaques of hypercholesterolaemic rabbits into fibrous le... Br J Pharmacol. 2008 Jul;154(5):949-57."	9	.	.	.	.	.	.	.	.	.	.	hsa00100:Steroid biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics	R-HSA-191273:Cholesterol biosynthesis; R-HSA-1989781:PPARA activates gene expression; R-HSA-2426168:Activation of gene expression by SREBF (SREBP)	MetaCyc:HS01329-MON	P37268
TTIKWV4	Geranyltranstransferase (FDPS)	P14324	FPPS_HUMAN	Alkyl aryl transferase	"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"	FDPS	"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."	EC 2.5.1.10	5YGI; 5KSX; 5JV2; 5JV1; 5JV0	MPLSRWLRSVGVFLLPAPYWAPRERWLGSLRRPSLVHGYPVLAWHSARCWCQAWTEEPRALCSSLRMNGDQNSDVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGKYNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK	Successful	Inhibition of geranylgeranyl diphosphate synthase by bisphosphonates: a crystallographic and computational investigation. J Med Chem. 2008 Sep 25;51(18):5594-607.	34	EC:2.5	.	FPP/GGPP synthase family.	2.5.1.10	"Transferring alkyl or aryl groups, other than methyl groups"	Polyprenyl synthetase	PF00348	PF00348; polyprenyl_synt	.	.	hsa00900:Terpenoid backbone biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics	R-HSA-191273:Cholesterol biosynthesis; R-HSA-2426168:Activation of gene expression by SREBF (SREBP)	MetaCyc:ENSG00000160752-MON	P14324
TT3W4IX	NADPH:adrenodoxin oxidoreductase (FDXR)	P22570	ADRO_HUMAN	Ferredoxin--NADP reductase type 1	"NADPH:adrenodoxin oxidoreductase, mitochondrial; FerredoxinNADP(+) reductase; Ferredoxin reductase; FDXR; Adrenodoxin reductase"	FDXR	"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."	EC 1.18.1.6	.	MASRCWRWWGWSAWPRTRLPPAGSTPSFCHHFSTQEKTPQICVVGSGPAGFYTAQHLLKHPQAHVDIYEKQPVPFGLVRFGVAPDHPEVKNVINTFTQTAHSGRCAFWGNVEVGRDVTVPELREAYHAVVLSYGAEDHRALEIPGEELPGVCSARAFVGWYNGLPENQELEPDLSCDTAVILGQGNVALDVARILLTPPEHLERTDITKAALGVLRQSRVKTVWLVGRRGPLQVAFTIKELREMIQLPGARPILDPVDFLGLQDKIKEVPRPRKRLTELLLRTATEKPGPAEAARQASASRAWGLRFFRSPQQVLPSPDGRRAAGVRLAVTRLEGVDEATRAVPTGDMEDLPCGLVLSSIGYKSRPVDPSVPFDSKLGVIPNVEGRVMDVPGLYCSGWVKRGPTGVIATTMTDSFLTGQMLLQDLKAGLLPSGPRPGYAAIQALLSSRGVRPVSFSDWEKLDAEEVARGQGTGKPREKLVDPQEMLRLLGH	Literature-reported	Plasma membrane NADH-oxidoreductase system: a critical review of the structural and functional data. Antioxid Redox Signal. 2000 Summer;2(2):197-212.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-196108: Pregnenolone biosynthesis; R-HSA-211976: Endogenous sterols; R-HSA-2395516: Electron transport from NADPH to Ferredoxin; R-HSA-5579026: Defective CYP11A1 causes AICSR	MetaCyc:HS08587-MON	P22570
TTQ6VF4	Ferrochelatase (FECH)	P22830	HEMH_HUMAN	Ferrochelatase	Protoheme ferro-lyase; Heme synthetase; FECH	FECH	Catalyzes the ferrous insertion into protoporphyrin IX.	EC 4.99.1.1	4MK4; 4KMM; 4KLR; 4KLC; 4KLA	MRSLGANMAAALRAAGVLLRDPLASSSWRVCQPWRWKSGAAAAAVTTETAQHAQGAKPQVQPQKRKPKTGILMLNMGGPETLGDVHDFLLRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQEQYRRIGGGSPIKIWTSKQGEGMVKLLDELSPNTAPHKYYIGFRYVHPLTEEAIEEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNQVGRKPTMKWSTIDRWPTHHLLIQCFADHILKELDHFPLEKRSEVVILFSAHSLPMSVVNRGDPYPQEVSATVQKVMERLEYCNPYRLVWQSKVGPMPWLGPQTDESIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAKECGVENIRRAESLNGNPLFSKALADLVHSHIQSNELCSKQLTLSCPLCVNPVCRETKSFFTSQQL	Successful	Low-dose methotrexate enhances aminolevulinate-based photodynamic therapy in skin carcinoma cells in vitro and in vivo. Clin Cancer Res. 2009 May 15;15(10):3333-43.	34	.	.	.	.	.	.	.	.	.	.	hsa00860:Porphyrin and chlorophyll metabolism; hsa01100:Metabolic pathways	R-HSA-189451: Heme biosynthesis	MetaCyc:HS00891-MON	P22830
TTRA9G0	Proto-oncogene c-Fer (FER)	P16591	FER_HUMAN	Kinase	p94-Fer; Tyrosine-protein kinase Fer; Tyrosine kinase 3; TYK3; Fujinami poultry sarcoma/Feline sarcoma-related protein Fer; Feline encephalitis virus-related kinase FER	FER	"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."	EC 2.7.10.2	2KK6	MGFGSDLKNSHEAVLKLQDWELRLLETVKKFMALRIKSDKEYASTLQNLCNQVDKESTVQMNYVSNVSKSWLLMIQQTEQLSRIMKTHAEDLNSGPLHRLTMMIKDKQQVKKSYIGVHQQIEAEMIKVTKTELEKLKCSYRQLIKEMNSAKEKYKEALAKGKETEKAKERYDKATMKLHMLHNQYVLALKGAQLHQNQYYDITLPLLLDSLQKMQEEMIKALKGIFDEYSQITSLVTEEIVNVHKEIQMSVEQIDPSTEYNNFIDVHRTTAAKEQEIEFDTSLLEENENLQANEIMWNNLTAESLQVMLKTLAEELMQTQQMLLNKEEAVLELEKRIEESSETCEKKSDIVLLLSQKQALEELKQSVQQLRCTEAKFSAQKELLEQKVQENDGKEPPPVVNYEEDARSVTSMERKERLSKFESIRHSIAGIIRSPKSALGSSALSDMISISEKPLAEQDWYHGAIPRIEAQELLKKQGDFLVRESHGKPGEYVLSVYSDGQRRHFIIQYVDNMYRFEGTGFSNIPQLIDHHYTTKQVITKKSGVVLLNPIPKDKKWILSHEDVILGELLGKGNFGEVYKGTLKDKTSVAVKTCKEDLPQELKIKFLQEAKILKQYDHPNIVKLIGVCTQRQPVYIIMELVSGGDFLTFLRRKKDELKLKQLVKFSLDAAAGMLYLESKNCIHRDLAARNCLVGENNVLKISDFGMSRQEDGGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVERGYRMSAPQHCPEDISKIMMKCWDYKPENRPKFSELQKELTIIKRKLT	Literature-reported	Design of potent and selective inhibitors to overcome clinical anaplastic lymphoma kinase mutations resistant to crizotinib. J Med Chem.> 2014 Feb 27;57(4):1170-87.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily.	2.7.10.2	Transferring phosphorus-containing groups	"Fes/CIP4, and EFC/F-BAR homology domain; Protein tyrosine kinase; SH2 domain"	PF00611; PF07714; PF00017	PF00611; FCH; PF07714; Pkinase_Tyr; PF00017; SH2	.	.	hsa04520: Adherens junction	R-HSA-1433557: Signaling by SCF-KIT	.	P16591
TTLBY21	Proto-oncogene c-Fes (FES)	P07332	FES_HUMAN	Kinase	p93c-fes; Tyrosine-protein kinase Fes/Fps; Proto-oncogene c-Fps; Feline sarcoma/Fujinami avian sarcoma oncogene homolog; FPS	FES	"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."	EC 2.7.10.2	4DYL; 4.00E+93; 3CD3; 3CBL; 3BKB	MGFSSELCSPQGHGVLQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDSGGQSRAISPDSPISQSWAEITSQTEGLSRLLRQHAEDLNSGPLSKLSLLIRERQQLRKTYSEQWQQLQQELTKTHSQDIEKLKSQYRALARDSAQAKRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHQHHHQLLLPGLLRSLQDLHEEMACILKEILQEYLEISSLVQDEVVAIHREMAAAAARIQPEAEYQGFLRQYGSAPDVPPCVTFDESLLEEGEPLEPGELQLNELTVESVQHTLTSVTDELAVATEMVFRRQEMVTQLQQELRNEEENTHPRERVQLLGKRQVLQEALQGLQVALCSQAKLQAQQELLQTKLEHLGPGEPPPVLLLQDDRHSTSSSEQEREGGRTPTLEILKSHISGIFRPKFSLPPPLQLIPEVQKPLHEQLWYHGAIPRAEVAELLVHSGDFLVRESQGKQEYVLSVLWDGLPRHFIIQSLDNLYRLEGEGFPSIPLLIDHLLSTQQPLTKKSGVVLHRAVPKDKWVLNHEDLVLGEQIGRGNFGEVFSGRLRADNTLVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGARLRVKTLLQMVGDAAAGMEYLESKCCIHRDLAARNCLVTEKNVLKISDFGMSREEADGVYAASGGLRQVPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGASPYPNLSNQQTREFVEKGGRLPCPELCPDAVFRLMEQCWAYEPGQRPSFSTIYQELQSIRKRHR	Literature-reported	Design of potent and selective inhibitors to overcome clinical anaplastic lymphoma kinase mutations resistant to crizotinib. J Med Chem.> 2014 Feb 27;57(4):1170-87.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily.	2.7.10.2	Transferring phosphorus-containing groups	Protein tyrosine kinase; SH2 domain	PF07714; PF00017	PF07714; Pkinase_Tyr; PF00017; SH2	.	.	hsa04360: Axon guidance	R-HSA-1433557: Signaling by SCF-KIT; R-HSA-399954: Sema3A PAK dependent Axon repulsion; R-HSA-399955: SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion; R-HSA-399956: CRMPs in Sema3A signaling	.	P07332
TTB8FUC	Free fatty acid receptor 1 (GPR40)	O14842	FFAR1_HUMAN	GPCR rhodopsin	Gprotein coupled receptor 40; FFAR1	FFAR1	"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."	.	5TZY; 5TZR; 5KW2; 4PHU	MDLPPQLSFGLYVAAFALGFPLNVLAIRGATAHARLRLTPSLVYALNLGCSDLLLTVSLPLKAVEALASGAWPLPASLCPVFAVAHFFPLYAGGGFLAALSAGRYLGAAFPLGYQAFRRPCYSWGVCAAIWALVLCHLGLVFGLEAPGGWLDHSNTSLGINTPVNGSPVCLEAWDPASAGPARFSLSLLLFFLPLAITAFCYVGCLRALARSGLTHRRKLRAAWVAGGALLTLLLCVGPYNASNVASFLYPNLGGSWRKLGLITGAWSVVLNPLVTGYLGRGPGLKTVCAARTQGGKSQK	Clinical trial	"A novel antidiabetic drug, fasiglifam/TAK-875, acts as an ago-allosteric modulator of FFAR1. PLoS One. 2013 Oct 10;8(10):e76280."	25	.	.	.	.	.	.	.	.	.	.	hsa04911:Insulin secretion	R-HSA-416476:G alpha (q) signalling events; R-HSA-434316:Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion	.	O14842
TT0FYAN	Free fatty acid receptor 2 (FFAR2)	O15552	FFAR2_HUMAN	GPCR rhodopsin	Gprotein coupled receptor 43; FFAR2	FFAR2	"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)."	.	.	MLPDWKSSLILMAYIIIFLTGLPANLLALRAFVGRIRQPQPAPVHILLLSLTLADLLLLLLLPFKIIEAASNFRWYLPKVVCALTSFGFYSSIYCSTWLLAGISIERYLGVAFPVQYKLSRRPLYGVIAALVAWVMSFGHCTIVIIVQYLNTTEQVRSGNEITCYENFTDNQLDVVLPVRLELCLVLFFIPMAVTIFCYWRFVWIMLSQPLVGAQRRRRAVGLAVVTLLNFLVCFGPYNVSHLVGYHQRKSPWWRSIAVVFSSLNASLDPLLFYFSSSVVRRAFGRGLQVLRNQGSSLLGRRGKDTAEGTNEDRGVGQGEGMPSSDFTTE	Clinical trial	Discovery and optimization of an azetidine chemical series as a free fatty acid receptor 2 (FFA2) antagonist: from hit to clinic. J Med Chem. 2014 Dec 11;57(23):10044-57.	21	.	.	.	.	.	.	.	.	.	.	hsa04024:cAMP signaling pathway	R-HSA-416476:G alpha (q) signalling events	.	O15552
TTXDOHN	Free fatty acid receptor 3 (FFAR3)	O14843	FFAR3_HUMAN	GPCR rhodopsin	GPR41; G-protein coupled receptor 41	FFAR3	"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."	.	.	MDTGPDQSYFSGNHWFVFSVYLLTFLVGLPLNLLALVVFVGKLQRRPVAVDVLLLNLTASDLLLLLFLPFRMVEAANGMHWPLPFILCPLSGFIFFTTIYLTALFLAAVSIERFLSVAHPLWYKTRPRLGQAGLVSVACWLLASAHCSVVYVIEFSGDISHSQGTNGTCYLEFRKDQLAILLPVRLEMAVVLFVVPLIITSYCYSRLVWILGRGGSHRRQRRVAGLLAATLLNFLVCFGPYNVSHVVGYICGESPAWRIYVTLLSTLNSCVDPFVYYFSSSGFQADFHELLRRLCGLWGQWQQESSMELKEQKGGEEQRADRPAERKTSEHSQGCGTGGQVACAES	Literature-reported	Short-chain fatty acids stimulate leptin production in adipocytes through the G protein-coupled receptor GPR41. Proc Natl Acad Sci U S A. 2004 Jan 27;101(4):1045-50.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-416476: G alpha (q) signalling events; R-HSA-444209: Free fatty acid receptors	.	O14843
TT08JVB	G-protein coupled receptor 120 (GPR120)	Q5NUL3	FFAR4_HUMAN	GPCR rhodopsin	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	FFAR4	"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)."	.	.	MSPECARAAGDAPLRSLEQANRTRFPFFSDVKGDHRLVLAAVETTVLVLIFAVSLLGNVCALVLVARRRRRGATACLVLNLFCADLLFISAIPLVLAVRWTEAWLLGPVACHLLFYVMTLSGSVTILTLAAVSLERMVCIVHLQRGVRGPGRRARAVLLALIWGYSAVAALPLCVFFRVVPQRLPGADQEISICTLIWPTIPGEISWDVSFVTLNFLVPGLVIVISYSKILQITKASRKRLTVSLAYSESHQIRVSQQDFRLFRTLFLLMVSFFIMWSPIIITILLILIQNFKQDLVIWPSLFFWVVAFTFANSALNPILYNMTLCRNEWKKIFCCFWFPEKGAILTDTSVKRNDLSIISG	Literature-reported	PPAR ligands and their therapeutic applications: a patent review (2008 - 2014).Expert Opin Ther Pat. 2015 Feb;25(2):175-91.	15.5	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	.	"R-HSA-381771: Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1); R-HSA-416476: G alpha (q) signalling events; R-HSA-444209: Free fatty acid receptors"	.	Q5NUL3
TTWODQF	Fibrin (FG)	P02671 (20-35); P02675 (31-44)	FIBA_HUMAN; FIBB_HUMAN	.	Fibrinogen (31-44)	FGA	"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."	.	.	MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTWNPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNVSPGTRREYHTEKLVTSKGDKELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTKEVVTSEDGSDCPEAMDLGTLSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEFVSETESRGSESGIFTNTKESSSHHPGIAEFPSRGKSSSYSKQFTSSTSYNRGDSTFESKSYKMADEAGSEADHEGTHSTKRGHAKSRPVRDCDDVLQTHPSGTQSGIFNIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQRGSVLRVELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSHNNMQFSTFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENGVVWVSFRGADYSLRAVRMKIRPLVTQ	Successful	Pancreaticojejunostomy using a fibrin adhesive sealant (TachoComb) for the prevention of pancreatic fistula after pancreaticoduodenectomy. Hepatogastroenterology. 2011 Jan-Feb;58(105):187-91.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	P02671
TTMY81X	Heparin-binding growth factor 1 (FGF1)	P05230	FGF1_HUMAN	Growth factor	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	FGF1	"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."	.	4YOL; 4XKI; 4QO3; 4QC4; 4QBV	MAEGEITTFTALTEKFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD	Clinical trial	"Clinical pipeline report, company report or official report of CVBT."	21	Growth factor	Growth factor	heparin-binding growth factors family.	.	.	Fibroblast growth factor	PF00167	PF00167; FGF	.	.	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	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	.	P05230
TTNPEFX	Fibroblast growth factor-10 (FGF10)	O15520	FGF10_HUMAN	Growth factor	Fibroblast growth factor 10; FGF10	FGF10	"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."	.	1NUN	MWKWILTHCASAFPHLPGCCCCCFLLLFLVSSVPVTCQALGQDMVSPEATNSSSSSFSSPSSAGRHVRSYNHLQGDVRWRKLFSFTKYFLKIEKNGKVSGTKKENCPYSILEITSVEIGVVAVKAINSNYYLAMNKKGKLYGSKEFNNDCKLKERIEENGYNTYASFNWQHNGRQMYVALNGKGAPRRGQKTRRKNTSAHFLPMVVHS	Discontinued	"Repifermin (keratinocyte growth factor-2) for the treatment of active ulcerative colitis: a randomized, double-blind, placebo-controlled, dose-escalation trial. Aliment Pharmacol Ther. 2003 Jun 1;17(11):1355-64."	5	.	.	.	.	.	.	.	.	.	.	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	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	.	O15520
TTKJX1V	Fibroblast growth factor-14 (FGF14)	Q92915	FGF14_HUMAN	Growth factor	Fibroblast growth factor homologous factor 4; Fibroblast growth factor 14; FHF4; FGF14	FGF14	Probably involved in nervous system development and function.	.	.	MAAAIASGLIRQKRQAREQHWDRPSASRRRSSPSKNRGLCNGNLVDIFSKVRIFGLKKRRLRRQDPQLKGIVTRLYCRQGYYLQMHPDGALDGTKDDSTNSTLFNLIPVGLRVVAIQGVKTGLYIAMNGEGYLYPSELFTPECKFKESVFENYYVIYSSMLYRQQESGRAWFLGLNKEGQAMKGNRVKKTKPAAHFLPKPLEVAMYREPSLHDVGETVPKPGVTPSKSTSASAIMNGGKPVNKSKTT	Literature-reported	Fibroblast Growth Factor 14 Modulates the Neurogenesis of Granule Neurons in the Adult Dentate Gyrus. Mol Neurobiol. 2016 Dec;53(10):7254-7270.	.	.	.	.	.	.	.	.	.	.	.	hsa05017: Spinocerebellar ataxia	R-HSA-5576892: Phase 0 - rapid depolarisation	.	Q92915
TT6ICRA	Fibroblast growth factor-18 (FGF18)	O76093	FGF18_HUMAN	Growth factor	zFGF5; Fibroblast growth factor 18; FGF18	FGF18	"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."	.	4CJM	MYSAPSACTCLCLHFLLLCFQVQVLVAEENVDFRIHVENQTRARDDVSRKQLRLYQLYSRTSGKHIQVLGRRISARGEDGDKYAQLLVETDTFGSQVRIKGKETEFYLCMNRKGKLVGKPDGTSKECVFIEKVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKRYPKGQPELQKPFKYTTVTKRSRRIRPTHPA	Clinical trial	"Intraarticular sprifermin (recombinant human fibroblast growth factor 18) in knee osteoarthritis: a randomized, double-blind, placebo-controlled trial. Arthritis Rheumatol. 2014 Jul;66(7):1820-31."	21	.	.	.	.	.	.	.	.	.	.	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	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	.	O76093
TTGCH11	Fibroblast growth factor 19 (FGF19)	O95750	FGF19_HUMAN	Heparin-binding growth factors family	FGF-19	FGF19	"Involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression, following positive regulation of the JNK and ERK1/2 cascades. Stimulates glucose uptake in adipocytes. Activity requires the presence of KLB and FGFR4. {ECO:0000269|PubMed:12815072, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:19085950}."	.	1PWA;2P23;6KTR;6NFJ	MRSGCVVVHVWILAGLWLAVAGRPLAFSDAGPHVHYGWGDPIRLRHLYTSGPHGLSSCFLRIRADGVVDCARGQSAHSLLEIKAVALRTVAIKGVHSVRYLCMGADGKMQGLLQYSEEDCAFEEEIRPDGYNVYRSEKHRLPVSLSSAKQRQLYKNRGFLPLSHFLPMLPMVPEEPEDLRGHLESDMFSSPLETDSMDPFGLVTGLEAVRSPSFEK	Clinical trial	"Efficacy and Safety of Aldafermin, an Engineered FGF19 Analog, in a Randomized, Double-Blind, Placebo-Controlled Trial of Patients With Nonalcoholic Steatohepatitis. Gastroenterology. 2021 Jan;160(1):219-231.e1."	.	.	.	.	.	.	.	.	.	.	.	hsa:9965	R-HSA-109704;R-HSA-1257604;R-HSA-1307965;R-HSA-190322;R-HSA-2219530;R-HSA-5654228;R-HSA-5654712;R-HSA-5654719;R-HSA-5654720;R-HSA-5654733;R-HSA-5673001;R-HSA-6811558;	.	O95750;
TTGKIED	Fibroblast growth factor-2 (FGF2)	P09038	FGF2_HUMAN	Growth factor	bFGF; Heparin-binding growth factor 2; HBGF-2; Fibroblast growth factor 2; FGFB; FGF-2; Basic fibroblast growth factor	FGF2	"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."	.	5X1O; 4OEG; 4OEF; 4OEE; 4FGF	MVGVGGGDVEDVTPRPGGCQISGRGARGCNGIPGAAAWEAALPRRRPRRHPSVNPRSRAAGSPRTRGRRTEERPSGSRLGDRGRGRALPGGRLGGRGRGRAPERVGGRGRGRGTAAPRAAPAARGSRPGPAGTMAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS	Successful	Assessment of sucralfate coating by sequential scintigraphic imaging in radiation-induced esophageal lesions. Gastrointest Endosc. 1995 Feb;41(2):109-14.	34	Growth factor	Growth factor	heparin-binding growth factors family.	.	.	Fibroblast growth factor	PF00167	PF00167; FGF	1.A.108.1.1	The Fibroblast Growth Factor 2 (FGF2) Family	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	"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"	.	P09038
TTQ916P	Fibroblast growth factor-21 (FGF21)	Q9NSA1	FGF21_HUMAN	Growth factor	UNQ3115/PRO10196; Fibroblast growth factor 21; FGF-21	FGF21	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).	.	5VAQ	MDSDETGFEHSGLWVSVLAGLLLGACQAHPIPDSSPLLQFGGQVRQRYLYTDDAQQTEAHLEIREDGTVGGAADQSPESLLQLKALKPGVIQILGVKTSRFLCQRPDGALYGSLHFDPEACSFRELLLEDGYNVYQSEAHGLPLHLPGNKSPHRDPAPRGPARFLPLPGLPPALPEPPGILAPQPPDVGSSDPLSMVGPSQGRSPSYAS	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	Growth factor	Growth factor	heparin-binding growth factors family.	.	.	Fibroblast growth factor	PF00167	PF00167; FGF	.	.	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	R-HSA-428790:Facilitative Na+-independent glucose transporters; R-HSA-70153:Glucose transport	.	Q9NSA1
TT2IZ4K	Fibroblast growth factor-23 (FGF23)	Q9GZV9	FGF23_HUMAN	Growth factor	Tumor-derived hypophosphatemia-inducing factor; Phosphatonin; HYPF; Fibroblast growth factor 23; FGF-23	FGF23	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.	.	5W21; 2P39	MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARNSYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPGMNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRARMTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRPFAKFI	Successful	2018 FDA drug approvals.Nat Rev Drug Discov. 2019 Feb;18(2):85-89. 	34	.	.	.	.	.	.	.	.	.	.	"hsa04010: MAPK signaling pathway; hsa04014: Ras signaling pathway; hsa04015: Rap1 signaling pathway; hsa04020: Calcium signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04810: Regulation of actin cytoskeleton; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa05200: Pathways in cancer; hsa05218: Melanoma; hsa05224: Breast cancer; hsa05226: Gastric cancer"	"R-HSA-109704: PI3K Cascade; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1839122: Signaling by activated point mutants of FGFR1; R-HSA-1839130: Signaling by activated point mutants of FGFR3; R-HSA-190322: FGFR4 ligand binding and activation; R-HSA-190372: FGFR3c ligand binding and activation; R-HSA-190373: FGFR1c ligand binding and activation; R-HSA-190374: FGFR1c and Klotho ligand binding and activation; R-HSA-190375: FGFR2c ligand binding and activation; R-HSA-2033519: Activated point mutants of FGFR2; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-5654219: Phospholipase C-mediated cascade: FGFR1; R-HSA-5654221: Phospholipase C-mediated cascade, FGFR2; R-HSA-5654227: Phospholipase C-mediated cascade, FGFR3; R-HSA-5654228: Phospholipase C-mediated cascade, FGFR4; R-HSA-5654687: Downstream signaling of activated FGFR1; 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-5655253: Signaling by FGFR2 in disease; R-HSA-5655302: Signaling by FGFR1 in disease; R-HSA-5655332: Signaling by FGFR3 in disease; R-HSA-5658623: FGFRL1 modulation of FGFR1 signaling; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-8957275: Post-translational protein phosphorylation"	.	Q9GZV9
TTCEKVZ	Fibroblast growth factor-4 (FGF4)	P08620	FGF4_HUMAN	Heparin-binding growth factors family	Transforming protein KS3; Heparinbinding growth factor 4; Heparin secretorytransforming protein 1; HST1; HST; HBGF4; Fibroblast growth factor 4; FGF4	FGF4	"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."	.	1IJT	MSGPGTAAVALLPAVLLALLAPWAGRGGAAAPTAPNGTLEAELERRWESLVALSLARLPVAAQPKEAAVQSGAGDYLLGIKRLRRLYCNVGIGFHLQALPDGRIGGAHADTRDSLLELSPVERGVVSIFGVASRFFVAMSSKGKLYGSPFFTDECTFKEILLPNNYNAYESYKYPGMFIALSKNGKTKKGNRVSPTMKVTHFLPRL	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	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	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	.	P08620
TTFY134	Keratinocyte growth factor (FGF7)	P21781	FGF7_HUMAN	Growth factor	KGF; Heparin-binding growth factor 7; HBGF-7; Fibroblast growth factor 7; FGF-7	FGF7	"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."	.	.	MHKWILTWILPTLLYRSCFHIICLVGTISLACNDMTPEQMATNVNCSSPERHTRSYDYMEGGDIRVRRLFCRTQWYLRIDKRGKVKGTQEMKNNYNIMEIRTVAVGIVAIKGVESEFYLAMNKEGKLYAKKECNEDCNFKELILENHYNTYASAKWTHNGGEMFVALNQKGIPVRGKKTKKEQKTAHFLPMAIT	Clinical trial	Keratinocyte growth factor.Cell Biol Int.1995 May;19(5):399-411.	17	Growth factor	.	heparin-binding growth factors family.	.	.	Fibroblast growth factor	PF00167	PF00167; FGF	.	.	hsa04010: MAPK signaling pathway; hsa04014: Ras signaling pathway; hsa04015: Rap1 signaling pathway; hsa04020: Calcium signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04810: Regulation of actin cytoskeleton; hsa05200: Pathways in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05218: Melanoma; hsa05224: Breast cancer; hsa05226: Gastric cancer	"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-5654221: Phospholipase C-mediated cascade, FGFR2; R-HSA-5654695: PI-3K cascade:FGFR2; R-HSA-5654699: SHC-mediated cascade:FGFR2; R-HSA-5654700: FRS-mediated FGFR2 signaling; R-HSA-5654727: Negative regulation of FGFR2 signaling; R-HSA-5655253: Signaling by FGFR2 in disease; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling"	.	P21781
TTIUF3J	Fibroblast growth factor-8 (FGF8)	P55075	FGF8_HUMAN	Growth factor	Heparin-binding growth factor 8; HBGF-8; Fibroblast growth factor 8; FGF-8; Androgen-induced growth factor; AIGF	FGF8	"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."	.	2FDB	MGSPRSALSCLLLHLLVLCLQAQEGPGRGPALGRELASLFRAGREPQGVSQQHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKKGKLIAKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPRGHHTTEQSLRFEFLNYPPFTRSLRGSQRTWAPEPR	Literature-reported	Biomarkers for eosinophilic esophagitis: a review. Ann Allergy Asthma Immunol. 2012 Sep;109(3):155-9. 	.	Growth factor	Growth factor	heparin-binding growth factors family.	.	.	Fibroblast growth factor	PF00167	PF00167; FGF	.	.	hsa04010: MAPK signaling pathway; hsa04014: Ras signaling pathway; hsa04015: Rap1 signaling pathway; hsa04020: Calcium signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04810: Regulation of actin cytoskeleton; hsa05200: Pathways in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05218: Melanoma; hsa05224: Breast cancer; hsa05226: Gastric cancer	"R-HSA-109704: PI3K Cascade; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1839122: Signaling by activated point mutants of FGFR1; R-HSA-1839130: Signaling by activated point mutants of FGFR3; R-HSA-190322: FGFR4 ligand binding and activation; R-HSA-190371: FGFR3b ligand binding and activation; R-HSA-190372: FGFR3c ligand binding and activation; R-HSA-190373: FGFR1c ligand binding and activation; R-HSA-190375: FGFR2c 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, FGFR2; R-HSA-5654227: Phospholipase C-mediated cascade, FGFR3; R-HSA-5654228: Phospholipase C-mediated cascade, FGFR4; R-HSA-5654687: Downstream signaling of activated FGFR1; 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-5655253: Signaling by FGFR2 in disease; R-HSA-5655302: Signaling by FGFR1 in disease; R-HSA-5655332: Signaling by FGFR3 in disease; R-HSA-5658623: FGFRL1 modulation of FGFR1 signaling; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling"	.	P55075
TTV1YFT	Heparin binding protein (FGFBP1)	Q14512	FGFP1_HUMAN	Fibroblast growth factor-binding	HBp17; HBP17 heparin-binding and FGF-binding protein; Fibroblast growth factor binding protein 1; FGFBP1; FGF-binding protein HBp17; FGF-BP	FGFBP1	"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."	.	.	MKICSLTLLSFLLLAAQVLLVEGKKKVKNGLHSKVVSEQKDTLGNTQIKQKSRPGNKGKFVTKDQANCRWAATEQEEGISLKVECTQLDHEFSCVFAGNPTSCLKLKDERVYWKQVARNLRSQKDICRYSKTAVKTRVCRKDFPESSLKLVSSTLFGNTKPRKEKTEMSPREHIKGKETTPSSLAVTQTMATKAPECVEDPDMANQRKTALEFCGETWSSLCTFFLSIVQDTSC	Literature-reported	Ribozyme-targeting of a secreted FGF-binding protein (FGF-BP) inhibits proliferation of prostate cancer cells in vitro and in vivo. Oncogene. 2002 Aug 22;21(37):5733-42.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-190377: FGFR2b ligand binding and activation	.	Q14512
TTRLW2X	Fibroblast growth factor receptor 1 (FGFR1)	P11362	FGFR1_HUMAN	Kinase	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	FGFR1	"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."	EC 2.7.10.1	6MZW; 6MZQ; 6C1O; 6C1C; 6C1B	MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPAQLANGGLKRR	Successful	Anthranilic acid amides: a novel class of antiangiogenic VEGF receptor kinase inhibitors. J Med Chem. 2002 Dec 19;45(26):5687-93.	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.	2.7.10.1 	Transferring phosphorus-containing groups	Fibroblast growth factor receptor 3 transmembrane domain; Immunoglobulin I-set domain; Immunoglobulin domain; Protein tyrosine kinase	PF18123; PF07679; PF00047; PF07714	PF18123; FGFR3_TM; PF07679; I-set; PF00047; ig; PF07714; Pkinase_Tyr	8.A.23.1.7	The Basigin (Basigin) Family	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	"R-HSA-109704: PI3K Cascade; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1839120: Signaling by FGFR1 amplification mutants; R-HSA-1839122: Signaling by activated point mutants of FGFR1; R-HSA-190370: FGFR1b ligand binding and activation; R-HSA-190373: FGFR1c ligand binding and activation; R-HSA-190374: FGFR1c and Klotho ligand binding and activation; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-375165: NCAM signaling for neurite out-growth; R-HSA-445144: Signal transduction by L1; R-HSA-5654219: Phospholipase C-mediated cascade: FGFR1; R-HSA-5654687: Downstream signaling of activated FGFR1; R-HSA-5654688: SHC-mediated cascade:FGFR1; R-HSA-5654689: PI-3K cascade:FGFR1; R-HSA-5654693: FRS-mediated FGFR1 signaling; R-HSA-5654726: Negative regulation of FGFR1 signaling; R-HSA-5655302: Signaling by FGFR1 in disease; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-8853336: Signaling by plasma membrane FGFR1 fusions"	.	P11362
TTGJVQM	Fibroblast growth factor receptor 2 (FGFR2)	P21802	FGFR2_HUMAN	Kinase	Keratinocyte growth factor receptor 2; Keratinocyte growth factor receptor; KSAM; KGFR; K-sam; FGFR-2; FGF-2 receptor; CD332; BEK	FGFR2	"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."	EC 2.7.10.1	5UI0; 5UHN; 5UGX; 5UGL; 5EG3	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT	Successful	Keratinocyte growth factor. Expert Opin Biol Ther. 2009 Jun;9(6):779-87.	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.	2.7.10.1 	Transferring phosphorus-containing groups	Fibroblast growth factor receptor 3 transmembrane domain; Immunoglobulin I-set domain; Protein tyrosine kinase	PF18123; PF07679; PF07714	PF18123; FGFR3_TM; PF07679; I-set; PF07714; Pkinase_Tyr	.	.	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	R-HSA-2033519:Activated point mutants of FGFR2	.	P21802
TTST7KB	Fibroblast growth factor receptor 3 (FGFR3)	P22607	FGFR3_HUMAN	Kinase	JTK4; FGFR-3; CD333	FGFR3	"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."	EC 2.7.10.1	4K33; 2LZL; 1RY7	MGAPACALALCVAVAIVAGASSESLGTEQRVVGRAAEVPGPEPGQQEQLVFGSGDAVELSCPPPGGGPMGPTVWVKDGTGLVPSERVLVGPQRLQVLNASHEDSGAYSCRQRLTQRVLCHFSVRVTDAPSSGDDEDGEDEAEDTGVDTGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKTAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHSAWLVVLPAEEELVEADEAGSVYAGILSYGVGFFLFILVVAAVTLCRLRSPPKKGLGSPTVHKISRFPLKRQVSLESNASMSSNTPLVRIARLSSGEGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQDTPSSSSSGDDSVFAHDLLPPAPPSSGGSRT	Successful	Emerging therapies for multiple myeloma. Expert Opin Emerg Drugs. 2009 Mar;14(1):99-127.	31	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Fibroblast growth factor receptor 3 transmembrane domain; Immunoglobulin I-set domain; Protein tyrosine kinase	PF18123; PF07679; PF07714	PF18123; FGFR3_TM; PF07679; I-set; PF07714; Pkinase_Tyr	.	.	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	R-HSA-2033514:FGFR3 mutant receptor activation	.	P22607
TTFPD8J	Fusion protein FGFR3-TACC3 (FGFR3-TACC3)	P22607-Q9Y6A5	FGFR3_HUMAN-TACC3_HUMAN	.	FGFR3-TACC3 gene fusion; FGFR3-TACC3	FGFR3-TACC3	An oncogenic function in respiratory epithelium.	.	.	MSLQVLNDKNVSNEKNTENCDFLFSPPEVTGRSSVLRVSQKENVPPKNLAKAMKVTFQTPLRDPQTHRILSPSMASKLEAPFTQDDTLGLENSHPVWTQKENQQLIKEVDAKTTHGILQKPVEADTDLLGDASPAFGSGSSSESGPGALADLDCSSSSQSPGSSENQMVSPGKVSGSPEQAVEENLSSYSLDRRVTPASETLEDPCRTESQHKAETPHGAEEECKAETPHGAEEECRHGGVCAPAAVATSPPGAIPKEACGGAPLQGLPGEALGCPAGVGTPVPADGTQTLTCAHTSAPESTAPTNHLVAGRAMTLSPQEEVAAGQMASSSRSGPVKLEFDVSDGATSKRAPPPRRLGERSGLKPPLRKAAVRQQKAPQEVEEDDGRSGAGEDPPMPASRGSYHLDWDKMDDPNFIPFGGDTKSGCSEAQPPESPETRLGQPAAEQLHAGPATEEPGPCLSQQLHSASAEDTPVVQLAAETPTAESKERALNSASTSLPTSCPGSEPVPTHQQGQPALELKEESFRDPAEVLGTGAEVDYLEQFGTSSFKESALRKQSLYLKFDPLLRDSPGRPVPVATETSSMHGANETPSGRPREAKLVEFDFLGALDIPVPGPPPGVPAPGGPPLSTGPIVDLLQYSQKDLDAVVKATQEENRELRSRCEELHGKNLELGKIMDRFEEVVYQAMEEVQKQKELSKAEIQKVLKEKDQLTTDLNSMEKSFSDLFKRFEKQKEVIEGYRKNEESLKKCVEDYLARITQEGQRYQALKAHAEEKLQLANEEIAQVRSKAQAEALALQASLRKEQMRIQSLEKTVEQKTKENEELTRICDDLISKMEKIMGAPACALALCVAVAIVAGASSESLGTEQRVVGRAAEVPGPEPGQQEQLVFGSGDAVELSCPPPGGGPMGPTVWVKDGTGLVPSERVLVGPQRLQVLNASHEDSGAYSCRQRLTQRVLCHFSVRVTDAPSSGDDEDGEDEAEDTGVDTGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKTAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHSAWLVVLPAEEELVEADEAGSVYAGILSYGVGFFLFILVVAAVTLCRLRSPPKKGLGSPTVHKISRFPLKRQVSLESNASMSSNTPLVRIARLSSGEGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQDTPSSSSSGDDSVFAHDLLPPAPPSSGGSRT	Clinical trial	Recurrent FGFR3-TACC3 fusion gene in nasopharyngeal carcinoma.Cancer Biol Ther. 2014;15(12):1613-21.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	P22607
TT1KX2S	FGFR4 messenger RNA (FGFR4 mRNA)	P22455	FGFR4_HUMAN	mRNA target	TKF (mRNA); JTK2 (mRNA); FGFR-4 (mRNA); CD334 (mRNA)	FGFR4	"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."	EC 2.7.10.1	6JPJ; 5XFJ; 5XFF; 5NWZ; 5NUD	MRLLLALLGVLLSVPGPPVLSLEASEEVELEPCLAPSLEQQEQELTVALGQPVRLCCGRAERGGHWYKEGSRLAPAGRVRGWRGRLEIASFLPEDAGRYLCLARGSMIVLQNLTLITGDSLTSSNDDEDPKSHRDPSNRHSYPQQAPYWTHPQRMEKKLHAVPAGNTVKFRCPAAGNPTPTIRWLKDGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENAVGSIRYNYLLDVLERSPHRPILQAGLPANTTAVVGSDVELLCKVYSDAQPHIQWLKHIVINGSSFGADGFPYVQVLKTADINSSEVEVLYLRNVSAEDAGEYTCLAGNSIGLSYQSAWLTVLPEEDPTWTAAAPEARYTDIILYASGSLALAVLLLLAGLYRGQALHGRHPRPPATVQKLSRFPLARQFSLESGSSGKSSSSLVRGVRLSSSGPALLAGLVSLDLPLDPLWEFPRDRLVLGKPLGEGCFGQVVRAEAFGMDPARPDQASTVAVKMLKDNASDKDLADLVSEMEVMKLIGRHKNIINLLGVCTQEGPLYVIVECAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPVLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDNVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMDRPPHCPPELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEYLDLRLTFGPYSPSGGDASSTCSSSDSVFSHDPLPLGSSSFPFGSGVQT	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	19	mRNA	mRNA target	.	.	.	Immunoglobulin I-set domain; Protein tyrosine kinase	PF07679; PF07714	PF07679; I-set; PF07714; Pkinase_Tyr	.	.	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	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	.	P22455
TT5BR7T	Fibroblast growth factor receptor 4 (FGFR4)	P22455	FGFR4_HUMAN	Kinase	TKF; JTK2; FGFR-4; CD334	FGFR4	"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."	EC 2.7.10.1	6JPJ; 5XFJ; 5XFF; 5NWZ; 5NUD	MRLLLALLGVLLSVPGPPVLSLEASEEVELEPCLAPSLEQQEQELTVALGQPVRLCCGRAERGGHWYKEGSRLAPAGRVRGWRGRLEIASFLPEDAGRYLCLARGSMIVLQNLTLITGDSLTSSNDDEDPKSHRDPSNRHSYPQQAPYWTHPQRMEKKLHAVPAGNTVKFRCPAAGNPTPTIRWLKDGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENAVGSIRYNYLLDVLERSPHRPILQAGLPANTTAVVGSDVELLCKVYSDAQPHIQWLKHIVINGSSFGADGFPYVQVLKTADINSSEVEVLYLRNVSAEDAGEYTCLAGNSIGLSYQSAWLTVLPEEDPTWTAAAPEARYTDIILYASGSLALAVLLLLAGLYRGQALHGRHPRPPATVQKLSRFPLARQFSLESGSSGKSSSSLVRGVRLSSSGPALLAGLVSLDLPLDPLWEFPRDRLVLGKPLGEGCFGQVVRAEAFGMDPARPDQASTVAVKMLKDNASDKDLADLVSEMEVMKLIGRHKNIINLLGVCTQEGPLYVIVECAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPVLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDNVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMDRPPHCPPELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEYLDLRLTFGPYSPSGGDASSTCSSSDSVFSHDPLPLGSSSFPFGSGVQT	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1811).	21	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Immunoglobulin I-set domain; Protein tyrosine kinase	PF07679; PF07714	PF07679; I-set; PF07714; Pkinase_Tyr	8.A.23.1.9	The Basigin (Basigin) Family	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	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	.	P22455
TTR31L7	Fibrinogen (FGG)	P02679	FIBG_HUMAN	Fibrinogen protein	PRO2061; Fibrinogen gamma chain	FGG	"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."	.	4B60; 3HUS; 3H32; 3GHG; 3FIB	MSWSLHPRNLILYFYALLFLSSTCVAYVATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTIGEGQQHHLGGAKQVRPEHPAETEYDSLYPEDDL	Literature-reported	FGG promotes migration and invasion in hepatocellular carcinoma cells through activating epithelial to mesenchymal transition. Cancer Manag Res. 2019 Feb 19;11:1653-1665.	.	Fibrinogen	Fibrinogen	.	.	.	"Fibrinogen alpha/beta chain family; Fibrinogen beta and gamma chains, C-terminal globular domain"	PF08702; PF00147	PF08702; Fib_alpha; PF00147; Fibrinogen_C	.	.	hsa04610: Complement and coagulation cascades; hsa04611: Platelet activation; hsa04613: Neutrophil extracellular trap formation; hsa05150: Staphylococcus aureus infection; hsa05171: Coronavirus disease - COVID-19	R-HSA-114608: Platelet degranulation; R-HSA-1236974: ER-Phagosome pathway; R-HSA-140875: Common Pathway of Fibrin Clot Formation; R-HSA-166058: MyD88:MAL(TIRAP) cascade initiated on plasma membrane; R-HSA-216083: Integrin cell surface interactions; R-HSA-354192: Integrin 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-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-5602498: MyD88 deficiency (TLR2/4); R-HSA-5603041: IRAK4 deficiency (TLR2/4); R-HSA-5674135: MAP2K and MAPK activation; R-HSA-5686938: Regulation of TLR by endogenous ligand; R-HSA-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-8957275: Post-translational protein phosphorylation; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants	.	P02679
TTYBS89	Fibroleukin (FGL2)	Q14314	FGL2_HUMAN	Fibrinogen	PT49; Hfgl2; Fibrinogen-like protein 2; FGL2	FGL2	May play a role in physiologic lymphocyte functions at mucosal sites.	.	.	MKLANWYWLSSAVLATYGFLVVANNETEEIKDERAKDVCPVRLESRGKCEEAGECPYQVSLPPLTIQLPKQFSRIEEVFKEVQNLKEIVNSLKKSCQDCKLQADDNGDPGRNGLLLPSTGAPGEVGDNRVRELESEVNKLSSELKNAKEEINVLHGRLEKLNLVNMNNIENYVDSKVANLTFVVNSLDGKCSKCPSQEQIQSRPVQHLIYKDCSDYYAIGKRSSETYRVTPDPKNSSFEVYCDMETMGGGWTVLQARLDGSTNFTRTWQDYKAGFGNLRREFWLGNDKIHLLTKSKEMILRIDLEDFNGVELYALYDQFYVANEFLKYRLHVGNYNGTAGDALRFNKHYNHDLKFFTTPDKDNDRYPSGNCGLYYSSGWWFDACLSANLNGKYYHQKYRGVRNGIFWGTWPGVSEAHPGGYKSSFKEAKMMIRPKHFKP	Literature-reported	Expression of human fibrinogen-like protein 2/fibroleukin in renal acute allograft rejection and its potential clinical implication. Zhonghua Yi Xue Za Zhi. 2004 Mar 17;84(6):474-7.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-6798695: Neutrophil degranulation	.	Q14314
TTPOGS1	Tyrosine-protein kinase Fgr (FGR)	P09769	FGR_HUMAN	Kinase	p58c-Fgr; p58-Fgr; p55-Fgr; SRC2; Proto-oncogene c-Fgr; Gardner-Rasheed feline sarcoma viral (v-fgr) oncogene homolog	FGR	"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."	EC 2.7.10.2	.	MGCVFCKKLEPVATAKEDAGLEGDFRSYGAADHYGPDPTKARPASSFAHIPNYSNFSSQAINPGFLDSGTIRGVSGIGVTLFIALYDYEARTEDDLTFTKGEKFHILNNTEGDWWEARSLSSGKTGCIPSNYVAPVDSIQAEEWYFGKIGRKDAERQLLSPGNPQGAFLIRESETTKGAYSLSIRDWDQTRGDHVKHYKIRKLDMGGYYITTRVQFNSVQELVQHYMEVNDGLCNLLIAPCTIMKPQTLGLAKDAWEISRSSITLERRLGTGCFGDVWLGTWNGSTKVAVKTLKPGTMSPKAFLEEAQVMKLLRHDKLVQLYAVVSEEPIYIVTEFMCHGSLLDFLKNPEGQDLRLPQLVDMAAQVAEGMAYMERMNYIHRDLRAANILVGERLACKIADFGLARLIKDDEYNPCQGSKFPIKWTAPEAALFGRFTIKSDVWSFGILLTELITKGRIPYPGMNKREVLEQVEQGYHMPCPPGCPASLYEAMEQTWRLDPEERPTFEYLQSFLEDYFTSAEPQYQPGDQT	Literature-reported	Discovery of novel 2-(aminoheteroaryl)-thiazole-5-carboxamides as potent and orally active Src-family kinase p56(Lck) inhibitors. Bioorg Med Chem Lett. 2004 Dec 20;14(24):6061-6.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. SRC subfamily.	2.7.10.2	Transferring phosphorus-containing groups	Protein tyrosine kinase; SH2 domain; SH3 domain	PF07714; PF00017; PF00018	PF07714; Pkinase_Tyr; PF00017; SH2; PF00018; SH3_1	.	.	hsa04062: Chemokine signaling pathway	R-HSA-2029481: FCGR activation; R-HSA-432142: Platelet sensitization by LDL; R-HSA-6798695: Neutrophil degranulation; R-HSA-9664323: FCGR3A-mediated IL10 synthesis; R-HSA-9664422: FCGR3A-mediated phagocytosis	.	P09769
TTMS54D	Fragile histidine triad protein (FHIT)	P49789	FHIT_HUMAN	Acid anhydride hydrolase	"Fragile histidinetriad protein; Fragile histidinetriad (FHIT) gene; Dinucleosidetriphosphatase; Diadenosine 5',5'''-P1,P3-triphosphate hydrolase; Bis(5'-adenosyl)-triphosphatase; AP3AASE; AP3A hydrolase"	FHIT	"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."	EC 3.6.1.29	6FIT; 5FIT; 4FIT; 3FIT; 2FIT	MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSIYEELQKHDKEDFPASWRSEEEMAAEAAALRVYFQ	Successful	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	34	EC:3.6	Acid anhydrides hydrolase	.	3.6.1.29	Acting on acid anhydrides	HIT domain	PF01230	PF01230; HIT	.	.	hsa00230: Purine metabolism; hsa01100: Metabolic pathways; hsa05222: Small cell lung cancer; hsa05223: Non-small cell lung cancer	.	.	P49789
TTI7ENL	Skeletal muscle LIM-protein 1 (FHL1)	Q13642	FHL1_HUMAN	.	Skeletal muscle LIMprotein 1; SLIM1; SLIM; Four and a half LIM domains protein 1; FHL1	FHL1	May have an involvement in muscle development or hypertrophy.	.	2EGQ; 2CUR; 2CUP; 1X63	MAEKFDCHYCRDPLQGKKYVQKDGHHCCLKCFDKFCANTCVECRKPIGADSKEVHYKNRFWHDTCFRCAKCLHPLANETFVAKDNKILCNKCTTREDSPKCKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGEDFYCVTCHETKFAKHCVKCNKAITSGGITYQDQPWHADCFVCVTCSKKLAGQRFTAVEDQYYCVDCYKNFVAKKCAGCKNPITGKRTVSRVSHPVSKARKPPVCHGKRLPLTLFPSANLRGRHPGGERTCPSWVVVLYRKNRSLAAPRGPGLVKAPVWWPMKDNPGTTTASTAKNAP	Literature-reported	Epigenetic analysis of FHL1 tumor suppressor gene in human liver cancer. Oncol Lett. 2017 Nov;14(5):6109-6116.	.	.	.	.	.	.	.	.	.	.	.	hsa04630: JAK-STAT signaling pathway	.	.	Q13642
TT4P8O2	HUMAN FK506 binding protein 10 (FKBP10)	Q96AY3	FKB10_HUMAN	.	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	FKBP10	"Human protein FK506 binding protein 10 interacts with SARS-CoV-2 Orf8 protein with high significance, which indicates FKBP10 as a potential therapeutic target."	EC 5.2.1.8	.	MFPAGPPSHSLLRLPLLQLLLLVVQAVGRGLGRASPAGGPLEDVVIERYHIPRACPREVQMGDFVRYHYNGTFEDGKKFDSSYDRNTLVAIVVGVGRLITGMDRGLMGMCVNERRRLIVPPHLGYGSIGLAGLIPPDATLYFDVVLLDVWNKEDTVQVSTLLRPPHCPRMVQDGDFVRYHYNGTLLDGTSFDTSYSKGGTYDTYVGSGWLIKGMDQGLLGMCPGERRKIIIPPFLAYGEKGYGTVIPPQASLVFHVLLIDVHNPKDAVQLETLELPPGCVRRAGAGDFMRYHYNGSLMDGTLFDSSYSRNHTYNTYIGQGYIIPGMDQGLQGACMGERRRITIPPHLAYGENGTGDKIPGSAVLIFNVHVIDFHNPADVVEIRTLSRPSETCNETTKLGDFVRYHYNCSLLDGTQLFTSHDYGAPQEATLGANKVIEGLDTGLQGMCVGERRQLIVPPHLAHGESGARGVPGSAVLLFEVELVSREDGLPTGYLFVWHKDPPANLFEDMDLNKDGEVPPEEFSTFIKAQVSEGKGRLMPGQDPEKTIGDMFQNQDRNQDGKITVDELKLKSDEDEERVHEEL	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q96AY3
TT1XEQO	HUMAN FK506 binding protein 15 (FKBP15)	Q5T1M5	FKB15_HUMAN	FKBP-type PPIase family	WASP- and FKBP-like protein; WAFL; FKBP-15; FKBP-133; FK506-binding protein 15; 133 kDa FKBP; 133 kDa FK506-binding protein	FKBP15	"Human protein FK506 binding protein 15 interacts with SARS-CoV-2 Nsp2 protein with high significance, which indicates FKBP15 as a potential therapeutic target."	.	.	MFGAGDEDDTDFLSPSGGARLASLFGLDQAAAGHGNEFFQYTAPKQPKKGQGTAATGNQATPKTAPATMSTPTILVATAVHAYRYTNGQYVKQGKFGAAVLGNHTAREYRILLYISQQQPVTVARIHVNFELMVRPNNYSTFYDDQRQNWSIMFESEKAAVEFNKQVCIAKCNSTSSLDAVLSQDLIVADGPAVEVGDSLEVAYTGWLFQNHVLGQVFDSTANKDKLLRLKLGSGKVIKGWEDGMLGMKKGGKRLLIVPPACAVGSEGVIGWTQATDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAAPSPIPGADNLSADPVVSPPTSIPFKSGEPALRTKSNSLSEQLAINTSPDAVKAKLISRMAKMGQPMLPILPPQLDSNDSEIEDVNTLQGGGQPVVTPSVQPSLHPAHPALPQMTSQAPQPSVTGLQAPSAALMQVSSLDSHSAVSGNAQSFQPYAGMQAYAYPQASAVTSQLQPVRPLYPAPLSQPPHFQGSGDMASFLMTEARQHNTEIRMAVSKVADKMDHLMTKVEELQKHSAGNSMLIPSMSVTMETSMIMSNIQRIIQENERLKQEILEKSNRIEEQNDKISELIERNQRYVEQSNLMMEKRNNSLQTATENTQARVLHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQMQLTESLKETDLLRGQLTKVQAKLSELQETSEQAQSKFKSEKQNRKQLELKVTSLEEELTDLRVEKESLEKNLSERKKKSAQERSQAEEEIDEIRKSYQEELDKLRQLLKKTRVSTDQAAAEQLSLVQAELQTQWEAKCEHLLASAKDEHLQQYQEVCAQRDAYQQKLVQLQEKCLALQAQITALTKQNEQHIKELEKNKSQMSGVEAAASDPSEKVKKIMNQVFQSLRREFELEESYNGRTILGTIMNTIKMVTLQLLNQQEQEKEESSSEEEEEKAEERPRRPSQEQSASASSGQPQAPLNRERPESPMVPSEQVVEEAVPLPPQALTTSQDGHRRKGDSEAEALSEIKDGSLPPELSCIPSHRVLGPPTSIPPEPLGPVSMDSECEESLAASPMAAKPDNPSGKVCVREVAPDGPLQESSTRLSLTSDPEEGDPLALGPESPGEPQPPQLKKDDVTSSTGPHKELSSTEAGSTVAGAALRPSHHSQRSSLSGDEEDELFKGATLKALRPKAQPEEEDEDEVSMKGRPPPTPLFGDDDDDDDIDWLG	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q5T1M5
TTMW94E	FK506-binding protein 1A (FKBP1A)	P62942	FKB1A_HUMAN	Cis-trans-isomerase	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	FKBP1A	"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."	EC 5.2.1.8	5I7Q; 5I7P; 4ODR; 4ODQ; 4ODP	MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE	Successful	Neural roles of immunophilins and their ligands. Mol Neurobiol. 1997 Oct;15(2):223-39.	34	EC:5.2	Cis trans isomerase	FKBP-type PPIase family. FKBP1 subfamily.	5.2.1.8 	cis-trans-Isomerases	FKBP-type peptidyl-prolyl cis-trans isomerase	PF00254	PF00254; FKBP_C	8.A.11.1.2	The Immunophilin-like Prolyl:peptidyl Isomerase Regulator (I-PPI) Family	.	R-HSA-166208: mTORC1-mediated signalling; R-HSA-2025928: Calcineurin activates NFAT; R-HSA-2173789: TGF-beta receptor signaling activates SMADs; R-HSA-2173791: TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition); R-HSA-3656535: TGFBR1 LBD Mutants in Cancer; R-HSA-9679191: Potential therapeutics for SARS	.	P62942
TTHY0FT	FK506-binding protein 4 (FKBP4)	Q02790	FKBP4_HUMAN	Cis-trans-isomerase	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	FKBP4	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.	EC 5.2.1.8	4TW8; 4LAY; 4LAX; 4LAW; 4LAV	MTAEEMKATESGAQSAPLPMEGVDISPKQDEGVLKVIKREGTGTEMPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAIATMKVGEVCHITCKPEYAYGSAGSPPKIPPNATLVFEVELFEFKGEDLTEEEDGGIIRRIQTRGEGYAKPNEGAIVEVALEGYYKDKLFDQRELRFEIGEGENLDLPYGLERAIQRMEKGEHSIVYLKPSYAFGSVGKEKFQIPPNAELKYELHLKSFEKAKESWEMNSEEKLEQSTIVKERGTVYFKEGKYKQALLQYKKIVSWLEYESSFSNEEAQKAQALRLASHLNLAMCHLKLQAFSAAIESCNKALELDSNNEKGLFRRGEAHLAVNDFELARADFQKVLQLYPNNKAAKTQLAVCQQRIRRQLAREKKLYANMFERLAEEENKAKAEASSGDHPTDTEMKEEQKSNTAGSQSQVETEA	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	EC:5.2	Cis-trans-isomerases	.	5.2.1.8	cis-trans-Isomerases	FKBP-type peptidyl-prolyl cis-trans isomerase; Tetratricopeptide repeat; Tetratricopeptide repeat	PF00254; PF00515; PF07719	PF00254; FKBP_C; PF00515; TPR_1; PF07719; TPR_2	.	.	hsa04915: Estrogen signaling pathway	R-HSA-3371497: HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand; R-HSA-3371568: Attenuation phase; R-HSA-8939211: ESR-mediated signaling; R-HSA-9018519: Estrogen-dependent gene expression; R-HSA-9679191: Potential therapeutics for SARS	.	Q02790
TT0J5KQ	FK506-binding protein 5 (FKBP5)	Q13451	FKBP5_HUMAN	Cis-trans-isomerase	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	FKBP5	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.	EC 5.2.1.8	5OMP; 5OBK; 5NJX; 5DIV; 5DIU	MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV	Literature-reported	Biomarkers for eosinophilic esophagitis: a review. Ann Allergy Asthma Immunol. 2012 Sep;109(3):155-9. 	.	EC:5.2	Cis-trans-isomerases	.	5.2.1.8	cis-trans-Isomerases	FKBP-type peptidyl-prolyl cis-trans isomerase; Tetratricopeptide repeat; Tetratricopeptide repeat	PF00254; PF00515; PF13181	PF00254; FKBP_C; PF00515; TPR_1; PF13181; TPR_8	.	.	hsa04915: Estrogen signaling pathway	R-HSA-3371497: HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand; R-HSA-8939211: ESR-mediated signaling; R-HSA-9022699: MECP2 regulates neuronal receptors and channels	.	Q13451
TTO1ENI	HUMAN FK506 binding protein 7 (FKBP7)	Q9Y680	FKBP7_HUMAN	.	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	FKBP7	"Human protein FK506 binding protein 7 interacts with SARS-CoV-2 Orf8 protein with high significance, which indicates FKBP7 as a potential therapeutic target."	EC 5.2.1.8	.	MPKTMHFLFRFIVFFYLWGLFTAQRQKKEESTEEVKIEVLHRPENCSKTSKKGDLLNAHYDGYLAKDGSKFYCSRTQNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYAEGKIPPDATLIFEIELYAVTKGPRSIETFKQIDMDNDRQLSKAEINLYLQREFEKDEKPRDKSYQDAVLEDIFKKNDHDGDGFISPKEYNVYQHDEL	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9Y680
TTYLZ71	Flavivirus Serine protease NS2B-NS3 (FlaV NS2B-NS3)	P03314 (1355-2107)	POLG_YEFV1	.	FlavivirusNon-structural protein 2B-Non-structural protein 3; Flavivirus Flavivirin protease NS2B regulatory subunit-Flavivirin protease NS3 catalytic subunit Non-structural protein 3	FlaV NS2B-NS3	"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."	.	6IW4; 6IW2; 6IW1; 6IW0; 6EPK	SIPVNEALAAAGLVGVLAGLAFQEMENFLGPIAVGGLLMMLVSVAGRVDGLELKKLGEVSWEEEAEISGSSARYDVALSEQGEFKLLSEEKVPWDQVVMTSLALVGAALHPFALLLVLAGWLFHVRGARRSGDVLWDIPTPKIIEECEHLEDGIYGIFQSTFLGASQRGVGVAQGGVFHTMWHVTRGAFLVRNGKKLIPSWASVKEDLVAYGGSWKLEGRWDGEEEVQLIAAVPGKNVVNVQTKPSLFKVRNGGEIGAVALDYPSGTSGSPIVNRNGEVIGLYGNGILVGDNSFVSAISQTEVKEEGKEELQEIPTMLKKGMTTVLDFHPGAGKTRRFLPQILAECARRRLRTLVLAPTRVVLSEMKEAFHGLDVKFHTQAFSAHGSGREVIDAMCHATLTYRMLEPTRVVNWEVIIMDEAHFLDPASIAARGWAAHRARANESATILMTATPPGTSDEFPHSNGEIEDVQTDIPSEPWNTGHDWILADKRPTAWFLPSIRAANVMAASLRKAGKSVVVLNRKTFEREYPTIKQKKPDFILATDIAEMGANLCVERVLDCRTAFKPVLVDEGRKVAIKGPLRISASSAAQRRGRIGRNPNRDGDSYYYSEPTSENNAHHVCWLEASMLLDNMEVRGGMVAPLYGVEGTKTPVSPGEMRLRDDQRKVFRELVRNCDLPVWLSWQVAKAGLKTNDRKWCFEGPEEHEILNDSGETVKCRAPGGAKKPLRPRWCDERVSSDQSALSEFIKFAEGRR	Literature-reported	The flavivirus NS2B-NS3 protease-helicase as a target for antiviral drug development. Antiviral Res. 2015 Jun;118:148-58.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTPGLDJ	Flavivirus RNA-directed RNA polymerase NS5 (FlaV NS5)	P03314 (2507-3411)	POLG_YEFV1	.	Flavivirus Non-structural protein 5	FlaV NS5	"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."	EC 2.1.1.56	6IW4; 6IW2; 6IW1; 6IW0; 6EPK	GSANGKTLGEVWKRELNLLDKRQFELYKRTDIVEVDRDTARRHLAEGKVDTGVAVSRGTAKLRWFHERGYVKLEGRVIDLGCGRGGWCYYAAAQKEVSGVKGFTLGRDGHEKPMNVQSLGWNIITFKDKTDIHRLEPVKCDTLLCDIGESSSSSVTEGERTVRVLDTVEKWLACGVDNFCVKVLAPYMPDVLEKLELLQRRFGGTVIRNPLSRNSTHEMYYVSGARSNVTFTVNQTSRLLMRRMRRPTGKVTLEADVILPIGTRSVETDKGPLDKEAIEERVERIKSEYMTSWFYDNDNPYRTWHYCGSYVTKTSGSAASMVNGVIKILTYPWDRIEEVTRMAMTDTTPFGQQRVFKEKVDTRAKDPPAGTRKIMKVVNRWLFRHLAREKNPRLCTKEEFIAKVRSHAAIGAYLEEQEQWKTANEAVQDPKFWELVDEERKLHQQGRCRTCVYNMMGKREKKLSEFGKAKGSRAIWYMWLGARYLEFEALGFLNEDHWASRENSGGGVEGIGLQYLGYVIRDLAAMDGGGFYADDTAGWDTRITEADLDDEQEILNYMSPHHKKLAQAVMEMTYKNKVVKVLRPAPGGKAYMDVISRRDQRGSGQVVTYALNTITNLKVQLIRMAEAEMVIHHQHVQDCDESVLTRLEAWLTEHGCDRLKRMAVSGDDCVVRPIDDRFGLALSHLNAMSKVRKDISEWQPSKGWNDWENVPFCSHHFHELQLKDGRRIVVPCREQDELIGRGRVSPGNGWMIKETACLSKAYANMWSLMYFHKRDMRLLSLAVSSAVPTSWVPQGRTTWSIHGKGEWMTTEDMLEVWNRVWITNNPHMQDKTMVKKWRDVPYLTKRQDKLCGSLIGMTNRATWASHIHLVIHRIRTLIGQEKYTDYLTVMDRYSVDADLQLGELI	Literature-reported	Murine Efficacy and Pharmacokinetic Evaluation of the Flaviviral NS5 Capping Enzyme 2-Thioxothiazolidin-4-One Inhibitor BG-323. PLoS One. 2015 Jun 15;10(6):e0130083.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTSTRZY	Filamin A (FLNA)	P21333	FLNA_HUMAN	Dystrophin protein	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	FLNA	"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."	.	6EW1; 6D8C; 5XR1; 4P3W; 4M9P	MSSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKKRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLFAGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGTGEVEVVIQDPMGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNPSACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLSRTGVELGKPTHFTVNAKAAGKGKLDVQFSGLTKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVNVTYGGDPIPKSPFSVAVSPSLDLSKIKVSGLGEKVDVGKDQEFTVKSKGAGGQGKVASKIVGPSGAAVPCKVEPGLGADNSVVRFLPREEGPYEVEVTYDGVPVPGSPFPLEAVAPTKPSKVKAFGPGLQGGSAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILFADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQCYGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVEYTPYEEGLHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKVPVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGPYSISVLYGDEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAGKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTALAGDQPSVQPPLRSQQLAPQYTYAQGGQQTWAPERPLVGVNGLDVTSLRPFDLVIPFTIKKGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYVDYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDLSLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVISQSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDGTCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHCDLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGTHTVSVKYKGQHVPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPSKAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSLQESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAGALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPRLVSNHSLHETSSVFVDSLTKATCAPQHGAPGPGPADASKVVAKGLGLSKAYVGQKSSFTVDCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGSPYRVVVP	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	TC=8.A.66	Filamin family	filamin family.	.	.	Calponin homology (CH) domain; Filamin/ABP280 repeat	PF00307; PF00630	PF00307; CH; PF00630; Filamin	8.A.66.1.4	The Dystrophin (Dystrophin) Family	hsa04010: MAPK signaling pathway; hsa04510: Focal adhesion; hsa05132: Salmonella infection; hsa05205: Proteoglycans in cancer	R-HSA-114608: Platelet degranulation; R-HSA-430116: GP1b-IX-V activation signalling; R-HSA-446353: Cell-extracellular matrix interactions; R-HSA-5627123: RHO GTPases activate PAKs; R-HSA-8983711: OAS antiviral response	.	P21333
TT1VAUK	VEGFR1 messenger RNA (VEGFR1 mRNA)	P17948	VGFR1_HUMAN	mRNA target	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)	FLT1	"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."	EC 2.7.10.1	5T89; 5EX3; 5ABD; 4CL7; 4CKV	MVSYWDTGVLLCALLSCLLLTGSSSGSKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERLSITKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAIYIFISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQTNTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNKRASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGLYTCRVRSGPSFKSVNTSVHIYDKAFITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSIKQSNVFKNLTATLIVNVKPQIYEKAVSSFPDPALYPLGSRQILTCTAYGIPQPTIKWFWHPCNHNHSEARCDFCSNNEESFILDADSNMGNRIESITQRMAIIEGKNKMASTLVVADSRISGIYICIASNKVGTVGRNISFYITDVPNGFHVNLEKMPTEGEDLKLSCTVNKFLYRDVTWILLRTVNNRTMHYSISKQKMAITKEHSITLNLTIMNVSLQDSGTYACRARNVYTGEEILQKKEITIRDQEAPYLLRNLSDHTVAISSSTTLDCHANGVPEPQITWFKNNHKIQQEPGIILGPGSSTLFIERVTEEDEGVYHCKATNQKGSVESSAYLTVQGTSDKSNLELITLTCTCVAATLFWLLLTLFIRKMKRSSSEIKTDYLSIIMDPDEVPLDEQCERLPYDASKWEFARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCRTVAVKMLKEGATASEYKALMTELKILTHIGHHLNVVNLLGACTKQGGPLMVIVEYCKYGNLSNYLKSKRDLFFLNKDAALHMEPKKEKMEPGLEQGKKPRLDSVTSSESFASSGFQEDKSLSDVEEEEDSDGFYKEPITMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKGDTRLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGGSPYPGVQMDEDFCSRLREGMRMRAPEYSTPEIYQIMLDCWHRDPKERPRFAELVEKLGDLLQANVQQDGKDYIPINAILTGNSGFTYSTPAFSEDFFKESISAPKFNSGSSDDVRYVNAFKFMSLERIKTFEELLPNATSMFDDYQGDSSTLLASPMLKRFTWTDSKPKASLKIDLRVTSKSKESGLSDVSRPSFCHSSCGHVSEGKRRFTYDHAELERKIACCSPPPDYNSVVLYSTPPI	Successful	New anilinophthalazines as potent and orally well absorbed inhibitors of the VEGF receptor tyrosine kinases useful as antagonists of tumor-driven a... J Med Chem. 2000 Jun 15;43(12):2310-23.	34	mRNA	mRNA target	.	.	.	Immunoglobulin I-set domain; Immunoglobulin domain; Protein tyrosine kinase; VEGFR-2 Transmembrane domain	PF07679; PF00047; PF07714; PF17988	PF07679; I-set; PF00047; ig; PF07714; Pkinase_Tyr; PF17988; VEGFR-2_TMD	.	.	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	R-HSA-194306:Neurophilin interactions with VEGF and VEGFR; R-HSA-195399:VEGF binds to VEGFR leading to receptor dimerization	.	P17948
TT2Q6G1	Vascular endothelial growth factor receptor 1 (FLT-1)	P17948	VGFR1_HUMAN	Kinase	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	FLT1	"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."	EC 2.7.10.1	5T89; 5EX3; 5ABD; 4CL7; 4CKV	MVSYWDTGVLLCALLSCLLLTGSSSGSKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERLSITKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAIYIFISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQTNTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNKRASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGLYTCRVRSGPSFKSVNTSVHIYDKAFITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSIKQSNVFKNLTATLIVNVKPQIYEKAVSSFPDPALYPLGSRQILTCTAYGIPQPTIKWFWHPCNHNHSEARCDFCSNNEESFILDADSNMGNRIESITQRMAIIEGKNKMASTLVVADSRISGIYICIASNKVGTVGRNISFYITDVPNGFHVNLEKMPTEGEDLKLSCTVNKFLYRDVTWILLRTVNNRTMHYSISKQKMAITKEHSITLNLTIMNVSLQDSGTYACRARNVYTGEEILQKKEITIRDQEAPYLLRNLSDHTVAISSSTTLDCHANGVPEPQITWFKNNHKIQQEPGIILGPGSSTLFIERVTEEDEGVYHCKATNQKGSVESSAYLTVQGTSDKSNLELITLTCTCVAATLFWLLLTLFIRKMKRSSSEIKTDYLSIIMDPDEVPLDEQCERLPYDASKWEFARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCRTVAVKMLKEGATASEYKALMTELKILTHIGHHLNVVNLLGACTKQGGPLMVIVEYCKYGNLSNYLKSKRDLFFLNKDAALHMEPKKEKMEPGLEQGKKPRLDSVTSSESFASSGFQEDKSLSDVEEEEDSDGFYKEPITMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKGDTRLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGGSPYPGVQMDEDFCSRLREGMRMRAPEYSTPEIYQIMLDCWHRDPKERPRFAELVEKLGDLLQANVQQDGKDYIPINAILTGNSGFTYSTPAFSEDFFKESISAPKFNSGSSDDVRYVNAFKFMSLERIKTFEELLPNATSMFDDYQGDSSTLLASPMLKRFTWTDSKPKASLKIDLRVTSKSKESGLSDVSRPSFCHSSCGHVSEGKRRFTYDHAELERKIACCSPPPDYNSVVLYSTPPI	Successful	"Development of ranibizumab, an anti-vascular endothelial growth factor antigen binding fragment, as therapy for neovascular age-related macular degeneration. Retina. 2006 Oct;26(8):859-70."	25	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Immunoglobulin I-set domain; Immunoglobulin domain; Protein tyrosine kinase; VEGFR-2 Transmembrane domain	PF07679; PF00047; PF07714; PF17988	PF07679; I-set; PF00047; ig; PF07714; Pkinase_Tyr; PF17988; VEGFR-2_TMD	.	.	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	R-HSA-194306:Neurophilin interactions with VEGF and VEGFR; R-HSA-195399:VEGF binds to VEGFR leading to receptor dimerization	.	P17948
TTGJCWZ	Fms-like tyrosine kinase 3 (FLT-3)	P36888	FLT3_HUMAN	Kinase	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	FLT3	"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."	EC 2.7.10.1	6IL3; 5X02; 4XUF; 4RT7; 3QS9	MPALARDGGQLPLLVVFSAMIFGTITNQDLPVIKCVLINHKNNDSSVGKSSSYPMVSESPEDLGCALRPQSSGTVYEAAAVEVDVSASITLQVLVDAPGNISCLWVFKHSSLNCQPHFDLQNRGVVSMVILKMTETQAGEYLLFIQSEATNYTILFTVSIRNTLLYTLRRPYFRKMENQDALVCISESVPEPIVEWVLCDSQGESCKEESPAVVKKEEKVLHELFGTDIRCCARNELGRECTRLFTIDLNQTPQTTLPQLFLKVGEPLWIRCKAVHVNHGFGLTWELENKALEEGNYFEMSTYSTNRTMIRILFAFVSSVARNDTGYYTCSSSKHPSQSALVTIVEKGFINATNSSEDYEIDQYEEFCFSVRFKAYPQIRCTWTFSRKSFPCEQKGLDNGYSISKFCNHKHQPGEYIFHAENDDAQFTKMFTLNIRRKPQVLAEASASQASCFSDGYPLPSWTWKKCSDKSPNCTEEITEGVWNRKANRKVFGQWVSSSTLNMSEAIKGFLVKCCAYNSLGTSCETILLNSPGPFPFIQDNISFYATIGVCLLFIVVLTLLICHKYKKQFRYESQLQMVQVTGSSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKADSSEREALMSELKMMTQLGSHENIVNLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFHRTWTEIFKEHNFSFYPTFQSHPNSSMPGSREVQIHPDSDQISGLHGNSFHSEDEIEYENQKRLEEEEDLNVLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLTSFLGCQLADAEEAMYQNVDGRVSECPHTYQNRRPFSREMDLGLLSPQAQVEDS	Successful	A comparison of physicochemical property profiles of marketed oral drugs and orally bioavailable anti-cancer protein kinase inhibitors in clinical development. Curr Top Med Chem. 2007;7(14):1408-22.	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Immunoglobulin domain; Protein tyrosine kinase	PF00047; PF07714	PF00047; ig; PF07714; Pkinase_Tyr	.	.	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	"R-HSA-109704: PI3K Cascade; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-9607240: FLT3 Signaling; R-HSA-9645135: STAT5 Activation; R-HSA-9702509: FLT3 mutants bind TKIs; R-HSA-9702518: STAT5 activation downstream of FLT3 ITD mutants; R-HSA-9702569: KW2449-resistant FLT3 mutants; R-HSA-9702577: semaxanib-resistant FLT3 mutants; R-HSA-9702581: crenolanib-resistant FLT3 mutants; R-HSA-9702590: gilteritinib-resistant FLT3 mutants; R-HSA-9702596: lestaurtinib-resistant FLT3 mutants; R-HSA-9702600: midostaurin-resistant FLT3 mutants; R-HSA-9702605: pexidartinib-resistant FLT3 mutants; R-HSA-9702614: ponatinib-resistant FLT3 mutants; R-HSA-9702620: quizartinib-resistant FLT3 mutants; R-HSA-9702624: sorafenib-resistant FLT3 mutants; R-HSA-9702632: sunitinib-resistant FLT3 mutants; R-HSA-9702636: tandutinib-resistant FLT3 mutants; R-HSA-9702998: linifanib-resistant FLT3 mutants; R-HSA-9703009: tamatinib-resistant FLT3 mutants; R-HSA-9703648: Signaling by FLT3 ITD and TKD mutants; R-HSA-9706369: Negative regulation of FLT3; R-HSA-9706374: FLT3 signaling through SRC family kinases; R-HSA-9706377: FLT3 signaling by CBL mutants"	.	P36888
TTDCBX5	Vascular endothelial growth factor receptor 3 (FLT-4)	P35916	VGFR3_HUMAN	Kinase	VEGFR3; VEGFR-3; VEGF-3 receptor; Tyrosine-protein kinase receptor FLT4; Fms-like tyrosine kinase 4	FLT4	"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."	EC 2.7.10.1	4BSK; 4BSJ	MQRGAALCLRLWLCLGLLDGLVSGYSMTPPTLNITEESHVIDTGDSLSISCRGQHPLEWAWPGAQEAPATGDKDSEDTGVVRDCEGTDARPYCKVLLLHEVHANDTGSYVCYYKYIKARIEGTTAASSYVFVRDFEQPFINKPDTLLVNRKDAMWVPCLVSIPGLNVTLRSQSSVLWPDGQEVVWDDRRGMLVSTPLLHDALYLQCETTWGDQDFLSNPFLVHITGNELYDIQLLPRKSLELLVGEKLVLNCTVWAEFNSGVTFDWDYPGKQAERGKWVPERRSQQTHTELSSILTIHNVSQHDLGSYVCKANNGIQRFRESTEVIVHENPFISVEWLKGPILEATAGDELVKLPVKLAAYPPPEFQWYKDGKALSGRHSPHALVLKEVTEASTGTYTLALWNSAAGLRRNISLELVVNVPPQIHEKEASSPSIYSRHSRQALTCTAYGVPLPLSIQWHWRPWTPCKMFAQRSLRRRQQQDLMPQCRDWRAVTTQDAVNPIESLDTWTEFVEGKNKTVSKLVIQNANVSAMYKCVVSNKVGQDERLIYFYVTTIPDGFTIESKPSEELLEGQPVLLSCQADSYKYEHLRWYRLNLSTLHDAHGNPLLLDCKNVHLFATPLAASLEEVAPGARHATLSLSIPRVAPEHEGHYVCEVQDRRSHDKHCHKKYLSVQALEAPRLTQNLTDLLVNVSDSLEMQCLVAGAHAPSIVWYKDERLLEEKSGVDLADSNQKLSIQRVREEDAGRYLCSVCNAKGCVNSSASVAVEGSEDKGSMEIVILVGTGVIAVFFWVLLLLIFCNMRRPAHADIKTGYLSIIMDPGEVPLEEQCEYLSYDASQWEFPRERLHLGRVLGYGAFGKVVEASAFGIHKGSSCDTVAVKMLKEGATASEHRALMSELKILIHIGNHLNVVNLLGACTKPQGPLMVIVEFCKYGNLSNFLRAKRDAFSPCAEKSPEQRGRFRAMVELARLDRRRPGSSDRVLFARFSKTEGGARRASPDQEAEDLWLSPLTMEDLVCYSFQVARGMEFLASRKCIHRDLAARNILLSESDVVKICDFGLARDIYKDPDYVRKGSARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFCQRLRDGTRMRAPELATPAIRRIMLNCWSGDPKARPAFSELVEILGDLLQGRGLQEEEEVCMAPRSSQSSEEGSFSQVSTMALHIAQADAEDSPPSLQRHSLAARYYNWVSFPGCLARGAETRGSSRMKTFEEFPMTPTTYKGSVDNQTDSGMVLASEEFEQIESRHRQESGFSCKGPGQNVAVTRAHPDSQGRRRRPERGARGGQVFYNSEYGELSEPSEEDHCSPSARVTFFTDNSY	Successful	Company report (Medigen)	25	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Immunoglobulin I-set domain; Protein tyrosine kinase; VEGFR-2 Transmembrane domain	PF07679; PF07714; PF17988	PF07679; I-set; PF07714; Pkinase_Tyr; PF17988; VEGFR-2_TMD	.	.	hsa04014:Ras signaling pathway; hsa04015:Rap1 signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04510:Focal adhesion	R-HSA-195399:VEGF binds to VEGFR leading to receptor dimerization	.	P35916
TTJQ08V	Foot-and-mouth disease virus Capsid VP1 (FMDV VP1)	P03305 (725-935)	POLG_FMDVO	.	Foot-and-mouth disease virus P1D; Foot-and-mouth disease virus Virion protein 1	FMDV VP1	"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."	.	6FFA; 4QBB; 2JQG; 2JQF; 1QQP	TTSAGESADPVTTTVENYGGETQIQRRQHTDVSFIMDRFVKVTPQNQINILDLMQIPSHTLVGALLRASTYYFSDLEIAVKHEGDLTWVPNGAPEKALDNTTNPTAYHKAPLTRLALPYTAPHRVLATVYNGECRYNRNAVPNLRGDLQVLAQKVARTLPTSFNYGAIKATRVTELLYRMKRAETYCPRPLLAIHPTEARHKQKIVAPVKQ	Literature-reported	Identification of a conformational neutralizing epitope on the VP1 protein of type A foot-and-mouth disease virus. Res Vet Sci. 2017 Dec;115:374-381.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTD9KFV	Foot-and-mouth disease virus Capsid VP2 (FMDV VP2)	P03305 (287-504)	POLG_FMDVO	.	Foot-and-mouth disease virus P1B; Foot-and-mouth disease virus Virion protein 2	FMDV VP2	"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."	.	6FFA; 4QBB; 2JQG; 2JQF; 1QQP	DKKTEETTLLEDRILTTRNGHTTSTTQSSVGVTYGYATAEDFVSGPNTSGLETRVVQAERFFKTHLFDWVTSDSFGRCHLLELPTDHKGVYGSLTDSYAYMRNGWDVEVTAVGNQFNGGCLLVAMVPELYSIQKRELYQLTLFPHQFINPRTNMTAHITVPFVGVNRYDQYKVHKPWTLVVMVVAPLTVNTEGAPQIKVYANIAPTNVHVAGEFPSKE	Literature-reported	Foot-and-mouth disease virus capsid protein VP2 activates the cellular EIF2S1-ATF4 pathway and induces autophagy via HSPB1. Autophagy. 2018;14(2):336-346.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTB27Y5	Foot-and-mouth disease virus Capsid VP3 (FMDV VP3)	P03305 (505-724)	POLG_FMDVO	.	Foot-and-mouth disease virus P1C; Foot-and-mouth disease virus Virion protein 3	FMDV VP3	"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."	.	6FFA; 4QBB; 2JQG; 2JQF; 1QQP	GIFPVACSDGYGGLVTTDPKTADPVYGKVFNPPRNQLPGRFTNLLDVAEACPTFLRFEGGVPYVTTKTDSDRVLAQFDMSLAAKQMSNTFLAGLAQYYTQYSGTINLHFMFTGPTDAKARYMVAYAPPGMEPPKTPEAAAHCIHAEWDTGLNSKFTFSIPYLSAADYAYTASGVAETTNVQGWVCLFQITHGKADGDALVVLASAGKDFELRLPVDA	Literature-reported	The VP3 structural protein of foot-and-mouth disease virus inhibits the IFN- signaling pathway. FASEB J. 2016 May;30(5):1757-66.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTW20PQ	Formin-like protein 1 (FMNL1)	O95466	FMNL1_HUMAN	Formin homology family	Leukocyte formin; FRL1; FMNL; CLL-associated antigen KW-13; C17orf1B; C17orf1	FMNL1	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.	.	4YDH	MGNAAGSAEQPAGPAAPPPKQPAPPKQPMPAAGELEERFNRALNCMNLPPDKVQLLSQYDNEKKWELICDQERFQVKNPPAAYIQKLKSYVDTGGVSRKVAADWMSNLGFKRRVQESTQVLRELETSLRTNHIGWVQEFLNEENRGLDVLLEYLAFAQCSVTYDMESTDNGASNSEKNKPLEQSVEDLSKGPPSSVPKSRHLTIKLTPAHSRKALRNSRIVSQKDDVHVCIMCLRAIMNYQSGFSLVMNHPACVNEIALSLNNKNPRTKALVLELLAAVCLVRGGHDIILAAFDNFKEVCGEQHRFEKLMEYFRNEDSNIDFMVACMQFINIVVHSVENMNFRVFLQYEFTHLGLDLYLERLRLTESDKLQVQIQAYLDNIFDVGALLEDTETKNAVLEHMEELQEQVALLTERLRDAENESMAKIAELEKQLSQARKELETLRERFSESTAMGPSRRPPEPEKAPPAAPTRPSALELKVEELEEKGLIRILRGPGDAVSIEILPVAVATPSGGDAPTPGVPTGSPSPDLAPAAEPAPGAAPPPPPPLPGLPSPQEAPPSAPPQAPPLPGSPEPPPAPPLPGDLPPPPPPPPPPPGTDGPVPPPPPPPPPPPGGPPDALGRRDSELGPGVKAKKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEKVLQELDMSDFEEQFKTKSQGPSLDLSALKSKAAQKAPSKATLIEANRAKNLAITLRKGNLGAERICQAIEAYDLQALGLDFLELLMRFLPTEYERSLITRFEREQRPMEELSEEDRFMLCFSRIPRLPERMTTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNSSKRGAAYGFRLQSLDALLEMKSTDRKQTLLHYLVKVIAEKYPQLTGFHSDLHFLDKAGSVSLDSVLADVRSLQRGLELTQREFVRQDDCMVLKEFLRANSPTMDKLLADSKTAQEAFESVVEYFGENPKTTSPGLFFSLFSRFIKAYKKAEQEVEQWKKEAAAQEAGADTPGKGEPPAPKSPPKARRPQMDLISELKRRQQKEPLIYESDRDGAIEDIITVIKTVPFTARTGKRTSRLLCEASLGEEMPL	Literature-reported	Formin like 1 expression is increased on CD4+ T lymphocytes in spontaneous autoimmune uveitis. J Proteomics. 2017 Feb 10;154:102-108.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-5663220: RHO GTPases Activate Formins; R-HSA-9013148: CDC42 GTPase cycle; R-HSA-9013149: RAC1 GTPase cycle	.	O95466
TTPJ921	Fibronectin (FN1)	P02751	FINC_HUMAN	Fibronectin protein	FN; Cold-insoluble globulin; CIG	FN1	"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."	.	6HNF; 5N48; 5N47; 5M0A; 5J7C	MLRGPGPGLLLLAVQCLGTAVPSTGASKSKRQAQQMVQPQSPVAVSQSKPGCYDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEAEETCFDKYTGNTYRVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDTWRRPHETGGYMLECVCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSVQTTSSGSGPFTDVRAAVYQPQPHPQPPPYGHCVTDSGVVYSVGMQWLKTQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHTVLVQTRGGNSNGALCHFPFLYNNHNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDMGHMMRCTCVGNGRGEWTCIAYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPVDQCQDSETGTFYQIGDSWEKYVHGVRYQCYCYGRGIGEWHCQPLQTYPSSSGPVEVFITETPSQPNSHPIQWNAPQPSHISKYILRWRPKNSVGRWKEATIPGHLNSYTIKGLKPGVVYEGQLISIQQYGHQEVTRFDFTTTSTSTPVTSNTVTGETTPFSPLVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDTTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTGTPRSDTVPSPRDLQFVEVTDVKVTIMWTPPESAVTGYRVDVIPVNLPGEHGQRLPISRNTFAEVTGLSPGVTYYFKVFAVSHGRESKPLTAQQTTKLDAPTNLQFVNETDSTVLVRWTPPRAQITGYRLTVGLTRRGQPRQYNVGPSVSKYPLRNLQPASEYTVSLVAIKGNQESPKATGVFTTLQPGSSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYVYTIQVLRDGQERDAPIVNKVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGNSLEEVVHADQSSCTFDNLSPGLEYNVSVYTVKDDKESVPISDTIIPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIDLTNFLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYVVSVSSVYEQHESTPLRGRQKTGLDSPTGIDFSDITANSFTVHWIAPRATITGYRIRHHPEHFSGRPREDRVPHSRNSITLTNLTPGTEYVVSIVALNGREESPLLIGQQSTVSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIDKPSQMQVTDVQDNSISVKWLPSSSPVTGYRVTTTPKNGPGPTKTKTAGPDQTEMTIEGLQPTVEYVVSVYAQNPSGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDGEEDTAELQGLRPGSEYTVSVVALHDDMESQPLIGTQSTAIPAPTDLKFTQVTPTSLSAQWTPPNVQLTGYRVRVTPKEKTGPMKEINLAPDSSSVVVSGLMVATKYEVSVYALKDTLTSRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAVPANGQTPIQRTIKPDVRSYTITGLQPGTDYKIYLYTLNDNARSSPVVIDASTAIDAPSNLRFLATTPNSLLVSWQPPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTHPGYDTGNGIQLPGTSGQQPSVGQQMIFEEHGFRRTTPPTTATPIRHRPRPYPPNVGEEIQIGHIPREDVDYHLYPHGPGLNPNASTGQEALSQTTISWAPFQDTSEYIISCHPVGTDEEPLQFRVPGTSTSATLTGLTRGATYNVIVEALKDQQRHKVREEVVTVGNSVNEGLNQPTDDSCFDPYTVSHYAVGDEWERMSESGFKLLCQCLGFGSGHFRCDSSRWCHDNGVNYKIGEKWDRQGENGQMMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGGEPSPEGTTGQSYNQYSQRYHQRTNTNVNCPIECFMPLDVQADREDSRE	Clinical trial	National Cancer Institute Drug Dictionary (drug id 686947).	21	Fibronectin	Fibronectin	.	.	.	Fibronectin type I domain; Fibronectin type II domain; Fibronectin type III domain	PF00039; PF00040; PF00041	PF00039; fn1; PF00040; fn2; PF00041; fn3	.	.	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	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	.	P02751
TTP6W8J	Fructosamine-3-kinase (FN3K)	Q9H479	FN3K_HUMAN	Kinase	Fructosamine 3 kinase; FN3K; F3K	FN3K	"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."	EC 2.7.1.-	.	MEQLLRAELRTATLRAFGGPGAGCISEGRAYDTDAGPVFVKVNRRTQARQMFEGEVASLEALRSTGLVRVPRPMKVIDLPGGGAAFVMEHLKMKSLSSQASKLGEQMADLHLYNQKLREKLKEEENTVGRRGEGAEPQYVDKFGFHTVTCCGFIPQVNEWQDDWPTFFARHRLQAQLDLIEKDYADREARELWSRLQVKIPDLFCGLEIVPALLHGDLWSGNVAEDDVGPIIYDPASFYGHSEFELAIALMFGGFPRSFFTAYHRKIPKAPGFDQRLLLYQLFNYLNHWNHFGREYRSPSLGTMRRLLK	Literature-reported	Evidence That Differences in Fructosamine-3-Kinase Activity May Be Associated With the Glycation Gap in Human Diabetes. Diabetes. 2018 Jan;67(1):131-136.	.	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-163841: Gamma carboxylation, hypusine formation and arylsulfatase activation"	MetaCyc:ENSG00000167363-MON	Q9H479
TTQJCV8	Activation-associated cDNA protein (FNDC1)	Q4ZHG4	FNDC1_HUMAN	.	MEL4B3; KIAA1866; Fibronectin type III domain-containing protein 1; FNDC2; Expressed in synovial lining protein	FNDC1	May be an activator of G protein signaling.	.	.	MAPEAGATLRAPRRLSWAALLLLAALLPVASSAAASVDHPLKPRHVKLLSTKMGLKVTWDPPKDATSRPVEHYNIAYGKSLKSLKYIKVNAETYSFLIEDVEPGVVYFVLLTAENHSGVSRPVYRAESPPGGEWIEIDGFPIKGPGPFNETVTEKEVPNKPLRVRVRSSDDRLSVAWKAPRLSGAKSPRRSRGFLLGYGESGRKMNYVPLTRDERTHEIKKLASESVYVVSLQSMNSQGRSQPVYRAALTKRKISEEDELDVPDDISVRVMSSQSVLVSWVDPVLEKQKKVVASRQYTVRYREKGELARWDYKQIANRRVLIENLIPDTVYEFAVRISQGERDGKWSTSVFQRTPESAPTTAPENLNVWPVNGKPTVVAASWDALPETEGKVKEYILSYAPALKPFGAKSLTYPGDTTSALVDGLQPGERYLFKIRATNRRGLGPHSKAFIVAMPTTSKADVEQNTEDNGKPEKPEPSSPSPRAPASSQHPSVPASPQGRNAKDLLLDLKNKILANGGAPRKPQLRAKKAEELDLQSTEITGEEELGSREDSPMSPSDTQDQKRTLRPPSRHGHSVVAPGRTAVRARMPALPRREGVDKPGFSLATQPRPGAPPSASASPAHHASTQGTSHRPSLPASLNDNDLVDSDEDERAVGSLHPKGAFAQPRPALSPSRQSPSSVLRDRSSVHPGAKPASPARRTPHSGAAEEDSSASAPPSRLSPPHGGSSRLLPTQPHLSSPLSKGGKDGEDAPATNSNAPSRSTMSSSVSSHLSSRTQVSEGAEASDGESHGDGDREDGGRQAEATAQTLRARPASGHFHLLRHKPFAANGRSPSRFSIGRGPRLQPSSSPQSTVPSRAHPRVPSHSDSHPKLSSGIHGDEEDEKPLPATVVNDHVPSSSRQPISRGWEDLRRSPQRGASLHRKEPIPENPKSTGADTHPQGKYSSLASKAQDVQQSTDADTEGHSPKAQPGSTDRHASPARPPAARSQQHPSVPRRMTPGRAPQQQPPPPVATSQHHPGPQSRDAGRSPSQPRLSLTQAGRPRPTSQGRSHSSSDPYTASSRGMLPTALQNQDEDAQGSYDDDSTEVEAQDVRAPAHAARAKEAAASLPKHQQVESPTGAGAGGDHRSQRGHAASPARPSRPGGPQSRARVPSRAAPGKSEPPSKRPLSSKSQQSVSAEDDEEEDAGFFKGGKEDLLSSSVPKWPSSSTPRGGKDADGSLAKEEREPAIALAPRGGSLAPVKRPLPPPPGSSPRASHVPSRLPPRSAATVSPVAGTHPWPQYTTRAPPGHFSTTPMLSLRQRMMHARFRNPLSRQPARPSYRQGYNGRPNVEGKVLPGSNGKPNGQRIINGPQGTKWVVDLDRGLVLNAEGRYLQDSHGNPLRIKLGGDGRTIVDLEGTPVVSPDGLPLFGQGRHGTPLANAQDKPILSLGGKPLVGLEVIKKTTHPPTTTMQPTTTTTPLPTTTTPRPTTATTRRTTTTRRTTTRRPTTTVRTTTRTTTTTTPTPTTPIPTCPPGTLERHDDDGNLIMSSNGIPECYAEEDEFSGLETDTAVPTEEAYVIYDEDYEFETSRPPTTTEPSTTATTPRVIPEEGAISSFPEEEFDLAGRKRFVAPYVTYLNKDPSAPCSLTDALDHFQVDSLDEIIPNDLKKSDLPPQHAPRNITVVAVEGCHSFVIVDWDKATPGDVVTGYLVYSASYEDFIRNKWSTQASSVTHLPIENLKPNTRYYFKVQAQNPHGYGPISPSVSFVTESDNPLLVVRPPGGEPIWIPFAFKHDPSYTDCHGRQYVKRTWYRKFVGVVLCNSLRYKIYLSDNLKDTFYSIGDSWGRGEDHCQFVDSHLDGRTGPQSYVEALPTIQGYYRQYRQEPVRFGNIGFGTPYYYVGWYECGVSIPGKW	Literature-reported	Activator of G-protein signaling 8 is involved in VEGF-mediated signal processing during angiogenesis. J Cell Sci. 2016 Mar 15;129(6):1210-22.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q4ZHG4
TT7WZIJ	CAAX farnesyltransferase beta (FNTB)	P49356	FNTB_HUMAN	Alkyl aryl transferase	RAS proteins prenyltransferasebeta; FTase-beta; FNTB; CAAX farnesyltransferase beta subunit	FNTB	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.	EC 2.5.1.58	3.00E+37; 2IEJ; 2H6I; 2H6H; 2H6G	MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPVPGFEELKDETSAEPATD	Literature-reported	"US patent application no. 2005,0227,929, Combination therapy comprising a cox-2 inhibitor and an antineoplastic agent."	2	.	.	.	.	.	.	.	.	.	.	hsa00900:Terpenoid backbone biosynthesis; hsa01130:Biosynthesis of antibiotics	"R-HSA-2514859:Inactivation, recovery and regulation of the phototransduction cascade"	.	P49356
TTXQKM3	Farnesyl protein transferase (Ftase)	P49354; P49356	FNTA_HUMAN; FNTB_HUMAN	Alkyl aryl transferase	Ras proteins prenyltransferase; Protein farnesyltransferase; Ftase; CAAX farnesyltransferase	FNTB	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.	.	.	MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDSPSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLRDPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQRYFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLLDLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIGRSLQSKHSTENDSPTNVQQ	Successful	Tipifarnib in the treatment of newly diagnosed acute myelogenous leukemia. Biologics. 2008 Sep;2(3):491-500.	21	.	.	.	.	.	.	.	.	.	.	hsa00900:Terpenoid backbone biosynthesis; hsa01130:Biosynthesis of antibiotics	"R-HSA-111465:Apoptotic cleavage of cellular proteins; R-HSA-2514859:Inactivation, recovery and regulation of the phototransduction cascade"	.	P49354
TT9G4N0	Glutamate carboxypeptidase II (GCPII)	Q04609	FOLH1_HUMAN	Peptidase	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	FOLH1	"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."	EC 3.4.17.21	6HKZ; 6HKJ; 6H7Z; 6H7Y; 6FE5	MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLFGWFIKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA	Successful	Synergistic value of single-photon emission computed tomography/computed tomography fusion to radioimmunoscintigraphic imaging of prostate cancer. Semin Nucl Med. 2007 Jan;37(1):17-28.	34	EC:3.4	.	peptidase M28 family. M28B subfamily.	3.4.17.21	Acting on peptide bonds (peptidases)	PA domain; Peptidase family M28; Transferrin receptor-like dimerisation domain	PF02225; PF04389; PF04253	PF02225; PA; PF04389; Peptidase_M28; PF04253; TFR_dimer	.	.	"hsa00250:Alanine, aspartate and glutamate metabolism; hsa01100:Metabolic pathways; hsa04977:Vitamin digestion and absorption"	R-HSA-70614:Amino acid synthesis and interconversion (transamination)	.	Q04609
TTVC37M	Folate receptor alpha (FOLR1)	P15328	FOLR1_HUMAN	Folate receptor	"Ovarian tumorassociated antigen MOv18; KB cells FBP; Folate receptor, adult; Folate receptor 1; FRalpha; FOLR1; Adult folatebinding protein"	FOLR1	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.	.	5IZQ; 4LRH; 4KMX; 4KM7; 4KM6	MAQRMTTQLLLLLVWVAVVGEAQTRIAWARTELLNVCMNAKHHKEKPGPEDKLHEQCRPWRKNACCSTNTSQEAHKDVSYLYRFNWNHCGEMAPACKRHFIQDTCLYECSPNLGPWIQQVDQSWRKERVLNVPLCKEDCEQWWEDCRTSYTCKSNWHKGWNWTSGFNKCAVGAACQPFHFYFPTPTVLCNEIWTHSYKVSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAAAMSGAGPWAAWPFLLSLALMLLWLLS	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	hsa04144:Endocytosis	R-HSA-204005:COPII (Coat Protein 2) Mediated Vesicle Transport; R-HSA-5694530:Cargo concentration in the ER	.	P15328
TTT54CI	Folate receptor beta (FOLR2)	P14207	FOLR2_HUMAN	Folate receptor	"Placental folate-binding protein; Folate receptor, fetal/placental; Folate receptor type-beta; Folate receptor 2; FR-beta; FOLR2"	FOLR2	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.	.	4KN2; 4KN1; 4KN0; 4KMZ; 4KMY	MVWKWMPLLLLLVCVATMCSAQDRTDLLNVCMDAKHHKTKPGPEDKLHDQCSPWKKNACCTASTSQELHKDTSRLYNFNWDHCGKMEPACKRHFIQDTCLYECSPNLGPWIQQVNQSWRKERFLDVPLCKEDCQRWWEDCHTSHTCKSNWHRGWDWTSGVNKCPAGALCRTFESYFPTPAALCEGLWSHSYKVSNYSRGSGRCIQMWFDSAQGNPNEEVARFYAAAMHVNAGEMLHGTGGLLLSLALMLQLWLLG	Literature-reported	Strategy for the treatment of acute myelogenous leukemia based on folate receptor beta-targeted liposomal doxorubicin combined with receptor induct... Blood. 2002 Jul 15;100(2):594-602.	.	.	.	.	.	.	.	.	.	.	.	hsa01523: Antifolate resistance; hsa04144: Endocytosis	R-HSA-163125: Post-translational modification: synthesis of GPI-anchored proteins; R-HSA-196757: Metabolism of folate and pterines	.	P14207
TTSM9YR	Folate receptor gamma (FOLR3)	P41439	FOLR3_HUMAN	Folate receptor	Folate receptor 3; FRgamma; FOLR3	FOLR3	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.	.	.	MDMAWQMMQLLLLALVTAAGSAQPRSARARTDLLNVCMNAKHHKTQPSPEDELYGQCSPWKKNACCTASTSQELHKDTSRLYNFNWDHCGKMEPTCKRHFIQDSCLYECSPNLGPWIRQVNQSWRKERILNVPLCKEDCERWWEDCRTSYTCKSNWHKGWNWTSGINECPAGALCSTFESYFPTPAALCEGLWSHSFKVSNYSRGSGRCIQMWFDSAQGNPNEEVAKFYAAAMNAGAPSRGIIDS	Literature-reported	Expression of the folate receptor genes FOLR1 and FOLR3 differentiates ovarian carcinoma from breast carcinoma and malignant mesothelioma in serous... Hum Pathol. 2009 Oct;40(10):1453-60.	.	.	.	.	.	.	.	.	.	.	.	hsa01523: Antifolate resistance; hsa04144: Endocytosis	R-HSA-6798695: Neutrophil degranulation	.	P41439
TTOM5AU	c-Fos messenger RNA (c-Fos mRNA)	P01100	FOS_HUMAN	mRNA target	Proto-oncogene c-Fos (mRNA); G0S7 (mRNA); G0/G1 switch regulatory protein 7 (mRNA); Cellular oncogene fos (mRNA); C-fos (mRNA)	FOS	"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."	.	1S9K; 1FOS; 1A02	MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL	Literature-reported	"US patent application no. 6,312,900, Antisense oligonucleotide compositions and methods for the modulation of activating protein 1."	0	mRNA	mRNA target	.	.	.	bZIP transcription factor	PF00170	PF00170; bZIP_1	.	.	"hsa01522: Endocrine resistance; hsa04010: MAPK signaling pathway; hsa04024: cAMP signaling pathway; hsa04210: Apoptosis; hsa04380: Osteoclast differentiation; hsa04620: Toll-like receptor signaling pathway; hsa04657: IL-17 signaling pathway; hsa04658: Th1 and Th2 cell differentiation; hsa04659: Th17 cell differentiation; hsa04660: T cell receptor signaling pathway; hsa04662: B cell receptor signaling pathway; hsa04668: TNF signaling pathway; hsa04713: Circadian entrainment; hsa04725: Cholinergic synapse; hsa04728: Dopaminergic synapse; hsa04915: Estrogen signaling pathway; hsa04917: Prolactin signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04926: Relaxin signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04932: Non-alcoholic fatty liver disease; hsa04935: Growth hormone synthesis, secretion and action; hsa05031: Amphetamine addiction; hsa05130: Pathogenic Escherichia coli infection; hsa05132: Salmonella infection; hsa05133: Pertussis; hsa05135: Yersinia infection; hsa05140: Leishmaniasis; hsa05142: Chagas disease; hsa05161: Hepatitis B; hsa05162: Measles; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05210: Colorectal cancer; hsa05224: Breast cancer; hsa05231: Choline metabolism in cancer; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer; hsa05323: Rheumatoid arthritis; hsa05417: Lipid and atherosclerosis; hsa05418: Fluid shear stress and atherosclerosis"	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-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6796648: TP53 Regulates Transcription of DNA Repair Genes; R-HSA-9018519: Estrogen-dependent gene expression; R-HSA-9031628: NGF-stimulated transcription; R-HSA-9634638: Estrogen-dependent nuclear events downstream of ESR-membrane signaling	.	P01100
TTE2W36	Proto-oncogene c-Fos (c-Fos)	P01100	FOS_HUMAN	Basic leucine zipper bZIP	G0S7; G0/G1 switch regulatory protein 7; Cellular oncogene fos; C-fos	FOS	"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."	.	1S9K; 1FOS; 1A02	MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL	Literature-reported	Proto-oncogene c-fos induction in thiamine-deficient encephalopathy. Protective effects of nicardipine on pyrithiamine-induced lesions. J Neurol Sci. 1993 Sep;118(2):175-80.	.	bZIP	.	bZIP family. Fos subfamily.	.	.	bZIP transcription factor	PF00170	PF00170; bZIP_1	.	.	"hsa01522: Endocrine resistance; hsa04010: MAPK signaling pathway; hsa04024: cAMP signaling pathway; hsa04210: Apoptosis; hsa04380: Osteoclast differentiation; hsa04620: Toll-like receptor signaling pathway; hsa04657: IL-17 signaling pathway; hsa04658: Th1 and Th2 cell differentiation; hsa04659: Th17 cell differentiation; hsa04660: T cell receptor signaling pathway; hsa04662: B cell receptor signaling pathway; hsa04668: TNF signaling pathway; hsa04713: Circadian entrainment; hsa04725: Cholinergic synapse; hsa04728: Dopaminergic synapse; hsa04915: Estrogen signaling pathway; hsa04917: Prolactin signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04926: Relaxin signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04932: Non-alcoholic fatty liver disease; hsa04935: Growth hormone synthesis, secretion and action; hsa05031: Amphetamine addiction; hsa05130: Pathogenic Escherichia coli infection; hsa05132: Salmonella infection; hsa05133: Pertussis; hsa05135: Yersinia infection; hsa05140: Leishmaniasis; hsa05142: Chagas disease; hsa05161: Hepatitis B; hsa05162: Measles; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05210: Colorectal cancer; hsa05224: Breast cancer; hsa05231: Choline metabolism in cancer; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer; hsa05323: Rheumatoid arthritis; hsa05417: Lipid and atherosclerosis; hsa05418: Fluid shear stress and atherosclerosis"	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-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6796648: TP53 Regulates Transcription of DNA Repair Genes; R-HSA-9018519: Estrogen-dependent gene expression; R-HSA-9031628: NGF-stimulated transcription; R-HSA-9634638: Estrogen-dependent nuclear events downstream of ESR-membrane signaling	.	P01100
TTY8LZG	Fos-related antigen 1 (FOSL1)	P15407	FOSL1_HUMAN	Basic leucine zipper bZIP	Fra-1; FRA1	FOSL1	"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."	.	.	MFRDFGEPGPSSGNGGGYGGPAQPPAAAQAAQQKFHLVPSINTMSGSQELQWMVQPHFLGPSSYPRPLTYPQYSPPQPRPGVIRALGPPPGVRRRPCEQISPEEEERRRVRRERNKLAAAKCRNRRKELTDFLQAETDKLEDEKSGLQREIEELQKQKERLELVLEAHRPICKIPEGAKEGDTGSTSGTSSPPAPCRPVPCISLSPGPVLEPEALHTPTLMTTPSLTPFTPSLVFTYPSTPEPCASAHRKSSSSSGDPSSDPLGSPTLLAL	Literature-reported	Fra-1: a novel target for retinoid action. FEBS Lett. 1999 Apr 1;448(1):45-8.	.	bZIP	.	bZIP family. Fos subfamily.	.	.	bZIP transcription factor	PF00170	PF00170; bZIP_1	.	.	hsa04310: Wnt signaling pathway; hsa04380: Osteoclast differentiation; hsa04657: IL-17 signaling pathway; hsa05166: Human T-cell leukemia virus 1 infection	R-HSA-9031628: NGF-stimulated transcription	.	P15407
TT689IR	Fos-related antigen 2 (FOSL2)	P15408	FOSL2_HUMAN	Basic leucine zipper bZIP	FRA2; FRA-2	FOSL2	"As a dimer with JUN, activates LIF transcription. Activates CEBPB transcription in PGE2-activated osteoblasts. Controls osteoclast survival and size."	.	.	MYQDYPGNFDTSSRGSSGSPAHAESYSSGGGGQQKFRVDMPGSGSAFIPTINAITTSQDLQWMVQPTVITSMSNPYPRSHPYSPLPGLASVPGHMALPRPGVIKTIGTTVGRRRRDEQLSPEEEEKRRIRRERNKLAAAKCRNRRRELTEKLQAETEELEEEKSGLQKEIAELQKEKEKLEFMLVAHGPVCKISPEERRSPPAPGLQPMRSGGGSVGAVVVKQEPLEEDSPSSSSAGLDKAQRSVIKPISIAGGFYGEEPLHTPIVVTSTPAVTPGTSNLVFTYPSVLEQESPASPSESCSKAHRRSSSSGDQSSDSLNSPTLLAL	Literature-reported	Fos-like antigen 2 (FOSL2) promotes metastasis in colon cancer. Exp Cell Res. 2018 Dec 15;373(1-2):57-61.	.	bZIP	.	bZIP family. Fos subfamily.	.	.	bZIP transcription factor	PF00170	PF00170; bZIP_1	.	.	hsa04380: Osteoclast differentiation	.	.	P15408
TTNT3YA	Forkhead box protein C1 (FOXC1)	Q12948	FOXC1_HUMAN	.	Forkhead-related transcription factor 3; Forkhead-related protein FKHL7; FREAC3; FREAC-3; FKHL7	FOXC1	"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."	.	.	MQARYSVSSPNSLGVVPYLGGEQSYYRAAAAAAGGGYTAMPAPMSVYSHPAHAEQYPGGMARAYGPYTPQPQPKDMVKPPYSYIALITMAIQNAPDKKITLNGIYQFIMDRFPFYRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDAVKDKEEKDRLHLKEPPPPGRQPPPAPPEQADGNAPGPQPPPVRIQDIKTENGTCPSPPQPLSPAAALGSGSAAAVPKIESPDSSSSSLSSGSSPPGSLPSARPLSLDGADSAPPPPAPSAPPPHHSQGFSVDNIMTSLRGSPQSAAAELSSGLLASAAASSRAGIAPPLALGAYSPGQSSLYSSPCSQTSSAGSSGGGGGGAGAAGGAGGAGTYHCNLQAMSLYAAGERGGHLQGAPGGAGGSAVDDPLPDYSLPPVTSSSSSSLSHGGGGGGGGGGQEAGHHPAAHQGRLTSWYLNQAGGDLGHLASAAAAAAAAGYPGQQQNFHSVREMFESQRIGLNNSPVNGNSSCQMAFPSSQSLYRTSGAFVYDCSKF	Literature-reported	FOXC1: an emerging marker and therapeutic target for cancer. Oncogene. 2017 Jul 13;36(28):3957-3963.	.	.	.	.	.	.	Forkhead domain	PF00250	PF00250; Forkhead	.	.	.	.	.	Q12948
TTLBAP1	Forkhead box protein C2 (FOXC2)	Q99958	FOXC2_HUMAN	.	Transcription factor FKH14; Mesenchyme fork head protein 1; MFH1 protein; Forkheadrelated protein FKHL14; FOXC2	FOXC2	Transcriptional activator. Might be involved in the formation of special mesenchymal tissues.	.	6AKP; 6AKO; 1D5V	MQARYSVSDPNALGVVPYLSEQNYYRAAGSYGGMASPMGVYSGHPEQYSAGMGRSYAPYHHHQPAAPKDLVKPPYSYIALITMAIQNAPEKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDVSKEKEERAHLKEPPPAASKGAPATPHLADAPKEAEKKVVIKSEAASPALPVITKVETLSPESALQGSPRSAASTPAGSPDGSLPEHHAAAPNGLPGFSVENIMTLRTSPPGGELSPGAGRAGLVVPPLALPYAAAPPAAYGQPCAQGLEAGAAGGYQCSMRAMSLYTGAERPAHMCVPPALDEALSDHPSGPTSPLSALNLAAGQEGALAATGHHHQHHGHHHPQAPPPPPAPQPQPTPQPGAAAAQAASWYLNHSGDLNHLPGHTFAAQQQTFPNVREMFNSHRLGIENSTLGESQVSGNASCQLPYRSTPPLYRHAAPYSYDCTKY	Literature-reported	Forkhead Box Protein C2 (FOXC2) Promotes the Resistance of Human Ovarian Cancer Cells to Cisplatin In Vitro and In Vivo. Cell Physiol Biochem. 2016;39(1):242-52.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q99958
TTV1FDA	Forkhead box protein J2 (FOXJ2)	Q9P0K8	FOXJ2_HUMAN	.	Fork head homologous X; FHX	FOXJ2	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.	.	.	MASDLESSLTSIDWLPQLTLRATIEKLGSASQAGPPGSSRKCSPGSPTDPNATLSKDEAAVHQDGKPRYSYATLITYAINSSPAKKMTLSEIYRWICDNFPYYKNAGIGWKNSIRHNLSLNKCFRKVPRPRDDPGKGSYWTIDTCPDISRKRRHPPDDDLSQDSPEQEASKSPRGGVAGSGEASLPPEGNPQMSLQSPTSIASYSQGTGSVDGGAVAAGASGRESAEGPPPLYNTNHDFKFSYSEINFQDLSWSFRNLYKSMLEKSSSSSQHGFSSLLGDIPPSNNYYMYQQQQPPPPQQQQQQQQPPQPPPQQSQPQQQQAPAQGPSAVGGAPPLHTPSTDGCTPPGGKQAGAEGYGPPPVMAMHPPPLQHGGYHPHQHHPHSHPAQQPPPPQPQAQGQAPINNTGFAFPSDWCSNIDSLKESFKMVNRLNWSSIEQSQFSELMESLRQAEQKNWTLDQHHIANLCDSLNHFLTQTGHVPPQGGTHRPPAPARIADSCALTSGKQESAMSQVNSYGHPQAPHLYPGPSPMYPIPTQDSAGYNRPAHHMVPRPSVPPPGANEEIPDDFDWDLIT	Literature-reported	Overexpression of forkhead box J2 can decrease the migration of breast cancer cells. J Cell Biochem. 2012 Aug;113(8):2729-37.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9P0K8
TTD3KOX	Forkhead box protein M1 (FOXM1)	Q08050	FOXM1_HUMAN	.	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	FOXM1	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.	.	3G73	MKTSPRRPLILKRRRLPLPVQNAPSETSEEEPKRSPAQQESNQAEASKEVAESNSCKFPAGIKIINHPTMPNTQVVAIPNNANIHSIITALTAKGKESGSSGPNKFILISCGGAPTQPPGLRPQTQTSYDAKRTEVTLETLGPKPAARDVNLPRPPGALCEQKRETCADGEAAGCTINNSLSNIQWLRKMSSDGLGSRSIKQEMEEKENCHLEQRQVKVEEPSRPSASWQNSVSERPPYSYMAMIQFAINSTERKRMTLKDIYTWIEDHFPYFKHIAKPGWKNSIRHNLSLHDMFVRETSANGKVSFWTIHPSANRYLTLDQVFKPLDPGSPQLPEHLESQQKRPNPELRRNMTIKTELPLGARRKMKPLLPRVSSYLVPIQFPVNQSLVLQPSVKVPLPLAASLMSSELARHSKRVRIAPKVLLAEEGIAPLSSAGPGKEEKLLFGEGFSPLLPVQTIKEEEIQPGEEMPHLARPIKVESPPLEEWPSPAPSFKEESSHSWEDSSQSPTPRPKKSYSGLRSPTRCVSEMLVIQHRERRERSRSRRKQHLLPPCVDEPELLFSEGPSTSRWAAELPFPADSSDPASQLSYSQEVGGPFKTPIKETLPISSTPSKSVLPRTPESWRLTPPAKVGGLDFSPVQTSQGASDPLPDPLGLMDLSTTPLQSAPPLESPQRLLSSEPLDLISVPFGNSSPSDIDVPKPGSPEPQVSGLAANRSLTEGLVLDTMNDSLSKILLDISFPGLDEDPLGPDNINWSQFIPELQ	Literature-reported	Foxm1b transcription factor is essential for development of hepatocellular carcinomas and is negatively regulated by the p19ARF tumor suppressor. Genes Dev. 2004 Apr 1;18(7):830-50.	0	.	.	.	.	.	Forkhead domain	PF00250	PF00250; Forkhead	.	.	hsa04218: Cellular senescence	R-HSA-156711:Polo-like kinase mediated events; R-HSA-69273:Cyclin A/B1 associated events during G2/M transition	.	Q08050
TTLRVIA	Forkhead box O1A messenger RNA (FOXO1 mRNA)	Q12778	FOXO1_HUMAN	mRNA target	Forkhead in rhabdomyosarcoma (mRNA); Forkhead box protein O1A (mRNA); Forkhead box protein O1 (mRNA); FOXO1A (mRNA); FKHR (mRNA)	FOXO1	"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."	.	5DUI; 4LG0; 3COA; 3CO7; 3CO6	MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGSAAANPDAAAGLPSASAAAVSADFMSNLSLLEESEDFPQAPGSVAAAVAAAAAAAATGGLCGDFQGPEAGCLHPAPPQPPPPGPLSQHPPVPPAAAGPLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRSRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGEGDVHSMVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGTMMQQTPCYSFAPPNTSLNSPSPNYQKYTYGQSSMSPLPQMPIQTLQDNKSSYGGMSQYNCAPGLLKELLTSDSPPHNDIMTPVDPGVAQPNSRVLGQNVMMGPNSVMSTYGSQASHNKMMNPSSHTHPGHAQQTSAVNGRPLPHTVSTMPHTSGMNRLTQVKTPVQVPLPHPMQMSALGGYSSVSSCNGYGRMGLLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG	Literature-reported	"US patent application no. 7,229,976, Modulation of forkhead box O1A expression."	0	mRNA	mRNA target	.	.	.	"Forkhead domain; Transactivation domain of FOXO protein family; KIX-binding domain of forkhead box O, CR2"	PF00250; PF16676; PF16675	PF00250; Forkhead; PF16676; FOXO-TAD; PF16675; FOXO_KIX_bdg	.	.	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	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	.	Q12778
TTHAVTS	Forkhead box protein O1A (FOXO1)	Q12778	FOXO1_HUMAN	.	Forkhead in rhabdomyosarcoma; Forkhead box protein O1; FOXO1A; FKHR	FOXO1	"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)."	.	5DUI; 4LG0; 3COA; 3CO7; 3CO6	MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGSAAANPDAAAGLPSASAAAVSADFMSNLSLLEESEDFPQAPGSVAAAVAAAAAAAATGGLCGDFQGPEAGCLHPAPPQPPPPGPLSQHPPVPPAAAGPLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRSRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGEGDVHSMVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGTMMQQTPCYSFAPPNTSLNSPSPNYQKYTYGQSSMSPLPQMPIQTLQDNKSSYGGMSQYNCAPGLLKELLTSDSPPHNDIMTPVDPGVAQPNSRVLGQNVMMGPNSVMSTYGSQASHNKMMNPSSHTHPGHAQQTSAVNGRPLPHTVSTMPHTSGMNRLTQVKTPVQVPLPHPMQMSALGGYSSVSSCNGYGRMGLLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG	Literature-reported	Effects of the novel Foxo1 inhibitor AS1708727 on plasma glucose and triglyceride levels in diabetic db/db mice. Eur J Pharmacol. 2010 Oct 25;645(1-3):185-91.	0	.	.	.	.	.	"Forkhead domain; Transactivation domain of FOXO protein family; KIX-binding domain of forkhead box O, CR2"	PF00250; PF16676; PF16675	PF00250; Forkhead; PF16676; FOXO-TAD; PF16675; FOXO_KIX_bdg	.	.	hsa04068: FoxO signaling pathway; hsa04152: AMPK signaling pathway; hsa04211: Longevity regulating pathway; hsa04213: Longevity regulating pathway - multiple species; hsa04218: Cellular senescence; hsa04910: Insulin signaling pathway; hsa04919: Thyroid hormone signaling pathway; hsa04922: Glucagon signaling pathway; hsa04931: Insulin resistance; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04936: Alcoholic liver disease; hsa05131: Shigellosis; hsa05165: Human papillomavirus infection; hsa05200: Pathways in cancer; hsa05202: Transcriptional misregulation in cancer; hsa05215: Prostate cancer	"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; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9614399: Regulation of localization of FOXO transcription factors; R-HSA-9614657: FOXO-mediated transcription of cell death genes; R-HSA-9615017: FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes; R-HSA-9617629: Regulation of FOXO transcriptional activity by acetylation; R-HSA-9617828: FOXO-mediated transcription of cell cycle genes"	.	Q12778
TTKW9CI	FOXO4-P53 interaction (FOXO4-P53 PPI)	P98177-P04637	FOXO4_HUMAN-P53_HUMAN	.	.	FOXO4-TP53	.	.	.	.	Preclinical	FOXO4-DRI alleviates age-related testosterone secretion insufficiency by targeting senescent Leydig cells in aged mice. Aging (Albany NY). 2020 Jan 20;12(2):1272-1284.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P98177
TT0MUCI	Forkhead box protein P1 (FOXP1)	Q9H334	FOXP1_HUMAN	.	Mac-1-regulated forkhead; MFH; FOXP1-ES	FOXP1	"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)."	.	2KIU	MMQESGTETKSNGSAIQNGSGGSNHLLECGGLREGRSNGETPAVDIGAADLAHAQQQQQQALQVARQLLLQQQQQQQVSGLKSPKRNDKQPALQVPVSVAMMTPQVITPQQMQQILQQQVLSPQQLQVLLQQQQALMLQQQQLQEFYKKQQEQLQLQLLQQQHAGKQPKEQQQVATQQLAFQQQLLQMQQLQQQHLLSLQRQGLLTIQPGQPALPLQPLAQGMIPTELQQLWKEVTSAHTAEETTGNNHSSLDLTTTCVSSSAPSKTSLIMNPHASTNGQLSVHTPKRESLSHEEHPHSHPLYGHGVCKWPGCEAVCEDFQSFLKHLNSEHALDDRSTAQCRVQMQVVQQLELQLAKDKERLQAMMTHLHVKSTEPKAAPQPLNLVSSVTLSKSASEASPQSLPHTPTTPTAPLTPVTQGPSVITTTSMHTVGPIRRRYSDKYNVPISSADIAQNQEFYKNAEVRPPFTYASLIRQAILESPEKQLTLNEIYNWFTRMFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKGAVWTVDEVEFQKRRPQKISGNPSLIKNMQSSHAYCTPLNAALQASMAENSIPLYTTASMGNPTLGNLASAIREELNGAMEHTNSNESDSSPGRSPMQAVHPVHVKEEPLDPEEAEGPLSLVTTANHSPDFDHDRDYEDEPVNEDME	Literature-reported	Can Forkhead Box P1 be a novel therapeutic target for atherosclerosis Atherosclerosis. 2011 Sep;218(1):26-7.	.	.	.	.	.	.	.	.	.	.	.	hsa05206:MicroRNAs in cancer	R-HSA-452723: Transcriptional regulation of pluripotent stem cells	.	Q9H334
TT1X3QF	FOXP3 messenger RNA (FOXP3 mRNA)	Q9BZS1	FOXP3_HUMAN	.	Scurfin	FOXP3	"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)."	.	.	MPNPRPGKPSAPSLALGPSPGASPSWRAAPKASDLLGARGPGGTFQGRDLRGGAHASSSSLNPMPPSQLQLPTLPLVMVAPSGARLGPLPHLQALLQDRPHFMHQLSTVDAHARTPVLQVHPLESPAMISLTPPTTATGVFSLKARPGLPPGINVASLEWVSREPALLCTFPNPSAPRKDSTLSAVPQSSYPLLANGVCKWPGCEKVFEEPEDFLKHCQADHLLDEKGRAQCLLQREMVQSLEQQLVLEKEKLSAMQAHLAGKMALTKASSVASSDKGSCCIVAAGSQGPVVPAWSGPREAPDSLFAVRRHLWGSHGNSTFPEFLHNMDYFKFHNMRPPFTYATLIRWAILEAPEKQRTLNEIYHWFTRMFAFFRNHPATWKNAIRHNLSLHKCFVRVESEKGAVWTVDELEFRKKRSQRPSRCSNPTPGP	Clinical trial	"Clinical pipeline report, company report or official report of Ionis Pharmaceuticals."	.	.	.	.	.	.	.	.	.	.	.	hsa04659: Th17 cell differentiation; hsa05321: Inflammatory bowel disease	R-HSA-8877330: RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs); R-HSA-8939256: RUNX1 regulates transcription of genes involved in WNT signaling	.	Q9BZS1
TTEJZOL	Forkhead box protein Q1 (FOXQ1)	Q9C009	FOXQ1_HUMAN	.	Hepatocyte nuclear factor 3 forkhead homolog 1; HNF3/forkheadlike protein 1; HNF-3/forkhead-like protein 1; HFH1; HFH-1	FOXQ1	Plays a role in hair follicle differentiation.	.	.	MKLEVFVPRAAHGDKQGSDLEGAGGSDAPSPLSAAGDDSLGSDGDCAANSPAAGGGARDTQGDGEQSAGGGPGAEEAIPAAAAAAVVAEGAEAGAAGPGAGGAGSGEGARSKPYTRRPKPPYSYIALIAMAIRDSAGGRLTLAEINEYLMGKFPFFRGSYTGWRNSVRHNLSLNDCFVKVLRDPSRPWGKDNYWMLNPNSEYTFADGVFRRRRKRLSHRAPVPAPGLRPEEAPGLPAAPPPAPAAPASPRMRSPARQEERASPAGKFSSSFAIDSILRKPFRSRRLRDTAPGTTLQWGAAPCPPLPAFPALLPAAPCRALLPLCAYGAGEPARLGAREAEVPPTAPPLLLAPLPAAAPAKPLRGPAAGGAHLYCPLRLPAALQAASVRRPGPHLPYPVETLLA	Literature-reported	Melanoma Suppressor Functions of the Carcinoma Oncogene FOXQ1. Cell Rep. 2017 Sep 19;20(12):2820-2832.	.	.	.	.	.	.	Forkhead domain	PF00250	PF00250; Forkhead	.	.	.	.	.	Q9C009
TT5Y4EM	N-formyl peptide receptor (FPR1)	P21462	FPR1_HUMAN	GPCR rhodopsin	N-formylpeptide chemoattractant receptor; FPR1; FPR	FPR1	"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)."	.	.	METNSSLPTNISGGTPAVSAGYLFLDIITYLVFAVTFVLGVLGNGLVIWVAGFRMTHTVTTISYLNLAVADFCFTSTLPFFMVRKAMGGHWPFGWFLCKFVFTIVDINLFGSVFLIALIALDRCVCVLHPVWTQNHRTVSLAKKVIIGPWVMALLLTLPVIIRVTTVPGKTGTVACTFNFSPWTNDPKERINVAVAMLTVRGIIRFIIGFSAPMSIVAVSYGLIATKIHKQGLIKSSRPLRVLSFVAAAFFLCWSPYQVVALIATVRIRELLQGMYKEIGIAVDVTSALAFFNSCLNPMLYVFMGQDFRERLIHALPASLERALTEDSTQTSDTATNSTLPSAEVELQAK	Clinical trial	Rebamipide suppresses formyl-methionyl-leucyl-phenylalanine (fMLP)-induced superoxide production by inhibiting fMLP-receptor binding in human neutrophils. J Pharmacol Exp Ther. 2001 Apr;297(1):388-94.	25	.	.	.	.	.	.	.	.	.	.	hsa04015:Rap1 signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa05150:Staphylococcus aureus infection	R-HSA-418594:G alpha (i) signalling events	.	P21462
TTOJ1NF	FMLP-related receptor I (FPR2)	P25090	FPR2_HUMAN	GPCR rhodopsin	RFP; Lipoxin A4 receptor; LXA4 receptor; HM63; G-protein-coupled receptor FPR-Like-1; Formyl peptide receptor-like 1; FPRL1; FPR2; FMLP-R-I	FPR2	"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)."	.	.	METNFSTPLNEYEEVSYESAGYTVLRILPLVVLGVTFVLGVLGNGLVIWVAGFRMTRTVTTICYLNLALADFSFTATLPFLIVSMAMGEKWPFGWFLCKLIHIVVDINLFGSVFLIGFIALDRCICVLHPVWAQNHRTVSLAMKVIVGPWILALVLTLPVFLFLTTVTIPNGDTYCTFNFASWGGTPEERLKVAITMLTARGIIRFVIGFSLPMSIVAICYGLIAAKIHKKGMIKSSRPLRVLTAVVASFFICWFPFQLVALLGTVWLKEMLFYGKYKIIDILVNPTSSLAFFNSCLNPMLYVFVGQDFRERLIHSLPTSLERALSEDSAPTNDTAANSASPPAETELQAM	Literature-reported	Resolvin D1 receptor stereoselectivity and regulation of inflammation and proresolving microRNAs. Am J Pathol. 2012 May;180(5):2018-27.	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04613: Neutrophil extracellular trap formation; hsa05150: Staphylococcus aureus infection	R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events	.	P25090
TT16TM5	N-formyl peptide receptor 3 (FPR3)	P25089	FPR3_HUMAN	.	Formyl peptide receptor-like 2; FPRL2; FPRH1; FMLP-related receptor II; FMLP-R-II	FPR3	"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."	.	.	METNFSIPLNETEEVLPEPAGHTVLWIFSLLVHGVTFVFGVLGNGLVIWVAGFRMTRTVNTICYLNLALADFSFSAILPFRMVSVAMREKWPFGSFLCKLVHVMIDINLFVSVYLITIIALDRCICVLHPAWAQNHRTMSLAKRVMTGLWIFTIVLTLPNFIFWTTISTTNGDTYCIFNFAFWGDTAVERLNVFITMAKVFLILHFIIGFSVPMSIITVCYGIIAAKIHRNHMIKSSRPLRVFAAVVASFFICWFPYELIGILMAVWLKEMLLNGKYKIILVLINPTSSLAFFNSCLNPILYVFMGRNFQERLIRSLPTSLERALTEVPDSAQTSNTDTTSASPPEETELQAM	Literature-reported	N-Formylated humanin activates both formyl peptide receptor-like 1 and 2. Biochem Biophys Res Commun. 2004 Nov 5;324(1):255-61.	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04613: Neutrophil extracellular trap formation; hsa05150: Staphylococcus aureus infection	R-HSA-418594: G alpha (i) signalling events; R-HSA-444473: Formyl peptide receptors bind formyl peptides and many other ligands	.	P25089
TTTRS9B	Fascin (FSCN1)	Q16658	FSCN1_HUMAN	.	Singed-like protein; SNL; HSN; FAN1; 55 kDa actin-bundling protein; 55 kDa actin bundling protein	FSCN1	"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."	.	6I18; 6I17; 6I16; 6I15; 6I14	MTANGTAEAVQIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPGPDCRFLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTADHRFLRHDGRLVARPEPATGYTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTATGGVQSTASSKNASCYFDIEWRDRRITLRASNGKFVTSKKNGQLAASVETAGDSELFLMKLINRPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVAIKVGGRYLKGDHAGVLKASAETVDPASLWEY	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	fascin family.	.	.	Fascin domain	PF06268	PF06268; Fascin	.	.	hsa05206: MicroRNAs in cancer	R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling	.	Q16658
TT13GFV	Follicle stimulating hormone (FSHB)	P01225	FSHB_HUMAN	Hormone	Follitropin subunit beta; Follitropin beta chain; Follicle-stimulating hormone beta subunit; FSH-beta; FSH-B	FSHB	"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."	.	4MQW; 4AY9; 1XWD; 1FL7	MKTLQFFFLFCCWKAICCNSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDPARPKIQKTCTFKELVYETVRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFGEMKE	Clinical trial	Company report (Glycotope)	21	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04912:GnRH signaling pathway; hsa04913:Ovarian steroidogenesis; hsa04917:Prolactin signaling pathway; hsa04918:Thyroid hormone synthesis; hsa05320:Autoimmune thyroid disease	R-HSA-209968:Thyroxine biosynthesis; R-HSA-375281:Hormone ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events	.	P01225
TTZFDBT	Follicle-stimulating hormone receptor (FSHR)	P23945	FSHR_HUMAN	GPCR rhodopsin	LGR1; Follitropin receptor; FSH-R	FSHR	"G protein-coupled receptor for follitropin, the follicle-stimulating hormone. Through cAMP production activates the downstream PI3K-AKT and ERK1/ERK2 signaling pathways."	.	4MQW; 4AY9; 1XWD; 1XUN	MALLLVSLLAFLSLGSGCHHRICHCSNRVFLCQESKVTEIPSDLPRNAIELRFVLTKLRVIQKGAFSGFGDLEKIEISQNDVLEVIEADVFSNLPKLHEIRIEKANNLLYINPEAFQNLPNLQYLLISNTGIKHLPDVHKIHSLQKVLLDIQDNINIHTIERNSFVGLSFESVILWLNKNGIQEIHNCAFNGTQLDELNLSDNNNLEELPNDVFHGASGPVILDISRTRIHSLPSYGLENLKKLRARSTYNLKKLPTLEKLVALMEASLTYPSHCCAFANWRRQISELHPICNKSILRQEVDYMTQARGQRSSLAEDNESSYSRGFDMTYTEFDYDLCNEVVDVTCSPKPDAFNPCEDIMGYNILRVLIWFISILAITGNIIVLVILTTSQYKLTVPRFLMCNLAFADLCIGIYLLLIASVDIHTKSQYHNYAIDWQTGAGCDAAGFFTVFASELSVYTLTAITLERWHTITHAMQLDCKVQLRHAASVMVMGWIFAFAAALFPIFGISSYMKVSICLPMDIDSPLSQLYVMSLLVLNVLAFVVICGCYIHIYLTVRNPNIVSSSSDTRIAKRMAMLIFTDFLCMAPISFFAISASLKVPLITVSKAKILLVLFHPINSCANPFLYAIFTKNFRRDFFILLSKCGCYEMQAQIYRTETSSTVHNTHPRNGHCSSAPRVTNGSTYILVPLSHLAQN	Successful	The role of gonadotropins in ovulation induction. Am J Obstet Gynecol. 1995 Feb;172(2 Pt 2):759-65.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family. FSH/LSH/TSH subfamily.	.	.	7 transmembrane receptor (rhodopsin family); Gonadotropin hormone receptor transmembrane region ; BspA type Leucine rich repeat region (6 copies); Leucine rich repeat N-terminal domain	PF00001; PF12369; PF13306; PF01462	PF00001; 7tm_1; PF12369; GnHR_trans; PF13306; LRR_5; PF01462; LRRNT	9.A.14.1.5	The G-protein-coupled receptor (GPCR) Family	hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04913:Ovarian steroidogenesis	R-HSA-375281:Hormone ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events	.	P23945
TTDNM9W	Follistatin (FST)	P19883	FST_HUMAN	.	FST; FS; Activinbinding protein	FST	Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH).	.	5JHW; 3HH2; 2P6A; 2B0U	MVRARHQPGGLCLLLLLLCQFMEDRSAQAGNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGLDGKTYRNECALLKARCKEQPELEVQYQGRCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNRICPEPASSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAYEGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCNSISEDTEEEEEDEDQDYSFPISSILEW	Literature-reported	"Role of activin, follistatin, and inhibin in the regulation of kiss-1 gene expression in hypothalamic cell models. Biol Reprod. 2019 Jun 5. pii: ioz094."	.	.	.	.	.	.	.	.	.	.	.	hsa04350: TGF-beta signaling pathway	R-HSA-2473224: Antagonism of Activin by Follistatin	.	P19883
TTWRPM8	Follistatin-related protein 3 (FSTL3)	O95633	FSTL3_HUMAN	.	UNQ674/PRO1308; Follistatin-related gene protein; Follistatin-related gene; Follistatin-like 3; FSTL3; FLRG	FSTL3	"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."	.	3SEK; 3B4V; 2KCX	MRPGAPGPLWPLPWGALAWAVGFVSSMGSGNPAPGGVCWLQQGQEATCSLVLQTDVTRAECCASGNIDTAWSNLTHPGNKINLLGFLGLVHCLPCKDSCDGVECGPGKACRMLGGRPRCECAPDCSGLPARLQVCGSDGATYRDECELRAARCRGHPDLSVMYRGRCRKSCEHVVCPRPQSCVVDQTGSAHCVVCRAAPCPVPSSPGQELCGNNNVTYISSCHMRQATCFLGRSIGVRHAGSCAGTPEEPPGGESAEEEENFV	Literature-reported	"FLRG (follistatin-related gene), a new target of chromosomal rearrangement in malignant blood disorders. Oncogene. 1998 Jun 4;16(22):2949-54."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2473224: Antagonism of Activin by Follistatin; R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation	.	O95633
TT975ZT	Ferritin (FTH1)	P02794	FRIH_HUMAN	Metal ion oxidoreductase	PIG15; OK/SW-cl.84; Ferritin heavy chain; Ferritin H subunit; FTHL6; FTH; Cell proliferationinducing gene 15 protein; Cell proliferation-inducing gene 15 protein	FTH1	"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."	EC 1.16.3.1	6IPQ; 6IPP; 6IPO; 6IPC; 6H5I	MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNES	Clinical trial	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800019964)"	19	EC:1.16	Metal ion oxidoreductase	ferritin family.	1.16.3.1	Oxidizing metal ions	Ferritin-like domain	PF00210	PF00210; Ferritin	.	.	hsa04978:Mineral absorption	R-HSA-3000480:Scavenging by Class A Receptors; R-HSA-432722:Golgi Associated Vesicle Biogenesis; R-HSA-917937:Iron uptake and transport	.	P02794
TTFW3BT	N1-methyl adenine demethylase	.	FTO_HUMAN	Single Protein	Alpha-ketoglutarate-dependent dioxygenase FTO; Fat mass and obesity-associated protein; U6 small nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small nuclear RNA N(6)-methyladenosine-demethylase FTO; m6A(m)-demethylase FTO; mRNA (2'-O-methyladenosine-N(6)-)-demethylase FTO; mRNA N(6)-methyladenosine demethylase FTO; tRNA N1-methyl adenine demethylase FTO	FTO	"RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis. Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. M6A demethylation by FTO affects mRNA expression and stability. Also able to demethylate m6A in U6 small nuclear RNA (snRNA)."	.	.	MKRTPTAEEREREAKKLRLLEELEDTWLPYLTPKDDEFYQQWQLKYPKLILREASSVSEELHKEVQEAFLTLHKHGCLFRDLVRIQGKDLLTPVSRILIGNPGCTYKYLNTRLFTVPWPVKGSNIKHTEAEIAAACETFLKLNDYLQIETIQALEELAAKEKANEDAVPLCMSADFPRVGMGSSYNGQDEVDIKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGPEEESEDDSHLEGRDPDIWHVGFKISWDIETPGLAIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSSTHRVAECSTGTLDYILQRCQLALQNVCDDVDNDDVSLKSFEPAVLKQGEEIHNEVEFEWLRQFWFQGNRYRKCTDWWCQPMAQLEALWKKMEGVTNAVLHEVKREGLPVEQRNEILTAILASLTARQNLRREWHARCQSRIARTLPADQKPECRPYWEKDDASMPLPFDLTDIVSELRGQLLEAKP	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9C0B1
TTIEJ23	Fungal RNA triphosphatase (Fung CET1)	O13297	CET1_YEAST	Phosphoric monoester hydrolase	TPase; Polynucleotide 5'-triphosphatase; MRNA capping enzyme beta subunit; MRNA 5'-triphosphatase; CET1	Fung CET1	First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.	.	3KYH; 1D8I; 1D8H	MSYTDNPPQTKRALSLDDLVNHDENEKVKLQKLSEAANGSRPFAENLESDINQTETGQAAPIDNYKESTGHGSHSQKPKSRKSSNDDEETDTDDEMGASGEINFDSEMDFDYDKQHRNLLSNGSPPMNDGSDANAKLEKPSDDSIHQNSKSDEEQRIPKQGNEGNIASNYITQVPLQKQKQTEKKIAGNAVGSVVKKEEEANAAVDNIFEEKATLQSKKNNIKRDLEVLNEISASSKPSKYRNVPIWAQKWKPTIKALQSINVKDLKIDPSFLNIIPDDDLTKSVQDWVYATIYSIAPELRSFIELEMKFGVIIDAKGPDRVNPPVSSQCVFTELDAHLTPNIDASLFKELSKYIRGISEVTENTGKFSIIESQTRDSVYRVGLSTQRPRFLRMSTDIKTGRVGQFIEKRHVAQLLLYSPKDSYDVKISLNLELPVPDNDPPEKYKSQSPISERTKDRVSYIHNDSCTRIDITKVENHNQNSKSRQSETTHEVELEINTPALLNAFDNITNDSKEYASLIRTFLNNGTIIRRKLSSLSYEIFEGSKKVM	Literature-reported	Trypanosoma brucei RNA triphosphatase. Antiprotozoal drug target and guide to eukaryotic phylogeny. J Biol Chem. 2001 Dec 7;276(49):46182-6.	.	.	.	.	.	.	.	.	.	.	.	.	.	MetaCyc:G3O-34116-MON; YEAST:G3O-34116-MON	O13297
TTWQ8IY	Fungal Sterol 24-C-methyltransferase (Fung erg6)	Q96WX4	ERG6_PNEC8	Methyltransferase	erg6; SAM:SMT; S-adenosyl-L-methionine:sterol C-24 methyl transferase; S-adenosyl-L-methionine-C-24-delta-sterol-methyltransferase	Fung erg6	Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol.	EC 2.1.1.-	.	MSFELERIDIEKDREFSEIMHGKDAAKERGLLSSFRKDKEAQKIALDSYFGFWGDKCTSEKNDIHQQERFKFYATLTRHYYNLVTDFYEYGWSTSFHFCRFAKDESFSQAIARHEHYIALHAGIREGETVLDVGCGVGGPACQISVFTGANIVGLNNNDYQIQRAKYYSEKKGLSDKLKFIKGDFMQMPFPENSFDKIYSIEATIHAPSLEGVYSEIYRVLKPGGLYASYEWVMLNKYDENDPEHQQIVYGIEIGDSIPKISKIGEAEAALIKVGFEIIHSEELSTKNSPLPWYYYLDGDLRKVRSFRDFISIARMTTIGKWLISSFIGLMEFIGLLPKGSKKVNDILLVAADSLVKAGKKEIFTPMQLWVCRKPLV	Literature-reported	Inactivation of soybean sterol 24-C-methyltransferase by elongated sterol side chains at C26. Bioorg Med Chem Lett. 2007 Nov 1;17(21):5902-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q96WX4
TTZMS1L	Fungal Papulacandin B resistance protein 1 (Fung FKS1)	P38631	FKS1_YEAST	Hexosyltransferase	"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"	Fung FKS1	"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."	EC 2.4.1.34	.	MNTDQQPYQGQTDYTQGPGNGQSQEQDYDQYGQPLYPSQADGYYDPNVAAGTEADMYGQQPPNESYDQDYTNGEYYGQPPNMAAQDGENFSDFSSYGPPGTPGYDSYGGQYTASQMSYGEPNSSGTSTPIYGNYDPNAIAMALPNEPYPAWTADSQSPVSIEQIEDIFIDLTNRLGFQRDSMRNMFDHFMVLLDSRSSRMSPDQALLSLHADYIGGDTANYKKWYFAAQLDMDDEIGFRNMSLGKLSRKARKAKKKNKKAMEEANPEDTEETLNKIEGDNSLEAADFRWKAKMNQLSPLERVRHIALYLLCWGEANQVRFTAECLCFIYKCALDYLDSPLCQQRQEPMPEGDFLNRVITPIYHFIRNQVYEIVDGRFVKRERDHNKIVGYDDLNQLFWYPEGIAKIVLEDGTKLIELPLEERYLRLGDVVWDDVFFKTYKETRTWLHLVTNFNRIWVMHISIFWMYFAYNSPTFYTHNYQQLVDNQPLAAYKWASCALGGTVASLIQIVATLCEWSFVPRKWAGAQHLSRRFWFLCIIFGINLGPIIFVFAYDKDTVYSTAAHVVAAVMFFVAVATIIFFSIMPLGGLFTSYMKKSTRRYVASQTFTAAFAPLHGLDRWMSYLVWVTVFAAKYSESYYFLVLSLRDPIRILSTTAMRCTGEYWWGAVLCKVQPKIVLGLVIATDFILFFLDTYLWYIIVNTIFSVGKSFYLGISILTPWRNIFTRLPKRIYSKILATTDMEIKYKPKVLISQVWNAIIISMYREHLLAIDHVQKLLYHQVPSEIEGKRTLRAPTFFVSQDDNNFETEFFPRDSEAERRISFFAQSLSTPIPEPLPVDNMPTFTVLTPHYAERILLSLREIIREDDQFSRVTLLEYLKQLHPVEWECFVKDTKILAEETAAYEGNENEAEKEDALKSQIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTISGFMNYSRAIKLLYRVENPEIVQMFGGNAEGLERELEKMARRKFKFLVSMQRLAKFKPHELENAEFLLRAYPDLQIAYLDEEPPLTEGEEPRIYSALIDGHCEILDNGRRRPKFRVQLSGNPILGDGKSDNQNHALIFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEELNVEQVNPYAPGLRYEEQTTNHPVAIVGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLSQIGGKLHYGHPDFINATFMTTRGGVSKAQKGLHLNEDIYAGMNAMLRGGRIKHCEYYQCGKGRDLGFGTILNFTTKIGAGMGEQMLSREYYYLGTQLPVDRFLTFYYAHPGFHLNNLFIQLSLQMFMLTLVNLSSLAHESIMCIYDRNKPKTDVLVPIGCYNFQPAVDWVRRYTLSIFIVFWIAFVPIVVQELIERGLWKATQRFFCHLLSLSPMFEVFAGQIYSSALLSDLAIGGARYISTGRGFATSRIPFSILYSRFAGSAIYMGARSMLMLLFGTVAHWQAPLLWFWASLSSLIFAPFVFNPHQFAWEDFFLDYRDYIRWLSRGNNQYHRNSWIGYVRMSRARITGFKRKLVGDESEKAAGDASRAHRTNLIMAEIIPCAIYAAGCFIAFTFINAQTGVKTTDDDRVNSVLRIIICTLAPIAVNLGVLFFCMGMSCCSGPLFGMCCKKTGSVMAGIAHGVAVIVHIAFFIVMWVLESFNFVRMLIGVVTCIQCQRLIFHCMTALMLTREFKNDHANTAFWTGKWYGKGMGYMAWTQPSRELTAKVIELSEFAADFVLGHVILICQLPLIIIPKIDKFHSIMLFWLKPSRQIRPPIYSLKQTRLRKRMVKKYCSLYFLVLAIFAGCIIGPAVASAKIHKHIGDSLDGVVHNLFQPINTTNNDTGSQMSTYQSHYYTHTPSLKTWSTIK	Clinical trial	Pfizer. Product Development Pipeline. March 31 2009.	25	.	.	.	.	.	.	.	.	.	.	sce00500:Starch and sucrose metabolism; sce04011:MAPK signaling pathway - yeast	.	YEAST:YLR342W-MON	P38631
TT0SFXH	"Fungal 1,3-beta-glucan synthase (Fung GSC2)"	P40989	FKS2_YEAST	Hexosyltransferase	GSC2	Fung GSC2	"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."	EC 2.4.1.34	.	MSYNDPNLNGQYYSNGDGTGDGNYPTYQVTQDQSAYDEYGQPIYTQNQLDDGYYDPNEQYVDGTQFPQGQDPSQDQGPYNNDASYYNQPPNMMNPSSQDGENFSDFSSYGPPSGTYPNDQYTPSQMSYPDQDGSSGASTPYGNGVVNGNGQYYDPNAIEMALPNDPYPAWTADPQSPLPIEQIEDIFIDLTNKFGFQRDSMRNMFDHFMTLLDSRSSRMSPEQALLSLHADYIGGDTANYKKWYFAAQLDMDDEIGFRNMKLGKLSRKARKAKKKNKKAMQEASPEDTEETLNQIEGDNSLEAADFRWKSKMNQLSPFEMVRQIALFLLCWGEANQVRFTPECLCFIYKCASDYLDSAQCQQRPDPLPEGDFLNRVITPLYRFIRSQVYEIVDGRYVKSEKDHNKVIGYDDVNQLFWYPEGIAKIVMEDGTRLIDLPAEERYLKLGEIPWDDVFFKTYKETRSWLHLVTNFNRIWIMHISVYWMYCAYNAPTFYTHNYQQLVDNQPLAAYKWATAALGGTVASLIQVAATLCEWSFVPRKWAGAQHLSRRFWFLCVIMGINLGPVIFVFAYDKDTVYSTAAHVVGAVMFFVAVATLVFFSVMPLGGLFTSYMKKSTRSYVASQTFTASFAPLHGLDRWMSYLVWVTVFAAKYAESYFFLILSLRDPIRILSTTSMRCTGEYWWGNKICKVQPKIVLGLMIATDFILFFLDTYLWYIVVNTVFSVGKSFYLGISILTPWRNIFTRLPKRIYSKILATTDMEIKYKPKVLISQIWNAIIISMYREHLLAIDHVQKLLYHQVPSEIEGKRTLRAPTFFVSQDDNNFETEFFPRDSEAERRISFFAQSLSTPIPEPLPVDNMPTFTVLTPHYAERILLSLREIIREDDQFSRVTLLEYLKQLHPVEWDCFVKDTKILAEETAAYENNEDEPEKEDALKSQIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTISGFMNYSRAIKLLYRVENPEIVQMFGGNADGLERELEKMARRKFKFLVSMQRLAKFKPHELENAEFLLRAYPDLQIAYLDEEPPLNEGEEPRIYSALIDGHCEILENGRRRPKFRVQLSGNPILGDGKSDNQNHALIFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEELGIEQIHPYTPGLKYEDQSTNHPVAIVGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLAQIGGKLHYGHPDFINATFMTTRGGVSKAQKGLHLNEDIYAGMNAVLRGGRIKHCEYYQCGKGRDLGFGTILNFTTKIGAGMGEQMLSREYYYLGTQLPIDRFLTFYYAHPGFHLNNLFIQLSLQMFMLTLVNLHALAHESILCVYDRDKPITDVLYPIGCYNFHPAIDWVRRYTLSIFIVFWIAFVPIVVQELIERGLWKATQRFFRHILSLSPMFEVFAGQIYSSALLSDIAVGGARYISTGRGFATSRIPFSILYSRFAGSAIYMGSRSMLMLLFGTVAHWQAPLLWFWASLSALIFAPFIFNPHQFAWEDFFLDYRDYIRWLSRGNNKYHRNSWIGYVRMSRSRVTGFKRKLVGDESEKSAGDASRAHRTNLIMAEIIPCAIYAAGCFIAFTFINAQTGVKTTDEDRVNSTLRIIICTLAPIVIDIGVLFFCMGLSCCSGPLLGMCCKKTGSVMAGIAHGIAVVVHIVFFIVMWVLEGFSFVRMLIGVVTCIQCQRLIFHCMTVLLLTREFKNDHANTAFWTGKWYSTGLGYMAWTQPTRELTAKVIELSEFAADFVLGHVILIFQLPVICIPKIDKFHSIMLFWLKPSRQIRPPIYSLKQARLRKRMVRRYCSLYFLVLIIFAGCIVGPAVASAHVPKDLGSGLTGTFHNLVQPRNVSNNDTGSQMSTYKSHYYTHTPSLKTWSTIK	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	sce00500:Starch and sucrose metabolism; sce04011:MAPK signaling pathway - yeast	.	YEAST:YGR032W-MON	P40989
TTVO9RI	Fungal Probable histone deacetylase HOS2 (Fung HOS2)	P53096	HOS2_YEAST	.	.	Fung HOS2	"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."	EC 3.5.1.98	.	MSGTFSYDVKTKENEPLFEFNSAYSPRVSYHFNSKVSHYHYGVKHPMKPFRLMLTDHLVSSYGLHKIMDLYETRSATRDELLQFHSEDYVNFLSKVSPENANKLPRGTLENFNIGDDCPIFQNLYDYTTLYTGASLDATRKLINNQSDIAINWSGGLHHAKKNSPSGFCYVNDIVLSILNLLRYHPRILYIDIDLHHGDGVQEAFYTTDRVFTLSFHKYNGEFFPGTGDLTEIGCDKGKHFALNVPLEDGIDDDSYINLFKSIVDPLIMTFKPTLIVQQCGADSLGHDRLGCFNLNIKAHGECVKFVKSFGLPMLVVGGGGYTPRNVSRLWTYETGILNDVLLPEDIPEDIPFRDSFGPDYSLYPMLDDLYENKNSKKLLEDIRIRCLENIRYLQGAPSVRMDAECIPTQDISALTEEEDKIIQEMNEETEADSSNRLEEMEKENSGLIAFS	Clinical trial	"Activity of MGCD290, a Hos2 histone deacetylase inhibitor, in combination with azole antifungals against opportunistic fungal pathogens. J Clin Microbiol. 2009 Dec;47(12):3797-804."	.	.	.	.	.	.	.	.	.	.	.	.	R-SCE-3214815: HDACs deacetylate histones	YEAST:G3O-30675-MON	P53096
TTBZHDM	Fungal Isoleucyl t-RNA synthetase (Fung ILS1)	P09436	SYIC_YEAST	Carbon-oxygen ligase	"Fung Isoleucyl-tRNA synthetase; Fung Isoleucine--tRNA ligase, cytoplasmic; Fung IleRS"	Fung ILS1	Has aminoacyl-tRNA editing and isoleucine-tRNA ligase activity.	EC 6.1.1.5	.	MSESNAHFSFPKEEEKVLSLWDEIDAFHTSLELTKDKPEFSFFDGPPFATGTPHYGHILASTIKDIVPRYATMTGHHVERRFGWDTHGVPIEHIIDKKLGITGKDDVFKYGLENYNNECRSIVMTYASDWRKTIGRLGRWIDFDNDYKTMYPSFMESTWWAFKQLHEKGQVYRGFKVMPYSTGLTTPLSNFEAQQNYKDVNDPAVTIGFNVIGQEKTQLVAWTTTPWTLPSNLSLCVNADFEYVKIYDETRDRYFILLESLIKTLYKKPKNEKYKIVEKIKGSDLVGLKYEPLFPYFAEQFHETAFRVISDDYVTSDSGTGIVHNAPAFGEEDNAACLKNGVISEDSVLPNAIDDLGRFTKDVPDFEGVYVKDADKLIIKYLTNTGNLLLASQIRHSYPFCWRSDTPLLYRSVPAWFVRVKNIVPQMLDSVMKSHWVPNTIKEKRFANWIANARDWNVSRNRYWGTPIPLWVSDDFEEVVCVGSIKELEELTGVRNITDLHRDVIDKLTIPSKQGKGDLKRIEEVFDCWFESGSMPYASQHYPFENTEKFDERVPANFISEGLDQTRGWFYTLAVLGTHLFGSVPYKNVIVSGIVLAADGRKMSKSLKNYPDPSIVLNKYGADALRLYLINSPVLKAESLKFKEEGVKEVVSKVLLPWWNSFKFLDGQIALLKKMSNIDFQYDDSVKSDNVMDRWILASMQSLVQFIHEEMGQYKLYTVVPKLLNFIDELTNWYIRFNRRRLKGENGVEDCLKALNSLFDALFTFVRAMAPFTPFLSESIYLRLKEYIPEAVLAKYGKDGRSVHFLSYPVVKKEYFDEAIETAVSRMQSVIDLGRNIREKKTISLKTPLKTLVILHSDESYLKDVEALKNYIIEELNVRDVVITSDEAKYGVEYKAVADWPVLGKKLKKDAKKVKDALPSVTSEQVREYLESGKLEVAGIELVKGDLNAIRGLPESAVQAGQETRTDQDVLIIMDTNIYSELKSEGLARELVNRIQKLRKKCGLEATDDVLVEYELVKDTIDFEAIVKEHFDMLSKTCRSDIAKYDGSKTDPIGDEEQSINDTIFKLKVFKL	Clinical trial	"Efficacy, plasma pharmacokinetics, and safety of icofungipen, an inhibitor of Candida isoleucyl-tRNA synthetase, in treatment of experimental disseminated candidiasis in persistently neutropenic rabbits. Antimicrob Agents Chemother. 2005 May;49(5):2084-92."	21	.	.	.	.	.	.	.	.	.	.	sce00970: Aminoacyl-tRNA biosynthesis	.	YEAST:G3O-28968-MON	P09436
TTSA20Z	Fungal Kexin-like serine endoprotease (Fung klse)	Q9UVD0	Q9UVD0_PNECA	Peptidase	Kexin-like serine endoprotease	Fung klse	"Cleave secretory proproteins to their active forms.  Required for N-Glycan processing, morphogenesis and virulence"	.	.	EPPAPPSQPEPPAPQPQPEPPAPPPQPEPPAPPPQPEPPAPPPQPEPPAPPSQPEPPAPPPQPEPPAPPPQPEPPAPPPKPQPEQKPTSITSSTFTTSSSKTKISTIRKASSTKTSSTTKTSTRPSPTEGTFTGSSASYLSFFEKRHLLLQMILLLFFFLFLSYSF	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT6WCPZ	Fungal Laccase (Fung lcc1)	Q12570	LAC1_BOTFU	Diphenol donor oxidoreductase	lcc1; Urishiol oxidase; Fragment; Diphenol oxidase; Benzenediol:oxygen oxidoreductase	Fung lcc1	Lignin degradation and detoxification of lignin-derived products.	EC 1.10.3.2	.	MKNSFFSSLAKFASLSLAFALPTAEVIPSALEERQSCANTATTRSCWGQYSASTNSYTTVPKTGYWLVVQNTTLSADGVSRPTLNFNGTIPGPQITADWGDDVIVHVTNKLTSNGTSIHWHGIRQLNNAQYDGVPGITQCPIAPGGTLTYKFHADNYGSSWYHSHFILQYGDGLFGPLVINGPATANYDVDLGMLFLNDWNHVPVQSLWDKAKTGAPPTLLTGLMNGTNTYNGAGKKFQTTFTPGLKYRIRVVNTAVDGHFQFSIDGHSFQVIAMDFVPIVPYNATSILVSIAQRYDIIVTANAAVGNYWIRAGWQTACSGNTNAANITGILRYTGSSSTADPTTTSTVTASTSCLDEPLASLVPFVPINPVASSIMKTTLTTGGGQWLFNGSSLLLNWTDPTLLTVLNSGNIWPTEYNVIPIESTTANKGWAVLAISGPNGPNHPIHLHGHDFWTLSQGTGAYTATTALNLVNPPRRDVMTLPTGGHLVIAFQIDNPGSWLMHCHIAWHASEGLALQFVESESSILPTIGTADVSTFQNTCAAWKAWTPTEPFPQDDSGI	Literature-reported	Laccase and melanin in the pathogenesis of Cryptococcus neoformans. Front Biosci. 1997 Nov 1;2:e99-107.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q12570
TT0K7WC	Fungal Glycosylphosphatidylinositol-aspartyl-protease (Fung MKC7)	P53379	MKC7_YEAST	Peptidase	Yapsin 2; MKC7; Glycosylphosphatidylinositol-anchored protein; GPI-anchored aspartyl protease	Fung MKC7	Cleaves proteins C-terminally to the most C-terminal basic residue. Can process the alpha-mating factor precursor. Required for cell wall integrity.	.	.	MKLSVLTFVVDALLVCSSIVDAGVTDFPSLPSNEVYVKMNFQKKYGSSFENALDDTKGRTRLMTRDDDYELVELTNQNSFYSVELDIGTPPQKVTVLVDTGSSDLWVTGSDNPYCSTKKKDTTGSSFKQVNKDALASVVESVFTEISYDTTIVTSEATATFDSTASTSQLIDCATYGTFNTSKSSTFNSNNTEFSIAYGDTTFASGTWGHDQLSLNDLNITGLSFAVANETNSTVGVLGIGLPGLESTYSGVSLSSVQKSYTYNNFPMVLKNSGVIKSTAYSLFANDSDSKHGTILFGAVDHGKYAGDLYTIPIINTLQHRGYKDPIQFQVTLQGLGTSKGDKEDNLTTLTTTKIPVLLDSGTTISYMPTELVKMLADQVGATYSSAYGYYIMDCIKEMEEESSIIFDFGGFYLSNWLSDFQLVTDSRSNICILGIAPQSDPTIILGDNFLANTYVVYDLDNMEISMAQANFSDDGEYIEIIESAVPSALKAPGYSSTWSTYESIVSGGNMFSTAANSSISYFASTSHSATSSSSSKGQKTQTSTTALSISKSTSSTSSTGMLSPTSSSSTRKENGGHNLNPPFFARFITAIFHHI	Literature-reported	Glycosylphosphatidylinositol-anchored proteins play an important role in the biogenesis of the Alzheimer's amyloid beta-protein. J Biol Chem. 1999 Sep 17;274(38):26810-4.	.	.	.	.	.	.	.	.	.	.	.	sce04011: MAPK signaling pathway - yeast	.	YEAST:G3O-29741-MON	P53379
TTS3H9L	Fungal Phosphatidylinositol 4-kinase PIK1 (Fung PIK1)	P39104	PIK1_YEAST	Kinase	PtdIns4kinase; Phosphatidylinositol 4kinase PIK1; PIK1; PI4kinase	Fung PIK1	"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."	EC 2.7.1.67	2JU0	MHKASSSKKSFDDTIELKKNEQLLKLINSSEFTLHNCVELLCKHSENIGIHYYLCQKLATFPHSELQFYIPQLVQVLVTMETESMALEDLLLRLRAENPHFALLTFWQLQALLTDLSTDPASYGFQVARRVLNNLQTNLFNTSSGSDKNVKIHENVAPALVLSSMIMSAIAFPQLSEVTKPLVESQGRRQKAFVFKLARSAMKDFTKNMTLKNTLLNKKTSRSKRVSSNRSSTPTSPIDLIDPIKTKEDASFRKSRHSEVKLDFDIVDDIGNQVFEERISSSIKLPKRKPKYLDNSYVHRTYDGKNINRDGSISNTAKALDGNKGDYISPKGRNDENNEIGNNEDETGGETEEDADALNSDHFTSSMPDLHNIQPRTSSASSASLEGTPKLNRTNSQPLSRQAFKNSKKANSSLSQEIDLSQLSTTSKIKMLKANYFRCETQFAIALETISQRLARVPTEARLSALRAELFLLNRDLPAEVDIPTLLPPNKKGKLHKLVTITANEAQVLNSAEKVPYLLLIEYLRDEFDFDPTSETNERLLKKISGNQGGLIFDLNYMNRKENNENRNESTLTSNNTRSSVYDSNSFNNGASRNEGLSSTSRSDSASTAHVRTEVNKEEDLGDMSMVKVRNRTDDEAYRNALVIQSAANVPILPDDSQDRSPELNFGSNLDEVLIENGINSKNIHSQTDALADQMRVSAVMLAQLDKSPQQLSESTKQIRAQIISSMKEVQDKFGYHDLEALHGMAGERKLENDLMTGGIDTSYLGEDWATKKERIRKTSEYGHFENWDLCSVIAKTGDDLRQEAFAYQMIQAMANIWVKEKVDVWVKRMKILITSANTGLVETITNAMSVHSIKKALTKKMIEDAELDDKGGIASLNDHFLRAFGNPNGFKYRRAQDNFASSLAAYSVICYLLQVKDRHNGNIMIDNEGHVSHIDFGFMLSNSPGSVGFEAAPFKLTYEYIELLGGVEGEAFKKFVELTKSSFKALRKYADQIVSMCEIMQKDNMQPCFDAGEQTSVQLRQRFQLDLSEKEVDDFVENFLIGKSLGSIYTRIYDQFQLITQGIYS	Literature-reported	Real-time nanoscale proteomic analysis of the novel multi-kinase pathway inhibitor rigosertib to measure the response to treatment of cancer. Expert Opin Investig Drugs. 2013 Nov;22(11):1495-509.	.	.	.	.	.	.	.	.	.	.	.	sce00562:Inositol phosphate metabolism; sce01100:Metabolic pathways; sce04070:Phosphatidylinositol signaling system	R-SCE-1660514: Synthesis of PIPs at the Golgi membrane	YEAST:YNL267W-MON	P39104
TTBZG7K	Fungal cAMP-dependent protein kinase (Fung pka1)	P40376	KAPB_SCHPO	Kinase	cAMP-dependent protein kinase catalytic subunit	Fung pka1	Has cAMP-dependent protein kinase and protein serine/threonine kinase activity. 	.	.	MDTTAVASKGSTNVGSSTDTLSTSASLHPSMNAGSVNEYSEQQRHGTNSFNGKPSVHDSVGSDASVSNGHNNHNESSLWTSGIPKALEEATKSKKPDSLVSTSTSGCASAHSVGYQNIDNLIPSPLPESASRSSSQSSHQRHSRDGRGELGSEHGERRSAMDGLRDRHIRKVRVSQLLDLQRRRIRPADHTTKDRYGIQDFNFLQTLGTGSFGRVHLVQSNHNRLYYAIKVLEKKKIVDMKQIEHTCDERYILSRVQHPFITILWGTFQDAKNLFMVMDFAEGGELFSLLRKCHRFPEKVAKFYAAEVILALDYLHHNQIVYRDLKPENLLLDRFGHLKIVDFGFAKRVSTSNCCTLCGTPDYLAPEIISLKPYNKAADWWSLGILIFEMLAGYPPFYSENPMKLYENILEGKVNYPSYFSPASIDLLSHLLQRDITCRYGNLKDGSMDIIMHPWFRDISWDKILTRKIEVPYVPPIQAGMGDSSQFDAYADVATDYGTSEDPEFTSIFKDF	Literature-reported	Extracellular catalytic subunit activity of the cAMP-dependent protein kinase in prostate cancer. Clin Cancer Res. 2000 Jun;6(6):2309-17.	.	.	.	.	.	.	.	.	.	.	.	spo04113: Meiosis - yeast; spo04138: Autophagy - yeast	R-SPO-163615: PKA activation; R-SPO-164378: PKA activation in glucagon signalling; R-SPO-180024: DARPP-32 events; R-SPO-432040: Vasopressin regulates renal water homeostasis via Aquaporins; R-SPO-442720: CREB1 phosphorylation through the activation of Adenylate Cyclase; R-SPO-5610787: Hedgehog 'off' state; R-SPO-9634597: GPER1 signaling; R-SPO-983231: Factors involved in megakaryocyte development and platelet production	.	P40376
TTV4J2X	Fungal Plasma membrane H(+)-ATPase (Fung pma)	Q01680	Q01680_PNECA	.	Plasma membrane H(+)-ATPase	Fung pma	"Essential to fungal cell physiology, being required for the formation of a large electrochemical proton gradient and the maintenance of intracellular pH."	.	.	DDIDALIDDLESQDGDQEDNIEDTEFQSQRQVPEELLATDTRIGLTSQEVINRRKKYGLNKMKEEKENMIIKFLMYFVGPIQFVMEAAAILAAGLQDWVEFGVICALLLLNAFVGFIQEFQAGSIVDELKKTLALKATVLRDGRLIDIEAEEVVPGDILQLEEGSIVPADGRIVTEEAYLQVDQSAITGESLAVDIHKGDSIYSSSVAKPGETFMVVTATGDRT	Literature-reported	The plasma membrane H(+)-ATPase of fungi. A candidate drug target Ann N Y Acad Sci. 1997 Nov 3;834:609-17.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT9XT7G	Fungal Pre-mRNA splicing factor PRP8 (Fung PRP8)	P33334	PRP8_YEAST	.	Prp8 intein; PRP8; Intein (PRP8)	Fung PRP8	"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."	.	6J6Q; 6J6N; 6J6H; 6J6G; 6EXN	MSGLPPPPPGFEEDSDLALPPPPPPPPGYEIEELDNPMVPSSVNEDTFLPPPPPPPSNFEINAEEIVDFTLPPPPPPPGLDELETKAEKKVELHGKRKLDIGKDTFVTRKSRKRAKKMTKKAKRSNLYTPKAEMPPEHLRKIINTHSDMASKMYNTDKKAFLGALKYLPHAILKLLENMPHPWEQAKEVKVLYHTSGAITFVNETPRVIEPVYTAQWSATWIAMRREKRDRTHFKRMRFPPFDDDEPPLSYEQHIENIEPLDPINLPLDSQDDEYVKDWLYDSRPLEEDSKKVNGTSYKKWSFDLPEMSNLYRLSTPLRDEVTDKNYYYLFDKKSFFNGKALNNAIPGGPKFEPLYPREEEEDYNEFNSIDRVIFRVPIRSEYKVAFPHLYNSRPRSVRIPWYNNPVSCIIQNDEEYDTPALFFDPSLNPIPHFIDNNSSLNVSNTKENGDFTLPEDFAPLLAEEEELILPNTKDAMSLYHSPFPFNRTKGKMVRAQDVALAKKWFLQHPDEEYPVKVKVSYQKLLKNYVLNELHPTLPTNHNKTKLLKSLKNTKYFQQTTIDWVEAGLQLCRQGHNMLNLLIHRKGLTYLHLDYNFNLKPTKTLTTKERKKSRLGNSFHLMRELLKMMKLIVDTHVQFRLGNVDAFQLADGIHYILNHIGQLTGIYRYKYKVMHQIRACKDLKHIIYYKFNKNLGKGPGCGFWQPAWRVWLNFLRGTIPLLERYIGNLITRQFEGRSNEIVKTTTKQRLDAYYDLELRNSVMDDILEMMPESIRQKKARTILQHLSEAWRCWKANIPWDVPGMPAPIKKIIERYIKSKADAWVSAAHYNRERIKRGAHVEKTMVKKNLGRLTRLWIKNEQERQRQIQKNGPEITPEEATTIFSVMVEWLESRSFSPIPFPPLTYKNDTKILVLALEDLKDVYASKVRLNASEREELALIEEAYDNPHDTLNRIKKYLLTQRVFKPVDITMMENYQNISPVYSVDPLEKITDAYLDQYLWYEADQRKLFPNWIKPSDSEIPPLLVYKWTQGINNLSEIWDVSRGQSAVLLETTLGEMAEKIDFTLLNRLLRLIVDPNIADYITAKNNVVINFKDMSHVNKYGLIRGLKFASFIFQYYGLVIDLLLLGQERATDLAGPANNPNEFMQFKSKEVEKAHPIRLYTRYLDRIYMLFHFEEDEGEELTDEYLAENPDPNFENSIGYNNRKCWPKDSRMRLIRQDVNLGRAVFWEIQSRVPTSLTSIKWENAFVSVYSKNNPNLLFSMCGFEVRILPRQRMEEVVSNDEGVWDLVDERTKQRTAKAYLKVSEEEIKKFDSRIRGILMASGSTTFTKVAAKWNTSLISLFTYFREAIVATEPLLDILVKGETRIQNRVKLGLNSKMPTRFPPAVFYTPKELGGLGMISASHILIPASDLSWSKQTDTGITHFRAGMTHEDEKLIPTIFRYITTWENEFLDSQRVWAEYATKRQEAIQQNRRLAFEELEGSWDRGIPRISTLFQRDRHTLAYDRGHRIRREFKQYSLERNSPFWWTNSHHDGKLWNLNAYRTDVIQALGGIETILEHTLFKGTGFNSWEGLFWEKASGFEDSMQFKKLTHAQRTGLSQIPNRRFTLWWSPTINRANVYVGFLVQLDLTGIFLHGKIPTLKISLIQIFRAHLWQKIHESIVFDICQILDGELDVLQIESVTKETVHPRKSYKMNSSAADITMESVHEWEVSKPSLLHETNDSFKGLITNKMWFDVQLRYGDYDSHDISRYVRAKFLDYTTDNVSMYPSPTGVMIGIDLAYNMYDAYGNWFNGLKPLIQNSMRTIMKANPALYVLRERIRKGLQIYQSSVQEPFLNSSNYAELFNNDIKLFVDDTNVYRVTVHKTFEGNVATKAINGCIFTLNPKTGHLFLKIIHTSVWAGQKRLSQLAKWKTAEEVSALVRSLPKEEQPKQIIVTRKAMLDPLEVHMLDFPNIAIRPTELRLPFSAAMSIDKLSDVVMKATEPQMVLFNIYDDWLDRISSYTAFSRLTLLLRALKTNEESAKMILLSDPTITIKSYHLWPSFTDEQWITIESQMRDLILTEYGRKYNVNISALTQTEIKDIILGQNIKAPSVKRQKMAELEAARSEKQNDEEAAGASTVMKTKTINAQGEEIVVVASADYESQTFSSKNEWRKSAIANTLLYLRLKNIYVSADDFVEEQNVYVLPKNLLKKFIEISDVKIQVAAFIYGMSAKDHPKVKEIKTVVLVPQLGHVGSVQISNIPDIGDLPDTEGLELLGWIHTQTEELKFMAASEVATHSKLFADKKRDCIDISIFSTPGSVSLSAYNLTDEGYQWGEENKDIMNVLSEGFEPTFSTHAQLLLSDRITGNFIIPSGNVWNYTFMGTAFNQEGDYNFKYGIPLEFYNEMHRPVHFLQFSELAGDEELEAEQIDVFS	Literature-reported	Prp8 intein in fungal pathogens: target for potential antifungal drugs. FEBS Lett. 2004 Aug 13;572(1-3):46-50.	.	.	.	.	.	.	.	.	.	.	.	sce03040: Spliceosome	.	YEAST:G3O-31199-MON	P33334
TTC4SOT	Fungal Pyridoxin biosynthesis pyroA (Fung pyroA)	Q9UW83	PDX1_EMENI	.	pyroA; Pdx1 homolog	Fung pyroA	"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."	EC 4.3.3.6	.	MAATNGASNDFTVKAGLAQMLKGGVIMDVVNAEQARIAEEAGAAAVMALERVPADIRAQGGVARMSDPSMIKEIMEAVTIPVMAKARIGHFVECQILEAIGVDYIDESEVLTPADNLYHVTKHNFKAPFVCGCRNLGEALRRISEGAAMIRTKGEAGTGDVVEAVKHMRTVNAEIARARAILQSSPDPEPELRAYARELEAPYELLREAAEKGRLPVVNFAAGGVATPADAALMMQLGCDGVFVGSGIFKSGDAKKRAKAIVQAVTHYKDPKVLAEVSQGLGEAMVGINVSHMKDEDKLAKRGW	Literature-reported	Sequence analysis of an exceptionally conserved operon suggests enzymes for a new link between histidine and purine biosynthesis. Mol Microbiol. 1997 Apr;24(2):443-5.	.	.	.	.	.	.	.	.	.	.	.	ani00750: Vitamin B6 metabolism; ani01100: Metabolic pathways; ani01240: Biosynthesis of cofactors	.	.	Q9UW83
TT64EPS	Fungal Scytalone dehydratase (Fung SDH1)	P56221	SCYD_MAGO7	Alpha-carbonic anhydrase	SDH1	Fung SDH1	Catalyzes two steps in melanin biosynthesis. From scytalone they are two dehydration steps and one reduction step to yield melanin.	EC 4.2.1.94	7STD; 6STD; 5STD; 4STD; 3STD	MGSQVQKSDEITFSDYLGLMTCVYEWADSYDSKDWDRLRKVIAPTLRIDYRSFLDKLWEAMPAEEFVGMVSSKQVLGDPTLRTQHFIGGTRWEKVSEDEVIGYHQLRVPHQRYKDTTMKEVTMKGHAHSANLHWYKKIDGVWKFAGLKPDIRWGEFDFDRIFEDGRETFGDK	Literature-reported	Enzymatic characterization of scytalone dehydratase Val75Met variant found in melanin biosynthesis dehydratase inhibitor (MBI-D) resistant strains of the rice blast fungus. Biosci Biotechnol Biochem.2004 Mar;68(3):615-21.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P56221
TT2OW84	Fungal Pyridoxin biosynthesis protein SNZ1 (Fung SNZ1)	Q03148	SNZ1_YEAST	.	SNZ1; PDX1 homolog 1; Fung P35	Fung SNZ1	"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."	EC 4.3.3.6	3O07; 3O06; 3O05; 3FEM	MTGEDFKIKSGLAQMLKGGVIMDVVTPEQAKIAEKSGACAVMALESIPADMRKSGKVCRMSDPKMIKDIMNSVSIPVMAKVRIGHFVEAQIIEALEVDYIDESEVLTPADWTHHIEKDKFKVPFVCGAKDLGEALRRINEGAAMIRTKGEAGTGDVSEAVKHIRRITEEIKACQQLKSEDDIAKVAEEMRVPVSLLKDVLEKGKLPVVNFAAGGVATPADAALLMQLGCDGVFVGSGIFKSSNPVRLATAVVEATTHFDNPSKLLEVSSDLGELMGGVSIESISHASNGVRLSEIGW	Literature-reported	Sequence analysis of an exceptionally conserved operon suggests enzymes for a new link between histidine and purine biosynthesis. Mol Microbiol. 1997 Apr;24(2):443-5.	.	.	.	.	.	.	.	.	.	.	.	sce00750: Vitamin B6 metabolism; sce01100: Metabolic pathways; sce01240: Biosynthesis of cofactors	.	MetaCyc:G3O-32796-MON; YEAST:G3O-32796-MON	Q03148
TTH567K	Fungal GDP-mannose transporter (Fung VRG4)	P40107	GMT1_YEAST	.	VRG4 gene; VRG4; Golgi GDP-mannose transporter	Fung VRG4	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.	.	5OGK; 5OGE	MSELKTGHAGHNPWASVANSGPISILSYCGSSILMTVTNKFVVNLKDFNMNFVMLFVQSLVCTITLIILRILGYAKFRSLNKTDAKNWFPISFLLVLMIYTSSKALQYLAVPIYTIFKNLTIILIAYGEVLFFGGSVTSMELSSFLLMVLSSVVATWGDQQAVAAKAASLAEGAAGAVASFNPGYFWMFTNCITSALFVLIMRKRIKLTNFKDFDTMFYNNVLALPILLLFSFCVEDWSSVNLTNNFSNDSLTAMIISGVASVGISYCSGWCVRVTSSTTYSMVGALNKLPIALSGLIFFDAPRNFLSILSIFIGFLSGIIYAVAKQKKQQAQPLRK	Literature-reported	"Molecular and phenotypic analysis of CaVRG4, encoding an essential Golgi apparatus GDP-mannose transporter. J Bacteriol. 2002 Jan;184(1):29-42."	.	.	.	.	.	.	.	.	.	.	.	.	.	YEAST:G3O-30699-MON	P40107
TTYVI76	Fungal Protein kinase A (Fung ypkA)	Q56921	Q56921_YEREN	Kinase	Protein kinase A	Fung ypkA	Exists as a heterotetramer consisting of two regulatory subunits that bind and inactivate two catalytic subunits.	.	.	MKIMGTMSPSISLAKAHERISKHWQNPVGELNIEGKRYRIIDNQVVRLNPHSGFSLFREGVGKIFSGKMFSFSIARNLTDTLHAAQKTTSQELRSDIPNALSNLFGAKPQTELPLGWKGKPLSGAPDLEGMRVAETDKFAEGESHISIIETKDKQRLVAKIERSIAEGHLFAELEAYKHIYKTAGKHPNLANVHGMAVVPYGNRKEEALLMDEVDGWRCSDTLRSLADSWKQGKINSEAYWGTIKFIAHRLLDVTNHLAKAGIVHNDIKPGNVVFDRASGEPVVIDLGLHSRSGEQPKGFTESFKAPELGVGNLGASEKSDVFLVVSSLLHGIEGFEKDPEIKPNQGLRFITSEPAHVMDENGYPIHRPGIAGVETAYTRFITDILGVSADSRPDSNEARLHEFLSDGTIDEESAKQILKDTLTGEMSPLPTDVRRITPKKLRELSDLLRTHLSSAATKQLDMGVVLSDLDTMLVALDKAEREGGVDKDQLKSFNSLILKTYSVIGAYIKGREGDTKSSSTEVSPYHRSNFMLSIVEPSLQRIQKHLDQTHSSDIGSLMRAHKHLETLLEVLVTLSQQGQPVTSETYSFLNRLAEAKVTLSQQLNTLQQQQESAKAQLSILINRSGSWADVARQSLLRFDSTRPVVKFGTEQYTAIHRQMMAAHAAITLQEVSEFTDDMRNFTADSIPLLIQLGRSSLMDEHLVEQREKLRELTTIAERLNRLEREWM	Literature-reported	Joys of molecules. 2. Endeavors in chemical biology and medicinal chemistry. J Med Chem. 2005 Sep 8;48(18):5613-38. Address;	2	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTH9WF6	Dibasic-processing enzyme (Furin)	P09958	FURIN_HUMAN	Peptidase	Paired basic amino acid residuecleaving enzyme; Paired basic amino acid residue-cleaving enzyme; PCSK3; PACE; FUR; Dibasicprocessing enzyme	FURIN	"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."	EC 3.4.21.75	6HZD; 6HZC; 6HZB; 6HZA; 6HLE	MELRPWLLWVVAATGTLVLLAADAQGQKVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCEEGFSLHQKSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALTDCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAGLLPSHLPEVVAGLSCAFIVLVFVTVFLVLQLRSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL	Preclinical	"Design, synthesis, and structure-activity relationship studies of a potent PACE4 inhibitor. J Med Chem. 2014 Jan 9;57(1):98-109."	0	EC:3.4	Peptidase	peptidase S8 family. Furin subfamily.	3.4.21.75 	Acting on peptide bonds (peptidases)	Proprotein convertase P-domain; Subtilase family; Peptidase S8 pro-domain	PF01483; PF00082; PF16470	PF01483; P_proprotein; PF00082; Peptidase_S8; PF16470; S8_pro-domain	.	.	hsa03250: Viral life cycle - HIV-1	R-HSA-1181150: Signaling by NODAL; R-HSA-1442490: Collagen degradation; R-HSA-1566948: Elastic fibre formation; R-HSA-1592389: Activation of Matrix Metalloproteinases; R-HSA-159782: Removal of aminoterminal propeptides from gamma-carboxylated proteins; R-HSA-167060: NGF processing; R-HSA-171286: Synthesis and processing of ENV and VPU; R-HSA-186797: Signaling by PDGF; R-HSA-1912420: Pre-NOTCH Processing in Golgi; R-HSA-2173789: TGF-beta receptor signaling activates SMADs; R-HSA-5210891: Uptake and function of anthrax toxins; R-HSA-6809371: Formation of the cornified envelope; R-HSA-8963889: Assembly of active LPL and LIPC lipase complexes; R-HSA-9662834: CD163 mediating an anti-inflammatory response; R-HSA-9679191: Potential therapeutics for SARS; R-HSA-9694614: Attachment and Entry; R-HSA-977225: Amyloid fiber formation	.	P09958
TTUD6MS	HUMAN dibasic-processing enzyme (Furin)	P09958	FURIN_HUMAN	Peptidase	Paired basic amino acid residuecleaving enzyme; Paired basic amino acid residue-cleaving enzyme; PCSK3; PACE; FUR; Dibasicprocessing enzyme	FURIN	"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."	EC 3.4.21.75	6HZD; 6HZC; 6HZB; 6HZA; 6HLE	MELRPWLLWVVAATGTLVLLAADAQGQKVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCEEGFSLHQKSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALTDCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAGLLPSHLPEVVAGLSCAFIVLVFVTVFLVLQLRSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL	.	Coronaviruses - drug discovery and therapeutic options. Nat Rev Drug Discov. 2016 May;15(5):327-47.	0	EC:3.4	Peptidase	peptidase S8 family. Furin subfamily.	3.4.21.75 	Acting on peptide bonds (peptidases)	Proprotein convertase P-domain; Subtilase family; Peptidase S8 pro-domain	PF01483; PF00082; PF16470	PF01483; P_proprotein; PF00082; Peptidase_S8; PF16470; S8_pro-domain	.	.	hsa03250: Viral life cycle - HIV-1	R-HSA-1181150: Signaling by NODAL; R-HSA-1442490: Collagen degradation; R-HSA-1566948: Elastic fibre formation; R-HSA-1592389: Activation of Matrix Metalloproteinases; R-HSA-159782: Removal of aminoterminal propeptides from gamma-carboxylated proteins; R-HSA-167060: NGF processing; R-HSA-171286: Synthesis and processing of ENV and VPU; R-HSA-186797: Signaling by PDGF; R-HSA-1912420: Pre-NOTCH Processing in Golgi; R-HSA-2173789: TGF-beta receptor signaling activates SMADs; R-HSA-5210891: Uptake and function of anthrax toxins; R-HSA-6809371: Formation of the cornified envelope; R-HSA-8963889: Assembly of active LPL and LIPC lipase complexes; R-HSA-9662834: CD163 mediating an anti-inflammatory response; R-HSA-9679191: Potential therapeutics for SARS; R-HSA-9694614: Attachment and Entry; R-HSA-977225: Amyloid fiber formation	.	P09958
TTKGYZ9	RNA-binding protein FUS messenger RNA (FUS mRNA)	P35637	FUS_HUMAN	mRNA target	75 kDa DNA-pairing protein (mRNA); Oncogene FUS (mRNA); Oncogene TLS (mRNA); POMp75 (mRNA); Translocated in liposarcoma protein (mRNA)	FUS	"DNA/RNA-binding protein that plays a role in various cellular processes such as transcription regulation, RNA splicing, RNA transport, DNA repair and damage response (PubMed:27731383). Binds to nascent pre-mRNAs and acts as a molecular mediator between RNA polymerase II and U1 small nuclear ribonucleoprotein thereby coupling transcription and splicing (PubMed:26124092). Binds also its own pre-mRNA and autoregulates its expression; this autoregulation mechanism is mediated by non-sense-mediated decay (PubMed:24204307). Plays a role in DNA repair mechanisms by promoting D-loop formation and homologous recombination during DNA double-strand break repair (PubMed:10567410). In neuronal cells, plays crucial roles in dendritic spine formation and stability, RNA transport, mRNA stability and synaptic homeostasis (By similarity). {ECO:0000250|UniProtKB:P56959, ECO:0000269|PubMed:10567410, ECO:0000269|PubMed:24204307, ECO:0000269|PubMed:26124092, ECO:0000269|PubMed:27731383}."	.	2LA6;2LCW;4FDD;4FQ3;5W3N;5XRR;5XSG;5YVG;5YVH;5YVI;6BWZ;6BXV;6BZP;6G99;6GBM;6KJ1;6KJ2;6KJ3;6KJ4;6SNJ;6XFM;7CYL;7VQQ	MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYSQSTDTSGYGQSSYSSYGQSQNTGYGTQSTPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQDRGGRGRGGSGGGGGGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKEFSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGGGQQRAGDWKCPNPTCENMNFSWRNECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY	Clinical trial	Antisense oligonucleotide silencing of FUS expression as a therapeutic approach in amyotrophic lateral sclerosis. Nat Med. 2022 Jan;28(1):104-116.	.	.	.	.	.	.	.	.	.	.	.	hsa:2521	R-HSA-72163;R-HSA-72203;	.	P35637;
TTUPAD7	Galactoside 3(4)-L-fucosyltransferase (FUT3)	P21217	FUT3_HUMAN	Hexosyltransferase	Lewis FT; Fucosyltransferase III; Fucosyltransferase 3; FucTIII; FUT3; Blood group Lewis alpha4fucosyltransferase	FUT3	"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."	EC 2.4.1.65	.	MDPLGAAKPQWPWRRCLAALLFQLLVAVCFFSYLRVSRDDATGSPRAPSGSSRQDTTPTRPTLLILLWTWPFHIPVALSRCSEMVPGTADCHITADRKVYPQADTVIVHHWDIMSNPKSRLPPSPRPQGQRWIWFNLEPPPNCQHLEALDRYFNLTMSYRSDSDIFTPYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWKPDSARVRYYQSLQAHLKVDVYGRSHKPLPKGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPKDLARYLQELDKDHARYLSYFRWRETLRPRSFSWALDFCKACWKLQQESRYQTVRSIAAWFT	Clinical trial	"A phase II trial with anti-Lewis-Y monoclonal antibody (hu3S193) for the treatment of platinum resistant/refractory ovarian, fallopian tube and primary peritoneal carcinoma. Gynecol Oncol. 2015 Aug;138(2):272-7."	21	.	.	.	.	.	.	.	.	.	.	hsa00601: Glycosphingolipid biosynthesis - lacto and neolacto series; hsa01100: Metabolic pathways	R-HSA-9037629: Lewis blood group biosynthesis; R-HSA-975578: Reactions specific to the complex N-glycan synthesis pathway	MetaCyc:HS10249-MON	P21217
TTNV1KZ	Fucosyltransferase IV (CD15)	P22083	FUT4_HUMAN	Glycosyltransferases	"Galactoside 3-L-fucosyltransferase; Fucosyltransferase 4; FucT-IV; Fuc-TIV; FCT3A; ELFT; ELAM-1 ligand fucosyltransferase; Alpha-(1,3)-fucosyltransferase 4"	FUT4	"May catalyze alpha-1,3 glycosidic linkages involved in the expression of Lewis X/SSEA-1 and VIM-2 antigens."	EC 2.4.1.-	.	MRRLWGAARKPSGAGWEKEWAEAPQEAPGAWSGRLGPGRSGRKGRAVPGWASWPAHLALAARPARHLGGAGQGPRPLHSGTAPFHSRASGERQRRLEPQLQHESRCRSSTPADAWRAEAALPVRAMGAPWGSPTAAAGGRRGWRRGRGLPWTVCVLAAAGLTCTALITYACWGQLPPLPWASPTPSRPVGVLLWWEPFGGRDSAPRPPPDCRLRFNISGCRLLTDRASYGEAQAVLFHHRDLVKGPPDWPPPWGIQAHTAEEVDLRVLDYEEAAAAAEALATSSPRPPGQRWVWMNFESPSHSPGLRSLASNLFNWTLSYRADSDVFVPYGYLYPRSHPGDPPSGLAPPLSRKQGLVAWVVSHWDERQARVRYYHQLSQHVTVDVFGRGGPGQPVPEIGLLHTVARYKFYLAFENSQHLDYITEKLWRNALLAGAVPVVLGPDRANYERFVPRGAFIHVDDFPSASSLASYLLFLDRNPAVYRRYFHWRRSYAVHITSFWDEPWCRVCQAVQRAGDRPKSIRNLASWFER	Successful	2004 approvals: the demise of the blockbuster. Nat Rev Drug Discov. 2005 Feb;4(2):93-4.	34	EC:2.4	.	glycosyltransferase 10 family.	2.4.1.-	Glycosyltransferases	"Fucosyltransferase, N-terminal; Glycosyltransferase family 10 (fucosyltransferase) C-term"	PF17039; PF00852	PF17039; Glyco_tran_10_N; PF00852; Glyco_transf_10	.	.	hsa00515: Mannose type O-glycan biosynthesis; hsa00601: Glycosphingolipid biosynthesis - lacto and neolacto series; hsa01100: Metabolic pathways	R-HSA-9037629: Lewis blood group biosynthesis	MetaCyc:HS07593-MON	P22083
TT2B9KF	Fyn tyrosine protein kinase (FYN)	P06241	FYN_HUMAN	Kinase	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	FYN	"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."	EC 2.7.10.2	6IPZ; 6IPY; 6EDF; 4ZNX; 4U1P	MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQSFLEDYFTATEPQYQPGENL	Successful	A comparison of physicochemical property profiles of marketed oral drugs and orally bioavailable anti-cancer protein kinase inhibitors in clinical development. Curr Top Med Chem. 2007;7(14):1408-22.	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. SRC subfamily.	2.7.10.2	Transferring phosphorus-containing groups	Protein tyrosine kinase; SH2 domain; SH3 domain	PF07714; PF00017; PF00018	PF07714; Pkinase_Tyr; PF00017; SH2; PF00018; SH3_1	.	.	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	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	.	P06241
TTP1S2F	Frizzled-10 (FZD10)	Q9ULW2	FZD10_HUMAN	.	Fz-10; hFz10; FzE7; DE   AltName: CD_antigen=CD350	FZD10	"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)."	.	.	MQRPGPRLWLVLQVMGSCAAISSMDMERPGDGKCQPIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHGHLRFFLCSLYAPMCTEQVSTPIPACRVMCEQARLKCSPIMEQFNFKWPDSLDCRKLPNKNDPNYLCMEAPNNGSDEPTRGSGLFPPLFRPQRPHSAQEHPLKDGGPGRGGCDNPGKFHHVEKSASCAPLCTPGVDVYWSREDKRFAVVWLAIWAVLCFFSSAFTVLTFLIDPARFRYPERPIIFLSMCYCVYSVGYLIRLFAGAESIACDRDSGQLYVIQEGLESTGCTLVFLVLYYFGMASSLWWVVLTLTWFLAAGKKWGHEAIEANSSYFHLAAWAIPAVKTILILVMRRVAGDELTGVCYVGSMDVNALTGFVLIPLACYLVIGTSFILSGFVALFHIRRVMKTGGENTDKLEKLMVRIGLFSVLYTVPATCVIACYFYERLNMDYWKILAAQHKCKMNNQTKTLDCLMAASIPAVEIFMVKIFMLLVVGITSGMWIWTSKTLQSWQQVCSRRLKKKSRRKPASVITSGGIYKKAQHPQKTHHGKYEIPAQSPTCV	Clinical trial	"A first-in-human study investigating biodistribution, safety and recommended dose of a new radiolabeled MAb targeting FZD10 in metastatic synovial sarcoma patients. BMC Cancer. 2018 Jun 8;18(1):646."	.	.	.	.	.	.	.	.	.	.	.	hsa04150: mTOR signaling pathway; hsa04310: Wnt signaling pathway; hsa04390: Hippo signaling pathway; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04916: Melanogenesis; hsa04934: Cushing syndrome; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05165: Human papillomavirus infection; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05217: Basal cell carcinoma; hsa05224: Breast cancer; hsa05225: Hepatocellular carcinoma; hsa05226: Gastric cancer	R-HSA-373080: Class B/2 (Secretin family receptors)	.	Q9ULW2
TTUQMO5	Frizzled-7 receptor (FZD7)	O75084	FZD7_HUMAN	GPCR frizzled	hFz7; FzE3; Fz7; Fz-7; Frizzled7; Frizzled-7	FZD7	"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."	.	6O3B; 6O3A; 6NE4; 6NE2; 5WBS	MRDPGAAAPLSSLGLCALVLALLGALSAGAGAQPYHGEKGISVPDHGFCQPISIPLCTDIAYNQTILPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLDQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDGSGGPGGGPTAYPTAPYLPDLPFTALPPGASDGRGRPAFPFSCPRQLKVPPYLGYRFLGERDCGAPCEPGRANGLMYFKEEERRFARLWVGVWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAHVAGFLLEDRAVCVERFSDDGYRTVAQGTKKEGCTILFMVLYFFGMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQVDGDLLSGVCYVGLSSVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVLACYFYEQAFREHWERTWLLQTCKSYAVPCPPGHFPPMSPDFTVFMIKYLMTMIVGITTGFWIWSGKTLQSWRRFYHRLSHSSKGETAV	Clinical trial	Wnt pathway inhibition via the targeting of Frizzled receptors results in decreased growth and tumorigenicity of human tumors. Proc Natl Acad Sci U S A. 2012 Jul 17;109(29):11717-22.	17	PF01534	GPCR frizzled	G-protein coupled receptor Fz/Smo family.	.	.	Frizzled/Smoothened family membrane region; Fz domain	PF01534; PF01392	PF01534; Frizzled; PF01392; Fz	.	.	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	R-HSA-373080:Class B/2 (Secretin family receptors); R-HSA-4086400:PCP/CE pathway	.	O75084
TTG0R8Z	GAP SH3 domain-binding protein 1 (G3BP1)	Q13283	G3BP1_HUMAN	Acid anhydride hydrolase	hDH VIII; Ras GTPase-activating protein-binding protein 1; G3BP-1; G3BP; ATP-dependent DNA helicase VIII	G3BP1	"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."	EC 3.6.4.12	5FW5; 4IIA; 4FCM; 4FCJ; 3Q90	MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQEDLRTFSWASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ	Literature-reported	The roles and mechanisms of G3BP1 in tumour promotion. J Drug Target. 2019 Mar;27(3):300-305.	.	EC:3.6	Acid anhydrides hydrolase	.	3.6.4.12 	Acting on acid anhydrides	"Nuclear transport factor 2 (NTF2) domain; RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)"	PF02136; PF00076	PF02136; NTF2; PF00076; RRM_1	.	.	.	R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses	.	Q13283
TTBQMJ8	Glucose-6-phosphatase (G6PC)	P35575	G6PC_HUMAN	Phosphoric monoester hydrolase	Glucose-6-phosphatase alpha; G6Pase-alpha; G6Pase; G6PT; G-6-Pase	G6PC	"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."	EC 3.1.3.9	.	MEEGMNVLHDFGIQSTHYLQVNYQDSQDWFILVSVIADLRNAFYVLFPIWFHLQEAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVLDTDYYSNTSVPLIKQFPVTCETGPGSPSGHAMGTAGVYYVMVTSTLSIFQGKIKPTYRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVVAGVLSGIAVAETFSHIHSIYNASLKKYFLITFFLFSFAIGFYLLLKGLGVDLLWTLEKAQRWCEQPEWVHIDTTPFASLLKNLGTLFGLGLALNSSMYRESCKGKLSKWLPFRLSSIVASLVLLHVFDSLKPPSQVELVFYVLSFCKSAVVPLASVSVIPYCLAQVLGQPHKKSL	Clinical trial	The antihyperglycemic effect of estrone sulfate in genetically obese-diabetic (ob/ob) mice is associated with reduced hepatic glucose-6-phosphatase. Horm Metab Res. 2001 Dec;33(12):721-6.	.	EC:3.1.3	Phosphoric monoester hydrolases	glucose-6-phosphatase family.	3.1.3.9	Acting on ester bonds	PAP2 superfamily	PF01569	PF01569; PAP2	.	.	hsa00010: Glycolysis / Gluconeogenesis; hsa00052: Galactose metabolism; hsa00500: Starch and sucrose metabolism; hsa01100: Metabolic pathways; hsa04068: FoxO signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04152: AMPK signaling pathway; hsa04910: Insulin signaling pathway; hsa04920: Adipocytokine signaling pathway; hsa04922: Glucagon signaling pathway; hsa04931: Insulin resistance; hsa04973: Carbohydrate digestion and absorption	"R-HSA-3274531: Glycogen storage disease type Ia (G6PC); R-HSA-70263: Gluconeogenesis; R-HSA-9615017: FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes"	MetaCyc:HS05538-MON	.
TTL5KSF	Glucose-6-phosphatase catalytic subunit 1 messenger RNA (G6PC1 mRNA)	P35575	G6PC1_HUMAN	mRNA target	Glucose-6-phosphatase (mRNA); G-6-Pase (mRNA); G6Pase (mRNA); Glucose-6-phosphatase alpha (mRNA); G6Pase-alpha (mRNA)	G6PC1	"Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production in the terminal step of glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels. {ECO:0000269|PubMed:10960498, ECO:0000269|PubMed:12093795, ECO:0000269|PubMed:15542400, ECO:0000269|PubMed:9332655, ECO:0000269|PubMed:9497333}."	EC 3.1.3.9	.	MEEGMNVLHDFGIQSTHYLQVNYQDSQDWFILVSVIADLRNAFYVLFPIWFHLQEAVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVLDTDYYSNTSVPLIKQFPVTCETGPGSPSGHAMGTAGVYYVMVTSTLSIFQGKIKPTYRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQVVAGVLSGIAVAETFSHIHSIYNASLKKYFLITFFLFSFAIGFYLLLKGLGVDLLWTLEKAQRWCEQPEWVHIDTTPFASLLKNLGTLFGLGLALNSSMYRESCKGKLSKWLPFRLSSIVASLVLLHVFDSLKPPSQVELVFYVLSFCKSAVVPLASVSVIPYCLAQVLGQPHKKSL	Clinical trial	"Clinical pipeline report, company report or official report of Moderna"	.	.	.	.	.	.	.	.	.	.	.	hsa:2538	R-HSA-3274531;R-HSA-70263;R-HSA-9615017;	MetaCyc:HS05538-MONOMER;	P35575;
TT7EV4P	Glucose-6-phosphatase 2 (G6PC2)	Q9NQR9	G6PC2_HUMAN	Phosphoric monoester hydrolase	IGRP; G6PC2	G6PC2	May hydrolyze glucose-6-phosphate to glucose in the endoplasmic reticulum. May be responsible for glucose production through glycogenolysis and gluconeogenesis.	EC 3.1.3.9	.	MDFLHRNGVLIIQHLQKDYRAYYTFLNFMSNVGDPRNIFFIYFPLCFQFNQTVGTKMIWVAVIGDWLNLIFKWILFGHRPYWWVQETQIYPNHSSPCLEQFPTTCETGPGSPSGHAMGASCVWYVMVTAALSHTVCGMDKFSITLHRLTWSFLWSVFWLIQISVCISRVFIATHFPHQVILGVIGGMLVAEAFEHTPGIQTASLGTYLKTNLFLFLFAVGFYLLLRVLNIDLLWSVPIAKKWCANPDWIHIDTTPFAGLVRNLGVLFGLGFAINSEMFLLSCRGGNNYTLSFRLLCALTSLTILQLYHFLQIPTHEEHLFYVLSFCKSASIPLTVVAFIPYSVHMLMKQSGKKSQ	Literature-reported	Identification of the beta cell antigen targeted by a prevalent population of pathogenic CD8+ T cells in autoimmune diabetes. Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8384-8.	.	.	.	.	.	.	.	.	.	.	.	hsa00010: Glycolysis / Gluconeogenesis; hsa00052: Galactose metabolism; hsa00500: Starch and sucrose metabolism; hsa01100: Metabolic pathways; hsa04068: FoxO signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04152: AMPK signaling pathway; hsa04910: Insulin signaling pathway; hsa04920: Adipocytokine signaling pathway; hsa04922: Glucagon signaling pathway; hsa04931: Insulin resistance; hsa04973: Carbohydrate digestion and absorption	R-HSA-70263: Gluconeogenesis	MetaCyc:HS14422-MON	Q9NQR9
TTKN8W0	Glucose-6-phosphate dehydrogenase (G6PD)	P11413	G6PD_HUMAN	CH-OH donor oxidoreductase	Glucose-6-phosphate 1-dehydrogenase	G6PD	"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."	EC 1.1.1.49	6.00E+08; 6.00E+07; 5UKW; 2BHL; 2BH9	MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSSDRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGKALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPIPYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL	Successful	"Glucose utilization and activity of glucose-6-phosphate dehydrogenase, isocitrate dehydrogenase and malate dehydrogenase in rat erythrocytes after treatment with tuberculostatic agents. Vopr Med Khim. 1986 Sep-Oct;32(5):32-5."	34	EC:1.1	Short-chain dehydrogenases reductases	glucose-6-phosphate dehydrogenase family.	1.1.1.49	Acting on the CH-OH group of donors	"Glucose-6-phosphate dehydrogenase, C-terminal domain; Glucose-6-phosphate dehydrogenase, NAD binding domain"	PF02781; PF00479	PF02781; G6PD_C; PF00479; G6PD_N	.	.	hsa00030:Pentose phosphate pathway; hsa00480:Glutathione metabolism; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa01200:Carbon metabolism; hsa05230:Central carbon metabolism in cancer	R-HSA-5628897:TP53 Regulates Metabolic Genes	MetaCyc:HS08467-MON	P11413
TTLPC70	Lysosomal alpha-glucosidase (GAA)	P10253	LYAG_HUMAN	Glycosylase	GAA; Aglucosidase alfa; Acid maltase	GAA	Essential for the degradation of glygogen to glucose in lysosomes.	EC 3.2.1.20	5NN8; 5NN6; 5NN5; 5NN4; 5NN3	MGVRHPPCSHRLLAVCALVSLATAALLGHILLHDFLLVPRELSGSSPVLEETHPAHQQGASRPGPRDAQAHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGAQMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLHFTIKDPANRRYEVPLETPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTTVAPLFFADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLALEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELENPPYVPGVVGGTLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTVPVEALGSLPPPPAAPREPAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQGPGLTTTESRQQPMALAVALTKGGEARGELFWDDGESLEVLERGAYTQVIFLARNNTIVNELVRVTSEGAGLQLQKVTVLGVATAPQQVLSNGVPVSNFTYSPDTKVLDICVSLLMGEQFLVSWC	Clinical trial	"Clinical pipeline report, company report or official report of BioMarin Pharma."	25	.	.	.	.	.	.	.	.	.	.	hsa00052:Galactose metabolism; hsa00500:Starch and sucrose metabolism; hsa01100:Metabolic pathways; hsa04142:Lysosome	R-HSA-5357609: Glycogen storage disease type II (GAA); R-HSA-6798695: Neutrophil degranulation; R-HSA-70221: Glycogen breakdown (glycogenolysis)	.	P10253
TTHCF4J	Alpha-glucosidase (GLA)	P10253; Q14697; Q8TET4	LYAG_HUMAN; GANAB_HUMAN; GANC_HUMAN	.	Maltase-glucoamylase; Maltase; Glucosidosucrase; Glucosidoinvertase; Glucoinvertase; Alpha-glucoside hydrolase; Alpha-glucopyranosidase; Alpha-D-glucoside glucohydrolase; Alpha-D-glucosidase; Alpha-1;4-glucosidase	GAA	Breaks down starch and disaccharides to glucose.	.	.	MGVRHPPCSHRLLAVCALVSLATAALLGHILLHDFLLVPRELSGSSPVLEETHPAHQQGASRPGPRDAQAHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGAQMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLHFTIKDPANRRYEVPLETPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTTVAPLFFADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLALEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELENPPYVPGVVGGTLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTVPVEALGSLPPPPAAPREPAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQGPGLTTTESRQQPMALAVALTKGGEARGELFWDDGESLEVLERGAYTQVIFLARNNTIVNELVRVTSEGAGLQLQKVTVLGVATAPQQVLSNGVPVSNFTYSPDTKVLDICVSLLMGEQFLVSWC	Clinical trial	Nitrogen-in-the-ring pyranoses and furanoses: structural basis of inhibition of mammalian glycosidases. J Med Chem. 1994 Oct 28;37(22):3701-6.	25	.	.	.	.	.	.	.	.	.	.	hsa00052: Galactose metabolism; hsa00500: Starch and sucrose metabolism; hsa01100: Metabolic pathways; hsa04142: Lysosome	R-HSA-5357609: Glycogen storage disease type II (GAA); R-HSA-6798695: Neutrophil degranulation; R-HSA-70221: Glycogen breakdown (glycogenolysis)	.	P10253
TTDCVZW	Gamma-aminobutyric acid B receptor (GABBR)	Q9UBS5; O75899	GABR1_HUMAN; GABR2_HUMAN	GPCR glutamate	Gamma-aminobutyric acid type B receptor; GPRC3; GABABR; GABA-BR; GABA-B-R; GABA-B receptor	GABBR1	"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."	.	.	MLLLLLLAPLFLRPPGAGGAQTPNATSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPHSERRAVYIGALFPMSGGWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKIYDPSINCTVDEMTEAVEGHITTEIVMLNPANTRSISNMTSQEFVEKLTKRLKRHPEETGGFQEAPLAYDAIWALALALNKTSGGGGRSGVRLEDFNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGSYKKIGYYDSTKDDLSWSKTDKWIGGSPPADQTLVIKTFRFLSQKLFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRNQFPFVCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDVLTLAIWQIVDPLHRTIETFAKEEPKEDIDVSILPQLEHCSSRKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPKMRRLITRGEWQSEAQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQLQSRQQLRSRRHPPTPPEPSGGLPRGPPEPPDRLSCDGSRVHLLYK	Successful	Interactions between dopamine and GABA in the control of ambulatory activity and neophobia in the mouse. Pharmacol Biochem Behav. 1998 Jan;59(1):239-47.	34	PF00003	GPCR glutamate	G-protein coupled receptor 3 family. GABA-B receptor subfamily.	.	.	7 transmembrane sweet-taste receptor of 3 GCPR; Receptor family ligand binding region; Gamma-aminobutyric acid type B receptor subunit 2 coiled-coil domain	PF00003; PF01094; PF18455	PF00003; 7tm_3; PF01094; ANF_receptor; PF18455; GBR2_CC	9.A.14.15.1	The G-protein-coupled receptor (GPCR) Family	hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04727:GABAergic synapse; hsa04915:Estrogen signaling pathway; hsa05032:Morphine addiction	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	.	Q9UBS5
TT1MPAY	GABA(A) receptor alpha-1 (GABRA1)	P14867	GBRA1_HUMAN	Ligand-gated ion channel	Gamma-aminobutyric acid receptor subunit alpha-1; GABA(A) receptor subunit alpha-1	GABRA1	"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)."	.	6I53; 6D6U; 6D6T; 6D1S; 6CDU	MRKSPGLSDCLWAWILLLSTLTGRSYGQPSLQDELKDNTTVFTRILDRLLDGYDNRLRPGLGERVTEVKTDIFVTSFGPVSDHDMEYTIDVFFRQSWKDERLKFKGPMTVLRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRITEDGTLLYTMRLTVRAECPMHLEDFPMDAHACPLKFGSYAYTRAEVVYEWTREPARSVVVAEDGSRLNQYDLLGQTVDSGIVQSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGYAWDGKSVVPEKPKKVKDPLIKKNNTYAPTATSYTPNLARGDPGLATIAKSATIEPKEVKPETKPPEPKKTFNSVSKIDRLSRIAFPLLFGIFNLVYWATYLNREPQLKAPTPHQ	Successful	"DrugBank: a knowledgebase for drugs, drug actions and drug targets. Nucleic Acids Res. 2008 Jan;36(Database issue):D901-6."	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction	R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation	.	P14867
TTBMV1G	GABA(A) receptor alpha-2 (GABRA2)	P47869	GBRA2_HUMAN	Neurotransmitter receptor	GABRA2; GABA-A receptor alpha 2; GABA(A)Gamma-aminobutyric-acid receptor alpha-2 subunit precursor receptor	GABRA2	"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."	.	.	MKTKLNIYNMQFLLFVFLVWDPARLVLANIQEDEAKNNITIFTRILDRLLDGYDNRLRPGLGDSITEVFTNIYVTSFGPVSDTDMEYTIDVFFRQKWKDERLKFKGPMNILRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRIQDDGTLLYTMRLTVQAECPMHLEDFPMDAHSCPLKFGSYAYTTSEVTYIWTYNASDSVQVAPDGSRLNQYDLLGQSIGKETIKSSTGEYTVMTAHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGWAWDGKSVVNDKKKEKASVMIQNNAYAVAVANYAPNLSKDPVLSTISKSATTPEPNKKPENKPAEAKKTFNSVSKIDRMSRIVFPVLFGTFNLVYWATYLNREPVLGVSP	Successful	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 405).	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction	R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation	.	P47869
TT37EDJ	GABA(A) receptor alpha-3 (GABRA3)	P34903	GBRA3_HUMAN	Neurotransmitter receptor	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	GABRA3	"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."	.	.	MIITQTSHCYMTSLGILFLINILPGTTGQGESRRQEPGDFVKQDIGGLSPKHAPDIPDDSTDNITIFTRILDRLLDGYDNRLRPGLGDAVTEVKTDIYVTSFGPVSDTDMEYTIDVFFRQTWHDERLKFDGPMKILPLNNLLASKIWTPDTFFHNGKKSVAHNMTTPNKLLRLVDNGTLLYTMRLTIHAECPMHLEDFPMDVHACPLKFGSYAYTTAEVVYSWTLGKNKSVEVAQDGSRLNQYDLLGHVVGTEIIRSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRSWAWEGKKVPEALEMKKKTPAAPAKKTSTTFNIVGTTYPINLAKDTEFSTISKGAAPSASSTPTIIASPKATYVQDSPTETKTYNSVSKVDKISRIIFPVLFAIFNLVYWATYVNRESAIKGMIRKQ	Successful	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 406).	34	TC=1.A.9	Ligand-gated ion channel	ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRA3 sub-subfamily. 	.	.	Neurotransmitter-gated ion-channel ligand binding domain; Neurotransmitter-gated ion-channel transmembrane region	PF02931; PF02932	PF02931; Neur_chan_LBD; PF02932; Neur_chan_memb	1.A.9.5.7	"The Neurotransmitter Receptor, Cys loop, Ligand-gated Ion Channel (LIC) Family"	hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction	R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation	.	P34903
TTNZPQ1	GABA(A) receptor alpha-5 (GABRA5)	P31644	GBRA5_HUMAN	Ligand-gated ion channel	GABRA5; GABAA alpha 5; GABA-A alpha-5	GABRA5	"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."	.	6A96; 5OJM; 5O8F	MDNGMFSGFIMIKNLLLFCISMNLSSHFGFSQMPTSSVKDETNDNITIFTRILDGLLDGYDNRLRPGLGERITQVRTDIYVTSFGPVSDTEMEYTIDVFFRQSWKDERLRFKGPMQRLPLNNLLASKIWTPDTFFHNGKKSIAHNMTTPNKLLRLEDDGTLLYTMRLTISAECPMQLEDFPMDAHACPLKFGSYAYPNSEVVYVWTNGSTKSVVVAEDGSRLNQYHLMGQTVGTENISTSTGEYTIMTAHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGWAWDGKKALEAAKIKKKREVILNKSTNAFTTGKMSHPPNIPKEQTPAGTSNTTSVSVKPSEEKTSESKKTYNSISKIDKMSRIVFPVLFGTFNLVYWATYLNREPVIKGAASPK	Successful	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 408).	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction	R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation	.	P31644
TTZA1NY	GABA(A) receptor beta-2 (GABRB2)	P47870	GBRB2_HUMAN	Neurotransmitter receptor	GABRB2; GABA(A) receptor subunit beta-2	GABRB2	"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."	.	6D6U; 6D6T	MWRVRKRGYFGIWSFPLIIAAVCAQSVNDPSNMSLVKETVDRLLKGYDIRLRPDFGGPPVAVGMNIDIASIDMVSEVNMDYTLTMYFQQAWRDKRLSYNVIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGDDNAVTGVTKIELPQFSIVDYKLITKKVVFSTGSYPRLSLSFKLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFMALLEYALVNYIFFGRGPQRQKKAAEKAASANNEKMRLDVNKIFYKDIKQNGTQYRSLWDPTGNLSPTRRTTNYDFSLYTMDPHENILLSTLEIKNEMATSEAVMGLGDPRSTMLAYDASSIQYRKAGLPRHSFGRNALERHVAQKKSRLRRRASQLKITIPDLTDVNAIDRWSRIFFPVVFSFFNIVYWLYYVN	Successful	"DrugBank: a knowledgebase for drugs, drug actions and drug targets. Nucleic Acids Res. 2008 Jan;36(Database issue):D901-6."	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04726:Serotonergic synapse; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction	R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation	.	P47870
TTGXH6N	GABA(A) receptor delta (GABRD)	O14764	GBRD_HUMAN	Ligand-gated ion channel	Gammaaminobutyric acid receptor subunit delta; GABRD; GABA(A) receptor subunit delta	GABRD	"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."	.	.	MDAPARLLAPLLLLCAQQLRGTRAMNDIGDYVGSNLEISWLPNLDGLIAGYARNFRPGIGGPPVNVALALEVASIDHISEANMEYTMTVFLHQSWRDSRLSYNHTNETLGLDSRFVDKLWLPDTFIVNAKSAWFHDVTVENKLIRLQPDGVILYSIRITSTVACDMDLAKYPMDEQECMLDLESYGYSSEDIVYYWSESQEHIHGLDKLQLAQFTITSYRFTTELMNFKSAGQFPRLSLHFHLRRNRGVYIIQSYMPSVLLVAMSWVSFWISQAAVPARVSLGITTVLTMTTLMVSARSSLPRASAIKALDVYFWICYVFVFAALVEYAFAHFNADYRKKQKAKVKVSRPRAEMDVRNAIVLFSLSAAGVTQELAISRRQRRVPGNLMGSYRSVGVETGETKKEGAARSGGQGGIRARLRPIDADTIDIYARAVFPAAFAAVNVIYWAAYAM	Successful	Gaboxadol--a new awakening in sleep.Curr Opin Pharmacol.2006 Feb;6(1):30-6.	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction	.	.	O14764
TTBY4OD	GABA(A) receptor epsilon (GABRE)	P78334	GBRE_HUMAN	.	Gamma-aminobutyric acid receptor subunit epsilon; GABA(A) receptor subunit epsilon	GABRE	"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."	.	.	MLSKVLPVLLGILLILQSRVEGPQTESKNEASSRDVVYGPQPQPLENQLLSEETKSTETETGSRVGKLPEASRILNTILSNYDHKLRPGIGEKPTVVTVEISVNSLGPLSILDMEYTIDIIFSQTWYDERLCYNDTFESLVLNGNVVSQLWIPDTFFRNSKRTHEHEITMPNQMVRIYKDGKVLYTIRMTIDAGCSLHMLRFPMDSHSCPLSFSSFSYPENEMIYKWENFKLEINEKNSWKLFQFDFTGVSNKTEIITTPVGDFMVMTIFFNVSRRFGYVAFQNYVPSSVTTMLSWVSFWIKTESAPARTSLGITSVLTMTTLGTFSRKNFPRVSYITALDFYIAICFVFCFCALLEFAVLNFLIYNQTKAHASPKLRHPRINSRAHARTRARSRACARQHQEAFVCQIVTTEGSDGEERPSCSAQQPPSPGSPEGPRSLCSKLACCEWCKRFKKYFCMVPDCEGSTWQQGRLCIHVYRLDNYSRVVFPVTFFFFNVLYWLVCLNL	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 417).	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04723: Retrograde endocannabinoid signaling; hsa04727: GABAergic synapse; hsa05032: Morphine addiction; hsa05033: Nicotine addiction	.	.	P78334
TT06RH5	GABA(A) receptor gamma-2 (GABRG2)	P18507	GBRG2_HUMAN	Neurotransmitter receptor	Gamma-aminobutyric acid receptor subunit gamma-2; GABA(A) receptor subunit gamma-2	GABRG2	"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."	.	6I53; 6HUP; 6HUO; 6HUK; 6HUJ	MSSPNIWSTGSSVYSTPVFSQKMTVWILLLLSLYPGFTSQKSDDDYEDYASNKTWVLTPKVPEGDVTVILNNLLEGYDNKLRPDIGVKPTLIHTDMYVNSIGPVNAINMEYTIDIFFAQTWYDRRLKFNSTIKVLRLNSNMVGKIWIPDTFFRNSKKADAHWITTPNRMLRIWNDGRVLYTLRLTIDAECQLQLHNFPMDEHSCPLEFSSYGYPREEIVYQWKRSSVEVGDTRSWRLYQFSFVGLRNTTEVVKTTSGDYVVMSVYFDLSRRMGYFTIQTYIPCTLIVVLSWVSFWINKDAVPARTSLGITTVLTMTTLSTIARKSLPKVSYVTAMDLFVSVCFIFVFSALVEYGTLHYFVSNRKPSKDKDKKKKNPAPTIDIRPRSATIQMNNATHLQERDEEYGYECLDGKDCASFFCCFEDCRTGAWRHGRIHIRIAKMDSYARIFFPTAFCLFNLVYWVSYLYL	Successful	3-demethoxy-3-glycosylaminothiocolchicines: Synthesis of a new class of putative muscle relaxant compounds. J Med Chem. 2006 Sep 7;49(18):5571-7.	34	TC=1.A.9	Ligand gated ion channel	ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRG2 sub-subfamily. 	.	.	Neurotransmitter-gated ion-channel ligand binding domain; Neurotransmitter-gated ion-channel transmembrane region	PF02931; PF02932	PF02931; Neur_chan_LBD; PF02932; Neur_chan_memb	1.A.9.5.4	"The Neurotransmitter Receptor, Cys loop, Ligand-gated Ion Channel (LIC) Family"	hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction	R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation	.	P18507
TTEX6LM	GABA(A) receptor gamma-3 (GABRG3)	Q99928	GBRG3_HUMAN	Ligand-gated ion channel	GABRG3	GABRG3	"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."	.	.	MAPKLLLLLCLFSGLHARSRKVEEDEYEDSSSNQKWVLAPKSQDTDVTLILNKLLREYDKKLRPDIGIKPTVIDVDIYVNSIGPVSSINMEYQIDIFFAQTWTDSRLRFNSTMKILTLNSNMVGLIWIPDTIFRNSKTAEAHWITTPNQLLRIWNDGKILYTLRLTINAECQLQLHNFPMDEHSCPLIFSSYGYPKEEMIYRWRKNSVEAADQKSWRLYQFDFMGLRNTTEIVTTSAGDYVVMTIYFELSRRMGYFTIQTYIPCILTVVLSWVSFWIKKDATPARTALGITTVLTMTTLSTIARKSLPRVSYVTAMDLFVTVCFLFVFAALMEYATLNYYSSCRKPTTTKKTTSLLHPDSSRWIPERISLQAPSNYSLLDMRPPPTAMITLNNSVYWQEFEDTCVYECLDGKDCQSFFCCYEECKSGSWRKGRIHIDILELDSYSRVFFPTSFLLFNLVYWVGYLYL	Successful	"Prodynorphin gene deletion increased anxiety-like behaviours, impaired the anxiolytic effect of bromazepam and altered GABAA receptor subunits gene expression in the amygdala. J Psychopharmacol. 2011Jan;25(1):87-96."	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04723:Retrograde endocannabinoid signaling; hsa04727:GABAergic synapse; hsa05032:Morphine addiction; hsa05033:Nicotine addiction	R-HSA-975298:Ligand-gated ion channel transport; R-HSA-977441:GABA A receptor activation	.	Q99928
TT3E0DI	GABA(A) receptor pi (GABRP)	O00591	GBRP_HUMAN	.	Gamma-aminobutyric acid receptor subunit pi; GABA(A) receptor subunit pi	GABRP	"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."	.	.	MNYSLHLAFVCLSLFTERMCIQGSQFNVEVGRSDKLSLPGFENLTAGYNKFLRPNFGGEPVQIALTLDIASISSISESNMDYTATIYLRQRWMDQRLVFEGNKSFTLDARLVEFLWVPDTYIVESKKSFLHEVTVGNRLIRLFSNGTVLYALRITTTVACNMDLSKYPMDTQTCKLQLESWGYDGNDVEFTWLRGNDSVRGLEHLRLAQYTIERYFTLVTRSQQETGNYTRLVLQFELRRNVLYFILETYVPSTFLVVLSWVSFWISLDSVPARTCIGVTTVLSMTTLMIGSRTSLPNTNCFIKAIDVYLGICFSFVFGALLEYAVAHYSSLQQMAAKDRGTTKEVEEVSITNIINSSISSFKRKISFASIEISSDNVDYSDLTMKTSDKFKFVFREKMGRIVDYFTIQNPSNVDHYSKLLFPLIFMLANVFYWAYYMYF	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 419).	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04723: Retrograde endocannabinoid signaling; hsa04727: GABAergic synapse; hsa05032: Morphine addiction; hsa05033: Nicotine addiction	.	.	O00591
TTXDUR9	GABA(A) receptor theta (GABRQ)	Q9UN88	GBRT_HUMAN	.	Gamma-aminobutyric acid receptor subunit theta; GABA(A) receptor subunit theta	GABRQ	"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."	.	.	MGIRGMLRAAVILLLIRTWLAEGNYPSPIPKFHFEFSSAVPEVVLNLFNCKNCANEAVVQKILDRVLSRYDVRLRPNFGGAPVPVRISIYVTSIEQISEMNMDYTITMFFHQTWKDSRLAYYETTLNLTLDYRMHEKLWVPDCYFLNSKDAFVHDVTVENRVFQLHPDGTVRYGIRLTTTAACSLDLHKFPMDKQACNLVVESYGYTVEDIILFWDDNGNAIHMTEELHIPQFTFLGRTITSKEVYFYTGSYIRLILKFQVQREVNSYLVQVYWPTVLTTITSWISFWMNYDSSAARVTIGLTSMLILTTIDSHLRDKLPNISCIKAIDIYILVCLFFVFLSLLEYVYINYLFYSRGPRRQPRRHRRPRRVIARYRYQQVVVGNVQDGLINVEDGVSSLPITPAQAPLASPESLGSLTSTSEQAQLATSESLSPLTSLSGQAPLATGESLSDLPSTSEQARHSYGVRFNGFQADDSIFPTEIRNRVEAHGHGVTHDHEDSNESLSSDERHGHGPSGKPMLHHGEKGVQEAGWDLDDNNDKSDCLAIKEQFKCDTNSTWGLNDDELMAHGQEKDSSSESEDSCPPSPGCSFTEGFSFDLFNPDYVPKVDKWSRFLFPLAFGLFNIVYWVYHMY	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 418).	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04723: Retrograde endocannabinoid signaling; hsa04727: GABAergic synapse; hsa05032: Morphine addiction; hsa05033: Nicotine addiction	R-HSA-1236394: Signaling by ERBB4; R-HSA-977443: GABA receptor activation	.	Q9UN88
TT6XFEU	GABA(A) receptor rho1 (GABRR1)	P24046	GBRR1_HUMAN	.	Gamma-aminobutyric acid receptor subunit rho-1; GABA(C) receptor1; GABA(A) receptor subunit rho-1	GABRR1	"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."	.	.	MLAVPNMRFGIFLLWWGWVLATESRMHWPGREVHEMSKKGRPQRQRREVHEDAHKQVSPILRRSPDITKSPLTKSEQLLRIDDHDFSMRPGFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLSFPSTNNLSMTFDGRLVKKIWVPDMFFVHSKRSFIHDTTTDNVMLRVQPDGKVLYSLRVTVTAMCNMDFSRFPLDTQTCSLEIESYAYTEDDLMLYWKKGNDSLKTDERISLSQFLIQEFHTTTKLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDRRAVPARVPLGITTVLTMSTIITGVNASMPRVSYIKAVDIYLWVSFVFVFLSVLEYAAVNYLTTVQERKEQKLREKLPCTSGLPPPRTAMLDGNYSDGEVNDLDNYMPENGEKPDRMMVQLTLASERSSPQRKSQRSSYVSMRIDTHAIDKYSRIIFPAAYILFNLIYWSIFS	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 420).	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04723: Retrograde endocannabinoid signaling; hsa04727: GABAergic synapse; hsa05032: Morphine addiction; hsa05033: Nicotine addiction	R-HSA-977443: GABA receptor activation	.	P24046
TTQMXLS	GABA(A) receptor rho2 (GABRR2)	P28476	GBRR2_HUMAN	.	Gamma-aminobutyric acid receptor subunit rho-2; GABA(C) receptor2; GABA(A) receptor subunit rho-2	GABRR2	"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."	.	.	MPYFTRLILFLFCLMVLVESRKPKRKRWTGQVEMPKPSHLYKKNLDVTKIRKGKPQQLLRVDEHDFSMRPAFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLAFSSASNKSMTFDGRLVKKIWVPDVFFVHSKRSFTHDTTTDNIMLRVFPDGHVLYSMRITVTAMCNMDFSHFPLDSQTCSLELESYAYTDEDLMLYWKNGDESLKTDEKISLSQFLIQKFHTTSRLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDRRAVPARVSLGITTVLTMTTIITGVNASMPRVSYVKAVDIYLWVSFVFVFLSVLEYAAVNYLTTVQERKERKLREKFPCMCGMLHSKTMMLDGSYSESEANSLAGYPRSHILTEEERQDKIVVHLGLSGEANAARKKGLLKGQTGFRIFQNTHAIDKYSRLIFPASYIFFNLIYWSVFS	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 421).	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04723: Retrograde endocannabinoid signaling; hsa04727: GABAergic synapse; hsa05032: Morphine addiction; hsa05033: Nicotine addiction	R-HSA-977443: GABA receptor activation	.	P28476
TT4N6D8	GABA(A) receptor rho3 (GABRR3)	A8MPY1	GBRR3_HUMAN	.	Gamma-aminobutyric acid receptor subunit rho-3; GABA(C) receptor3; GABA(A) receptor subunit rho-3	GABRR3	"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."	.	.	MVLAFQLVSFTYIWIILKPNVCAASNIKMTHQRCSSSMKQTCKQETRMKKDDSTKARPQKYEQLLHIEDNDFAMRPGFGGSPVPVGIDVHVESIDSISETNMDFTMTFYLRHYWKDERLSFPSTANKSMTFDHRLTRKIWVPDIFFVHSKRSFIHDTTMENIMLRVHPDGNVLLSLRITVSAMCFMDFSRFPLDTQNCSLELESYAYNEDDLMLYWKHGNKSLNTEEHMSLSQFFIEDFSASSGLAFYSSTGWYNRLFINFVLRRHVFFFVLQTYFPAILMVMLSWVSFWIDRRAVPARVSLGITTVLTMSTIITAVSASMPQVSYLKAVDVYLWVSSLFVFLSVIEYAAVNYLTTVEERKQFKKTGKISRMYNIDAVQAMAFDGCYHDSEIDMDQTSLSLNSEDFMRRKSICSPSTDSSRIKRRKSLGGHVGRIILENNHVIDTYSRILFPIVYILFNLFYWGVYV	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 422).	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04723: Retrograde endocannabinoid signaling; hsa04727: GABAergic synapse; hsa05032: Morphine addiction; hsa05033: Nicotine addiction	R-HSA-977443: GABA receptor activation	.	A8MPY1
TTKGEP3	Glutamic acid decarboxylase 1 (GAD1)	Q99259	DCE1_HUMAN	.	Glutamate decarboxylase 67 kDa isoform; Glutamate decarboxylase 1; GAD67; GAD-67; GAD; 67 kDa glutamic acid decarboxylase	GAD1	Catalyzes the production of GABA.	EC 4.1.1.15	3VP6; 2OKJ	MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEKSRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEVVDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGVRTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWSSKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAALGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAPKIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1272).	0	.	.	.	.	.	.	.	.	.	.	"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"	"R-HSA-888568: GABA synthesis; R-HSA-888590: GABA synthesis, release, reuptake and degradation; R-HSA-9022927: MECP2 regulates transcription of genes involved in GABA signaling"	MetaCyc:HS05215-MON	Q99259
TT7UY6K	Glutamate decarboxylase 2 (GAD2)	Q05329	DCE2_HUMAN	Carbon-carbon lyase	Glutamate decarboxylase 65 kDa isoform; GAD65; GAD2; 65 kDa glutamic acid decarboxylase	GAD2	Catalyzes the production of GABA.	EC 4.1.1.15	2OKK; 1ES0	MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGGSQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQYVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFSPGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVILIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIWMHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEYLYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEYGTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL	Clinical trial	"Clinical pipeline report, company report or official report of Diamyd Medical."	25	.	.	.	.	.	.	.	.	.	.	"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"	"R-HSA-888568: GABA synthesis; R-HSA-888590: GABA synthesis, release, reuptake and degradation; R-HSA-9022927: MECP2 regulates transcription of genes involved in GABA signaling"	MetaCyc:HS06208-MON	Q05329
TTFLWN6	Growth arrest and DNA-damage-inducible protein (GADD45)	P24522; O75293; O95257	GA45A_HUMAN; GA45B_HUMAN; GA45G_HUMAN	.	Growth arrest and DNA damage-inducible protein GADD45; DNA damage-inducible transcript protein; DDIT	GADD45A	Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK.	.	.	MTLEEFSAGEQKTERMDKVGDALEEVLSKALSQRTITVGVYEAAKLLNVDPDNVVLCLLAADEDDDRDVALQIHFTLIQAFCCENDINILRVSNPGRLAELLLLETDAGPAASEGAEQPPDLHCVLVTNPHSSQWKDPALSQLICFCRESRYMDQWVPVINLPER	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	.	.	.	.	.	.	.	.	.	.	hsa04010: MAPK signaling pathway; hsa04064: NF-kappa B signaling pathway; hsa04068: FoxO signaling pathway; hsa04110: Cell cycle; hsa04115: p53 signaling pathway; hsa04210: Apoptosis; hsa04218: Cellular senescence; hsa05169: Epstein-Barr virus infection; hsa05200: Pathways in cancer; hsa05202: Transcriptional misregulation in cancer; hsa05210: Colorectal cancer; hsa05212: Pancreatic cancer; hsa05213: Endometrial cancer; hsa05214: Glioma; hsa05216: Thyroid cancer; hsa05217: Basal cell carcinoma; hsa05218: Melanoma; hsa05220: Chronic myeloid leukemia; hsa05222: Small cell lung cancer; hsa05223: Non-small cell lung cancer; hsa05224: Breast cancer; hsa05225: Hepatocellular carcinoma; hsa05226: Gastric cancer	R-HSA-6804114: TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest; R-HSA-9617828: FOXO-mediated transcription of cell cycle genes	.	P24522
TTMDW9L	Negative growth-regulatory protein MyD118 (GADD45B)	O75293	GA45B_HUMAN	Ribosomal protein	Myeloid differentiation primary response protein MyD118; GADD45beta; GADD45B; DNA damage-inducible gene 45beta	GADD45B	Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK.	.	.	MTLEELVACDNAAQKMQTVTAAVEELLVAAQRQDRLTVGVYESAKLMNVDPDSVVLCLLAIDEEEEDDIALQIHFTLIQSFCCDNDINIVRVSGMQRLAQLLGEPAETQGTTEARDLHCLLVTNPHTDAWKSHGLVEVASYCEESRGNNQWVPYISLQER	Literature-reported	Down-regulation of growth arrest DNA damage-inducible gene 45beta expression is associated with human hepatocellular carcinoma. Am J Pathol. 2003 Jun;162(6):1961-74.	.	.	.	.	.	.	.	.	.	.	.	hsa04010: MAPK signaling pathway; hsa04064: NF-kappa B signaling pathway; hsa04068: FoxO signaling pathway; hsa04110: Cell cycle; hsa04115: p53 signaling pathway; hsa04210: Apoptosis; hsa04218: Cellular senescence; hsa05169: Epstein-Barr virus infection; hsa05200: Pathways in cancer; hsa05202: Transcriptional misregulation in cancer; hsa05210: Colorectal cancer; hsa05212: Pancreatic cancer; hsa05213: Endometrial cancer; hsa05214: Glioma; hsa05216: Thyroid cancer; hsa05217: Basal cell carcinoma; hsa05218: Melanoma; hsa05220: Chronic myeloid leukemia; hsa05222: Small cell lung cancer; hsa05223: Non-small cell lung cancer; hsa05224: Breast cancer; hsa05225: Hepatocellular carcinoma; hsa05226: Gastric cancer	.	.	O75293
TT0AGBL	HUMAN cyclin G-associated kinase (GAK)	O14976	GAK_HUMAN	Ser/Thr protein kinase family	cyclin G associated kinase	GAK	"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."	EC 2.7.11.1	4C57; 4C58; 4C59; 4Y8D; 5Y7Z	MSLLQSALDFLAGPGSLGGASGRDQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDVGSGREYALKRLLSNEEEKNRAIIQEVCFMKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLTELCKGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEEITRNTTPMYRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIAAARNVNPKSPITELLEQNGGYGSATLSRGPPPPVGPAGSGYSGGLALAEYDQPYGGFLDILRGGTERLFTNLKDTSSKVIQSVANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYMCDMVAEEPITPHSKPILVRAVVMTPVPLFSKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDVLIVIYHARSTLGGRLQAKMASMKMFQIQFHTGFVPRNATTVKFAKYDLDACDIQEKYPDLFQVNLEVEVEPRDRPSREAPPWENSSMRGLNPKILFSSREEQQDILSKFGKPELPRQPGSTAQYDAGAGSPEAEPTDSDSPPSSSADASRFLHTLDWQEEKEAETGAENASSKESESALMEDRDESEVSDEGGSPISSEGQEPRADPEPPGLAAGLVQQDLVFEVETPAVLPEPVPQEDGVDLLGLHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPPEAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPFGPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPPPSCSADFLHLGDLPGEPSKMTASSSNPDLLGGWAAWTETAASAVAPTPATEGPLFSPGGQPAPCGSQASWTKSQNPDPFADLGDLSSGLQGSPAGFPPGGFIPKTATTPKGSSSWQTSRPPAQGASWPPQAKPPPKACTQPRPNYASNFSVIGAREERGVRAPSFAQKPKVSENDFEDLLSNQGFSSRSDKKGPKTIAEMRKQDLAKDTDPLKLKLLDWIEGKERNIRALLSTLHTVLWDGESRWTPVGMADLVAPEQVKKHYRRAVLAVHPDKAAGQPYEQHAKMIFMELNDAWSEFENQGSRPLF	.	Baricitinib as potential treatment for 2019-nCoV acute respiratory disease. Lancet. 2020 Feb 15;395(10223):e30-e31.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-432722: Golgi Associated Vesicle Biogenesis; R-HSA-8856828: Clathrin-mediated endocytosis	.	O14976
TTXZAJ5	Galanin (GAL)	P22466	GALA_HUMAN	Galanin family	Galanin peptides; Galanin messageassociated peptide; GMAP; GAL	GAL	"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."	.	.	MARGSALLLASLLLAAALSASAGLWSPAKEKRGWTLNSAGYLLGPHAVGNHRSFSDKNGLTSKRELRPEDDMKPGSFDRSIPENNIMRTIIEFLSFLHLKEAGALDRLLDLPAAASSEDIERS	Literature-reported	Evaluation of an anxiety-related phenotype in galanin overexpressing transgenic mice. J Mol Neurosci. 2002 Feb-Apr;18(1-2):151-65.	.	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-418594: G alpha (i) signalling events	.	P22466
TT5IZRB	Galactocerebrosidase (GALC)	P54803	GALC_HUMAN	Glycosylase	Galactosylceramide betagalactosidase; Galactosylceramide beta-galactosidase; Galactosylceramidase; Galactocerebroside betagalactosidase; Galactocerebroside beta-galactosidase; GALCERase	GALC	"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."	EC 3.2.1.46	.	MAEWLLSASWQRRAKAMTAAAGSAGRAAVPLLLCALLAPGGAYVLDDSDGLGREFDGIGAVSGGGATSRLLVNYPEPYRSQILDYLFKPNFGASLHILKVEIGGDGQTTDGTEPSHMHYALDENYFRGYEWWLMKEAKKRNPNITLIGLPWSFPGWLGKGFDWPYVNLQLTAYYVVTWIVGAKRYHDLDIDYIGIWNERSYNANYIKILRKMLNYQGLQRVKIIASDNLWESISASMLLDAELFKVVDVIGAHYPGTHSAKDAKLTGKKLWSSEDFSTLNSDMGAGCWGRILNQNYINGYMTSTIAWNLVASYYEQLPYGRCGLMTAQEPWSGHYVVESPVWVSAHTTQFTQPGWYYLKTVGHLEKGGSYVALTDGLGNLTIIIETMSHKHSKCIRPFLPYFNVSQQFATFVLKGSFSEIPELQVWYTKLGKTSERFLFKQLDSLWLLDSDGSFTLSLHEDELFTLTTLTTGRKGSYPLPPKSQPFPSTYKDDFNVDYPFFSEAPNFADQTGVFEYFTNIEDPGEHHFTLRQVLNQRPITWAADASNTISIIGDYNWTNLTIKCDVYIETPDTGGVFIAGRVNKGGILIRSARGIFFWIFANGSYRVTGDLAGWIIYALGRVEVTAKKWYTLTLTIKGHFTSGMLNDKSLWTDIPVNFPKNGWAAIGTHSFEFAQFDNFLVEATR	Literature-reported	Galactocerebrosidase deficiency in globoid cell leucodystrophy of late onset. Arch Dis Child. 1972 Jun;47(253):449-50.	.	EC:3.2	Glycosylases	glycosyl hydrolase 59 family.	3.2.1.46	Glycosylases	Glycosyl hydrolase family 59; Glycosyl hydrolase family 59 central domain	PF02057; PF17387	PF02057; Glyco_hydro_59; PF17387; Glyco_hydro_59M	.	.	hsa00600: Sphingolipid metabolism; hsa01100: Metabolic pathways; hsa04142: Lysosome	R-HSA-1660662: Glycosphingolipid metabolism	.	P54803
TTGRHIB	UDP-glucose 4-epimerase (GALE)	Q14376	GALE_HUMAN	Racemases and epimerase	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	GALE	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.	EC 5.1.3.2	1I3N; 1I3M; 1I3L; 1I3K; 1HZJ	MAEKVLVTGGAGYIGSHTVLELLEAGYLPVVIDNFHNAFRGGGSLPESLRRVQELTGRSVEFEEMDILDQGALQRLFKKYSFMAVIHFAGLKAVGESVQKPLDYYRVNLTGTIQLLEIMKAHGVKNLVFSSSATVYGNPQYLPLDEAHPTGGCTNPYGKSKFFIEEMIRDLCQADKTWNAVLLRYFNPTGAHASGCIGEDPQGIPNNLMPYVSQVAIGRREALNVFGNDYDTEDGTGVRDYIHVVDLAKGHIAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARREGDVAACYANPSLAQEELGWTAALGLDRMCEDLWRWQKQNPSGFGTQA	Literature-reported	"Crystal structure of beta1,4-galactosyltransferase complex with UDP-Gal reveals an oligosaccharide acceptor binding site. J Mol Biol. 2002 Apr 26;318(2):491-502."	0	EC:5.1	Racemases and epimerases	NAD(P)-dependent epimerase/dehydratase family.	5.1.3.2 	Racemases and epimerases	"GDP-mannose 4,6 dehydratase"	PF16363	PF16363; GDP_Man_Dehyd	.	.	hsa00052:Galactose metabolism; hsa00520:Amino sugar and nucleotide sugar metabolism; hsa01100:Metabolic pathways	R-HSA-5609977: Defective GALE causes EDG; R-HSA-70370: Galactose catabolism	MetaCyc:HS04117-MON	Q14376
TTT9YPO	N-acetylgalactosamine 6 sulfatase (GALNS)	P34059	GALNS_HUMAN	Sulfuric ester hydrolase	N-acetylgalactosamine-6-sulfate sulfatase; N-acetylgalactosamine-6-sulfatase; Galactose-6-sulfate sulfatase; GalNAc6S sulfatase; GalN6S; Chondroitinsulfatase; Chondroitinase	GALNS	"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."	EC 3.1.6.4	4FDJ; 4FDI	MAAVVAATRWWQLLLVLSAAGMGASGAPQPPNILLLLMDDMGWGDLGVYGEPSRETPNLDRMAAEGLLFPNFYSANPLCSPSRAALLTGRLPIRNGFYTTNAHARNAYTPQEIVGGIPDSEQLLPELLKKAGYVSKIVGKWHLGHRPQFHPLKHGFDEWFGSPNCHFGPYDNKARPNIPVYRDWEMVGRYYEEFPINLKTGEANLTQIYLQEALDFIKRQARHHPFFLYWAVDATHAPVYASKPFLGTSQRGRYGDAVREIDDSIGKILELLQDLHVADNTFVFFTSDNGAALISAPEQGGSNGPFLCGKQTTFEGGMREPALAWWPGHVTAGQVSHQLGSIMDLFTTSLALAGLTPPSDRAIDGLNLLPTLLQGRLMDRPIFYYRGDTLMAATLGQHKAHFWTWTNSWENFRQGIDFCPGQNVSGVTTHNLEDHTKLPLIFHLGRDPGERFPLSFASAEYQEALSRITSVVQQHQEALVPAQPQLNVCNWAVMNWAPPGCEKLGKCLTPPESIPKKCLWSH	Successful	2014 FDA drug approvals. Nat Rev Drug Discov. 2015 Feb;14(2):77-81.	34	.	.	.	.	.	.	.	.	.	.	hsa00531:Glycosaminoglycan degradation; hsa01100:Metabolic pathways; hsa04142:Lysosome	R-HSA-2022857: Keratan sulfate degradation; R-HSA-2206290: MPS IV - Morquio syndrome A; R-HSA-6798695: Neutrophil degranulation	MetaCyc:HS06790-MON	P34059
TTX3HNZ	Galanin receptor type 1 (GAL1-R)	P47211	GALR1_HUMAN	GPCR rhodopsin	GALR1; GALR-1; GALNR1; GALN1R; GAL1-R	GALR1	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.	.	.	MELAVGNLSEGNASWPEPPAPEPGPLFGIGVENFVTLVVFGLIFALGVLGNSLVITVLARSKPGKPRSTTNLFILNLSIADLAYLLFCIPFQATVYALPTWVLGAFICKFIHYFFTVSMLVSIFTLAAMSVDRYVAIVHSRRSSSLRVSRNALLGVGCIWALSIAMASPVAYHQGLFHPRASNQTFCWEQWPDPRHKKAYVVCTFVFGYLLPLLLICFCYAKVLNHLHKKLKNMSKKSEASKKKTAQTVLVVVVVFGISWLPHHIIHLWAEFGVFPLTPASFLFRITAHCLAYSNSSVNPIIYAFLSENFRKAYKQVFKCHIRKDSHLSDTKESKSRIDTPPSTNCTHV	Literature-reported	Progress report on new antiepileptic drugs: a summary of the Ninth Eilat Conference (EILAT IX). Epilepsy Res. 2009 Jan;83(1):1-43.	0	PF00001	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events	.	P47211
TTOPAY7	Galanin receptor (GAL-R)	P47211; O43603; O60755	GALR1_HUMAN; GALR2_HUMAN; GALR3_HUMAN	GPCR rhodopsin	GALR; GALNR; GAL-R	GALR1	Receptor for the hormone galanin. Receptor for the hormone spexin-1.	.	.	MELAVGNLSEGNASWPEPPAPEPGPLFGIGVENFVTLVVFGLIFALGVLGNSLVITVLARSKPGKPRSTTNLFILNLSIADLAYLLFCIPFQATVYALPTWVLGAFICKFIHYFFTVSMLVSIFTLAAMSVDRYVAIVHSRRSSSLRVSRNALLGVGCIWALSIAMASPVAYHQGLFHPRASNQTFCWEQWPDPRHKKAYVVCTFVFGYLLPLLLICFCYAKVLNHLHKKLKNMSKKSEASKKKTAQTVLVVVVVFGISWLPHHIIHLWAEFGVFPLTPASFLFRITAHCLAYSNSSVNPIIYAFLSENFRKAYKQVFKCHIRKDSHLSDTKESKSRIDTPPSTNCTHV	Clinical trial	Anxiolytic- and antidepressant-like profiles of the galanin-3 receptor (Gal3) antagonists SNAP 37889 and SNAP 398299. Proc Natl Acad Sci U S A. 2005 Nov 29;102(48):17489-94.	19	PF00001	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events	.	P47211
TTBPW3J	Galanin receptor type 2 (GAL2-R)	O43603	GALR2_HUMAN	GPCR rhodopsin	GALR2; GALR-2; GALNR2; GAL2-R	GALR2	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.	.	.	MNVSGCPGAGNASQAGGGGGWHPEAVIVPLLFALIFLVGTVGNTLVLAVLLRGGQAVSTTNLFILNLGVADLCFILCCVPFQATIYTLDGWVFGSLLCKAVHFLIFLTMHASSFTLAAVSLDRYLAIRYPLHSRELRTPRNALAAIGLIWGLSLLFSGPYLSYYRQSQLANLTVCHPAWSAPRRRAMDICTFVFSYLLPVLVLGLTYARTLRYLWRAVDPVAAGSGARRAKRKVTRMILIVAALFCLCWMPHHALILCVWFGQFPLTRATYALRILSHLVSYANSCVNPIVYALVSKHFRKGFRTICAGLLGRAPGRASGRVCAAARGTHSGSVLERESSDLLHMSEAAGALRPCPGASQPCILEPCPGPSWQGPKAGDSILTVDVA	Literature-reported	Engineering galanin analogues that discriminate between GalR1 and GalR2 receptor subtypes and exhibit anticonvulsant activity following systemic de... J Med Chem. 2010 Feb 25;53(4):1871-5.	0	PF00001	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events	.	O43603
TT6WNG2	Gigaxonin (GAN)	Q9H2C0	GAN_HUMAN	.	Kelch-like protein 16	GAN	"Probable cytoskeletal component that directly or indirectly plays an important role in neurofilament architecture. May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Controls degradation of TBCB. Controls degradation of MAP1B and MAP1S, and is critical for neuronal maintenance and survival. {ECO:0000269|PubMed:12147674, ECO:0000269|PubMed:15983046, ECO:0000269|PubMed:16227972, ECO:0000269|PubMed:16303566}."	.	2PPI;3HVE	MAEGSAVSDPQHAARLLRALSSFREESRFCDAHLVLDGEEIPVQKNILAAASPYIRTKLNYNPPKDDGSTYKIELEGISVMVMREILDYIFSGQIRLNEDTIQDVVQAADLLLLTDLKTLCCEFLEGCIAAENCIGIRDFALHYCLHHVHYLATEYLETHFRDVSSTEEFLELSPQKLKEVISLEKLNVGNERYVFEAVIRWIAHDTEIRKVHMKDVMSALWVSGLDSSYLREQMLNEPLVREIVKECSNIPLSQPQQGEAMLANFKPRGYSECIVTVGGEERVSRKPTAAMRCMCPLYDPNRQLWIELAPLSMPRINHGVLSAEGFLFVFGGQDENKQTLSSGEKYDPDANTWTALPPMNEARHNFGIVEIDGMLYILGGEDGEKELISMECYDIYSKTWTKQPDLTMVRKIGCYAAMKKKIYAMGGGSYGKLFESVECYDPRTQQWTAICPLKERRFGAVACGVAMELYVFGGVRSREDAQGSEMVTCKSEFYHDEFKRWIYLNDQNLCIPASSSFVYGAVPIGASIYVIGDLDTGTNYDYVREFKRSTGTWHHTKPLLPSDLRRTGCAALRIANCKLFRLQLQQGLFRIRVHSP	Clinical trial	"Clinical pipeline report, company report or official report of Taysha Gene Therapies"	.	.	.	.	.	.	.	.	.	.	.	hsa:8139	R-HSA-8951664;R-HSA-983168;	.	Q9H2C0;
TTSGLN5	Neuromodulin (GAP43)	P17677	NEUM_HUMAN	Neuromodulin family	pp46; Neural phosphoprotein B-50; Growth-associated protein 43; Axonal membrane protein GAP-43	GAP43	"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."	.	.	MLCCMRRTKQVEKNDDDQKIEQDGIKPEDKAHKAATKIQASFRGHITRKKLKGEKKDDVQAAEAEANKKDEAPVADGVEKKGEGTTTAEAAPATGSKPDEPGKAGETPSEEKKGEGDAATEQAAPQAPASSEEKAGSAETESATKASTDNSPSSKAEDAPAKEEPKQADVPAAVTAAAATTPAAEDAAAKATAQPPTETGESSQAEENIEAVDETKPKESARQDEGKEEEPEADQEHA	Literature-reported	GAP-43 distribution is correlated with development of growth cones and presynaptic terminals. J Neurocytol. 1992 Jun;21(6):413-25.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-373760: L1CAM interactions	.	P17677
TTUGSWA	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)	P04406	G3P_HUMAN	Aldehyde/oxo donor oxidoreductase	Peptidyl-cysteine S-nitrosylase GAPDH; OK/SW-cl.12; GAPD; D-glyceraldehyde-3-phosphate dehydrogenase; CDABP0047	GAPDH	"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."	EC 1.2.1.12	6ADE; 4WNI; 4WNC; 3GPD; 2FEH	MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE	Clinical trial	Neuroprotection by pharmacologic blockade of the GAPDH death cascade. Proc Natl Acad Sci U S A. 2006 Mar 7;103(10):3887-9.	21	EC:1.2	Glyceraldehyde-3-phosphate	glyceraldehyde-3-phosphate dehydrogenase family.	1.2.1.12	Acting on the aldehyde or oxo group of donors	"Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain"	PF02800; PF00044	PF02800; Gp_dh_C; PF00044; Gp_dh_N	.	.	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	R-HSA-70171:Glycolysis; R-HSA-70263:Gluconeogenesis	MetaCyc:HS03433-MON	P04406
TTEXB9Z	Glycinamide ribonucleotide formyltransferase (GART)	P22102	PUR2_HUMAN	Carbon-nitrogen ligase	Trifunctional purine biosynthetic protein adenosine-3; PRGS; PGFT	GART	"A trifunctional polypeptide. Has Phosphoribosylamineglycine ligase, Phosphoribosylglycinamide formyltransferase, AIR synthetase (FGAM cyclase) activity which is required for de novo purine biosynthesis."	.	5J9F; 4ZZ3; 4ZZ2; 4ZZ1; 4ZZ0	MAARVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTAISISDHTALAQFCKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAFGAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAPQVSNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLCTSLPVWLENHTALTVVMASKGYPGDYTKGVEITGFPEAQALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEAKKGLAAIKFEGAIYRKDVGFRAIAFLQQPRSLTYKESGVDIAAGNMLVKKIQPLAKATSRSGCKVDLGGFAGLFDLKAAGFKDPLLASGTDGVGTKLKIAQLCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSCGKLDLSVTEAVVAGIAKACGKAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERDQKLPHLERITEGDVVVGIASSGLHSNGFSLVRKIVAKSSLQYSSPAPDGCGDQTLGDLLLTPTRIYSHSLLPVLRSGHVKAFAHITGGGLLENIPRVLPEKLGVDLDAQTWRIPRVFSWLQQEGHLSEEEMARTFNCGVGAVLVVSKEQTEQILRDIQQHKEEAWVIGSVVARAEGSPRVKVKNLIESMQINGSVLKNGSLTNHFSFEKKKARVAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILSGPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE	Clinical trial	"Results of 2 phase I studies of intravenous (iv) pelitrexol (AG2037), a glycinamide ribonucleotide formyltransferase (GARFT) inhibitor, in patients (pts) with solid tumors. J Clin Oncol (Meeting Abstracts) July 2004 vol. 22 no. 14_suppl 3075."	21	.	.	.	.	.	.	.	.	.	.	hsa00230:Purine metabolism; hsa00670:One carbon pool by folate; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics	R-HSA-73817:Purine ribonucleoside monophosphate biosynthesis	MetaCyc:HS08358-MON	P22102
TTCSJBZ	GAR transformylase (GART)	P22102 (810-1010)	PUR2_HUMAN	.	Phosphoribosylglycinamide formyltransferase; 5'-phosphoribosylglycinamide transformylase; GART	GART	"A folate-dependent enzyme, essential  for the de novo purine synthesis pathway."	EC 2.1.2.2	5J9F; 4ZZ3; 4ZZ2; 4ZZ1; 4ZZ0	VAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILSGPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEAVPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE	Clinical trial	"Phase I study of AG2034, a targeted GARFT inhibitor, administered once every 3 weeks. Cancer Chemother Pharmacol. 2000;45(5):423-7."	17	.	.	.	.	.	.	.	.	.	.	.	.	.	P22102
TT69QD2	AXL receptor tyrosine kinase ligand (GAS6)	Q14393	GAS6_HUMAN	.	Growth arrest-specific protein 6; GAS-6; AXLLG	GAS6	"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."	.	5VXZ; 4RA0; 2C5D; 1H30	MAPSLSPGPAALRRAPQLLLLLLAAECALAALLPAREATQFLRPRQRRAFQVFEEAKQGHLERECVEELCSREEAREVFENDPETDYFYPRYLDCINKYGSPYTKNSGFATCVQNLPDQCTPNPCDRKGTQACQDLMGNFFCLCKAGWGGRLCDKDVNECSQENGGCLQICHNKPGSFHCSCHSGFELSSDGRTCQDIDECADSEACGEARCKNLPGSYSCLCDEGFAYSSQEKACRDVDECLQGRCEQVCVNSPGSYTCHCDGRGGLKLSQDMDTCEDILPCVPFSVAKSVKSLYLGRMFSGTPVIRLRFKRLQPTRLVAEFDFRTFDPEGILLFAGGHQDSTWIVLALRAGRLELQLRYNGVGRVTSSGPVINHGMWQTISVEELARNLVIKVNRDAVMKIAVAGDLFQPERGLYHLNLTVGGIPFHEKDLVQPINPRLDGCMRSWNWLNGEDTTIQETVKVNTRMQCFSVTERGSFYPGSGFAFYSLDYMRTPLDVGTESTWEVEVVAHIRPAADTGVLFALWAPDLRAVPLSVALVDYHSTKKLKKQLVVLAVEHTALALMEIKVCDGQEHVVTVSLRDGEATLEVDGTRGQSEVSAAQLQERLAVLERHLRSPVLTFAGGLPDVPVTSAPVTAFYRGCMTLEVNRRLLDLDEAAYKHSDITAHSCPPVEPAAA	Clinical trial	Management of fetal endocrine disorders. Growth Horm IGF Res. 2003 Aug;13 Suppl A:S55-61.	.	.	.	.	.	.	.	.	.	.	.	hsa01521: EGFR tyrosine kinase inhibitor resistance	R-HSA-114608: Platelet degranulation; 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-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation	.	Q14393
TT4LRVO	Gastrin (GAST)	P01350	GAST_HUMAN	Gastrin cholecystokinin	Gastrin6; GAST; G52; G34; G14	GAST	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.	.	5WRJ	MQRLCVYVLIFALALAAFSEASWKPRSQQPDAPLGTGANRDLELPWLEQQGPASHHRRQLGPQGPPHLVADPSKKQGPWLEEEEEAYGWMDFGRRSAEDEN	Clinical trial	G17DT: an antigastrin immunogen for the treatment of gastrointestinal malignancy. Expert Opin Biol Ther. 2007 Mar;7(3):397-404.	25	.	.	.	.	.	.	.	.	.	.	hsa04971:Gastric acid secretion	R-HSA-416476:G alpha (q) signalling events; R-HSA-881907:Gastrin-CREB signalling pathway via PKC and MAPK	.	P01350
TT45KOB	GATA-binding factor 3 (GATA3)	P23771	GATA3_HUMAN	Zinc-finger	Trans-acting T-cell-specific transcription factor GATA-3	GATA3	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.	.	4HCA; 4HC9; 4HC7	MEVTADQPRWVSHHHPAVLNGQHPDTHHPGLSHSYMDAAQYPLPEEVDVLFNIDGQGNHVPPYYGNSVRATVQRYPPTHHGSQVCRPPLLHGSLPWLDGGKALGSHHTASPWNLSPFSKTSIHHGSPGPLSVYPPASSSSLSGGHASPHLFTFPPTPPKDVSPDPSLSTPGSAGSARQDEKECLKYQVPLPDSMKLESSHSRGSMTALGGASSSTHHPITTYPPYVPEYSSGLFPPSSLLGGSPTGFGCKSRPKARSSTGRECVNCGATSTPLWRRDGTGHYLCNACGLYHKMNGQNRPLIKPKRRLSAARRAGTSCANCQTTTTTLWRRNANGDPVCNACGLYYKLHNINRPLTMKKEGIQTRNRKMSSKSKKCKKVHDSLEDFPKNSSFNPAALSRHMSSLSHISPFSHSSHMLTTPTPMHPPSSLSFGPHHPSSMVTAMG	Literature-reported	Upregulation of the transcription factor GATA-3 in upper airway mucosa after in vivo and in vitro allergen challenge. J Allergy Clin Immunol. 2000 Jun;105(6 Pt 1):1146-52.	.	Zinc-finger	Zinc-finger	.	.	.	GATA zinc finger	PF00320	PF00320; GATA	.	.	"hsa04658: Th1 and Th2 cell differentiation; hsa04659: Th17 cell differentiation; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa05321: Inflammatory bowel disease"	R-HSA-5689880: Ub-specific processing proteases; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-8939236: RUNX1 regulates transcription of genes involved in differentiation of HSCs; R-HSA-9018519: Estrogen-dependent gene expression; R-HSA-983231: Factors involved in megakaryocyte development and platelet production	.	P23771
TT1VDN2	GATA-binding factor 4 (GATA4)	P43694	GATA4_HUMAN	Zinc-finger	Transcription factor GATA-4; GATA-4; GATA binding factor-4	GATA4	"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."	.	2M9W	MYQSLAMAANHGPPPGAYEAGGPGAFMHGAGAASSPVYVPTPRVPSSVLGLSYLQGGGAGSASGGASGGSSGGAASGAGPGTQQGSPGWSQAGADGAAYTPPPVSPRFSFPGTTGSLAAAAAAAAAREAAAYSSGGGAAGAGLAGREQYGRAGFAGSYSSPYPAYMADVGASWAAAAAASAGPFDSPVLHSLPGRANPAARHPNLDMFDDFSEGRECVNCGAMSTPLWRRDGTGHYLCNACGLYHKMNGINRPLIKPQRRLSASRRVGLSCANCQTTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMRKEGIQTRKRKPKNLNKSKTPAAPSGSESLPPASGASSNSSNATTSSSEEMRPIKTEPGLSSHYGHSSSVSQTFSVSAMSGHGPSIHPVLSALKLSPQGYASPVSQSPQTSSKQDSWNSLVLADSHGDIITA	Literature-reported	Activation of GATA-4 by serotonin in pulmonary artery smooth muscle cells. J Biol Chem. 2003 May 9;278(19):17525-31.	.	Zinc-finger	Zinc-finger	.	.	.	"GATA zinc finger; GATA-type transcription activator, N-terminal "	PF00320; PF05349	PF00320; GATA; PF05349; GATA-N	.	.	hsa04022: cGMP-PKG signaling pathway; hsa04218: Cellular senescence; hsa04530: Tight junction; hsa04919: Thyroid hormone signaling pathway	"R-HSA-2032785: YAP1- and WWTR1 (TAZ)-stimulated gene expression; R-HSA-400511: Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP); R-HSA-5578768: Physiological factors; R-HSA-9690406: Transcriptional regulation of testis differentiation; R-HSA-983231: Factors involved in megakaryocyte development and platelet production"	.	P43694
TT1B5PU	Glucosylceramidase (GBA)	P04062	GLCM_HUMAN	Glycosylase	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	GBA	"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."	EC 3.2.1.45	6Q6N; 6Q6L; 6Q6K; 5LVX; 3RIL	MEFSSPSREECPKPLSRVSIMAGSLTGLLLLQAVSWASGARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ	Successful	Nat Rev Drug Discov. 2013 Feb;12(2):87-90.	34	.	.	.	.	.	.	.	.	.	.	hsa00511:Other glycan degradation; hsa00600:Sphingolipid metabolism; hsa01100:Metabolic pathways; hsa04142:Lysosome	R-HSA-1660662:Glycosphingolipid metabolism	.	P04062
TTCYHJ4	Lysosomal acid glucosylceramidase (GBA1)	P04062	GBA1_HUMAN	Glycosyl hydrolase	Lysosomal acid GCase; Acid beta-glucosidase; Alglucerase; Beta-glucocerebrosidase; Beta-GC; Beta-glucosylceramidase 1; Cholesterol glucosyltransferase; SGTase; Cholesteryl-beta-glucosidase; D-glucosyl-N-acylsphingosine glucohydrolase; Glucosylceramidase beta 1; Imiglucerase; Lysosomal cholesterol glycosyltransferase; Lysosomal galactosylceramidase; Lysosomal glycosylceramidase	GBA1	"Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) into free ceramides (such as N-acylsphing-4-enine) and glucose (PubMed:9201993, PubMed:24211208, PubMed:15916907, PubMed:32144204). Plays a central role in the degradation of complex lipids and the turnover of cellular membranes (PubMed:27378698). Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation (PubMed:19279011). Catalyzes the glucosylation of cholesterol, through a transglucosylation reaction where glucose is transferred from GlcCer to cholesterol (PubMed:24211208, PubMed:26724485, PubMed:32144204). GlcCer containing mono-unsaturated fatty acids (such as beta-D-glucosyl-N-(9Z-octadecenoyl)-sphing-4-enine) are preferred as glucose donors for cholesterol glucosylation when compared with GlcCer containing same chain length of saturated fatty acids (such as beta-D-glucosyl-N-octadecanoyl-sphing-4-enine) (PubMed:24211208). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl 3-beta-D-glucoside to ceramide (PubMed:26724485) (Probable). Can also hydrolyze cholesteryl 3-beta-D-glucoside producing glucose and cholesterol (PubMed:24211208, PubMed:26724485). Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine), as well as the transfer of galactose between GalCers and cholesterol in vitro, but with lower activity than with GlcCers (PubMed:32144204). Contrary to GlcCer and GalCer, xylosylceramide/XylCer (such as beta-D-xyosyl-(1<->1')-N-acylsphing-4-enine) is not a good substrate for hydrolysis, however it is a good xylose donor for transxylosylation activity to form cholesteryl 3-beta-D-xyloside (PubMed:33361282). {ECO:0000269|PubMed:15916907, ECO:0000269|PubMed:19279011, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:27378698, ECO:0000269|PubMed:32144204, ECO:0000269|PubMed:33361282, ECO:0000269|PubMed:9201993, ECO:0000305|PubMed:32144204}."	EC 2.4.1.-; EC 3.2.1.-; EC 3.2.1.45; EC 3.2.1.46	1OGS;1Y7V;2F61;2J25;2NSX;2NT0;2NT1;2V3D;2V3E;2V3F;2VT0;2WCG;2WKL;2XWD;2XWE;3GXD;3GXF;3GXI;3GXM;3KE0;3KEH;3RIK;3RIL;5LVX;6MOZ;6Q1N;6Q1P;6Q6K;6Q6L;6Q6N;6T13;6TJJ;6TJK;6TJQ;6TN1;6YTP;6YTR;6YUT;6YV3;6Z39;6Z3I;7NWV	MEFSSPSREECPKPLSRVSIMAGSLTGLLLLQAVSWASGARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ	Clinical trial	"ClinicalTrials.gov (NCT05815004) Guard3: An Open-label, Parallel-arm, Randomized, Controlled, Phase 2/Phase 3 Study Evaluating the Efficacy and Safety of Autologous HSC Gene Therapy, AVR-RD-02, Compared to ERT for Gaucher Disease Type 3 in Participants Aged 2 to 25. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	hsa:2629	R-HSA-390471;R-HSA-9840310;	.	P04062;
TT6Y4PN	Glucagon-like peptide 1 (GLP-1:7-37)	P01275 (92-128)	GLUC_HUMAN	Glucagon	Glucagon-like peptide-1(7-36)-amide; GLP-1 (92-128); GLP; GCG	GCG	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.	.	6EDS; 5YQZ; 5VAI; 5OTX; 5OTW	HDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG	Literature-reported	Promising new approaches to the management of obesity. Drugs. 2000 Jul;60(1):1-9.	.	.	.	.	.	.	.	.	.	.	.	hsa04911:Insulin secretion; hsa04922:Glucagon signaling pathway	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	.	P01275
TT0NUFM	Glucagon (GCG)	P01275	GLUC_HUMAN	Glucagon	GRPP; GLP2; GLP1; GLP-1	GCG	"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."	.	6EDS; 5YQZ; 5VAI; 5OTX; 5OTW	MKSIYFVAGLFVMLVQGSWQRSLQDTEEKSRSFSASQADPLSDPDQMNEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIVEELGRRHADGSFSDEMNTILDNLAARDFINWLIQTKITDRK	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04714:Thermogenesis; hsa04911:Insulin secretion; hsa04922:Glucagon signaling pathway	"R-HSA-163359: Glucagon signaling in metabolic regulation; R-HSA-381676: Glucagon-like Peptide-1 (GLP1) regulates insulin secretion; R-HSA-381771: Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1); R-HSA-416476: G alpha (q) signalling events; R-HSA-418555: G alpha (s) signalling events; R-HSA-420092: Glucagon-type ligand receptors; R-HSA-422085: Synthesis, secretion, and deacylation of Ghrelin; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production"	.	P01275
TT9O6WS	Glucagon receptor (GCGR)	P47871	GLR_HUMAN	GPCR secretin	GLR; GL-R	GCGR	"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."	.	5XEZ; 5EE7; 4LF3; 4L6R; 4ERS	MPPCQPQRPLLLLLLLLACQPQVPSAQVMDFLFEKWKLYGDQCHHNLSLLPPPTELVCNRTFDKYSCWPDTPANTTANISCPWYLPWHHKVQHRFVFKRCGPDGQWVRGPRGQPWRDASQCQMDGEEIEVQKEVAKMYSSFQVMYTVGYSLSLGALLLALAILGGLSKLHCTRNAIHANLFASFVLKASSVLVIDGLLRTRYSQKIGDDLSVSTWLSDGAVAGCRVAAVFMQYGIVANYCWLLVEGLYLHNLLGLATLPERSFFSLYLGIGWGAPMLFVVPWAVVKCLFENVQCWTSNDNMGFWWILRFPVFLAILINFFIFVRIVQLLVAKLRARQMHHTDYKFRLAKSTLTLIPLLGVHEVVFAFVTDEHAQGTLRSAKLFFDLFLSSFQGLLVAVLYCFLNKEVQSELRRRWHRWRLGKVLWEERNTSNHRASSSPGHGPPSKELQFGRGGGSQDSSAETPLAGGLPRLAESPF	Successful	Glucagon receptor expression and glucagon stimulation of ghrelin secretion in rat stomach. Biochem Biophys Res Commun. 2007 Jun 15;357(4):865-70.	34	PF00002	GPCR secretin	G-protein coupled receptor 2 family.	.	.	7 transmembrane receptor (Secretin family); Hormone receptor domain	PF00002; PF02793	PF00002; 7tm_2; PF02793; HRM	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04922:Glucagon signaling pathway	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	.	P47871
TTLMJSC	Glucagon receptor messenger RNA (GCGR mRNA)	P47871	GLR_HUMAN	mRNA target	Glucagon receptor (mRNA); GLR (mRNA); GL-R (mRNA)	GCGR	"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."	.	5XEZ; 5EE7; 4LF3; 4L6R; 4ERS	MPPCQPQRPLLLLLLLLACQPQVPSAQVMDFLFEKWKLYGDQCHHNLSLLPPPTELVCNRTFDKYSCWPDTPANTTANISCPWYLPWHHKVQHRFVFKRCGPDGQWVRGPRGQPWRDASQCQMDGEEIEVQKEVAKMYSSFQVMYTVGYSLSLGALLLALAILGGLSKLHCTRNAIHANLFASFVLKASSVLVIDGLLRTRYSQKIGDDLSVSTWLSDGAVAGCRVAAVFMQYGIVANYCWLLVEGLYLHNLLGLATLPERSFFSLYLGIGWGAPMLFVVPWAVVKCLFENVQCWTSNDNMGFWWILRFPVFLAILINFFIFVRIVQLLVAKLRARQMHHTDYKFRLAKSTLTLIPLLGVHEVVFAFVTDEHAQGTLRSAKLFFDLFLSSFQGLLVAVLYCFLNKEVQSELRRRWHRWRLGKVLWEERNTSNHRASSSPGHGPPSKELQFGRGGGSQDSSAETPLAGGLPRLAESPF	Clinical trial	Design and development of antisense drugs. Expert Opin. Drug Discov. 2008 3(10):1189-1207.	17	mRNA	mRNA target	.	.	.	7 transmembrane receptor (Secretin family); Hormone receptor domain	PF00002; PF02793	PF00002; 7tm_2; PF02793; HRM	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04922: Glucagon signaling pathway	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	.	P47871
TTLSWP6	GTP cyclohydrolase-I (GCH1)	P30793	GCH1_HUMAN	Carbon-nitrogen hydrolase	Guanosine triphosphate cyclohydrolase I; GTP-CH-I; GTP cyclohydrolase I; GTP cyclohydrolase 1; GCH; DYT5	GCH1	"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)."	EC 3.5.4.16	1FB1	MEKGPVRAPAEKPRGARCSNGFPERDPPRPGPSRPAEKPPRPEAKSAQPADGWKGERPRSEEDNELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS	Clinical trial	GTP cyclohydrolase I feedback regulatory protein-dependent and -independent inhibitors of GTP cyclohydrolase I. Arch Biochem Biophys. 2001 Apr 1;388(1):67-73.	25	EC:3.5	Carbon nitrogen hydrolase	GTP cyclohydrolase I family.	3.5.4.16 	"Acting on carbon-nitrogen bonds, other than peptide bonds"	GTP cyclohydrolase I	PF01227	PF01227; GTP_cyclohydroI	.	.	hsa00790: Folate biosynthesis; hsa01100: Metabolic pathways; hsa01240: Biosynthesis of cofactors	"R-HSA-1474151:Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation"	MetaCyc:HS05586-MON	P30793
TTDLNGZ	Glucokinase (GCK)	P35557	HXK4_HUMAN	Kinase	Hexokinase type IV; Hexokinase D; HK4; HK IV	GCK	"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."	EC 2.7.1.2	5V4X; 5V4W; 4RCH; 4NO7; 4MLH	MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ	Clinical trial	"Clinical pipeline report, company report or official report of AstraZeneca (2009)."	21	.	.	.	.	.	.	.	.	.	.	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	R-HSA-210745:Regulation of gene expression in beta cells; R-HSA-70153:Glucose transport; R-HSA-70171:Glycolysis	MetaCyc:HS02935-MON	P35557
TTNFESW	Glutamate--cysteine ligase modifier (GCLM)	Q9UB86	GSH0_HUMAN	Aldo/keto reductase family	Glutamate--cysteine ligase modifier subunit; Gamma-glutamylcysteine synthetase regulatory subunit; Gamma-ECS regulatory subunit; GCS light chain	GCLM	"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."	.	.	MGTDSRAAKALLARARTLHLQTGNLLNWGRLRKKCPSTHSEELHDCIQKTLNEWSSQINPDLVREFPDVLECTVSHAVEKINPDEREEMKVSAKLFIVESNSSSSTRSAVDMACSVLGVAQLDSVIIASPPIEDGVNLSLEHLQPYWEELENLVQSKKIVAIGTSDLDKTQLEQLYQWAQVKPNSNQVNLASCCVMPPDLTAFAKQFDIQLLTHNDPKELLSEASFQEALQESIPDIQAHEWVPLWLLRYSVIVKSRGIIKSKGYILQAKRRGS	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	hsa00480:Glutathione metabolism; hsa01100:Metabolic pathways	.	.	P48507
TTK4JTZ	Guanine deaminase (GDA)	Q9Y2T3	GUAD_HUMAN	Metallo-dependent hydrolase superfamily. ATZ/TRZ family	p51-nedasin; KIAA1258; Guanine aminohydrolase; Guanase; GAH	GDA	"Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia."	EC 3.5.4.3	4AQL; 3E0L; 2UZ9	MCAAQMPPLAHIFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEEASQQEKLAKEWCFKPCEIRELSHHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDTFPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLFYGDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVVPFSSSV	Literature-reported	Studies on guanine deaminase and its inhibitors in rat tissue. Biochem J. 1967 Mar;102(3):691-704.	.	.	.	.	.	.	.	.	.	.	.	hsa00230:Purine metabolism; hsa01100:Metabolic pathways	R-HSA-74259: Purine catabolism	MetaCyc:HS04276-MON	Q9Y2T3
TT4MXVG	Growth/differentiation factor 15 (GDF15)	Q99988	GDF15_HUMAN	Growth factor	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	GDF15	"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)."	.	5VZ4; 5VZ3; 5VT2	MPGQELRTVNGSQMLLVLLVLSWLPHGGALSLAEASRASFPGPSELHSEDSRFRELRKRYEDLLTRLRANQSWEDSNTDLVPAPAVRILTPEVRLGSGGHLHLRISRAALPEGLPEASRLHRALFRLSPTASRSWDVTRPLRRQLSLARPQAPALHLRLSPPPSQSDQLLAESSSARPQLELHLRPQAARGRRRARARNGDHCPLGPGRCCRLHTVRASLEDLGWADWVLSPREVQVTMCIGACPSQFRAANMHAQIKTSLHRLKPDTVPAPCCVPASYNPMVLIQKTDTGVSLQTYDDLLAKDCHCI	Literature-reported	GDF-15 as a Target and Biomarker for Diabetes and Cardiovascular Diseases: A Translational Prospective. J Diabetes Res. 2015;2015:490842.	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction	.	.	Q99988
TTAP4T1	Growth/differentiation factor 2 (GDF2)	Q9UK05	GDF2_HUMAN	Growth factor	GDF2; Bone morphogenetic protein 9; BMP9	GDF2	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.	.	5I05; 5HZW; 4YCI; 4YCG; 4MPL	MCPGALWVALPLLSLLAGSLQGKPLQSWGRGSAGGNAHSPLGVPGGGLPEHTFNLKMFLENVKVDFLRSLNLSGVPSQDKTRVEPPQYMIDLYNRYTSDKSTTPASNIVRSFSMEDAISITATEDFPFQKHILLFNISIPRHEQITRAELRLYVSCQNHVDPSHDLKGSVVIYDVLDGTDAWDSATETKTFLVSQDIQDEGWETLEVSSAVKRWVRSDSTKSKNKLEVTVESHRKGCDTLDISVPPGSRNLPFFVVFSNDHSSGTKETRLELREMISHEQESVLKKLSKDGSTEAGESSHEEDTDGHVAAGSTLARRKRSAGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVGKACCVPTKLSPISVLYKDDMGVPTLKYHYEGMSVAECGCR	Clinical trial	Company report (Acceleron Pharma)	17	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction	R-HSA-201451: Signaling by BMP	.	Q9UK05
TT37XV9	Growth/differentiation factor 5 (GDF-5)	P43026	GDF5_HUMAN	Growth factor	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	GDF5	"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."	.	5HK5; 3QB4; 3EVS; 2BHK; 1WAQ	MRLPKLLTFLLWYLAWLDLEFICTVLGAPDLGQRPQGTRPGLAKAEAKERPPLARNVFRPGGHSYGGGATNANARAKGGTGQTGGLTQPKKDEPKKLPPRPGGPEPKPGHPPQTRQATARTVTPKGQLPGGKAPPKAGSVPSSFLLKKAREPGPPREPKEPFRPPPITPHEYMLSLYRTLSDADRKGGNSSVKLEAGLANTITSFIDKGQDDRGPVVRKQRYVFDISALEKDGLLGAELRILRKKPSDTAKPAAPGGGRAAQLKLSSCPSGRQPASLLDVRSVPGLDGSGWEVFDIWKLFRNFKNSAQLCLELEAWERGRAVDLRGLGFDRAARQVHEKALFLVFGRTKKRDLFFNEIKARSGQDDKTVYEYLFSQRRKRRAPLATRQGKRPSKNLKARCSRKALHVNFKDMGWDDWIIAPLEYEAFHCEGLCEFPLRSHLEPTNHAVIQTLMNSMDPESTPPTCCVPTRLSPISILFIDSANNVVYKQYEDMVVESCGCR	Clinical trial	"Superior effect of MD05, beta-tricalcium phosphate coated with recombinant human growth/differentiation factor-5, compared to conventional bone substitutes in the rat calvarial defect model. J Periodontol. 2006 Sep;77(9):1582-90."	21	Growth factor	Growth factor	TGF-beta family.	.	.	Transforming growth factor beta like domain; TGF-beta propeptide	PF00019; PF00688	PF00019; TGF_beta; PF00688; TGFb_propeptide	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04350:TGF-beta signaling pathway; hsa04390:Hippo signaling pathway	R-HSA-2129379:Molecules associated with elastic fibres	.	P43026
TTF23ML	Glial cell line-derived neurotrophic factor (GDNF)	P39905	GDNF_HUMAN	Growth factor	hGDNF; Glial cell linederived neurotrophic factor; Astrocytederived trophic factor; Astrocyte-derived trophic factor; ATF	GDNF	Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake.	.	4UX8; 3FUB; 2V5E	MKLWDVVAVCLVLLHTASAFPLPAGKRPPEAPAEDRSLGRRRAPFALSSDSNMPEDYPDQFDDVMDFIQATIKRLKRSPDKQMAVLPRRERNRQAAAANPENSRGKGRRGQRGKNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCDAAETTYDKILKNLSRNRRLVSDKVGQACCRPIAFDDDLSFLDDNLVYHILRKHSAKRCGCI	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	19	Growth factor	Transforming growth factor	TGF-beta family. GDNF subfamily.	.	.	Transforming growth factor beta like domain	PF00019	PF00019; TGF_beta	.	.	hsa04020: Calcium signaling pathway	R-HSA-419037: NCAM1 interactions; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-8853659: RET signaling	.	P39905
TTAZF9M	RAS-like protein KIR (GEM)	P55040	GEM_HUMAN	Small GTPase superfamily	RASlike protein KIR; GTPbinding protein GEM; GTPbinding mitogeninduced Tcell protein	GEM	"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."	.	2HT6; 2G3Y; 2CJW	MTLNNVTMRQGTVGMQPQQQRWSIPADGRHLMVQKEPHQYSHRNRHSATPEDHCRRSWSSDSTDSVISSESGNTYYRVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVLGEDTYERTLMVDGESATIILLDMWENKGENEWLHDHCMQVGDAYLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGIVRQVRLRRDSKEKNERRLAYQKRKESMPRKARRFWGKIVAKNNKNMAFKLKSKSCHDLSVL	Clinical trial	Anti-tumoral efficacy of therapeutic human anti-KIR antibody (Lirilumab/BMS-986015/IPH2102) in a preclinical xenograft tumor model. J Immunother Cancer. 2013; 1(Suppl 1): P40.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	P55040
TTI6FFX	Glial fibrillary acidic protein messenger RNA (GFAP mRNA)	P14136	GFAP_HUMAN	mRNA target	GFAP (mRNA)	GFAP	"GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells."	.	6A9P	MERRRITSAARRSYVSSGEMMVGGLAPGRRLGPGTRLSLARMPPPLPTRVDFSLAGALNAGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNLAQDLATVRQKLQDETNLRLEAENNLAAYRQEADEATLARLDLERKIESLEEEIRFLRKIHEEEVRELQEQLARQQVHVELDVAKPDLTAALKEIRTQYEAMASSNMHEAEEWYRSKFADLTDAAARNAELLRQAKHEANDYRRQLQSLTCDLESLRGTNESLERQMREQEERHVREAASYQEALARLEEEGQSLKDEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRITIPVQTFSNLQIRETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKESKQEHKDVM	Clinical trial	"Clinical pipeline report, company report or official report of Ionis"	.	.	.	.	.	.	.	.	.	.	.	hsa:2670	R-HSA-1251985;R-HSA-9613829;	.	P14136;
TT63XRS	GDNF receptor alpha-3 (GFRA3)	O60609	GFRA3_HUMAN	.	UNQ339/PRO538/PRO3664; GFR-alpha-3; GDNFR-alpha-3; GDNF family receptor alpha-3	GFRA3	"Mediates the artemin-induced autophosphorylation and activation of the RET receptor tyrosine kinase. Receptor for the glial cell line-derived neurotrophic factor, ARTN (artemin)."	.	2GH0	MVRPLNPRPLPPVVLMLLLLLPPSPLPLAAGDPLPTESRLMNSCLQARRKCQADPTCSAAYHHLDSCTSSISTPLPSEEPSVPADCLEAAQQLRNSSLIGCMCHRRMKNQVACLDIYWTVHRARSLGNYELDVSPYEDTVTSKPWKMNLSKLNMLKPDSDLCLKFAMLCTLNDKCDRLRKAYGEACSGPHCQRHVCLRQLLTFFEKAAEPHAQGLLLCPCAPNDRGCGERRRNTIAPNCALPPVAPNCLELRRLCFSDPLCRSRLVDFQTHCHPMDILGTCATEQSRCLRAYLGLIGTAMTPNFVSNVNTSVALSCTCRGSGNLQEECEMLEGFFSHNPCLTEAIAAKMRFHSQLFSQDWPHPTFAVMAHQNENPAVRPQPWVPSLFSCTLPLILLLSLW	Clinical trial	"First-In-Human, Double-Blind, Placebo-Controlled, Randomized, Dose-Escalation Study of BG00010, a Glial Cell Line-Derived Neurotrophic Factor Family Member, in Subjects with Unilateral Sciatica. PLoSOne. 2015 May 11;10(5):e0125034."	21	.	GDNFR family	GDNFR family.	.	.	GDNF/GAS1 domain	PF02351	PF02351; GDNF	.	.	.	R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-8853659: RET signaling	.	O60609
TTE61UB	GDNF family receptor alpha-like (GFRAL)	Q6UXV0	GFRAL_HUMAN	.	.	GFRAL	"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."	.	.	MIVFIFLAMGLSLENEYTSQTNNCTYLREQCLRDANGCKHAWRVMEDACNDSDPGDPCKMRNSSYCNLSIQYLVESNFQFKECLCTDDFYCTVNKLLGKKCINKSDNVKEDKFKWNLTTRSHHGFKGMWSCLEVAEACVGDVVCNAQLASYLKACSANGNPCDLKQCQAAIRFFYQNIPFNIAQMLAFCDCAQSDIPCQQSKEALHSKTCAVNMVPPPTCLSVIRSCQNDELCRRHYRTFQSKCWQRVTRKCHEDENCISTLSKQDLTCSGSDDCKAAYIDILGTVLQVQCTCRTITQSEESLCKIFQHMLHRKSCFNYPTLSNVKGMALYTRKHANKITLTGFHSPFNGEVIYAAMCMTVTCGILLLVMVKLRTSRISSKARDPSSIQIPGEL	Clinical trial	"Clinical pipeline report, company report or official report of NGM Biopharmaceuticals."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q6UXV0
TT76OLR	Vitamin K-dependent gamma-carboxylase (GGCX)	P38435	VKGC_HUMAN	Carbon-carbon lyase	Vitamin K gamma glutamyl carboxylase; Gamma-glutamyl carboxylase; GGCX	GGCX	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.	EC 4.1.1.90	.	MAVSAGSARTSPSSDKVQKDKAELISGPRQDSRIGKLLGFEWTDLSSWRRLVTLLNRPTDPASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSPFKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFSYVMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSVSCVYKRSRGKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQPLLMDLSPWRAKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTTSPSPSCYMYVYVNTTELALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNTPFHERFFRFLLRKLYVFRRSFLMTCISLRNLILGRPSLEQLAQEVTYANLRPFEAVGELNPSNTDSSHSNPPESNPDPVHSEF	Successful	Quinone oxidoreductases and vitamin K metabolism. Vitam Horm. 2008;78:85-101.	34	.	.	.	.	.	.	.	.	.	.	hsa00130:Ubiquinone and other terpenoid-quinone biosynthesis	R-HSA-159740:Gamma-carboxylation of protein precursors	MetaCyc:HS03897-MON	P38435
TTZJRL0	Gamma-glutamyl hydrolase (GGH)	Q92820	GGH_HUMAN	Peptidase	Human glutamyl hydrolase; Gamma-Glu-X carboxypeptidase; GGH; Conjugase	GGH	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.	EC 3.4.19.9	1L9X	MASPGCLLCVLGLLLCGAASLELSRPHGDTAKKPIIGILMQKCRNKVMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRSDYAKVAKIFYNLSIQSFDDGDYFPVWGTCLGFEELSLLISGECLLTATDTVDVAMPLNFTGGQLHSRMFQNFPTELLLSLAVEPLTANFHKWSLSVKNFTMNEKLKKFFNVLTTNTDGKIEFISTMEGYKYPVYGVQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQFSPIYTGNISSFQQCYIFD	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	.	.	.	.	.	.	.	.	.	.	hsa00790: Folate biosynthesis; hsa01240: Biosynthesis of cofactors; hsa01523: Antifolate resistance	R-HSA-6798695: Neutrophil degranulation	.	Q92820
TTZVT7O	Leukotriene-C4 hydrolase	.	GGT1_HUMAN	Single Protein	Glutathione hydrolase 1 proenzyme; CD224; GGT 1; Gamma-glutamyltransferase 1; Gamma-glutamyltranspeptidase 1; GGT1; GGT	GGT1	"Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates and other gamma-glutamyl compounds, such as leukotriene C4 (LTC4). The metabolism of glutathione by GGT1 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, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound."	.	.	MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRDGGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKDIQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSRESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISDDTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTATALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P19440
TTFNO7W	Gamma glutamyltranspeptidase (GGT)	P19440; P36268	GGT1_HUMAN; GGT2_HUMAN	.	Gamma-glutamyltranspeptidase; Gamma-glutamyltransferase; GGT	GGT1	"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."	.	.	MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRDGGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKDIQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSRESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISDDTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTATALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY	Literature-reported	"Elevation of serum gamma-glutamyltranspeptidase activity is frequent in chronic hepatitis C, and is associated with insulin resistance. Dig Liver Dis. 2009 Aug;41(8):586-90."	.	.	.	.	.	.	.	.	.	.	.	hsa00430: Taurine and hypotaurine metabolism; hsa00480: Glutathione metabolism; hsa00590: Arachidonic acid metabolism; hsa01100: Metabolic pathways	R-HSA-174403: Glutathione synthesis and recycling; R-HSA-2142691: Synthesis of Leukotrienes (LT) and Eoxins (EX); R-HSA-5423646: Aflatoxin activation and detoxification; R-HSA-5579022: Defective GGT1 causes GLUTH; R-HSA-9035968: Defective GGT1 in aflatoxin detoxification causes GLUTH; R-HSA-9664535: LTC4-CYSLTR mediated IL4 production; R-HSA-9753281: Paracetamol ADME	MetaCyc:MON66-34394	P19440
TT62BC7	Gamma-glutamyl transferase 7 (GGT7)	Q9UJ14	GGT7_HUMAN	Peptidase	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	GGT7	"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."	EC 3.4.19.13	.	MAAENEASQESALGAYSPVDYMSITSFPRLPEDEPAPAAPLRGRKDEDAFLGDPDTDPDSFLKSARLQRLPSSSSEMGSQDGSPLRETRKDPFSAAAAECSCRQDGLTVIVTACLTFATGVTVALVMQIYFGDPQIFQQGAVVTDAARCTSLGIEVLSKQGSSVDAAVAAALCLGIVAPHSSGLGGGGVMLVHDIRRNESHLIDFRESAPGALREETLQRSWETKPGLLVGVPGMVKGLHEAHQLYGRLPWSQVLAFAAAVAQDGFNVTHDLARALAEQLPPNMSERFRETFLPSGRPPLPGSLLHRPDLAEVLDVLGTSGPAAFYAGGNLTLEMVAEAQHAGGVITEEDFSNYSALVEKPVCGVYRGHLVLSPPPPHTGPALISALNILEGFNLTSLVSREQALHWVAETLKIALALASRLGDPVYDSTITESMDDMLSKVEAAYLRGHINDSQAAPAPLLPVYELDGAPTAAQVLIMGPDDFIVAMVSSLNQPFGSGLITPSGILLNSQMLDFSWPNRTANHSAPSLENSVQPGKRPLSFLLPTVVRPAEGLCGTYLALGANGAARGLSGLTQVLLNVLTLNRNLSDSLARGRLHPDLQSNLLQVDSEFTEEEIEFLEARGHHVEKVDVLSWVHGSRRTNNFIIAVKDPRSPDAAGATIL	Literature-reported	-Glutamyl transferase 7 is a novel regulator of glioblastoma growth. BMC Cancer. 2015 Apr 7;15:225.	.	EC:3.4	.	.	.	.	.	.	.	.	.	hsa00430: Taurine and hypotaurine metabolism; hsa00480: Glutathione metabolism; hsa01100: Metabolic pathways	R-HSA-174403: Glutathione synthesis and recycling; R-HSA-5423646: Aflatoxin activation and detoxification; R-HSA-9753281: Paracetamol ADME	.	Q9UJ14
TTT3YKH	Somatotropin (GH1)	P01241	SOMA_HUMAN	Somatotropin/prolactin	Pituitary growth hormone; Growth hormone 1; Growth hormone; GH-N; GH	GH1	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.	.	3HHR; 1KF9; 1HWH; 1HWG; 1HUW	MATGSRTSLLLAFGLLCLPWLQEGSAFPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF	Clinical trial	"Developments in human growth hormone preparations: sustained-release, prolonged half-life, novel injection devices, and alternative delivery routes. Int J Nanomedicine. 2014; 9: 3527-3538."	25	Somatotropin/prolactin	Somatotropin hormone family	somatotropin/prolactin family.	.	.	Somatotropin hormone family	PF00103	PF00103; Hormone_1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway	R-HSA-1170546:Prolactin receptor signaling; R-HSA-982772:Growth hormone receptor signaling	.	P01241
TTHJWYD	GHR messenger RNA (GHR mRNA)	P10912	GHR_HUMAN	mRNA target	Somatotropin receptor (mRNA); Serum bindingprotein (mRNA); Growth hormone receptor (mRNA); GH receptor (mRNA)	GHR	"On ligand binding, couples to the JAK2/STAT5 pathway. Receptor for pituitary gland growth hormone involved in regulating postnatal body growth."	.	5OHD; 5OEK; 3HHR; 2AEW; 1KF9	MDLWQLLLTLALAGSSDAFSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFYFPWLLIIIFGIFGLTVMLFVFLFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILAIHDSYKPEFHSDDSWVEFIELDIDEPDEKTEESDTDRLLSSDHEKSHSNLGVKDGDSGRTSCCEPDILETDFNANDIHEGTSEVAQPQRLKGEADLLCLDQKNQNNSPYHDACPATQQPSVIQAEKNKPQPLPTEGAESTHQAAHIQLSNPSSLSNIDFYAQVSDITPAGSVVLSPGQKNKAGMSQCDMHPEMVSLCQENFLMDNAYFCEADAKKCIPVAPHIKVESHIQPSLNQEDIYITTESLTTAAGRPGTGEHVPGSEMPVPDYTSIHIVQSPQGLILNATALPLPDKEFLSSCGYVSTDQLNKIMP	Clinical trial	"Clinical pipeline report, company report or official report of ISIS Pharmaceuticals (2009)."	17	mRNA	mRNA target	.	.	.	"Erythropoietin receptor, ligand binding; Fibronectin type III domain; Growth hormone receptor binding"	PF09067; PF00041; PF12772	PF09067; EpoR_lig-bind; PF00041; fn3; PF12772; GHBP	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway	R-HSA-1170546:Prolactin receptor signaling; R-HSA-982772:Growth hormone receptor signaling	.	P10912
TTKMAZ6	Growth hormone receptor (GHR)	P10912	GHR_HUMAN	Cytokine receptor	Somatotropin receptor; Serum bindingprotein; GH receptor	GHR	"On ligand binding, couples to the JAK2/STAT5 pathway. Receptor for pituitary gland growth hormone involved in regulating postnatal body growth."	.	5OHD; 5OEK; 3HHR; 2AEW; 1KF9	MDLWQLLLTLALAGSSDAFSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFYFPWLLIIIFGIFGLTVMLFVFLFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILAIHDSYKPEFHSDDSWVEFIELDIDEPDEKTEESDTDRLLSSDHEKSHSNLGVKDGDSGRTSCCEPDILETDFNANDIHEGTSEVAQPQRLKGEADLLCLDQKNQNNSPYHDACPATQQPSVIQAEKNKPQPLPTEGAESTHQAAHIQLSNPSSLSNIDFYAQVSDITPAGSVVLSPGQKNKAGMSQCDMHPEMVSLCQENFLMDNAYFCEADAKKCIPVAPHIKVESHIQPSLNQEDIYITTESLTTAAGRPGTGEHVPGSEMPVPDYTSIHIVQSPQGLILNATALPLPDKEFLSSCGYVSTDQLNKIMP	Successful	Growth hormone receptor antagonist treatment reduces exercise performance in young males. J Clin Endocrinol Metab. 2009 Sep;94(9):3265-72.	34	Cytokine receptor	Transmembrane protein	type I cytokine receptor family. Type 1 subfamily.	.	.	"Erythropoietin receptor, ligand binding; Fibronectin type III domain; Growth hormone receptor binding"	PF09067; PF00041; PF12772	PF09067; EpoR_lig-bind; PF00041; fn3; PF12772; GHBP	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway	R-HSA-1170546:Prolactin receptor signaling; R-HSA-982772:Growth hormone receptor signaling	.	P10912
TTG4R8V	Growth hormone-releasing hormone receptor (GHRHR)	Q02643	GHRHR_HUMAN	GPCR secretin	GRFR; GRF receptor; GHRHR; GHRH receptor	GHRHR	"Receptor for GRF,coupled to G proteins which activate adenylyl cyclase. Stimulates somatotroph cell growth, growth hormone gene transcription and growth hormone secretion."	.	2XDG	MDRRMWGAHVFCVLSPLPTVLGHMHPECDFITQLREDESACLQAAEEMPNTTLGCPATWDGLLCWPTAGSGEWVTLPCPDFFSHFSSESGAVKRDCTITGWSEPFPPYPVACPVPLELLAEEESYFSTVKIIYTVGHSISIVALFVAITILVALRRLHCPRNYVHTQLFTTFILKAGAVFLKDAALFHSDDTDHCSFSTVLCKVSVAASHFATMTNFSWLLAEAVYLNCLLASTSPSSRRAFWWLVLAGWGLPVLFTGTWVSCKLAFEDIACWDLDDTSPYWWIIKGPIVLSVGVNFGLFLNIIRILVRKLEPAQGSLHTQSQYWRLSKSTLFLIPLFGIHYIIFNFLPDNAGLGIRLPLELGLGSFQGFIVAILYCFLNQEVRTEISRKWHGHDPELLPAWRTRAKWTTPSRSAAKVLTSMC	Successful	Mullard A: 2010 FDA drug approvals. Nat Rev Drug Discov. 2011 Feb;10(2):82-5.	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors	.	Q02643
TT1OCL0	Ghrelin (GHRL)	Q9UBU3	GHRL_HUMAN	.	UNQ524/PRO1066; Motilin-related peptide; M46 protein; Growth hormone secretagogue; Growth hormone releasing peptide; Gastric peptide ghrelin; GHRL	GHRL	"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."	.	1P7X	MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRVQQRKESKKPPAKLQPRALAGWLRPEDGGQAEGAEDELEVRFNAPFDVGIKLSGVQYQQHSQALGKFLQDILWEEAKEAPADK	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	hsa04024:cAMP signaling pathway	"R-HSA-375276: Peptide ligand-binding receptors; R-HSA-416476: G alpha (q) signalling events; R-HSA-422085: Synthesis, secretion, and deacylation of Ghrelin"	.	Q9UBU3
TTWDC17	Growth hormone secretagogue receptor 1 (GHSR)	Q92847	GHSR_HUMAN	GPCR rhodopsin	Growth hormone secretagogue receptor; Ghrelin receptor; GHSR; GHS-R; GHRP; GH-releasing peptide receptor	GHSR	"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)."	.	.	MWNATPSEEPGFNLTLADLDWDASPGNDSLGDELLQLFPAPLLAGVTATCVALFVVGIAGNLLTMLVVSRFRELRTTTNLYLSSMAFSDLLIFLCMPLDLVRLWQYRPWNFGDLLCKLFQFVSESCTYATVLTITALSVERYFAICFPLRAKVVVTKGRVKLVIFVIWAVAFCSAGPIFVLVGVEHENGTDPWDTNECRPTEFAVRSGLLTVMVWVSSIFFFLPVFCLTVLYSLIGRKLWRRRRGDAVVGASLRDQNHKQTVKMLAVVVFAFILCWLPFHVGRYLFSKSFEPGSLEIAQISQYCNLVSFVLFYLSAAINPILYNIMSKKYRVAVFRLLGFEPFSQRKLSTLKDESSRAWTESSINT	Successful	National Cancer Institute Drug Dictionary (drug id 735530).	34	.	.	.	.	.	.	.	.	.	.	hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events	.	Q92847
TT40HS5	Gastric inhibitory polypeptide (GIP)	P09681	GIP_HUMAN	Glucagon	Glucose-dependent insulinotropic polypeptide; GIP	GIP	Potent stimulator of insulin secretion and relatively poor inhibitor of gastric acid secretion.	.	2QKH; 2OBU; 2L71; 2L70; 2B4N	MVATKTFALLLLSLFLAVGLGEKKEGHFSALPSLPVGSHAKVSSPQPRGPRYAEGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQREARALELASQANRKEEEAVEPQSSPAKNPSDEDLLRDLLIQELLACLLDQTNLCRLRSR	Literature-reported	NCBI GEO: archive for functional genomics data sets--update. Nucleic Acids Res. 2013 Jan;41(Database issue):D991-5.	.	.	.	.	.	.	.	.	.	.	.	hsa04911:Insulin secretion	R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors	.	P09681
TTYMKBE	Gastric inhibitory polypeptide receptor (GIPR)	P48546	GIPR_HUMAN	GPCR secretin	Glucosedependent insulinotropic polypeptide receptor; GIPR	GIPR	This is a receptor for GIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.	.	6DKJ; 4HJ0; 2QKH	MTTSPILQLLLRLSLCGLLLQRAETGSKGQTAGELYQRWERYRRECQETLAAAEPPSGLACNGSFDMYVCWDYAAPNATARASCPWYLPWHHHVAAGFVLRQCGSDGQWGLWRDHTQCENPEKNEAFLDQRLILERLQVMYTVGYSLSLATLLLALLILSLFRRLHCTRNYIHINLFTSFMLRAAAILSRDRLLPRPGPYLGDQALALWNQALAACRTAQIVTQYCVGANYTWLLVEGVYLHSLLVLVGGSEEGHFRYYLLLGWGAPALFVIPWVIVRYLYENTQCWERNEVKAIWWIIRTPILMTILINFLIFIRILGILLSKLRTRQMRCRDYRLRLARSTLTLVPLLGVHEVVFAPVTEEQARGALRFAKLGFEIFLSSFQGFLVSVLYCFINKEVQSEIRRGWHHCRLRRSLGEEQRQLPERAFRALPSGSGPGEVPTSRGLSSGTLPGPGNEASRELESYC	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction	R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors	.	P48546
TT4F7SL	Gap junction alpha-1 protein (GJA1)	P17302	CXA1_HUMAN	Gap junction-forming connexin	Gap junction 43 kDa heart protein; GJAL; Cx43; Connexin-43; Connexin 43	GJA1	"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."	.	2LL2	MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVDMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSIFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGKSDPYHATSGALSPAKDCGSQKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNSKKLAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI	Clinical trial	Company report (FirstString Research)	25	TC=1.A.24	.	connexin family. Alpha-type (group II) subfamily.	.	.	Connexin; Gap junction alpha-1 protein (Cx43)	PF00029; PF03508	PF00029; Connexin; PF03508; Connexin43	.	.	hsa04540:Gap junction; hsa05412:Arrhythmogenic right ventricular cardiomyopathy (ARVC)	R-HSA-190840:Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane; R-HSA-190861:Gap junction assembly	.	P17302
TTQMI2N	Connexin-62 (Cx62)	Q969M2	CXA10_HUMAN	Gap junction-forming connexin	Gap junction alpha-10 protein; CX62	GJA10	"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."	.	.	MGDWNLLGGILEEVHSHSTIVGKIWLTILFIFRMLVLRVAAEDVWDDEQSAFACNTRQPGCNNICYDDAFPISLIRFWVLQIIFVSSPSLVYMGHALYRLRAFEKDRQRKKSHLRAQMENPDLDLEEQQRIDRELRRLEEQKRIHKVPLKGCLLRTYVLHILTRSVLEVGFMIGQYILYGFQMHPLYKCTQPPCPNAVDCFVSRPTEKTIFMLFMHSIAAISLLLNILEIFHLGIRKIMRTLYKKSSSEGIEDETGPPFHLKKYSVAQQCMICSSLPERISPLQANNQQQVIRVNVPKSKTMWQIPQPRQLEVDPSNGKKDWSEKDQHSGQLHVHSPCPWAGSAGNQHLGQQSDHSSFGLQNTMSQSWLGTTTAPRNCPSFAVGTWEQSQDPEPSGEPLTDLHSHCRDSEGSMRESGVWIDRSRPGSRKASFLSRLLSEKRHLHSDSGSSGSRNSSCLDFPHWENSPSPLPSVTGHRTSMVRQAALPIMELSQELFHSGCFLFPFFLPGVCMYVCVDREADGGGDYLWRDKIIHSIHSVKFNS	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 734).	0	TC=1.A.24	.	connexin family. Alpha-type (group II) subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	.	.	.	R-HSA-112303: Electric Transmission Across Gap Junctions; R-HSA-190861: Gap junction assembly	.	Q969M2
TTFZRG0	Gap junction alpha-3 protein (Cx46)	Q9Y6H8	CXA3_HUMAN	Gap junction-forming connexin	Connexin-46	GJA3	"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."	.	.	MGDWSFLGRLLENAQEHSTVIGKVWLTVLFIFRILVLGAAAEDVWGDEQSDFTCNTQQPGCENVCYDRAFPISHIRFWALQIIFVSTPTLIYLGHVLHIVRMEEKKKEREEEEQLKRESPSPKEPPQDNPSSRDDRGRVRMAGALLRTYVFNIIFKTLFEVGFIAGQYFLYGFELKPLYRCDRWPCPNTVDCFISRPTEKTIFIIFMLAVACASLLLNMLEIYHLGWKKLKQGVTSRLGPDASEAPLGTADPPPLPPSSRPPAVAIGFPPYYAHTAAPLGQARAVGYPGAPPPAADFKLLALTEARGKGQSAKLYNGHHHLLMTEQNWANQAAERQPPALKAYPAASTPAAPSPVGSSSPPLAHEAEAGAAPLLLDGSGSSLEGSALAGTPEEEEQAVTTAAQMHQPPLPLGDPGRASKASRASSGRARPEDLAI	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 730).	0	TC=1.A.24	.	connexin family. Alpha-type (group II) subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	1.A.24.1.5	The Gap Junction-forming Connexin (Connexin) Family	.	R-HSA-190861: Gap junction assembly	.	Q9Y6H8
TTQO1VY	Gap junction alpha-4 protein (Cx37)	P35212	CXA4_HUMAN	Gap junction-forming connexin	Connexin-37	GJA4	"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."	.	.	MGDWGFLEKLLDQVQEHSTVVGKIWLTVLFIFRILILGLAGESVWGDEQSDFECNTAQPGCTNVCYDQAFPISHIRYWVLQFLFVSTPTLVYLGHVIYLSRREERLRQKEGELRALPAKDPQVERALAAVERQMAKISVAEDGRLRIRGALMGTYVASVLCKSVLEAGFLYGQWRLYGWTMEPVFVCQRAPCPYLVDCFVSRPTEKTIFIIFMLVVGLISLVLNLLELVHLLCRCLSRGMRARQGQDAPPTQGTSSDPYTDQVFFYLPVGQGPSSPPCPTYNGLSSSEQNWANLTTEERLASSRPPLFLDPPPQNGQKPPSRPSSSASKKQYV	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 725).	0	TC=1.A.24	.	connexin family. Alpha-type (group II) subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	1.A.24.1.6	The Gap Junction-forming Connexin (Connexin) Family	.	R-HSA-190861: Gap junction assembly	.	P35212
TTFQKZ7	Gap junction alpha-5 protein (Cx40)	P36382	CXA5_HUMAN	Gap junction-forming connexin	Connexin-40	GJA5	"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."	.	.	MGDWSFLGNFLEEVHKHSTVVGKVWLTVLFIFRMLVLGTAAESSWGDEQADFRCDTIQPGCQNVCYDQAFPISHIRYWVLQIIFVSTPSLVYMGHAMHTVRMQEKRKLREAERAKEVRGSGSYEYPVAEKAELSCWEEGNGRIALQGTLLNTYVCSILIRTTMEVGFIVGQYFIYGIFLTTLHVCRRSPCPHPVNCYVSRPTEKNVFIVFMLAVAALSLLLSLAELYHLGWKKIRQRFVKPRQHMAKCQLSGPSVGIVQSCTPPPDFNQCLENGPGGKFFNPFSNNMASQQNTDNLVTEQVRGQEQTPGEGFIQVRYGQKPEVPNGVSPGHRLPHGYHSDKRRLSKASSKARSDDLSV	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 726).	0	TC=1.A.24	.	connexin family. Alpha-type (group II) subfamily.	.	.	Connexin; Connexin 40 C-terminal domain	PF00029; PF16791	PF00029; Connexin; PF16791; Connexin40_C	.	.	.	R-HSA-190861: Gap junction assembly	.	P36382
TTJ7ATH	Gap junction alpha-8 protein (Cx50)	P48165	CXA8_HUMAN	Gap junction-forming connexin	Lens fiber protein MP70; GJA8; Cx50; Connexin50	GJA8	"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."	.	.	MGDWSFLGNILEEVNEHSTVIGRVWLTVLFIFRILILGTAAEFVWGDEQSDFVCNTQQPGCENVCYDEAFPISHIRLWVLQIIFVSTPSLMYVGHAVHYVRMEEKRKSREAEELGQQAGTNGGPDQGSVKKSSGSKGTKKFRLEGTLLRTYICHIIFKTLFEVGFIVGHYFLYGFRILPLYRCSRWPCPNVVDCFVSRPTEKTIFILFMLSVASVSLFLNVMELGHLGLKGIRSALKRPVEQPLGEIPEKSLHSIAVSSIQKAKGYQLLEEEKIVSHYFPLTEVGMVETSPLPAKPFNQFEEKISTGPLGDLSRGYQETLPSYAQVGAQEVEGEGPPAEEGAEPEVGEKKEEAERLTTEEQEKVAVPEGEKVETPGVDKEGEKEEPQSEKVSKQGLPAEKTPSLCPELTTDDARPLSRLSKASSRARSDDLTV	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 732).	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-190861: Gap junction assembly	.	P48165
TTYP9NL	Connexin-59 (Cx59)	P57773	CXA9_HUMAN	Gap junction-forming connexin	Gap junction alpha-9 protein; GJA10; Cx58; Connexin-58	GJA9	"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."	.	.	MGDWNLLGDTLEEVHIHSTMIGKIWLTILFIFRMLVLGVAAEDVWNDEQSGFICNTEQPGCRNVCYDQAFPISLIRYWVLQVIFVSSPSLVYMGHALYRLRVLEEERQRMKAQLRVELEEVEFEMPRDRRRLEQELCQLEKRKLNKAPLRGTLLCTYVIHIFTRSVVEVGFMIGQYLLYGFHLEPLFKCHGHPCPNIIDCFVSRPTEKTIFLLFMQSIATISLFLNILEIFHLGFKKIKRGLWGKYKLKKEHNEFHANKAKQNVAKYQSTSANSLKRLPSAPDYNLLVEKQTHTAVYPSLNSSSVFQPNPDNHSVNDEKCILDEQETVLSNEISTLSTSCSHFQHISSNNNKDTHKIFGKELNGNQLMEKRETEGKDSKRNYYSRGHRSIPGVAIDGENNMRQSPQTVFSLPANCDWKPRWLRATWGSSTEHENRGSPPKGNLKGQFRKGTVRTLPPSQGDSQSLDIPNTADSLGGLSFEPGLVRTCNNPVCPPNHVVSLTNNLIGRRVPTDLQI	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 733).	0	TC=1.A.24	.	connexin family. Alpha-type (group II) subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	.	.	.	R-HSA-190861: Gap junction assembly	.	P57773
TTSJIRP	Connexin 32 messenger RNA (GJB1 mRNA)	P08034	CXB1_HUMAN	mRNA target	Gap junction beta-1 protein (mRNA); GAP junction 28 kDa liver protein (mRNA); CX32 (mRNA)	GJB1	"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."	.	5KK9; 1TXH	MNWTGLYTLLSGVNRHSTAIGRVWLSVIFIFRIMVLVVAAESVWGDEKSSFICNTLQPGCNSVCYDQFFPISHVRLWSLQLILVSTPALLVAMHVAHQQHIEKKMLRLEGHGDPLHLEEVKRHKVHISGTLWWTYVISVVFRLLFEAVFMYVFYLLYPGYAMVRLVKCDVYPCPNTVDCFVSRPTEKTVFTVFMLAASGICIILNVAEVVYLIIRACARRAQRRSNPPSRKGSGFGHRLSPEYKQNEINKLLSEQDGSLKDILRRSPGTGAGLAEKSDRCSAC	Literature-reported	"Connexin Antibodies. Report from santa cruz biotechnology, inc. Santa cruz biotechnology. 2009."	0	mRNA	mRNA target	.	.	.	Connexin	PF00029	PF00029; Connexin	.	.	.	R-HSA-190704: Oligomerization of connexins into connexons; R-HSA-190827: Transport of connexins along the secretory pathway; R-HSA-190861: Gap junction assembly	.	P08034
TTHWA40	Connexin-32 (Cx32)	P08034	CXB1_HUMAN	Gap junction-forming connexin	Gap junction beta-1 protein; GAP junction 28 kDa liver protein; CX32	GJB1	"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."	.	5KK9; 1TXH	MNWTGLYTLLSGVNRHSTAIGRVWLSVIFIFRIMVLVVAAESVWGDEKSSFICNTLQPGCNSVCYDQFFPISHVRLWSLQLILVSTPALLVAMHVAHQQHIEKKMLRLEGHGDPLHLEEVKRHKVHISGTLWWTYVISVVFRLLFEAVFMYVFYLLYPGYAMVRLVKCDVYPCPNTVDCFVSRPTEKTVFTVFMLAASGICIILNVAEVVYLIIRACARRAQRRSNPPSRKGSGFGHRLSPEYKQNEINKLLSEQDGSLKDILRRSPGTGAGLAEKSDRCSAC	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 723).	0	TC=1.A.24	.	connexin family. Beta-type (group I) subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	1.A.24.1.3	The Gap Junction-forming Connexin (Connexin) Family	.	R-HSA-190704: Oligomerization of connexins into connexons; R-HSA-190827: Transport of connexins along the secretory pathway; R-HSA-190861: Gap junction assembly	.	P08034
TTRGZX3	Gap junction beta-2 protein (Cx26)	P29033	CXB2_HUMAN	Gap junction-forming connexin	Connexin-26	GJB2	"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."	.	5KJG; 5KJ3; 5ERA; 5ER7; 3IZ2	MDWGTLQTILGGVNKHSTSIGKIWLTVLFIFRIMILVVAAKEVWGDEQADFVCNTLQPGCKNVCYDHYFPISHIRLWALQLIFVSTPALLVAMHVAYRRHEKKRKFIKGEIKSEFKDIEEIKTQKVRIEGSLWWTYTSSIFFRVIFEAAFMYVFYVMYDGFSMQRLVKCNAWPCPNTVDCFVSRPTEKTVFTVFMIAVSGICILLNVTELCYLLIRYCSGKSKKPV	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 716).	0	TC=1.A.24	.	connexin family. Beta-type (group I) subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	1.A.24.1.3	The Gap Junction-forming Connexin (Connexin) Family	.	R-HSA-190704: Oligomerization of connexins into connexons; R-HSA-190827: Transport of connexins along the secretory pathway; R-HSA-190861: Gap junction assembly; R-HSA-190872: Transport of connexons to the plasma membrane	.	P29033
TTVRQ8L	Gap junction beta-3 protein (Cx31)	O75712	CXB3_HUMAN	Gap junction-forming connexin	Connexin-31; CX31	GJB3	"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."	.	.	MDWKTLQALLSGVNKYSTAFGRIWLSVVFVFRVLVYVVAAERVWGDEQKDFDCNTKQPGCTNVCYDNYFPISNIRLWALQLIFVTCPSLLVILHVAYREERERRHRQKHGDQCAKLYDNAGKKHGGLWWTYLFSLIFKLIIEFLFLYLLHTLWHGFNMPRLVQCANVAPCPNIVDCYIARPTEKKIFTYFMVGASAVCIVLTICELCYLICHRVLRGLHKDKPRGGCSPSSSASRASTCRCHHKLVEAGEVDPDPGNNKLQASAPNLTPI	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 720).	0	TC=1.A.24	.	connexin family. Beta-type (group I) subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	1.A.24.1.10	The Gap Junction-forming Connexin (Connexin) Family	.	R-HSA-190861: Gap junction assembly	.	O75712
TTBRDFI	Gap junction beta-4 protein (Cx30.3)	Q9NTQ9	CXB4_HUMAN	Gap junction-forming connexin	Connexin-30.3	GJB4	"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."	.	.	MNWAFLQGLLSGVNKYSTVLSRIWLSVVFIFRVLVYVVAAEEVWDDEQKDFVCNTKQPGCPNVCYDEFFPVSHVRLWALQLILVTCPSLLVVMHVAYREERERKHHLKHGPNAPSLYDNLSKKRGGLWWTYLLSLIFKAAVDAGFLYIFHRLYKDYDMPRVVACSVEPCPHTVDCYISRPTEKKVFTYFMVTTAAICILLNLSEVFYLVGKRCMEIFGPRHRRPRCRECLPDTCPPYVLSQGGHPEDGNSVLMKAGSAPVDAGGYP	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 719).	0	TC=1.A.24	.	connexin family. Beta-type (group I) subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	.	.	.	R-HSA-190861: Gap junction assembly	.	Q9NTQ9
TTL9MHP	Gap junction beta-5 protein (Cx31.1)	O95377	CXB5_HUMAN	Gap junction-forming connexin	Connexin-31.1	GJB5	"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."	.	.	MNWSIFEGLLSGVNKYSTAFGRIWLSLVFIFRVLVYLVTAERVWSDDHKDFDCNTRQPGCSNVCFDEFFPVSHVRLWALQLILVTCPSLLVVMHVAYREVQEKRHREAHGENSGRLYLNPGKKRGGLWWTYVCSLVFKASVDIAFLYVFHSFYPKYILPPVVKCHADPCPNIVDCFISKPSEKNIFTLFMVATAAICILLNLVELIYLVSKRCHECLAARKAQAMCTGHHPHGTTSSCKQDDLLSGDLIFLGSDSHPPLLPDRPRDHVKKTIL	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 721).	0	TC=1.A.24	.	connexin family. Beta-type (group I) subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	.	.	.	R-HSA-190861: Gap junction assembly	.	O95377
TTAU8SJ	Connexin-30 (Cx30)	O95452	CXB6_HUMAN	Gap junction-forming connexin	Gap junction beta-6 protein	GJB6	"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."	.	.	MDWGTLHTFIGGVNKHSTSIGKVWITVIFIFRVMILVVAAQEVWGDEQEDFVCNTLQPGCKNVCYDHFFPVSHIRLWALQLIFVSTPALLVAMHVAYYRHETTRKFRRGEKRNDFKDIEDIKKQKVRIEGSLWWTYTSSIFFRIIFEAAFMYVFYFLYNGYHLPWVLKCGIDPCPNLVDCFISRPTEKTVFTIFMISASVICMLLNVAELCYLLLKVCFRRSKRAQTQKNHPNHALKESKQNEMNELISDSGQNAITGFPS	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 717).	0	TC=1.A.24	.	connexin family. Beta-type (group I) subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	.	.	.	R-HSA-190861: Gap junction assembly	.	O95452
TTZ7POK	Connexin-25 (Cx25)	Q6PEY0	CXB7_HUMAN	Gap junction-forming connexin	Gap junction beta-7 protein; CX25	GJB7	"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."	.	.	MSWMFLRDLLSGVNKYSTGTGWIWLAVVFVFRLLVYMVAAEHVWKDEQKEFECNSRQPGCKNVCFDDFFPISQVRLWALQLIMVSTPSLLVVLHVAYHEGREKRHRKKLYVSPGTMDGGLWYAYLISLIVKTGFEIGFLVLFYKLYDGFSVPYLIKCDLKPCPNTVDCFISKPTEKTIFILFLVITSCLCIVLNFIELSFLVLKCFIKCCLQKYLKKPQVLSV	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 715).	0	TC=1.A.24	.	connexin family. Beta-type (group I) subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	.	.	.	R-HSA-190861: Gap junction assembly	.	Q6PEY0
TTEP7OC	Connexin-45 (Cx45)	P36383	CXG1_HUMAN	Gap junction-forming connexin	Gap junction gamma-1 protein; Gap junction alpha-7 protein; GJA7	GJC1	"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."	.	3SHW	MSWSFLTRLLEEIHNHSTFVGKIWLTVLIVFRIVLTAVGGESIYYDEQSKFVCNTEQPGCENVCYDAFAPLSHVRFWVFQIILVATPSVMYLGYAIHKIAKMEHGEADKKAARSKPYAMRWKQHRALEETEEDNEEDPMMYPEMELESDKENKEQSQPKPKHDGRRRIREDGLMKIYVLQLLARTVFEVGFLIGQYFLYGFQVHPFYVCSRLPCPHKIDCFISRPTEKTIFLLIMYGVTGLCLLLNIWEMLHLGFGTIRDSLNSKRRELEDPGAYNYPFTWNTPSAPPGYNIAVKPDQIQYTELSNAKIAYKQNKANTAQEQQYGSHEENLPADLEALQREIRMAQERLDLAVQAYSHQNNPHGPREKKAKVGSKAGSNKSTASSKSGDGKTSVWI	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 729).	0	TC=1.A.24	.	connexin family. Gamma-type subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	1.A.24.2.4	The Gap Junction-forming Connexin (Connexin) Family	.	R-HSA-112303: Electric Transmission Across Gap Junctions; R-HSA-190861: Gap junction assembly	.	P36383
TTPOCAL	Gap junction gamma-2 protein (Cx47)	Q5T442	CXG2_HUMAN	Gap junction-forming connexin	Gap junction alpha-12 protein; GJA12; Cx46.6; Connexin-47; Connexin-46.6	GJC2	"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."	.	.	MTNMSWSFLTRLLEEIHNHSTFVGKVWLTVLVVFRIVLTAVGGEAIYSDEQAKFTCNTRQPGCDNVCYDAFAPLSHVRFWVFQIVVISTPSVMYLGYAVHRLARASEQERRRALRRRPGPRRAPRAHLPPPHAGWPEPADLGEEEPMLGLGEEEEEEETGAAEGAGEEAEEAGAEEACTKAVGADGKAAGTPGPTGQHDGRRRIQREGLMRVYVAQLVARAAFEVAFLVGQYLLYGFEVRPFFPCSRQPCPHVVDCFVSRPTEKTVFLLVMYVVSCLCLLLNLCEMAHLGLGSAQDAVRGRRGPPASAPAPAPRPPPCAFPAAAAGLACPPDYSLVVRAAERARAHDQNLANLALQALRDGAAAGDRDRDSSPCVGLPAASRGPPRAGAPASRTGSATSAGTVGEQGRPGTHERPGAKPRAGSEKGSASSRDGKTTVWI	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 731).	0	TC=1.A.24	.	connexin family. Gamma-type subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	.	.	.	R-HSA-190861: Gap junction assembly	.	Q5T442
TTUW608	Gap junction gamma-3 protein (Cx30.2)	Q8NFK1	CXG3_HUMAN	Gap junction-forming connexin	Gap junction epsilon-1 protein; GJE1; Cx31.3; Connexin-31.3; Connexin-30.2	GJC3	"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."	.	.	MCGRFLRRLLAEESRRSTPVGRLLLPVLLGFRLVLLAASGPGVYGDEQSEFVCHTQQPGCKAACFDAFHPLSPLRFWVFQVILVAVPSALYMGFTLYHVIWHWELSGKGKEEETLIQGREGNTDVPGAGSLRLLWAYVAQLGARLVLEGAALGLQYHLYGFQMPSSFACRREPCLGSITCNLSRPSEKTIFLKTMFGVSGFCLLFTFLELVLLGLGRWWRTWKHKSSSSKYFLTSESTRRHKKATDSLPVVETKEQFQEAVPGRSLAQEKQRPVGPRDA	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 718).	0	TC=1.A.24	.	connexin family. Gamma-type subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	1.A.24.1.7	The Gap Junction-forming Connexin (Connexin) Family	.	.	.	Q8NFK1
TTOZAFI	Gap junction delta-2 protein (Cx36)	Q9UKL4	CXD2_HUMAN	Gap junction-forming connexin	GJA9; Connexin-36	GJD2	"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."	.	2N6A	MGEWTILERLLEAAVQQHSTMIGRILLTVVVIFRILIVAIVGETVYDDEQTMFVCNTLQPGCNQACYDRAFPISHIRYWVFQIIMVCTPSLCFITYSVHQSAKQRERRYSTVFLALDRDPPESIGGPGGTGGGGSGGGKREDKKLQNAIVNGVLQNTENTSKETEPDCLEVKELTPHPSGLRTASKSKLRRQEGISRFYIIQVVFRNALEIGFLVGQYFLYGFSVPGLYECNRYPCIKEVECYVSRPTEKTVFLVFMFAVSGICVVLNLAELNHLGWRKIKLAVRGAQAKRKSIYEIRNKDLPRVSVPNFGRTQSSDSAYV	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 724).	0	TC=1.A.24	.	connexin family. Delta-type subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	1.A.24.1.13	The Gap Junction-forming Connexin (Connexin) Family	hsa04540: Gap junction	R-HSA-112303: Electric Transmission Across Gap Junctions; R-HSA-190861: Gap junction assembly	.	Q9UKL4
TT7C18W	Gap junction delta-3 protein (Cx31.9)	Q8N144	CXD3_HUMAN	Gap junction-forming connexin	Gap junction chi-1 protein; Gap junction alpha-11 protein; GJC1; GJA11; Connexin-31.9	GJD3	"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."	.	.	MGEWAFLGSLLDAVQLQSPLVGRLWLVVMLIFRILVLATVGGAVFEDEQEEFVCNTLQPGCRQTCYDRAFPVSHYRFWLFHILLLSAPPVLFVVYSMHRAGKEAGGAEAAAQCAPGLPEAQCAPCALRARRARRCYLLSVALRLLAELTFLGGQALLYGFRVAPHFACAGPPCPHTVDCFVSRPTEKTVFVLFYFAVGLLSALLSVAELGHLLWKGRPRAGERDNRCNRAHEEAQKLLPPPPPPPPPPALPSRRPGPEPCAPPAYAHPAPASLRECGSGRGKASPATGRRDLAI	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 722).	0	TC=1.A.24	.	connexin family. Delta-type subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	.	.	.	R-HSA-190861: Gap junction assembly	.	Q8N144
TTL07NQ	Gap junction delta-4 protein (Cx40.1)	Q96KN9	CXD4_HUMAN	Gap junction-forming connexin	Connexin-40.1; CX40.1	GJD4	"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."	.	.	MEGVDLLGFLIITLNCNVTMVGKLWFVLTMLLRMLVIVLAGRPVYQDEQERFVCNTLQPGCANVCYDVFSPVSHLRFWLIQGVCVLLPSAVFSVYVLHRGATLAALGPRRCPDPREPASGQRRCPRPFGERGGLQVPDFSAGYIIHLLLRTLLEAAFGALHYFLFGFLAPKKFPCTRPPCTGVVDCYVSRPTEKSLLMLFLWAVSALSFLLGLADLVCSLRRRMRRRPGPPTSPSIRKQSGASGHAEGRRTDEEGGREEEGAPAPPGARAGGEGAGSPRRTSRVSGHTKIPDEDESEVTSSASEKLGRQPRGRPHREAAQDPRGSGSEEQPSAAPSRLAAPPSCSSLQPPDPPASSSGAPHLRARKSEWV	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 727).	0	TC=1.A.24	.	connexin family. Delta-type subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	1.A.24.1.8	The Gap Junction-forming Connexin (Connexin) Family	.	R-HSA-190861: Gap junction assembly	.	Q96KN9
TTDQPXA	Connexin-23 (Cx23)	A6NN92	CXE1_HUMAN	Gap junction-forming connexin	Putative gap junction epsilon-1 protein	GJE1	"Does not form functional gap junctions. Mediates calcium-independent ATP release, suggesting activity as a hemichannel."	.	.	MSLNYIKNFYEGCVKPPTVIGQFHTLFFGSIRIFFLGVLGFAVYGNEALHFICDPDKREVNLFCYNQFRPITPQVSFSALQLVIVLVPGALFHLYAACKSINQECILQKPIYTIIYILSVLLRISLAAIAFWLQIYLFGFQVKSLYLCDARSLGENMIIRCMVPEHFEKTIFLIAINTFTTITILLFVAEIFEIIFRRLYFPFRQ	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 714).	0	TC=1.A.24	.	connexin family. Beta-type (group I) subfamily.	.	.	Connexin	PF00029	PF00029; Connexin	.	.	.	.	.	A6NN92
TTIS03D	Alpha-galactosidase A (GLA)	P06280	AGAL_HUMAN	Glycosylase	Melibiase; INN=Agalsidase; Alpha-D-galactoside galactohydrolase; Alpha-D-galactosidase A	GLA	"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."	EC 3.2.1.22	4NXS; 3TV8; 3S5Z; 3S5Y; 3LXC	MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENTMQMSLKDLL	Successful	AT-1001: a high-affinity alpha3beta4 nAChR ligand with novel nicotine-suppressive pharmacology. Br J Pharmacol. 2015 Apr;172(7):1834-45.	34	.	.	.	.	.	.	.	.	.	.	hsa00052:Galactose metabolism; hsa00561:Glycerolipid metabolism; hsa00600:Sphingolipid metabolism; hsa00603:Glycosphingolipid biosynthesis - globo series; hsa04142:Lysosome	R-HSA-1660662:Glycosphingolipid metabolism	MetaCyc:HS02389-MON	P06280
TTHF0JV	HUMAN alpha-galactosidase A (GLA)	P06280	AGAL_HUMAN	Glycosylase	Melibiase; Agalsidase; Alpha-D-galactoside galactohydrolase; Alpha-D-galactosidase A	GLA	"Human protein galactosidase alpha interacts with SARS-CoV-2 Nsp14 protein with high significance, which indicates GLA as a potential therapeutic target."	EC 3.2.1.22	4NXS; 3TV8; 3S5Z; 3S5Y; 3LXC	MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENTMQMSLKDLL	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa00052: Galactose metabolism; hsa00561: Glycerolipid metabolism; hsa00600: Sphingolipid metabolism; hsa00603: Glycosphingolipid biosynthesis - globo and isoglobo series; hsa01100: Metabolic pathways; hsa04142: Lysosome	R-HSA-1660662: Glycosphingolipid metabolism; R-HSA-6798695: Neutrophil degranulation	MetaCyc:HS02389-MON	P06280
TTNGJPH	Beta-galactosidase (GLB1)	P16278	BGAL_HUMAN	.	Lactase; Elastin receptor 1; ELNR1; Acid beta-galactosidase	GLB1	"Isoform 1: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans."	EC 3.2.1.23	3WF4; 3WF3; 3WF2; 3WF1; 3WF0	MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRTTLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENMGRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWGHRDSGHHDEAWAHNSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIGSSVTYDHPSKPVEKRLMPPPPQKNKDSWLDHV	Preclinical	Turnover of beta-galactosidase in fibroblasts from patients with genetically different types of beta-galactosidase deficiency. Biochem J. 1981 Oct 15;200(1):143-51.	.	.	.	.	.	.	.	.	.	.	.	hsa00052: Galactose metabolism; hsa00511: Other glycan degradation; hsa00531: Glycosaminoglycan degradation; hsa00600: Sphingolipid metabolism; hsa00604: Glycosphingolipid biosynthesis - ganglio series; hsa01100: Metabolic pathways; hsa04142: Lysosome	R-HSA-1660662: Glycosphingolipid metabolism; R-HSA-2022857: Keratan sulfate degradation; R-HSA-2024096: HS-GAG degradation; R-HSA-2206308: MPS IV - Morquio syndrome B; R-HSA-4085001: Sialic acid metabolism; R-HSA-4341670: Defective NEU1 causes sialidosis; R-HSA-6798695: Neutrophil degranulation	.	P16278
TTJOMH6	Zinc finger protein GLI1 (Gli1)	P08151	GLI1_HUMAN	.	Oncogene GLI; Glioma-associated oncogene; GLI	GLI1	"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."	.	5OM0; 4KMD; 4BLB; 2GLI	MFNSMTPPPISSYGEPCCLRPLPSQGAPSVGTEGLSGPPFCHQANLMSGPHSYGPARETNSCTEGPLFSSPRSAVKLTKKRALSISPLSDASLDLQTVIRTSPSSLVAFINSRCTSPGGSYGHLSIGTMSPSLGFPAQMNHQKGPSPSFGVQPCGPHDSARGGMIPHPQSRGPFPTCQLKSELDMLVGKCREEPLEGDMSSPNSTGIQDPLLGMLDGREDLEREEKREPESVYETDCRWDGCSQEFDSQEQLVHHINSEHIHGERKEFVCHWGGCSRELRPFKAQYMLVVHMRRHTGEKPHKCTFEGCRKSYSRLENLKTHLRSHTGEKPYMCEHEGCSKAFSNASDRAKHQNRTHSNEKPYVCKLPGCTKRYTDPSSLRKHVKTVHGPDAHVTKRHRGDGPLPRAPSISTVEPKREREGGPIREESRLTVPEGAMKPQPSPGAQSSCSSDHSPAGSAANTDSGVEMTGNAGGSTEDLSSLDEGPCIAGTGLSTLRRLENLRLDQLHQLRPIGTRGLKLPSLSHTGTTVSRRVGPPVSLERRSSSSSSISSAYTVSRRSSLASPFPPGSPPENGASSLPGLMPAQHYLLRARYASARGGGTSPTAASSLDRIGGLPMPPWRSRAEYPGYNPNAGVTRRASDPAQAADRPAPARVQRFKSLGCVHTPPTVAGGGQNFDPYLPTSVYSPQPPSITENAAMDARGLQEEPEVGTSMVGSGLNPYMDFPPTDTLGYGGPEGAAAEPYGARGPGSLPLGPGPPTNYGPNPCPQQASYPDPTQETWGEFPSHSGLYPGPKALGGTYSQCPRLEHYGQVQVKPEQGCPVGSDSTGLAPCLNAHPSEGPPHPQPLFSHYPQPSPPQYLQSGPYTQPPPDYLPSEPRPCLDFDSPTHSTGQLKAQLVCNYVQSQQELLWEGGGREDAPAQEPSYQSPKFLGGSQVSPSRAKAPVNTYGPGFGPNLPNHKSGSYPTPSPCHENFVVGANRASHRAAAPPRLLPPLPTCYGPLKVGGTNPSCGHPEVGRLGGGPALYPPPEGQVCNPLDSLDLDNTQLDFVAILDEPQGLSPPPSHDQRGSSGHTPPPSGPPNMAVGNMSVLLRSLPGETEFLNSSA	Patented-recorded	Evaluation of WO2014207069 A1: Multitarget Hedgehog pathway inhibitors and uses thereof.Expert Opin Ther Pat. 2016;26(4):529-35.	15.5	.	GLI C2H2-type zinc-finger	GLI C2H2-type zinc-finger protein family.	.	.	"Zinc finger, C2H2 type"	PF00096	PF00096; zf-C2H2	.	.	hsa04024: cAMP signaling pathway; hsa04340: Hedgehog signaling pathway; hsa05200: Pathways in cancer; hsa05217: Basal cell carcinoma	R-HSA-5610780: Degradation of GLI1 by the proteasome; R-HSA-5610787: Hedgehog 'off' state; R-HSA-5632684: Hedgehog 'on' state; R-HSA-5635851: GLI proteins bind promoters of Hh responsive genes to promote transcription	.	P08151
TT045OH	GLI2 messenger RNA (GLI2 mRNA)	P10070	GLI2_HUMAN	mRNA target	Zinc finger protein GLI2 (mRNA); Tax helper protein (mRNA); THP (mRNA); GLI family zinc finger protein 2 (mRNA)	GLI2	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.	.	.	METSASATASEKQEAKSGILEAAGFPDPGKKASPLVVAAAAAAAVAAQGVPQHLLPPFHAPLPIDMRHQEGRYHYEPHSVHGVHGPPALSGSPVISDISLIRLSPHPAGPGESPFNAPHPYVNPHMEHYLRSVHSSPTLSMISAARGLSPADVAQEHLKERGLFGLPAPGTTPSDYYHQMTLVAGHPAPYGDLLMQSGGAASAPHLHDYLNPVDVSRFSSPRVTPRLSRKRALSISPLSDASLDLQRMIRTSPNSLVAYINNSRSSSAASGSYGHLSAGALSPAFTFPHPINPVAYQQILSQQRGLGSAFGHTPPLIQPSPTFLAQQPMALTSINATPTQLSSSSNCLSDTNQNKQSSESAVSSTVNPVAIHKRSKVKTEPEGLRPASPLALTQGQVSGHGSCGCALPLSQEQLADLKEDLDRDDCKQEAEVVIYETNCHWEDCTKEYDTQEQLVHHINNEHIHGEKKEFVCRWQACTREQKPFKAQYMLVVHMRRHTGEKPHKCTFEGCSKAYSRLENLKTHLRSHTGEKPYVCEHEGCNKAFSNASDRAKHQNRTHSNEKPYICKIPGCTKRYTDPSSLRKHVKTVHGPDAHVTKKQRNDVHLRTPLLKENGDSEAGTEPGGPESTEASSTSQAVEDCLHVRAIKTESSGLCQSSPGAQSSCSSEPSPLGSAPNNDSGVEMPGTGPGSLGDLTALDDTPPGADTSALAAPSAGGLQLRKHMTTMHRFEQLKKEKLKSLKDSCSWAGPTPHTRNTKLPPLPGSGSILENFSGSGGGGPAGLLPNPRLSELSASEVTMLSQLQERRDSSTSTVSSAYTVSRRSSGISPYFSSRRSSEASPLGAGRPHNASSADSYDPISTDASRRSSEASQCSGGSGLLNLTPAQQYSLRAKYAAATGGPPPTPLPGLERMSLRTRLALLDAPERTLPAGCPRPLGPRRGSDGPTYGHGHAGAAPAFPHEAPGGGARRASDPVRRPDALSLPRVQRFHSTHNVNPGPLPPCADRRGLRLQSHPSTDGGLARGAYSPRPPSISENVAMEAVAAGVDGAGPEADLGLPEDDLVLPDDVVQYIKAHASGALDEGTGQVYPTESTGFSDNPRLPSPGLHGQRRMVAADSNVGPSAPMLGGCQLGFGAPSSLNKNNMPVQWNEVSSGTVDALASQVKPPPFPQGNLAVVQQKPAFGQYPGYSPQGLQASPGGLDSTQPHLQPRSGAPSQGIPRVNYMQQLRQPVAGSQCPGMTTTMSPHACYGQVHPQLSPSTISGALNQFPQSCSNMPAKPGHLGHPQQTEVAPDPTTMGNRHRELGVPDSALAGVPPPHPVQSYPQQSHHLAASMSQEGYHQVPSLLPARQPGFMEPQTGPMGVATAGFGLVQPRPPLEPSPTGRHRGVRAVQQQLAYARATGHAMAAMPSSQETAEAVPKGAMGNMGSVPPQPPPQDAGGAPDHSMLYYYGQIHMYEQDGGLENLGSCQVMRSQPPQPQACQDSIQPQPLPSPGVNQVSSTVDSQLLEAPQIDFDAIMDDGDHSSLFSGALSPSLLHSLSQNSSRLTTPRNSLTLPSIPAGISNMAVGDMSSMLTSLAEESKFLNMMT	Literature-reported	Long non-coding RNA metastasis-associated lung adenocarcinoma transcript 1 regulates the expression of Gli2 by miR-202 to strengthen gastric cancer... Biomed Pharmacother. 2017 Jan;85:264-271.	.	mRNA	mRNA target	.	.	.	"Zinc finger, C2H2 type"	PF00096	PF00096; zf-C2H2	.	.	hsa04340: Hedgehog signaling pathway; hsa04390: Hippo signaling pathway; hsa05200: Pathways in cancer; hsa05217: Basal cell carcinoma	R-HSA-5610783: Degradation of GLI2 by the proteasome; R-HSA-5610787: Hedgehog 'off' state; R-HSA-5632684: Hedgehog 'on' state; R-HSA-5635851: GLI proteins bind promoters of Hh responsive genes to promote transcription; R-HSA-8941284: RUNX2 regulates chondrocyte maturation	.	P10070
TTEQF1O	Glioma pathogenesis-related protein 1 (GLIPR1)	P48060	GLIP1_HUMAN	Cysteine-rich secretory protein	RTVP1; Protein RTVP-1; GliPR 1; GLIPR	GLIPR1	Similarity to both the pathogenesis-related protein (PR) superfamily and the cysteine-rich secretory protein (CRISP) family	.	3Q2U; 3Q2R	MRVTLATIAWMVSFVSNYSHTANILPDIENEDFIKDCVRIHNKFRSEVKPTASDMLYMTWDPALAQIAKAWASNCQFSHNTRLKPPHKLHPNFTSLGENIWTGSVPIFSVSSAITNWYDEIQDYDFKTRICKKVCGHYTQVVWADSYKVGCAVQFCPKVSGFDALSNGAHFICNYGPGGNYPTWPYKRGATCSACPNNDKCLDNLCVNRQRDQVKRYYSVVYPGWPIYPRNRYTSLFLIVNSVILILSVIITILVQHKYPNLVLLD	Clinical trial	Adenoviral vector-mediated RTVP-1 gene-modified tumor cell-based vaccine suppresses the development of experimental prostate cancer. Cancer Gene Ther. 2006 Jul;13(7):658-63.	17	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1989781:PPARA activates gene expression	.	P48060
TT2UV5C	FKBP-associated protein (FAP48)	Q92990	GLMN_HUMAN	.	Glomulin; FK506-binding protein-associated protein; FAP48	GLMN	"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."	.	4F52	MAVEELQSIIKRCQILEEQDFKEEDFGLFQLAGQRCIEEGHTDQLLEIIQNEKNKVIIKNMGWNLVGPVVRCLLCKDKEDSKRKVYFLIFDLLVKLCNPKELLLGLLELIEEPSGKQISQSILLLLQPLQTVIQKLHNKAYSIGLALSTLWNQLSLLPVPYSKEQIQMDDYGLCQCCKALIEFTKPFVEEVIDNKENSLENEKLKDELLKFCFKSLKCPLLTAQFFEQSEEGGNDPFRYFASEIIGFLSAIGHPFPKMIFNHGRKKRTWNYLEFEEEENKQLADSMASLAYLVFVQGIHIDQLPMVLSPLYLLQFNMGHIEVFLQRTEESVISKGLELLENSLLRIEDNSLLYQYLEIKSFLTVPQGLVKVMTLCPIETLRKKSLAMLQLYINKLDSQGKYTLFRCLLNTSNHSGVEAFIIQNIKNQIDMSLKRTRNNKWFTGPQLISLLDLVLFLPEGAETDLLQNSDRIMASLNLLRYLVIKDNENDNQTGLWTELGNIENNFLKPLHIGLNMSKAHYEAEIKNSQEAQKSKDLCSITVSGEEIPNMPPEMQLKVLHSALFTFDLIESVLARVEELIEIKTKSTSEENIGIK	Literature-reported	The FKBP-associated protein FAP48 is an antiproliferative molecule and a player in T cell activation that increases IL2 synthesis. Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2444-9.	.	.	.	.	.	.	.	.	.	.	.	hsa05131: Shigellosis	R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	Q92990
TTV9A7R	Lactoylglutathione lyase (GLO1)	Q04760	LGUL_HUMAN	Carbon-sulfur lyases	S-D-lactoylglutathione methylglyoxal lyase; Methylglyoxalase; Ketone-aldehyde mutase; Glyoxalase I; GlxI; Glx I; GLO1; Aldoketomutase	GLO1	"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."	EC 4.4.1.5	3W0U; 3W0T; 3VW9; 1QIP; 1QIN	MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM	Clinical trial	Structure-activity relationship of human GLO I inhibitory natural flavonoids and their growth inhibitory effects. Bioorg Med Chem. 2008 Apr 1;16(7):3969-75.	17	.	.	.	.	.	.	.	.	.	.	hsa00620:Pyruvate metabolism	R-HSA-70268:Pyruvate metabolism	.	Q04760
TTVIMDE	Glucagon-like peptide 1 receptor (GLP1R)	P43220	GLP1R_HUMAN	GPCR secretin	GLP-1R; GLP-1-R; GLP-1 receptor	GLP1R	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).	.	6GB1; 6B3J; 5VEX; 5VEW; 5OTX	MAGAPGPLRLALLLLGMVGRAGPRPQGATVSLWETVQKWREYRRQCQRSLTEDPPPATDLFCNRTFDEYACWPDGEPGSFVNVSCPWYLPWASSVPQGHVYRFCTAEGLWLQKDNSSLPWRDLSECEESKRGERSSPEEQLLFLYIIYTVGYALSFSALVIASAILLGFRHLHCTRNYIHLNLFASFILRALSVFIKDAALKWMYSTAAQQHQWDGLLSYQDSLSCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVLSEQWIFRLYVSIGWGVPLLFVVPWGIVKYLYEDEGCWTRNSNMNYWLIIRLPILFAIGVNFLIFVRVICIVVSKLKANLMCKTDIKCRLAKSTLTLIPLLGTHEVIFAFVMDEHARGTLRFIKLFTELSFTSFQGLMVAILYCFVNNEVQLEFRKSWERWRLEHLHIQRDSSMKPLKCPTSSLSSGATAGSSMYTATCQASCS	Successful	Emerging drugs for obesity: linking novel biological mechanisms to pharmaceutical pipelines. Expert Opin Emerg Drugs. 2005 Aug;10(3):643-60.	34	PF00002	GPCR secretin	G-protein coupled receptor 2 family.	.	.	7 transmembrane receptor (Secretin family); Hormone receptor domain	PF00002; PF02793	PF00002; 7tm_2; PF02793; HRM	9.A.14.4.6	The G-protein-coupled receptor (GPCR) Family	hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04911:Insulin secretion	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	.	P43220
TT1YWO5	Glucagon-like peptide 2 receptor (GLP2R)	O95838	GLP2R_HUMAN	GPCR secretin	GLP2R; GLP2 receptor	GLP2R	This is a receptor for glucagon-like peptide 2. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.	.	.	MKLGSSRAGPGRGSAGLLPGVHELPMGIPAPWGTSPLSFHRKCSLWAPGRPFLTLVLLVSIKQVTGSLLEETTRKWAQYKQACLRDLLKEPSGIFCNGTFDQYVCWPHSSPGNVSVPCPSYLPWWSEESSGRAYRHCLAQGTWQTIENATDIWQDDSECSENHSFKQNVDRYALLSTLQLMYTVGYSFSLISLFLALTLLLFLRKLHCTRNYIHMNLFASFILRTLAVLVKDVVFYNSYSKRPDNENGWMSYLSEMSTSCRSVQVLLHYFVGANYLWLLVEGLYLHTLLEPTVLPERRLWPRYLLLGWAFPVLFVVPWGFARAHLENTGCWTTNGNKKIWWIIRGPMMLCVTVNFFIFLKILKLLISKLKAHQMCFRDYKYRLAKSTLVLIPLLGVHEILFSFITDDQVEGFAKLIRLFIQLTLSSFHGFLVALQYGFANGEVKAELRKYWVRFLLARHSGCRACVLGKDFRFLGKCPKKLSEGDGAEKLRKLQPSLNSGRLLHLAMRGLGELGAQPQQDHARWPRGSSLSECSEGDVTMANTMEEILEESEI	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. 2015	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-418555:G alpha (s) signalling events; R-HSA-420092:Glucagon-type ligand receptors	.	O95838
TTF45NW	Strychnine-binding glycine receptor (GLRA1)	P23415	GLRA1_HUMAN	Neurotransmitter receptor	Strychnine-insensitive glycine receptor; Strychnine binding subunit; Glycine receptor 48 kDa subunit; GLRA1	GLRA1	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).	.	4X5T; 2M6I; 2M6B; 1VRY; 1MOT	MYSFNTLRLYLWETIVFFSLAASKEAEAARSAPKPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVSCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYNEYPDDSLDLDPSMLDSIWKPDLFFANEKGAHFHEITTDNKLLRISRNGNVLYSIRITLTLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQEQGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHLERQMGYYLIQMYIPSLLIVILSWISFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRRHHKSPMLNLFQEDEAGEGRFNFSAYGMGPACLQAKDGISVKGANNSNTTNPPPAPSKSPEEMRKLFIQRAKKIDKISRIGFPMAFLIFNMFYWIIYKIVRREDVHNQ	Successful	3-demethoxy-3-glycosylaminothiocolchicines: Synthesis of a new class of putative muscle relaxant compounds. J Med Chem. 2006 Sep 7;49(18):5571-7.	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-975298:Ligand-gated ion channel transport	.	P23415
TTZ8EM9	Glycine receptor (GlyR)	P23415; P23416; O75311; Q5JXX5; P48167	GLRA1_HUMAN; GLRA2_HUMAN; GLRA3_HUMAN; GLRA4_HUMAN; GLRB_HUMAN	Neurotransmitter receptor	Glycine receptor	GLRA1	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).	.	.	MYSFNTLRLYLWETIVFFSLAASKEAEAARSAPKPMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVSCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYNEYPDDSLDLDPSMLDSIWKPDLFFANEKGAHFHEITTDNKLLRISRNGNVLYSIRITLTLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWQEQGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHLERQMGYYLIQMYIPSLLIVILSWISFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRRHHKSPMLNLFQEDEAGEGRFNFSAYGMGPACLQAKDGISVKGANNSNTTNPPPAPSKSPEEMRKLFIQRAKKIDKISRIGFPMAFLIFNMFYWIIYKIVRREDVHNQ	Successful	3-demethoxy-3-glycosylaminothiocolchicines: Synthesis of a new class of putative muscle relaxant compounds. J Med Chem. 2006 Sep 7;49(18):5571-7.	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-975298:Ligand-gated ion channel transport	.	P23415
TTRJCNG	Glutaredoxin-1 (GLRX)	P35754	GLRX1_HUMAN	.	Thioltransferase-1; TTase-1; GRX	GLRX	Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.	.	4RQR; 1JHB; 1B4Q	MAQEFVNCKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGELLTRLKQIGALQ	Literature-reported	Glutaredoxin-1 Deficiency Causes Fatty Liver and Dyslipidemia by Inhibiting Sirtuin-1. Antioxid Redox Signal. 2017 Aug 20;27(6):313-327.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-499943: Interconversion of nucleotide di- and triphosphates	MetaCyc:HS04268-MON	P35754
TTESHRV	Glutaredoxin-2 (GLRX2)	Q9NS18	GLRX2_HUMAN	.	"Glutaredoxin-2, mitochondrial; GRX2; CGI-133"	GLRX2	"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."	.	2HT9; 2FLS; 2CQ9	MIWRRAALAGTRLVWSRSGSAGWLDRAAGAAGAAAAAASGMESNTSSSLENLATAPVNQIQETISDNCVVIFSKTSCSYCTMAKKLFHDMNVNYKVVELDLLEYGNQFQDALYKMTGERTVPRIFVNGTFIGGATDTHRLHKEGKLLPLVHQCYLKKSKRKEFQ	Literature-reported	Characterization of the impact of glutaredoxin-2 (GRX2) deficiency on superoxide/hydrogen peroxide release from cardiac and liver mitochondria. Redox Biol. 2018 May;15:216-227.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9NS18
TTCW0KX	Glutaminase (GLS)	O94925; Q9UI32	GLSK_HUMAN; GLSL_HUMAN	Carbon-nitrogen hydrolase	"L-glutamine amidohydrolase; Glutaminase, mitochondrial; GLS"	GLS	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.	.	.	MMRLRGSGMLRDLLLRSPAGVSATLRRAQPLVTLCRRPRGGGRPAAGPAAAARLHPWWGGGGWPAEPLARGLSSSPSEILQELGKGSTHPQPGVSPPAAPAAPGPKDGPGETDAFGNSEGKELVASGENKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQTVHKNLDGLL	Clinical trial	Antitumor activity of the glutaminase inhibitor CB-839 in triple-negative breast cancer. Mol Cancer Ther. 2014 Apr;13(4):890-901.	21	.	.	.	.	.	.	.	.	.	.	"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"	R-HSA-210500: Glutamate Neurotransmitter Release Cycle; R-HSA-5628897: TP53 Regulates Metabolic Genes; R-HSA-8964539: Glutamate and glutamine metabolism	.	O94925
TTURQ2G	Glutamate decarboxylase (GLUL)	P15104	GLNA_HUMAN	Carbon-nitrogen ligase	Glutamateammonia ligase	GLUL	"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."	EC 6.3.1.2	2QC8; 2OJW	MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEWNFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCLLNETGDEPFQYKN	Discontinued	"NLX-P101, an adeno-associated virus gene therapy encoding glutamic acid decarboxylase, for the potential treatment of Parkinson's disease. Curr Opin Investig Drugs. 2010 Jul;11(7):813-22."	5	EC:6.3	Carbon-nitrogen ligase	glutamine synthetase family.	6.3.1.2 	Forming carbon-nitrogen bonds	"Glutamine synthetase, catalytic domain; Glutamine synthetase, beta-Grasp domain"	PF00120; PF03951	PF00120; Gln-synt_C; PF03951; Gln-synt_N	.	.	"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"	R-HSA-70614:Amino acid synthesis and interconversion (transamination)	MetaCyc:HS06066-MON	P15104
TT2BJ1X	Astrocyte glutamine synthetase (GLUL)	P15104	GLNA_HUMAN	.	Palmitoyltransferase GLUL; Glutamine synthetase; Glutamate--ammonia ligase; GS; GLNS	GLUL	"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."	EC 6.3.1.2	2QC8; 2OJW	MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEWNFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCLLNETGDEPFQYKN	Literature-reported	Regulation of astrocyte glutamine synthetase in epilepsy. Neurochem Int. 2013 Dec;63(7):670-81.	.	.	.	.	.	.	.	.	.	.	.	"hsa00220: Arginine biosynthesis; hsa00250: Alanine, aspartate and glutamate metabolism; hsa00630: Glyoxylate and dicarboxylate metabolism; hsa00910: Nitrogen metabolism; hsa01100: Metabolic pathways; hsa01230: Biosynthesis of amino acids; hsa04217: Necroptosis; hsa04724: Glutamatergic synapse; hsa04727: GABAergic synapse"	R-HSA-210455: Astrocytic Glutamate-Glutamine Uptake And Metabolism; R-HSA-8964539: Glutamate and glutamine metabolism	MetaCyc:HS06066-MON	P15104
TTGOFW6	Ganglioside GM2 activator (GM2A)	P17900	SAP3_HUMAN	.	Sphingolipid activator protein 3; SAP3; Ganglioside GM2 activator isoform short; GM2AP; GM2A; Cerebroside sulfate activator protein	GM2A	"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."	.	2AG9; 2AG4; 2AG2; 2AF9; 1TJJ	MQSLMQAPLLIALGLLLAAPAQAHLKKPSQLSSFSWDNCDEGKDPAVIRSLTLEPDPIIVPGNVTLSVMGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHFCDVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSSGKRLGCIKIAASLKGI	Clinical trial	Genetically engineered humanized anti-ganglioside GM2 antibody against multiple organ metastasis produced by GM2-expressing small-cell lung cancer cells. Cancer Sci. 2011 Dec;102(12):2157-63.	19	.	.	.	.	.	.	.	.	.	.	hsa04142: Lysosome	R-HSA-1660662: Glycosphingolipid metabolism; R-HSA-6798695: Neutrophil degranulation	.	P17900
TT390KA	Geminin (GMNN)	O75496	GEMI_HUMAN	.	geminin DNA replication inhibitor; MGORS6	GMNN	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).	.	4BRY; 2WVR; 2LP0; 1UII; 1T6F	MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI	Literature-reported	Peptide binding to Geminin and inhibitory for DNA replication. Biochem Biophys Res Commun. 2004 Apr 23;317(1):218-22.	.	.	Geminin family	geminin family.	.	.	Geminin	PF07412	PF07412; Geminin	.	.	.	R-HSA-68867: Assembly of the pre-replicative complex; R-HSA-68962: Activation of the pre-replicative complex; R-HSA-69052: Switching of origins to a post-replicative state	.	O75496
TTCFP0V	Glutamine amidotransferase (GMPS)	P49915	GUAA_HUMAN	Carbon-nitrogen ligase	GMP synthetase; GMP synthase [glutamine-hydrolyzing]	GMPS	"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."	EC 6.3.5.2	2VXO; 2VPI	MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAAHSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPEEVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVRILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPHTLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDWESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILRESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVEVVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE	Literature-reported	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	0	EC:6.3	Carbon-nitrogen ligase	.	6.3.5.2	Forming carbon-nitrogen bonds	Glutamine amidotransferase class-I; GMP synthase C terminal domain; NAD synthase	PF00117; PF00958; PF02540	PF00117; GATase; PF00958; GMP_synt_C; PF02540; NAD_synthase	.	.	hsa00230:Purine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways	R-HSA-73817:Purine ribonucleoside monophosphate biosynthesis	.	P49915
TTSRXJW	G-alpha-11 messenger RNA (GNA11 mRNA)	P29992	GNA11_HUMAN	mRNA target	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)	GNA11	Acts as an activator of phospholipase C. Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.	.	6OIJ	MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGAGYSEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEKVTTFEHQYVSAIKTLWEDPGIQECYDRRREYQLSDSAKYYLTDVDRIATLGYLPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEDKILYSHLVDYFPEFDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV	Literature-reported	"US patent application no. 5,951,455, Antisense modulation of G-alpha-11 expression."	0	mRNA	mRNA target	.	.	.	G-protein alpha subunit	PF00503	PF00503; G-alpha	.	.	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	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)	.	P29992
TTL1HWR	Guanine-binding G(i) alpha-1	.	GNAI1_HUMAN	Single Protein	Guanine nucleotide-binding protein G(i) subunit alpha-1; Adenylate cyclase-inhibiting G alpha protein	GNAI1	"Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal."	.	.	MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P63096
TT8QF3W	Guanine-binding G(i) alpha-3	.	GNAI3_HUMAN	Single Protein	Guanine nucleotide-binding protein G(i) subunit alpha-3; G(i) alpha-3	GNAI3	"Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal."	.	.	MGCTLSAEDKAAVERSKMIDRNLREDGEKAAKEVKLLLLGAGESGKSTIVKQMKIIHEDGYSEDECKQYKVVVYSNTIQSIIAIIRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMTPELAGVIKRLWRDGGVQACFSRSREYQLNDSASYYLNDLDRISQSNYIPTQQDVLRTRVKTTGIVETHFTFKDLYFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTETSIILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAAAYIQCQFEDLNRRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKECGLY	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P08754
TTAXD8Z	Guanine-binding G(o) alpha	.	GNAO_HUMAN	Single Protein	Guanine nucleotide-binding protein G(o) subunit alpha; G protein subunit alpha o1; GNAO1	GNAO1	Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear. Stimulated by RGS14.	.	.	MGCTLSAEERAALERSKAIEKNLKEDGISAAKDVKLLLLGAGESGKSTIVKQMKIIHEDGFSGEDVKQYKPVVYSNTIQSLAAIVRAMDTLGIEYGDKERKADAKMVCDVVSRMEDTEPFSAELLSAMMRLWGDSGIQECFNRSREYQLNDSAKYYLDSLDRIGAADYQPTEQDILRTRVKTTGIVETHFTFKNLHFRLFDVGGQRSERKKWIHCFEDVTAIIFCVALSGYDQVLHEDETTNRMHESLMLFDSICNNKFFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYTGPNTYEDAAAYIQAQFESKNRSPNKEIYCHMTCATDTNNIQVVFDAVTDIIIANNLRGCGLY	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P09471
TTL1SRG	Guanine nucleotide-binding alpha-q (GNAQ)	P50148	GNAQ_HUMAN	.	GNAQ; G alphaq; G alpha(q)	GNAQ	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).	.	.	MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV	Literature-reported	Defective platelet activation in G alpha(q)-deficient mice. Nature. 1997 Sep 11;389(6647):183-6.	.	.	.	.	.	.	.	.	.	.	.	"hsa04015: Rap1 signaling pathway; hsa04020: Calcium signaling pathway; hsa04022: cGMP-PKG signaling pathway; hsa04062: Chemokine signaling pathway; hsa04071: Sphingolipid signaling pathway; hsa04261: Adrenergic signaling in cardiomyocytes; hsa04270: Vascular smooth muscle contraction; hsa04371: Apelin 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; hsa04728: Dopaminergic synapse; hsa04730: Long-term depression; hsa04750: Inflammatory mediator regulation of TRP channels; hsa04911: Insulin secretion; hsa04912: GnRH signaling pathway; hsa04915: Estrogen signaling pathway; hsa04916: Melanogenesis; hsa04918: Thyroid hormone synthesis; hsa04921: Oxytocin signaling pathway; hsa04922: Glucagon signaling pathway; hsa04924: Renin secretion; hsa04925: Aldosterone synthesis and secretion; hsa04927: Cortisol synthesis and secretion; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04929: GnRH secretion; hsa04934: Cushing syndrome; hsa04935: Growth hormone synthesis, secretion and action; hsa04961: Endocrine and other factor-regulated calcium reabsorption; hsa04970: Salivary secretion; hsa04971: Gastric acid secretion; hsa04972: Pancreatic secretion; hsa05010: Alzheimer disease; hsa05016: Huntington disease; hsa05017: Spinocerebellar ataxia; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05135: Yersinia infection; hsa05142: Chagas disease; hsa05143: African trypanosomiasis; hsa05146: Amoebiasis; hsa05163: Human cytomegalovirus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05200: Pathways in cancer"	R-HSA-112043: PLC beta mediated events; R-HSA-202040: G-protein activation; 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); R-HSA-6814122: Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding	.	P50148
TT4DP5S	N-acetylmannosamine kinase (GNE)	Q9Y223	GLCNE_HUMAN	Kinase	UDPGlcNAc2epimerase/ManAc kinase; GNE; Bifunctional UDPNacetylglucosamine 2epimerase/Nacetylmannosamine kinase	GNE	"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}."	.	4ZHT; 3EO3; 2YI1; 2YHY; 2YHW	MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDVKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASMVLDYTTRRIY	Clinical trial	Hereditary inclusion body myopathy: single patient response to intravenous dosing of GNE gene lipoplex. Hum Gene Ther. 2011 Nov;22(11):1331-41.	17	.	.	.	.	.	.	.	.	.	.	hsa00520:Amino sugar and nucleotide sugar metabolism; hsa01100:Metabolic pathways	R-HSA-4085001:Sialic acid metabolism	.	Q9Y223
TTCMBKF	GN-binding protein G(I)/G(S)/G(O) gamma-7 (GNG7)	O60262	GBG7_HUMAN	.	Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7; GNGT7; G protein gamma 7	GNG7	"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."	.	.	MSATNNIAQARKLVEQLRIEAGIERIKVSKAASDLMSYCEQHARNDPLLVGVPASENPFKDKKPCIIL	Literature-reported	G-protein gamma 7 is down-regulated in cancers and associated with p 27kip1-induced growth arrest. Cancer Res. 1999 Mar 1;59(5):1096-101.	.	.	.	G protein gamma family.	.	.	GGL domain	PF00631	PF00631; G-gamma	.	.	hsa04014: Ras signaling pathway; hsa04062: Chemokine signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04371: Apelin signaling pathway; hsa04713: Circadian entrainment; hsa04723: Retrograde endocannabinoid signaling; hsa04724: Glutamatergic synapse; hsa04725: Cholinergic synapse; hsa04726: Serotonergic synapse; hsa04727: GABAergic synapse; hsa04728: Dopaminergic synapse; hsa04740: Olfactory transduction; hsa04926: Relaxin signaling pathway; hsa05032: Morphine addiction; hsa05034: Alcoholism; hsa05163: Human cytomegalovirus infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05200: Pathways in cancer	"R-HSA-1296041: Activation of G protein gated Potassium channels; R-HSA-163359: Glucagon signaling in metabolic regulation; R-HSA-202040: G-protein activation; R-HSA-381676: Glucagon-like Peptide-1 (GLP1) regulates insulin secretion; R-HSA-392170: ADP signalling through P2Y purinoceptor 12; R-HSA-392451: G beta:gamma signalling through PI3Kgamma; R-HSA-392851: Prostacyclin signalling through prostacyclin receptor; R-HSA-400042: Adrenaline,noradrenaline inhibits insulin secretion; R-HSA-4086398: Ca2+ pathway; R-HSA-416476: G alpha (q) signalling events; R-HSA-416482: G alpha (12/13) signalling events; R-HSA-418217: G beta:gamma signalling through PLC beta; R-HSA-418555: G alpha (s) signalling events; R-HSA-418592: ADP signalling through P2Y purinoceptor 1; R-HSA-418594: G alpha (i) signalling events; R-HSA-418597: G alpha (z) signalling events; R-HSA-420092: Glucagon-type ligand receptors; R-HSA-428930: Thromboxane signalling through TP receptor; R-HSA-432040: Vasopressin regulates renal water homeostasis via Aquaporins; R-HSA-456926: Thrombin signalling through proteinase activated receptors (PARs); R-HSA-500657: Presynaptic function of Kainate receptors; R-HSA-6814122: Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding; R-HSA-8964315: G beta:gamma signalling through BTK; R-HSA-8964616: G beta:gamma signalling through CDC42; R-HSA-9009391: Extra-nuclear estrogen signaling; R-HSA-9634597: GPER1 signaling; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production; R-HSA-997272: Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits"	.	O60262
TT0ID4A	Leutinizing-hormone-releasing hormone (GNRH1)	P01148	GON1_HUMAN	Gonadotropin-releasing hormone	Progonadoliberin-1; Progonadoliberin I; LHRH; GRH; GNRH	GNRH1	Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones.	.	4D5M	MKPIQKLLAGLILLTWCVEGCSSQHWSYGLRPGGKRDAENLIDSFQEIVKEVGQLAETQRFECTTHQPRSPLRDLKGALESLIEEETGQKKI	Successful	"Increased risk of metabolic syndrome, diabetes mellitus, and cardiovascular disease in men receiving androgen deprivation therapy for prostate cancer. Pharmacotherapy. 2008 Dec;28(12):1511-22."	34	.	.	.	.	.	.	.	.	.	.	hsa04912:GnRH signaling pathway	R-HSA-375281:Hormone ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events	.	P01148
TT8R70G	Gonadotropin-releasing hormone receptor (GNRHR)	P30968	GNRHR_HUMAN	GPCR rhodopsin	Hypothalamic gonadotropin-releasing hormone receptor; Gonadotrophin releasing hormone receptor; GnRH-R; GnRH receptor; GRHR	GNRHR	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.	.	.	MANSASPEQNQNHCSAINNSIPLMQGNLPTLTLSGKIRVTVTFFLFLLSATFNASFLLKLQKWTQKKEKGKKLSRMKLLLKHLTLANLLETLIVMPLDGMWNITVQWYAGELLCKVLSYLKLFSMYAPAFMMVVISLDRSLAITRPLALKSNSKVGQSMVGLAWILSSVFAGPQLYIFRMIHLADSSGQTKVFSQCVTHCSFSQWWHQAFYNFFTFSCLFIIPLFIMLICNAKIIFTLTRVLHQDPHELQLNQSKNNIPRARLKTLKMTVAFATSFTVCWTPYYVLGIWYWFDPEMLNRLSDPVNHFFFLFAFLNPCFDPLIYGYFSL	Successful	Gonadotropin releasing hormone analogs induce apoptosis by extrinsic pathway involving p53 phosphorylation in primary cell cultures of human prostatic adenocarcinomas. Prostate. 2009 Jul 1;69(10):1025-33.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.10.1	The G-protein-coupled receptor (GPCR) Family	hsa04080:Neuroactive ligand-receptor interaction; hsa04912:GnRH signaling pathway	R-HSA-375281:Hormone ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events	.	P30968
TTU507L	Cytoplasmic aspartate aminotransferase (GOT1)	P17174	AATC_HUMAN	Transaminase	Glutamate oxaloacetate transaminase-1; GOT1	GOT1	"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."	EC 2.6.1.1	6DND; 6DNB; 6DNA; 3WZF; 3II0	MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQKIANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFLARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLENAPEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWAIRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPPAQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGMFSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ	Literature-reported	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	0	.	.	.	.	.	.	.	.	.	.	"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"	R-HSA-70263:Gluconeogenesis; R-HSA-70614:Amino acid synthesis and interconversion (transamination)	MetaCyc:HS04361-MON	P17174
TTVB0Q9	Platelet glycoprotein Ib alpha (CD42b)	P07359	GP1BA_HUMAN	.	Platelet glycoprotein Ib alpha chain; Glycoprotein Ibalpha; Glycocalicin; GPIbalpha; GPIbA; GPIb-alpha; GPIb alpha; GP-Ib alpha; Antigen CD42balpha; Antigen CD42b-alpha	GP1BA	"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."	.	4YR6; 4MGX; 4CH8; 4CH2; 4C2B	MPLLLLLLLLPSPLHPHPICEVSKVASHLEVNCDKRNLTALPPDLPKDTTILHLSENLLYTFSLATLMPYTRLTQLNLDRCELTKLQVDGTLPVLGTLDLSHNQLQSLPLLGQTLPALTVLDVSFNRLTSLPLGALRGLGELQELYLKGNELKTLPPGLLTPTPKLEKLSLANNNLTELPAGLLNGLENLDTLLLQENSLYTIPKGFFGSHLLPFAFLHGNPWLCNCEILYFRRWLQDNAENVYVWKQGVDVKAMTSNVASVQCDNSDKFPVYKYPGKGCPTLGDEGDTDLYDYYPEEDTEGDKVRATRTVVKFPTKAHTTPWGLFYSWSTASLDSQMPSSLHPTQESTKEQTTFPPRWTPNFTLHMESITFSKTPKSTTEPTPSPTTSEPVPEPAPNMTTLEPTPSPTTPEPTSEPAPSPTTPEPTSEPAPSPTTPEPTSEPAPSPTTPEPTPIPTIATSPTILVSATSLITPKSTFLTTTKPVSLLESTKKTIPELDQPPKLRGVLQGHLESSRNDPFLHPDFCCLLPLGFYVLGLFWLLFASVVLILLLSWVGHVKPQALDSGQGAALTTATQTTHLELQRGRQVTVPRAWLLFLRGSLPTFRSSLFLWVRPNGRVGPLVAGRRPSALSQGRGQDLLSTVSIRYSGHSL	Clinical trial	"Anfibatide, a novel GPIb complex antagonist, inhibits platelet adhesion and thrombus formation in vitro and in vivo in murine models of thrombosis. Thromb Haemost. 2014 Feb;111(2):279-89."	19	.	Leucine rich repeat	.	.	.	Leucine rich repeat; Leucine rich repeat N-terminal domain	PF13855; PF01462	PF13855; LRR_8; PF01462; LRRNT	.	.	hsa04512:ECM-receptor interaction; hsa04611:Platelet activation; hsa04640:Hematopoietic cell lineage	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	.	P07359
TTTJUVZ	Platelet glycoprotein VI (GP6)	Q9HCN6	GPVI_HUMAN	.	Glycoprotein 6; GPVI	GP6	"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."	.	5OU9; 5OU8; 5OU7; 2GI7	MSPSPTALFCLGLCLGRVPAQSGPLPKPSLQALPSSLVPLEKPVTLRCQGPPGVDLYRLEKLSSSRYQDQAVLFIPAMKRSLAGRYRCSYQNGSLWSLPSDQLELVATGVFAKPSLSAQPGPAVSSGGDVTLQCQTRYGFDQFALYKEGDPAPYKNPERWYRASFPIITVTAAHSGTYRCYSFSSRDPYLWSAPSDPLELVVTGTSVTPSRLPTEPPSPVAEFSEATAELTVSFTNEVFTTETSRSITASPKESDSPAGPARQYYTKGNLVRICLGAVILIILAGFLAEDWHSRRKRLRHRGRAVQRPLPPLPPLPLTRKSNGGQDGGRQDVHSRGLCS	Clinical trial	Novel antiplatelet drug revacept (Dimeric Glycoprotein VI-Fc) specifically and efficiently inhibited collagen-induced platelet aggregation without affecting general hemostasis in humans. Circulation.2011 May 3;123(17):1891-9.	21	.	.	.	.	.	Immunoglobulin domain	PF13895	PF13895; Ig_2	.	.	hsa04512:ECM-receptor interaction; hsa04611:Platelet activation	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	.	Q9HCN6
TT96HUR	Cell surface A33 antigen (GPA33)	Q99795	GPA33_HUMAN	Immunoglobulin	GPA33; A33 cognate antigen; A33 antigen	GPA33	May play a role in cell-cell recognition and signaling.	.	.	MVGKMWPVLWTLCAVRVTVDAISVETPQDVLRASQGKSVTLPCTYHTSTSSREGLIQWDKLLLTHTERVVIWPFSNKNYIHGELYKNRVSISNNAEQSDASITIDQLTMADNGTYECSVSLMSDLEGNTKSRVRLLVLVPPSKPECGIEGETIIGNNIQLTCQSKEGSPTPQYSWKRYNILNQEQPLAQPASGQPVSLKNISTDTSGYYICTSSNEEGTQFCNITVAVRSPSMNVALYVGIAVGVVAALIIIGIIIYCCCCRGKDDNTEDKEDARPNREAYEEPPEQLRELSREREEEDDYRQEEQRSTGRESPDHLDQ	Clinical trial	"Phase 1/2 study of KRN330, a fully human anti-A33 monoclonal antibody, plus irinotecan as second-line treatment for patients with metastatic colorectal cancer. Invest New Drugs. 2014 Aug;32(4):682-90."	19	.	.	.	.	.	.	.	.	.	.	.	.	.	Q99795
TTSDVTR	G-protein coupled bile acid receptor 1 (GPBAR1)	Q8TDU6	GPBAR_HUMAN	GPCR rhodopsin	hGPCR19; hBG37; TGR5; Membrane-type receptor for bile acids; M-BAR; G-protein coupled receptor GPCR19; BG37	GPBAR1	"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."	.	.	MTPNSTGEVPSPIPKGALGLSLALASLIITANLLLALGIAWDRRLRSPPAGCFFLSLLLAGLLTGLALPTLPGLWNQSRRGYWSCLLVYLAPNFSFLSLLANLLLVHGERYMAVLRPLQPPGSIRLALLLTWAGPLLFASLPALGWNHWTPGANCSSQAIFPAPYLYLEVYGLLLPAVGAAAFLSVRVLATAHRQLQDICRLERAVCRDEPSALARALTWRQARAQAGAMLLFGLCWGPYVATLLLSVLAYEQRPPLGPGTLLSLLSLGSASAAAVPVAMGLGDQRYTAPWRAAAQRCLQGLWGRASRDSPGPSIAYHPSSQSSVDLDLN	Clinical trial	"Bile acids and sphingosine-1-phosphate receptor 2 in hepatic lipid metabolism.Acta Pharmaceutica Sinica B Volume 5, Issue 2, March 2015, Pages 151-157."	19	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.21.1	The G-protein-coupled receptor (GPCR) Family	.	R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418555:G alpha (s) signalling events	.	Q8TDU6
TTJTSX4	Glypican-3 (GPC3)	P51654	GPC3_HUMAN	.	Secreted glypican3; OCI5; MXR7; Intestinal protein OCI5; Intestinal protein OCI-5; GTR22; GTR2-2	GPC3	"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."	.	.	MAGTVRTACLVVAMLLSLDFPGQAQPPPPPPDATCHQVRSFFQRLQPGLKWVPETPVPGSDLQVCLPKGPTCCSRKMEEKYQLTARLNMEQLLQSASMELKFLIIQNAAVFQEAFEIVVRHAKNYTNAMFKNNYPSLTPQAFEFVGEFFTDVSLYILGSDINVDDMVNELFDSLFPVIYTQLMNPGLPDSALDINECLRGARRDLKVFGNFPKLIMTQVSKSLQVTRIFLQALNLGIEVINTTDHLKFSKDCGRMLTRMWYCSYCQGLMMVKPCGGYCNVVMQGCMAGVVEIDKYWREYILSLEELVNGMYRIYDMENVLLGLFSTIHDSIQYVQKNAGKLTTTIGKLCAHSQQRQYRSAYYPEDLFIDKKVLKVAHVEHEETLSSRRRELIQKLKSFISFYSALPGYICSHSPVAENDTLCWNGQELVERYSQKAARNGMKNQFNLHELKMKGPEPVVSQIIDKLKHINQLLRTMSMPKGRVLDKNLDEEGFESGDCGDDEDECIGGSGDGMIKVKNQLRFLAELAYDLDVDDAPGNSQQATPKDNEISTFHNLGNVHSPLKLLTSMAISVVCFFFLVH	Clinical trial	"Usefulness of a novel oncofetal antigen, glypican-3, for diagnosis and immunotherapy of hepatocellular carcinoma. Nihon Rinsho Meneki Gakkai Kaishi. 2008 Oct;31(5):383-91."	21	.	.	glypican family.	.	.	Glypican	PF01153	PF01153; Glypican	.	.	hsa05205:Proteoglycans in cancer	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	.	P51654
TTKTEAH	Glycerol-3-phosphate dehydrogenase (GPD1)	P21695	GPDA_HUMAN	Short-chain dehydrogenases reductase	"Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic; GPDH-C; GPD-C"	GPD1	"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."	EC 1.1.1.8	6E8Z; 6E8Y; 6.00E+90; 1X0X; 1X0V	MASKKVCIVGSGNWGSAIAKIVGGNAAQLAQFDPRVTMWVFEEDIGGKKLTEIINTQHENVKYLPGHKLPPNVVAVPDVVQAAEDADILIFVVPHQFIGKICDQLKGHLKANATGISLIKGVDEGPNGLKLISEVIGERLGIPMSVLMGANIASEVADEKFCETTIGCKDPAQGQLLKELMQTPNFRITVVQEVDTVEICGALKNVVAVGAGFCDGLGFGDNTKAAVIRLGLMEMIAFAKLFCSGPVSSATFLESCGVADLITTCYGGRNRKVAEAFARTGKSIEQLEKELLNGQKLQGPETARELYSILQHKGLVDKFPLFMAVYKVCYEGQPVGEFIHCLQNHPEHM	Literature-reported	A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishma... Structure. 2000 May 15;8(5):541-52.	.	.	.	.	.	.	.	.	.	.	.	hsa00564: Glycerophospholipid metabolism	R-HSA-1483166: Synthesis of PA	MetaCyc:HS09586-MON	P21695
TTDSB34	G-protein coupled estrogen receptor 1 (GPER1)	Q99527	GPER1_HUMAN	GPCR rhodopsin	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	GPER1	Receptor for estrogen. .	.	.	MDVTSQARGVGLEMYPGTAQPAAPNTTSPELNLSHPLLGTALANGTGELSEHQQYVIGLFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAVADLILVADSLIEVFNLHERYYDIAVLCTFMSLFLQVNMYSSVFFLTWMSFDRYIALARAMRCSLFRTKHHARLSCGLIWMASVSATLVPFTAVHLQHTDEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRVLVRAHRHRGLRPRRQKALRMILAVVLVFFVCWLPENVFISVHLLQRTQPGAAPCKQSFRHAHPLTGHIVNLAAFSNSCLNPLIYSFLGETFRDKLRLYIEQKTNLPALNRFCHAALKAVIPDSTEQSDVRFSSAV	Successful	2018 FDA drug approvals.Nat Rev Drug Discov. 2019 Feb;18(2):85-89. 	34	.	.	.	.	.	.	.	.	.	.	hsa01522: Endocrine resistance; hsa04915: Estrogen signaling pathway; hsa04929: GnRH secretion	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418594:G alpha (i) signalling events	.	Q99527
TT19JIZ	Glucose-6-phosphate isomerase (GPI)	P06744	G6PI_HUMAN	Intramolecular oxidoreductases	Sperm antigen 36; SA-36; Phosphohexose isomerase; Phosphoglucose isomerase; PHI; PGI; Neuroleukin; NLK; GPI; Autocrine motility factor; AMF	GPI	"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."	EC 5.3.1.9	1NUH; 1JLH; 1JIQ; 1IRI; 1IAT	MAALTRDPQFQKLQQWYREHRSELNLRRLFDANKDRFNHFSLTLNTNHGHILVDYSKNLVTEDVMRMLVDLAKSRGVEAARERMFNGEKINYTEGRAVLHVALRNRSNTPILVDGKDVMPEVNKVLDKMKSFCQRVRSGDWKGYTGKTITDVINIGIGGSDLGPLMVTEALKPYSSGGPRVWYVSNIDGTHIAKTLAQLNPESSLFIIASKTFTTQETITNAETAKEWFLQAAKDPSAVAKHFVALSTNTTKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDNFEQLLSGAHWMDQHFRTTPLEKNAPVLLALLGIWYINCFGCETHAMLPYDQYLHRFAAYFQQGDMESNGKYITKSGTRVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKMIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMRGKSTEEARKELQAAGKSPEDLERLLPHKVFEGNRPTNSIVFTKLTPFMLGALVAMYEHKIFVQGIIWDINSFDQWGVELGKQLAKKIEPELDGSAQVTSHDASTNGLINFIKQQREARVQ	Literature-reported	Molecular association of glucose-6-phosphate isomerase and pyruvate kinase M2 with glyceraldehyde-3-phosphate dehydrogenase in cancer cells. BMC Cancer. 2016 Feb 24;16:152.	.	.	.	.	.	.	.	.	.	.	.	hsa00010: Glycolysis / Gluconeogenesis; hsa00030: Pentose phosphate pathway; hsa00500: Starch and sucrose metabolism; hsa00520: Amino sugar and nucleotide sugar metabolism; hsa01100: Metabolic pathways; hsa01200: Carbon metabolism; hsa01250: Biosynthesis of nucleotide sugars	R-HSA-5628897: TP53 Regulates Metabolic Genes; R-HSA-6798695: Neutrophil degranulation; R-HSA-70171: Glycolysis; R-HSA-70263: Gluconeogenesis	MetaCyc:HS02693-MON	P06744
TT7315J	Transmembrane glycoprotein NMB (GPNMB)	Q14956	GPNMB_HUMAN	.	NMB; Hematopoietic growth factor inducible neurokinin-1 type; HGFIN	GPNMB	Could be a melanogenic enzyme.	.	.	MECLYYFLGFLLLAARLPLDAAKRFHDVLGNERPSAYMREHNQLNGWSSDENDWNEKLYPVWKRGDMRWKNSWKGGRVQAVLTSDSPALVGSNITFAVNLIFPRCQKEDANGNIVYEKNCRNEAGLSADPYVYNWTAWSEDSDGENGTGQSHHNVFPDGKPFPHHPGWRRWNFIYVFHTLGQYFQKLGRCSVRVSVNTANVTLGPQLMEVTVYRRHGRAYVPIAQVKDVYVVTDQIPVFVTMFQKNDRNSSDETFLKDLPIMFDVLIHDPSHFLNYSTINYKWSFGDNTGLFVSTNHTVNHTYVLNGTFSLNLTVKAAAPGPCPPPPPPPRPSKPTPSLATTLKSYDSNTPGPAGDNPLELSRIPDENCQINRYGHFQATITIVEGILEVNIIQMTDVLMPVPWPESSLIDFVVTCQGSIPTEVCTIISDPTCEITQNTVCSPVDVDEMCLLTVRRTFNGSGTYCVNLTLGDDTSLALTSTLISVPDRDPASPLRMANSALISVGCLAIFVTVISLLVYKKHKEYNPIENSPGNVVRSKGLSVFLNRAKAVFFPGNQEKDPLLKNQEFKGVS	Literature-reported	2011 FDA drug approvals. Nat Rev Drug Discov. 2012 Feb 1;11(2):91-4.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-8857538: PTK6 promotes HIF1A stabilization	.	Q14956
TTUKZVG	G protein coupled receptor 101 (GPR101)	Q96P66	GP101_HUMAN	GPCR rhodopsin	Probable Gprotein coupled receptor 101; GPR101	GPR101	Orphan receptor.	.	.	MTSTCTNSTRESNSSHTCMPLSKMPISLAHGIIRSTVLVIFLAASFVGNIVLALVLQRKPQLLQVTNRFIFNLLVTDLLQISLVAPWVVATSVPLFWPLNSHFCTALVSLTHLFAFASVNTIVVVSVDRYLSIIHPLSYPSKMTQRRGYLLLYGTWIVAILQSTPPLYGWGQAAFDERNALCSMIWGASPSYTILSVVSFIVIPLIVMIACYSVVFCAARRQHALLYNVKRHSLEVRVKDCVENEDEEGAEKKEEFQDESEFRRQHEGEVKAKEGRMEAKDGSLKAKEGSTGTSESSVEARGSEEVRESSTVASDGSMEGKEGSTKVEENSMKADKGRTEVNQCSIDLGEDDMEFGEDDINFSEDDVEAVNIPESLPPSRRNSNSNPPLPRCYQCKAAKVIFIIIFSYVLSLGPYCFLAVLAVWVDVETQVPQWVITIIIWLFFLQCCIHPYVYGYMHKTIKKEIQDMLKKFFCKEKPPKEDSHPDLPGTEGGTEGKIVPSYDSATFP	Literature-reported	Screening for GPR101 defects in pediatric pituitary corticotropinomas. Endocr Relat Cancer. 2016 Jun 1;23(5):357-365.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q96P66
TT7QNVC	Glucose-dependent insulinotropic receptor (GPR119)	Q8TDV5	GP119_HUMAN	GPCR rhodopsin	GPR119; G-protein coupled receptor 119	GPR119	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.	.	.	MESSFSFGVILAVLASLIIATNTLVAVAVLLLIHKNDGVSLCFTLNLAVADTLIGVAISGLLTDQLSSPSRPTQKTLCSLRMAFVTSSAAASVLTVMLITFDRYLAIKQPFRYLKIMSGFVAGACIAGLWLVSYLIGFLPLGIPMFQQTAYKGQCSFFAVFHPHFVLTLSCVGFFPAMLLFVFFYCDMLKIASMHSQQIRKMEHAGAMAGGYRSPRTPSDFKALRTVSVLIGSFALSWTPFLITGIVQVACQECHLYLVLERYLWLLGVGNSLLNPLIYAYWQKEVRLQLYHMALGVKKVLTSFLLFLSARNCGPERPRESSCHIVTISSSEFDG	Successful	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 126).	34	.	.	.	.	.	.	.	.	.	.	hsa04024:cAMP signaling pathway; hsa04911:Insulin secretion	"R-HSA-381771: Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1); R-HSA-400511: Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP)"	.	Q8TDV5
TT3IPW2	G-protein coupled receptor 12 (GPR12)	P47775	GPR12_HUMAN	.	G-protein coupled receptor 12	GPR12	Promotes neurite outgrowth and blocks myelin inhibition in neurons (By similarity). Receptor with constitutive G(s) signaling activity that stimulates cyclic AMP production.	.	.	MNEDLKVNLSGLPRDYLDAAAAENISAAVSSRVPAVEPEPELVVNPWDIVLCTSGTLISCENAIVVLIIFHNPSLRAPMFLLIGSLALADLLAGIGLITNFVFAYLLQSEATKLVTIGLIVASFSASVCSLLAITVDRYLSLYYALTYHSERTVTFTYVMLVMLWGTSICLGLLPVMGWNCLRDESTCSVVRPLTKNNAAILSVSFLFMFALMLQLYIQICKIVMRHAHQIALQHHFLATSHYVTTRKGVSTLAIILGTFAACWMPFTLYSLIADYTYPSIYTYATLLPATYNSIINPVIYAFRNQEIQKALCLICCGCIPSSLAQRARSPSDV	Literature-reported	Role of the G-protein-coupled receptor GPR12 as high-affinity receptor for sphingosylphosphorylcholine and its expression and function in brain development. J Neurosci. 2003 Feb 1;23(3):907-14.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P47775
TTNBW4F	G2 accumulation protein (GPR132)	Q9UNW8	GP132_HUMAN	.	Probable G-protein coupled receptor 132; G2A	GPR132	"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."	.	.	MCPMLLKNGYNGNATPVTTTAPWASLGLSAKTCNNVSFEESRIVLVVVYSAVCTLGVPANCLTAWLALLQVLQGNVLAVYLLCLALCELLYTGTLPLWVIYIRNQHRWTLGLLACKVTAYIFFCNIYVSILFLCCISCDRFVAVVYALESRGRRRRRTAILISACIFILVGIVHYPVFQTEDKETCFDMLQMDSRIAGYYYARFTVGFAIPLSIIAFTNHRIFRSIKQSMGLSAAQKAKVKHSAIAVVVIFLVCFAPYHLVLLVKAAAFSYYRGDRNAMCGLEERLYTASVVFLCLSTVNGVADPIIYVLATDHSRQEVSRIHKGWKEWSMKTDVTRLTHSRDTEELQSPVALADHYTFSRPVHPPGSPCPAKRLIEESC	Literature-reported	Identification of 9-hydroxyoctadecadienoic acid and other oxidized free fatty acids as ligands of the G protein-coupled receptor G2A. J Biol Chem. 2005 Dec 9;280(49):40676-83.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-373076: Class A/1 (Rhodopsin-like receptors); R-HSA-416476: G alpha (q) signalling events	.	Q9UNW8
TTATO6X	Integral membrane protein GPR137 (GPR137)	Q96N19	G137A_HUMAN	.	Transmembrane 7 superfamily member 1-like 1 protein; TM7SF1L1; GPR137A; C11orf4	GPR137	"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."	.	.	MESNLSGLVPAAGLVPALPPAVTLGLTAAYTTLYALLFFSVYAQLWLVLLYGHKRLSYQTVFLALCLLWAALRTTLFSFYFRDTPRANRLGPLPFWLLYCCPVCLQFFTLTLMNLYFAQVVFKAKVKRRPEMSRGLLAVRGAFVGASLLFLLVNVLCAVLSHRRRAQPWALLLVRVLVSDSLFVICALSLAACLCLVARRAPSTSIYLEAKGTSVCQAAAMGGAMVLLYASRACYNLTALALAPQSRLDTFDYDWYNVSDQADLVNDLGNKGYLVFGLILFVWELLPTTLLVGFFRVHRPPQDLSTSHILNGQVFASRSYFFDRAGHCEDEGCSWEHSRGESTRCQDQAATTTVSTPPHRRDPPPSPTEYPGPSPPHPRPLCQVCLPLLAQDPGGRGYPLLWPAPCCSCHSELVPSP	Literature-reported	Down-regulation of GPR137 expression inhibits proliferation of colon cancer cells. RETRACTED ARTICLESee: Retraction NoticeActa Biochim Biophys Sin (Shanghai). 2014 Nov;46(11):935-41.	.	.	.	GPR137 family.	.	.	.	.	.	.	.	.	.	.	Q96N19
TTOL9B0	G-protein-coupled receptor PGR3 (GPR139)	Q6DWJ6	GP139_HUMAN	.	Probable G-protein coupled receptor 139; PGR3; GPRG1; G(q)-coupled orphan receptor GPRg1	GPR139	Orphan receptor. Seems to act through a G(q/11)-mediated pathway.	.	.	MEHTHAHLAANSSLSWWSPGSACGLGFVPVVYYSLLLCLGLPANILTVIILSQLVARRQKSSYNYLLALAAADILVLFFIVFVDFLLEDFILNMQMPQVPDKIIEVLEFSSIHTSIWITVPLTIDRYIAVCHPLKYHTVSYPARTRKVIVSVYITCFLTSIPYYWWPNIWTEDYISTSVHHVLIWIHCFTVYLVPCSIFFILNSIIVYKLRRKSNFRLRGYSTGKTTAILFTITSIFATLWAPRIIMILYHLYGAPIQNRWLVHIMSDIANMLALLNTAINFFLYCFISKRFRTMAAATLKAFFKCQKQPVQFYTNHNFSITSSPWISPANSHCIKMLVYQYDKNGKPIKVSP	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	.	.	.	Q6DWJ6
TTMPART	Uracil nucleotide/cysteinyl leukotriene receptor (GPR17)	Q13304	GPR17_HUMAN	.	UDP/CysLT receptor; R12; G-protein coupled receptor 17	GPR17	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.	.	.	MSKRSWWAGSRKPPREMLKLSGSDSSQSMNGLEVAPPGLITNFSLATAEQCGQETPLENMLFASFYLLDFILALVGNTLALWLFIRDHKSGTPANVFLMHLAVADLSCVLVLPTRLVYHFSGNHWPFGEIACRLTGFLFYLNMYASIYFLTCISADRFLAIVHPVKSLKLRRPLYAHLACAFLWVVVAVAMAPLLVSPQTVQTNHTVVCLQLYREKASHHALVSLAVAFTFPFITTVTCYLLIIRSLRQGLRVEKRLKTKAVRMIAIVLAIFLVCFVPYHVNRSVYVLHYRSHGASCATQRILALANRITSCLTSLNGALDPIMYFFVAEKFRHALCNLLCGKRLKGPPPSFEGKTNESSLSAKSEL	Literature-reported	The orphan receptor GPR17 identified as a new dual uracil nucleotides/cysteinyl-leukotrienes receptor. EMBO J. 2006 Oct 4;25(19):4615-27.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-391906: Leukotriene receptors; R-HSA-416476: G alpha (q) signalling events; R-HSA-417957: P2Y receptors; R-HSA-418594: G alpha (i) signalling events	.	Q13304
TTYUB4M	G-protein coupled receptor 174 (GPR174)	Q9BXC1	GP174_HUMAN	.	Probable G-protein coupled receptor 174	GPR174	Putative receptor for purines coupled to G-proteins.	.	.	MPANYTCTRPDGDNTDFRYFIYAVTYTVILVPGLIGNILALWVFYGYMKETKRAVIFMINLAIADLLQVLSLPLRIFYYLNHDWPFGPGLCMFCFYLKYVNMYASIYFLVCISVRRFWFLMYPFRFHDCKQKYDLYISIAGWLIICLACVLFPLLRTSDDTSGNRTKCFVDLPTRNVNLAQSVVMMTIGELIGFVTPLLIVLYCTWKTVLSLQDKYPMAQDLGEKQKALKMILTCAGVFLICFAPYHFSFPLDFLVKSNEIKSCLARRVILIFHSVALCLASLNSCLDPVIYYFSTNEFRRRLSRQDLHDSIQLHAKSFVSNHTASTMTPELC	Literature-reported	TGFalpha shedding assay: an accurate and versatile method for detecting GPCR activation. Nat Methods. 2012 Oct;9(10):1021-9.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9BXC1
TTSLJAR	N-arachidonyl glycine receptor (GPR18)	Q14330	GPR18_HUMAN	.	NAGly receptor; GPCRW; G-protein coupled receptor 18	GPR18	"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."	.	.	MITLNNQDQPVPFNSSHPDEYKIAALVFYSCIFIIGLFVNITALWVFSCTTKKRTTVTIYMMNVALVDLIFIMTLPFRMFYYAKDEWPFGEYFCQILGALTVFYPSIALWLLAFISADRYMAIVQPKYAKELKNTCKAVLACVGVWIMTLTTTTPLLLLYKDPDKDSTPATCLKISDIIYLKAVNVLNLTRLTFFFLIPLFIMIGCYLVIIHNLLHGRTSKLKPKVKEKSIRIIITLLVQVLVCFMPFHICFAFLMLGTGENSYNPWGAFTTFLMNLSTCLDVILYYIVSKQFQARVISVMLYRNYLRSMRRKSFRSGSLRSLSNINSEML	Literature-reported	Identification of N-arachidonylglycine as the endogenous ligand for orphan G-protein-coupled receptor GPR18. Biochem Biophys Res Commun. 2006 Sep 1;347(3):827-32.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-373076: Class A/1 (Rhodopsin-like receptors); R-HSA-418594: G alpha (i) signalling events	.	Q14330
TTT23CG	G protein coupled receptor 182 (GPR182)	O15218	GP182_HUMAN	GPCR rhodopsin	Gprotein coupled receptor 182; GPR182	GPR182	Orphan receptor.	.	.	MSVKPSWGPGPSEGVTAVPTSDLGEIHNWTELLDLFNHTLSECHVELSQSTKRVVLFALYLAMFVVGLVENLLVICVNWRGSGRAGLMNLYILNMAIADLGIVLSLPVWMLEVTLDYTWLWGSFSCRFTHYFYFVNMYSSIFFLVCLSVDRYVTLTSASPSWQRYQHRVRRAMCAGIWVLSAIIPLPEVVHIQLVEGPEPMCLFMAPFETYSTWALAVALSTTILGFLLPFPLITVFNVLTACRLRQPGQPKSRRHCLLLCAYVAVFVMCWLPYHVTLLLLTLHGTHISLHCHLVHLLYFFYDVIDCFSMLHCVINPILYNFLSPHFRGRLLNAVVHYLPKDQTKAGTCASSSSCSTQHSIIITKGDSQPAAAAPHPEPSLSFQAHHLLPNTSPISPTQPLTPS	Literature-reported	Orphan Gpr182 suppresses ERK-mediated intestinal proliferation during regeneration and adenoma formation. J Clin Invest. 2017 Feb 1;127(2):593-607.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	O15218
TTME5YJ	EBV-induced G-protein coupled receptor 2 (GPR183)	P32249	GP183_HUMAN	.	hEBI2; G-protein coupled receptor 183; Epstein-Barr virus-induced G-protein coupled receptor 2; EBI2	GPR183	"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)."	.	.	MDIQMANNFTPPSATPQGNDCDLYAHHSTARIVMPLHYSLVFIIGLVGNLLALVVIVQNRKKINSTTLYSTNLVISDILFTTALPTRIAYYAMGFDWRIGDALCRITALVFYINTYAGVNFMTCLSIDRFIAVVHPLRYNKIKRIEHAKGVCIFVWILVFAQTLPLLINPMSKQEAERITCMEYPNFEETKSLPWILLGACFIGYVLPLIIILICYSQICCKLFRTAKQNPLTEKSGVNKKALNTIILIIVVFVLCFTPYHVAIIQHMIKKLRFSNFLECSQRHSFQISLHFTVCLMNFNCCMDPFIYFFACKGYKRKVMRMLKRQVSVSISSAVKSAPEENSREMTETQMMIHSKSSNGK	Literature-reported	Oxysterols direct immune cell migration via EBI2. Nature. 2011 Jul 27;475(7357):524-7.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-373076: Class A/1 (Rhodopsin-like receptors); R-HSA-418594: G alpha (i) signalling events	.	P32249
TT26C7Z	G-protein coupled receptor 20 (GPR20)	Q99678	GPR20_HUMAN	.	.	GPR20	Orphan receptor with constitutive G(i) signaling activity that activate cyclic AMP.	.	.	MPSVSPAGPSAGAVPNATAVTTVRTNASGLEVPLFHLFARLDEELHGTFPGLWLALMAVHGAIFLAGLVLNGLALYVFCCRTRAKTPSVIYTINLVVTDLLVGLSLPTRFAVYYGARGCLRCAFPHVLGYFLNMHCSILFLTCICVDRYLAIVRPEGSRRCRQPACARAVCAFVWLAAGAVTLSVLGVTGSRPCCRVFALTVLEFLLPLLVISVFTGRIMCALSRPGLLHQGRQRRVRAMQLLLTVLIIFLVCFTPFHARQVAVALWPDMPHHTSLVVYHVAVTLSSLNSCMDPIVYCFVTSGFQATVRGLFGQHGEREPSSGDVVSMHRSSKGSGRHHILSAGPHALTQALANGPEA	Clinical trial	"Identification and Therapeutic Targeting of GPR20, Selectively Expressed in Gastrointestinal Stromal Tumors, with DS-6157a, a First-in-Class Antibody-Drug Conjugate. Cancer Discov. 2021 Jun;11(6):1508-1523."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-418555: G alpha (s) signalling events; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production	.	Q99678
TTHZVSK	G protein-coupled receptor 3 (GPR3)	P46089	GPR3_HUMAN	.	G-protein coupled receptor 3; ACCA orphan receptor; ACCA	GPR3	"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)."	.	.	MMWGAGSPLAWLSAGSGNVNVSSVGPAEGPTGPAAPLPSPKAWDVVLCISGTLVSCENALVVAIIVGTPAFRAPMFLLVGSLAVADLLAGLGLVLHFAAVFCIGSAEMSLVLVGVLAMAFTASIGSLLAITVDRYLSLYNALTYYSETTVTRTYVMLALVWGGALGLGLLPVLAWNCLDGLTTCGVVYPLSKNHLVVLAIAFFMVFGIMLQLYAQICRIVCRHAQQIALQRHLLPASHYVATRKGIATLAVVLGAFAACWLPFTVYCLLGDAHSPPLYTYLTLLPATYNSMINPIIYAFRNQDVQKVLWAVCCCCSSSKIPFRSRSPSDV	Literature-reported	Identification of a novel small-molecule agonist for human G protein-coupled receptor 3. J Pharmacol Exp Ther. 2014 Jun;349(3):437-43.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P46089
TT71ZLK	G-protein coupled receptor 31 (GPR31)	O00270	GPR31_HUMAN	.	"12-HETER; 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid receptor; 12-(S)-HETE receptor"	GPR31	"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."	.	.	MPFPNCSAPSTVVATAVGVLLGLECGLGLLGNAVALWTFLFRVRVWKPYAVYLLNLALADLLLAACLPFLAAFYLSLQAWHLGRVGCWALHFLLDLSRSVGMAFLAAVALDRYLRVVHPRLKVNLLSPQAALGVSGLVWLLMVALTCPGLLISEAAQNSTRCHSFYSRADGSFSIIWQEALSCLQFVLPFGLIVFCNAGIIRALQKRLREPEKQPKLQRAQALVTLVVVLFALCFLPCFLARVLMHIFQNLGSCRALCAVAHTSDVTGSLTYLHSVLNPVVYCFSSPTFRSSYRRVFHTLRGKGQAAEPPDFNPRDSYS	Literature-reported	Identification of the orphan G protein-coupled receptor GPR31 as a receptor for 12-(S)-hydroxyeicosatetraenoic acid. J Biol Chem. 2011 Sep 30;286(39):33832-40.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-418594: G alpha (i) signalling events; R-HSA-444209: Free fatty acid receptors	.	O00270
TT7OCUB	G-protein coupled receptor 32 (GPR32)	O75388	GPR32_HUMAN	.	Probable G-protein coupled receptor 32	GPR32	Orphan receptor.	.	.	MNGVSEGTRGCSDRQPGVLTRDRSCSRKMNSSGCLSEEVGSLRPLTVVILSASIVVGVLGNGLVLWMTVFRMARTVSTVCFFHLALADFMLSLSLPIAMYYIVSRQWLLGEWACKLYITFVFLSYFASNCLLVFISVDRCISVLYPVWALNHRTVQRASWLAFGVWLLAAALCSAHLKFRTTRKWNGCTHCYLAFNSDNETAQIWIEGVVEGHIIGTIGHFLLGFLGPLAIIGTCAHLIRAKLLREGWVHANRPKRLLLVLVSAFFIFWSPFNVVLLVHLWRRVMLKEIYHPRMLLILQASFALGCVNSSLNPFLYVFVGRDFQEKFFQSLTSALARAFGEEEFLSSCPRGNAPRE	Literature-reported	Resolvin D1 receptor stereoselectivity and regulation of inflammation and proresolving microRNAs. Am J Pathol. 2012 May;180(5):2018-27.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-418555: G alpha (s) signalling events; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production	.	O75388
TTVXSTQ	G-protein coupled receptor 34 (GPR34)	Q9UPC5	GPR34_HUMAN	.	Probable G-protein coupled receptor 34	GPR34	Orphan receptor.	.	.	MRSHTITMTTTSVSSWPYSSHRMRFITNHSDQPPQNFSATPNVTTCPMDEKLLSTVLTTSYSVIFIVGLVGNIIALYVFLGIHRKRNSIQIYLLNVAIADLLLIFCLPFRIMYHINQNKWTLGVILCKVVGTLFYMNMYISIILLGFISLDRYIKINRSIQQRKAITTKQSIYVCCIVWMLALGGFLTMIILTLKKGGHNSTMCFHYRDKHNAKGEAIFNFILVVMFWLIFLLIILSYIKIGKNLLRISKRRSKFPNSGKYATTARNSFIVLIIFTICFVPYHAFRFIYISSQLNVSSCYWKEIVHKTNEIMLVLSSFNSCLDPVMYFLMSSNIRKIMCQLLFRRFQGEPSRSESTSEFKPGYSLHDTSVAVKIQSSSKST	Literature-reported	GPR34 is a receptor for lysophosphatidylserine with a fatty acid at the sn-2 position. J Biochem. 2012 May;151(5):511-8.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9UPC5
TT254XD	Kynurenic acid receptor (GPR35)	Q9HC97	GPR35_HUMAN	GPCR rhodopsin	KYNA receptor; Gprotein coupled receptor 35; GPR35	GPR35	"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."	.	.	MNGTYNTCGSSDLTWPPAIKLGFYAYLGVLLVLGLLLNSLALWVFCCRMQQWTETRIYMTNLAVADLCLLCTLPFVLHSLRDTSDTPLCQLSQGIYLTNRYMSISLVTAIAVDRYVAVRHPLRARGLRSPRQAAAVCAVLWVLVIGSLVARWLLGIQEGGFCFRSTRHNFNSMAFPLLGFYLPLAVVVFCSLKVVTALAQRPPTDVGQAEATRKAARMVWANLLVFVVCFLPLHVGLTVRLAVGWNACALLETIRRALYITSKLSDANCCLDAICYYYMAKEFQEASALAVAPSAKAHKSQDSLCVTLA	Literature-reported	Identification of novel species-selective agonists of the G-protein-coupled receptor GPR35 that promote recruitment of beta-arrestin-2 and activate Galpha13. Biochem J. 2010 Dec 15;432(3):451-9.	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction	R-HSA-373076: Class A/1 (Rhodopsin-like receptors)	.	Q9HC97
TTTPCNU	G-protein coupled receptor 39 (GPR39)	O43194	GPR39_HUMAN	GPCR rhodopsin	Gprotein coupled receptor 39; GPR39	GPR39	"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."	.	.	MASPSLPGSDCSQIIDHSHVPEFEVATWIKITLILVYLIIFVMGLLGNSATIRVTQVLQKKGYLQKEVTDHMVSLACSDILVFLIGMPMEFYSIIWNPLTTSSYTLSCKLHTFLFEACSYATLLHVLTLSFERYIAICHPFRYKAVSGPCQVKLLIGFVWVTSALVALPLLFAMGTEYPLVNVPSHRGLTCNRSSTRHHEQPETSNMSICTNLSSRWTVFQSSIFGAFVVYLVVLLSVAFMCWNMMQVLMKSQKGSLAGGTRPPQLRKSESEESRTARRQTIIFLRLIVVTLAVCWMPNQIRRIMAAAKPKHDWTRSYFRAYMILLPFSETFFYLSSVINPLLYTVSSQQFRRVFVQVLCCRLSLQHANHEKRLRVHAHSTTDSARFVQRPLLFASRRQSSARRTEKIFLSTFQSEAEPQSKSQSLSLESLEPNSGAKPANSAAENGFQEHEV	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 105).	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-373076:Class A/1 (Rhodopsin-like receptors)	.	O43194
TTNET8J	G-protein coupled receptor 55 (GPR55)	Q9Y2T6	GPR55_HUMAN	GPCR rhodopsin	LPIR1	GPR55	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.	.	.	MSQQNTSGDCLFDGVNELMKTLQFAVHIPTFVLGLLLNLLAIHGFSTFLKNRWPDYAATSIYMINLAVFDLLLVLSLPFKMVLSQVQSPFPSLCTLVECLYFVSMYGSVFTICFISMDRFLAIRYPLLVSHLRSPRKIFGICCTIWVLVWTGSIPIYSFHGKVEKYMCFHNMSDDTWSAKVFFPLEVFGFLLPMGIMGFCCSRSIHILLGRRDHTQDWVQQKACIYSIAASLAVFVVSFLPVHLGFFLQFLVRNSFIVECRAKQSISFFLQLSMCFSNVNCCLDVFCYYFVIKEFRMNIRAHRPSRVQLVLQDTTISRG	Successful	The orphan receptor GPR55 is a novel cannabinoid receptor. Br J Pharmacol. 2007 Dec;152(7):1092-101.	34	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	.	R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418594:G alpha (i) signalling events	.	Q9Y2T6
TTSDWS5	G-protein coupled receptor 6 (GPR6)	P46095	GPR6_HUMAN	G-protein coupled receptor 1 family	Sphingosine 1-phosphate receptor GPR6	GPR6	Orphan receptor with constitutive G(s) signaling activity that activate cyclic AMP. Promotes neurite outgrowth and blocks myelin inhibition in neurons (By similarity). {ECO:0000250}.	.	.	MNASAASLNDSQVVVVAAEGAAAAATAAGGPDTGEWGPPAAAALGAGGGANGSLELSSQLSAGPPGLLLPAVNPWDVLLCVSGTVIAGENALVVALIASTPALRTPMFVLVGSLATADLLAGCGLILHFVFQYLVPSETVSLLTVGFLVASFAASVSSLLAITVDRYLSLYNALTYYSRRTLLGVHLLLAATWTVSLGLGLLPVLGWNCLAERAACSVVRPLARSHVALLSAAFFMVFGIMLHLYVRICQVVWRHAHQIALQQHCLAPPHLAATRKGVGTLAVVLGTFGASWLPFAIYCVVGSHEDPAVYTYATLLPATYNSMINPIIYAFRNQEIQRALWLLLCGCFQSKVPFRSRSPSEV	Clinical trial	Development of CVN424: A Selective and Novel GPR6 Inverse Agonist Effective in Models of Parkinson Disease. J Pharmacol Exp Ther. 2021 Jun;377(3):407-416.	.	.	.	.	.	.	.	.	.	.	.	hsa:2830	.	.	P46095;
TT2D5VM	G-protein coupled receptor 63 (GPR63)	Q9BZJ6	GPR63_HUMAN	.	Probable G-protein coupled receptor 63; PSP24B; PSP24-beta; PSP24-2	GPR63	Orphan receptor. May play a role in brain function.	.	.	MVFSAVLTAFHTGTSNTTFVVYENTYMNITLPPPFQHPDLSPLLRYSFETMAPTGLSSLTVNSTAVPTTPAAFKSLNLPLQITLSAIMIFILFVSFLGNLVVCLMVYQKAAMRSAINILLASLAFADMLLAVLNMPFALVTILTTRWIFGKFFCRVSAMFFWLFVIEGVAILLIISIDRFLIIVQRQDKLNPYRAKVLIAVSWATSFCVAFPLAVGNPDLQIPSRAPQCVFGYTTNPGYQAYVILISLISFFIPFLVILYSFMGILNTLRHNALRIHSYPEGICLSQASKLGLMSLQRPFQMSIDMGFKTRAFTTILILFAVFIVCWAPFTTYSLVATFSKHFYYQHNFFEISTWLLWLCYLKSALNPLIYYWRIKKFHDACLDMMPKSFKFLPQLPGHTKRRIRPSAVYVCGEHRTVV	Literature-reported	Sphingosine 1-phosphate and dioleoylphosphatidic acid are low affinity agonists for the orphan receptor GPR63. Cell Signal. 2003 Apr;15(4):435-46.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9BZJ6
TTG0MQD	Inflammation-related GPCR EX33 (GPR84)	Q9NQS5	GPR84_HUMAN	.	Inflammation-related G-protein coupled receptor EX33; G-protein coupled receptor 84; EX33	GPR84	"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."	.	.	MWNSSDANFSCYHESVLGYRYVAVSWGVVVAVTGTVGNVLTLLALAIQPKLRTRFNLLIANLTLADLLYCTLLQPFSVDTYLHLHWRTGATFCRVFGLLLFASNSVSILTLCLIALGRYLLIAHPKLFPQVFSAKGIVLALVSTWVVGVASFAPLWPIYILVPVVCTCSFDRIRGRPYTTILMGIYFVLGLSSVGIFYCLIHRQVKRAAQALDQYKLRQASIHSNHVARTDEAMPGRFQELDSRLASGGPSEGISSEPVSAATTQTLEGDSSEVGDQINSKRAKQMAEKSPPEASAKAQPIKGARRAPDSSSEFGKVTRMCFAVFLCFALSYIPFLLLNILDARVQAPRVVHMLAANLTWLNGCINPVLYAAMNRQFRQAYGSILKRGPRSFHRLH	Clinical trial	Medium-chain fatty acids as ligands for orphan G protein-coupled receptor GPR84. J Biol Chem. 2006 Nov 10;281(45):34457-64.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-418555: G alpha (s) signalling events; R-HSA-6798695: Neutrophil degranulation; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production	.	Q9NQS5
TTNRQJ3	Super conserved receptor brain 2 (GPR85)	P60893	GPR85_HUMAN	GPCR rhodopsin	Super conserved receptor expressed in brain 2; SREB2; Probable Gprotein coupled receptor 85; Probable G-protein coupled receptor 85	GPR85	Orphan receptor.	.	.	MANYSHAADNILQNLSPLTAFLKLTSLGFIIGVSVVGNLLISILLVKDKTLHRAPYYFLLDLCCSDILRSAICFPFVFNSVKNGSTWTYGTLTCKVIAFLGVLSCFHTAFMLFCISVTRYLAIAHHRFYTKRLTFWTCLAVICMVWTLSVAMAFPPVLDVGTYSFIREEDQCTFQHRSFRANDSLGFMLLLALILLATQLVYLKLIFFVHDRRKMKPVQFVAAVSQNWTFHGPGASGQAAANWLAGFGRGPTPPTLLGIRQNANTTGRRRLLVLDEFKMEKRISRMFYIMTFLFLTLWGPYLVACYWRVFARGPVVPGGFLTAAVWMSFAQAGINPFVCIFSNRELRRCFSTTLLYCRKSRLPREPYCVI	Literature-reported	"SREB2/GPR85, a schizophrenia risk factor, negatively regulates hippocampal adult neurogenesis and neurogenesis-dependent learning and memory. Eur J Neurosci. 2012 Sep;36(5):2597-608."	.	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	.	.	.	P60893
TTO897C	G protein coupled receptor 87 (GPR87)	Q9BY21	GPR87_HUMAN	GPCR rhodopsin	GPR87; G-protein coupled receptor 95; G-protein coupled receptor 87	GPR87	Receptor for lysophosphatidic acid (LPA). Necessary for p53/TP53-dependent survival in response to DNA damage.	.	.	MGFNLTLAKLPNNELHGQESHNSGNRSDGPGKNTTLHNEFDTIVLPVLYLIIFVASILLNGLAVWIFFHIRNKTSFIFYLKNIVVADLIMTLTFPFRIVHDAGFGPWYFKFILCRYTSVLFYANMYTSIVFLGLISIDRYLKVVKPFGDSRMYSITFTKVLSVCVWVIMAVLSLPNIILTNGQPTEDNIHDCSKLKSPLGVKWHTAVTYVNSCLFVAVLVILIGCYIAISRYIHKSSRQFISQSSRKRKHNQSIRVVVAVFFTCFLPYHLCRIPFTFSHLDRLLDESAQKILYYCKEITLFLSACNVCLDPIIYFFMCRSFSRRLFKKSNIRTRSESIRSLQSVRRSEVRIYYDYTDV	Literature-reported	The orphan GPCR GPR87 was deorphanized and shown to be a lysophosphatidic acid receptor. Biochem Biophys Res Commun. 2007 Nov 23;363(3):861-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9BY21
TTMRQY1	Striatum-specific G-protein coupled receptor (GPR88)	Q9GZN0	GPR88_HUMAN	.	STRG; Probable G-protein coupled receptor 88	GPR88	"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."	.	.	MTNSSSTSTSSTTGGSLLLLCEEEESWAGRRIPVSLLYSGLAIGGTLANGMVIYLVSSFRKLQTTSNAFIVNGCAADLSVCALWMPQEAVLGLLPTGSAEPPADWDGAGGSYRLLRGGLLGLGLTVSLLSHCLVALNRYLLITRAPATYQALYQRRHTAGMLALSWALALGLVLLLPPWAPRPGAAPPRVHYPALLAAAALLAQTALLLHCYLGIVRRVRVSVKRVSVLNFHLLHQLPGCAAAAAAFPGAQHAPGPGGAAHPAQAQPLPPALHPRRAQRRLSGLSVLLLCCVFLLATQPLVWVSLASGFSLPVPWGVQAASWLLCCALSALNPLLYTWRNEEFRRSVRSVLPGVGDAAAAAVAATAVPAVSQAQLGTRAAGQHW	Literature-reported	"Synthesis, pharmacological characterization, and structure-activity relationship studies of small molecular agonists for the orphan GPR88 receptor. ACS Chem Neurosci. 2014 Jul 16;5(7):576-87."	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9GZN0
TTHRAPJ	G-protein coupled receptor C 5D (GPRC5D)	Q9NZD1	GPC5D_HUMAN	.	.	GPRC5D	"extracellular exosome, intracellular membrane-bounded organelle, plasma membrane, receptor complex, protein kinase activator activity"	.	.	MYKDCIESTGDYFLLCDAEGPWGIILESLAILGIVVTILLLLAFLFLMRKIQDCSQWNVLPTQLLFLLSVLGLFGLAFAFIIELNQQTAPVRYFLFGVLFALCFSCLLAHASNLVKLVRGCVSFSWTTILCIAIGCSLLQIIIATEYVTLIMTRGMMFVNMTPCQLNVDFVVLLVYVLFLMALTFFVSKATFCGPCENWKQHGRLIFITVLFSIIIWVVWISMLLRGNPQFQRQPQWDDPVVCIALVTNAWVFLLLYIVPELCILYRSCRQECPLQGNACPVTAYQHSFQVENQELSRARDSDGAEEDVALTSYGTPIQPQTVDPTQECFIPQAKLSPQQDAGGV	Clinical trial	GPRC5D is a target for the immunotherapy of multiple myeloma with rationally designed CAR T cells. Sci Transl Med. 2019 Mar 27;11(485):eaau7746.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9NZD1
TTI1PRE	G-protein coupled receptor GPCR33 (GPRC6A)	Q5T6X5	GPC6A_HUMAN	.	hGPRC6A; hGPCR33; G-protein coupled receptor family C group 6 member A	GPRC6A	"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."	.	.	MAFLIILITCFVIILATSQPCQTPDDFVAATSPGHIIIGGLFAIHEKMLSSEDSPRRPQIQECVGFEISVFLQTLAMIHSIEMINNSTLLPGVKLGYEIYDTCTEVTVAMAATLRFLSKFNCSRETVEFKCDYSSYMPRVKAVIGSGYSEITMAVSRMLNLQLMPQVGYESTAEILSDKIRFPSFLRTVPSDFHQIKAMAHLIQKSGWNWIGIITTDDDYGRLALNTFIIQAEANNVCIAFKEVLPAFLSDNTIEVRINRTLKKIILEAQVNVIVVFLRQFHVFDLFNKAIEMNINKMWIASDNWSTATKITTIPNVKKIGKVVGFAFRRGNISSFHSFLQNLHLLPSDSHKLLHEYAMHLSACAYVKDTDLSQCIFNHSQRTLAYKANKAIERNFVMRNDFLWDYAEPGLIHSIQLAVFALGYAIRDLCQARDCQNPNAFQPWELLGVLKNVTFTDGWNSFHFDAHGDLNTGYDVVLWKEINGHMTVTKMAEYDLQNDVFIIPDQETKNEFRNLKQIQSKCSKECSPGQMKKTTRSQHICCYECQNCPENHYTNQTDMPHCLLCNNKTHWAPVRSTMCFEKEVEYLNWNDSLAILLLILSLLGIIFVLVVGIIFTRNLNTPVVKSSGGLRVCYVILLCHFLNFASTSFFIGEPQDFTCKTRQTMFGVSFTLCISCILTKSLKILLAFSFDPKLQKFLKCLYRPILIIFTCTGIQVVICTLWLIFAAPTVEVNVSLPRVIILECEEGSILAFGTMLGYIAILAFICFIFAFKGKYENYNEAKFITFGMLIYFIAWITFIPIYATTFGKYVPAVEIIVILISNYGILYCTFIPKCYVIICKQEINTKSAFLKMIYSYSSHSVSSIALSPASLDSMSGNVTMTNPSSSGKSATWQKSKDLQAQAFAHICRENATSVSKTLPRKRMSSI	Literature-reported	Deorphanization of GPRC6A: a promiscuous L-alpha-amino acid receptor with preference for basic amino acids. Mol Pharmacol. 2005 Mar;67(3):589-97.	0	.	.	.	.	.	.	.	.	.	.	hsa04621: NOD-like receptor signaling pathway	R-HSA-416476: G alpha (q) signalling events; R-HSA-420499: Class C/3 (Metabotropic glutamate/pheromone receptors)	.	Q5T6X5
TTYAHBP	Glutathione peroxidase (GPX1)	P07203	GPX1_HUMAN	Peroxidases	GSHPx-1; GPX1; Cellular glutathione peroxidase	GPX1	Protects the hemoglobin in erythrocytes from oxidative breakdown.	EC 1.11.1.9	2F8A	MCAARLAAAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRRFQTIDIEPDIEALLSQGPSCA	Literature-reported	CSF markers in amyotrophic lateral sclerosis. J Neural Transm (Vienna). 2012 Jul;119(7):747-57. 	.	.	.	.	.	.	.	.	.	.	.	hsa00480: Glutathione metabolism; hsa00590: Arachidonic acid metabolism; hsa01100: Metabolic pathways; hsa04918: Thyroid hormone synthesis; hsa05014: Amyotrophic lateral sclerosis; hsa05016: Huntington disease; hsa05022: Pathways of neurodegeneration - multiple diseases	R-HSA-2142688: Synthesis of 5-eicosatetraenoic acids; R-HSA-2142712: Synthesis of 12-eicosatetraenoic acid derivatives; R-HSA-2142770: Synthesis of 15-eicosatetraenoic acid derivatives; R-HSA-3299685: Detoxification of Reactive Oxygen Species	MetaCyc:HS00019-MON	.
TTEYRJ9	GRB2 messenger RNA (GRB2 mRNA)	P62993	GRB2_HUMAN	mRNA target	SH2/SH3 adapter GRB2 (mRNA); Protein Ash (mRNA); Growth factor receptor-bound protein 2 (mRNA); Adapter protein GRB2 (mRNA); ASH (mRNA)	GRB2	Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway.	.	5CDW; 4P9Z; 4P9V; 3WA4; 3S8O	MEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQQPTYVQALFDFDPQEDGELGFRRGDFIHVMDNSDPNWWKGACHGQTGMFPRNYVTPVNRNV	Clinical trial	"ClinicalTrials.gov (NCT01159028) Clinical Trial of BP1001 (L-Grb-2 Antisense Oligonucleotide) in CML, AML, ALL & MDS. U.S. National Institutes of Health."	21	mRNA	mRNA target	.	.	.	SH2 domain; SH3 domain	PF00017; PF00018	PF00017; SH2; PF00018; SH3_1	.	.	"hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa01522: Endocrine resistance; hsa04010: MAPK signaling pathway; hsa04012: ErbB signaling pathway; hsa04014: Ras signaling pathway; hsa04062: Chemokine signaling pathway; hsa04068: FoxO signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04380: Osteoclast differentiation; hsa04510: Focal adhesion; hsa04540: Gap junction; hsa04550: Signaling pathways regulating pluripotency of stem cells; 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; hsa04714: Thermogenesis; hsa04722: Neurotrophin signaling pathway; hsa04910: Insulin signaling pathway; hsa04912: GnRH signaling pathway; hsa04915: Estrogen signaling pathway; hsa04917: Prolactin signaling pathway; hsa04926: Relaxin signaling pathway; hsa04935: Growth hormone synthesis, secretion and action; hsa05034: Alcoholism; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05163: Human cytomegalovirus infection; hsa05165: Human papillomavirus infection; hsa05200: Pathways in cancer; hsa05203: Viral carcinogenesis; hsa05205: Proteoglycans in cancer; hsa05206: MicroRNAs in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05210: Colorectal cancer; hsa05211: Renal cell carcinoma; hsa05213: Endometrial cancer; hsa05214: Glioma; hsa05215: Prostate cancer; hsa05220: Chronic myeloid leukemia; hsa05221: Acute myeloid leukemia; hsa05223: Non-small cell lung cancer; hsa05224: Breast cancer; hsa05225: Hepatocellular carcinoma; hsa05226: Gastric cancer; hsa05231: Choline metabolism in cancer"	"R-HSA-109704: PI3K Cascade; R-HSA-112412: SOS-mediated signalling; 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-1257604: PIP3 activates AKT signaling; R-HSA-1295596: Spry regulation of FGF signaling; R-HSA-1433557: Signaling by SCF-KIT; R-HSA-1433559: Regulation of KIT signaling; R-HSA-167044: Signalling to RAS; 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-1839117: Signaling by cytosolic FGFR1 fusion mutants; R-HSA-186763: Downstream signal transduction; R-HSA-1963640: GRB2 events in ERBB2 signaling; R-HSA-1963642: PI3K events in ERBB2 signaling; R-HSA-2029482: Regulation of actin dynamics for phagocytic cup formation; R-HSA-210993: Tie2 Signaling; R-HSA-2179392: EGFR Transactivation by Gastrin; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-2424491: DAP12 signaling; R-HSA-2428933: SHC-related events triggered by IGF1R; 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-354194: GRB2:SOS provides linkage to MAPK signaling for Integrins; R-HSA-375165: NCAM signaling for neurite out-growth; R-HSA-388841: Costimulation by the CD28 family; R-HSA-389359: CD28 dependent Vav1 pathway; R-HSA-391160: Signal regulatory protein family interactions; R-HSA-512988: Interleukin-3, Interleukin-5 and GM-CSF signaling; R-HSA-5637810: Constitutive Signaling by EGFRvIII; 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-5655253: Signaling by FGFR2 in disease; R-HSA-5655291: Signaling by FGFR4 in disease; R-HSA-5655302: Signaling by FGFR1 in disease; R-HSA-5655332: Signaling by FGFR3 in disease; R-HSA-5663213: RHO GTPases Activate WASPs and WAVEs; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6807004: Negative regulation of MET activity; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-74749: Signal attenuation; R-HSA-74751: Insulin receptor signalling cascade; R-HSA-8851805: MET activates RAS signaling; R-HSA-8851907: MET activates PI3K/AKT signaling; R-HSA-8853659: RET signaling; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis; R-HSA-8865999: MET activates PTPN11; R-HSA-8875360: InlB-mediated entry of Listeria monocytogenes into host cell; R-HSA-8875555: MET activates RAP1 and RAC1; R-HSA-8875656: MET receptor recycling; R-HSA-8983432: Interleukin-15 signaling; R-HSA-9013420: RHOU GTPase cycle; R-HSA-9026519: Activated NTRK2 signals through RAS; R-HSA-9027284: Erythropoietin activates RAS; R-HSA-9028335: Activated NTRK2 signals through PI3K; R-HSA-9028731: Activated NTRK2 signals through FRS2 and FRS3; R-HSA-9034864: Activated NTRK3 signals through RAS; R-HSA-912526: Interleukin receptor SHC signaling; R-HSA-912631: Regulation of signaling by CBL; R-HSA-9607240: FLT3 Signaling; R-HSA-9634285: Constitutive Signaling by Overexpressed ERBB2; R-HSA-9645135: STAT5 Activation; R-HSA-9664422: FCGR3A-mediated phagocytosis; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665348: Signaling by ERBB2 ECD mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants; R-HSA-9670439: Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants; R-HSA-9673767: Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants; R-HSA-9673770: Signaling by PDGFRA extracellular domain mutants; R-HSA-9674555: Signaling by CSF3 (G-CSF); R-HSA-9702518: STAT5 activation downstream of FLT3 ITD mutants; R-HSA-9703465: Signaling by FLT3 fusion proteins; R-HSA-9703648: Signaling by FLT3 ITD and TKD mutants; R-HSA-9725370: Signaling by ALK fusions and activated point mutants; R-HSA-983695: Antigen activates B Cell Receptor (BCR) leading to generation of second messenger"	.	P62993
TTOUZN5	Gremlin-1 (Gremlin-1)	O60565	GREM1_HUMAN	.	"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"	GREM1	"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."	.	5AEJ	MSRTAYTVGALLLLLGTLLPAAEGKKKGSQGAIPPPDKAQHNDSEQTQSPQQPGSRNRGRGQGRGTAMPGEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHIRKEEGSFQSCSFCKPKKFTTMMVTLNCPELQPPTKKKRVTRVKQCRCISIDLD	Patented-recorded	VEGFR-2 inhibitors and the therapeutic applications thereof: a patent review (2012-2016).Expert Opin Ther Pat. 2017 Sep;27(9):987-1004.	15.5	.	.	DAN family.	.	.	DAN domain	PF03045	PF03045; DAN	.	.	hsa04350: TGF-beta signaling pathway	.	.	O60565
TTUGH4C	Grainyhead-like 2 (GRHL2)	Q6ISB3	GRHL2_HUMAN	.	Transcription factor CP2like 3; Grainyheadlike protein 2 homolog; GRHL2; Brother of mammalian grainyhead	GRHL2	"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)."	.	5MR7	MSQESDNNKRLVALVPMPSDPPFNTRRAYTSEDEAWKSYLENPLTAATKAMMSINGDEDSAAALGLLYDYYKVPRDKRLLSVSKASDSQEDQEKRNCLGTSEAQSNLSGGENRVQVLKTVPVNLSLNQDHLENSKREQYSISFPESSAIIPVSGITVVKAEDFTPVFMAPPVHYPRGDGEEQRVVIFEQTQYDVPSLATHSAYLKDDQRSTPDSTYSESFKDAATEKFRSASVGAEEYMYDQTSSGTFQYTLEATKSLRQKQGEGPMTYLNKGQFYAITLSETGDNKCFRHPISKVRSVVMVVFSEDKNRDEQLKYWKYWHSRQHTAKQRVLDIADYKESFNTIGNIEEIAYNAVSFTWDVNEEAKIFITVNCLSTDFSSQKGVKGLPLMIQIDTYSYNNRSNKPIHRAYCQIKVFCDKGAERKIRDEERKQNRKKGKGQASQTQCNSSSDGKLAAIPLQKKSDITYFKTMPDLHSQPVLFIPDVHFANLQRTGQVYYNTDDEREGGSVLVKRMFRPMEEEFGPVPSKQMKEEGTKRVLLYVRKETDDVFDALMLKSPTVKGLMEAISEKYGLPVEKIAKLYKKSKKGILVNMDDNIIEHYSNEDTFILNMESMVEGFKVTLMEI	Literature-reported	Grainyhead-like 2 (GRHL2) regulates epithelial plasticity in pancreatic cancer progression. Cancer Med. 2017 Nov;6(11):2686-2696.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q6ISB3
TTVPQTF	Glutamate receptor AMPA 1 (GRIA1)	P42261	GRIA1_HUMAN	Glutamate-gated ion channel	"Glutamate receptor ionotropic, AMPA 1; Glutamate receptor 1; GluR-K1; GluR-A; GluR-1; GluA1; GLUR1; GLUH1; AMPA-selective glutamate receptor 1"	GRIA1	"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."	.	.	MQHIFAFFCTGFLGAVVGANFPNNIQIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGALHVCFITPSFPVDTSNQFVLQLRPELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNILTTTEEGYRMLFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNYTDTIPAKIMQQWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFVPAATDAQAGGDNSSVQNRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHSEEFEEGRDQTTSDQSNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILIGGLGLAMLVALIEFCYKSRSESKRMKGFCLIPQQSINEAIRTSTLPRNSGAGASSGGSGENGRVVSHDFPKSMQSIPCMSHSSGMPLGATGL	Successful	Antibodies and venom peptides: new modalities for ion channels. Nat Rev Drug Discov. 2019 May;18(5):339-357.	34	TC=1.A.10	Glutamate gated ion channel	glutamate-gated ion channel (TC 1.A.10.1) family. GRIA1 subfamily. 	.	.	Receptor family ligand binding region; Ligand-gated ion channel; Ligated ion channel L-glutamate- and glycine-binding site	PF01094; PF00060; PF10613	PF01094; ANF_receptor; PF00060; Lig_chan; PF10613; Lig_chan-Glu_bd	1.A.10.1.23	The Glutamate-gated Ion Channel (GIC) Family of Neurotransmitter Receptors	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	"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"	.	P42261
TTWM461	Phosphorylated GluA2 (pGluA2)	P42262 (phosphorylated)	GRIA2_HUMAN	.	"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)"	GRIA2	"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)."	.	5ZG3; 5ZG2; 5ZG1; 5ZG0; 5YBG	MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDEMYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLRNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI	Literature-reported	Disruption of GluA2 phosphorylation potentiates stress responsivity. Behav Brain Res. 2017 Aug 30;333:83-89.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P42262
TT9HLZ0	Glutamate receptor AMPA 2 (GRIA2)	P42262	GRIA2_HUMAN	Glutamate-gated ion channel	"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"	GRIA2	"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."	.	5ZG3; 5ZG2; 5ZG1; 5ZG0; 5YBG	MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDEMYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLRNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI	Successful	Antibodies and venom peptides: new modalities for ion channels. Nat Rev Drug Discov. 2019 May;18(5):339-357.	34	TC=1.A.10	Glutamate-gated ion channel family	glutamate-gated ion channel (TC 1.A.10.1) family. GRIA2 subfamily. 	.	.	Receptor family ligand binding region; Ligand-gated ion channel; Ligated ion channel L-glutamate- and glycine-binding site	PF01094; PF00060; PF10613	PF01094; ANF_receptor; PF00060; Lig_chan; PF10613; Lig_chan-Glu_bd	1.A.10.1.13	The Glutamate-gated Ion Channel (GIC) Family of Neurotransmitter Receptors	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; hsa05016: Huntington disease; hsa05017: Spinocerebellar ataxia; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05030: Cocaine addiction; hsa05031: Amphetamine addiction; hsa05033: Nicotine addiction	"R-HSA-399710: Activation of AMPA receptors; R-HSA-416993: Trafficking of GluR2-containing AMPA receptors; R-HSA-438066: Unblocking of NMDA receptors, glutamate binding and activation; R-HSA-9022699: MECP2 regulates neuronal receptors and channels; R-HSA-9620244: Long-term potentiation"	.	P42262
TT82EZV	Glutamate receptor AMPA 3 (GRIA3)	P42263	GRIA3_HUMAN	Glutamate-gated ion channel	"Glutamate receptor ionotropic, AMPA 3; GluRK3; GluRC; GluR3; GluA3; GRIA3; AMPAselective glutamate receptor 3"	GRIA3	"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."	.	.	MARQKKMGQSVLRAVFFLVLGLLGHSHGGFPNTISIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTSFCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVGNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVNNENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFVPFSDQQISNDSASSENRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHLEDNNEEPRDPQSPPDPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILVGGLGLAMMVALIEFCYKSRAESKRMKLTKNTQNFKPAPATNTQNYATYREGYNVYGTESVKI	Successful	Antibodies and venom peptides: new modalities for ion channels. Nat Rev Drug Discov. 2019 May;18(5):339-357.	34	.	.	.	.	.	.	.	.	.	.	hsa04024: cAMP signaling pathway; hsa04080: Neuroactive ligand-receptor interaction; hsa04713: Circadian entrainment; hsa04723: Retrograde endocannabinoid signaling; hsa04724: Glutamatergic synapse; hsa04728: Dopaminergic synapse; hsa04730: Long-term depression; hsa05016: Huntington disease; hsa05017: Spinocerebellar ataxia; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05031: Amphetamine addiction; hsa05033: Nicotine addiction; hsa05202: Transcriptional misregulation in cancer	"R-HSA-399710: Activation of AMPA receptors; R-HSA-399719: Trafficking of AMPA receptors; R-HSA-416993: Trafficking of GluR2-containing AMPA receptors; R-HSA-438066: Unblocking of NMDA receptors, glutamate binding and activation; R-HSA-8849932: Synaptic adhesion-like molecules"	.	P42263
TTPJR0G	Glutamate receptor AMPA 4 (GRIA4)	P48058	GRIA4_HUMAN	Glutamate-gated ion channel	"Glutamate receptor ionotropic, AMPA 4; GluRD; GluR4; GluA4; GRIA4; AMPAselective glutamate receptor 4"	GRIA4	"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."	.	.	MRIISRQIVLLFSGFWGLAMGAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPMVIKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQDVPTLGNDTAAIENRTVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLSEAGVLDKLKNKWWYDKGECGPKDSGSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKLTFSEAIRNKARLSITGSVGENGRVLTPDCPKAVHTGTAIRQSSGLAVIASDLP	Successful	Antibodies and venom peptides: new modalities for ion channels. Nat Rev Drug Discov. 2019 May;18(5):339-357.	34	.	.	.	.	.	.	.	.	.	.	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	"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"	.	P48058
TT0MYE2	Glutamate receptor ionotropic kainate 1 (GRIK1)	P39086	GRIK1_HUMAN	Glutamate-gated ion channel	Glutamate receptor 5; GluR5 kainate receptor; GluR5; GluR-5; GRIK1; Excitatory amino acid receptor 3; EAA3	GRIK1	"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."	.	4MF3; 3FVO; 3FVN; 3FVK; 3FVG	MEHGTLLAQPGLWTRDTSWALLYFLCYILPQTAPQVLRIGGIFETVENEPVNVEELAFKFAVTSINRNRTLMPNTTLTYDIQRINLFDSFEASRRACDQLALGVAALFGPSHSSSVSAVQSICNALEVPHIQTRWKHPSVDNKDLFYINLYPDYAAISRAILDLVLYYNWKTVTVVYEDSTGLIRLQELIKAPSRYNIKIKIRQLPSGNKDAKPLLKEMKKGKEFYVIFDCSHETAAEILKQILFMGMMTEYYHYFFTTLDLFALDLELYRYSGVNMTGFRLLNIDNPHVSSIIEKWSMERLQAPPRPETGLLDGMMTTEAALMYDAVYMVAIASHRASQLTVSSLQCHRHKPWRLGPRFMNLIKEARWDGLTGHITFNKTNGLRKDFDLDIISLKEEGTEKAAGEVSKHLYKVWKKIGIWNSNSGLNMTDSNKDKSSNITDSLANRTLIVTTILEEPYVMYRKSDKPLYGNDRFEGYCLDLLKELSNILGFIYDVKLVPDGKYGAQNDKGEWNGMVKELIDHRADLAVAPLTITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYVLLACLGVSCVLFVIARFTPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVRDGSTMTFFKKSKISTYEKMWAFMSSRQQTALVRNSDEGIQRVLTTDYALLMESTSIEYVTQRNCNLTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEDNKEASALGVENIGGIFIVLAAGLVLSVFVAIGEFIYKSRKNNDIEQAFCFFYGLQCKQTHPTNSTSGTTLSTDLECGKLIREERGIRKQSSVHTV	Successful	Development of medications for alcohol use disorders: recent advances and ongoing challenges. Expert Opin Emerg Drugs. 2005 May;10(2):323-43.	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04724:Glutamatergic synapse	R-HSA-451307: Activation of Na-permeable kainate receptors; R-HSA-451308: Activation of Ca-permeable Kainate Receptor	.	P39086
TT0K5RG	Glutamate receptor ionotropic kainate 2 (GRIK2)	Q13002	GRIK2_HUMAN	Glutamate-gated ion channel	"Glutamate receptor ionotropic, kainate 2; Glutamate receptor 6; GluR6; GluR-6; GluK2; Excitatory amino acid receptor 4; EAA4"	GRIK2	"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."	.	5CMM; 3QXM	MKIIFPILSNPVFRRTVKLLLCLLWIGYSQGTTHVLRFGGIFEYVESGPMGAEELAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAVQSICNALGVPHIQTRWKHQVSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNLRLKIRQLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNTENTQVSSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVVSVAVQQFPQMTVSSLQCNRHKPWRFGTRFMSLIKEAHWEGLTGRITFNKTNGLRTDFDLDVISLKEEGLEKIGTWDPASGLNMTESQKGKPANITDSLSNRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDANGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEESKEASALGVQNIGGIFIVLAAGLVLSVFVAVGEFLYKSKKNAQLEKRSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKETMA	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 451).	0	TC=1.A.10	.	glutamate-gated ion channel (TC 1.A.10.1) family. GRIK2 subfamily. 	.	.	Receptor family ligand binding region; Ligand-gated ion channel; Ligated ion channel L-glutamate- and glycine-binding site	PF01094; PF00060; PF10613	PF01094; ANF_receptor; PF00060; Lig_chan; PF10613; Lig_chan-Glu_bd	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04724: Glutamatergic synapse	R-HSA-451307: Activation of Na-permeable kainate receptors; R-HSA-451308: Activation of Ca-permeable Kainate Receptor	.	Q13002
TTNP6O2	Glutamate receptor ionotropic kainate 3 (GluK3)	Q13003	GRIK3_HUMAN	.	"Glutamate receptor ionotropic, kainate 3; Glutamate receptor 7; GluR7; GluR-7; GluK3; Excitatory amino acid receptor 5; EAA5"	GRIK3	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.	.	.	MTAPWRRLRSLVWEYWAGLLVCAFWIPDSRGMPHVIRIGGIFEYADGPNAQVMNAEEHAFRFSANIINRNRTLLPNTTLTYDIQRIHFHDSFEATKKACDQLALGVVAIFGPSQGSCTNAVQSICNALEVPHIQLRWKHHPLDNKDTFYVNLYPDYASLSHAILDLVQYLKWRSATVVYDDSTGLIRLQELIMAPSRYNIRLKIRQLPIDSDDSRPLLKEMKRGREFRIIFDCSHTMAAQILKQAMAMGMMTEYYHFIFTTLDLYALDLEPYRYSGVNLTGFRILNVDNPHVSAIVEKWSMERLQAAPRSESGLLDGVMMTDAALLYDAVHIVSVCYQRAPQMTVNSLQCHRHKAWRFGGRFMNFIKEAQWEGLTGRIVFNKTSGLRTDFDLDIISLKEDGLEKVGVWSPADGLNITEVAKGRGPNVTDSLTNRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKGQWNGMVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEWYDAHPCNPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMSSKPSALVKNNEEGIQRALTADYALLMESTTIEYVTQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWWRGSGCPEEENKEASALGIQKIGGIFIVLAAGLVLSVLVAVGEFVYKLRKTAEREQRSFCSTVADEIRFSLTCQRRVKHKPQPPMMVKTDAVINMHTFNDRRLPGKDSMACSTSLAPVFP	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 452).	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04724: Glutamatergic synapse	R-HSA-451308: Activation of Ca-permeable Kainate Receptor; R-HSA-500657: Presynaptic function of Kainate receptors	.	Q13003
TTQV6BO	Glutamate receptor ionotropic kainate 4 (GluK4)	Q16099	GRIK4_HUMAN	.	"KA1; Glutamate receptor ionotropic, kainate 4; Glutamate receptor KA-1; GluK4; GRIK; Excitatory amino acid receptor 1; EAA1"	GRIK4	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.	.	.	MPRVSAPLVLLPAWLVMVACSPHSLRIAAILDDPMECSRGERLSITLAKNRINRAPERLGKAKVEVDIFELLRDSEYETAETMCQILPKGVVAVLGPSSSPASSSIISNICGEKEVPHFKVAPEEFVKFQFQRFTTLNLHPSNTDISVAVAGILNFFNCTTACLICAKAECLLNLEKLLRQFLISKDTLSVRMLDDTRDPTPLLKEIRDDKTATIIIHANASMSHTILLKAAELGMVSAYYTYIFTNLEFSLQRMDSLVDDRVNILGFSIFNQSHAFFQEFAQSLNQSWQENCDHVPFTGPALSSALLFDAVYAVVTAVQELNRSQEIGVKPLSCGSAQIWQHGTSLMNYLRMVELEGLTGHIEFNSKGQRSNYALKILQFTRNGFRQIGQWHVAEGLSMDSHLYASNISDTLFNTTLVVTTILENPYLMLKGNHQEMEGNDRYEGFCVDMLKELAEILRFNYKIRLVGDGVYGVPEANGTWTGMVGELIARKADLAVAGLTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVARLTPYEWYSPHPCAQGRCNLLVNQYSLGNSLWFPVGGFMQQGSTIAPRALSTRCVSGVWWAFTLIIISSYTANLAAFLTVQRMDVPIESVDDLADQTAIEYGTIHGGSSMTFFQNSRYQTYQRMWNYMYSKQPSVFVKSTEEGIARVLNSNYAFLLESTMNEYYRQRNCNLTQIGGLLDTKGYGIGMPVGSVFRDEFDLAILQLQENNRLEILKRKWWEGGKCPKEEDHRAKGLGMENIGGIFVVLICGLIVAIFMAMLEFLWTLRHSEATEVSVCQEMVTELRSIILCQDSIHPRRRRAAVPPPRPPIPEERRPRGTATLSNGKLCGAGEPDQLAQRLAQEAALVARGCTHIRVCPECRRFQGLRARPSPARSEESLEWEKTTNSSEPE	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 453).	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04724: Glutamatergic synapse	R-HSA-451308: Activation of Ca-permeable Kainate Receptor	.	Q16099
TTO6LI7	Glutamate receptor ionotropic kainate 5 (GRIK5)	Q16478	GRIK5_HUMAN	Glutamate-gated ion channel	"KA2; Glutamate receptor ionotropic, kainate 5; Glutamate receptor KA-2; GluK5; GRIK2; Excitatory amino acid receptor 2; EAA2"	GRIK5	"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."	.	.	MPAELLLLLIVAFASPSCQVLSSLRMAAILDDQTVCGRGERLALALAREQINGIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSPASASTVSHICGEKEIPHIKVGPEETPRLQYLRFASVSLYPSNEDVSLAVSRILKSFNYPSASLICAKAECLLRLEELVRGFLISKETLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLILRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSSNILGFSMFNTSHPFYPEFVRSLNMSWRENCEASTYLGPALSAALMFDAVHVVVSAVRELNRSQEIGVKPLACTSANIWPHGTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWYSNRTLAMNATTLDINLSQTLANKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPAVWLFMLLAYLAVSCVLFLAARLSPYEWYNPHPCLRARPHILENQYTLGNSLWFPVGGFMQQGSEIMPRALSTRCVSGVWWAFTLIIISSYTANLAAFLTVQRMEVPVESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWEGGRCPKEEDHRAKGLGMENIGGIFIVLICGLIIAVFVAVMEFIWSTRRSAESEEVSVCQEMLQELRHAVSCRKTSRSRRRRRPGGPSRALLSLRAVREMRLSNGKLYSAGAGGDAGSAHGGPQRLLDDPGPPSGARPAAPTPCTHVRVCQECRRIQALRASGAGAPPRGLGVPAEATSPPRPRPGPAGPRELAEHE	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 454).	0	TC=1.A.10	.	glutamate-gated ion channel (TC 1.A.10.1) family. GRIK5 subfamily. 	.	.	Receptor family ligand binding region; Ligand-gated ion channel; Ligated ion channel L-glutamate- and glycine-binding site	PF01094; PF00060; PF10613	PF01094; ANF_receptor; PF00060; Lig_chan; PF10613; Lig_chan-Glu_bd	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04724: Glutamatergic synapse	R-HSA-451308: Activation of Ca-permeable Kainate Receptor	.	Q16478
TTLD29N	Glutamate receptor ionotropic NMDA 1 (NMDAR1)	Q05586	NMDZ1_HUMAN	Glutamate-gated ion channel	"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"	GRIN1	"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."	.	6IRH; 6IRG; 6IRF; 6IRA; 5TPA	MSTMRLLTLALLFSCSVARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGILGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDTSTGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES	Successful	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	34	TC=1.A.10	.	glutamate-gated ion channel (TC 1.A.10.1) family. NR1/GRIN1 subfamily. 	.	.	Receptor family ligand binding region; Calmodulin-binding domain C0 of NMDA receptor NR1 subunit; Ligand-gated ion channel; Ligated ion channel L-glutamate- and glycine-binding site	PF01094; PF10562; PF00060; PF10613	PF01094; ANF_receptor; PF10562; CaM_bdg_C0; PF00060; Lig_chan; PF10613; Lig_chan-Glu_bd	1.A.10.1.20	The Glutamate-gated Ion Channel (GIC) Family of Neurotransmitter Receptors	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	"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"	.	Q05586
TTKJEMQ	Glutamate receptor ionotropic NMDA 2A (NMDAR2A)	Q12879	NMDE1_HUMAN	Glutamate-gated ion channel	"NR2A; NMDA receptor NR2A; N-methyl D-aspartate receptor subtype 2A; HNR2A; Glutamate receptor ionotropic, NMDA 2A; Glutamate [NMDA] receptor subunit epsilon-1; GluN2A"	GRIN2A	"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."	.	6IRH; 6IRG; 6IRF; 6IRA; 5TPA	MGRVGYWTLLVLPALLVWRGPAPSAAAEKGPPALNIAVMLGHSHDVTERELRTLWGPEQAAGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLVFGDDTDQEAVAQMLDFISSHTFVPILGIHGGASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDYDWHVFSLVTTIFPGYREFISFVKTTVDNSFVGWDMQNVITLDTSFEDAKTQVQLKKIHSSVILLYCSKDEAVLILSEARSLGLTGYDFFWIVPSLVSGNTELIPKEFPSGLISVSYDDWDYSLEARVRDGIGILTTAASSMLEKFSYIPEAKASCYGQMERPEVPMHTLHPFMVNVTWDGKDLSFTEEGYQVHPRLVVIVLNKDREWEKVGKWENHTLSLRHAVWPRYKSFSDCEPDDNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNSTNEGMNVKKCCKGFCIDILKKLSRTVKFTYDLYLVTNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNGTVSPSAFLEPFSASVWVMMFVMLLIVSAIAVFVFEYFSPVGYNRNLAKGKAPHGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEFVDQVTGLSDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGICHNEKNEVMSSQLDIDNMAGVFYMLAAAMALSLITFIWEHLFYWKLRFCFTGVCSDRPGLLFSISRGIYSCIHGVHIEEKKKSPDFNLTGSQSNMLKLLRSAKNISSMSNMNSSRMDSPKRAADFIQRGSLIMDMVSDKGNLMYSDNRSFQGKESIFGDNMNELQTFVANRQKDNLNNYVFQGQHPLTLNESNPNTVEVAVSTESKANSRPRQLWKKSVDSIRQDSLSQNPVSQRDEATAENRTHSLKSPRYLPEEMAHSDISETSNRATCHREPDNSKNHKTKDNFKRSVASKYPKDCSEVERTYLKTKSSSPRDKIYTIDGEKEPGFHLDPPQFVENVTLPENVDFPDPYQDPSENFRKGDSTLPMNRNPLHNEEGLSNNDQYKLYSKHFTLKDKGSPHSETSERYRQNSTHCRSCLSNMPTYSGHFTMRSPFKCDACLRMGNLYDIDEDQMLQETGNPATGEQVYQQDWAQNNALQLQKNKLRISRQHSYDNIVDKPRELDLSRPSRSISLKDRERLLEGNFYGSLFSVPSSKLSGKKSSLFPQGLEDSKRSKSLLPDHTSDNPFLHSHRDDQRLVIGRCPSDPYKHSLPSQAVNDSYLRSSLRSTASYCSRDSRGHNDVYISEHVMPYAANKNNMYSTPRVLNSCSNRRVYKKMPSIESDV	Successful	Glycine transport inhibitors for the treatment of schizophrenia: Symptom and disease modification. Curr Opin Drug Discov Devel. 2009 Jul;12(4):468-78.	34	TC=1.A.10	Glutamate gated ion channel	glutamate-gated ion channel (TC 1.A.10.1) family. NR2A/GRIN2A subfamily. 	.	.	Receptor family ligand binding region; Ligand-gated ion channel; Ligated ion channel L-glutamate- and glycine-binding site; N-methyl D-aspartate receptor 2B3 C-terminus	PF01094; PF00060; PF10613; PF10565	PF01094; ANF_receptor; PF00060; Lig_chan; PF10613; Lig_chan-Glu_bd; PF10565; NMDAR2_C	1.A.10.1.20	The Glutamate-gated Ion Channel (GIC) Family of Neurotransmitter Receptors	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	"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"	.	Q12879
TTN9D8E	Glutamate receptor ionotropic NMDA 2B (NMDAR2B)	Q13224	NMDE2_HUMAN	Glutamate-gated ion channel	"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"	GRIN2B	"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."	.	5EWM; 5EWL; 5EWJ; 2IPV; 1S2S	MKPRAECCSPKFWLVLAVLAVSGSRARSQKSPPSIGIAVILVGTSDEVAIKDAHEKDDFHHLSVVPRVELVAMNETDPKSIITRICDLMSDRKIQGVVFADDTDQEAIAQILDFISAQTLTPILGIHGGSSMIMADKDESSMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFVNKIRSTIENSFVGWELEEVLLLDMSLDDGDSKIQNQLKKLQSPIILLYCTKEEATYIFEVANSVGLTGYGYTWIVPSLVAGDTDTVPAEFPTGLISVSYDEWDYGLPARVRDGIAIITTAASDMLSEHSFIPEPKSSCYNTHEKRIYQSNMLNRYLINVTFEGRNLSFSEDGYQMHPKLVIILLNKERKWERVGKWKDKSLQMKYYVWPRMCPETEEQEDDHLSIVTLEEAPFVIVESVDPLSGTCMRNTVPCQKRIVTENKTDEEPGYIKKCCKGFCIDILKKISKSVKFTYDLYLVTNGKHGKKINGTWNGMIGEVVMKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSRSNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYVDQVSGLSDKKFQRPNDFSPPFRFGTVPNGSTERNIRNNYAEMHAYMGKFNQRGVDDALLSLKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLGAAMALSLITFICEHLFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSVMNSPTATMNNTHSNILRLLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSYNNPPCEENLFSDYISEVERTFGNLQLKDSNVYQDHYHHHHRPHSIGSASSIDGLYDCDNPPFTTQSRSISKKPLDIGLPSSKHSQLSDLYGKFSFKSDRYSGHDDLIRSDVSDISTHTVTYGNIEGNAAKRRKQQYKDSLKKRPASAKSRREFDEIELAYRRRPPRSPDHKRYFRDKEGLRDFYLDQFRTKENSPHWEHVDLTDIYKERSDDFKRDSVSGGGPCTNRSHIKHGTGDKHGVVSGVPAPWEKNLTNVEWEDRSGGNFCRSCPSKLHNYSTTVTGQNSGRQACIRCEACKKAGNLYDISEDNSLQELDQPAAPVAVTSNASTTKYPQSPTNSKAQKKNRNKLRRQHSYDTFVDLQKEEAALAPRSVSLKDKGRFMDGSPYAHMFEMSAGESTFANNKSSVPTAGHHHHNNPGGGYMLSKSLYPDRVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVAGASKARPDFRALVTNKPVVSALHGAVPARFQKDICIGNQSNPCVPNNKNPRAFNGSSNGHVYEKLSSIESDV	Successful	NMDA receptor stimulation induces reversible fission of the neuronal endoplasmic reticulum. PLoS One. 2009;4(4):e5250.	34	TC=1.A.10	Glutamate gated ion channel	glutamate-gated ion channel (TC 1.A.10.1) family. NR2B/GRIN2B subfamily. 	.	.	Receptor family ligand binding region; Ligand-gated ion channel; Ligated ion channel L-glutamate- and glycine-binding site; N-methyl D-aspartate receptor 2B3 C-terminus	PF01094; PF00060; PF10613; PF10565	PF01094; ANF_receptor; PF00060; Lig_chan; PF10613; Lig_chan-Glu_bd; PF10565; NMDAR2_C	.	.	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	"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"	.	Q13224
TT1M8OW	Glutamate receptor ionotropic NMDA 2C (GluN2C)	Q14957	NMDE3_HUMAN	.	"NR2C; NMDAR2C; N-methyl D-aspartate receptor subtype 2C; Glutamate receptor ionotropic, NMDA 2C; Glutamate [NMDA] receptor subunit epsilon-3; GluN2C"	GRIN2C	"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)."	.	.	MGGALGPALLLTSLFGAWAGLGPGQGEQGMTVAVVFSSSGPPQAQFRARLTPQSFLDLPLEIQPLTVGVNTTNPSSLLTQICGLLGAAHVHGIVFEDNVDTEAVAQILDFISSQTHVPILSISGGSAVVLTPKEPGSAFLQLGVSLEQQLQVLFKVLEEYDWSAFAVITSLHPGHALFLEGVRAVADASHVSWRLLDVVTLELGPGGPRARTQRLLRQLDAPVFVAYCSREEAEVLFAEAAQAGLVGPGHVWLVPNLALGSTDAPPATFPVGLISVVTESWRLSLRQKVRDGVAILALGAHSYWRQHGTLPAPAGDCRVHPGPVSPAREAFYRHLLNVTWEGRDFSFSPGGYLVQPTMVVIALNRHRLWEMVGRWEHGVLYMKYPVWPRYSASLQPVVDSRHLTVATLEERPFVIVESPDPGTGGCVPNTVPCRRQSNHTFSSGDVAPYTKLCCKGFCIDILKKLARVVKFSYDLYLVTNGKHGKRVRGVWNGMIGEVYYKRADMAIGSLTINEERSEIVDFSVPFVETGISVMVARSNGTVSPSAFLEPYSPAVWVMMFVMCLTVVAITVFMFEYFSPVSYNQNLTRGKKSGGPAFTIGKSVWLLWALVFNNSVPIENPRGTTSKIMVLVWAFFAVIFLASYTANLAAFMIQEQYIDTVSGLSDKKFQRPQDQYPPFRFGTVPNGSTERNIRSNYRDMHTHMVKFNQRSVEDALTSLKMGKLDAFIYDAAVLNYMAGKDEGCKLVTIGSGKVFATTGYGIAMQKDSHWKRAIDLALLQFLGDGETQKLETVWLSGICQNEKNEVMSSKLDIDNMAGVFYMLLVAMGLALLVFAWEHLVYWKLRHSVPNSSQLDFLLAFSRGIYSCFSGVQSLASPPRQASPDLTASSAQASVLKMLQAARDMVTTAGVSSSLDRATRTIENWGGGRRAPPPSPCPTPRSGPSPCLPTPDPPPEPSPTGWGPPDGGRAALVRRAPQPPGRPPTPGPPLSDVSRVSRRPAWEARWPVRTGHCGRHLSASERPLSPARCHYSSFPRADRSGRPFLPLFPELEDLPLLGPEQLARREALLHAAWARGSRPRHASLPSSVAEAFARPSSLPAGCTGPACARPDGHSACRRLAQAQSMCLPIYREACQEGEQAGAPAWQHRQHVCLHAHAHLPFCWGAVCPHLPPCASHGSWLSGAWGPLGHRGRTLGLGTGYRDSGGLDEISRVARGTQGFPGPCTWRRISSLESEV	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 458).	2	.	.	.	.	.	.	.	.	.	.	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 disease; hsa05014: Amyotrophic lateral sclerosis; hsa05017: Spinocerebellar ataxia; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05030: Cocaine addiction; hsa05031: Amphetamine addiction; hsa05033: Nicotine addiction; hsa05034: Alcoholism	"R-HSA-438066: Unblocking of NMDA receptors, glutamate binding and activation; R-HSA-6794361: Neurexins and neuroligins; R-HSA-8849932: Synaptic adhesion-like molecules; R-HSA-9609736: Assembly and cell surface presentation of NMDA receptors; R-HSA-9617324: Negative regulation of NMDA receptor-mediated neuronal transmission; R-HSA-9620244: Long-term potentiation"	.	Q14957
TT5POTG	Glutamate receptor ionotropic NMDA 2D (GluN2D)	O15399	NMDE4_HUMAN	.	"NR2D; NMDAR2D; N-methyl D-aspartate receptor subtype 2D; Glutamate receptor ionotropic, NMDA 2D; Glutamate [NMDA] receptor subunit epsilon-4; GluN2D; EB11"	GRIN2D	"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."	.	.	MRGAGGPRGPRGPAKMLLLLALACASPFPEEAPGPGGAGGPGGGLGGARPLNVALVFSGPAYAAEAARLGPAVAAAVRSPGLDVRPVALVLNGSDPRSLVLQLCDLLSGLRVHGVVFEDDSRAPAVAPILDFLSAQTSLPIVAVHGGAALVLTPKEKGSTFLQLGSSTEQQLQVIFEVLEEYDWTSFVAVTTRAPGHRAFLSYIEVLTDGSLVGWEHRGALTLDPGAGEAVLSAQLRSVSAQIRLLFCAREEAEPVFRAAEEAGLTGSGYVWFMVGPQLAGGGGSGAPGEPPLLPGGAPLPAGLFAVRSAGWRDDLARRVAAGVAVVARGAQALLRDYGFLPELGHDCRAQNRTHRGESLHRYFMNITWDNRDYSFNEDGFLVNPSLVVISLTRDRTWEVVGSWEQQTLRLKYPLWSRYGRFLQPVDDTQHLTVATLEERPFVIVEPADPISGTCIRDSVPCRSQLNRTHSPPPDAPRPEKRCCKGFCIDILKRLAHTIGFSYDLYLVTNGKHGKKIDGVWNGMIGEVFYQRADMAIGSLTINEERSEIVDFSVPFVETGISVMVARSNGTVSPSAFLEPYSPAVWVMMFVMCLTVVAVTVFIFEYLSPVGYNRSLATGKRPGGSTFTIGKSIWLLWALVFNNSVPVENPRGTTSKIMVLVWAFFAVIFLASYTANLAAFMIQEEYVDTVSGLSDRKFQRPQEQYPPLKFGTVPNGSTEKNIRSNYPDMHSYMVRYNQPRVEEALTQLKAGKLDAFIYDAAVLNYMARKDEGCKLVTIGSGKVFATTGYGIALHKGSRWKRPIDLALLQFLGDDEIEMLERLWLSGICHNDKIEVMSSKLDIDNMAGVFYMLLVAMGLSLLVFAWEHLVYWRLRHCLGPTHRMDFLLAFSRGMYSCCSAEAAPPPAKPPPPPQPLPSPAYPAPRPAPGPAPFVPRERASVDRWRRTKGAGPPGGAGLADGFHRYYGPIEPQGLGLGLGEARAAPRGAAGRPLSPPAAQPPQKPPPSYFAIVRDKEPAEPPAGAFPGFPSPPAPPAAAATAVGPPLCRLAFEDESPPAPARWPRSDPESQPLLGPGAGGAGGTGGAGGGAPAAPPPCRAAPPPCPYLDLEPSPSDSEDSESLGGASLGGLEPWWFADFPYPYAERLGPPPGRYWSVDKLGGWRAGSWDYLPPRSGPAAWHCRHCASLELLPPPRHLSCSHDGLDGGWWAPPPPPWAAGPLPRRRARCGCPRSHPHRPRASHRTPAAAAPHHHRHRRAAGGWDLPPPAPTSRSLEDLSSCPRAAPARRLTGPSRHARRCPHAAHWGPPLPTASHRRHRGGDLGTRRGSAHFSSLESEV	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 459).	2	.	.	.	.	.	.	.	.	.	.	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 disease; hsa05014: Amyotrophic lateral sclerosis; hsa05017: Spinocerebellar ataxia; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05030: Cocaine addiction; hsa05031: Amphetamine addiction; hsa05033: Nicotine addiction; hsa05034: Alcoholism	"R-HSA-438066: Unblocking of NMDA receptors, glutamate binding and activation; R-HSA-442982: Ras activation upon Ca2+ influx through NMDA receptor; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6794361: Neurexins and neuroligins; R-HSA-8849932: Synaptic adhesion-like molecules; R-HSA-9609736: Assembly and cell surface presentation of NMDA receptors; R-HSA-9617324: Negative regulation of NMDA receptor-mediated neuronal transmission; R-HSA-9620244: Long-term potentiation"	.	O15399
TTAZ3MN	Beta-adrenergic receptor kinase 1 (ADRBK1)	P25098	ARBK1_HUMAN	Kinase	GRK2; G-protein coupled receptor kinase 2; BetaARK1; Beta-ARK-1; Beta ARK1	GRK2	"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."	EC 2.7.11.15	6C2Y; 5WG5; 5WG4; 5WG3; 5UVC	MADLEAVLADVSYLMAMEKSKATPAARASKKILLPEPSIRSVMQKYLEDRGEVTFEKIFSQKLGYLLFRDFCLNHLEEARPLVEFYEEIKKYEKLETEEERVARSREIFDSYIMKELLACSHPFSKSATEHVQGHLGKKQVPPDLFQPYIEEICQNLRGDVFQKFIESDKFTRFCQWKNVELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSEADMRFYAAEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRLGCLGRGAQEVKESPFFRSLDWQMVFLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDSDQELYRNFPLTISERWQQEVAETVFDTINAETDRLEARKKAKNKQLGHEEDYALGKDCIMHGYMSKMGNPFLTQWQRRYFYLFPNRLEWRGEGEAPQSLLTMEEIQSVEETQIKERKCLLLKIRGGKQFILQCDSDPELVQWKKELRDAYREAQQLVQRVPKMKNKPRSPVVELSKVPLVQRGSANGL	Patented-recorded	Molecular mechanism of selectivity among G protein-coupled receptor kinase 2 inhibitors. Mol Pharmacol. 2011 Aug;80(2):294-303.	0	.	.	.	.	.	.	.	.	.	.	hsa04062:Chemokine signaling pathway; hsa04144:Endocytosis; hsa04724:Glutamatergic synapse; hsa05032:Morphine addiction	R-HSA-111933:Calmodulin induced events; R-HSA-416476:G alpha (q) signalling events; R-HSA-5635838:Activation of SMO	.	P25098
TT5A4DX	Beta-adrenergic receptor kinase 2 (ADRBK2)	P35626	ARBK2_HUMAN	.	G-protein-coupled receptor kinase 3; Beta-ARK-2; BARK2; ADRBK2	GRK3	Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors.	EC 2.7.11.15	.	MADLEAVLADVSYLMAMEKSKATPAARASKRIVLPEPSIRSVMQKYLAERNEITFDKIFNQKIGFLLFKDFCLNEINEAVPQVKFYEEIKEYEKLDNEEDRLCRSRQIYDAYIMKELLSCSHPFSKQAVEHVQSHLSKKQVTSTLFQPYIEEICESLRGDIFQKFMESDKFTRFCQWKNVELNIHLTMNEFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHARISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDTFSPELKSLLEGLLQRDVSKRLGCHGGGSQEVKEHSFFKGVDWQHVYLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDCDQELYKNFPLVISERWQQEVTETVYEAVNADTDKIEARKRAKNKQLGHEEDYALGKDCIMHGYMLKLGNPFLTQWQRRYFYLFPNRLEWRGEGESRQNLLTMEQILSVEETQIKDKKCILFRIKGGKQFVLQCESDPEFVQWKKELNETFKEAQRLLRRAPKFLNKPRSGTVELPKPSLCHRNSNGL	Literature-reported	Molecular mechanism of selectivity among G protein-coupled receptor kinase 2 inhibitors. Mol Pharmacol. 2011 Aug;80(2):294-303.	0	.	.	.	.	.	.	.	.	.	.	hsa04062: Chemokine signaling pathway; hsa04144: Endocytosis; hsa04340: Hedgehog signaling pathway; hsa04724: Glutamatergic synapse; hsa04740: Olfactory transduction; hsa05032: Morphine addiction	R-HSA-418555: G alpha (s) signalling events; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis	.	P35626
TTTCXO0	G protein-coupled receptor kinase 5 (GRK5)	P34947	GRK5_HUMAN	.	GPRK5; G protein-coupled receptor kinase GRK5	GRK5	"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)."	EC 2.7.11.16	4TND; 4TNB	MELENIVANTVLLKAREGGGGKRKGKSKKWKEILKFPHISQCEDLRRTIDRDYCSLCDKQPIGRLLFRQFCETRPGLECYIQFLDSVAEYEVTPDEKLGEKGKEIMTKYLTPKSPVFIAQVGQDLVSQTEEKLLQKPCKELFSACAQSVHEYLRGEPFHEYLDSMFFDRFLQWKWLERQPVTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGDLIRGRVGTVGYMAPEVLNNQRYGLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSHKFSEEAKSICKMLLTKDAKQRLGCQEEGAAEVKRHPFFRNMNFKRLEAGMLDPPFVPDPRAVYCKDVLDIEQFSTVKGVNLDHTDDDFYSKFSTGSVSIPWQNEMIETECFKELNVFGPNGTLPPDLNRNHPPEPPKKGLLQRLFKRQHQNNSKSSPSSKTSFNHHINSNHVSSNSTGSS	Patented-recorded	Design and synthesis of novel 3-(benzo[d]oxazol-2-yl)-5-(1-(piperidin-4-yl)-1H-pyrazol-4-yl)pyridin-2-amine derivatives as selective G-protein-coupled receptor kinase-2 and -5 inhibitors. Bioorg Med Chem Lett. 2013 Dec 15;23(24):6711-6.	0	.	.	.	.	.	.	.	.	.	.	hsa04062: Chemokine signaling pathway; hsa04144: Endocytosis; hsa05032: Morphine addiction	R-HSA-416476: G alpha (q) signalling events; R-HSA-418555: G alpha (s) signalling events	.	P34947
TTVBPDM	Metabotropic glutamate receptor 1 (mGluR1)	Q13255	GRM1_HUMAN	GPCR glutamate	mGLUR1; Glutamate receptor mGLU1; GPRC1A	GRM1	"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."	.	4OR2; 3KS9	MVGLLLFFFPAIFLEVSLLPRSPGRKVLLAGASSQRSVARMDGDVIIGALFSVHHQPPAEKVPERKCGEIREQYGIQRVEAMFHTLDKINADPVLLPNITLGSEIRDSCWHSSVALEQSIEFIRDSLISIRDEKDGINRCLPDGQSLPPGRTKKPIAGVIGPGSSSVAIQVQNLLQLFDIPQIAYSATSIDLSDKTLYKYFLRVVPSDTLQARAMLDIVKRYNWTYVSAVHTEGNYGESGMDAFKELAAQEGLCIAHSDKIYSNAGEKSFDRLLRKLRERLPKARVVVCFCEGMTVRGLLSAMRRLGVVGEFSLIGSDGWADRDEVIEGYEVEANGGITIKLQSPEVRSFDDYFLKLRLDTNTRNPWFPEFWQHRFQCRLPGHLLENPNFKRICTGNESLEENYVQDSKMGFVINAIYAMAHGLQNMHHALCPGHVGLCDAMKPIDGSKLLDFLIKSSFIGVSGEEVWFDEKGDAPGRYDIMNLQYTEANRYDYVHVGTWHEGVLNIDDYKIQMNKSGVVRSVCSEPCLKGQIKVIRKGEVSCCWICTACKENEYVQDEFTCKACDLGWWPNADLTGCEPIPVRYLEWSNIESIIAIAFSCLGILVTLFVTLIFVLYRDTPVVKSSSRELCYIILAGIFLGYVCPFTLIAKPTTTSCYLQRLLVGLSSAMCYSALVTKTNRIARILAGSKKKICTRKPRFMSAWAQVIIASILISVQLTLVVTLIIMEPPMPILSYPSIKEVYLICNTSNLGVVAPLGYNGLLIMSCTYYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITTCFAVSLSVTVALGCMFTPKMYIIIAKPERNVRSAFTTSDVVRMHVGDGKLPCRSNTFLNIFRRKKAGAGNANSNGKSVSWSEPGGGQVPKGQHMWHRLSVHVKTNETACNQTAVIKPLTKSYQGSGKSLTFSDTSTKTLYNVEEEEDAQPIRFSPPGSPSMVVHRRVPSAATTPPLPSHLTAEETPLFLAEPALPKGLPPPLQQQQQPPPQQKSLMDQLQGVVSNFSTAIPDFHAVLAGPGGPGNGLRSLYPPPPPPQHLQMLPLQLSTFGEELVSPPADDDDDSERFKLLQEYVYEHEREGNTEEDELEEEEEDLQAASKLTPDDSPALTPPSPFRDSVASGSSVPSSPVSESVLCTPPNVSYASVILRDYKQSSSTL	Discontinued	Comparison of the mGluR1 antagonist A-841720 in rat models of pain and cognition. Behav Pharmacol. 2007 Jul;18(4):273-81.	9	PF00003	GPCR glutamate	G-protein coupled receptor 3 family.	.	.	7 transmembrane sweet-taste receptor of 3 GCPR; Receptor family ligand binding region; Homer-binding domain of metabotropic glutamate receptor ; Nine Cysteines Domain of family 3 GPCR	PF00003; PF01094; PF10606; PF07562	PF00003; 7tm_3; PF01094; ANF_receptor; PF10606; GluR_Homer-bdg; PF07562; NCD3G	9.A.14.7.1	The G-protein-coupled receptor (GPCR) Family	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	R-HSA-416476:G alpha (q) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors)	.	Q13255
TTXJ47W	Metabotropic glutamate receptor 2 (mGluR2)	Q14416	GRM2_HUMAN	GPCR glutamate	mGLUR2; Group II metabotropic glutamate receptor; Glutamate receptor mGLU2; GPRC1B	GRM2	"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."	.	5KZQ; 5KZN; 5CNJ; 5CNI; 4XAS	MGSLLALLALLLLWGAVAEGPAKKVLTLEGDLVLGGLFPVHQKGGPAEDCGPVNEHRGIQRLEAMLFALDRINRDPHLLPGVRLGAHILDSCSKDTHALEQALDFVRASLSRGADGSRHICPDGSYATHGDAPTAITGVIGGSYSDVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFFQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFELEARARNICVATSEKVGRAMSRAAFEGVVRALLQKPSARVAVLFTRSEDARELLAASQRLNASFTWVASDGWGALESVVAGSEGAAEGAITIELASYPISDFASYFQSLDPWNNSRNPWFREFWEQRFRCSFRQRDCAAHSLRAVPFEQESKIMFVVNAVYAMAHALHNMHRALCPNTTRLCDAMRPVNGRRLYKDFVLNVKFDAPFRPADTHNEVRFDRFGDGIGRYNIFTYLRAGSGRYRYQKVGYWAEGLTLDTSLIPWASPSAGPLPASRCSEPCLQNEVKSVQPGEVCCWLCIPCQPYEYRLDEFTCADCGLGYWPNASLTGCFELPQEYIRWGDAWAVGPVTIACLGALATLFVLGVFVRHNATPVVKASGRELCYILLGGVFLCYCMTFIFIAKPSTAVCTLRRLGLGTAFSVCYSALLTKTNRIARIFGGAREGAQRPRFISPASQVAICLALISGQLLIVVAWLVVEAPGTGKETAPERREVVTLRCNHRDASMLGSLAYNVLLIALCTLYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCVSVSLSGSVVLGCLFAPKLHIILFQPQKNVVSHRAPTSRFGSAAARASSSLGQGSGSQFVPTVCNGREVVDSTTSSL	Clinical trial	"LY-2140023, a prodrug of the group II metabotropic glutamate receptor agonist LY-404039 for the potential treatment of schizophrenia. Curr Opin Investig Drugs. 2010 Jul;11(7):833-45."	25	PF00003	GPCR glutamate	G-protein coupled receptor 3 family.	.	.	7 transmembrane sweet-taste receptor of 3 GCPR; Receptor family ligand binding region; Nine Cysteines Domain of family 3 GPCR	PF00003; PF01094; PF07562	PF00003; 7tm_3; PF01094; ANF_receptor; PF07562; NCD3G	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04724:Glutamatergic synapse; hsa05030:Cocaine addiction	R-HSA-418594:G alpha (i) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors)	.	Q14416
TT8A9EF	Metabotropic glutamate receptor 3 (mGluR3)	Q14832	GRM3_HUMAN	GPCR glutamate	mGLUR3; Group III metabotropic glutamate receptor; GPRC1C	GRM3	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.	.	6B7H; 5CNM; 5CNK; 4XAR; 3SM9	MKMLTRLQVLTLALFSKGFLLSLGDHNFLRREIKIEGDLVLGGLFPINEKGTGTEECGRINEDRGIQRLEAMLFAIDEINKDDYLLPGVKLGVHILDTCSRDTYALEQSLEFVRASLTKVDEAEYMCPDGSYAIQENIPLLIAGVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRNICIATAEKVGRSNIRKSYDSVIRELLQKPNARVVVLFMRSDDSRELIAAASRANASFTWVASDGWGAQESIIKGSEHVAYGAITLELASQPVRQFDRYFQSLNPYNNHRNPWFRDFWEQKFQCSLQNKRNHRRVCDKHLAIDSSNYEQESKIMFVVNAVYAMAHALHKMQRTLCPNTTKLCDAMKILDGKKLYKDYLLKINFTAPFNPNKDADSIVKFDTFGDGMGRYNVFNFQNVGGKYSYLKVGHWAETLSLDVNSIHWSRNSVPTSQCSDPCAPNEMKNMQPGDVCCWICIPCEPYEYLADEFTCMDCGSGQWPTADLTGCYDLPEDYIRWEDAWAIGPVTIACLGFMCTCMVVTVFIKHNNTPLVKASGRELCYILLFGVGLSYCMTFFFIAKPSPVICALRRLGLGSSFAICYSALLTKTNCIARIFDGVKNGAQRPKFISPSSQVFICLGLILVQIVMVSVWLILEAPGTRRYTLAEKRETVILKCNVKDSSMLISLTYDVILVILCTVYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCISVSLSGFVVLGCLFAPKVHIILFQPQKNVVTHRLHLNRFSVSGTGTTYSQSSASTYVPTVCNGREVLDSTTSSL	Clinical trial	Positive allosteric modulators of the metabotropic glutamate receptor 2 for the treatment of schizophrenia. Expert Opin Ther Pat. 2009 Sep;19(9):1259-75.	25	PF00003	GPCR glutamate	G-protein coupled receptor 3 family.	.	.	7 transmembrane sweet-taste receptor of 3 GCPR; Receptor family ligand binding region; Nine Cysteines Domain of family 3 GPCR	PF00003; PF01094; PF07562	PF00003; 7tm_3; PF01094; ANF_receptor; PF07562; NCD3G	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04724:Glutamatergic synapse; hsa05030:Cocaine addiction	R-HSA-418594:G alpha (i) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors)	.	Q14832
TTICZ1O	Metabotropic glutamate receptor 4 (mGluR4)	Q14833	GRM4_HUMAN	GPCR glutamate	mGluR4; Group III metabotropic glutamate receptor 4; GPRC1D	GRM4	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.	.	.	MPGKRGLGWWWARLPLCLLLSLYGPWMPSSLGKPKGHPHMNSIRIDGDITLGGLFPVHGRGSEGKPCGELKKEKGIHRLEAMLFALDRINNDPDLLPNITLGARILDTCSRDTHALEQSLTFVQALIEKDGTEVRCGSGGPPIITKPERVVGVIGASGSSVSIMVANILRLFKIPQISYASTAPDLSDNSRYDFFSRVVPSDTYQAQAMVDIVRALKWNYVSTVASEGSYGESGVEAFIQKSREDGGVCIAQSVKIPREPKAGEFDKIIRRLLETSNARAVIIFANEDDIRRVLEAARRANQTGHFFWMGSDSWGSKIAPVLHLEEVAEGAVTILPKRMSVRGFDRYFSSRTLDNNRRNIWFAEFWEDNFHCKLSRHALKKGSHVKKCTNRERIGQDSAYEQEGKVQFVIDAVYAMGHALHAMHRDLCPGRVGLCPRMDPVDGTQLLKYIRNVNFSGIAGNPVTFNENGDAPGRYDIYQYQLRNDSAEYKVIGSWTDHLHLRIERMHWPGSGQQLPRSICSLPCQPGERKKTVKGMPCCWHCEPCTGYQYQVDRYTCKTCPYDMRPTENRTGCRPIPIIKLEWGSPWAVLPLFLAVVGIAATLFVVITFVRYNDTPIVKASGRELSYVLLAGIFLCYATTFLMIAEPDLGTCSLRRIFLGLGMSISYAALLTKTNRIYRIFEQGKRSVSAPRFISPASQLAITFSLISLQLLGICVWFVVDPSHSVVDFQDQRTLDPRFARGVLKCDISDLSLICLLGYSMLLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTCIVWLAFIPIFFGTSQSADKLYIQTTTLTVSVSLSASVSLGMLYMPKVYIILFHPEQNVPKRKRSLKAVVTAATMSNKFTQKGNFRPNGEAKSELCENLEAPALATKQTYVTYTNHAI	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 292).	0	PF00003	GPCR glutamate	G-protein coupled receptor 3 family.	.	.	7 transmembrane sweet-taste receptor of 3 GCPR; Receptor family ligand binding region; Nine Cysteines Domain of family 3 GPCR	PF00003; PF01094; PF07562	PF00003; 7tm_3; PF01094; ANF_receptor; PF07562; NCD3G	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04724:Glutamatergic synapse; hsa04742:Taste transduction	R-HSA-418594:G alpha (i) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors)	.	Q14833
TTHS256	Metabotropic glutamate receptor 5 (mGluR5)	P41594	GRM5_HUMAN	GPCR glutamate	MGLUR5; GPRC1E	GRM5	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.	.	6N52; 6N51; 6N50; 6N4Y; 6N4X	MVLLLILSVLLLKEDVRGSAQSSERRVVAHMPGDIIIGALFSVHHQPTVDKVHERKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRDSLISSEEEEGLVRCVDGSSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLTSHLPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKLRPETNHRNPWFQEFWQHRFQCRLEGFPQENSKYNKTCNSSLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAGLCDAMKPIDGRKLLESLMKTNFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELKMDDDEVWSKKSNIIRSVCSEPCEKGQIKVIRKGEVSCCWTCTPCKENEYVFDEYTCKACQLGSWPTDDLTGCDLIPVQYLRWGDPEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCMFVPKVYIILAKPERNVRSAFTTSTVVRMHVGDGKSSSAASRSSSLVNLWKRRGSSGETLRYKDRRLAQHKSEIECFTPKGSMGNGGRATMSSSNGKSVTWAQNEKSSRGQHLWQRLSIHINKKENPNQTAVIKPFPKSTESRGLGAGAGAGGSAGGVGATGGAGCAGAGPGGPESPDAGPKALYDVAEAEEHFPAPARPRSPSPISTLSHRAGSASRTDDDVPSLHSEPVARSSSSQGSLMEQISSVVTRFTANISELNSMMLSTAAPSPGVGAPLCSSYLIPKEIQLPTTMTTFAEIQPLPAIEVTGGAQPAAGAQAAGDAARESPAAGPEAAAAKPDLEELVALTPPSPFRDSVDSGSTTPNSPVSESALCIPSSPKYDTLIIRDYTQSSSSL	Clinical trial	Metabolism and disposition of the metabotropic glutamate receptor 5 antagonist (mGluR5) mavoglurant (AFQ056) in healthy subjects. Drug Metab Dispos. 2013 Sep;41(9):1626-41.	24	PF00003	GPCR glutamate	G-protein coupled receptor 3 family.	.	.	7 transmembrane sweet-taste receptor of 3 GCPR; Receptor family ligand binding region; Homer-binding domain of metabotropic glutamate receptor ; Nine Cysteines Domain of family 3 GPCR	PF00003; PF01094; PF10606; PF07562	PF00003; 7tm_3; PF01094; ANF_receptor; PF10606; GluR_Homer-bdg; PF07562; NCD3G	.	.	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	R-HSA-416476:G alpha (q) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors)	.	P41594
TTWRP2F	Metabotropic glutamate receptor 6 (mGluR6)	O15303	GRM6_HUMAN	GPCR glutamate	MGLUR6; GPRC1F	GRM6	"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."	.	.	MARPRRAREPLLVALLPLAWLAQAGLARAAGSVRLAGGLTLGGLFPVHARGAAGRACGQLKKEQGVHRLEAMLYALDRVNADPELLPGVRLGARLLDTCSRDTYALEQALSFVQALIRGRGDGDEVGVRCPGGVPPLRPAPPERVVAVVGASASSVSIMVANVLRLFAIPQISYASTAPELSDSTRYDFFSRVVPPDSYQAQAMVDIVRALGWNYVSTLASEGNYGESGVEAFVQISREAGGVCIAQSIKIPREPKPGEFSKVIRRLMETPNARGIIIFANEDDIRRVLEAARQANLTGHFLWVGSDSWGAKTSPILSLEDVAVGAITILPKRASIDGFDQYFMTRSLENNRRNIWFAEFWEENFNCKLTSSGTQSDDSTRKCTGEERIGRDSTYEQEGKVQFVIDAVYAIAHALHSMHQALCPGHTGLCPAMEPTDGRMLLQYIRAVRFNGSAGTPVMFNENGDAPGRYDIFQYQATNGSASSGGYQAVGQWAETLRLDVEALQWSGDPHEVPSSLCSLPCGPGERKKMVKGVPCCWHCEACDGYRFQVDEFTCEACPGDMRPTPNHTGCRPTPVVRLSWSSPWAAPPLLLAVLGIVATTTVVATFVRYNNTPIVRASGRELSYVLLTGIFLIYAITFLMVAEPGAAVCAARRLFLGLGTTLSYSALLTKTNRIYRIFEQGKRSVTPPPFISPTSQLVITFSLTSLQVVGMIAWLGARPPHSVIDYEEQRTVDPEQARGVLKCDMSDLSLIGCLGYSLLLMVTCTVYAIKARGVPETFNEAKPIGFTMYTTCIIWLAFVPIFFGTAQSAEKIYIQTTTLTVSLSLSASVSLGMLYVPKTYVILFHPEQNVQKRKRSLKATSTVAAPPKGEDAEAHK	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 294).	0	.	.	.	.	.	.	.	.	.	.	hsa04072: Phospholipase D signaling pathway; hsa04080: Neuroactive ligand-receptor interaction; hsa04724: Glutamatergic synapse	R-HSA-418594: G alpha (i) signalling events; R-HSA-420499: Class C/3 (Metabotropic glutamate/pheromone receptors)	.	O15303
TT0I76D	Metabotropic glutamate receptor 7 (mGluR7)	Q14831	GRM7_HUMAN	GPCR glutamate	mGluR7; GPRC1G	GRM7	"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."	.	5C5C; 3MQ4	MVQLRKLLRVLTLMKFPCCVLEVLLCALAAAARGQEMYAPHSIRIEGDVTLGGLFPVHAKGPSGVPCGDIKRENGIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLTFVQALIQKDTSDVRCTNGEPPVFVKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFTQISKEAGGLCIAQSVRIPQERKDRTIDFDRIIKQLLDTPNSRAVVIFANDEDIKQILAAAKRADQVGHFLWVGSDSWGSKINPLHQHEDIAEGAITIQPKRATVEGFDAYFTSRTLENNRRNVWFAEYWEENFNCKLTISGSKKEDTDRKCTGQERIGKDSNYEQEGKVQFVIDAVYAMAHALHHMNKDLCADYRGVCPEMEQAGGKKLLKYIRNVNFNGSAGTPVMFNKNGDAPGRYDIFQYQTTNTSNPGYRLIGQWTDELQLNIEDMQWGKGVREIPASVCTLPCKPGQRKKTQKGTPCCWTCEPCDGYQYQFDEMTCQHCPYDQRPNENRTGCQDIPIIKLEWHSPWAVIPVFLAMLGIIATIFVMATFIRYNDTPIVRASGRELSYVLLTGIFLCYIITFLMIAKPDVAVCSFRRVFLGLGMCISYAALLTKTNRIYRIFEQGKKSVTAPRLISPTSQLAITSSLISVQLLGVFIWFGVDPPNIIIDYDEHKTMNPEQARGVLKCDITDLQIICSLGYSILLMVTCTVYAIKTRGVPENFNEAKPIGFTMYTTCIVWLAFIPIFFGTAQSAEKLYIQTTTLTISMNLSASVALGMLYMPKVYIIIFHPELNVQKRKRSFKAVVTAATMSSRLSHKPSDRPNGEAKTELCENVDPNSPAAKKKYVSYNNLVI	Literature-reported	"Binding of [3H](2S,1'S,2'S)-2-(9-xanthylmethyl)-2-(2'-carboxycyclopropyl) glycine ([3H]LY341495) to cell membranes expressing recombinant human group III metabotropic glutamate receptor subtypes. Naunyn Schmiedebergs Arch Pharmacol. 2000 Dec;362(6):546-54."	0	PF00003	GPCR glutamate	G-protein coupled receptor 3 family.	.	.	7 transmembrane sweet-taste receptor of 3 GCPR; Receptor family ligand binding region; Nine Cysteines Domain of family 3 GPCR	PF00003; PF01094; PF07562	PF00003; 7tm_3; PF01094; ANF_receptor; PF07562; NCD3G	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04724:Glutamatergic synapse	R-HSA-418594:G alpha (i) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors)	.	Q14831
TT0IFKL	Metabotropic glutamate receptor 8 (mGluR8)	O00222	GRM8_HUMAN	GPCR glutamate	MGluR8a; MGLUR8; Glutamate receptor mGLU8; GRM8	GRM8	Receptor for glutamate. The activity of this receptor is mediated by a g-protein that inhibits adenylate cyclase activity.	.	6E5V; 6BT5; 6BSZ	MVCEGKRSASCPCFFLLTAKFYWILTMMQRTHSQEYAHSIRVDGDIILGGLFPVHAKGERGVPCGELKKEKGIHRLEAMLYAIDQINKDPDLLSNITLGVRILDTCSRDTYALEQSLTFVQALIEKDASDVKCANGDPPIFTKPDKISGVIGAAASSVSIMVANILRLFKIPQISYASTAPELSDNTRYDFFSRVVPPDSYQAQAMVDIVTALGWNYVSTLASEGNYGESGVEAFTQISREIGGVCIAQSQKIPREPRPGEFEKIIKRLLETPNARAVIMFANEDDIRRILEAAKKLNQSGHFLWIGSDSWGSKIAPVYQQEEIAEGAVTILPKRASIDGFDRYFRSRTLANNRRNVWFAEFWEENFGCKLGSHGKRNSHIKKCTGLERIARDSSYEQEGKVQFVIDAVYSMAYALHNMHKDLCPGYIGLCPRMSTIDGKELLGYIRAVNFNGSAGTPVTFNENGDAPGRYDIFQYQITNKSTEYKVIGHWTNQLHLKVEDMQWAHREHTHPASVCSLPCKPGERKKTVKGVPCCWHCERCEGYNYQVDELSCELCPLDQRPNMNRTGCQLIPIIKLEWHSPWAVVPVFVAILGIIATTFVIVTFVRYNDTPIVRASGRELSYVLLTGIFLCYSITFLMIAAPDTIICSFRRVFLGLGMCFSYAALLTKTNRIHRIFEQGKKSVTAPKFISPASQLVITFSLISVQLLGVFVWFVVDPPHIIIDYGEQRTLDPEKARGVLKCDISDLSLICSLGYSILLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTCIIWLAFIPIFFGTAQSAEKMYIQTTTLTVSMSLSASVSLGMLYMPKVYIIIFHPEQNVQKRKRSFKAVVTAATMQSKLIQKGNDRPNGEVKSELCESLETNTSSTKTTYISYSNHSI	Literature-reported	"Group III human metabotropic glutamate receptors 4, 7 and 8: molecular cloning, functional expression, and comparison of pharmacological properties in RGT cells. Brain Res Mol Brain Res. 1998 Jan;53(1-2):88-97."	0	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04724:Glutamatergic synapse	R-HSA-418594:G alpha (i) signalling events; R-HSA-420499:Class C/3 (Metabotropic glutamate/pheromone receptors)	.	O00222
TT0LWE3	Granulin (GRN)	P28799 (58-573)	GRN_HUMAN	.	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)	GRN	"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."	.	2JYV; 2JYU; 2JYT; 2JYE; 1G26	GGPCQVDAHCSAGHSCIFTVSGTSSCCPFPEAVACGDGHHCCPRGFHCSADGRSCFQRSGNNSVGAIQCPDSQFECPDFSTCCVMVDGSWGCCPMPQASCCEDRVHCCPHGAFCDLVHTRCITPTGTHPLAKKLPAQRTNRAVALSSSVMCPDARSRCPDGSTCCELPSGKYGCCPMPNATCCSDHLHCCPQDTVCDLIQSKCLSKENATTDLLTKLPAHTVGDVKCDMEVSCPDGYTCCRLQSGAWGCCPFTQAVCCEDHIHCCPAGFTCDTQKGTCEQGPHQVPWMEKAPAHLSLPDPQALKRDVPCDNVSSCPSSDTCCQLTSGEWGCCPIPEAVCCSDHQHCCPQGYTCVAEGQCQRGSEIVAGLEKMPARRASLSHPRDIGCDQHTSCPVGQTCCPSLGGSWACCQLPHAVCCEDRQHCCPAGYTCNVKARSCEKEVVSAQPATFLARSPHVGVKDVECGEGHFCHDNQTCCRDNRQGWACCPYRQGVCCADRRHCCPAGFRCAARGTKCL	Literature-reported	Clinical phenotypes and genetic biomarkers of FTLD. J Neural Transm (Vienna). 2012 Jul;119(7):851-60. 	.	.	.	granulin family.	.	.	Granulin	PF00396	PF00396; Granulin	.	.	.	.	.	P28799
TT4LM0E	Progranulin (PGRN)	P28799	GRN_HUMAN	.	Proepithelin; PGRN; PEPI; PCDGF; PC cell-derived growth factor; Granulin precursor; Glycoprotein of 88 Kda; Glycoprotein 88; GP88; Epithelin precursor; Acrogranin	GRN	"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."	.	2JYV; 2JYU; 2JYT; 2JYE; 1G26	MWTLVSWVALTAGLVAGTRCPDGQFCPVACCLDPGGASYSCCRPLLDKWPTTLSRHLGGPCQVDAHCSAGHSCIFTVSGTSSCCPFPEAVACGDGHHCCPRGFHCSADGRSCFQRSGNNSVGAIQCPDSQFECPDFSTCCVMVDGSWGCCPMPQASCCEDRVHCCPHGAFCDLVHTRCITPTGTHPLAKKLPAQRTNRAVALSSSVMCPDARSRCPDGSTCCELPSGKYGCCPMPNATCCSDHLHCCPQDTVCDLIQSKCLSKENATTDLLTKLPAHTVGDVKCDMEVSCPDGYTCCRLQSGAWGCCPFTQAVCCEDHIHCCPAGFTCDTQKGTCEQGPHQVPWMEKAPAHLSLPDPQALKRDVPCDNVSSCPSSDTCCQLTSGEWGCCPIPEAVCCSDHQHCCPQGYTCVAEGQCQRGSEIVAGLEKMPARRASLSHPRDIGCDQHTSCPVGQTCCPSLGGSWACCQLPHAVCCEDRQHCCPAGYTCNVKARSCEKEVVSAQPATFLARSPHVGVKDVECGEGHFCHDNQTCCRDNRQGWACCPYRQGVCCADRRHCCPAGFRCAARGTKCLRREAPRWDAPLRDPALRQLL	Literature-reported	Granulin-epithelin precursor renders hepatocellular carcinoma cells resistant to natural killer cytotoxicity. Cancer Immunol Res. 2014 Dec;2(12):1209-19.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-6798695: Neutrophil degranulation	.	P28799
TTC1MVT	Gastrin-releasing peptide receptor (GRPR)	P30550	GRPR_HUMAN	GPCR rhodopsin	GRPR; GRP-preferring bombesin receptor; GRP-R; Bombesin/gastrin-releasing peptide receptor	GRPR	"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."	.	.	MALNDCFLLNLEVDHFMHCNISSHSADLPVNDDWSHPGILYVIPAVYGVIILIGLIGNITLIKIFCTVKSMRNVPNLFISSLALGDLLLLITCAPVDASRYLADRWLFGRIGCKLIPFIQLTSVGVSVFTLTALSADRYKAIVRPMDIQASHALMKICLKAAFIWIISMLLAIPEAVFSDLHPFHEESTNQTFISCAPYPHSNELHPKIHSMASFLVFYVIPLSIISVYYYFIAKNLIQSAYNLPVEGNIHVKKQIESRKRLAKTVLVFVGLFAFCWLPNHVIYLYRSYHYSEVDTSMLHFVTSICARLLAFTNSCVNPFALYLLSKSFRKQFNTQLLCCQPGLIIRSHSTGRSTTCMTSLKSTNPSVATFSLINGNICHERYV	Clinical trial	Astellas and Drais Partner To Develop Third Astellas Compound through Tacurion	21	PF00001	.	.	.	.	.	.	.	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events	.	P30550
TTQWAU1	GSK3A messenger RNA (GSK3A mRNA)	P49840	GSK3A_HUMAN	mRNA target	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)	GSK3A	"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."	EC 2.7.11.26	2DFM	MSGGGPSGGGPGGSGRARTSSFAEPGGGGGGGGGGPGGSASGPGGTGGGKASVGAMGGGVGASSSGGGPGGSGGGGSGGPGAGTSFPPPGVKLGRDSGKVTTVVATLGQGPERSQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDELYLNLVLEYVPETVYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFKSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFFDELRCLGTQLPNNRPLPPLFNFSAGELSIQPSLNAILIPPHLRSPAGTTTLTPSSQALTETPTSSDWQSTDATPTLTNSS	Literature-reported	Selective glycogen synthase kinase 3 inhibitors potentiate insulin activation of glucose transport and utilization in vitro and in vivo. Diabetes. 2003 Mar;52(3):588-95.	15.5	mRNA	mRNA target	.	.	.	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04062:Chemokine signaling pathway; hsa04728:Dopaminergic synapse; hsa04932:Non-alcoholic fatty liver disease (NAFLD)	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	.	P49840
TTRZQE3	Glycogen synthase kinase-3 alpha (GSK-3A)	P49840	GSK3A_HUMAN	Kinase	Serine/threonineprotein kinase GSK3A; Serine/threonine-protein kinase GSK3A; Glycogen synthase kinase3 alpha; Glycogen synthase kinase 3; GSK3 alpha; GSK-3 alpha; GSK-3	GSK3A	"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."	EC 2.7.11.26	2DFM	MSGGGPSGGGPGGSGRARTSSFAEPGGGGGGGGGGPGGSASGPGGTGGGKASVGAMGGGVGASSSGGGPGGSGGGGSGGPGAGTSFPPPGVKLGRDSGKVTTVVATLGQGPERSQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDELYLNLVLEYVPETVYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFKSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFFDELRCLGTQLPNNRPLPPLFNFSAGELSIQPSLNAILIPPHLRSPAGTTTLTPSSQALTETPTSSDWQSTDATPTLTNSS	Successful	Challenges and new opportunities in the investigation of new drug therapies to treat frontotemporal dementia. Expert Opin Ther Targets. 2008 Nov;12(11):1367-76.	34	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.	2.7.11.26	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04062: Chemokine signaling pathway; hsa04728: Dopaminergic synapse; hsa04932: Non-alcoholic fatty liver disease; hsa05131: Shigellosis	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	.	P49840
TTRSMW9	Glycogen synthase kinase-3 beta (GSK-3B)	P49841	GSK3B_HUMAN	Kinase	Serine/threonine-protein kinase GSK3B; GSK-3 beta	GSK3B	"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."	EC 2.7.11.26	6NPZ; 6H0U; 6GN1; 6GJO; 6BUU	MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDANTGDRGQTNNAASASASNST	Clinical trial	Evidence for irreversible inhibition of glycogen synthase kinase-3beta by tideglusib. J Biol Chem. 2012 Jan 6;287(2):893-904.	21	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.	2.7.11.26	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	P49841
TTUH7OM	Gelsolin (GSN)	P06396	GELS_HUMAN	.	GSN; Brevin; Actindepolymerizing factor; AGEL	GSN	"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}."	.	6H1F; 5UBO; 5O2Z; 5H3N; 5H3M	MAPHRPAPALLCALSLALCALSLPVRAATASRGASQAGAPQGRVPEARPNSMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWESFNNGDCFILDLGNNIHQWCGSNSNRYERLKATQVSKGIRDNERSGRARVHVSEEGTEPEAMLQVLGPKPALPAGTEDTAKEDAANRKLAKLYKVSNGAGTMSVSLVADENPFAQGALKSEDCFILDHGKDGKIFVWKGKQANTEERKAALKTASDFITKMDYPKQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGLGLSYLSSHIANVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSREGGQTAPASTRLFQVRANSAGATRAVEVLPKAGALNSNDAFVLKTPSAAYLWVGTGASEAEKTGAQELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDKKMDAHPPRLFACSNKIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVKQGFEPPSFVGWFLGWDDDYWSVDPLDRAMAELAA	Literature-reported	Gelsolin as therapeutic target in Alzheimer's disease. Expert Opin Ther Targets. 2010 Jun;14(6):585-92.	.	.	.	.	.	.	.	.	.	.	.	hsa04666:Fc gamma R-mediated phagocytosis; hsa04810:Regulation of actin cytoskeleton; hsa05203:Viral carcinogenesis	R-HSA-264870:Caspase-mediated cleavage of cytoskeletal proteins; R-HSA-977225:Amyloid formation	.	P06396
TTEP6RV	Glutathione reductase (GR)	P00390	GSHR_HUMAN	Sulfur donor oxidoreductase	"Glutathione reductase, mitochondrial; GRase; GRD1; GLUR"	GSR	Maintains high levels of reduced glutathione in the cytosol.	EC 1.8.1.7	5GRT; 4GRT; 4GR1; 3SQP; 3GRT	MALLPRALSAGAGPSWRRAARAFRGFLLLLPEPAALTRALSRAMACRQEPQPQGPPPAAGAVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR	Patented-recorded	DrugBank 3.0: a comprehensive resource for 'omics' research on drugs. Nucleic Acids Res. 2011 Jan;39(Database issue):D1035-41.	15.5	EC:1.8	Oxidoreductases acting on a sulfur group of donors	class-I pyridine nucleotide-disulfide oxidoreductase family.	1.8.1.7	Acting on a sulfur group of donors	"Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain"	PF07992; PF02852	PF07992; Pyr_redox_2; PF02852; Pyr_redox_dim	.	.	hsa00480:Glutathione metabolism; hsa04918:Thyroid hormone synthesis	R-HSA-2408550: Metabolism of ingested H2SeO4 and H2SeO3 into H2Se; R-HSA-3299685: Detoxification of Reactive Oxygen Species; R-HSA-499943: Interconversion of nucleotide di- and triphosphates; R-HSA-5628897: TP53 Regulates Metabolic Genes; R-HSA-9759194: Nuclear events mediated by NFE2L2	MetaCyc:HS02602-MON	P00390
TTVEWR4	Glutathione synthetase (GSS)	P48637	GSHB_HUMAN	.	Glutathione synthase; GSH-S; GSH synthetase	GSS	"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."	EC 6.3.2.3	2HGS	MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSALLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVFLGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKILSNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFEDISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQLAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSRFVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVVQCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV	Literature-reported	Nineteen-year follow-up of a patient with severe glutathione synthetase deficiency. J Hum Genet. 2016 Jul;61(7):669-72.	.	.	.	.	.	.	.	.	.	.	.	hsa00270: Cysteine and methionine metabolism; hsa00480: Glutathione metabolism; hsa01100: Metabolic pathways; hsa01240: Biosynthesis of cofactors; hsa04216: Ferroptosis	R-HSA-174403: Glutathione synthesis and recycling; R-HSA-5579006: Defective GSS causes GSS deficiency	MetaCyc:HS02174-MON	P48637
TT4P8DE	Glutathione S-transferase A1 (GSTA1)	P08263	GSTA1_HUMAN	.	"GTH1; GSTA1-1; GST-epsilon; GST class-alpha member 1; GST HA subunit 1; Androst-5-ene-3,17-dione isomerase; 13-hydroperoxyoctadecadienoate peroxidase"	GSTA1	"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."	EC 2.5.1.18	6ATR; 6ATQ; 6ATP; 6ATO; 5LD0	MAEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF	Literature-reported	Glutathione S-transferase A1 (GSTA1) as a marker of acetaminophen-induced hepatocyte injury in vitro. Toxicol Mech Methods. 2017 Jul;27(6):401-407.	.	.	.	.	.	.	.	.	.	.	.	hsa00480: Glutathione metabolism; hsa00980: Metabolism of xenobiotics by cytochrome P450; hsa00982: Drug metabolism - cytochrome P450; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa01524: Platinum drug resistance; hsa05200: Pathways in cancer; hsa05204: Chemical carcinogenesis - DNA adducts; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05225: Hepatocellular carcinoma; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-156590: Glutathione conjugation; R-HSA-189483: Heme degradation; R-HSA-9748787: Azathioprine ADME; R-HSA-9759194: Nuclear events mediated by NFE2L2	MetaCyc:G66-32542-MON	P08263
TTNLFBE	Glutathione S-transferase A2 (GSTA2)	P09210	GSTA2_HUMAN	.	GTH2; GSTA2-2; GST2; GST-gamma; GST class-alpha member 2; GST HA subunit 2	GSTA2	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.	EC 2.5.1.18	4ACS; 2WJU; 2VCT; 1AGS	MAEKPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIADLGEMILLLPFSQPEEQDAKLALIQEKTKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEESRKIFRF	Literature-reported	"Human glutathione S-transferase A2 polymorphisms: variant expression, distribution in prostate cancer cases/controls and a novel form. Pharmacogenetics. 2004 Jan;14(1):35-44."	.	.	.	.	.	.	.	.	.	.	.	hsa00480: Glutathione metabolism; hsa00980: Metabolism of xenobiotics by cytochrome P450; hsa00982: Drug metabolism - cytochrome P450; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa01524: Platinum drug resistance; hsa05200: Pathways in cancer; hsa05204: Chemical carcinogenesis - DNA adducts; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05225: Hepatocellular carcinoma; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-156590: Glutathione conjugation; R-HSA-8950505: Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation; R-HSA-9748787: Azathioprine ADME	MetaCyc:HS01846-MON	P09210
TT29VDX	Glutathione S-transferase A3 (GSTA3)	Q16772	GSTA3_HUMAN	.	Glutathione S-transferase A3-3; GST class-alpha member 3	GSTA3	"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."	EC 2.5.1.18	2VCV; 1TDI	MAGKPKLHYFNGRGRMEPIRWLLAAAGVEFEEKFIGSAEDLGKLRNDGSLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYTEGMADLNEMILLLPLCRPEEKDAKIALIKEKTKSRYFPAFEKVLQSHGQDYLVGNKLSRADISLVELLYYVEELDSSLISNFPLLKALKTRISNLPTVKKFLQPGSPRKPPADAKALEEARKIFRF	Literature-reported	Glutathione-S-transferase A3 knockout mice are sensitive to acute cytotoxic and genotoxic effects of aflatoxin B1. Toxicol Appl Pharmacol. 2010 Feb 1;242(3):241-6.	.	.	.	.	.	.	.	.	.	.	.	hsa00480: Glutathione metabolism; hsa00980: Metabolism of xenobiotics by cytochrome P450; hsa00982: Drug metabolism - cytochrome P450; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa01524: Platinum drug resistance; hsa05200: Pathways in cancer; hsa05204: Chemical carcinogenesis - DNA adducts; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05225: Hepatocellular carcinoma; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-156590: Glutathione conjugation; R-HSA-9759194: Nuclear events mediated by NFE2L2	.	Q16772
TTWO3SH	Glutathione S-transferase omega-1 (GSTO-1)	P78417	GSTO1_HUMAN	.	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	GSTO1	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.	EC 2.5.1.18	6MHD; 6MHC; 6MHB; 5YVO; 5YVN	MSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMILELFSKVPSLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVLTNKKTTFFGGNSISMIDYLIWPWFERLEAMKLNECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELYLQNSPEACDYGL	Preclinical	Mechanistic evaluation and transcriptional signature of a glutathione S-transferase omega 1 inhibitor. Nat Commun. 2016 Oct 5;7:13084.	.	.	.	.	.	.	.	.	.	.	.	hsa00480: Glutathione metabolism; hsa00980: Metabolism of xenobiotics by cytochrome P450; hsa00982: Drug metabolism - cytochrome P450; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa01524: Platinum drug resistance; hsa05200: Pathways in cancer; hsa05204: Chemical carcinogenesis - DNA adducts; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05225: Hepatocellular carcinoma; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-156581: Methylation; R-HSA-156590: Glutathione conjugation; R-HSA-196836: Vitamin C (ascorbate) metabolism; R-HSA-8950505: Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation	MetaCyc:HS07564-MON	P78417
TT40K12	Glutathione S-transferase P (GSTP1)	P09211	GSTP1_HUMAN	Alkyl aryl transferase	GSTP11; GSTP1-1; GST3; GST classpi; GST class-pi; FAEES3	GSTP1	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.	EC 2.5.1.18	9GSS; 8GSS; 7GSS; 6GSS; 6AP9	MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ	Clinical trial	"Mechanism of glutathione transferase P1-1-catalyzed activation of the prodrug canfosfamide (TLK286, TELCYTA). Biochemistry. 2013 Nov 12;52(45):8069-78."	25	EC:2.5	Alkyl aryl transferase	GST superfamily. Pi family.	2.5.1.18	"Transferring alkyl or aryl groups, other than methyl groups"	"Glutathione S-transferase, C-terminal domain; Glutathione S-transferase, N-terminal domain"	PF14497; PF02798	PF14497; GST_C_3; PF02798; GST_N	.	.	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	R-HSA-156590: Glutathione conjugation; R-HSA-3299685: Detoxification of Reactive Oxygen Species; R-HSA-6798695: Neutrophil degranulation; R-HSA-9753281: Paracetamol ADME	.	P09211
TT48Z3K	GSTP1 messenger RNA (GSTP1 mRNA)	P09211	GSTP1_HUMAN	.	GST class-pi; GSTP1-1	GSTP1	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.	EC 2.5.1.18	.	MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ	Clinical trial	"Clinical pipeline report, company report or official report of Nitto Biopharma."	.	.	.	.	.	.	.	.	.	.	.	hsa00480: Glutathione metabolism; hsa00980: Metabolism of xenobiotics by cytochrome P450; hsa00982: Drug metabolism - cytochrome P450; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa01524: Platinum drug resistance; hsa05200: Pathways in cancer; hsa05204: Chemical carcinogenesis - DNA adducts; hsa05215: Prostate cancer; hsa05225: Hepatocellular carcinoma; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-156590: Glutathione conjugation; R-HSA-3299685: Detoxification of Reactive Oxygen Species; R-HSA-6798695: Neutrophil degranulation; R-HSA-9753281: Paracetamol ADME	.	P09211
TT23PYC	Soluble guanylate cyclase (GCS)	Q02108; Q02153	GCYA1_HUMAN; GCYB1_HUMAN	Phosphorus-oxygen lyase	GUCY1; GUCS; GUC1; GCS	GUCY1A1	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.	.	.	MFCTKLKDLKITGECPFSLLAPGQVPNESSEEAAGSSESCKATVPICQDIPEKNIQESLPQRKTSRSRVYLHTLAESICKLIFPEFERLNVALQRTLAKHKIKESRKSLEREDFEKTIAEQAVAAGVPVEVIKESLGEEVFKICYEEDENILGVVGGTLKDFLNSFSTLLKQSSHCQEAGKRGRLEDASILCLDKEDDFLHVYYFFPKRTTSLILPGIIKAAAHVLYETEVEVSLMPPCFHNDCSEFVNQPYLLYSVHMKSTKPSLSPSKPQSSLVIPTSLFCKTFPFHFMFDKDMTILQFGNGIRRLMNRRDFQGKPNFEEYFEILTPKINQTFSGIMTMLNMQFVVRVRRWDNSVKKSSRVMDLKGQMIYIVESSAILFLGSPCVDRLEDFTGRGLYLSDIPIHNALRDVVLIGEQARAQDGLKKRLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQLWQGQVVQAKKFSNVTMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHKESDTHAVQIALMALKMMELSDEVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNNVTLANKFESCSVPRKINVSPTTYRLLKDCPGFVFTPRSREELPPNFPSEIPGICHFLDAYQQGTNSKPCFQKKDVEDGNANFLGKASGID	Successful	Activators of soluble guanylate cyclase for the treatment of male erectile dysfunction. Int J Impot Res. 2002 Feb;14(1):8-14.	34	.	.	.	.	.	.	.	.	.	.	hsa00230: Purine metabolism; hsa01100: Metabolic pathways; 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; hsa04924: Renin secretion; hsa04970: Salivary secretion	R-HSA-392154: Nitric oxide stimulates guanylate cyclase; R-HSA-445355: Smooth Muscle Contraction	.	Q02108
TTLBYH1	Guanylate cyclase soluble beta-1 (GUCY1B1)	Q02153	GCYB1_HUMAN	Phosphorus-oxygen lyase	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	GUCY1B1	Mediates responses to nitric oxide (NO) by catalyzing the biosynthesis of the signaling molecule cGMP.	EC 4.6.1.2	5MNW; 4NI2; 3UVJ; 2WZ1	MYGFVNHALELLVIRNYGPEVWEDIKKEAQLDEEGQFLVRIIYDDSKTYDLVAAASKVLNLNAGEILQMFGKMFFVFCQESGYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSFRCTDAEKGKGLILHYYSEREGLQDIVIGIIKTVAQQIHGTEIDMKVIQQRNEECDHTQFLIEEKESKEEDFYEDLDRFEENGTQESRISPYTFCKAFPFHIIFDRDLVVTQCGNAIYRVLPQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLDVEKLECEDELTGTEISCLRLKGQMIYLPEADSILFLCSPSVMNLDDLTRRGLYLSDIPLHDATRDLVLLGEQFREEYKLTQELEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANELRHKRPVPAKRYDNVTILFSGIVGFNAFCSKHASGEGAMKIVNLLNDLYTRFDTLTDSRKNPFVYKVETVGDKYMTVSGLPEPCIHHARSICHLALDMMEIAGQVQVDGESVQITIGIHTGEVVTGVIGQRMPRYCLFGNTVNLTSRTETTGEKGKINVSEYTYRCLMSPENSDPQFHLEHRGPVSMKGKKEPMQVWFLSRKNTGTEETKQDDD	Clinical trial	Rationale and design of the SOluble guanylate Cyclase stimulatoR in heArT failurE Studies (SOCRATES). Eur J Heart Fail. 2014 Sep;16(9):1026-38.	21	.	.	.	.	.	.	.	.	.	.	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	R-HSA-392154:Nitric oxide stimulates guanylate cyclase	.	Q02153
TTLDPRG	Guanylyl cyclase C (GUCY2C)	P25092	GUC2C_HUMAN	Phosphorus-oxygen lyase	hSTAR; STA receptor; Intestinal guanylate cyclase; Heat-stable enterotoxin receptor; GUC2C; GC-C	GUCY2C	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.	EC 4.6.1.2	.	MKTLLLDLALWSLLFQPGWLSFSSQVSQNCHNGSYEISVLMMGNSAFAEPLKNLEDAVNEGLEIVRGRLQNAGLNVTVNATFMYSDGLIHNSGDCRSSTCEGLDLLRKISNAQRMGCVLIGPSCTYSTFQMYLDTELSYPMISAGSFGLSCDYKETLTRLMSPARKLMYFLVNFWKTNDLPFKTYSWSTSYVYKNGTETEDCFWYLNALEASVSYFSHELGFKVVLRQDKEFQDILMDHNRKSNVIIMCGGPEFLYKLKGDRAVAEDIVIILVDLFNDQYFEDNVTAPDYMKNVLVLTLSPGNSLLNSSFSRNLSPTKRDFALAYLNGILLFGHMLKIFLENGENITTPKFAHAFRNLTFEGYDGPVTLDDWGDVDSTMVLLYTSVDTKKYKVLLTYDTHVNKTYPVDMSPTFTWKNSKLPNDITGRGPQILMIAVFTLTGAVVLLLLVALLMLRKYRKDYELRQKKWSHIPPENIFPLETNETNHVSLKIDDDKRRDTIQRLRQCKYDKKRVILKDLKHNDGNFTEKQKIELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLREVLNDTISYPDGTFMDWEFKISVLYDIAKGMSYLHSSKTEVHGRLKSTNCVVDSRMVVKITDFGCNSILPPKKDLWTAPEHLRQANISQKGDVYSYGIIAQEIILRKETFYTLSCRDRNEKIFRVENSNGMKPFRPDLFLETAEEKELEVYLLVKNCWEEDPEKRPDFKKIETTLAKIFGLFHDQKNESYMDTLIRRLQLYSRNLEHLVEERTQLYKAERDRADRLNFMLLPRLVVKSLKEKGFVEPELYEEVTIYFSDIVGFTTICKYSTPMEVVDMLNDIYKSFDHIVDHHDVYKVETIGDAYMVASGLPKRNGNRHAIDIAKMALEILSFMGTFELEHLPGLPIWIRIGVHSGPCAAGVVGIKMPRYCLFGDTVNTASRMESTGLPLRIHVSGSTIAILKRTECQFLYEVRGETYLKGRGNETTYWLTGMKDQKFNLPTPPTVENQQRLQAEFSDMIANSLQKRQAAGIRSQKPRRVASYKKGTLEYLQLNTTDKESTYF	Successful	Emerging drugs for postoperative ileus. Expert Opin Emerg Drugs. 2007 Nov;12(4):619-26.	34	.	.	.	.	.	.	.	.	.	.	hsa00230: Purine metabolism; hsa01100: Metabolic pathways	R-HSA-8935690: Digestion; R-HSA-8942233: Intestinal infectious diseases	.	P25092
TTWNFC2	Soluble guanylyl cyclase (GUCY2D)	Q02846	GUC2D_HUMAN	.	"Rod outer segment membrane guanylate cyclase; Retinal guanylyl cyclase 1; ROS-GC; RETGC1; RETGC-1; RETGC; Guanylate cyclase 2D, retinal; GUC2D; GUC1A4; CORD6"	GUCY2D	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.	EC 4.6.1.2	1AWL	MTACARRAGGLPDPGLCGPAWWAPSLPRLPRALPRLPLLLLLLLLQPPALSAVFTVGVLGPWACDPIFSRARPDLAARLAAARLNRDPGLAGGPRFEVALLPEPCRTPGSLGAVSSALARVSGLVGPVNPAACRPAELLAEEAGIALVPWGCPWTQAEGTTAPAVTPAADALYALLRAFGWARVALVTAPQDLWVEAGRSLSTALRARGLPVASVTSMEPLDLSGAREALRKVRDGPRVTAVIMVMHSVLLGGEEQRYLLEAAEELGLTDGSLVFLPFDTIHYALSPGPEALAALANSSQLRRAHDAVLTLTRHCPSEGSVLDSLRRAQERRELPSDLNLQQVSPLFGTIYDAVFLLARGVAEARAAAGGRWVSGAAVARHIRDAQVPGFCGDLGGDEEPPFVLLDTDAAGDRLFATYMLDPARGSFLSAGTRMHFPRGGSAPGPDPSCWFDPNNICGGGLEPGLVFLGFLLVVGMGLAGAFLAHYVRHRLLHMQMVSGPNKIILTVDDITFLHPHGGTSRKVAQGSRSSLGARSMSDIRSGPSQHLDSPNIGVYEGDRVWLKKFPGDQHIAIRPATKTAFSKLQELRHENVALYLGLFLARGAEGPAALWEGNLAVVSEHCTRGSLQDLLAQREIKLDWMFKSSLLLDLIKGIRYLHHRGVAHGRLKSRNCIVDGRFVLKITDHGHGRLLEAQKVLPEPPRAEDQLWTAPELLRDPALERRGTLAGDVFSLAIIMQEVVCRSAPYAMLELTPEEVVQRVRSPPPLCRPLVSMDQAPVECILLMKQCWAEQPELRPSMDHTFDLFKNINKGRKTNIIDSMLRMLEQYSSNLEDLIRERTEELELEKQKTDRLLTQMLPPSVAEALKTGTPVEPEYFEQVTLYFSDIVGFTTISAMSEPIEVVDLLNDLYTLFDAIIGSHDVYKVETIGDAYMVASGLPQRNGQRHAAEIANMSLDILSAVGTFRMRHMPEVPVRIRIGLHSGPCVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHVNLSTVGILRALDSGYQVELRGRTELKGKGAEDTFWLVGRRGFNKPIPKPPDLQPGSSNHGISLQEIPPERRRKLEKARPGQFS	Successful	Radium 223 dichloride for prostate cancer treatment. Drug Des Devel Ther. 2017 Sep 6;11:2643-2651.	34	.	.	.	.	.	.	.	.	.	.	hsa00230: Purine metabolism; hsa01100: Metabolic pathways; hsa04740: Olfactory transduction; hsa04744: Phototransduction	"R-HSA-2514859: Inactivation, recovery and regulation of the phototransduction cascade"	.	Q02846
TTHS7CM	Beta-glucuronidase (GUSB)	P08236	BGLR_HUMAN	.	Beta-G1	GUSB	Plays an important role in the degradation of dermatan and keratan sulfates.	EC 3.2.1.31	3HN3; 1BHG	MARGSAVAWAALGPLLWGCALGLQGGMLYPQESPSRECKELDGLWSFRADFSDNRRRGFEEQWYRRPLWESGPTVDMPVPSSFNDISQDWRLRHFVGWVWYEREVILPERWTQDLRTRVVLRIGSAHSYAIVWVNGVDTLEHEGGYLPFEADISNLVQVGPLPSRLRITIAINNTLTPTTLPPGTIQYLTDTSKYPKGYFVQNTYFDFFNYAGLQRSVLLYTTPTTYIDDITVTTSVEQDSGLVNYQISVKGSNLFKLEVRLLDAENKVVANGTGTQGQLKVPGVSLWWPYLMHERPAYLYSLEVQLTAQTSLGPVSDFYTLPVGIRTVAVTKSQFLINGKPFYFHGVNKHEDADIRGKGFDWPLLVKDFNLLRWLGANAFRTSHYPYAEEVMQMCDRYGIVVIDECPGVGLALPQFFNNVSLHHHMQVMEEVVRRDKNHPAVVMWSVANEPASHLESAGYYLKMVIAHTKSLDPSRPVTFVSNSNYAADKGAPYVDVICLNSYYSWYHDYGHLELIQLQLATQFENWYKKYQKPIIQSEYGAETIAGFHQDPPLMFTEEYQKSLLEQYHLGLDQKRRKYVVGELIWNFADFMTEQSPTRVLGNKKGIFTRQRQPKSAAFLLRERYWKIANETRYPHSVAKSQCLENSLFT	Successful	2017 FDA drug approvals.Nat Rev Drug Discov. 2018 Feb;17(2):81-85. 	34	.	.	.	.	.	.	.	.	.	.	hsa00040: Pentose and glucuronate interconversions; hsa00053: Ascorbate and aldarate metabolism; hsa00531: Glycosaminoglycan degradation; hsa00860: Porphyrin metabolism; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa01240: Biosynthesis of cofactors; hsa04142: Lysosome	R-HSA-2024096: HS-GAG degradation; R-HSA-2160916: Hyaluronan uptake and degradation; R-HSA-2206292: MPS VII - Sly syndrome; R-HSA-6798695: Neutrophil degranulation	.	P08236
TTKEPHX	Granzyme B (GZMB)	P10144	GRAB_HUMAN	Peptidase	Tcell serine protease 13E; SECT; Lymphocyte protease; Human lymphocyte protein; Granzyme2; GZMB; Fragmentin2; Cytotoxic Tlymphocyte proteinase 2; Cathepsin Glike 1; CTSGL1; CTLA1; C11	GZMB	"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."	EC 3.4.21.79	1IAU; 1FQ3	MQPILLLLAFLLLPRADAGEIIGGHEAKPHSRPYMAYLMIWDQKSLKRCGGFLIRDDFVLTAAHCWGSSINVTLGAHNIKEQEPTQQFIPVKRPIPHPAYNPKNFSNDIMLLQLERKAKRTRAVQPLRLPSNKAQVKPGQTCSVAGWGQTAPLGKHSHTLQEVKMTVQEDRKCESDLRHYYDSTIELCVGDPEIKKTSFKGDSGGPLVCNKVAQGIVSYGRNNGMPPRACTKVSSFVHWIKKTMKRY	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2369).	0	.	.	.	.	.	.	.	.	.	.	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	R-HSA-2197563:NOTCH2 intracellular domain regulates transcription	.	P10144
TTNQTLJ	Gamma-Histone H2AX (H2AFX)	P16104	H2AX_HUMAN	.	Phosphorylation of H2AX; Histone H2AX; Histone H2A.x; H2a/x; H2AX	H2AFX	"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."	.	3U3Z; 3SZM; 3SQD; 3SHV; 2DYP	MSGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTSATVGPKAPSGGKKATQASQEY	Literature-reported	Evaluating Gamma-H2AX Expression as a Biomarker of DNA Damage after X-ray in Angiography Patients. J Biomed Phys Eng. 2018 Dec 1;8(4):393-402.	.	.	.	histone H2A family.	.	.	Core histone H2A/H2B/H3/H4; C-terminus of histone H2A	PF00125; PF16211	PF00125; Histone; PF16211; Histone_H2A_C	.	.	hsa04217: Necroptosis; hsa04613: Neutrophil extracellular trap formation; hsa05034: Alcoholism; hsa05322: Systemic lupus erythematosus	R-HSA-110328: Recognition and association of DNA glycosylase with site containing an affected pyrimidine; R-HSA-110329: Cleavage of the damaged pyrimidine; R-HSA-110330: Recognition and association of DNA glycosylase with site containing an affected purine; R-HSA-110331: Cleavage of the damaged purine; R-HSA-1221632: Meiotic synapsis; R-HSA-171306: Packaging Of Telomere Ends; R-HSA-1912408: Pre-NOTCH Transcription and Translation; R-HSA-201722: Formation of the beta-catenin:TCF transactivating complex; R-HSA-212300: PRC2 methylates histones and DNA; R-HSA-2299718: Condensation of Prophase Chromosomes; R-HSA-2559580: Oxidative Stress Induced Senescence; R-HSA-2559582: Senescence-Associated Secretory Phenotype (SASP); R-HSA-2559586: DNA Damage/Telomere Stress Induced Senescence; R-HSA-3214858: RMTs methylate histone arginines; R-HSA-427359: SIRT1 negatively regulates rRNA expression; R-HSA-427389: ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression; R-HSA-427413: NoRC negatively regulates rRNA expression; R-HSA-5250924: B-WICH complex positively regulates rRNA expression; R-HSA-5334118: DNA methylation; R-HSA-5578749: Transcriptional regulation by small RNAs; R-HSA-5617472: Activation of anterior HOX genes in hindbrain development during early embryogenesis; R-HSA-5625886: Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3; 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-606279: Deposition of new CENPA-containing nucleosomes at the centromere; R-HSA-68616: Assembly of the ORC complex at the origin of replication; R-HSA-69473: G2/M DNA damage checkpoint; R-HSA-73728: RNA Polymerase I Promoter Opening; R-HSA-73772: RNA Polymerase I Promoter Escape; R-HSA-8936459: RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function; R-HSA-8939236: RUNX1 regulates transcription of genes involved in differentiation of HSCs; R-HSA-9018519: Estrogen-dependent gene expression; R-HSA-912446: Meiotic recombination; R-HSA-9616222: Transcriptional regulation of granulopoiesis; R-HSA-9670095: Inhibition of DNA recombination at telomere; R-HSA-9710421: Defective pyroptosis; R-HSA-977225: Amyloid fiber formation	.	P16104
TTQZ1TP	Histone variant H2A.Z (H2AFZ)	P0C0S5	H2AZ_HUMAN	.	Histone H2A.Z; H2AZ; H2A/z	H2AFZ	"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."	.	5Z30; 5FUG; 5CHL; 5B33; 5B32	MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV	Literature-reported	Histone variant H2A.Z can serve as a new target for breast cancer therapy. Curr Med Chem. 2010;17(28):3155-61.	.	.	.	.	.	.	.	.	.	.	.	hsa04217: Necroptosis; hsa04613: Neutrophil extracellular trap formation; hsa05034: Alcoholism; hsa05322: Systemic lupus erythematosus	R-HSA-110328: Recognition and association of DNA glycosylase with site containing an affected pyrimidine; R-HSA-110329: Cleavage of the damaged pyrimidine; R-HSA-110330: Recognition and association of DNA glycosylase with site containing an affected purine; R-HSA-110331: Cleavage of the damaged purine; R-HSA-1221632: Meiotic synapsis; R-HSA-171306: Packaging Of Telomere Ends; R-HSA-1912408: Pre-NOTCH Transcription and Translation; R-HSA-201722: Formation of the beta-catenin:TCF transactivating complex; R-HSA-212300: PRC2 methylates histones and DNA; R-HSA-2299718: Condensation of Prophase Chromosomes; R-HSA-2559580: Oxidative Stress Induced Senescence; R-HSA-2559582: Senescence-Associated Secretory Phenotype (SASP); R-HSA-2559586: DNA Damage/Telomere Stress Induced Senescence; R-HSA-3214858: RMTs methylate histone arginines; R-HSA-427359: SIRT1 negatively regulates rRNA expression; R-HSA-427389: ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression; R-HSA-427413: NoRC negatively regulates rRNA expression; R-HSA-5250924: B-WICH complex positively regulates rRNA expression; R-HSA-5334118: DNA methylation; R-HSA-5578749: Transcriptional regulation by small RNAs; R-HSA-5617472: Activation of anterior HOX genes in hindbrain development during early embryogenesis; R-HSA-5625886: Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3; R-HSA-606279: Deposition of new CENPA-containing nucleosomes at the centromere; R-HSA-68616: Assembly of the ORC complex at the origin of replication; R-HSA-73728: RNA Polymerase I Promoter Opening; R-HSA-73772: RNA Polymerase I Promoter Escape; R-HSA-8936459: RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function; R-HSA-8939236: RUNX1 regulates transcription of genes involved in differentiation of HSCs; R-HSA-9018519: Estrogen-dependent gene expression; R-HSA-912446: Meiotic recombination; R-HSA-9616222: Transcriptional regulation of granulopoiesis; R-HSA-9670095: Inhibition of DNA recombination at telomere; R-HSA-9710421: Defective pyroptosis; R-HSA-977225: Amyloid fiber formation	.	P0C0S5
TT16NHT	Mutated Histone H3.3 (H3F3A)	P84243	H33_HUMAN	.	PP781; Histone H3.3; H3F3; H3.3B; H3.3A	H3F3A	"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."	.	6J51; 6J50; 6J4Z; 6J4Y; 6J4X	MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA	Literature-reported	K27M-mutant histone-3 as a novel target for glioma immunotherapy. Oncoimmunology. 2017 May 12;6(7):e1328340.	.	.	.	.	.	.	.	.	.	.	.	hsa04613: Neutrophil extracellular trap formation; hsa05034: Alcoholism; hsa05131: Shigellosis; hsa05202: Transcriptional misregulation in cancer; hsa05322: Systemic lupus erythematosus	R-HSA-1912408: Pre-NOTCH Transcription and Translation; R-HSA-201722: Formation of the beta-catenin:TCF transactivating complex; R-HSA-212300: PRC2 methylates histones and DNA; R-HSA-2299718: Condensation of Prophase Chromosomes; R-HSA-2559580: Oxidative Stress Induced Senescence; R-HSA-2559582: Senescence-Associated Secretory Phenotype (SASP); R-HSA-427359: SIRT1 negatively regulates rRNA expression; R-HSA-427389: ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression; R-HSA-427413: NoRC negatively regulates rRNA expression; R-HSA-5250924: B-WICH complex positively regulates rRNA expression; R-HSA-5334118: DNA methylation; R-HSA-5578749: Transcriptional regulation by small RNAs; R-HSA-5617472: Activation of anterior HOX genes in hindbrain development during early embryogenesis; R-HSA-5625886: Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3; R-HSA-68616: Assembly of the ORC complex at the origin of replication; R-HSA-73728: RNA Polymerase I Promoter Opening; R-HSA-73772: RNA Polymerase I Promoter Escape; R-HSA-8936459: RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function; R-HSA-8939236: RUNX1 regulates transcription of genes involved in differentiation of HSCs; R-HSA-9018519: Estrogen-dependent gene expression; R-HSA-912446: Meiotic recombination; R-HSA-9616222: Transcriptional regulation of granulopoiesis; R-HSA-9670095: Inhibition of DNA recombination at telomere; R-HSA-9710421: Defective pyroptosis; R-HSA-977225: Amyloid fiber formation; R-HSA-983231: Factors involved in megakaryocyte development and platelet production	.	P84243
TTWON83	3-hydroxyanthranilate oxygenase (HAAO)	P46952	3HAO_HUMAN	.	"h3HAO; HAD; 3-hydroxyanthranilic acid dioxygenase; 3-hydroxyanthranilate 3,4-dioxygenase; 3-HAO"	HAAO	"Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate."	EC 1.13.11.6	5TKQ; 5TK5; 2QNK	MERRLGVRAWVKENRGSFQPPVCNKLMHQEQLKVMFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPARVPHSPQRFANTVGLVVERRRLETELDGLRYYVGDTMDVLFEKWFYCKDLGTQLAPIIQEFFSSEQYRTGKPIPDQLLKEPPFPLSTRSIMEPMSLDAWLDSHHRELQAGTPLSLFGDTYETQVIAYGQGSSEGLRQNVDVWLWQLEGSSVVTMGGRRLSLAPDDSLLVLAGTSYAWERTQGSVALSVTQDPACKKPLG	Literature-reported	"NAD Deficiency, Congenital Malformations, and Niacin Supplementation. N Engl J Med. 2017 Aug 10;377(6):544-552."	.	.	.	.	.	.	.	.	.	.	.	hsa00380: Tryptophan metabolism; hsa01100: Metabolic pathways; hsa01240: Biosynthesis of cofactors	R-HSA-71240: Tryptophan catabolism	MetaCyc:HS08749-MON	P46952
TTFLMXC	Haemophilus influenzae Iron-transporter ferric ion-binding (Hae-influ fbpA)	P35755	FBPA_HAEIN	ABC transporter	Major ferric iron binding protein; MIRP; Iron-regulated 40 kDa protein; Fe(3+)-binding protein; Fe(+3)Iron-utilization periplasmic protein precursor-binding protein	Hae-influ fbpA	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.	.	3ODB; 3OD7; 3KN8; 3KN7; 2O6A	MQFKHFKLATLAAALAFSANSFADITVYNGQHKEAATAVAKAFEQETGIKVTLNSGKSEQLAGQLKEEGDKTPADVFYTEQTATFADLSEAGLLAPISEQTIQQTAQKGVPLAPKKDWIALSGRSRVVVYDHTKLSEKDMEKSVLDYATPKWKGKIGYVSTSGAFLEQVVALSKMKGDKVALNWLKGLKENGKLYAKNSVALQAVENGEVPAALINNYYWYNLAKEKGVENLKSRLYFVRHQDPGALVSYSGAAVLKASKNQAEAQKFVDFLASKKGQEALVAARAEYPLRADVVSPFNLEPYEKLEAPVVSATTAQDKEHAIKLIEEAGLK	Literature-reported	Structure of Haemophilus influenzae Fe(+3)-binding protein reveals convergent evolution within a superfamily. Nat Struct Biol. 1997 Nov;4(11):919-24.	.	.	.	.	.	.	.	.	.	.	.	hin02010: ABC transporters	.	HINF71421:G1GJ1-102-MON	P35755
TTE72ID	Haemophilus influenzae DNA gyrase A (Hae-influ gyrA)	P43700	GYRA_HAEIN	ATP-hydrolyzing DNA topoisomerase	GyrA; DNA gyrase subunit A of Haemophilus influenzae	Hae-influ gyrA	"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."	EC 5.6.2.3	.	MTDSIQSSITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLFSMDREGNTANKKYVKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDAPAAMRYTEVRMQKITQALLTDLDKETVNFSPNYDGELMIPDVLPTRIPALLANGSSGIAVGMATNIPPHNLNEVLNGCLAYIDKNEITIDELMQHIPGPDFPTAALINGRKGIEEAYRTGRGKVYVRARATVETNEKGREQIIVSELPYQVNKAKLVEKIAELIREKKIEGISNITDLSNKEGIRIEIDIKRDAVGEVVLNHLYSLTQMQVTFGINMVALDHGQPRLFNLKEIIEAFVLHRREVVTRRSIFELRKARERTHILEGLAVARSNIDEMIAIIRNSKNREEAATSISSRSWTLHSDIINLLDASARPDELEENLGIQGEQYYLSPAQVNAILELRLHRLTGIAFEEVIKEYEELLVKIADLLHILSSAERLMEVIREELEEVKAQFGDDRLTEITAASGDIDLEDLIAQEDVVVTLSHEGYVKYQPLTDYEAQRRGGKGKSATKMKEEDFIEKLLVANTHDTILCFSSRGRLYWLKVYQLPQASRGARGRPIVNILPLQENERITAILPVSAYEEDKFVVMATAGGIVKKIALTEFSRPRSNGIIALNLRDEDELIGVDITDGSNEIMLFSSQGRVVRFAENAVRAMGRLATGVRGIKLALTNDISDDESAVEIEDISDDNAEASLDLNIDKVVSLVVPKGEGAILTATQNGYGKRTQLSEYPTKSRNTKGVISIKVSERNGKVVAATQVEETDQIMLITDAGTLVRTRVSEVSIVGRNTQGVRLIRTADDEHVVSLERVCDADEDDSLEESSSEE	Clinical trial	DNA topoisomerases and their poisoning by anticancer and antibacterial drugs. Chem Biol. 2010 May 28;17(5):421-33.	25	.	.	.	.	.	.	.	.	.	.	.	.	HINF71421:G1GJ1-1292-MON	P43700
TTYPTHI	Haemophilus influenzae Immunoglobulin A1 protease (Hae-influ iga)	P42782	IGA1_HAEIF	Peptidase	iga; IGA1 protease	Hae-influ iga	Virulence factor; cleaves host immunoglobulin A producing intact Fc and Fab fragments.	EC 3.4.21.72	.	MLNKKFKLNFIALTVAYALTPYTEAALVRDDVDYQIFRDFAENKGKFSVGATNVLVKDKNNKDLGTALPNGIPMIDFSVVDVDKRIATLINPQYVVGVKHVSNGVSELHFGNLNGNMNNGNAKAHRDVSSEENRYFSVEKNEYPTKLNGKTVTTEDQTQKRREDYYMPRLDKFVTEVAPIEASTASSDAGTYNDQNKYPAFVRLGSGSQFIYKKGDNYSLILNNHEVGGNNLKLVGDAYTYGIAGTPYKVNHENNGLIGFGNSKEEHSDPKGILSQDPLTNYAVLGDSGSPLFVYDREKGKWLFLGSYDFWAGYNKKSWQEWNIYKSQFTKDVLNKDSAGSLIGSKTDYSWSSNGKTSTITGGEKSLNVDLADGKDKPNHGKSVTFEGSGTLTLNNNIDQGAGGLFFEGDYEVKGTSDNTTWKGAGVSVAEGKTVTWKVHNPQYDRLAKIGKGTLIVEGTGDNKGSLKVGDGTVILKQQTNGSGQHAFASVGIVSGRSTLVLNDDKQVDPNSIYFGFRGGRLDLNGNSLTFDHIRNIDDGARLVNHNMTNASNITITGESLITDPNTITPYNIDAPDEDNPYAFRRIKDGGQLYLNLENYTYYALRKGASTRSELPKNSGESNENWLYMGKTSDEAKRNVMNHINNERMNGFNGYFGEEEGKNNGNLNVTFKGKSEQNRFLLTGGTNLNGDLTVEKGTLFLSGRPTPHARDIAGISSTKKDPHFAENNEVVVEDDWINRNFKATTMNVTGNASLYSGRNVANITSNITASNKAQVHIGYKTGDTVCVRSDYTGYVTCTTDKLSDKALNSFNPTNLRGNVNLTESANFVLGKANLFGTIQSRGNSQVRLTENSHWHLTGNSDVHQLDLANGHIHLNSADNSNNVTKYNTLTVNSLSGNGSFYYLTDLSNKQGDKVVVTKSATGNFTLQVADKTGEPNHNELTLFDASKAQRDHLNVSLVGNTVDLGAWKYKLRNVNGRYDLYNPEVEKRNQTVDTTNITTPNNIQADVPSVPSNNEEIARVDEAPVPPPAPATPSETTETVAENSKQESKTVEKNEQDATETTAQNREVAKEAKSNVKANTQTNEVAQSGSETKETQTTETKETATVEKEEKAKVETEKTQEVPKVTSQVSPKQEQSETVQPQAEPARENDPTVNIKEPQSQTNTTADTEQPAKETSSNVEQPVTESTTVNTGNSVVENPENTTPATTQPTVNSESSNKPKNRHRRSVRSVPHNVEPATTSSNDRSTVALCDLTSTNTNAVLSDARAKAQFVALNVGKAVSQHISQLEMNNEGQYNVWVSNTSMNKNYSSSQYRRFSSKSTQTQLGWDQTISNNVQLGGVFTYVRNSNNFDKATSKNTLAQVNFYSKYYADNHWYLGIDLGYGKFQSKLQTNHNAKFARHTAQFGLTAGKAFNLGNFGITPIVGVRYSYLSNADFALDQARIKVNPISVKTAFAQVDLSYTYHLGEFSVTPILSARYDANQGSGKINVNGYDFAYNVENQQQYNAGLKLKYHNVKLSLIGGLTKAKQAEKQKTAELKLSFSF	Literature-reported	Nontypeable Haemophilus influenzae in carriage and disease: a difference in IgA1 protease activity levels. JAMA. 2002 Apr 3;287(13):1699-705.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P42782
TT2D1J6	Haemophilus influenzae Acetylglucosamine deacetylase (Hae-influ lpxC)	Q4QLF2	LPXC_HAEI8	.	UDP-3-O-acyl-N-acetylglucosamine deacetylase; UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase; Hae-influ UDP-3-O-acyl-GlcNAc deacetylase	Hae-influ lpxC	"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."	EC 3.5.1.108	.	MIKQRTLKQSIKVTGVGLHSGNKVTLTLRPAMPNTGVVYYRTDLNPAVAFPADPNSVRDTMLCTALINDQGVRISTVEHLNAALAGLGIDNIIIEVDAPEIPIMDGSASPFIYLLLDAGIEEQNAAKKFIRIKEYVRVEDGDKWAEFKPYNGFRLDFTIDFDHPAIGKDVRNYEMNFSAQAFVHQISRARTFGFMKDIEYLQSQGLALGGSLDNAIVLDDYRILNEDGLRFKDELVRHKMLDAIGDLYMAGYNIIGDFKAYKSGHGLNNKLLRAVLANQEAWEFVTFEDKEQVPQGYVAPAQVLI	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	17	.	.	.	.	.	.	.	.	.	.	hit00540: Lipopolysaccharide biosynthesis; hit01100: Metabolic pathways	.	.	Q4QLF2
TTWUDYC	Haemophilus influenzae NadR protein (Hae-influ nadR)	P44308	NADR_HAEIN	Nicotinamide ribonucleoside uptake permease	nadR; Transcriptional regulator nadR	Hae-influ nadR	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(+).	.	1LW7	MGFTTGREFHPALRMRAKYNAKYLGTKSEREKYFHLAYNKHTQFLRYQEQIMSKTKEKKVGVIFGKFYPVHTGHINMIYEAFSKVDELHVIVCSDTVRDLKLFYDSKMKRMPTVQDRLRWMQQIFKYQKNQIFIHHLVEDGIPSYPNGWQSWSEAVKTLFHEKHFEPSIVFSSEPQDKAPYEKYLGLEVSLVDPDRTFFNVSATKIRTTPFQYWKFIPKEARPFFAKTVAILGGESSGKSVLVNKLAAVFNTTSAWEYGREFVFEKLGGDEQAMQYSDYPQMALGHQRYIDYAVRHSHKIAFIDTDFITTQAFCIQYEGKAHPFLDSMIKEYPFDVTILLKNNTEWVDDGLRSLGSQKQRQQFQQLLKKLLDKYKVPYIEIESPSYLDRYNQVKAVIEKVLNEEEISELQNTTFPIKGTSQ	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	hin00760: Nicotinate and nicotinamide metabolism; hin01100: Metabolic pathways	.	HINF71421:G1GJ1-803-MON; MetaCyc:MON-8322	P44308
TTXQOZW	Histidine ammonia-lyase (HAL)	P42357	HUTH_HUMAN	Carbon-nitrogen lyase	Histidine ammonialyase; Histidase; HIS	HAL	"Histidine ammonia-lyase activity, histidine catabolic process."	EC 4.3.1.3	.	MPRYTVHVRGEWLAVPCQDAQLTVGWLGREAVRRYIKNKPDNGGFTSVDDAHFLVRRCKGLGLLDNEDRLEVALENNEFVEVVIEGDAMSPDFIPSQPEGVYLYSKYREPEKYIELDGDRLTTEDLVNLGKGRYKIKLTPTAEKRVQKSREVIDSIIKEKTVVYGITTGFGKFARTVIPINKLQELQVNLVRSHSSGVGKPLSPERCRMLLALRINVLAKGYSGISLETLKQVIEMFNASCLPYVPEKGTVGASGDLAPLSHLALGLVGEGKMWSPKSGWADAKYVLEAHGLKPVILKPKEGLALINGTQMITSLGCEAVERASAIARQADIVAALTLEVLKGTTKAFDTDIHALRPHRGQIEVAFRFRSLLDSDHHPSEIAESHRFCDRVQDAYTLRCCPQVHGVVNDTIAFVKNIITTELNSATDNPMVFANRGETVSGGNFHGEYPAKALDYLAIGIHELAAISERRIERLCNPSLSELPAFLVAEGGLNSGFMIAHCTAAALVSENKALCHPSSVDSLSTSAATEDHVSMGGWAARKALRVIEHVEQVLAIELLAACQGIEFLRPLKTTTPLEKVYDLVRSVVRPWIKDRFMAPDIEAAHRLLLEQKVWEVAAPYIEKYRMEHIPESRPLSPTAFSLQFLHKKSTKIPESEDL	Literature-reported	On the nature of the irreversible inhibition of histidine ammonia lyase by cysteine and dioxygen. Bioorg Med Chem. 1996 Jul;4(7):1001-6.	.	EC:4.3	Carbon-nitrogen lyases	PAL/histidase family.	4.3.1.3	Carbon-nitrogen lyases	Aromatic amino acid lyase; N-terminal of Par3 and HAL proteins	PF00221; PF12053	PF00221; Lyase_aromatic; PF12053; Par3_HAL_N_term	.	.	hsa00340: Histidine metabolism; hsa01100: Metabolic pathways	R-HSA-70921: Histidine catabolism	MetaCyc:HS01466-MON	P42357
TTRV5YJ	Hepcidin messenger RNA (HAMP mRNA)	P81172	HEPC_HUMAN	mRNA target	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)	HAMP	"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."	.	4QAE; 3H0T; 2KEF; 1M4F; 1M4E	MALSSQIWAACLLLLLLLASLTSGSVFPQQTGQLAELQPQDRAGARASWMPMFQRRRRRDTHFPICIFCCGCCHRSKCGMCCKT	Literature-reported	Smad1/5 is required for erythropoietin-mediated suppression of hepcidin in mice. Blood. 2017 Jul 6;130(1):73-83.	.	mRNA	mRNA target	.	.	.	Hepcidin	PF06446	PF06446; Hepcidin	.	.	hsa04350: TGF-beta signaling pathway	.	.	P81172
TTPCG5T	Hepcidin (HAMP)	P81172	HEPC_HUMAN	Hepcidin family	Putative liver tumor regressor; PLTR; Liverexpressed antimicrobial peptide 1; LEAP1; Hepcidin20; Hepc25; Hepc20; HAMP	HAMP	"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)."	.	4QAE; 3H0T; 2KEF; 1M4F; 1M4E	MALSSQIWAACLLLLLLLASLTSGSVFPQQTGQLAELQPQDRAGARASWMPMFQRRRRRDTHFPICIFCCGCCHRSKCGMCCKT	Clinical trial	The effects of the anti-hepcidin Spiegelmer NOX-H94 on inflammation-induced anemia in cynomolgus monkeys. Blood. 2013 Mar 21;121(12):2311-5.	21	.	.	.	.	.	.	.	.	.	.	hsa04350: TGF-beta signaling pathway	.	.	P81172
TTS58YO	HAO1 messenger RNA (HAO1 mRNA)	Q9UJM8	HAOX1_HUMAN	.	HAOX1; Glycolate oxidase; GOX	HAO1	"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."	EC 1.1.3.15	.	MLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNRFKLPPQLRMKNFETSTLSFSPEENFGDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRGDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNPLAVSKI	Clinical trial	"Clinical pipeline report, company report or official report of Alnylam Pharmaceuticals."	.	.	.	.	.	.	.	.	.	.	.	hsa00630: Glyoxylate and dicarboxylate metabolism; hsa01100: Metabolic pathways; hsa01200: Carbon metabolism; hsa04146: Peroxisome	R-HSA-389661: Glyoxylate metabolism and glycine degradation; R-HSA-9033241: Peroxisomal protein import	.	Q9UJM8
TT0A11O	2-Hydroxyacid oxidase 1 (HAO1)	Q9UJM8	HAOX1_HUMAN	.	HAOX1; Glycolate oxidase; GO; GOX; Glyoxylate oxidase	HAO1	"Broad substrate specificity (S)-2-hydroxy-acid oxidase that preferentially oxidizes glycolate (PubMed:10777549, PubMed:17669354, PubMed:18215067, PubMed:10978532). The glyoxylate produced by the oxidation of glycolate can then be utilized by alanine-glyoxylate aminotransferase for the peroxisomal synthesis of glycine; this pathway appears to be an important step for the detoxification of glyoxylate which, if allowed to accumulate, may be metabolized to oxalate with formation of kidney stones (PubMed:10978532, PubMed:17669354). Can also catalyze the oxidation of glyoxylate, and long chain hydroxyacids such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate, albeit with much lower catalytic efficiency (PubMed:10777549, PubMed:17669354, PubMed:18215067). Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP), but O2 is believed to be the physiological electron acceptor, leading to the production of H2O2 (PubMed:10777549, PubMed:17669354, PubMed:18215067, PubMed:10978532). Is not active on L-lactate and 2-hydroxybutanoate (PubMed:10777549). {ECO:0000269|PubMed:10777549, ECO:0000269|PubMed:10978532, ECO:0000269|PubMed:17669354, ECO:0000269|PubMed:18215067, ECO:0000303|PubMed:10978532, ECO:0000303|PubMed:17669354}."	EC 1.1.3.15; EC 1.2.3.5	2NZL;2RDT;2RDU;2RDW;2W0U;5QIB;5QIC;5QID;5QIE;5QIF;5QIG;5QIH;6GMB;6GMC;6W44;6W45;6W4C;7M2O;7R4N;7R4O;7R4P	MLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNRFKLPPQLRMKNFETSTLSFSPEENFGDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRGDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNPLAVSKI	Clinical trial	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2023. Adis Insight"	.	.	.	.	.	.	.	.	.	.	.	hsa:54363	R-HSA-389661;R-HSA-9033241;	.	Q9UJM8;
TT21BYA	HCLS1-associated protein X-1 (HAX1)	O00165	HAX1_HUMAN	.	HSP1BP-1; HS1BP1; HS1-binding protein 1; HS1-associating protein X-1; HAX-1	HAX1	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.	.	.	MSLFDLFRGFFGFPGPRSHRDPFFGGMTRDEDDDEEEEEEGGSWGRGNPRFHSPQHPPEEFGFGFSFSPGGGIRFHDNFGFDDLVRDFNSIFSDMGAWTLPSHPPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFGGVLESDARSESPQPAPDWGSQRPFHRFDDVWPMDPHPRTREDNDLDSQVSQEGLGPVLQPQPKSYFKSISVTKITKPDGIVEERRTVVDSEGRTETTVTRHEADSSPRGDPESPRPPALDDAFSILDLFLGRWFRSR	Literature-reported	Kostmann's Disease and HCLS1-Associated Protein X-1 (HAX1). J Clin Immunol. 2017 Feb;37(2):117-122.	.	.	.	HAX1 family.	.	.	.	.	.	.	.	.	.	.	O00165
TTQO71U	Hemoglobin (HB)	P69905	HBA_HUMAN	Pore-forming globin	Hemoglobin subunit alpha; Hemoglobin alpha chain; HBA1; Alpha-globin	HBA2	Involved in oxygen transport from the lung to the various peripheral tissues.	.	6NBD; 6NBC; 6HBW; 6HAL; 6DI4	MVLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR	Successful	Efficacy and safety of total dose infusion of low molecular weight iron dextran in the treatment of iron deficiency anemia during pregnancy. J Coll Physicians Surg Pak. 2008 Jul;18(7):424-7.	34	TC=1.A.107	.	.	.	.	Globin	PF00042	PF00042; Globin	1.A.107.1.1	The Pore-forming Globin (Globin) Family	hsa05143:African trypanosomiasis; hsa05144:Malaria	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	.	P69905
TTM6HK1	Hemoglobin subunit beta (HBB)	P68871	HBB_HUMAN	Pore-forming globin	LVVhemorphin7; Hemoglobin beta chain; Betaglobin; Beta-globin	HBB	Involved in oxygen transport from the lung to the various peripheral tissues.	.	6NBD; 6NBC; 6HBW; 6HAL; 6FQF	MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH	Clinical trial	Preclinical evaluation of efficacy and safety of an improved lentiviral vector for the treatment of beta-thalassemia and sickle cell disease. Curr Gene Ther. 2015;15(1):64-81.	19	TC=1.A.107	.	.	.	.	Globin	PF00042	PF00042; Globin	1.A.107.1.2	The Pore-forming Globin (Globin) Family	hsa05143:African trypanosomiasis; hsa05144:Malaria	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	.	P68871
TT15SL0	Proheparin-binding EGF-like growth factor (HBEGF)	Q99075	HBEGF_HUMAN	Growth factor	Proheparinbinding EGFlike growth factor; Heparinbinding EGFlike growth factor; Heparin-binding EGF-like growth factor; HEGFL; HB-EGF; Diphtheria toxin receptor; DTS; DTR; DT-R	HBEGF	"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."	.	2M8S; 1XDT	MKLLPSVVLKLFLAAVLSALVTGESLERLRRGLAAGTSNPDPPTVSTDQLLPLGGGRDRKVRDLQEADLDLLRVTLSSKPQALATPNKEEHGKRKKKGKGLGKKRDPCLRKYKDFCIHGECKYVKELRAPSCICHPGYHGERCHGLSLPVENRLYTYDHTTILAVVAVVLSSVCLLVIVGLLMFRYHRRGGYDVENEEKVKLGMTNSH	Clinical trial	ClinicalTrials.gov (NCT01279291) Study of Anti-HB-EGF Antibody KHK2866 in Subjects With Advanced Solid Tumors and Ovarian Cancer. U.S. National Institutes of Health.	17	Growth factor	Growth factor	.	.	.	EGF-like domain	PF00008	PF00008; EGF	.	.	hsa04012:ErbB signaling pathway; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa05120:Epithelial cell signaling in Helicobacter pylori infection; hsa05205:Proteoglycans in cancer	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	.	Q99075
TTM42UJ	Hepatitis B virus Capsid protein (HBV C)	P03146	CAPSD_HBVD3	.	Core antigen; Core protein; HBcAg; p21.5	HBV C	"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."	.	.	MDIDPYKEFGATVELLSFLPSDFFPSVRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELMTLATWVGVNLEDPASRDLVVSYVNTNMGLKFRQLLWFHISCLTFGRETVIEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC	Clinical trial	"JNJ-56136379, an HBV Capsid Assembly Modulator, Is Well-Tolerated and Has Antiviral Activity in a Phase 1 Study of Patients With Chronic Infection. Gastroenterology. 2020 Aug;159(2):521-533.e9."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTT4SY6	Hepatitis B virus Polymerase (HBV P)	Q67889	Q67889_HBV	DNA-directed DNA polymerase	Protein P	HBV P	"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."	.	.	MPLSYQHFRKLLLLDDGTGPLEEELPRLADEGLNRRVAEDLNLGNLNVSIPWTHKVGNFTGLYSSTVPVFNPHWKTPSFPNIHLHQDIIKKCEQFVGPLTVNEKRRLQLIMPARFYPKVTKYLPLDKGIKPYYPEHLVNHYFQTRHYLHTLWKAGILYKRETTHSASFCGSPYSWEQDLQHGAESIHQQSSGILSRPPVGSSLQSKHRKSRLGLQSQQGHLARRQQGRSWSIRAGFHPTARRPFGVEPSGSGHTTNFASKSASCLHQSPVRKAAYPSVSTFEKHSSSGHAVELHNLPPNSARSKSERPVFPCWWLQFRNSKPCSDYCLSLIVNLREDWGPCDDHGEHHIRIPRTPARVRGGVFLVDKNPHNTAESRLVVDFSQFSRGNYRVSWPKFAVPNLPSLTNLLSSNLSWLSLDVSAAFYHIPLHPAAMPHLLVGSSGLSRYVARLSSNSRYFNNQHGTMQNLHDSCSRNLYVSLLLLYQTFGRKLHLYSHPIILGFRKIPMAVGLSPFLLAQFTSAICSVVRRAFPHCLGFSYMDDVVLGAKSVQHRESLYTAVTNFLLSLGIHLNPNKTKRWGYSLNFMGYIIGSWGTLPQDHIVQKIKHCFRKLPVNRPIDWKVWQRIVGLLGFAAPFTQCGYPALMPLYACIQAKQAFTFSPTYKAFLSKQYMNLYPVARQRPGLCQVFADATPTGWGLA	Successful	Nucleos(t)ide analogues for hepatitis B virus: strategies for long-term success. Best Pract Res Clin Gastroenterol. 2008;22(6):1081-92.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTS5K1M	Hepatitis B virus Reverse transcriptase (HBV RT)	P03159 (359-602)	DPOL_HBVA3	DNA-directed DNA polymerase	P; HBV reverse transcriptase	HBV RT	"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."	EC 2.7.7.49	.	EHHIRIPRTPARVTGGVFLVDKNPHNTAESRLVVDFSQFSRGISRVSWPKFAVPNLQSLTNLLSSNLSWLSLDVSAAFYHIPLHPAAMPHLLIGSSGLSRYVARLSSNSRINNNQYGTMQNLHDSCSRQLYVSLMLLYKTYGWKLHLYSHPIVLGFRKIPMGVGLSPFLLAQFTSAICSVVRRAFPHCLAFSYMDDVVLGAKSVQHRESLYTAVTNFLLSLGIHLNPNKTKRWGYSLNFMGYII	Successful	Effect of hepatitis B virus reverse transcriptase variations on entecavir treatment response. J Infect Dis. 2014 Sep 1;210(5):701-7.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT6KSF7	Hepatitis B virus Large envelope protein (HBV S)	P03141	HBSAG_HBVA3	Orthohepadnavirus major surface antigen	Major surface antigen; Large surface protein; Large envelope protein; Large S protein; LHB; L-HBsAg; L glycoprotein	HBV S	"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."	.	.	MGGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFGANSNNPDWDFNPVKDDWPAANQVGVGAFGPRLTPPHGGILGWSPQAQGILTTVSTIPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTAFHQTLQDPRVRGLYLPAGGSSSGTVNPAPNIASHISSISARTGDPVTNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGSPVCLGQNSQSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSTTTSTGPCKTCTTPAQGNSMFPSCCCTKPTDGNCTCIPIPSSWAFAKYLWEWASVRFSWLSLLVPFVQWFVGLSPTVWLSAIWMMWYWGPSLYSIVSPFIPLLPIFFCLWVYI	Clinical trial	In vitro stimulation with HBV therapeutic vaccine candidate Nasvac activates B and T cells from chronic hepatitis B patients and healthy donors. Mol Immunol. 2015 Feb;63(2):320-7.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTINUYD	Hepatitis B virus Large envelope protein (HBV S)	P03138	HBSAG_HBVD3	.	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	HBV S	"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."	.	.	MGQNLSTSNPLGFFPDHQLDPAFRANTANPDWDFNPNKDTWPDANKVGAGAFGLGFTPPHGGLLGWSPQAQGILQTLPANPPPASTNRQSGRQPTPLSPPLRNTHPQAMQWNSTTFHQTLQDPRVRGLYFPAGGSSSGTVNPVLTTASPLSSIFSRIGDPALNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSPTSNHSPTSCPPTCPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTCMTTAQGTSMYPSCCCTKPSDGNCTCIPIPSSWAFGKFLWEWASARFSWLSLLVPFVQWFVGLSPTVWLSVIWMMWYWGPSLYSILSPFLPLLPIFFCLWVYI	Clinical trial	"Clinical pipeline report, company report or official report of Vir Biotechnology."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTSJVOI	Hepatitis B virus Large envelope protein messenger RNA (HBV S mRNA)	P03138	HBSAG_HBVD3	.	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	HBV S mRNA	"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."	.	.	MGQNLSTSNPLGFFPDHQLDPAFRANTANPDWDFNPNKDTWPDANKVGAGAFGLGFTPPHGGLLGWSPQAQGILQTLPANPPPASTNRQSGRQPTPLSPPLRNTHPQAMQWNSTTFHQTLQDPRVRGLYFPAGGSSSGTVNPVLTTASPLSSIFSRIGDPALNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSPTSNHSPTSCPPTCPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTCMTTAQGTSMYPSCCCTKPSDGNCTCIPIPSSWAFGKFLWEWASARFSWLSLLVPFVQWFVGLSPTVWLSVIWMMWYWGPSLYSILSPFLPLLPIFFCLWVYI	Clinical trial	"Clinical pipeline report, company report or official report of GlaxoSmithKline."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTVK4ZO	G protein coupled receptor 81 (HCAR1)	Q9BXC0	HCAR1_HUMAN	GPCR rhodopsin	Hydroxycarboxylic acid receptor 1; HCAR1; Gprotein coupled receptor 81; Gprotein coupled receptor 104	HCAR1	Acts as a receptor for L-lactate and mediates its anti- lipolytic effect through a G(i)-protein-mediated pathway.	.	.	MYNGSCCRIEGDTISQVMPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLFNLAVADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAADRYFKVVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIMESANGWHDIMFQLEFFMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVFITCYLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPKFYNKLKICSLKPKQPGHSKTQRPEEMPISNLGRRSCISVANSFQSQSDGQWDPHIVEWH	Literature-reported	Role of GPR81 in lactate-mediated reduction of adipose lipolysis. Biochem Biophys Res Commun. 2008 Dec 19;377(3):987-91.	0	.	.	.	.	.	.	.	.	.	.	hsa04024:cAMP signaling pathway	R-HSA-418594:G alpha (i) signalling events	.	Q9BXC0
TTWNV8U	Nicotinic acid receptor (HCAR2)	Q8TDS4	HCAR2_HUMAN	GPCR rhodopsin	Niacin receptor 1; NIACR1; Hydroxycarboxylic acid receptor 2; HM74A; HCA2; GPR109A; G-protein coupled receptor HM74A; G-protein coupled receptor 109A	HCAR2	"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."	.	.	MNRHHLQDHFLEIDKKNCCVFRDDFIVKVLPPVLGLEFIFGLLGNGLALWIFCFHLKSWKSSRIFLFNLAVADFLLIICLPFLMDNYVRRWDWKFGDIPCRLMLFMLAMNRQGSIIFLTVVAVDRYFRVVHPHHALNKISNRTAAIISCLLWGITIGLTVHLLKKKMPIQNGGANLCSSFSICHTFQWHEAMFLLEFFLPLGIILFCSARIIWSLRQRQMDRHAKIKRAITFIMVVAIVFVICFLPSVVVRIRIFWLLHTSGTQNCEVYRSVDLAFFITLSFTYMNSMLDPVVYYFSSPSFPNFFSTLINRCLQRKMTGEPDNNRSTSVELTGDPNKTRGAPEALMANSGEPWSPSYLGPTSP	Successful	"Hakozaki T, Minwalla L, Zhuang J, Chhoa M, Matsubara A, Miyamoto K, Greatens A, Hillebrand GG, Bissett DL, Boissy RE: The effect of niacinamide on reducing cutaneous pigmentation and suppression of melanosome transfer. Br J Dermatol. 2002 Jul;147(1):20-31."	34	.	.	.	.	.	.	.	.	.	.	hsa04024:cAMP signaling pathway	R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418594:G alpha (i) signalling events	.	Q8TDS4
TT8WFXV	Hydroxycarboxylic acid receptor 3 (HCAR3)	P49019	HCAR3_HUMAN	.	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	HCAR3	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.	.	.	MNRHHLQDHFLEIDKKNCCVFRDDFIAKVLPPVLGLEFIFGLLGNGLALWIFCFHLKSWKSSRIFLFNLAVADFLLIICLPFVMDYYVRRSDWKFGDIPCRLVLFMFAMNRQGSIIFLTVVAVDRYFRVVHPHHALNKISNWTAAIISCLLWGITVGLTVHLLKKKLLIQNGTANVCISFSICHTFRWHEAMFLLEFFLPLGIILFCSARIIWSLRQRQMDRHAKIKRAITFIMVVAIVFVICFLPSVVVRIHIFWLLHTSGTQNCEVYRSVDLAFFITLSFTYMNSMLDPVVYYFSSPSFPNFFSTLINRCLQRKITGEPDNNRSTSVELTGDPNKTRGAPEALIANSGEPWSPSYLGPTSNNHSKKGHCHQEPASLEKQLGCCIE	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	hsa04024: cAMP signaling pathway	R-HSA-3296197: Hydroxycarboxylic acid-binding receptors; R-HSA-418594: G alpha (i) signalling events	.	P49019
TT42OGM	Hematopoietic cell kinase (HCK)	P08631	HCK_HUMAN	Kinase	p61Hck; p59Hck; p59-HCK/p60-HCK; Tyrosine-protein kinase HCK; Hemopoietic cell kinase	HCK	"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."	EC 2.7.10.2	5ZJ6; 5NUH; 5HCK; 5H0H; 5H0G	MGGRSSCEDPGCPRDEERAPRMGCMKSKFLQVGGNTFSKTETSASPHCPVYVPDPTSTIKPGPNSHNSNTPGIREAGSEDIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSLATRKEGYIPSNYVARVDSLETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSYSLSVRDYDPRQGDTVKHYKIRTLDNGGFYISPRSTFSTLQELVDHYKKGNDGLCQKLSVPCMSSKPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDFYTATESQYQQQP	Patented-recorded	Targeted polypharmacology: discovery of dual inhibitors of tyrosine and phosphoinositide kinases. Nat Chem Biol. 2008 Nov;4(11):691-9.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. SRC subfamily.	2.7.10.2	Transferring phosphorus-containing groups	Protein tyrosine kinase; SH2 domain; SH3 domain	PF07714; PF00017; PF00018	PF07714; Pkinase_Tyr; PF00017; SH2; PF00018; SH3_1	.	.	hsa04062: Chemokine signaling pathway; hsa04666: Fc gamma R-mediated phagocytosis; hsa05167: Kaposi sarcoma-associated herpesvirus infection	R-HSA-164944: Nef and signal transduction; R-HSA-2029481: FCGR activation; R-HSA-912631: Regulation of signaling by CBL; R-HSA-9664323: FCGR3A-mediated IL10 synthesis; R-HSA-9664422: FCGR3A-mediated phagocytosis; R-HSA-9674555: Signaling by CSF3 (G-CSF); R-HSA-9705462: Inactivation of CSF3 (G-CSF) signaling; R-HSA-9706374: FLT3 signaling through SRC family kinases	.	P08631
TTNB6UQ	Hyperpolarization cyclic nucleotide-gated channel 1 (HCN1)	O60741	HCN1_HUMAN	Voltage-gated ion channel	Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1; Brain cyclic nucleotide-gated channel 1; BCNG1; BCNG-1	HCN1	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.	.	5U6P; 5U6O	MEGGGKPNSSSNSRDDGNSVFPAKASATGAGPAAAEKRLGTPPGGGGAGAKEHGNSVCFKVDGGGGGGGGGGGGEEPAGGFEDAEGPRRQYGFMQRQFTSMLQPGVNKFSLRMFGSQKAVEKEQERVKTAGFWIIHPYSDFRFYWDLIMLIMMVGNLVIIPVGITFFTEQTTTPWIIFNVASDTVFLLDLIMNFRTGTVNEDSSEIILDPKVIKMNYLKSWFVVDFISSIPVDYIFLIVEKGMDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPLLQDFPPDCWVSLNEMVNDSWGKQYSYALFKAMSHMLCIGYGAQAPVSMSDLWITMLSMIVGATCYAMFVGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADMRQKIHDYYEHRYQGKIFDEENILNELNDPLREEIVNFNCRKLVATMPLFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVITKSSKEMKLTDGSYFGEICLLTKGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLQKFQKDLNTGVFNNQENEILKQIVKHDREMVQAIAPINYPQMTTLNSTSSTTTPTSRMRTQSPPVYTATSLSHSNLHSPSPSTQTPQPSAILSPCSYTTAVCSPPVQSPLAARTFHYASPTASQLSLMQQQPQQQVQQSQPPQTQPQQPSPQPQTPGSSTPKNEVHKSTQALHNTNLTREVRPLSASQPSLPHEVSTLISRPHPTVGESLASIPQPVTAVPGTGLQAGGRSTVPQRVTLFRQMSSGAIPPNRGVPPAPPPPAAALPRESSSVLNTDPDAEKPRFASNL	Literature-reported	Novel blockers of hyperpolarization-activated current with isoform selectivity in recombinant cells and native tissue. Br J Pharmacol. 2012 May;166(2):602-16.	0	TC=1.A.1	.	potassium channel HCN family.	.	.	Cyclic nucleotide-binding domain; Ion transport protein; Ion transport protein N-terminal	PF00027; PF00520; PF08412	PF00027; cNMP_binding; PF00520; Ion_trans; PF08412; Ion_trans_N	1.A.1.5.32	The Voltage-gated Ion Channel (VIC) Superfamily 	hsa04929: GnRH secretion	R-HSA-1296061: HCN channels	.	O60741
TT9EUT4	Hyperpolarization cyclic nucleotide-gated channel 2 (HCN2)	Q9UL51	HCN2_HUMAN	Voltage-gated ion channel	Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2; Brain cyclic nucleotide-gated channel 2; BCNG2; BCNG-2	HCN2	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.	.	3U10; 2MPF	MDARGGGGRPGESPGATPAPGPPPPPPPAPPQQQPPPPPPPAPPPGPGPAPPQHPPRAEALPPEAADEGGPRGRLRSRDSSCGRPGTPGAASTAKGSPNGECGRGEPQCSPAGPEGPARGPKVSFSCRGAASGPAPGPGPAEEAGSEEAGPAGEPRGSQASFMQRQFGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSDFRFYWDFTMLLFMVGNLIIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYIFLIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVMRICNLISMMLLLCHWDGCLQFLVPMLQDFPRNCWVSINGMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKEMKLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHKVQHDLNSGVFNNQENAIIQEIVKYDREMVQQAELGQRVGLFPPPPPPPQVTSAIATLQQAAAMSFCPQVARPLVGPLALGSPRLVRRPPPGPAPAAASPGPPPPASPPGAPASPRAPRTSPYGGLPAAPLAGPALPARRLSRASRPLSASQPSLPHGAPGPAASTRPASSSTPRLGPTPAARAAAPSPDRRDSASPGAAGGLDPQDSARSRLSSNL	Literature-reported	Regulation of gating and rundown of HCN hyperpolarization-activated channels by exogenous and endogenous PIP2. J Gen Physiol. 2006 Nov;128(5):593-604.	0	TC=1.A.1	.	potassium channel HCN family.	.	.	Cyclic nucleotide-binding domain; Ion transport protein; Ion transport protein N-terminal	PF00027; PF00520; PF08412	PF00027; cNMP_binding; PF00520; Ion_trans; PF08412; Ion_trans_N	1.A.1.5.11	The Voltage-gated Ion Channel (VIC) Superfamily 	hsa04024: cAMP signaling pathway; hsa04929: GnRH secretion	R-HSA-1296061: HCN channels	.	Q9UL51
TTQP04A	Hyperpolarization cyclic nucleotide-gated channel 4 (HCN4)	Q9Y3Q4	HCN4_HUMAN	Voltage-gated ion channel	Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4	HCN4	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.	.	6GYO; 6GYN; 4NVP; 4KL1; 4HBN	MDKLPPSMRKRLYSLPQQVGAKAWIMDEEEDAEEEGAGGRQDPSRRSIRLRPLPSPSPSAAAGGTESRSSALGAADSEGPARGAGKSSTNGDCRRFRGSLASLGSRGGGSGGTGSGSSHGHLHDSAEERRLIAEGDASPGEDRTPPGLAAEPERPGASAQPAASPPPPQQPPQPASASCEQPSVDTAIKVEGGAAAGDQILPEAEVRLGQAGFMQRQFGAMLQPGVNKFSLRMFGSQKAVEREQERVKSAGFWIIHPYSDFRFYWDLTMLLLMVGNLIIIPVGITFFKDENTTPWIVFNVVSDTFFLIDLVLNFRTGIVVEDNTEIILDPQRIKMKYLKSWFMVDFISSIPVDYIFLIVETRIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIVNLIGMMLLLCHWDGCLQFLVPMLQDFPDDCWVSINNMVNNSWGKQYSYALFKAMSHMLCIGYGRQAPVGMSDVWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPPDTRQRIHDYYEHRYQGKMFDEESILGELSEPLREEIINFNCRKLVASMPLFANADPNFVTSMLTKLRFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKETKLADGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVALDRLDRIGKKNSILLHKVQHDLNSGVFNYQENEIIQQIVQHDREMAHCAHRVQAAASATPTPTPVIWTPLIQAPLQAAAATTSVAIALTHHPRLPAAIFRPPPGSGLGNLGAGQTPRHLKRLQSLIPSALGSASPASSPSQVDTPSSSSFHIQQLAGFSAPAGLSPLLPSSSSSPPPGACGSPSAPTPSAGVAATTIAGFGHFHKALGGSLSSSDSPLLTPLQPGARSPQAAQPSPAPPGARGGLGLPEHFLPPPPSSRSPSSSPGQLGQPPGELSLGLATGPLSTPETPPRQPEPPSLVAGASGGASPVGFTPRGGLSPPGHSPGPPRTFPSAPPRASGSHGSLLLPPASSPPPPQVPQRRGTPPLTPGRLTQDLKLISASQPALPQDGAQTLRRASPHSSGESMAAFPLFPRAGGGSGGSGSSGGLGPPGRPYGAIPGQHVTLPRKTSSGSLPPPLSLFGARATSSGGPPLTAGPQREPGARPEPVRSKLPSNL	Literature-reported	Novel blockers of hyperpolarization-activated current with isoform selectivity in recombinant cells and native tissue. Br J Pharmacol. 2012 May;166(2):602-16.	0	TC=1.A.1	.	potassium channel HCN family.	.	.	Cyclic nucleotide-binding domain; Ion transport protein; Ion transport protein N-terminal	PF00027; PF00520; PF08412	PF00027; cNMP_binding; PF00520; Ion_trans; PF08412; Ion_trans_N	1.A.1.5.10	The Voltage-gated Ion Channel (VIC) Superfamily 	hsa04024: cAMP signaling pathway; hsa04742: Taste transduction	R-HSA-1296061: HCN channels	.	Q9Y3Q4
TT7LJGM	Coronavirus Nucleocapsid messenger RNA (HCoV Nucleoprotein mRNA)	P15130	NCAP_CVH22	mRNA target	Nc of HCoV (mRNA); N of HCoV (mRNA)	HCoV Nucleoprotein mRNA	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.	.	.	MATVKWADASEPQRGRQGRIPYSLYSPLLVDSEQPWKVIPRNLVPINKKDKNKLIGYWNVQKRFRTRKGKRVDLSPKLHFYYLGTGPHKDAKFRERVEGVVWVAVDGAKTEPTGYGVRRKNSEPEIPHFNQKLPNGVTVVEEPDSRAPSRSQSRSQSRGRGESKPQSRNPSSDRNHNSQDDIMKAVAAALKSLGFDKPQEKDKKSAKTGTPKPSRNQSPASSQTSAKSLARSQSSETKEQKHEMQKPRWKRQPNDDVTSNVTQCFGPRDLDHNFGSAGVVANGVKAKGYPQFAELVPSTAAMLFDSHIVSKESGNTVVLTFTTRVTVPKDHPHLGKFLEELNAFTREMQQHPLLNPSALEFNPSQTSPATAEPVRDEVSIETDIIDEVN	Literature-reported	Molecular cloning and sequence analysis of bovine respiratory syncytial virus mRNA encoding the major nucleocapsid protein. Virology. 1991 Jan;180(1):453-6.	.	mRNA	mRNA target	.	.	.	Coronavirus nucleocapsid protein	PF00937	PF00937; Corona_nucleoca	.	.	.	.	.	.
TTU5HJP	Orexin (HCRT)	O43612	OREX_HUMAN	.	Hypocretin; Hcrt	HCRT	"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."	.	1WSO; 1UVQ; 1R02; 1CQ0	MNLPSTKVSWAAVTLLLLLLLLPPALLSSGAAAQPLPDCCRQKTCSCRLYELLHGAGNHAAGILTLGKRRSGPPGLQGRLQRLLQASGNHAAGILTMGRRAGAEPAPRPCLGRRCSAPAAASVAPGGQSGI	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction	R-HSA-416476:G alpha (q) signalling events	.	O43612
TT60Q8D	Orexin receptor type 1 (HCRTR1)	O43613	OX1R_HUMAN	GPCR rhodopsin	Ox1r; Ox1-R; Ox-1-R; Orexin-1 receptor; Hypocretin receptor type 1; HFGAN72 receptor; 7-transmembrane G-protein coupledneuropeptide receptor	HCRTR1	"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."	.	4ZJC; 4ZJ8	MEPSATPGAQMGVPPGSREPSPVPPDYEDEFLRYLWRDYLYPKQYEWVLIAAYVAVFVVALVGNTLVCLAVWRNHHMRTVTNYFIVNLSLADVLVTAICLPASLLVDITESWLFGHALCKVIPYLQAVSVSVAVLTLSFIALDRWYAICHPLLFKSTARRARGSILGIWAVSLAIMVPQAAVMECSSVLPELANRTRLFSVCDERWADDLYPKIYHSCFFIVTYLAPLGLMAMAYFQIFRKLWGRQIPGTTSALVRNWKRPSDQLGDLEQGLSGEPQPRARAFLAEVKQMRARRKTAKMLMVVLLVFALCYLPISVLNVLKRVFGMFRQASDREAVYACFTFSHWLVYANSAANPIIYNFLSGKFREQFKAAFSCCLPGLGPCGSLKAPSPRSSASHKSLSLQSRCSISKISEHVVLTSVTTVLP	Clinical trial	"Clinical pipeline report, company report or official report of GlaxoSmithKline (2009)."	21	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-416476:G alpha (q) signalling events	.	O43613
TT9N02I	Orexin receptor type 2 (HCRTR2)	O43614	OX2R_HUMAN	GPCR rhodopsin	Ox2r; Ox2-R; Ox-2-R; Orexin-2 receptor; Hypocretin receptor type 2; HFGANP	HCRTR2	"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."	.	5WS3; 5WQC; 4S0V	MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPISILNVLKRVFGMFAHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCCLGVHHRQEDRLTRGRTSTESRKSLTTQISNFDNISKLSEQVVLTSISTLPAANGAGPLQNW	Successful	2014 FDA drug approvals. Nat Rev Drug Discov. 2015 Feb;14(2):77-81.	34	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family); Orexin receptor type 2	PF00001; PF03827	PF00001; 7tm_1; PF03827; Orexin_rec2	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-416476:G alpha (q) signalling events	.	O43614
TTQFZWR	Hepatitis C virus Core protein messenger RNA (HCV Core mRNA)	P26664	POLG_HCV1	mRNA target	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)	HCV Core mRNA	"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."	.	3SU4; 3RC5; 3RC4; 3QGI; 3QGH	MSTNPKPQKKNKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRTWAQPGYPWPLYGNEGCGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSTGLYHVTNDCPNSSIVYEAADAILHTPGCVPCVREGNASRCWVAMTPTVATRDGKLPATQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRRHWTTQGCNCSIYPGHITGHRMAWDMMMNWSPTTALVMAQLLRIPQAILDMIAGAHWGVLAGIAYFSMVGNWAKVLVVLLLFAGVDAETHVTGGSAGHTVSGFVSLLAPGAKQNVQLINTNGSWHLNSTALNCNDSLNTGWLAGLFYHHKFNSSGCPERLASCRPLTDFDQGWGPISYANGSGPDQRPYCWHYPPKPCGIVPAKSVCGPVYCFTPSPVVVGTTDRSGAPTYSWGENDTDVFVLNNTRPPLGNWFGCTWMNSTGFTKVCGAPPCVIGGAGNNTLHCPTDCFRKHPDATYSRCGSGPWITPRCLVDYPYRLWHYPCTINYTIFKIRMYVGGVEHRLEAACNWTRGERCDLEDRDRSELSPLLLTTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSSIASWAIKWEYVVLLFLLLADARVCSCLWMMLLISQAEAALENLVILNAASLAGTHGLVSFLVFFCFAWYLKGKWVPGAVYTFYGMWPLLLLLLALPQRAYALDTEVAASCGGVVLVGLMALTLSPYYKRYISWCLWWLQYFLTRVEAQLHVWIPPLNVRGGRDAVILLMCAVHPTLVFDITKLLLAVFGPLWILQASLLKVPYFVRVQGLLRFCALARKMIGGHYVQMVIIKLGALTGTYVYNHLTPLRDWAHNGLRDLAVAVEPVVFSQMETKLITWGADTAACGDIINGLPVSARRGREILLGPADGMVSKGWRLLAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPVVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETITLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQSGENLPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEITLTHPVTKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCVVIVGRVVLSGKPAIIPDREVLYREFDEMEECSQHLPYIEQGMMLAEQFKQKALGLLQTASRQAEVIAPAVQTNWQKLETFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSPLTTSQTLLFNILGGWVAAQLAAPGAATAFVGAGLAGAAIGSVGLGKVLIDILAGYGAGVAGALVAFKIMSGEVPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWISSECTTPCSGSWLRDIWDWICEVLSDFKTWLKAKLMPQLPGIPFVSCQRGYKGVWRVDGIMHTRCHCGAEITGHVKNGTMRIVGPRTCRNMWSGTFPINAYTTGPCTPLPAPNYTFALWRVSAEEYVEIRQVGDFHYVTGMTTDNLKCPCQVPSPEFFTELDGVRLHRFAPPCKPLLREEVSFRVGLHEYPVGSQLPCEPEPDVAVLTSMLTDPSHITAEAAGRRLARGSPPSVASSSASQLSAPSLKATCTANHDSPDAELIEANLLWRQEMGGNITRVESENKVVILDSFDPLVAEEDEREISVPAEILRKSRRFAQALPVWARPDYNPPLVETWKKPDYEPPVVHGCPLPPPKSPPVPPPRKKRTVVLTESTLSTALAELATRSFGSSSTSGITGDNTTTSSEPAPSGCPPDSDAESYSSMPPLEGEPGDPDLSDGSWSTVSSEANAEDVVCCSMSYSWTGALVTPCAAEEQKLPINALSNSLLRHHNLVYSTTSRSACQRQKKVTFDRLQVLDSHYQDVLKEVKAAASKVKANLLSVEEACSLTPPHSAKSKFGYGAKDVRCHARKAVTHINSVWKDLLEDNVTPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVTKLPLAVMGSSYGFQYSPGQRVEFLVQAWKSKKTPMGFSYDTRCFDSTVTESDIRTEEAIYQCCDLDPQARVAIKSLTERLYVGGPLTNSRGENCGYRRCRASGVLTTSCGNTLTCYIKARAACRAAGLQDCTMLVCGDDLVVICESAGVQEDAASLRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDGAGKRVYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMFAPTLWARMILMTHFFSVLIARDQLEQALDCEIYGACYSIEPLDLPPIIQRLHGLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRARSVRARLLARGGRAAICGKYLFNWAVRTKLKLTPIAAAGQLDLSGWFTAGYSGGDIYHSVSHARPRWIWFCLLLLAAGVGIYLLPNR	Patented-recorded	"US patent application no. 6,391,542, Compositions and methods for treatment of Hepatitis C virus-associated diseases."	0	mRNA	mRNA target	.	.	.	Flavivirus DEAD domain ; Hepatitis C virus capsid protein; Hepatitis C virus core protein; Hepatitis C virus envelope glycoprotein E1; Hepatitis C virus non-structural protein E2/NS1; Hepatitis C virus non-structural protein NS2; Hepatitis C virus non-structural protein NS4a; Hepatitis C virus non-structural protein NS4b; Hepatitis C virus non-structural 5a protein membrane anchor; Hepatitis C virus non-structural 5a zinc finger domain; Hepatitis C virus non-structural 5a domain 1b; HCV NS5a protein C-terminal region; Hepatitis C virus NS3 protease; Viral RNA dependent RNA polymerase	PF07652; PF01543; PF01542; PF01539; PF01560; PF01538; PF01006; PF01001; PF01506; PF08300; PF08301; PF12941; PF02907; PF00998	PF07652; Flavi_DEAD; PF01543; HCV_capsid; PF01542; HCV_core; PF01539; HCV_env; PF01560; HCV_NS1; PF01538; HCV_NS2; PF01006; HCV_NS4a; PF01001; HCV_NS4b; PF01506; HCV_NS5a; PF08300; HCV_NS5a_1a; PF08301; HCV_NS5a_1b; PF12941; HCV_NS5a_C; PF02907; Peptidase_S29; PF00998; RdRP_3	.	.	.	.	.	.
TTDBG95	Hepatitis C virus Envelope glycoprotein E2 (HCV NS1)	P26662 (384-746)	POLG_HCV1	.	Hepacivirus polyprotein	HCV NS1	NS5B is an RNA-dependent RNA polymerase that plays an essential role in the virus replication.	.	3SU4; 3RC5; 3RC4; 3QGI; 3QGH	ETHVTGGSAGHTVSGFVSLLAPGAKQNVQLINTNGSWHLNSTALNCNDSLNTGWLAGLFYHHKFNSSGCPERLASCRPLTDFDQGWGPISYANGSGPDQRPYCWHYPPKPCGIVPAKSVCGPVYCFTPSPVVVGTTDRSGAPTYSWGENDTDVFVLNNTRPPLGNWFGCTWMNSTGFTKVCGAPPCVIGGAGNNTLHCPTDCFRKHPDATYSRCGSGPWITPRCLVDYPYRLWHYPCTINYTIFKIRMYVGGVEHRLEAACNWTRGERCDLEDRDRSELSPLLLTTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSSIASWAIKWEYVVLLFLLLADARVCSCLWMMLLISQAEA	Clinical trial	Human monoclonal antibody MBL-HCV1 delays HCV viral rebound following liver transplantation: a randomized controlled study. Am J Transplant. 2013 Apr;13(4):1047-54.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYO7TW	Hepatitis C virus Protease NS2-3/3 (HCV NS2-3/3)	P26662 (810-1657)	POLG_HCV1	.	HCV p23/p70	HCV NS2-3/3	NS5B is an RNA-dependent RNA polymerase that plays an essential role in the virus replication.	EC 3.4.-.-	3SU4; 3RC5; 3RC4; 3QGI; 3QGH	LDTEVAASCGGVVLVGLMALTLSPYYKRYISWCLWWLQYFLTRVEAQLHVWIPPLNVRGGRDAVILLMCAVHPTLVFDITKLLLAVFGPLWILQASLLKVPYFVRVQGLLRFCALARKMIGGHYVQMVIIKLGALTGTYVYNHLTPLRDWAHNGLRDLAVAVEPVVFSQMETKLITWGADTAACGDIINGLPVSARRGREILLGPADGMVSKGWRLLAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPVVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETITLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQSGENLPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEITLTHPVTKYIMTCMSADLEVV	Literature-reported	Protease inhibitors as antiviral agents. Clin Microbiol Rev. 1998 Oct;11(4):614-27.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTWXB3E	Hepatitis C virus NS3 helicase (HCV NS3)	P26664 (1027-1657)	POLG_HCV1	Peptidase	HCV Hepacivirin; HCV NS3P; HCV p70	HCV NS3	"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)."	EC 3.4.21.98	3SU4; 3RC5; 3RC4; 3QGI; 3QGH	APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPVVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETITLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQSGENLPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEITLTHPVTKYIMTCMSADLEVVT	Successful	HCV Drug Resistance Challenges in Japan: The Role of Pre-Existing Variants and Emerging Resistant Strains in Direct Acting Antiviral Therapy	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT20AHC	Hepatitis C virus NS3 helicase messenger RNA (HCV NS3 mRNA)	P26664 (1027-1657)	POLG_HCV1	.	HCV Hepacivirin mRNA; HCV NS3P mRNA; HCV p70 Mrna	HCV NS3 mRNA	"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)."	EC 3.4.21.98	3SU4; 3RC5; 3RC4; 3QGI; 3QGH	APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPVVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETITLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQSGENLPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEITLTHPVTKYIMTCMSADLEVVT	Discontinued	Design and development of antisense drugs. Expert Opin. Drug Discov. 2008 3(10):1189-1207.	4	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHC7JD	Hepatitis C virus Serine protease NS3/4A (HCV NS3/4A)	P26664 (1027-1711)	POLG_HCV1	.	HCV Hepacivirin/NS4A; HCV NS3P/NS4A; HCV p70/NS4A	HCV NS3/4A	"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)."	.	3SU4; 3RC5; 3RC4; 3QGI; 3QGH	APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTAAQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPVVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGSPITYSTYGKFLADGGCSGGAYDIIICDECHSTDATSILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETITLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLEFWEGVFTGLTHIDAHFLSQTKQSGENLPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEITLTHPVTKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCVVIVGRVVLSGKPAIIPDREVLYREFDEMEEC	Successful	Radium 223 dichloride for prostate cancer treatment. Drug Des Devel Ther. 2017 Sep 6;11:2643-2651.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTRHUKY	Hepatitis C virus Serine protease NS4A (HCV NS4A)	P26664 (1658-1711)	POLG_HCV1	.	HCV p8	HCV NS4A	"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)."	.	3SU4; 3RC5; 3RC4; 3QGI; 3QGH	STWVLVGGVLAALAAYCLSTGCVVIVGRVVLSGKPAIIPDREVLYREFDEMEECSQHLPYIEQGMMLAEQFKQKALGLLQTASRQAEVIAPAVQTNWQKLETFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSPLTTSQTLLFNILGGWVAAQLAAPGAATAFVGAGLAGAAIGSVGLGKVLIDILAGYGAGVAGALVAFKIMSGEVPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWISSECTTPC	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTALKDS	Hepatitis C virus Non-structural 4B (HCV NS4B)	P26664 (1712-1972)	POLG_HCV1	Hepacivirus polyprotein	HCV p27	HCV NS4B	"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)."	.	3SU4; 3RC5; 3RC4; 3QGI; 3QGH	SQHLPYIEQGMMLAEQFKQKALGLLQTASRQAEVIAPAVQTNWQKLETFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSPLTTSQTLLFNILGGWVAAQLAAPGAATAFVGAGLAGAAIGSVGLGKVLIDILAGYGAGVAGALVAFKIMSGEVPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWISSECTTPC	Clinical trial	The hepatitis C virus (HCV) NS4B RNA binding inhibitor clemizole is highly synergistic with HCV protease inhibitors. J Infect Dis. 2010 Jul 1;202(1):65-74.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTCJ2X8	Hepatitis C virus Non-structural 5A (HCV NS5A)	P26662 (1973-2420)	POLG_HCV1	Hepacivirus polyprotein	HCV NS5A	HCV NS5A	"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)."	.	3SU4; 3RC5; 3RC4; 3QGI; 3QGH	SGSWLRDIWDWICEVLSDFKTWLKAKLMPQLPGIPFVSCQRGYKGVWRVDGIMHTRCHCGAEITGHVKNGTMRIVGPRTCRNMWSGTFPINAYTTGPCTPLPAPNYTFALWRVSAEEYVEIRQVGDFHYVTGMTTDNLKCPCQVPSPEFFTELDGVRLHRFAPPCKPLLREEVSFRVGLHEYPVGSQLPCEPEPDVAVLTSMLTDPSHITAEAAGRRLARGSPPSVASSSASQLSAPSLKATCTANHDSPDAELIEANLLWRQEMGGNITRVESENKVVILDSFDPLVAEEDEREISVPAEILRKSRRFAQALPVWARPDYNPPLVETWKKPDYEPPVVHGCPLPPPKSPPVPPPRKKRTVVLTESTLSTALAELATRSFGSSSTSGITGDNTTTSSEPAPSGCPPDSDAESYSSMPPLEGEPGDPDLSDGSWSTVSSEANAEDVVCC	Successful	2017 FDA drug approvals.Nat Rev Drug Discov. 2018 Feb;17(2):81-85. 	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMVBWH	Hepatitis C virus RNA-directed RNA polymerase (HCV NS5B)	P26664 (2421-3011)	POLG_HCV1	Peptidase	HCV NS5B; HCV p68	HCV NS5B	"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)."	EC 2.7.7.48	3SU4; 3RC5; 3RC4; 3QGI; 3QGH	SMSYSWTGALVTPCAAEEQKLPINALSNSLLRHHNLVYSTTSRSACQRQKKVTFDRLQVLDSHYQDVLKEVKAAASKVKANLLSVEEACSLTPPHSAKSKFGYGAKDVRCHARKAVTHINSVWKDLLEDNVTPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVTKLPLAVMGSSYGFQYSPGQRVEFLVQAWKSKKTPMGFSYDTRCFDSTVTESDIRTEEAIYQCCDLDPQARVAIKSLTERLYVGGPLTNSRGENCGYRRCRASGVLTTSCGNTLTCYIKARAACRAAGLQDCTMLVCGDDLVVICESAGVQEDAASLRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDGAGKRVYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMFAPTLWARMILMTHFFSVLIARDQLEQALDCEIYGACYSIEPLDLPPIIQRLHGLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRARSVRARLLARGGRAAICGKYLFNWAVRTKLKLTPIAAAGQLDLSGWFTAGYSGGDIYHSVSHARPRWIWFCLLLLAAGVGIYLLPNR	Successful	Radium 223 dichloride for prostate cancer treatment. Drug Des Devel Ther. 2017 Sep 6;11:2643-2651.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTLJWK4	Hepatitis C virus Protein p7 (HCV p7)	P26664 (747-809)	POLG_HCV1	.	HCV p7	HCV p7	"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)."	.	3SU4; 3RC5; 3RC4; 3QGI; 3QGH	ALENLVILNAASLAGTHGLVSFLVFFCFAWYLKGKWVPGAVYTFYGMWPLLLLLLALPQRAYA	Literature-reported	Systematic identification of anti-interferon function on hepatitis C virus genome reveals p7 as an immune evasion protein. Proc Natl Acad Sci U S A. 2017 Feb 21;114(8):2018-2023.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNDHVE	Cytomegalovirus 65kDa phosphoprotein (HCV UL83)	P06725	PP65_HCMVA	Herpesviridae pp65	pp65; UL83; Tegument protein UL83; Phosphoprotein UL83; 65 kDa phosphoprotein; 65 kDa matrix phosphoprotein	HCV UL83	"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."	.	3GSO; 2X4T; 2X4R	MESRGRRCPEMISVLGPISGHVLKAVFSRGDTPVLPHETRLLQTGIHVRVSQPSLILVSQYTPDSTPCHRGDNQLQVQHTYFTGSEVENVSVNVHNPTGRSICPSQEPMSIYVYALPLKMLNIPSINVHHYPSAAERKHRHLPVADAVIHASGKQMWQARLTVSGLAWTRQQNQWKEPDVYYTSAFVFPTKDVALRHVVCAHELVCSMENTRATKMQVIGDQYVKVYLESFCEDVPSGKLFMHVTLGSDVEEDLTMTRNPQPFMRPHERNGFTVLCPKNMIIKPGKISHIMLDVAFTSHEHFGLLCPKSIPGLSISGNLLMNGQQIFLEVQAIRETVELRQYDPVAALFFFDIDLLLQRGPQYSEHPTFTSQYRIQGKLEYRHTWDRHDEGAAQGDDDVWTSGSDSDEELVTTERKTPRVTGGGAMAGASTSAGRKRKSASSATACTSGVMTRGRLKAESTVAPEEDTDEDSDNEIHNPAVFTWPPWQAGILARNLVPMVATVQGQNLKYQEFFWDANDIYRIFAELEGVWQPAAQPKRRRHRQDALPGPCIASTPKKHRG	Clinical trial	National Cancer Institute Drug Dictionary (drug id 599982).	21	.	.	.	.	.	.	.	.	.	.	.	R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	.
TT6R7JZ	Histone deacetylase 1 (HDAC1)	Q13547	HDAC1_HUMAN	Carbon-nitrogen hydrolase	RPD3L1; HD1	HDAC1	"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)."	EC 3.5.1.98	5ICN; 4BKX; 1TYI	MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA	Successful	Protein methyltransferases as a target class for drug discovery. Nat Rev Drug Discov. 2009 Sep;8(9):724-32.	34	EC:3.5	Carbon nitrogen hydrolase	histone deacetylase family. HD type 1 subfamily.	3.5.1.98	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Histone deacetylase domain	PF00850	PF00850; Hist_deacetyl	.	.	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	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	.	Q13547
TTYHPU6	Histone deacetylase 10 (HDAC10)	Q969S8	HDA10_HUMAN	Carbon-nitrogen hydrolase	Polyamine deacetylase HDAC10; HD10	HDAC10	"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."	EC 3.5.1.48	.	MGTALVYHEDMTATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAVLEGGYHLESLAESVCMTVQTLLGDPAPPLSGPMAPCQSALESIQSARAAQAPHWKSLQQQDVTAVPMSPSSHSPEGRPPPLLPGGPVCKAAASAPSSLLDQPCLCPAPSVRTAVALTTPDITLVLPPDVIQQEASALREETEAWARPHESLAREEALTALGKLLYLLDGMLDGQVNSGIAATPASAAAATLDVAVRRGLSHGAQRLLCVALGQLDRPPDLAHDGRSLWLNIRGKEAAALSMFHVSTPLPVMTGGFLSCILGLVLPLAYGFQPDLVLVALGPGHGLQGPHAALLAAMLRGLAGGRVLALLEENSTPQLAGILARVLNGEAPPSLGPSSVASPEDVQALMYLRGQLEPQWKMLQCHPHLVA	Patented-recorded	HDAC inhibitors: a 2013-2017 patent survey.Expert Opin Ther Pat. 2018 Apr 19:1-17.	15.5	EC:3.5	.	histone deacetylase family. HD type 2 subfamily.	3.5.1.48 	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Histone deacetylase domain	PF00850	PF00850; Hist_deacetyl	.	.	hsa04613: Neutrophil extracellular trap formation; hsa05034: Alcoholism; hsa05203: Viral carcinogenesis	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-350054: Notch-HLH transcription pathway	.	Q969S8
TT8K17W	Histone deacetylase 11 (HDAC11)	Q96DB2	HDA11_HUMAN	Carbon-nitrogen hydrolase	HD11	HDAC11	"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)."	EC 3.5.1.98	.	MLHTTQLYQHVPETRWPIVYSPRYNITFMGLEKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVIFLPNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNLFGLGLIGPESPSVSAQNSDTPLLPPAVP	Patented-recorded	HDAC inhibitors: a 2013-2017 patent survey.Expert Opin Ther Pat. 2018 Apr 19:1-17.	15.5	EC:3.5	Histone deacetylase family	histone deacetylase family.	3.5.1.98	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Histone deacetylase domain	PF00850	PF00850; Hist_deacetyl	.	.	hsa05034:Alcoholism; hsa05203:Viral carcinogenesis	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-350054: Notch-HLH transcription pathway	.	Q96DB2
TTSHTOI	Histone deacetylase 2 (HDAC2)	Q92769	HDAC2_HUMAN	Carbon-nitrogen hydrolase	HD2	HDAC2	"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)."	EC 3.5.1.98	6G3O; 5IX0; 5IWG; 4LY1; 4LXZ	MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP	Clinical trial	"A phase I pharmacokinetic and pharmacodynamic study of CHR-3996, an oral class I selective histone deacetylase inhibitor in refractory solid tumors. Clin Cancer Res. 2012 May 1;18(9):2687-94."	17	EC:3.5	Carbon nitrogen hydrolase	histone deacetylase family. HD type 1 subfamily.	3.5.1.98	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Histone deacetylase domain	PF00850	PF00850; Hist_deacetyl	.	.	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	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	.	Q92769
TTCKXRW	HUMAN histone deacetylase 2 (HDAC2)	Q92769	HDAC2_HUMAN	Carbon-nitrogen hydrolase	HD2	HDAC2	"Human protein histone deacetylase 2 interacts with SARS-CoV-2 Nsp5 protein with high significance, which indicates HDAC2 as a potential therapeutic target."	EC 3.5.1.98	6G3O; 5IX0; 5IWG; 4LY1; 4LXZ	MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa04110: Cell cycle; hsa04213: Longevity regulating pathway - multiple species; hsa04330: Notch signaling pathway; hsa04613: Neutrophil extracellular trap formation; hsa04919: Thyroid hormone signaling pathway; hsa05016: Huntington disease; hsa05031: Amphetamine addiction; hsa05034: Alcoholism; hsa05165: Human papillomavirus infection; 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	"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-350054: Notch-HLH transcription pathway; R-HSA-427389: ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression; R-HSA-427413: NoRC negatively regulates rRNA expression; R-HSA-4551638: SUMOylation of chromatin organization proteins; R-HSA-6804758: Regulation of TP53 Activity through Acetylation; R-HSA-73762: RNA Polymerase I Transcription Initiation; R-HSA-8943724: Regulation of PTEN gene transcription; R-HSA-9022692: Regulation of MECP2 expression and activity; R-HSA-9022699: MECP2 regulates neuronal receptors and channels; R-HSA-9615017: FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes; R-HSA-9619665: EGR2 and SOX10-mediated initiation of Schwann cell myelination; R-HSA-9679191: Potential therapeutics for SARS; R-HSA-9701898: STAT3 nuclear events downstream of ALK signaling; R-HSA-983231: Factors involved in megakaryocyte development and platelet production"	.	Q92769
TT4YWTO	Histone deacetylase 3 (HDAC3)	O15379	HDAC3_HUMAN	Carbon-nitrogen hydrolase	SMAP45; RPD32; RPD3-2; HD3	HDAC3	"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."	EC 3.5.1.98	4A69	MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI	Clinical trial	"A phase I pharmacokinetic and pharmacodynamic study of CHR-3996, an oral class I selective histone deacetylase inhibitor in refractory solid tumors. Clin Cancer Res. 2012 May 1;18(9):2687-94."	17	EC:3.5	Carbon-nitrogen hydrolase	histone deacetylase family. HD type 1 subfamily.	3.5.1.98	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Histone deacetylase domain	PF00850	PF00850; Hist_deacetyl	.	.	hsa04919:Thyroid hormone signaling pathway; hsa05034:Alcoholism; hsa05203:Viral carcinogenesis	R-HSA-1368071: NR1D1 (REV-ERBA) represses gene expression; R-HSA-193670: p75NTR negatively regulates cell cycle via SC1; R-HSA-1989781: PPARA activates gene expression; R-HSA-2122947: NOTCH1 Intracellular Domain Regulates Transcription; R-HSA-2151201: Transcriptional activation of mitochondrial biogenesis; 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-350054: Notch-HLH transcription pathway; R-HSA-381340: Transcriptional regulation of white adipocyte differentiation; R-HSA-390471: Association of TriC/CCT with target proteins during biosynthesis; R-HSA-400206: Regulation of lipid metabolism by PPARalpha; R-HSA-400253: Circadian Clock; R-HSA-5617472: Activation of anterior HOX genes in hindbrain development during early embryogenesis; R-HSA-8940973: RUNX2 regulates osteoblast differentiation; R-HSA-8943724: Regulation of PTEN gene transcription; R-HSA-9022537: Loss of MECP2 binding ability to the NCoR/SMRT complex; R-HSA-9022692: Regulation of MECP2 expression and activity; R-HSA-9029569: NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux; R-HSA-9609690: HCMV Early Events; R-HSA-9701898: STAT3 nuclear events downstream of ALK signaling; R-HSA-9707564: Cytoprotection by HMOX1; R-HSA-9707616: Heme signaling	.	O15379
TTTQGH8	Histone deacetylase 4 (HDAC4)	P56524	HDAC4_HUMAN	Carbon-nitrogen hydrolase	KIAA0288; HD4	HDAC4	"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)."	EC 3.5.1.98	6FYZ; 5ZOP; 5ZOO; 5A2S; 4CBY	MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL	Clinical trial	Wikipedia: Quisinostat	21	EC:3.5	Carbon nitrogen hydrolase	histone deacetylase family. HD type 2 subfamily.	3.5.1.98	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Glutamine rich N terminal domain of histone deacetylase 4; Histone deacetylase domain	PF12203; PF00850	PF12203; HDAC4_Gln; PF00850; Hist_deacetyl	.	.	hsa05034:Alcoholism; hsa05169:Epstein-Barr virus infection; hsa05203:Viral carcinogenesis; hsa05206:MicroRNAs in cancer	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	.	P56524
TTUELN5	Histone deacetylase 5 (HDAC5)	Q9UQL6	HDAC5_HUMAN	Carbon-nitrogen hydrolase	KIAA0600; HD5; Antigen NY-CO-9	HDAC5	"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)."	EC 3.5.1.98	5UWI	MNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGGGGGGSPSPVELRGALVGSVDPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSSIPGCLLGVALEGDGSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQLQLGKILTKTGELPRQPTTHPEETEEELTEQQEVLLGEGALTMPREGSTESESTQEDLEEEDEEDDGEEEEDCIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAGETEEAETVSAMALLSVGAEQAQAAAAREHSPRPAEEPMEQEPAL	Patented-recorded	HDAC inhibitors: a 2013-2017 patent survey.Expert Opin Ther Pat. 2018 Apr 19:1-17.	15.5	EC:3.5	.	histone deacetylase family. HD type 2 subfamily.	3.5.1.98	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Glutamine rich N terminal domain of histone deacetylase 4; Histone deacetylase domain	PF12203; PF00850	PF12203; HDAC4_Gln; PF00850; Hist_deacetyl	.	.	hsa04371: Apelin signaling pathway; hsa04613: Neutrophil extracellular trap formation; hsa05034: Alcoholism; hsa05203: Viral carcinogenesis; hsa05206: MicroRNAs in cancer	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-350054: Notch-HLH transcription pathway; R-HSA-8943724: Regulation of PTEN gene transcription	.	Q9UQL6
TT5ZKDI	Histone deacetylase 6 (HDAC6)	Q9UBN7	HDAC6_HUMAN	Carbon-nitrogen hydrolase	KIAA0901; JM21; HD6	HDAC6	"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)."	EC 3.5.1.98	6CEF; 6CEE; 6CED; 6CEC; 6CEA	MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH	Clinical trial	Promising therapies in multiple myeloma. Blood. 2015 July 16; 126(3): 300-310.	19	EC:3.5	Carbon nitrogen hydrolase	histone deacetylase family. HD type 2 subfamily.	3.5.1.98	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Histone deacetylase domain; Zn-finger in ubiquitin-hydrolases and other protein	PF00850; PF02148	PF00850; Hist_deacetyl; PF02148; zf-UBP	.	.	hsa05034:Alcoholism; hsa05203:Viral carcinogenesis	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	MetaCyc:HS01799-MON	Q9UBN7
TTMUEK1	Histone deacetylase 7 (HDAC7)	Q8WUI4	HDAC7_HUMAN	Carbon-nitrogen hydrolase	Histone deacetylase 7A; HDAC7A; HD7a; HD7	HDAC7	"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)."	EC 3.5.1.98	3ZNS; 3ZNR; 3C10; 3C0Z; 3C0Y	MDLRVGQRPPVEPPPEPTLLALQRPQRLHHHLFLAGLQQQRSVEPMRLSMDTPMPELQVGPQEQELRQLLHKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPNSPGIPYRTLEPLETEGATRSMLSSFLPPVPSLPSDPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPILGSEALLGQRLRLQETSVAPFALPTVSLLPAITLGLPAPARADSDRRTHPTLGPRGPILGSPHTPLFLPHGLEPEAGGTLPSRLQPILLLDPSGSHAPLLTVPGLGPLPFHFAQSLMTTERLSGSGLHWPLSRTRSEPLPPSATAPPPPGPMQPRLEQLKTHVQVIKRSAKPSEKPRLRQIPSAEDLETDGGGPGQVVDDGLEHRELGHGQPEARGPAPLQQHPQVLLWEQQRLAGRLPRGSTGDTVLLPLAQGGHRPLSRAQSSPAAPASLSAPEPASQARVLSSSETPARTLPFTTGLIYDSVMLKHQCSCGDNSRHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQQSKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGNRVDPLSEEGWKQKPNLNAIRSLEAVIRVHSKYWGCMQRLASCPDSWVPRVPGADKEEVEAVTALASLSVGILAEDRPSEQLVEEEEPMNL	Patented-recorded	HDAC inhibitors: a 2013-2017 patent survey.Expert Opin Ther Pat. 2018 Apr 19:1-17.	15.5	EC:3.5	.	histone deacetylase family. HD type 2 subfamily.	3.5.1.98	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Histone deacetylase domain	PF00850	PF00850; Hist_deacetyl	.	.	hsa04613: Neutrophil extracellular trap formation; hsa05034: Alcoholism; hsa05203: Viral carcinogenesis	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-3108214: SUMOylation of DNA damage response and repair proteins; R-HSA-350054: Notch-HLH transcription pathway; R-HSA-8943724: Regulation of PTEN gene transcription	.	Q8WUI4
TTT6LFV	Histone deacetylase 8 (HDAC8)	Q9BY41	HDAC8_HUMAN	Carbon-nitrogen hydrolase	Histone deacetylase-8; HDACL1; HD8; CDA07	HDAC8	"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)."	EC 3.5.1.98	6HSK; 5VI6; 5THV; 5THU; 5THT	MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV	Clinical trial	HDAC inhibitors: a 2013-2017 patent survey.Expert Opin Ther Pat. 2018 Apr 19:1-17.	15.5	EC:3.5	Carbon-nitrogen hydrolase	histone deacetylase family. HD type 1 subfamily.	3.5.1.98	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Histone deacetylase domain	PF00850	PF00850; Hist_deacetyl	.	.	hsa05034:Alcoholism; hsa05203:Viral carcinogenesis	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	.	Q9BY41
TT8M4E1	Histone deacetylase 9 (HDAC9)	Q9UKV0	HDAC9_HUMAN	Carbon-nitrogen hydrolase	MITR; MEF2-interacting transcription repressor MITR; KIAA0744; Histone deacetylase-related protein; Histone deacetylase 7B; HDRP; HDAC7B; HDAC7; HD9; HD7b	HDAC9	"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)."	EC 3.5.1.98	.	MHSMISSVDVKSEVPVGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVSRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDAKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNVVTSFKKRMFEVTESSVSSSSPGSGPSSPNNGPTGSVTENETSVLPPTPHAEQMVSQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSQLNASNSLKEKQKCETQTLRQGVPLPGQYGGSIPASSSHPHVTLEGKPPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQAMQEDRAPSSGNSTRSDSSACVDDTLGQVGAVKVKEEPVDSDEDAQIQEMESGEQAAFMQQPFLEPTHTRALSVRQAPLAAVGMDGLEKHRLVSRTHSSPAASVLPHPAMDRPLQPGSATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSMSLKFS	Patented-recorded	HDAC inhibitors: a 2013-2017 patent survey.Expert Opin Ther Pat. 2018 Apr 19:1-17.	15.5	EC:3.5	.	histone deacetylase family. HD type 2 subfamily.	3.5.1.98	"Acting on carbon-nitrogen bonds, other than peptide bonds"	Glutamine rich N terminal domain of histone deacetylase 4; Histone deacetylase domain	PF12203; PF00850	PF12203; HDAC4_Gln; PF00850; Hist_deacetyl	.	.	hsa04613: Neutrophil extracellular trap formation; hsa05034: Alcoholism; hsa05203: Viral carcinogenesis	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-350054: Notch-HLH transcription pathway	.	Q9UKV0
TTV9GOF	Histidine decarboxylase (HDC)	P19113	DCHS_HUMAN	Carbon-carbon lyase	Human histidine decarboxylase	HDC	Catalyzes the biosynthesis of histamine from histidine.	EC 4.1.1.22	4E1O	MMEPEEYRERGREMVDYICQYLSTVRERRVTPDVQPGYLRAQLPESAPEDPDSWDSIFGDIERIIMPGVVHWQSPHMHAYYPALTSWPSLLGDMLADAINCLGFTWASSPACTELEMNVMDWLAKMLGLPEHFLHHHPSSQGGGVLQSTVSESTLIALLAARKNKILEMKTSEPDADESCLNARLVAYASDQAHSSVEKAGLISLVKMKFLPVDDNFSLRGEALQKAIEEDKQRGLVPVFVCATLGTTGVCAFDCLSELGPICAREGLWLHIDAAYAGTAFLCPEFRGFLKGIEYADSFTFNPSKWMMVHFDCTGFWVKDKYKLQQTFSVNPIYLRHANSGVATDFMHWQIPLSRRFRSVKLWFVIRSFGVKNLQAHVRHGTEMAKYFESLVRNDPSFEIPAKRHLGLVVFRLKGPNCLTENVLKEIAKAGRLFLIPATIQDKLIIRFTVTSQFTTRDDILRDWNLIRDAATLILSQHCTSQPSPRVGNLISQIRGARAWACGTSLQSVSGAGDDPVQARKIIKQPQRVGAGPMKRENGLHLETLLDPVDDCFSEEAPDATKHKLSSFLFSYLSVQTKKKTVRSLSCNSVPVSAQKPLPTEASVKNGGSSRVRIFSRFPEDMMMLKKSAFKKLIKFYSVPSFPECSSQCGLQLPCCPLQAMV	Clinical trial	"Clinical pipeline report, company report or official report of Biofrontera (2009)."	25	EC:4.1	Carbon-carbon lyase	group II decarboxylase family.	4.1.1.22	Carbon-carbon lyases	Pyridoxal-dependent decarboxylase conserved domain	PF00282	PF00282; Pyridoxal_deC	.	.	hsa00340:Histidine metabolism; hsa01100:Metabolic pathways	R-HSA-70921: Histidine catabolism	MetaCyc:HS06697-MON	P19113
TTKGV26	Hepatoma-derived growth factor (HDGF)	P51858	HDGF_HUMAN	.	High-mobility group protein 1-like 2; High mobility group protein 1-like 2; HMG1L2; HMG-1L2	HDGF	"Acts as a transcriptional repressor. Heparin-binding protein, with mitogenic activity for fibroblasts."	.	2NLU; 1RI0	MSRSNRQKEYKCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGLWEIENNPTVKASGYQSSQKKSCVEEPEPEPEAAEGDGDKKGNAEGSSDEEGKLVIDEPAKEKNEKGALKRRAGDLLEDSPKRPKEAENPEGEEKEAATLEVERPLPMEVEKNSTPSEPGSGRGPPQEEEEEEDEEEEATKEDAEAPGIRDHESL	Literature-reported	Hepatoma derived growth factor is a nuclear targeted mitogen. Curr Drug Targets. 2003 Jul;4(5):367-71.	.	.	.	HDGF family.	.	.	PWWP domain	PF00855	PF00855; PWWP	.	.	.	R-HSA-381038: XBP1(S) activates chaperone genes	.	P51858
TTG0RH7	Helicobacter pylori Heat shock protein A (HELPY HspA)	P0A0R3	CH10_HELPY	.	Protein Cpn10; Heat shock protein 10; HELPY 10 kDa chaperonin; GroES protein	HELPY HspA	Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	.	.	MKFQPLGERVLVERLEEENKTSSGIIIPDNAKEKPLMGVVKAVSHKISEGCKCVKEGDVIAFGKYKGAEIVLDGTEYMVLELEDILGIVGSGSCCHTGNHDHKHAKEHEACCHDHKKH	Literature-reported	The C terminus of HspA--a potential target for native Ni(II) and Bi(III) anti-ulcer drugs. Dalton Trans. 2010 Jul 7;39(25):5814-26.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P0A0R3
TT5OG9E	Helicobacter pylori Methylthioadenosine nucleosidase (HELPY mtnN)	O24915	MQMTN_HELPY	.	MTAN; MTA/SAH nucleosidase; Aminofutalosine nucleosidase; Aminodeoxyfutalosine nucleosidase; AFL nucleosidase; 6-amino-6-deoxyfutalosine N-ribosylhydrolase; 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase	HELPY mtnN	"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."	.	4BN0; 4BMZ; 4BMY; 4BMX	MVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKGVYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGVAGSLVKDLKINDLLVAIQLVQHDVDLSAFDHPLGFIPESAIFIETSESLNALAKEVANEQHIVLKEGVIASGDQFVHSKERKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISDNADEEANMSFDAFLEKSAQTSAKFLKSMVDEL	Literature-reported	Selective Inhibitors of Helicobacter pylori Methylthioadenosine Nucleosidase and Human Methylthioadenosine Phosphorylase. J Med Chem. 2019 Apr 11;62(7):3286-3296.	.	.	.	.	.	.	.	.	.	.	.	hpy00130: Ubiquinone and other terpenoid-quinone biosynthesis; hpy00270: Cysteine and methionine metabolism; hpy01100: Metabolic pathways; hpy01110: Biosynthesis of secondary metabolites; hpy01240: Biosynthesis of cofactors	.	MetaCyc:HP0089-MON	O24915
TT1RWL7	Hepatitis A virus cellular receptor 2 (TIM3)	Q8TDQ0	HAVR2_HUMAN	Immunoglobulin	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	Hepatitis A virus HAVCR2	"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."	.	6DHB; 5F71; 5DZL	MFSHLPFDCVLLLLLLLLTRSSEVEYRAEVGQNAYLPCFYTPAAPGNLVPVCWGKGACPVFECGNVVLRTDERDVNYWTSRYWLNGDFRKGDVSLTIENVTLADSGIYCCRIQIPGIMNDEKFNLKLVIKPAKVTPAPTRQRDFTAAFPRMLTTRGHGPAETQTLGSLPDINLTQISTLANELRDSRLANDLRDSGATIRIGIYIGAGICAGLALALIFGALIFKWYSHSKEKIQNLSLISLANLPPSGLANAVAEGIRSEENIYTIEENVYEVEEPNEYYCYVSSRQQPSQPLGCRFAMP	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	19	Immunoglobulin	Immunoglobulin superfamily	immunoglobulin superfamily. TIM family.	.	.	Immunoglobulin V-set domain	PF07686	PF07686; V-set	.	.	.	R-HSA-451927: Interleukin-2 family signaling	.	Q8TDQ0
TT3RWZF	Neuro/glioblastoma derived oncogene (Herstatin)	Q9UK79	Q9UK79_HUMAN	.	"V-erb-b2 erythroblastic leukemia viral oncogene homolog 2, neuro/glioblastoma derived oncogene homolog (Avian), isoform CRA_a; Herstatin; ERBB2"	HER-2	"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."	.	.	MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARGTHSLPPRPAAVPVPLRMQPGPAHPVLSFLRPSWDLVSAFYSLPLAPLSPTSVPISPVSVGRGPDPDAHVAVDLSRYEG	Literature-reported	HER-2 and TOP2A coamplification in urinary bladder cancer. Int J Cancer. 2003 Dec 10;107(5):764-72.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJI5JW	Beta-hexosaminidase subunit alpha (HEXA)	P06865	HEXA_HUMAN	Glycosyl hydrolase	Beta-N-acetylhexosaminidase subunit alpha; Hexosaminidase subunit A; N-acetyl-beta-glucosaminidase subunit alpha	HEXA	"Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides (PubMed:11707436, PubMed:9694901, PubMed:8672428, PubMed:8123671). The isozyme S is as active as the isozyme A on the anionic bis-sulfated glycans, the chondroitin-6-sulfate trisaccharide (C6S-3), and the dermatan sulfate pentasaccharide, and the sulfated glycosphingolipid SM2 (PubMed:11707436). The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide (PubMed:11707436). Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A (PubMed:9694901, PubMed:8672428, PubMed:8123671). {ECO:0000269|PubMed:11707436, ECO:0000269|PubMed:8123671, ECO:0000269|PubMed:8672428, ECO:0000269|PubMed:9694901}."	EC 3.2.1.52	2GJX;2GK1	MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYIVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT	Clinical trial	"ClinicalTrials.gov (NCT04798235) Phase 1/2, Open-Label Clinical Study to Evaluate the Safety and Efficacy of Intrathecal TSHA-101 Gene Therapy for Treatment of Infantile Onset GM2 Gangliosidosis. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	hsa:3073	R-HSA-2022857;R-HSA-2024101;R-HSA-2160916;R-HSA-3656234;R-HSA-9840310;	MetaCyc:ENSG00000140495-MONOMER;	P06865;
TTKIBKM	Beta-hexosaminidase subunit beta (HEXB)	P07686	HEXB_HUMAN	Glycosyl hydrolase	Beta-N-acetylhexosaminidase subunit beta; Hexosaminidase subunit B; Cervical cancer proto-oncogene 7 protein; HCC-7; N-acetyl-beta-glucosaminidase subunit beta	HEXB	"Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides (PubMed:11707436, PubMed:9694901, PubMed:8672428, PubMed:8123671). The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide (PubMed:11707436). Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A (PubMed:9694901, PubMed:8672428, PubMed:8123671). During fertilization is responsible, at least in part, for the zona block to polyspermy. Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and inactivates the sperm galactosyltransferase-binding site, accounting for the block in sperm binding to the zona pellucida (By similarity). {ECO:0000250|UniProtKB:P20060, ECO:0000269|PubMed:11707436, ECO:0000269|PubMed:8123671, ECO:0000269|PubMed:8672428, ECO:0000269|PubMed:9694901}."	EC 3.2.1.52	1NOU;1NOW;1NP0;1O7A;2GJX;2GK1;3LMY;5BRO	MELCGLGLPRPPMLLALLLATLLAAMLALLTQVALVVQVAEAARAPSVSAKPGPALWPLPLLVKMTPNLLHLAPENFYISHSPNSTAGPSCTLLEEAFRRYHGYIFGFYKWHHEPAEFQAKTQVQQLLVSITLQSECDAFPNISSDESYTLLVKEPVAVLKANRVWGALRGLETFSQLVYQDSYGTFTINESTIIDSPRFSHRGILIDTSRHYLPVKIILKTLDAMAFNKFNVLHWHIVDDQSFPYQSITFPELSNKGSYSLSHVYTPNDVRMVIEYARLRGIRVLPEFDTPGHTLSWGKGQKDLLTPCYSRQNKLDSFGPINPTLNTTYSFLTTFFKEISEVFPDQFIHLGGDEVEFKCWESNPKIQDFMRQKGFGTDFKKLESFYIQKVLDIIATINKGSIVWQEVFDDKAKLAPGTIVEVWKDSAYPEELSRVTASGFPVILSAPWYLDLISYGQDWRKYYKVEPLDFGGTQKQKQLFIGGEACLWGEYVDATNLTPRLWPRASAVGERLWSSKDVRDMDDAYDRLTRHRCRMVERGIAAQPLYAGYCNHENM	Clinical trial	"ClinicalTrials.gov (NCT04798235) Phase 1/2, Open-Label Clinical Study to Evaluate the Safety and Efficacy of Intrathecal TSHA-101 Gene Therapy for Treatment of Infantile Onset GM2 Gangliosidosis. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	hsa:3074	R-HSA-2022857;R-HSA-2024101;R-HSA-2160916;R-HSA-3656248;R-HSA-6798695;R-HSA-9840310;	MetaCyc:HS00629-MONOMER;	P07686;
TTFOKAH	Hexamethylene bis-acetamide-inducible protein 1 (HEXIM1)	O94992	HEXI1_HUMAN	.	Protein HEXIM1; Menage a quatre protein 1; MAQ1; HIS1; Estrogen down-regulated gene 1 protein; EDG1; Cardiac lineage protein 1; CLP1	HEXIM1	"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."	.	3S9G; 2GD7	MAEPFLSEYQHQPQTSNCTGAAAVQEELNPERPPGAEERVPEEDSRWQSRAFPQLGGRPGPEGEGSLESQPPPLQTQACPESSCLREGEKGQNGDDSSAGGDFPPPAEVEPTPEAELLAQPCHDSEASKLGAPAAGGEEEWGQQQRQLGKKKHRRRPSKKKRHWKPYYKLTWEEKKKFDEKQSLRASRIRAEMFAKGQPVAPYNTTQFLMDDHDQEEPDLKTGLYSKRAAAKSDDTSDDDFMEEGGEEDGGSDGMGGDGSEFLQRDFSETYERYHTESLQNMSKQELIKEYLELEKCLSRMEDENNRLRLESKRLGGDDARVRELELELDRLRAENLQLLTENELHRQQERAPLSKFGD	Literature-reported	Suppression of NF-kappaB-dependent gene expression by a hexamethylene bisacetamide-inducible protein HEXIM1 in human vascular smooth muscle cells. Genes Cells. 2003 Feb;8(2):95-107.	.	.	.	HEXIM family.	.	.	Hexamethylene bis-acetamide-inducible protein	PF15313	PF15313; HEXIM	.	.	.	.	.	O94992
TT4V2JM	Hepatocyte growth factor (HGF)	P14210	HGF_HUMAN	Peptidase	Scatter factor; SF; Hepatopoietin-A; Hepatopoeitin A; HPTA	HGF	"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."	.	5CT3; 5CT2; 5CT1; 5CSQ; 5CS9	MWVTKLLPALLLQHVLLHLLLLPIAIPYAEGQRKRRNTIHEFKKSAKTTLIKIDPALKIKTKKVNTADQCANRCTRNKGLPFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYENKDYIRNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQCSEVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTCADNTMNDTDVPLETTECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDGSESPWCFTTDPNIRVGYCSQIPNCDMSHGQDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPISRCEGDTTPTIVNLDHPVISCAKTKQLRVVNGIPTRTNIGWMVSLRYRNKHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDEKCKQVLNVSQLVYGPEGSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYTGLINYDGLLRVAHLYIMGNEKCSQHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKIILTYKVPQS	Clinical trial	Therapeutic angiogenesis using naked DNA expressing two isoforms of the hepatocyte growth factor in a porcine acute myocardial infarction model. Eur J Cardiothorac Surg. 2008 Oct;34(4):857-63.	25	EC:3.4	Peptidase	peptidase S1 family. Plasminogen subfamily.	.	.	Kringle domain; PAN domain; Trypsin	PF00051; PF00024; PF00089	PF00051; Kringle; PF00024; PAN_1; PF00089; Trypsin	.	.	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	R-HSA-114608:Platelet degranulation; R-HSA-1266695:Interleukin-7 signaling	.	P14210
TTD96RW	Hepatocyte growth factor activator (HGFAC)	Q04756	HGFA_HUMAN	Peptidase	Hepatocyte growth factor activator long chain; HGFAC; HGFA; HGF activator	HGFAC	Activates hepatocyte growth factor (HGF) by convertingit from a single chain to a heterodimeric form.	EC 3.4.21.-	3K2U; 2WUC; 2WUB; 2R0L; 2R0K	MGRWAWVPSPWPPPGLGPFLLLLLLLLLLPRGFQPQPGGNRTESPEPNATATPAIPTILVTSVTSETPATSAPEAEGPQSGGLPPPPRAVPSSSSPQAQALTEDGRPCRFPFRYGGRMLHACTSEGSAHRKWCATTHNYDRDRAWGYCVEATPPPGGPAALDPCASGPCLNGGSCSNTQDPQSYHCSCPRAFTGKDCGTEKCFDETRYEYLEGGDRWARVRQGHVEQCECFGGRTWCEGTRHTACLSSPCLNGGTCHLIVATGTTVCACPPGFAGRLCNIEPDERCFLGNGTGYRGVASTSASGLSCLAWNSDLLYQELHVDSVGAAALLGLGPHAYCRNPDNDERPWCYVVKDSALSWEYCRLEACESLTRVQLSPDLLATLPEPASPGRQACGRRHKKRTFLRPRIIGGSSSLPGSHPWLAAIYIGDSFCAGSLVHTCWVVSAAHCFSHSPPRDSVSVVLGQHFFNRTTDVTQTFGIEKYIPYTLYSVFNPSDHDLVLIRLKKKGDRCATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPLVADHKCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWINDRIRPPRRLVAPS	Literature-reported	Hepatocyte growth factor activator inhibitor type 1 in cancer: advances and perspectives (Review). Mol Med Rep. 2014 Dec;10(6):2779-85.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-6806942: MET Receptor Activation	.	Q04756
TT1VNCG	Protein-cysteine N-palmitoyltransferase HHAT (HHAT)	Q5VTY9	HHAT_HUMAN	Acyltransferase	Skinny hedgehog protein 1; Melanoma antigen recognized by T-cells 2; MART-2; Hedgehog acyltransferase; HHAT	HHAT	Catalyzes N-terminal palmitoylation of SHH; which is required for SHH signaling. May bind GTP. .	EC 2.3.1.-	.	MLPRWELALYLLASLGFHFYSFYEVYKVSREHEEELDQEFELETDTLFGGLKKDATDFEWSFWMEWGKQWLVWLLLGHMVVSQMATLLARKHRPWILMLYGMWACWCVLGTPGVAMVLLHTTISFCVAQFRSQLLTWLCSLLLLSTLRLQGVEEVKRRWYKTENEYYLLQFTLTVRCLYYTSFSLELCWQQLPAASTSYSFPWMLAYVFYYPVLHNGPILSFSEFIKQMQQQEHDSLKASLCVLALGLGRLLCWWWLAELMAHLMYMHAIYSSIPLLETVSCWTLGGLALAQVLFFYVKYLVLFGVPALLMRLDGLTPPALPRCVSTMFSFTGMWRYFDVGLHNFLIRYVYIPVGGSQHGLLGTLFSTAMTFAFVSYWHGGYDYLWCWAALNWLGVTVENGVRRLVETPCIQDSLARYFSPQARRRFHAALASCSTSMLILSNLVFLGGNEVGKTYWNRIFIQGWPWVTLSVLGFLYCYSHVGIAWAQTYATD	Literature-reported	Hedgehog acyltransferase as a target in pancreatic ductal adenocarcinoma. Oncogene. 2015 Jan 8;34(2):263-8.	.	.	.	.	.	.	.	.	.	.	.	hsa04340: Hedgehog signaling pathway	R-HSA-5358346: Hedgehog ligand biogenesis; R-HSA-5658034: HHAT G278V doesn't palmitoylate Hh-Np	.	Q5VTY9
TTSN6QU	HIF1-alpha messenger RNA (HIF1A mRNA)	Q16665	HIF1A_HUMAN	mRNA target	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)	HIF1A	"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."	.	6GMR; 6GFX; 5LAS; 5LA9; 5L9V	MEGAGGANDKKKISSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDDMKAQMNCFYLKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGLVKKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTECVLKPVESSDMKMTQLFTKVESEDTSSLFDKLKKEPDALTLLAPAAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSPNEKLQNINLAMSPLPTAETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQTPSPSDGSTRQSSPEPNSPSEYCFYVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	mRNA	mRNA target	.	.	.	Hypoxia-inducible factor-1; HIF-1 alpha C terminal transactivation domain; PAS fold; PAS fold	PF11413; PF08778; PF00989; PF08447	PF11413; HIF-1; PF08778; HIF-1a_CTAD; PF00989; PAS; PF08447; PAS_3	.	.	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	"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"	.	Q16665
TTQHWNA	Hypoxia-inducible factor 1 alpha (HIF-1A)	Q16665	HIF1A_HUMAN	.	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	HIF1A	"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."	.	6GMR; 6GFX; 5LAS; 5LA9; 5L9V	MEGAGGANDKKKISSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDDMKAQMNCFYLKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGLVKKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTECVLKPVESSDMKMTQLFTKVESEDTSSLFDKLKKEPDALTLLAPAAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSPNEKLQNINLAMSPLPTAETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQTPSPSDGSTRQSSPEPNSPSEYCFYVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN	Clinical trial	"A RNA antagonist of hypoxia-inducible factor-1alpha, EZN-2968, inhibits tumor cell growth. Mol Cancer Ther. 2008 Nov;7(11):3598-608."	31	.	.	.	.	.	Hypoxia-inducible factor-1; HIF-1 alpha C terminal transactivation domain; PAS fold; PAS fold	PF11413; PF08778; PF00989; PF08447	PF11413; HIF-1; PF08778; HIF-1a_CTAD; PF00989; PAS; PF08447; PAS_3	.	.	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	"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"	.	Q16665
TTOB49C	Homeodomain interacting protein kinase 2 (HIPK2)	Q9H2X6	HIPK2_HUMAN	Kinase	hHIPk2; Homeodomain-interacting protein kinase 2	HIPK2	"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."	EC 2.7.11.1	.	MAPVYEGMASHVQVFSPHTLQSSAFCSVKKLKIEPSSNWDMTGYGSHSKVYSQSKNIPLSQPATTTVSTSLPVPNPSLPYEQTIVFPGSTGHIVVTSASSTSVTGQVLGGPHNLMRRSTVSLLDTYQKCGLKRKSEEIENTSSVQIIEEHPPMIQNNASGATVATATTSTATSKNSGSNSEGDYQLVQHEVLCSMTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADDYNFVRAYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPVLQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFNRDTDSPYPLWRLKTPDDHEAETGIKSKEARKYIFNCLDDMAQVNMTTDLEGSDMLVEKADRREFIDLLKKMLTIDADKRITPIETLNHPFVTMTHLLDFPHSTHVKSCFQNMEICKRRVNMYDTVNQSKTPFITHVAPSTSTNLTMTFNNQLTTVHNQAPSSTSATISLANPEVSILNYPSTLYQPSAASMAAVAQRSMPLQTGTAQICARPDPFQQALIVCPPGFQGLQASPSKHAGYSVRMENAVPIVTQAPGAQPLQIQPGLLAQQAWPSGTQQILLPPAWQQLTGVATHTSVQHATVIPETMAGTQQLADWRNTHAHGSHYNPIMQQPALLTGHVTLPAAQPLNVGVAHVMRQQPTSTTSSRKSKQHQSSVRNVSTCEVSSSQAISSPQRSKRVKENTPPRCAMVHSSPACSTSVTCGWGDVASSTTRERQRQTIVIPDTPSPTVSVITISSDTDEEEEQKHAPTSTVSKQRKNVISCVTVHDSPYSDSSSNTSPYSVQQRAGHNNANAFDTKGSLENHCTGNPRTIIVPPLKTQASEVLVECDSLVPVNTSHHSSSYKSKSSSNVTSTSGHSSGSSSGAITYRQQRPGPHFQQQQPLNLSQAQQHITTDRTGSHRRQQAYITPTMAQAPYSFPHNSPSHGTVHPHLAAAAAAAHLPTQPHLYTYTAPAALGSTGTVAHLVASQGSARHTVQHTAYPASIVHQVPVSMGPRVLPSPTIHPSQYPAQFAHQTYISASPASTVYTGYPLSPAKVNQYPYI	Literature-reported	"Structure and Property Based Design of Pyrazolo[1,5-a]pyrimidine Inhibitors of CK2 Kinase with Activity in Vivo. ACS Med Chem Lett. 2013 Jul 3;4(8):800-5."	0	EC:2.7	.	protein kinase superfamily. CMGC Ser/Thr protein kinase family. HIPK subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04218: Cellular senescence	R-HSA-2032785: YAP1- and WWTR1 (TAZ)-stimulated gene expression; R-HSA-3899300: SUMOylation of transcription cofactors; R-HSA-5578768: Physiological factors; R-HSA-6804756: Regulation of TP53 Activity through Phosphorylation; R-HSA-8939243: RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known; R-HSA-9022692: Regulation of MECP2 expression and activity	.	Q9H2X6
TTBFWZJ	Histone H1s-2 (H1.3)	P16402	H13_HUMAN	.	Histone H1s2; Histone H1c; HIST1H1D	HIST1H1D	"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."	.	.	MSETAPLAPTIPAPAEKTPVKKKAKKAGATAGKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEGKPKAKKAGAAKPRKPAGAAKKPKKVAGAATPKKSIKKTPKKVKKPATAAGTKKVAKSAKKVKTPQPKKAAKSPAKAKAPKPKAAKPKSGKPKVTKAKKAAPKKK	Literature-reported	Histone h1.3 suppresses h19 noncoding RNA expression and cell growth of ovarian cancer cells. Cancer Res. 2014 Nov 15;74(22):6463-73.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-140342: Apoptosis induced DNA fragmentation; R-HSA-2559584: Formation of Senescence-Associated Heterochromatin Foci (SAHF)	.	P16402
TTEC2T3	Human immunodeficiency virus Envelope glycoprotein gp160 (HIV env)	P04578	ENV_HV1H2	.	Envelope glycoprotein gp160; Env polyprotein	HIV env	"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."	.	6DLN; 6DE7; 6BXQ; 6BXP; 6B9K	MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL	Clinical trial	ClinicalTrials.gov (NCT00695877) Safety and Immune Response to a Recombinant Adenovirus HIV-1 Vaccine in Healthy Adults. U.S. National Institutes of Health.	17	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1462054: Alpha-defensins; R-HSA-162588: Budding and maturation of HIV virion; R-HSA-171286: Synthesis and processing of ENV and VPU; R-HSA-173107: Binding and entry of HIV virion; R-HSA-175474: Assembly Of The HIV Virion; R-HSA-5621480: Dectin-2 family	.	.
TTXVOJ5	Human immunodeficiency virus Envelope messenger RNA (HIV env mRNA)	P04578	ENV_HV1H2	mRNA target	HIV-1 HXB2 envelope glycoprotein gp160 (mRNA); HIV-1 HXB2 env polyprotein (mRNA)	HIV env mRNA	"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."	.	6DLN; 6DE7; 6BXQ; 6BXP; 6B9K	MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL	Successful	Design and development of antisense drugs. Expert Opin. Drug Discov. 2008 3(10):1189-1207.	34	mRNA	mRNA target	.	.	.	Envelope glycoprotein GP120; Retroviral envelope protein	PF00516; PF00517	PF00516; GP120; PF00517; GP41	.	.	.	R-HSA-1462054: Alpha-defensins; R-HSA-162588: Budding and maturation of HIV virion; R-HSA-171286: Synthesis and processing of ENV and VPU; R-HSA-173107: Binding and entry of HIV virion; R-HSA-175474: Assembly Of The HIV Virion; R-HSA-5621480: Dectin-2 family	.	.
TTFGZB6	Human immunodeficiency virus GAG protein (HIV gag)	P04591	GAG_HV1H2	.	Pr55Gag; Gag polyprotein	HIV gag	"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)."	.	6CQR; 6CQQ; 6CQN; 6CQL; 6CQJ	MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSNQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSYKGRPGNFLQSRPEPTAPPEESFRSGVETTTPPQKQEPIDKELYPLTSLRSLFGNDPSSQ	Clinical trial	Synthesis and biological evaluation of a new derivative of bevirimat that targets the Gag CA-SP1 cleavage site. Eur J Med Chem. 2013 Apr;62:453-65.	21	.	.	.	.	.	.	.	.	.	.	.	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	.	.
TTF6NLB	Human immunodeficiency virus GAG messenger RNA (HIV gag mRNA)	P04591	GAG_HV1H2	mRNA target	gag (mRNA); Pr55Gag (mRNA); Gag polyprotein (mRNA)	HIV gag mRNA	"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)."	.	6CQR; 6CQQ; 6CQN; 6CQL; 6CQJ	MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSNQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSYKGRPGNFLQSRPEPTAPPEESFRSGVETTTPPQKQEPIDKELYPLTSLRSLFGNDPSSQ	Literature-reported	Multiparametric characterization of rare HIV-infected cells using an RNA-flow FISH technique. Nat Protoc. 2017 Oct;12(10):2029-2049.	.	mRNA	mRNA target	.	.	.	gag gene protein p17 (matrix protein); gag gene protein p24 (core nucleocapsid protein); Gag protein p6; Zinc knuckle	PF00540; PF00607; PF08705; PF00098	PF00540; Gag_p17; PF00607; Gag_p24; PF08705; Gag_p6; PF00098; zf-CCHC	.	.	.	"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-174495: Synthesis And Processing Of GAG, GAGPOL Polyproteins; 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"	.	.
TTBYP1X	Human immunodeficiency virus Envelope glycoprotein gp120 (HIV gp120)	P04578 (512-856)	ENV_HV1H2	.	Env polyprotein gp120 (33-511)	HIV gp120	"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."	.	6DLN; 6DE7; 6BXQ; 6BXP; 6B9K	AVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL	Successful	"In vitro antiviral characteristics of HIV-1 attachment inhibitor BMS-626529, the active component of the prodrug BMS-663068. Antimicrob Agents Chemother. 2012 Jul;56(7):3498-507."	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTG90S6	Human immunodeficiency virus Glycoprotein 41 (HIV gp41)	P04578 (33-511)	ENV_HV1H2	.	Env polyprotein gp41 (33-511)	HIV gp41	"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."	.	6DLN; 6DE7; 6BXQ; 6BXP; 6B9K	KLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKR	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQ9HB0	Virus fusion protein HIV gp41-influenza HA (HIV gp41-Influ HA)	P04578 (33-511)-P03452	ENV_HV1H2-HEMA_I34A1	.	Virus fusion protein Env polyprotein-influenza Hemagglutinin	HIV gp41-Influ HA	Functions as a passive -helical anchor of the protein to the virus envelope during its merger with the cell membrane	.	.	KLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKMKANLLVLLCALAAADADTICIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDSHNGKLCRLKGIAPLQLGKCNIAGWLLGNPECDPLLPVRSWSYIVETPNSENGICYPGDFIDYEELREQLSSVSSFERFEIFPKESSWPNHNTNGVTAACSHEGKSSFYRNLLWLTEKEGSYPKLKNSYVNKKGKEVLVLWGIHHPPNSKEQQNLYQNENAYVSVVTSNYNRRFTPEIAERPKVRDQAGRMNYYWTLLKPGDTIIFEANGNLIAPMYAFALSRGFGSGIITSNASMHECNTKCQTPLGAINSSLPYQNIHPVTIGECPKYVRSAKLRMVTGLRNIPSIQSRGLFGAIAGFIEGGWTGMIDGWYGYHHQNEQGSGYAADQKSTQNAINGITNKVNTVIEKMNIQFTAVGKEFNKLEKRMENLNKKVDDGFLDIWTYNAELLVLLENERTLDFHDSNVKNLYEKVKSQLKNNAKEIGNGCFEFYHKCDNECMESVRNGTYDYPKYSEESKLNREKVDGVKLESMGIYQILAIYSTVASSLVLLVSLGAISFWMCSNGSLQCRICI	Literature-reported	Viral fusion protein transmembrane domain adopts -strand structure to facilitate membrane topological changes for virus-cell fusion. Proc Natl Acad Sci U S A. 2015 Sep 1;112(35):10926-31.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5FH9Y	Human immunodeficiency virus Integrase (HIV IN)	P03366 (1160-1447)	POL_HV1B1	Integrase	HIV IN	HIV IN	"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."	EC 2.7.7.-	6OE3; 6HAK; 6ELI; 6DUH; 6DUG	FLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGSNFTSATVKAACWWAGIKQEFGIPYNPQSQGVVESMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRNPLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED	Successful	Radium 223 dichloride for prostate cancer treatment. Drug Des Devel Ther. 2017 Sep 6;11:2643-2651.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTI3NXG	Human immunodeficiency virus Matrix p17 (HIV MA)	P03366 (2-132)	POL_HV1B1	.	gag	HIV MA	p6-gag: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1.	.	6OE3; 6HAK; 6ELI; 6DUH; 6DUG	GARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSSQVSQNY	Clinical trial	"EP patent application no. 2621528, Vaccine."	21	.	.	.	.	.	.	.	.	.	.	.	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	.	.
TT4NXYM	Human immunodeficiency virus Negative factor (HIV nef)	P03407	NEF_HV1A2	Lentivirus primate group Nef	nef; Nef protein; F-protein; 3'ORF; 27 kDa protein	HIV nef	Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors.	.	6B72; 5XOV; 4U5W; 4U1N; 4U1M	MGGKWSKRSMGGWSAIRERMRRAEPRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVRPQVPLRPMTYKAALDISHFLKEKGGLEGLIWSQRRQEILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCFKLVPVEPEKVEEANEGENNSLLHPMSLHGMEDAEKEVLVWRFDSKLAFHHMARELHPEYYKDC	Clinical trial	"EP patent application no. 2621528, Vaccine."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTTWS2G	Human immunodeficiency virus Capsid p24 (HIV p24)	P03366 (133-363)	POL_HV1B1	.	CA	HIV p24	"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."	.	6OE3; 6HAK; 6ELI; 6DUH; 6DUG	PIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVL	Clinical trial	"EP patent application no. 2621528, Vaccine."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8Z1OP	Human immunodeficiency virus Nucleocapsid p7 (HIV p7)	P03366 (378-432)	POL_HV1B1	.	HIV NC	HIV p7	"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."	.	6OE3; 6HAK; 6ELI; 6DUH; 6DUG	MQRGNFRNQRKMVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQAN	Clinical trial	"Clinical pipeline report, company report or official report of H-Phar."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5FNQT	Human immunodeficiency virus Protease (HIV PR)	P03366 (501-599)	POL_HV1B1	Peptidase	HIV Retropepsin; HIV PR	HIV PR	"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."	EC 3.4.23.16	6OE3; 6HAK; 6ELI; 6DUH; 6DUG	PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNF	Successful	Quantification of HIV protease inhibitors and non-nucleoside reverse transcriptase inhibitors in peripheral blood mononuclear cell lysate using liq... J Chromatogr B Analyt Technol Biomed Life Sci. 2009 Feb 15;877(5-6):575-80.	34	EC:3.4	.	.	.	.	.	.	.	.	.	.	.	.	.
TTF7I5O	Human immunodeficiency virus Rev protein (HIV rev)	P04618	REV_HV1H2	.	rev; Regulator of expression of viral proteins; Anti-repression transactivator; ART/TRS	HIV rev	"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."	.	.	MAGRSGDSDEELIRTVRLIKLLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERILGTYLGRSAEPVPLQLPPLERLTLDCNEDCGTSGTQGVGSPQILVESPTVLESGTKE	Clinical trial	"Antiretroviral drugs in development. A report from HIV DART 2008: Frontiers in Drug Development for Antiretroviral Therapies, 9-12 December 2008, Rio Grande, Puerto Rico. Expert Opin Investig Drugs. 2009 Apr;18(4):549-53."	17	.	.	.	.	.	.	.	.	.	.	.	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	.	.
TTRP4JT	Human immunodeficiency virus Rev messenger RNA (HIV rev mRNA)	P04618	REV_HV1H2	mRNA target	rev (mRNA); Regulator of expression of viral proteins (mRNA); Protein Rev (mRNA); Anti-repression transactivator (mRNA); ART/TRS (mRNA)	HIV rev mRNA	"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."	.	.	MAGRSGDSDEELIRTVRLIKLLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERILGTYLGRSAEPVPLQLPPLERLTLDCNEDCGTSGTQGVGSPQILVESPTVLESGTKE	Clinical trial	Design and development of antisense drugs. Expert Opin. Drug Discov. 2008 3(10):1189-1207.	21	mRNA	mRNA target	.	.	.	REV protein (anti-repression trans-activator protein)	PF00424	PF00424; REV	.	.	.	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-165054: Rev-mediated nuclear export of HIV RNA; 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-180746: Nuclear import of Rev protein; R-HSA-180910: Vpr-mediated nuclear import of PICs	.	.
TT37KAF	Human immunodeficiency virus Ribonuclease H (HIV RNH)	P03366 (600-1159)	POL_HV1B1	.	Retroviral ribonuclease H; RNase H (600-1159); RNH1	HIV RNH	Endonuclease that specifically degrades the RNA of RNA- DNA hybrids.	EC 2.7.7.49	6OE3; 6HAK; 6ELI; 6DUH; 6DUG	PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKIL	Literature-reported	"RNase H active site inhibitors of human immunodeficiency virus type 1 reverse transcriptase: design, biochemical activity, and structural information. J Med Chem. 2009 Oct 8;52(19):5781-4."	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT84ETX	Human immunodeficiency virus Reverse transcriptase (HIV RT)	P03366 (600-1159)	POL_HV1B1	.	HIV p66 RT; HIV Exoribonuclease H	HIV RT	"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."	EC 2.7.7.49	6OE3; 6HAK; 6ELI; 6DUH; 6DUG	PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKIL	Successful	Natural products as sources of new drugs over the last 25 years. J Nat Prod. 2007 Mar;70(3):461-77.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTBDH9A	Human immunodeficiency virus RT messenger RNA (HIV RT mRNA)	P03366 (600-1159)	POL_HV1B1	mRNA target	gag-pol (588-1147) (mRNA); Pr160Gag-Pol (588-1147) (mRNA); Gag-Pol polyprotein (588-1147) (mRNA)	HIV RT mRNA	"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)."	EC 2.7.7.49	6OE3; 6HAK; 6ELI; 6DUH; 6DUG	PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKIL	Literature-reported	Novel lentiviral vectors with mutated reverse transcriptase for mRNA delivery of TALE nucleases. Sci Rep. 2014 Sep 18;4:6409.	.	mRNA	mRNA target	.	.	.	gag gene protein p17 (matrix protein); gag gene protein p24 (core nucleocapsid protein); Integrase DNA binding domain; Integrase Zinc binding domain; RNase H; Integrase core domain; Retroviral aspartyl protease; Reverse transcriptase (RNA-dependent DNA polymerase); Reverse transcriptase connection domain; Reverse transcriptase thumb domain; Zinc knuckle	PF00540; PF00607; PF00552; PF02022; PF00075; PF00665; PF00077; PF00078; PF06815; PF06817; PF00098	PF00540; Gag_p17; PF00607; Gag_p24; PF00552; IN_DBD_C; PF02022; Integrase_Zn; PF00075; RNase_H; PF00665; rve; PF00077; RVP; PF00078; RVT_1; PF06815; RVT_connect; PF06817; RVT_thumb; PF00098; zf-CCHC	.	.	.	.	.	.
TTT3ZC9	Human immunodeficiency virus Tat protein (HIV tat)	P04608	TAT_HV1H2	Lentiviruses Tat family	Transactivating regulatory protein; TAT protein	HIV tat	"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."	.	6MCF; 6MCE; 5V61; 4OR5; 3MIA	MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRRAHQNSQTHQASLSKQPTSQPRGDPTGPKE	Successful	Docking studies reveal a selective binding of D-penicillamine to the transactivator protein of human immunodeficiency virus type 1. FEBS Lett. 2002 Apr 10;516(1-3):43-6.	34	.	.	.	.	.	.	.	.	.	.	.	R-HSA-167200: Formation of HIV-1 elongation complex containing HIV-1 Tat; R-HSA-167238: Pausing and recovery of Tat-mediated HIV elongation; R-HSA-167243: Tat-mediated HIV elongation arrest and recovery; R-HSA-167246: Tat-mediated elongation of the HIV-1 transcript; R-HSA-176034: Interactions of Tat with host cellular proteins	.	.
TTFP96H	Human immunodeficiency virus Tat messenger RNA (HIV tat mRNA)	P04608	TAT_HV1H2	mRNA target	tat (mRNA); Transactivating regulatory protein (mRNA); Protein Tat (mRNA)	HIV tat mRNA	"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."	.	6MCF; 6MCE; 5V61; 4OR5; 3MIA	MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRRAHQNSQTHQASLSKQPTSQPRGDPTGPKE	Clinical trial	Design and development of antisense drugs. Expert Opin. Drug Discov. 2008 3(10):1189-1207.	21	mRNA	mRNA target	.	.	.	Transactivating regulatory protein (Tat)	PF00539	PF00539; Tat	.	.	.	R-HSA-167200: Formation of HIV-1 elongation complex containing HIV-1 Tat; R-HSA-167238: Pausing and recovery of Tat-mediated HIV elongation; R-HSA-167243: Tat-mediated HIV elongation arrest and recovery; R-HSA-167246: Tat-mediated elongation of the HIV-1 transcript; R-HSA-176034: Interactions of Tat with host cellular proteins	.	.
TT8Z1FE	Human immunodeficiency virus Tat-TAR RNA interaction (HIV Tat-TAR PPI)	P04608-TAR RNA	TAT_HV1H2-TAR RNA	.	HIV Protein Tat-TAR RNA interaction	HIV Tat-TAR PPI	Inhibit Tat-dependent transcription of  HIV DNA.	.	.	MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRRAHQNSQTHQASLSKQPTSQPRGDPTGPKE	Literature-reported	The synthesis of 2'-O-methyl G-clamp containing oligonucleotides and their inhibition of the HIV-1 Tat-TAR interaction. Nucleosides Nucleotides Nucleic Acids. 2003 May-Aug;22(5-8):1259-62.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT74D0S	Human immunodeficiency virus Virion infectivity factor (HIV vif)	P03402	VIF_HV1A2	Primate lentivirus group Vif protein	Virion infectivity factor; Vif; SOR protein	HIV vif	"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."	.	.	MENRWQVMIVWQVDRMRIRTWKSLVKHHMYISKKAKGWFYRHHYESTHPRVSSEVHIPLGDAKLVITTYWGLHTGEREWHLGQGVAIEWRKKKYSTQVDPGLADQLIHLHYFDCFSESAIKNAILGYRVSPRCEYQAGHNKVGSLQYLALAALITPKKTKPPLPSVKKLTEDRWNKPQKTKGHRGSHTMNGH	Literature-reported	Functional neutralization of HIV-1 Vif protein by intracellular immunization inhibits reverse transcription and viral replication. J Biol Chem. 2002 Aug 30;277(35):32036-45.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTK02H8	Hexokinase-2 (HK2)	P52789	HXK2_HUMAN	Hexokinase family	Muscle form hexokinase; Hexokinase type II; HK II	HK2	"cytosol, membrane, mitochondrial outer membrane, fructokinase activity, glucokinase activity, hexokinase activity, mannokinase activity, apoptotic mitochondrial changes, canonical glycolysis, cellular glucose homeostasis."	EC 2.7.1.1	5HG1; 5HFU; 5HEX; 2NZT	MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIREAGQR	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	"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"	R-HSA-70171: Glycolysis	MetaCyc:HS08399-MON	P52789
TTVUI8G	Hexokinase HKDC1	.	HKDC1_HUMAN	Single Protein	Hexokinase domain-containing protein 1	HKDC1	"Catalyzes the phosphorylation of hexose to hexose 6-phosphate, although at very low level compared to other hexokinases. Has low glucose phosphorylating activity compared to other hexokinases. Involved in glucose homeostasis and hepatic lipid accumulation. Required to maintain whole-body glucose homeostasis during pregnancy; however additional evidences are required to confirm this role."	.	.	MFAVHLMAFYFSKLKEDQIKKVDRFLYHMRLSDDTLLDIMRRFRAEMEKGLAKDTNPTAAVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVAEEGKRHVQMESQFYPTPNEIIRGNGTELFEYVADCLADFMKTKDLKHKKLPLGLTFSFPCRQTKLEEGVLLSWTKKFKARGVQDTDVVSRLTKAMRRHKDMDVDILALVNDTVGTMMTCAYDDPYCEVGVIIGTGTNACYMEDMSNIDLVEGDEGRMCINTEWGAFGDDGALEDIRTEFDRELDLGSLNPGKQLFEKMISGLYLGELVRLILLKMAKAGLLFGGEKSSALHTKGKIETRHVAAMEKYKEGLANTREILVDLGLEPSEADCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKVERLRTTVGMDGTLYKIHPQYPKRLHKVVRKLVPSCDVRFLLSESGSTKGAAMVTAVASRVQAQRKQIDRVLALFQLTREQLVDVQAKMRAELEYGLKKKSHGLATVRMLPTYVCGLPDGTEKGKFLALDLGGTNFRVLLVKIRSGRRSVRMYNKIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGASLPLGFTFSFPCRQMSIDKGTLIGWTKGFKATDCEGEDVVDMLREAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPNCEIGLIAGTGSNMCYMEDMRNIEMVEGGEGKMCINTEWGGFGDNGCIDDIWTRYDTEVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLALLQVRRILQQLGLDSTCEDSIVVKEVCGAVSRRAAQLCGAGLAAIVEKRREDQGLEHLRITVGVDGTLYKLHPHFSRILQETVKELAPRCDVTFMLSEDGSGKGAALITAVAKRLQQAQKEN	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q2TB90
TTHONFT	MHC class I antigen A*33 (HLA-A)	P16190	1A33_HUMAN	MHC class I	"HLAA; HLA-A; HLA class I histocompatibility antigen, A33 alpha chain; Aw33; Aw19"	HLA-A	Involved in the presentation of foreign antigens to the immune system.	.	.	MAVMAPRTLLLLLSGALALTQTWAGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDQETRNVKAQSQTDRVDLGTLRGYYNQSEAGSHTIQIMYGCDVGSDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAAHEAEQLRAYLDGTCVEWLRRYLENGKETLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWELSSQPTIPIVGIIAGLVLLGAVITGAVVAAVMWRRKSSDRKGGSYTQAASSDSAQGSDVSLTACKV	Literature-reported	HLA-A33 is associated with susceptibility to enterovirus 71 infection. Pediatrics. 2008 Dec;122(6):1271-6.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOMP5Y	"HLA class I histocompatibility antigen, A alpha chain (HLA-A)"	P04439	HLAA_HUMAN	MHC class I	Human leukocyte antigen A; HLA-A	HLA-A	"Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-A-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells (PubMed:2456340, PubMed:2784196, PubMed:1402688, PubMed:7504010, PubMed:9862734, PubMed:10449296, PubMed:12138174, PubMed:12393434, PubMed:15893615, PubMed:17189421, PubMed:19543285, PubMed:21498667, PubMed:24192765, PubMed:7694806, PubMed:24395804, PubMed:28250417). May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity (PubMed:25880248, PubMed:7506728, PubMed:7679507). Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells (PubMed:12796775, PubMed:18275829, PubMed:19542454, PubMed:28250417). Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via IFNG-induced immunoproteasome or via endopeptidase IDE/insulin-degrading enzyme (PubMed:17189421, PubMed:20364150, PubMed:17079320, PubMed:26929325, PubMed:27049119). Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9 (PubMed:7504010, PubMed:9862734). {ECO:0000269|PubMed:10449296, ECO:0000269|PubMed:12138174, ECO:0000269|PubMed:12393434, ECO:0000269|PubMed:12796775, ECO:0000269|PubMed:1402688, ECO:0000269|PubMed:15893615, ECO:0000269|PubMed:17079320, ECO:0000269|PubMed:17189421, ECO:0000269|PubMed:18275829, ECO:0000269|PubMed:19542454, ECO:0000269|PubMed:19543285, ECO:0000269|PubMed:20364150, ECO:0000269|PubMed:21498667, ECO:0000269|PubMed:24192765, ECO:0000269|PubMed:24395804, ECO:0000269|PubMed:2456340, ECO:0000269|PubMed:25880248, ECO:0000269|PubMed:26929325, ECO:0000269|PubMed:27049119, ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:28250417, ECO:0000269|PubMed:7504010, ECO:0000269|PubMed:7506728, ECO:0000269|PubMed:7679507, ECO:0000269|PubMed:7694806, ECO:0000269|PubMed:9862734}.; Allele A*01:01: Presents a restricted peptide repertoire including viral epitopes derived from IAV NP/nucleoprotein (CTELKLSDY), IAV PB1/polymerase basic protein 1 (VSDGGPNLY), HAdV-11 capsid L3/hexon protein (LTDLGQNLLY), SARS-CoV-2 3a/ORF3a (FTSDYYQLY) as well as tumor peptide antigens including MAGE1 (EADPTGHSY), MAGEA3 (EVDPIGHLY) and WT1 (TSEKRPFMCAY), all having in common a canonical motif with a negatively charged Asp or Glu residue at position 3 and a Tyr anchor residue at the C-terminus (PubMed:1402688, PubMed:7504010, PubMed:17189421, PubMed:20364150, PubMed:25880248, PubMed:30530481, PubMed:19177349, PubMed:24395804, PubMed:26758806, PubMed:32887977). A number of HLA-A*01:01-restricted peptides carry a post-translational modification with oxidation and N-terminal acetylation being the most frequent (PubMed:25880248). Fails to present highly immunogenic peptides from the EBV latent antigens (PubMed:18779413). {ECO:0000269|PubMed:1402688, ECO:0000269|PubMed:17189421, ECO:0000269|PubMed:18779413, ECO:0000269|PubMed:19177349, ECO:0000269|PubMed:20364150, ECO:0000269|PubMed:24395804, ECO:0000269|PubMed:25880248, ECO:0000269|PubMed:26758806, ECO:0000269|PubMed:30530481, ECO:0000269|PubMed:7504010}.; Allele A*02:01: A major allele in human populations, presents immunodominant viral epitopes derived from IAV M/matrix protein 1 (GILGFVFTL), HIV-1 env (TLTSCNTSV), HIV-1 gag-pol (ILKEPVHGV), HTLV-1 Tax (LLFGYPVYV), HBV C/core antigen (FLPSDFFPS), HCMV UL83/pp65 (NLVPMVATV) as well as tumor peptide antigens including MAGEA4 (GVYDGREHTV), WT1 (RMFPNAPYL) and CTAG1A/NY-ESO-1 (SLLMWITQC), all having in common hydrophobic amino acids at position 2 and at the C-terminal anchors. {ECO:0000269|PubMed:11502003, ECO:0000269|PubMed:12138174, ECO:0000269|PubMed:12796775, ECO:0000269|PubMed:17079320, ECO:0000269|PubMed:18275829, ECO:0000269|PubMed:19542454, ECO:0000269|PubMed:20619457, ECO:0000269|PubMed:22245737, ECO:0000269|PubMed:26929325, ECO:0000269|PubMed:2784196, ECO:0000269|PubMed:28250417, ECO:0000269|PubMed:7694806, ECO:0000269|PubMed:7935798, ECO:0000269|PubMed:8630735, ECO:0000269|PubMed:8805302, ECO:0000269|PubMed:8906788, ECO:0000269|PubMed:9177355}.; Allele A*03:01: Presents viral epitopes derived from IAV NP (ILRGSVAHK), HIV-1 nef (QVPLRPMTYK), HIV-1 gag-pol (AIFQSSMTK), SARS-CoV-2 N/nucleoprotein (KTFPPTEPK) as well as tumor peptide antigens including PMEL (LIYRRRLMK), NODAL (HAYIQSLLK), TRP-2 (RMYNMVPFF), all having in common hydrophobic amino acids at position 2 and Lys or Arg anchor residues at the C-terminus (PubMed:7504010, PubMed:7679507, PubMed:9862734, PubMed:19543285, PubMed:21943705, PubMed:2456340, PubMed:32887977). May also display spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein (PubMed:27049119). {ECO:0000269|PubMed:19543285, ECO:0000269|PubMed:21943705, ECO:0000269|PubMed:2456340, ECO:0000269|PubMed:27049119, ECO:0000269|PubMed:7504010, ECO:0000269|PubMed:7679507, ECO:0000269|PubMed:9862734}.; Allele A*11:01: Presents several immunodominant epitopes derived from HIV-1 gag-pol and HHV-4 EBNA4, containing the peptide motif with Val, Ile, Thr, Leu, Tyr or Phe at position 2 and Lys anchor residue at the C-terminus. Important in the control of HIV-1, EBV and HBV infections (PubMed:10449296). Presents an immunodominant epitope derived from SARS-CoV-2 N/nucleoprotein (KTFPPTEPK) (PubMed:32887977). {ECO:0000269|PubMed:10449296, ECO:0000269|PubMed:32887977}.; Allele A*23:01: Interacts with natural killer (NK) cell receptor KIR3DL1 and may contribute to functional maturation of NK cells and self-nonself discrimination during innate immune response. {ECO:0000269|PubMed:17182537}.; Allele A*24:02: Presents viral epitopes derived from HIV-1 nef (RYPLTFGWCF), EBV lytic- and latent-cycle antigens BRLF1 (TYPVLEEMF), BMLF1 (DYNFVKQLF) and LMP2 (IYVLVMLVL), SARS-CoV nucleocapsid/N (QFKDNVILL), as well as tumor peptide antigens including PRAME (LYVDSLFFL), all sharing a common signature motif, namely an aromatic residue Tyr or Phe at position 2 and a nonhydrophobic anchor residue Phe, Leu or Iso at the C-terminus (PubMed:9047241, PubMed:12393434, PubMed:24192765, PubMed:20844028). Interacts with natural killer (NK) cell receptor KIR3DL1 and may contribute to functional maturation of NK cells and self-nonself discrimination during innate immune response (PubMed:17182537, PubMed:18502829). {ECO:0000269|PubMed:12393434, ECO:0000269|PubMed:17182537, ECO:0000269|PubMed:18502829, ECO:0000269|PubMed:20844028, ECO:0000269|PubMed:24192765, ECO:0000269|PubMed:9047241}.; Allele A*26:01: Presents several epitopes derived from HIV-1 gag-pol (EVIPMFSAL, ETKLGKAGY) and env (LVSDGGPNLY), carrying as anchor residues preferentially Glu at position 1, Val or Thr at position 2 and Tyr at the C-terminus. {ECO:0000269|PubMed:15893615}.; Allele A*29:02: Presents peptides having a common motif, namely a Glu residue at position 2 and Tyr or Leu anchor residues at the C-terminus. {ECO:0000269|PubMed:8622959}.; Allele A*32:01: Interacts with natural killer (NK) cell receptor KIR3DL1 and may contribute to functional maturation of NK cells and self-nonself discrimination during innate immune response. {ECO:0000269|PubMed:17182537}.; Allele A*68:01: Presents viral epitopes derived from IAV NP (KTGGPIYKR) and HIV-1 tat (ITKGLGISYGR), having a common signature motif namely, Val or Thr at position 2 and positively charged residues Arg or Lys at the C-terminal anchor. {ECO:0000269|PubMed:1448153, ECO:0000269|PubMed:1448154, ECO:0000269|PubMed:2784196}.; Allele A*74:01: Presents immunodominant HIV-1 epitopes derived from gag-pol (GQMVHQAISPR, QIYPGIKVR) and rev (RQIHSISER), carrying an aliphatic residue at position 2 and Arg anchor residue at the C-terminus. May contribute to viral load control in chronic HIV-1 infection. {ECO:0000269|PubMed:21498667}."	.	1AKJ;1AO7;1AQD;1B0G;1B0R;1BD2;1DUY;1DUZ;1EEY;1EEZ;1HHG;1HHH;1HHI;1HHJ;1HHK;1HLA;1HSB;1I1F;1I1Y;1I4F;1I7R;1I7T;1I7U;1IM3;1JF1;1JHT;1LP9;1OGA;1P7Q;1Q94;1QEW;1QR1;1QRN;1QSE;1QSF;1QVO;1S8D;1S9W;1S9X;1S9Y;1T1W;1T1X;1T1Y;1T1Z;1T20;1T21;1T22;1TMC;1TVB;1TVH;1W72;1X7Q;2AV1;2AV7;2BCK;2BNQ;2BNR;2C7U;2CLR;2F53;2F54;2GIT;2GJ6;2GT9;2GTW;2GTZ;2GUO;2HLA;2HN7;2J8U;2JCC;2P5E;2P5W;2PYE;2UWE;2V2W;2V2X;2VLJ;2VLK;2VLL;2VLR;2X4N;2X4O;2X4P;2X4Q;2X4R;2X4S;2X4T;2X4U;2X70;2XPG;3BGM;3BH8;3BH9;3BHB;3BO8;3D25;3D39;3D3V;3FQN;3FQR;3FQT;3FQU;3FQW;3FQX;3FT2;3FT3;3FT4;3GIV;3GJF;3GSN;3GSO;3GSQ;3GSR;3GSU;3GSV;3GSW;3GSX;3H7B;3H9H;3H9S;3HAE;3HLA;3HPJ;3I6G;3I6K;3I6L;3IXA;3KLA;3MGO;3MGT;3MR9;3MRB;3MRC;3MRD;3MRE;3MRF;3MRG;3MRH;3MRI;3MRJ;3MRK;3MRL;3MRM;3MRN;3MRO;3MRP;3MRQ;3MRR;3MYJ;3NFN;3O3A;3O3B;3O3D;3O3E;3O4L;3PWJ;3PWL;3PWN;3PWP;3QDG;3QDJ;3QDM;3QEQ;3QFD;3QFJ;3QZW;3REW;3RL1;3RL2;3TO2;3UTQ;3UTS;3UTT;3V5D;3V5H;3V5K;3VXM;3VXN;3VXO;3VXP;3VXR;3VXS;3VXU;3W0W;3WL9;3WLB;4E5X;4EMZ;4EN2;4EUP;4F7M;4F7P;4F7T;4FTV;4GKN;4GKS;4HWZ;4HX1;4I48;4I4W;4JFD;4JFE;4JFF;4JFO;4JFP;4JFQ;4K7F;4L29;4L3C;4L3E;4MJ5;4MJ6;4MNQ;4N8V;4NNX;4NNY;4NO0;4NO2;4NO3;4NO5;4NQV;4NQX;4OV5;4QOK;4U6X;4U6Y;4UQ2;4UQ3;4WJ5;4WU5;4WU7;4WUU;5BRZ;5BS0;5C07;5C08;5C09;5C0A;5C0B;5C0C;5C0D;5C0E;5C0F;5C0G;5C0I;5C0J;5D2L;5D2N;5D9S;5DDH;5E00;5E6I;5E9D;5ENW;5EOT;5EU3;5EU4;5EU5;5EU6;5EUO;5F7D;5F9J;5FA3;5FA4;5FDW;5GRD;5GRG;5GSD;5HGA;5HGB;5HGD;5HGH;5HHM;5HHN;5HHO;5HHP;5HHQ;5HYJ;5IRO;5ISZ;5JHD;5JZI;5MEN;5MEO;5MEP;5MEQ;5MER;5N1Y;5N6B;5NHT;5NME;5NMF;5NMG;5NMH;5NMK;5NQK;5SWQ;5TEZ;5W1W;5WJL;5WJN;5WKF;5WKH;5WSH;5WWI;5WWJ;5WWU;5WXC;5WXD;5XOV;5YXN;5YXU;6AM5;6AMT;6AMU;6APN;6AT9;6D78;6D7G;6DKP;6EI2;6ENY;6EQA;6EQB;6EWA;6EWC;6EWO;6G3J;6G3K;6ID4;6J1W;6J29;6J2A;6JOZ;6JP3;6MPP;6NCA;6O9B;6O9C;6OPD;6PBH;6PTB;6PTE;6Q3K;6Q3S;6R2L;6RP9;6RPA;6RPB;6RSY;6SS7;6SS8;6SS9;6SSA;7L1B;7L1C;7L1D;7MLE;7PHR;7QPD;7RK7;7RM4;7RRG;7STF;7UC5;7UX3;8D4C;8D4D;8D4E;8D4F;8D4G;8D9R;8D9S;8D9T;8D9U;8D9V;8D9W;8DVG	MAVMAPRTLLLLLSGALALTQTWAGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDQETRNVKAQSQTDRVDLGTLRGYYNQSEAGSHTIQIMYGCDVGSDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAAHEAEQLRAYLDGTCVEWLRRYLENGKETLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWELSSQPTIPIVGIIAGLVLLGAVITGAVVAAVMWRRKSSDRKGGSYTQAASSDSAQGSDVSLTACKV	Clinical trial	"Clinical pipeline report, company report or official report of Roche"	.	.	.	.	.	.	.	.	.	.	.	hsa:3105	R-HSA-1236974;R-HSA-1236977;R-HSA-164940;R-HSA-198933;R-HSA-877300;R-HSA-8866654;R-HSA-909733;R-HSA-9705671;R-HSA-983170;	.	P04439;
TTGS10J	HLA class I antigen B-7 (HLA-B)	P01889	1B07_HUMAN	MHC class I	"MHC class I antigen B*7; HLAB; HLA class I histocompatibility antigen, B7 alpha chain; HLA class I histocompatibility antigen, B-7 alpha chain"	HLA-B	Involved in the presentation of foreign antigens to the immune system.	.	6AVG; 6AVF; 6AT5; 5WMP; 5WMO	MLVMAPRTVLLLLSAALALTETWAGSHSMRYFYTSVSRPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWDRNTQIYKAQAQTDRESLRNLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHDQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAAREAEQRRAYLEGECVEWLRRYLENGKDKLERADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPSSQSTVPIVGIVAGLAVLAVVVIGAVVAAVMCRRKSSGGKGGSYSQAACSDSAQGSDVSLTA	Clinical trial	Velimogene aliplasmid. Expert Opin Biol Ther. 2010 May;10(5):841-51.	25	.	MHC class I family	MHC class I family.	.	.	"Immunoglobulin C1-set domain; Class I Histocompatibility antigen, domains alpha 1 and 2; MHC_I C-terminus"	PF07654; PF00129; PF06623	PF07654; C1-set; PF00129; MHC_I; PF06623; MHC_I_C	.	.	hsa04144: Endocytosis; hsa04145: Phagosome; hsa04218: Cellular senescence; hsa04514: Cell adhesion molecules; hsa04612: Antigen processing and presentation; hsa04650: Natural killer cell mediated cytotoxicity; hsa04940: Type I diabetes mellitus; hsa05163: Human cytomegalovirus infection; hsa05165: Human papillomavirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05203: Viral carcinogenesis; hsa05320: Autoimmune thyroid disease; hsa05330: Allograft rejection; hsa05332: Graft-versus-host disease; hsa05416: Viral myocarditis	"R-HSA-1236974: ER-Phagosome pathway; R-HSA-1236977: Endosomal/Vacuolar pathway; R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-2172127: DAP12 interactions; R-HSA-6798695: Neutrophil degranulation; R-HSA-877300: Interferon gamma signaling; R-HSA-909733: Interferon alpha/beta signaling; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses; R-HSA-983170: Antigen Presentation: Folding, assembly and peptide loading of class I MHC"	.	.
TTU2I3J	HLA class II antigen DQ-2 alpha (HLA-DQA1)	P01909	DQA1_HUMAN	MHC class II	"MHC class II DQA1; HLADQA1; HLADCA; HLA-DQA1; HLA class II histocompatibility antigen, DQ alpha 1 chain; DCalpha; DC1 alpha chain"	HLA-DQA1	"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."	.	6MFG; 6MFF; 5KSV; 5KSU; 5KSB	MILNKALMLGALALTTVMSPCGGEDIVADHVASYGVNLYQSYGPSGQYTHEFDGDEQFYVDLGRKETVWCLPVLRQFRFDPQFALTNIAVLKHNLNSLIKRSNSTAATNEVPEVTVFSKSPVTLGQPNILICLVDNIFPPVVNITWLSNGHSVTEGVSETSFLSKSDHSFFKISYLTLLPSAEESYDCKVEHWGLDKPLLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTVFIIRGLRSVGASRHQGPL	Literature-reported	Preferential presentation of herpes simplex virus T-cell antigen by HLA DQA1*0501/DQB1*0201 in comparison to HLA DQA1*0201/DQB1*0201. Hum Immunol. 1997 Apr 1;53(2):195-205.	.	.	.	.	.	.	.	.	.	.	.	hsa04145: Phagosome; hsa04514: Cell adhesion molecules; hsa04612: Antigen processing and presentation; hsa04640: Hematopoietic cell lineage; hsa04658: Th1 and Th2 cell differentiation; hsa04659: Th17 cell differentiation; 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: Human T-cell leukemia virus 1 infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05310: Asthma; hsa05320: Autoimmune thyroid disease; hsa05321: Inflammatory bowel disease; hsa05322: Systemic lupus erythematosus; hsa05323: Rheumatoid arthritis; hsa05330: Allograft rejection; hsa05332: Graft-versus-host disease; hsa05416: Viral myocarditis	R-HSA-202424: Downstream TCR 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-2132295: MHC class II antigen presentation; R-HSA-389948: PD-1 signaling; R-HSA-877300: Interferon gamma signaling	.	P01909
TTL7VOU	Leukocyte antigen class II (HLA-DQB2)	Q29870	DQB2_HUMAN	.	"MHC class II antigen DQB2; HLA-DXB; HLA class II histocompatibility antigen, DX beta chain; HLA class II histocompatibility antigen, DQ beta 2 chain"	HLA-DQB2	"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."	.	.	MSWKMALQIPGGFWAAAVTVMLVMLSTPVAEARDFPKDFLVQFKGMCYFTNGTERVRGVARYIYNREEYGRFDSDVGEFQAVTELGRSIEDWNNYKDFLEQERAAVDKVCRHNYEAELRTTLQRQVEPTVTISPSRTEALNHHNLLVCSVTDFYPAQIKVRWFRNDQEETAGVVSTSLIRNGDWTFQILVMLEITPQRGDIYTCQVEHPSLQSPITVEWRAQSESAQSKMLSGIGGFVLGLIFLGLGLIIRHRGQKGPRGPPPAGLLH	Literature-reported	HLA class II antibodies in the treatment of hematologic malignancies. Semin Oncol. 2003 Aug;30(4):465-75.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P05538
TTYA75N	MHC class II antigen DR (HLA-DR)	P01903; P01911; P79483; P13762; Q30154	DRA_HUMAN; 2B1F_HUMAN; DRB3_HUMAN; DRB4_HUMAN; DRB5_HUMAN	MHC class II	HLA class II histocompatibility antigen	HLA-DRA	"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."	.	.	MAISGVPVLGFFIIAVLMSAQESWAIKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYTPITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWEFDAPSPLPETTENVVCALGLTVGLVGIIIGTIFIIKGVRKSNAAERRGPL	Clinical trial	"The humanized anti-HLA-DR moAb, IMMU-114, depletes APCs and reduces alloreactive T cells: implications for preventing GVHD. Bone Marrow Transplant. 2012 Jul;47(7):967-80."	17	.	.	.	.	.	.	.	.	.	.	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	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	.	P01903
TTUXSTW	HLA class II antigen DR10 (HLA-DRB1)	Q30167	2B1A_HUMAN	MHC class II	"MHC class II antigen DRB1*10; HLADRB1; HLA class II histocompatibility antigen, DRB110 beta chain; DRw10"	HLA-DRB1	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.	.	.	MVCLKLPGGSCMTALTVTLMVLSSPLALSGDTRPRFLWQPKRECHFFNGTERVRFLDRYFYNQEESVRFDSDVGEFRAVTELGRPDAEYWNSQKDILEQARAAVDTYCRHNYGVVESFTVQRRVQPKVTVYPSKTQPLQHHNLLVCSVSGFYPGSIEVRWFLNGQEEKAGMVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSPLTVEWRARSESAQSKMLSGVGGFVLGLLFLGAGLFIYFRNQKGHSGLQPTGFLS	Clinical trial	"Clinical pipeline report, company report or official report of Peregrine Pharmaceuticals."	19	.	.	.	.	.	.	.	.	.	.	.	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	.	.
TTLCMWF	MHC class II antigen DRB1*1 (HLA-DRB1)	P04229	2B11_HUMAN	MHC class II	"HLA class II histocompatibility antigen, DRB1-1 beta chain; DR1; DR-1"	HLA-DRB1	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.	.	6CQR; 6CQJ; 4X5X; 4X5W; 4OV5	MVCLKLPGGSCMTALTVTLMVLSSPLALSGDTRPRFLWQPKRECHFFNGTERVRFLDRYFYNQEESVRFDSDVGEFRAVTELGRPDAEYWNSQKDILEQARAAVDTYCRHNYGVVESFTVQRRVQPKVTVYPSKTQPLQHHNLLVCSVSGFYPGSIEVRWFLNGQEEKAGMVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSPLTVEWRARSESAQSKMLSGVGGFVLGLLFLGAGLFIYFRNQKGHSGLQPTGFLS	Successful	Mechanism of action of glatiramer acetate in multiple sclerosis and its potential for the development of new applications. Proc Natl Acad Sci U S A. 2004 Oct 5;101 Suppl 2:14593-8.	34	.	.	.	.	.	.	.	.	.	.	.	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	.	.
TTLKFB3	MHC class I antigen G (HLA-G)	P17693	HLAG_HUMAN	.	HLA G antigen; MHC class I antigen G	HLA-G	"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."	.	.	MVVMAPRTLFLLLSGALTLTETWAGSHSMRYFSAAVSRPGRGEPRFIAMGYVDDTQFVRFDSDSACPRMEPRAPWVEQEGPEYWEEETRNTKAHAQTDRMNLQTLRGYYNQSEASSHTLQWMIGCDLGSDGRLLRGYEQYAYDGKDYLALNEDLRSWTAADTAAQISKRKCEAANVAEQRRAYLEGTCVEWLHRYLENGKEMLQRADPPKTHVTHHPVFDYEATLRCWALGFYPAEIILTWQRDGEDQTQDVELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLMLRWKQSSLPTIPIMGIVAGLVVLAAVVTGAAVAAVLWRKKSSD	Clinical trial	"Clinical pipeline report, company report or official report of Tizona Therapeutics."	.	.	.	.	.	.	.	.	.	.	.	hsa04144: Endocytosis; hsa04145: Phagosome; hsa04218: Cellular senescence; hsa04514: Cell adhesion molecules; hsa04612: Antigen processing and presentation; hsa04650: Natural killer cell mediated cytotoxicity; hsa04940: Type I diabetes mellitus; hsa05163: Human cytomegalovirus infection; hsa05165: Human papillomavirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05203: Viral carcinogenesis; hsa05320: Autoimmune thyroid disease; hsa05330: Allograft rejection; hsa05332: Graft-versus-host disease; hsa05416: Viral myocarditis	"R-HSA-1236974: ER-Phagosome pathway; R-HSA-1236977: Endosomal/Vacuolar pathway; R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-877300: Interferon gamma signaling; R-HSA-909733: Interferon alpha/beta signaling; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses; R-HSA-983170: Antigen Presentation: Folding, assembly and peptide loading of class I MHC"	.	P17693
TTT0HW3	Porphobilinogen deaminase (HMBS)	P08397	HEM3_HUMAN	Alkyl aryl transferase	Preuroporphyrinogen synthase; PBGD; Hydroxymethylbilane synthase; HMBS	HMBS	Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.	EC 2.5.1.61	5M7F; 5M6R; 3EQ1; 3ECR	MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTGDKILDTALSKIGEKSLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPHDAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQQEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHDPETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIHVPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNLGISLANLLLSKGAKNILDVARQLNDAH	Clinical trial	"Safety, pharmacokinetics and pharmocodynamics of recombinant human porphobilinogen deaminase in healthy subjects and asymptomatic carriers of the acute intermittent porphyria gene who have increased porphyrin precursor excretion. Clin Pharmacokinet. 2007;46(4):335-49."	21	.	.	.	.	.	.	.	.	.	.	hsa00860:Porphyrin and chlorophyll metabolism; hsa01100:Metabolic pathways	R-HSA-189451: Heme biosynthesis	MetaCyc:HS07607-MON	P08397
TTBA219	High mobility group protein HMG-I/Y (HMGA1)	P17096	HMGA1_HUMAN	.	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)	HMGA1	"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."	.	2EZG; 2EZF; 2EZE; 2EZD	MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ	Literature-reported	"HMG-I/Y, a new c-Myc target gene and potential oncogene. Mol Cell Biol. 2000 Aug;20(15):5490-502."	.	.	.	HMGA family.	.	.	.	.	.	.	.	.	R-HSA-162592: Integration of provirus; R-HSA-164843: 2-LTR circle formation; 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; R-HSA-2559584: Formation of Senescence-Associated Heterochromatin Foci (SAHF)	.	P17096
TTSTVM0	High mobility group protein HMGI-C (HMGA2)	P52926	HMGA2_HUMAN	.	High mobility group AThook protein 2; High mobility group AT-hook protein 2; HMGIC	HMGA2	"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."	.	.	MSARGEGAGQPSTSAQGQPAAPAPQKRGRGRPRKQQQEPTGEPSPKRPRGRPKGSKNKSPSKAAQKKAEATGEKRPRGRPRKWPQQVVQKKPAQEETEETSSQESAEED	Literature-reported	HMGA2 regulates lung cancer proliferation and metastasis. Thorac Cancer. 2017 Sep;8(5):501-510.	.	.	.	HMGA family.	.	.	AT hook motif	PF02178	PF02178; AT_hook	.	.	hsa05202: Transcriptional misregulation in cancer; hsa05206: MicroRNAs in cancer	R-HSA-2559584: Formation of Senescence-Associated Heterochromatin Foci (SAHF)	.	P52926
TTWQYB7	High mobility group protein B1 (HMGB1)	P09429	HMGB1_HUMAN	.	High mobility group protein 1; High mobility group box chromosomal protein 1; HMG1; HMG-1	HMGB1	"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."	.	6CIM; 6CIL; 6CIK; 6CIJ; 6CG0	MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	HMGB family.	.	.	HMG (high mobility group) box; HMG-box domain	PF00505; PF09011	PF00505; HMG_box; PF09011; HMG_box_2	.	.	hsa03410:Base excision repair	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	.	P09429
TTA78JQ	High-mobility group protein B2 (HMGB2)	P26583	HMGB2_HUMAN	.	High mobility group protein B2; High mobility group protein 2; HMG2; HMG-2	HMGB2	"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."	.	.	MGKGDPNKPRGKMSSYAFFVQTCREEHKKKHPDSSVNFAEFSKKCSERWKTMSAKEKSKFEDMAKSDKARYDREMKNYVPPKGDKKGKKKDPNAPKRPPSAFFLFCSEHRPKIKSEHPGLSIGDTAKKLGEMWSEQSAKDKQPYEQKAAKLKEKYEKDIAAYRAKGKSEAGKKGPGRPTGSKKKNEPEDEEEEEEEEDEDEEEEDEDEE	Literature-reported	HMGB2 promotes the malignancy of human gastric cancer and indicates poor survival outcome. Hum Pathol. 2019 Feb;84:133-141.	.	.	.	HMGB family.	.	.	HMG (high mobility group) box; HMG-box domain	PF00505; PF09011	PF00505; HMG_box; PF09011; HMG_box_2	.	.	.	R-HSA-140342: Apoptosis induced DNA fragmentation	.	P26583
TTPADOQ	HMG-CoA reductase (HMGCR)	P04035	HMDH_HUMAN	CH-OH donor oxidoreductase	3-hydroxy-3-methylglutaryl-coenzyme A reductase	HMGCR	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.	EC 1.1.1.34	3CDB; 3CDA; 3CD7; 3CD5; 3CD0	MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASTLAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKRIEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQTETESTLSLKNPITSPVVTQKKVPDNCCRREPMLVRNNQKCDSVEEETGINRERKVEVIKPLVAETDTPNRATFVVGNSSLLDTSSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA	Successful	Emerging drugs in peripheral arterial disease. Expert Opin Emerg Drugs. 2006 Mar;11(1):75-90.	34	EC:1.1	CH OH donor oxidoreductase	HMG-CoA reductase family.	1.1.1.34	Acting on the CH-OH group of donors	Hydroxymethylglutaryl-coenzyme A reductase; Sterol-sensing domain of SREBP cleavage-activation	PF00368; PF12349	PF00368; HMG-CoA_red; PF12349; Sterol-sensing	2.A.6.6.5	The Resistance-Nodulation-Cell Division (RND) Superfamily	hsa00900:Terpenoid backbone biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics; hsa04152:AMPK signaling pathway; hsa04976:Bile secretion	R-HSA-191273: Cholesterol biosynthesis; R-HSA-1989781: PPARA activates gene expression; R-HSA-2426168: Activation of gene expression by SREBF (SREBP); R-HSA-9619665: EGR2 and SOX10-mediated initiation of Schwann cell myelination	MetaCyc:HS03652-MON	P04035
TTQF4TK	Hydroxymethylglutaryl-CoA synthase 1 (HMGCS1)	Q01581	HMCS1_HUMAN	.	"Hydroxymethylglutaryl-CoA synthase, cytoplasmic; HMGCS; HMG-CoA synthase; 3-hydroxy-3-methylglutaryl coenzyme A synthase 1"	HMGCS1	"This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase."	EC 2.3.3.10	2P8U	MPGSLPLNAEACWPKDVGIVALEIYFPSQYVDQAELEKYDGVDAGKYTIGLGQAKMGFCTDREDINSLCMTVVQNLMERNNLSYDCIGRLEVGTETIIDKSKSVKTNLMQLFEESGNTDIEGIDTTNACYGGTAAVFNAVNWIESSSWDGRYALVVAGDIAVYATGNARPTGGVGAVALLIGPNAPLIFERGLRGTHMQHAYDFYKPDMLSEYPIVDGKLSIQCYLSALDRCYSVYCKKIHAQWQKEGNDKDFTLNDFGFMIFHSPYCKLVQKSLARMLLNDFLNDQNRDKNSIYSGLEAFGDVKLEDTYFDRDVEKAFMKASSELFSQKTKASLLVSNQNGNMYTSSVYGSLASVLAQYSPQQLAGKRIGVFSYGSGLAATLYSLKVTQDATPGSALDKITASLCDLKSRLDSRTGVAPDVFAENMKLREDTHHLVNYIPQGSIDSLFEGTWYLVRVDEKHRRTYARRPTPNDDTLDEGVGLVHSNIATEHIPSPAKKVPRLPATAAEPEAAVISNGEH	Literature-reported	Inhibition of 3-hydroxy-3-methylglutaryl-CoA synthase and cholesterol biosynthesis by beta-lactone inhibitors and binding of these inhibitors to the enzyme. Biochem J. 1993 Feb 1;289 ( Pt 3):889-95.	0	.	.	.	.	.	.	.	.	.	.	"hsa00280: Valine, leucine and isoleucine degradation; hsa00650: Butanoate metabolism; hsa00900: Terpenoid backbone biosynthesis; hsa01100: Metabolic pathways; hsa03320: PPAR signaling pathway"	R-HSA-191273: Cholesterol biosynthesis; R-HSA-1989781: PPARA activates gene expression; R-HSA-2426168: Activation of gene expression by SREBF (SREBP)	MetaCyc:ENSG00000112972-MON	Q01581
TTS0EZJ	Hydroxymethylglutaryl-CoA synthase 2 (HMGCS2)	P54868	HMCS2_HUMAN	Acyltransferase	HMGCS2; HMG-CoAsynthase; 3-hydroxy-3-methylglutaryl coenzyme A synthase 2	HMGCS2	"This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase."	EC 2.3.3.10	2WYA	MQRLLTPVKRILQLTRAVQETSLTPARLLPVAHQRFSTASAVPLAKTDTWPKDVGILALEVYFPAQYVDQTDLEKYNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERIQLPWDSVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSSWDGRYAMVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLALERGLRGTHMENVYDFYKPNLASEYPIVDGKLSIQCYLRALDRCYTSYRKKIQNQWKQAGSDRPFTLDDLQYMIFHTPFCKMVQKSLARLMFNDFLSASSDTQTSLYKGLEAFGGLKLEDTYTNKDLDKALLKASQDMFDKKTKASLYLSTHNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSQDAAPGSPLDKLVSSTSDLPKRLASRKCVSPEEFTEIMNQREQFYHKVNFSPPGDTNSLFPGTWYLERVDEQHRRKYARRPV	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	"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"	R-HSA-1989781:PPARA activates gene expression	MetaCyc:HS05836-MON	P54868
TTI6V2A	Heme oxygenase 1 (HMOX1)	P09601	HMOX1_HUMAN	Paired donor oxygen oxidoreductase	HO1; HO-1; HO	HMOX1	"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."	EC 1.14.14.18	6EHA; 5BTQ; 4WD4; 3TGM; 3K4F	MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM	Clinical trial	Chemoprevention of severe neonatal hyperbilirubinemia. Semin Perinatol. 2004 Oct;28(5):365-8.	21	EC:1.14	Oxidoreductases acting on paired donors	heme oxygenase family.	1.14.14.18 	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	Heme oxygenase	PF01126	PF01126; Heme_oxygenase	.	.	hsa00860:Porphyrin and chlorophyll metabolism; hsa04066:HIF-1 signaling pathway; hsa04978:Mineral absorption; hsa05206:MicroRNAs in cancer	R-HSA-917937:Iron uptake and transport	MetaCyc:HS02027-MON	P09601
TTWZRL4	Heme oxygenase 2 (HMOX2)	P30519	HMOX2_HUMAN	Paired donor oxygen oxidoreductase	HO2; HO-2	HMOX2	"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."	EC 1.14.14.18	5UCA; 5UC9; 5UC8; 4WMH; 2RGZ	MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQAGSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVLRKPSLQFILAAGVALAAGLLAWYYM	Literature-reported	Heme oxygenase-2 suppresses acute inflammation and improves the survival of skin allografts. Int Immunopharmacol. 2018 Oct;63:191-197.	.	EC:1.14	.	heme oxygenase family.	1.14.14.18 	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	Heme oxygenase	PF01126	PF01126; Heme_oxygenase	.	.	hsa00860: Porphyrin metabolism; hsa01100: Metabolic pathways; hsa04978: Mineral absorption	R-HSA-189483: Heme degradation; R-HSA-6798695: Neutrophil degranulation; R-HSA-8980692: RHOA GTPase cycle; R-HSA-917937: Iron uptake and transport; R-HSA-9707564: Cytoprotection by HMOX1	.	P30519
TT01M3K	Hepatocyte nuclear factor 1-alpha (HNF1A)	P20823	HNF1A_HUMAN	.	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	HNF1A	"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."	.	2GYP; 1IC8	MVSKLSQLQTELLAALLESGLSKEALIQALGEPGPYLLAGEGPLDKGESCGGGRGELAELPNGLGETRGSEDETDDDGEDFTPPILKELENLSPEEAAHQKAVVETLLQEDPWRVAKMVKSYLQQHNIPQREVVDTTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREVAQQFTHAGQGGLIEEPTGDELPTKKGRRNRFKWGPASQQILFQAYERQKNPSKEERETLVEECNRAECIQRGVSPSQAQGLGSNLVTEVRVYNWFANRRKEEAFRHKLAMDTYSGPPPGPGPGPALPAHSSPGLPPPALSPSKVHGVRYGQPATSETAEVPSSSGGPLVTVSTPLHQVSPTGLEPSHSLLSTEAKLVSAAGGPLPPVSTLTALHSLEQTSPGLNQQPQNLIMASLPGVMTIGPGEPASLGPTFTNTGASTLVIGLASTQAQSVPVINSMGSSLTTLQPVQFSQPLHPSYQQPLMPPVQSHVTQSPFMATMAQLQSPHALYSHKPEVAQYTHTGLLPQTMLITDTTNLSALASLTPTKQVFTSDTEASSESGLHTPASQATTLHVPSQDPAGIQHLQPAHRLSASPTVSSSSLVLYQSSDSSNGQSHLLPSNHSVIETFISTQMASSSQ	Clinical trial	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	19	.	.	HNF1 homeobox family.	.	.	"Hepatocyte nuclear factor 1 (HNF-1), N terminus; Hepatocyte nuclear factor 1 (HNF-1), alpha isoform C terminus; Hepatocyte nuclear factor 1 (HNF-1), beta isoform C terminus"	PF04814; PF04813; PF04812	PF04814; HNF-1_N; PF04813; HNF-1A_C; PF04812; HNF-1B_C	.	.	hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04950:Maturity onset diabetes of the young	R-HSA-210745:Regulation of gene expression in beta cells	.	P20823
TT2F3CD	Hepatocyte nuclear factor 4-alpha (HNF4A)	P41235	HNF4A_HUMAN	Nuclear hormone receptor	Transcription factor HNF-4; Transcription factor 14; TCF14; TCF-14; Nuclear receptor subfamily 2 group A member 1; NR2A1; HNF4; HNF-4-alpha	HNF4A	"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."	.	6CHT; 4IQR; 4B7W; 3FS1; 3CBB	MRLSKTLVDMDMADYSAALDPAYTTLEFENVQVLTMGNDTSPSEGTNLNAPNSLGVSALCAICGDRATGKHYGASSCDGCKGFFRRSVRKNHMYSCRFSRQCVVDKDKRNQCRYCRLKKCFRAGMKKEAVQNERDRISTRRSSYEDSSLPSINALLQAEVLSRQITSPVSGINGDIRAKKIASIADVCESMKEQLLVLVEWAKYIPAFCELPLDDQVALLRAHAGEHLLLGATKRSMVFKDVLLLGNDYIVPRHCPELAEMSRVSIRILDELVLPFQELQIDDNEYAYLKAIIFFDPDAKGLSDPGKIKRLRSQVQVSLEDYINDRQYDSRGRFGELLLLLPTLQSITWQMIEQIQFIKLFGMAKIDNLLQEMLLGGSPSDAPHAHHPLHPHLMQEHMGTNVIVANTMPTHLSNGQMCEWPRPRGQAATPETPQPSPPGGSGSEPYKLLPGAVATIVKPLSAIPQPTITKQEVI	Literature-reported	HNF4alpha antagonists discovered by a high-throughput screen for modulators of the human insulin promoter. Chem Biol. 2012 Jul 27;19(7):806-18.	0	Nuclear hormone receptor	Nuclear hormone receptor family	nuclear hormone receptor family. NR2 subfamily.	.	.	"Ligand-binding domain of nuclear hormone receptor; Zinc finger, C4 type (two domains)"	PF00104; PF00105	PF00104; Hormone_recep; PF00105; zf-C4	.	.	hsa04152:AMPK signaling pathway; hsa04950:Maturity onset diabetes of the young	R-HSA-383280:Nuclear Receptor transcription pathway	.	P41235
TT2B6EV	Histamine N-methyltransferase (HNMT)	P50135	HNMT_HUMAN	Methyltransferase	Histamine-N-methyltransferase; HNMT; HMT	HNMT	Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine.	EC 2.1.1.8	2AOX; 2AOW; 2AOV; 2AOU; 2AOT	MASSMRSLFSDHGKYVESFRRFLNHSTEHQCMQEFMDKKLPGIIGRIGDTKSEIKILSIGGGAGEIDLQILSKVQAQYPGVCINNEVVEPSAEQIAKYKELVAKTSNLENVKFAWHKETSSEYQSRMLEKKELQKWDFIHMIQMLYYVKDIPATLKFFHSLLGTNAKMLIIVVSGSSGWDKLWKKYGSRFPQDDLCQYITSDDLTQMLDNLGLKYECYDLLSTMDISDCFIDGNENGDLLWDFLTETCNFNATAPPDLRAELGKDLQEPEFSAKKEGKVLFNNTLSFIVIEA	Successful	"Effect of amodiaquine, a histamine N-methyltransferase inhibitor, on, Propionibacterium acnes and lipopolysaccharide-induced hepatitis in mice. Eur J Pharmacol. 2007 Mar 8;558(1-3):179-84."	34	.	.	.	.	.	.	.	.	.	.	hsa00340:Histidine metabolism	"R-HSA-2408508: Metabolism of ingested SeMet, Sec, MeSec into H2Se; R-HSA-70921: Histidine catabolism"	MetaCyc:HS07674-MON	P50135
TTPJ9XK	hnRNP A1 messenger RNA (HNRNPA1 mRNA)	P09651	ROA1_HUMAN	mRNA target	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)	HNRNPA1	"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."	.	6DCL; 6BXX; 5ZGL; 5MPL; 5MPG	MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGGYGGGGPGYSGGSRGYGSGGQGYGNQGSGYGGSGSYDSYNNGGGGGFGGGSGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF	Literature-reported	"US patent application no. 6,165,789, Antisense modulation of hnRNP A1 expression."	0	mRNA	mRNA target	.	.	.	"Nuclear factor hnRNPA1; RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)"	PF11627; PF00076	PF11627; HnRNPA1; PF00076; RRM_1	.	.	hsa03040:Spliceosome	R-HSA-72163:mRNA Splicing - Major Pathway	.	P09651
TT8UPW6	hnRNP A2/B1 messenger RNA (HNRNPA2B1 mRNA)	P22626	ROA2_HUMAN	mRNA target	hnRNP A2/B1 (mRNA); Heterogeneous nuclear ribonucleoproteins A2/B1 (mRNA); HNRPA2B1 (mRNA)	HNRNPA2B1	"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."	.	5WWG; 5WWF; 5WWE; 5HO4; 5EN1	MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY	Literature-reported	Galectin-3 interacts with components of the nuclear ribonucleoprotein complex. BMC Cancer. 2016 Jul 19;16:502.	.	mRNA	mRNA target	.	.	.	"RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)"	PF00076	PF00076; RRM_1	.	.	hsa05014: Amyotrophic lateral sclerosis	R-HSA-72163: mRNA Splicing - Major Pathway; R-HSA-72203: Processing of Capped Intron-Containing Pre-mRNA; R-HSA-8950505: Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation	.	P22626
TTEX4ZA	Homeobox protein Hox-A11 (HOXA11)	P31270	HXA11_HUMAN	.	Homeobox protein HoxA11; Homeobox protein Hox1I; Homeobox protein Hox-1I; HOX1I	HOXA11	Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.	.	.	MDFDERGPCSSNMYLPSCTYYVSGPDFSSLPSFLPQTPSSRPMTYSYSSNLPQVQPVREVTFREYAIEPATKWHPRGNLAHCYSAEELVHRDCLQAPSAAGVPGDVLAKSSANVYHHPTPAVSSNFYSTVGRNGVLPQAFDQFFETAYGTPENLASSDYPGDKSAEKGPPAATATSAAAAAAATGAPATSSSDSGGGGGCRETAAAAEEKERRRRPESSSSPESSSGHTEDKAGGSSGQRTRKKRCPYTKYQIRELEREFFFSVYINKEKRLQLSRMLNLTDRQVKIWFQNRRMKEKKINRDRLQYYSANPLL	Literature-reported	"Regulation of HOXA11-AS/miR-214-3p/EZH2 axis on the growth, migration and invasion of glioma cells. Biomed Pharmacother. 2017 Nov;95:1504-1513."	.	.	.	Abd-B homeobox family.	.	.	Protein of unknown function (DUF3528); Homeodomain	PF12045; PF00046	PF12045; DUF3528; PF00046; Homeodomain	.	.	hsa05202: Transcriptional misregulation in cancer	.	.	P31270
TTN26OM	Homeobox protein Hox-A13 (HOXA13)	P31271	HXA13_HUMAN	.	Homeobox protein HoxA13; Homeobox protein Hox1J; HOXA13	HOXA13	Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.	.	2L7Z	MTASVLLHPRWIEPTVMFLYDNGGGLVADELNKNMEGAAAAAAAAAAAAAAGAGGGGFPHPAAAAAGGNFSVAAAAAAAAAAAANQCRNLMAHPAPLAPGAASAYSSAPGEAPPSAAAAAAAAAAAAAAAAAASSSGGPGPAGPAGAEAAKQCSPCSAAAQSSSGPAALPYGYFGSGYYPCARMGPHPNAIKSCAQPASAAAAAAFADKYMDTAGPAAEEFSSRAKEFAFYHQGYAAGPYHHHQPMPGYLDMPVVPGLGGPGESRHEPLGLPMESYQPWALPNGWNGQMYCPKEQAQPPHLWKSTLPDVVSHPSDASSYRRGRKKRVPYTKVQLKELEREYATNKFITKDKRRRISATTNLSERQVTIWFQNRRVKEKKVINKLKTTS	Literature-reported	Transcriptional and posttranscriptional regulation of HOXA13 by lncRNA HOTTIP facilitates tumorigenesis and metastasis in esophageal squamous carci... Oncogene. 2017 Sep 21;36(38):5392-5406.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P31271
TTXSVQP	Homeobox protein Hox-A5 (HOXA5)	P20719	HXA5_HUMAN	Antp homeobox	Homeobox protein HoxA5; Homeobox protein Hox1C; Homeobox protein Hox-1C; HOX1C	HOXA5	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.	.	.	MSSYFVNSFCGRYPNGPDYQLHNYGDHSSVSEQFRDSASMHSGRYGYGYNGMDLSVGRSGSGHFGSGERARSYAASASAAPAEPRYSQPATSTHSPQPDPLPCSAVAPSPGSDSHHGGKNSLSNSSGASADAGSTHISSREGVGTASGAEEDAPASSEQASAQSEPSPAPPAQPQIYPWMRKLHISHDNIGGPEGKRARTAYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLSERQIKIWFQNRRMKWKKDNKLKSMSMAAAGGAFRP	Literature-reported	Knockdown of HOXA5 inhibits the tumorigenesis in esophageal squamous cell cancer. Biomed Pharmacother. 2017 Feb;86:149-154.	.	Antp homeobox	Antp homeobox family	Antp homeobox family.	.	.	Homeodomain	PF00046	PF00046; Homeodomain	.	.	.	.	.	P20719
TTMRE4Q	Homeobox protein Hox-A7 (HOXA7)	P31268	HXA7_HUMAN	Antp homeobox	HoxA7; Hox-1A; Hox 1.1; Homeobox protein Hox-1A; Homeobox protein Hox 1.1; HOX1A	HOXA7	Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.	.	.	MSSSYYVNALFSKYTAGASLFQNAEPTSCSFAPNSQRSGYGAGAGAFASTVPGLYNVNSPLYQSPFASGYGLGADAYGNLPCASYDQNIPGLCSDLAKGACDKTDEGALHGAAEANFRIYPWMRSSGPDRKRGRQTYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLTERQIKIWFQNRRMKWKKEHKDEGPTAAAAPEGAVPSAAATAAADKADEEDDDEEEEDEEE	Literature-reported	Functional contribution of EEN to leukemogenic transformation by MLL-EEN fusion protein. Oncogene. 2004 Apr 22;23(19):3385-94.	.	Antp homeobox	Antp homeobox family	Antp homeobox family.	.	.	Homeodomain	PF00046	PF00046; Homeodomain	.	.	.	.	.	P31268
TTZ6I58	Homeobox protein Hox-B13 (HOXB13)	Q92826	HXB13_HUMAN	.	Hoxb-13; HOXB13	HOXB13	Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.	.	5NO6; 5EGO; 5EG0; 5EF6; 5EEA	MEPGNYATLDGAKDIEGLLGAGGGRNLVAHSPLTSHPAAPTLMPAVNYAPLDLPGSAEPPKQCHPCPGVPQGTSPAPVPYGYFGGGYYSCRVSRSSLKPCAQAATLAAYPAETPTAGEEYPSRPTEFAFYPGYPGTYQPMASYLDVSVVQTLGAPGEPRHDSLLPVDSYQSWALAGGWNSQMCCQGEQNPPGPFWKAAFADSSGQHPPDACAFRRGRKKRIPYSKGQLRELEREYAANKFITKDKRRKISAATSLSERQITIWFQNRRVKEKKVLAKVKNSATP	Literature-reported	Androgen-independent expression of hoxb-13 in the mouse prostate. Prostate. 1999 Nov 1;41(3):203-7.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q92826
TTLC8E1	Haptoglobin (HP)	P00738	HPT_HUMAN	Peptidase	Haptoglobin beta chain; HP	HP	"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}."	.	5HU6; 4X0L; 4WJG	MSALGAVIALLLWGQLFAVDSGNDVTDIADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNDKKQWINKAVGDKLPECEADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNNEKQWINKAVGDKLPECEAVCGKPKNPANPVQRILGGHLDAKGSFPWQAKMVSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYSQVDIGLIKLKQKVSVNERVMPICLPSKDYAEVGRVGYVSGWGRNANFKFTDHLKYVMLPVADQDQCIRHYEGSTVPEKKTPKSPVGVQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDLEEDTWYATGILSFDKSCAVAEYGVYVKVTSIQDWVQKTIAEN	Clinical trial	"Zonulin, regulation of tight junctions, and autoimmune diseases"	25	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2168880: Scavenging of heme from plasma; R-HSA-6798695: Neutrophil degranulation	.	P00738
TT8DSFC	Hydroxyphenylpyruvate dioxygenase (HPD)	P32754	HPPD_HUMAN	Single donor oxidoreductase	HPPDase; HPD; F Alloantigen; 4HPPD	HPD	Key enzyme in the degradation of tyrosine.	EC 1.13.11.27	5EC3; 3ISQ	MTTYSDKGAKPERGRFLHFHSVTFWVGNAKQAASFYCSKMGFEPLAYRGLETGSREVVSHVIKQGKIVFVLSSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCDYIVQKARERGAKIMREPWVEQDKFGKVKFAVLQTYGDTTHTLVEKMNYIGQFLPGYEAPAFMDPLLPKLPKCSLEMIDHIVGNQPDQEMVSASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVANYEESIKMPINEPAPGKKKSQIQEYVDYNGGAGVQHIALKTEDIITAIRHLRERGLEFLSVPSTYYKQLREKLKTAKIKVKENIDALEELKILVDYDEKGYLLQIFTKPVQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQNLRGNLTNMETNGVVPGM	Successful	Experience of nitisinone for the pharmacological treatment of hereditary tyrosinaemia type 1. Expert Opin Pharmacother. 2008 May;9(7):1229-36.	34	.	.	.	.	.	.	.	.	.	.	mmu00130:Ubiquinone and other terpenoid-quinone biosynthesis; mmu00350:Tyrosine metabolism; mmu00360:Phenylalanine metabolism; mmu01100:Metabolic pathways	R-HSA-8963684: Tyrosine catabolism	MetaCyc:HS08267-MON	P32754
TTCYE56	Glutathione-dependent PGD synthase (HPGDS)	O60760	HPGDS_HUMAN	Intramolecular oxidoreductases	HPGDS; Glutathione-S-transferase; GST class-alpha	HPGDS	"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."	EC 5.3.99.2	6N4E; 5YX1; 5YWX; 5YWE; 5AIX	MPNYKLTYFNMRGRAEIIRYIFAYLDIQYEDHRIEQADWPEIKSTLPFGKIPILEVDGLTLHQSLAIARYLTKNTDLAGNTEMEQCHVDAIVDTLDDFMSCFPWAEKKQDVKEQMFNELLTYNAPHLMQDLDTYLGGREWLIGNSVTWADFYWEICSTTLLVFKPDLLDNHPRLVTLRKKVQAIPAVANWIKRRPQTKL	Successful	X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Mar 1;61(Pt 3):263-5.	34	.	.	.	.	.	.	.	.	.	.	hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways	R-HSA-156590: Glutathione conjugation; R-HSA-2162123: Synthesis of Prostaglandins (PG) and Thromboxanes (TX)	MetaCyc:HS08788-MON	O60760
TTA258K	Parainfluenza Hemagglutinin-neuraminidase glycoprotein (HPIV HN)	P16071	HN_PI1HW	.	Hemagglutinin-neuraminidase	HPIV HN	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).	EC 3.2.1.18	.	MAEKGKTNSSYWSTTRNDNSTVNTYIDTPAGKTHIWLLIATTMHTILSFIIMILCIDLIIKQDTCMKTNIMTVSSMNESAKTIKETITELIRQEVISRTINIQSSVQSGIPILLNKQSRDLTQLIEKSCNRQELAQICENTIAIHHADGISPLDPHDFWRCPVGEPLLSNNPNISLLPGPSLLSGSTTISGCVRLPSLSIGDAIYAYSSNLITQGCADIGKSYQVLQLGYISLNSDMYPDLKPVISHTYDINDNRKSCSVIAAGTRGYQLCSLPTVNETTDYSSEGIEDLVFDILDLKGKTKSHRYKNEDITFDHPFSAMYPSVGSGIKIENTLIFLGYGGLTTPLQGDTKCVTNRCANVNQSVCNDALKITWLKKRQVVNVLIRINNYLSDRPKIVVETIPITQNYLGAEGRLLKLGKKIYIYTRSSGWHSHLQIGSLDINNPMTIKWAPHEVLSRPGNQDCNWYNRCPRECISGVYTDAYPLSPDAVNVATTTLYANTSRVNPTIMYSNTSEIINMLRLKNVQLEAAYTTTSCITHFGKGYCFHIVEINQTSLNTLQPMLFKTSIPKICKITS	Literature-reported	Expression and characterization of soluble human parainfluenza virus type 1 hemagglutinin-neuraminidase glycoprotein. J Virol Methods. 2001 Oct;98(1):53-61.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT25MVL	Serine protease hepsin (HPN)	P05981	HEPS_HUMAN	Peptidase	"Transmembrane protease, serine 1; HPN; HEPSIN"	HPN	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.	EC 3.4.21.106	5CE1; 3T2N; 1Z8G; 1P57; 1O5F	MAQKEGGRTVPCCSRPKVAALTAGTLLLLTAIGAASWAIVAVLLRSDQEPLYPVQVSSADARLMVFDKTEGTWRLLCSSRSNARVAGLSCEEMGFLRALTHSELDVRTAGANGTSGFFCVDEGRLPHTQRLLEVISVCDCPRGRFLAAICQDCGRRKLPVDRIVGGRDTSLGRWPWQVSLRYDGAHLCGGSLLSGDWVLTAAHCFPERNRVLSRWRVFAGAVAQASPHGLQLGVQAVVYHGGYLPFRDPNSEENSNDIALVHLSSPLPLTEYIQPVCLPAAGQALVDGKICTVTGWGNTQYYGQQAGVLQEARVPIISNDVCNGADFYGNQIKPKMFCAGYPEGGIDACQGDSGGPFVCEDSISRTPRWRLCGIVSWGTGCALAQKPGVYTKVSDFREWIFQAIKTHSEASGMVTQL	Patented-recorded	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	0	.	.	.	.	.	.	.	.	.	.	hsa05203:Viral carcinogenesis	R-HSA-6806942: MET Receptor Activation; R-HSA-8852405: Signaling by MST1	.	P05981
TTR7GJO	Heparanase (HPSE)	Q9Y251	HPSE_HUMAN	Glycosylase	Hpa1; Heparanase-1; Heparanase 8 kDa subunit; Heparanase 50 kDa subunit; HSE1; HPSE1; HPR1; HPA; HEP protein; Endo-glucoronidase	HPSE	"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."	EC 3.2.1.166	5LA7; 5LA4; 5L9Z; 5L9Y; 5E9C	MLLRSKPALPPPLMLLLLGPLGPLSPGALPRPAQAQDVVDLDFFTQEPLHLVSPSFLSVTIDANLATDPRFLILLGSPKLRTLARGLSPAYLRFGGTKTDFLIFDPKKESTFEERSYWQSQVNQDICKYGSIPPDVEEKLRLEWPYQEQLLLREHYQKKFKNSTYSRSSVDVLYTFANCSGLDLIFGLNALLRTADLQWNSSNAQLLLDYCSSKGYNISWELGNEPNSFLKKADIFINGSQLGEDFIQLHKLLRKSTFKNAKLYGPDVGQPRRKTAKMLKSFLKAGGEVIDSVTWHHYYLNGRTATKEDFLNPDVLDIFISSVQKVFQVVESTRPGKKVWLGETSSAYGGGAPLLSDTFAAGFMWLDKLGLSARMGIEVVMRQVFFGAGNYHLVDENFDPLPDYWLSLLFKKLVGTKVLMASVQGSKRRKLRVYLHCTNTDNPRYKEGDLTLYAINLHNVTKYLRLPYPFSNKQVDKYLLRPLGPHGLLSKSVQLNGLTLKMVDDQTLPPLMEKPLRPGSSLGLPAFSYSFFVIRNAKVAACI	Successful	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Ligand id: 1728).	34	EC:3.2	Glycosylase	glycosyl hydrolase 79 family.	3.2.1.166	Glycosylases	"Glycosyl hydrolase family 79, N-terminal domain "	PF03662	PF03662; Glyco_hydro_79n	.	.	hsa00531:Glycosaminoglycan degradation; hsa01100:Metabolic pathways; hsa05205:Proteoglycans in cancer	R-HSA-2024096:HS-GAG degradation	MetaCyc:ENSG00000173083-MON	Q9Y251
TTK025N	Human papillomavirus E1 region messenger RNA (HPV E1 mRNA)	P04014	VE1_HPV11	mRNA target	Replication protein E1 (mRNA); E1 (mRNA); ATP-dependent helicase E1 (mRNA)	HPV E1 mRNA	"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."	EC 3.6.4.12	.	MADDSGTENEGSGCTGWFMVEAIVEHTTGTQISEDEEEEVEDSGYDMVDFIDDRHITQNSVEAQALFNRQEADAHYATVQDLKRKYLGSPYVSPISNVANAVESEISPRLDAIKLTTQPKKVKRRLFETRELTDSGYGYSEVEAATQVEKHGDPENGGDGQERDTGRDIEGEGVEHREAEAVDDSTREHADTSGILELLKCKDIRSTLHGKFKDCFGLSFVDLIRPFKSDRTTCADWVVAGFGIHHSIADAFQKLIEPLSLYAHIQWLTNAWGMVLLVLIRFKVNKSRCTVARTLGTLLNIPENHMLIEPPKIQSGVRALYWFRTGISNASTVIGEAPEWITRQTVIEHSLADSQFKLTEMVQWAYDNDICEESEIAFEYAQRGDFDSNARAFLNSNMQAKYVKDCAIMCRHYKHAEMKKMSIKQWIKYRGTKVDSVGNWKPIVQFLRHQNIEFIPFLSKLKLWLHGTPKKNCIAIVGPPDTGKSCFCMSLIKFLGGTVISYVNSCSHFWLQPLTDAKVALLDDATQPCWTYMDTYMRNLLDGNPMSIDRKHRALTLIKCPPLLVTSNIDISKEEKYKYLHSRVTTFTFPNPFPFDRNGNAVYELSDANWKCFFERLSSSLDIEDSEDEEDGSNSQAFRCVPGSVVRTL	Discontinued	Design and development of antisense drugs. Expert Opin. Drug Discov. 2008 3(10):1189-1207.	3	mRNA	mRNA target	.	.	.	"Papillomavirus helicase; E1 Protein, N terminal domain"	PF00519; PF00524	PF00519; PPV_E1_C; PF00524; PPV_E1_N	.	.	.	.	.	.
TTXQPKC	Human papillomavirus E2 transactivator messenger RNA (HPV E2 mRNA)	P06790	VE2_HPV18	mRNA target	Regulatory protein E2 (mRNA)	HPV E2 mRNA	"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."	.	1TUE; 1QQH; 1JJ4; 1F9F	MQTPKETLSERLSCVQDKIIDHYENDSKDIDSQIQYWQLIRWENAIFFAAREHGIQTLNHQVVPAYNISKSKAHKAIELQMALQGLAQSAYKTEDWTLQDTCEELWNTEPTHCFKKGGQTVQVYFDGNKDNCMTYVAWDSVYYMTDAGTWDKTATCVSHRGLYYVKEGYNTFYIEFKSECEKYGNTGTWEVHFGNNVIDCNDSMCSTSDDTVSATQLVKQLQHTPSPYSSTVSVGTAKTYGQTSAATRPGHCGLAEKQHCGPVNPLLGAATPTGNNKRRKLCSGNTTPIIHLKGDRNSLKCLRYRLRKHSDHYRDISSTWHWTGAGNEKTGILTVTYHSETQRTKFLNTVAIPDSVQILVGYMTM	Discontinued	"US patent application no. 5,665,580, Antisense oligonucleotide inhibition of papillomavirus transformed cells."	5	mRNA	mRNA target	.	.	.	"E2 (early) protein, C terminal; E2 (early) protein, N terminal"	PF00511; PF00508	PF00511; PPV_E2_C; PF00508; PPV_E2_N	.	.	.	.	.	.
TTF3I4E	Human papillomavirus E2 region messenger RNA (HPV E2 mRNA)	P03122	VE2_BPV1	mRNA target	BPV regulatory protein E2 (mRNA)	HPV E2 mRNA	"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."	.	6BUS; 2JEX; 2JEU; 2BOP; 1JJH	METACERLHVAQETQMQLIEKSSDKLQDHILYWTAVRTENTLLYAARKKGVTVLGHCRVPHSVVCQERAKQAIEMQLSLQELSKTEFGDEPWSLLDTSWDRYMSEPKRCFKKGARVVEVEFDGNASNTNWYTVYSNLYMRTEDGWQLAKAGADGTGLYYCTMAGAGRIYYSRFGDEAARFSTTGHYSVRDQDRVYAGVSSTSSDFRDRPDGVWVASEGPEGDPAGKEAEPAQPVSSLLGSPACGPIRAGLGWVRDGPRSHPYNFPAGSGGSILRSSSTPVQGTVPVDLASRQEEEEQSPDSTEEEPVTLPRRTTNDGFHLLKAGGSCFALISGTANQVKCYRFRVKKNHRHRYENCTTTWFTVADNGAERQGQAQILITFGSPSQRQDFLKHVPLPPGMNISGFTASLDF	Literature-reported	"US patent application no. 5,457,189, Antisense oligonucleotide inhibition of papillomavirus."	0	mRNA	mRNA target	.	.	.	"E2 (early) protein, C terminal; E2 (early) protein, N terminal"	PF00511; PF00508	PF00511; PPV_E2_C; PF00508; PPV_E2_N	.	.	.	.	.	.
TTE2N95	Human papillomavirus protein E6 (HPV E6)	P03126	VE6_HPV16	Papillomaviridae E protein	Protein E6; E6	HPV E6	"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."	.	6HKS; 4XR8; 4JOP; 4GIZ; 2LJZ	MHQKRTAMFQDPQERPRKLPQLCTELQTTIHDIILECVYCKQQLLRREVYDFAFRDLCIVYRDGNPYAVCDKCLKFYSKISEYRHYCYSLYGTTLEQQYNKPLCDLLIRCINCQKPLCPEEKQRHLDKKQRFHNIRGRWTGRCMSCCRSSRTRRETQL	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3CPZW	Human papillomavirus protein E7 (HPV E7)	P03129	VE7_HPV16	Papillomaviridae E protein	Protein E7; E7	HPV E7	"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."	.	6APN; 4YOZ	MHGDTPTLHEYMLDLQPETTDLYCYEQLNDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPICSQKP	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT7OU0X	Human papillomavirus-18 E6 region messenger RNA (HPV-18 E6 mRNA)	P06463	VE6_HPV18	mRNA target	HPV-18 protein E6 (mRNA); HPV-18 E6 (mRNA)	HPV-18 E6 mRNA	"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."	.	5K4F; 5IC3; 4JOR; 2I0L; 2I0I	MARFEDPTRRPYKLPDLCTELNTSLQDIEITCVYCKTVLELTEVFEFAFKDLFVVYRDSIPHAACHKCIDFYSRIRELRHYSDSVYGDTLEKLTNTGLYNLLIRCLRCQKPLNPAEKLRHLNEKRRFHNIAGHYRGQCHSCCNRARQERLQRRRETQV	Literature-reported	"US patent application no. 5,457,189, Antisense oligonucleotide inhibition of papillomavirus."	0	mRNA	mRNA target	.	.	.	Early Protein (E6)	PF00518	PF00518; E6	.	.	.	.	.	.
TTWMK2G	Human papillomavirus-18 E7 region messenger RNA (HPV-18 E7 mRNA)	P06788	VE7_HPV18	mRNA target	HPV-18 protein E7 (mRNA); HPV-18 E7 (mRNA)	HPV-18 E7 mRNA	"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."	.	.	MHGPKATLQDIVLHLEPQNEIPVDLLCHEQLSDSEEENDEIDGVNHQHLPARRAEPQRHTMLCMCCKCEARIKLVVESSADDLRAFQQLFLNTLSFVCPWCASQQ	Literature-reported	"US patent application no. 5,457,189, Antisense oligonucleotide inhibition of papillomavirus."	0	mRNA	mRNA target	.	.	.	"E7 protein, Early protein"	PF00527	PF00527; E7	.	.	.	.	.	.
TT28ZON	H-ras messenger RNA (HRAS mRNA)	P01112	RASH_HUMAN	mRNA target	"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)"	HRAS	Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Involved in the activation of Ras protein signal transduction.	.	821P; 721P; 6Q21; 6D5W; 6D5V	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS	Discontinued	"A phase I trial of ISIS 2503, an antisense inhibitor of H-ras, in combination with gemcitabine in patients with advanced cancer. Clin Cancer Res. 2003 Jan;9(1):115-23."	5	mRNA	mRNA target	.	.	.	Ras family	PF00071	PF00071; Ras	.	.	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	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	.	P01112
TTHO7TF	GTPase HRas (HRAS)	P01112	RASH_HUMAN	Small GTPase	"p21ras; cHras; c-H-ras; Transforming protein p21; HaRas; Ha-Ras; H-Ras-1; GTPase HRas, Nterminally processed"	HRAS	Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Involved in the activation of Ras protein signal transduction.	.	821P; 721P; 6Q21; 6D5W; 6D5V	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS	Literature-reported	HRAS as a potential therapeutic target of salirasib RAS inhibitor in bladder cancer. Int J Oncol. 2018 Aug;53(2):725-736.	.	Small GTPase	Ras family	small GTPase superfamily. Ras family.	.	.	Ras family	PF00071	PF00071; Ras	.	.	"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; hsa04144: Endocytosis; 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; hsa04510: Focal adhesion; hsa04540: Gap junction; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04625: C-type lectin 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; 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; hsa04915: Estrogen signaling pathway; hsa04916: Melanogenesis; hsa04917: Prolactin signaling pathway; hsa04919: Thyroid hormone signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04926: Relaxin signaling pathway; hsa04929: GnRH secretion; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04935: Growth hormone synthesis, secretion and action; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05034: Alcoholism; hsa05132: Salmonella infection; 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; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05210: Colorectal 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; 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; hsa05417: Lipid and atherosclerosis"	"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-1433557: Signaling by SCF-KIT; R-HSA-167044: Signalling to RAS; R-HSA-171007: p38MAPK events; R-HSA-179812: GRB2 events in EGFR signaling; R-HSA-180336: SHC1 events in EGFR signaling; R-HSA-186763: Downstream signal transduction; 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 upon Ca2+ influx 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-5655253: Signaling by FGFR2 in disease; R-HSA-5655291: Signaling by FGFR4 in disease; R-HSA-5655302: Signaling by FGFR1 in disease; R-HSA-5655332: Signaling by FGFR3 in disease; 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-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802953: RAS signaling downstream of NF1 loss-of-function variants; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-74751: Insulin receptor signalling cascade; R-HSA-8849471: PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases; R-HSA-8851805: MET activates RAS signaling; R-HSA-9026519: Activated NTRK2 signals through RAS; R-HSA-9027284: Erythropoietin activates RAS; R-HSA-9028731: Activated NTRK2 signals through FRS2 and FRS3; R-HSA-9034864: Activated NTRK3 signals through RAS; R-HSA-9607240: FLT3 Signaling; R-HSA-9634285: Constitutive Signaling by Overexpressed ERBB2; R-HSA-9634635: Estrogen-stimulated signaling through PRKCZ; R-HSA-9648002: RAS processing; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665348: Signaling by ERBB2 ECD mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants; R-HSA-9670439: Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants; R-HSA-9673767: Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants; R-HSA-9673770: Signaling by PDGFRA extracellular domain mutants; R-HSA-9703465: Signaling by FLT3 fusion proteins; R-HSA-9703648: Signaling by FLT3 ITD and TKD mutants; R-HSA-9753510: Signaling by RAS GAP mutants; R-HSA-9753512: Signaling by RAS GTPase mutants"	.	P01112
TTR4FKD	Histidine-rich calcium binding protein (HRC)	P23327	SRCH_HUMAN	.	Sarcoplasmic reticulum histidine-rich calcium-binding protein; HRC	HRC	May play a role in the regulation of calcium sequestration or release in the SR of skeletal and cardiac muscle.	.	.	MGHHRPWLHASVLWAGVASLLLPPAMTQQLRGDGLGFRNRNNSTGVAGLSEEASAELRHHLHSPRDHPDENKDVSTENGHHFWSHPDREKEDEDVSKEYGHLLPGHRSQDHKVGDEGVSGEEVFAEHGGQARGHRGHGSEDTEDSAEHRHHLPSHRSHSHQDEDEDEVVSSEHHHHILRHGHRGHDGEDDEGEEEEEEEEEEEEASTEYGHQAHRHRGHGSEEDEDVSDGHHHHGPSHRHQGHEEDDDDDDDDDDDDDDDDVSIEYRHQAHRHQGHGIEEDEDVSDGHHHRDPSHRHRSHEEDDNDDDDVSTEYGHQAHRHQDHRKEEVEAVSGEHHHHVPDHRHQGHRDEEEDEDVSTERWHQGPQHVHHGLVDEEEEEEEITVQFGHYVASHQPRGHKSDEEDFQDEYKTEVPHHHHHRVPREEDEEVSAELGHQAPSHRQSHQDEETGHGQRGSIKEMSHHPPGHTVVKDRSHLRKDDSEEEKEKEEDPGSHEEDDESSEQGEKGTHHGSRDQEDEEDEEEGHGLSLNQEEEEEEDKEEEEEEEDEERREERAEVGAPLSPDHSEEEEEEEEGLEEDEPRFTIIPNPLDRREEAGGASSEEESGEDTGPQDAQEYGNYQPGSLCGYCSFCNRCTECESCHCDEENMGEHCDQCQHCQFCYLCPLVCETVCAPGSYVDYFSSSLYQALADMLETPEP	Literature-reported	The histidine-rich calcium binding protein (HRC) promotes tumor metastasis in hepatocellular carcinoma and is upregulated by SATB1. Oncotarget. 2015 Mar 30;6(9):6811-24.	.	.	.	.	.	.	.	.	.	.	.	hsa04020: Calcium signaling pathway; hsa04260: Cardiac muscle contraction	R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation	.	P23327
TTTIBOJ	Histamine H1 receptor (H1R)	P35367	HRH1_HUMAN	GPCR rhodopsin	HH1R; H1R	HRH1	"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."	.	3RZE	MSLPNSSCLLEDKMCEGNKTTMASPQLMPLVVVLSTICLVTVGLNLLVLYAVRSERKLHTVGNLYIVSLSVADLIVGAVVMPMNILYLLMSKWSLGRPLCLFWLSMDYVASTASIFSVFILCIDRYRSVQQPLRYLKYRTKTRASATILGAWFLSFLWVIPILGWNHFMQQTSVRREDKCETDFYDVTWFKVMTAIINFYLPTLLMLWFYAKIYKAVRQHCQHRELINRSLPSFSEIKLRPENPKGDAKKPGKESPWEVLKRKPKDAGGGSVLKSPSQTPKEMKSPVVFSQEDDREVDKLYCFPLDIVHMQAAAEGSSRDYVAVNRSHGQLKTDEQGLNTHGASEISEDQMLGDSQSFSRTDSDTTTETAPGKGKLRSGSNTGLDYIKFTWKRLRSHSRQYVSGLHMNRERKAAKQLGFIMAAFILCWIPYFIFFMVIAFCKNCCNEHLHMFTIWLGYINSTLNPLIYPLCNENFKKTFKRILHIRS	Successful	Histamine upregulates keratinocyte MMP-9 production via the histamine H1 receptor. J Invest Dermatol. 2008 Dec;128(12):2783-91.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04750:Inflammatory mediator regulation of TRP channels	R-HSA-390650:Histamine receptors; R-HSA-416476:G alpha (q) signalling events	.	P35367
TTQHJ1K	Histamine H2 receptor (H2R)	P25021	HRH2_HUMAN	GPCR rhodopsin	Histamine receptor 2; HH2R; Gastric receptor I	HRH2	"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."	.	.	MAPNGTASSFCLDSTACKITITVVLAVLILITVAGNVVVCLAVGLNRRLRNLTNCFIVSLAITDLLLGLLVLPFSAIYQLSCKWSFGKVFCNIYTSLDVMLCTASILNLFMISLDRYCAVMDPLRYPVLVTPVRVAISLVLIWVISITLSFLSIHLGWNSRNETSKGNHTTSKCKVQVNEVYGLVDGLVTFYLPLLIMCITYYRIFKVARDQAKRINHISSWKAATIREHKATVTLAAVMGAFIICWFPYFTAFVYRGLRGDDAINEVLEAIVLWLGYANSALNPILYAALNRDFRTGYQQLFCCRLANRNSHKTSLRSNASQLSRTQSREPRQQEEKPLKLQVWSGTEVTAPQGATDR	Successful	Histamine H1 and H2 receptor antagonists accelerate skin barrier repair and prevent epidermal hyperplasia induced by barrier disruption in a dry environment. J Invest Dermatol. 2001 Feb;116(2):261-5.	34	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04971:Gastric acid secretion	R-HSA-390650:Histamine receptors; R-HSA-418555:G alpha (s) signalling events	.	P25021
TT9JNIC	Histamine H3 receptor (H3R)	Q9Y5N1	HRH3_HUMAN	GPCR rhodopsin	Histamine receptor 3; HH3R; GPCR97; G-protein coupled receptor 97; G protein-coupled receptor 97	HRH3	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.	.	.	MERAPPDGPLNASGALAGEAAAAGGARGFSAAWTAVLAALMALLIVATVLGNALVMLAFVADSSLRTQNNFFLLNLAISDFLVGAFCIPLYVPYVLTGRWTFGRGLCKLWLVVDYLLCTSSAFNIVLISYDRFLSVTRAVSYRAQQGDTRRAVRKMLLVWVLAFLLYGPAILSWEYLSGGSSIPEGHCYAEFFYNWYFLITASTLEFFTPFLSVTFFNLSIYLNIQRRTRLRLDGAREAAGPEPPPEAQPSPPPPPGCWGCWQKGHGEAMPLHRYGVGEAAVGAEAGEATLGGGGGGGSVASPTSSSGSSSRGTERPRSLKRGSKPSASSASLEKRMKMVSQSFTQRFRLSRDRKVAKSLAVIVSIFGLCWAPYTLLMIIRAACHGHCVPDYWYETSFWLLWANSAVNPVLYPLCHHSFRRAFTKLLCPQKLKIQPHSSLEHCWK	Successful	"Effects of pitolisant, a histamine H3 inverse agonist, in drug-resistant idiopathic and symptomatic hypersomnia: a chart review. Sleep Med. 2014 Jun;15(6):681-7."	25	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-390650:Histamine receptors; R-HSA-418594:G alpha (i) signalling events	.	Q9Y5N1
TTXJ178	Histamine H4 receptor (H4R)	Q9H3N8	HRH4_HUMAN	GPCR rhodopsin	SP9144; Pfi-013; HH4R; H4 receptor; GPRv53; GPCR105; G protein-coupled receptor 105; AXOR35	HRH4	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.	.	.	MPDTNSTINLSLSTRVTLAFFMSLVAFAIMLGNALVILAFVVDKNLRHRSSYFFLNLAISDFFVGVISIPLYIPHTLFEWDFGKEICVFWLTTDYLLCTASVYNIVLISYDRYLSVSNAVSYRTQHTGVLKIVTLMVAVWVLAFLVNGPMILVSESWKDEGSECEPGFFSEWYILAITSFLEFVIPVILVAYFNMNIYWSLWKRDHLSRCQSHPGLTAVSSNICGHSFRGRLSSRRSLSASTEVPASFHSERQRRKSSLMFSSRTKMNSNTIASKMGSFSQSDSVALHQREHVELLRARRLAKSLAILLGVFAVCWAPYSLFTIVLSFYSSATGPKSVWYRIAFWLQWFNSFVNPLLYPLCHKRFQKAFLKIFCIKKQPLPSQHSRSVSS	Clinical trial	Challenges of drug discovery in novel target space. The discovery and evaluation of PF-3893787: a novel histamine H4 receptor antagonist. Bioorg Med Chem Lett. 2011 Nov 1;21(21):6596-602.	21	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-390650:Histamine receptors; R-HSA-418594:G alpha (i) signalling events	.	Q9H3N8
TT6275O	HRSV RNA-directed RNA polymerase L (HRSV L)	P28887	L_HRSVA	.	Protein L; Large structural protein; Replicase; Transcriptase	HRSV L	"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."	.	.	MDPIINGNSANVYLTDSYLKGVISFSECNALGSYIFNGPYLKNDYTNLISRQNPLIEHMNLKKLNITQSLISKYHKGEIKLEEPTYFQSLLMTYKSMTSSEQIATTNLLKKIIRRAIEISDVKVYAILNKLGLKEKDKIKSNNGQDEDNSVITTIIKDDILSAVKDNQSHLKADKNHSTKQKDTIKTTLLKKLMCSMQHPPSWLIHWFNLYTKLNNILTQYRSNEVKNHGFTLIDNQTLSGFQFILNQYGCIVYHKELKRITVTTYNQFLTWKDISLSRLNVCLITWISNCLNTLNKSLGLRCGFNNVILTQLFLYGDCILKLFHNEGFYIIKEVEGFIMSLILNITEEDQFRKRFYNSMLNNITDAANKAQKNLLSRVCHTLLDKTVSDNIINGRWIILLSKFLKLIKLAGDNNLNNLSELYFLFRIFGHPMVDERQAMDAVKINCNETKFYLLSSLSMLRGAFIYRIIKGFVNNYNRWPTLRNAIVLPLRWLTYYKLNTYPSLLELTERDLIVLSGLRFYREFRLPKKVDLEMIINDKAISPPKNLIWTSFPRNYMPSHIQNYIEHEKLKFSESDKSRRVLEYYLRDNKFNECDLYNCVVNQSYLNNPNHVVSLTGKERELSVGRMFAMQPGMFRQVQILAEKMIAENILQFFPESLTRYGDLELQKILELKAGISNKSNRYNDNYNNYISKCSIITDLSKFNQAFRYETSCICSDVLDELHGVQSLFSWLHLTIPHVTIICTYRHAPPYIGDHIVDLNNVDEQSGLYRYHMGGIEGWCQKLWTIEAISLLDLISLKGKFSITALINGDNQSIDISKPIRLMEGQTHAQADYLLALNSLKLLYKEYAGIGHKLKGTETYISRDMQFMSKTIQHNGVYYPASIKKVLRVGPWINTILDDFKVSLESIGSLTQELEYRGESLLCSLIFRNVWLYNQIALQLKNHALCNNKLYLDILKVLKHLKTFFNLDNIDTALTLYMNLPMLFGGGDPNLLYRSFYRRTPDFLTEAIVHSVFILSYYTNHDLKDKLQDLSDDRLNKFLTCIITFDKNPNAEFVTLMRDPQALGSERQAKITSEINRLAVTEVLSTAPNKIFSKSAQHYTTTEIDLNDIMQNIEPTYPHGLRVVYESLPFYKAEKIVNLISGTKSITNILEKTSAIDLTDIDRATEMMRKNITLLIRILPLDCNRDKREILSMENLSITELSKYVRERSWSLSNIVGVTSPSIMYTMDIKYTTSTISSGIIIEKYNVNSLTRGERGPTKPWVGSSTQEKKTMPVYNRQVLTKKQRDQIDLLAKLDWVYASIDNKDEFMEELSIGTLGLTYEKAKKLFPQYLSVNYLHRLTVSSRPCEFPASIPAYRTTNYHFDTSPINRILTEKYGDEDIDIVFQNCISFGLSLMSVVEQFTNVCPNRIILIPKLNEIHLMKPPIFTGDVDIHKLKQVIQKQHMFLPDKISLTQYVELFLSNKTLKSGSHVNSNLILAHKISDYFHNTYILSTNLAGHWILIIQLMKDSKGIFEKDWGEGYITDHMFINLKVFFNAYKTYLLCFHKGYGKAKLECDMNTSDLLCVLELIDSSYWKSMSKVFLEQKVIKYILSQDASLHRVKGCHSFKLWFLKRLNVAEFTVCPWVVNIDYHPTHMKAILTYIDLVRMGLINIDRIHIKNKHKFNDEFYTSNLFYINYNFSDNTHLLTKHIRIANSELENNYNKLYHPTPETLENILANPIKSNDKKTLNDYCIGKNVDSIMLPLLSNKKLIKSSAMIRTNYSKQDLYNLFPMVVIDRIIDHSGNTAKSNQLYTTTSHQISLVHNSTSLYCMLPWHHINRFNFVFSSTGCKISIEYILKDLKIKDPNCIAFIGEGAGNLLLRTVVELHPDIRYIYRSLKDCNDHSLPIEFLRLYNGHINIDYGENLTIPATDATNNIHWSYLHIKFAEPISLFVCDAELSVTVNWSKIIIEWSKHVRKCKYCSSVNKCMLIVKYHAQDDIDFKLDNITILKTYVCLGSKLKGSEVYLVLTIGPANIFPVFNVVQNAKLILSRTKNFIMPKKADKESIDANIKSLIPFLCYPITKKGINTALSKLKSVVSGDILSYSIAGRNEVFSNKLINHKHMNILKWFNHVLNFRSTELNYNHLYMVESTYPYLSELLNSLTTNELKKLIKITGSLLYNFHNE	Clinical trial	Advances in respiratory virus therapeutics - A meeting report from the 6th isirv Antiviral Group conference. Antiviral Res. 2019 Jul;167:45-67.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTWSF5D	HRSV Nucleoprotein messenger RNA (HRSV N mRNA)	P03418	NCAP_HRSVA	.	Protein N; Nucleocapsid protein	HRSV N mRNA	"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."	.	.	MALSKVKLNDTLNKDQLLSSSKYTIQRSTGDSIDTPNYDVQKHINKLCGMLLITEDANHKFTGLIGMLYAMSRLGREDTIKILRDAGYHVKANGVDVTTHRQDINGKEMKFEVLTLASLTTEIQINIEIESRKSYKKMLKEMGEVAPEYRHDSPDCGMIILCIAALVITKLAAGDRSGLTAVIRRANNVLKNEMKRYKGLLPKDIANSFYEVFEKHPHFIDVFVHFGIAQSSTRGGSRVEGIFAGLFMNAYGAGQVMLRWGVLAKSVKNIMLGHASVQAEMEQVVEVYEYAQKLGGEAGFYHILNNPKASLLSLTQFPHFSSVVLGNAAGLGIMGEYRGTPRNQDLYDAAKAYAEQLKENGVINYSVLDLTAEELEAIKHQLNPKDNDVEL	Clinical trial	"Evaluation of the safety, tolerability and pharmacokinetics of ALN-RSV01, a novel RNAi antiviral therapeutic directed against respiratory syncytial virus (RSV). Antiviral Res. 2008 Mar;77(3):225-31."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2Y1AN	Rhinovirus Protein 1 (HRV P1D)	P12916 (567-857)	POLG_HRV1B	.	Rhinovirus Capsid protein VP1; Rhinovirus P1D; Rhinovirus Virion protein 1	HRV P1D	"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)."	.	1XR6	PIEQNPVENYIDEVLNEVLVVPNIKESHHTTSNSAPLLDAAETGHTSNVQPEDAIETRYVMTSQTRDEMSIESFLGRSGCVHISRIKVDYNDYNGVNKNFTTWKITLQEMAQIRRKFELFTYVRFDSEVTLVPCIAGRGDDIGHVVMQYMYVPPGAPIPKTRNDFSWQSGTNMSIFWQHGQPFPRFSLPFLSIASAYYMFYDGYDGDNSSSKYGSIVTNDMGTICSRIVTEKQEHPVVITTHIYHKAKHTKAWCPRPPRAVPYTHSRVTNYVPKTGDVTTAIVPRASMKTV	Discontinued	"In vitro activity of R 61837, a new antirhinovirus compound. Arch Virol. 1988;101(3-4):155-67."	5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTGW0DV	Rhinovirus Protease 3C (HRV P3C)	P04936 (1515-1696)	POLG_HRV2	.	Rhinovirus P3C	HRV P3C	"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)."	EC 3.4.22.28	6FFS; 6FFN; 5FX6; 5FX5; 4L3B	MSLIKHNSCVITTENGKFTGLGVYDRFVVVPTHADPGKEIQVDGITTKVIDSYDLYNKNGIKLEITVLKLDRNEKFRDIRRYIPNNEDDYPNCNLALLANQPEPTIINVGDVVSYGNILLSGNQTARMLKYSYPTKSGYCGGVLYKIGQVLGIHVGGNGRDGFSAMLLRSYFTDVQGQITLS	Clinical trial	"Enterovirus 71 and coxsackievirus A16 3C proteases: binding to rupintrivir and their substrates and anti-hand, foot, and mouth disease virus drug design. J Virol. 2011 Oct;85(19):10319-31."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8R3VP	Rhinovirus Capsid protein (HRV VP)	P23008 (2-857)	POLG_HRV1A	.	Rhinovirus Virion protein	HRV VP	"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)."	.	2HWF; 2HWE; 2HWD; 1R1A; 1AYN	GAQVSRQNVGTHSTQNSVSNGSSLNYFNINYFKDAASSGASRLDFSQDPSKFTDPVKDVLEKGIPTLQSPSVEACGYSDRIMQITRGDSTITSQDVANAVVGYGVWPHYLTPQDATAIDKPTQPDTSSNRFYTLESKHWNGSSKGWWWKLPDALKDMGIFGENMYYHFLGRSGYTVHVQCNASKFHQGTLLVAMIPEHQLASAKHGSVTAGYKLTHPGEAGRDVSQERDASLRQPSDDSWLNFDGTLLGNLLIFPHQFINLRSNNSATLIVPYVNAVPMDSMLRHNNWSLVIIPISPLRSETTSSNIVPITVSISPMCAEFSGARAKNIKQGLPVYITPGSGQFMTTDDMQSPCALPWYHPTKEISIPGEVKNLIEMCQVDTLIPVNNVGNNVGNVSMYTVQLGNQTGMAQKVFSIKVDITSQPLATTLIGEIASYYTHWTGSLRFSFMFCGTANTTLKLLLAYTPPGIDEPTTRKDAMLGTHVVWDVGLQSTISLVVPWVSASHFRLTADNKYSMAGYITCWYQTNLVVPPSTPQTADMLCFVSACKDFCLRMARDTDLHIQSGPIEQNPVENYIDEVLNEVLVVPNIKESHHTTSNSAPLLDAAETGHTSNVQPEDAIETRYVITSQTRDEMSIESFLGRSGCVHISRIKVDYTDYNGQDINFTKWKITLQEMAQIRRKFELFTYVRFDSEITLVPCIAGRGDDIGHIVMQYMYVPPGAPIPSKRNDFSWQSGTNMSIFWQHGQPFPRFSLPFLSIASAYYMFYDGYDGDNTSSKYGSVVTNDMGTICSRIVTEKQKHSVVITTHIYHKAKHTKAWCPRPPRAVPYTHSHVTNYMPETGDVTTAIVRRNTITTA	Clinical trial	Combating enterovirus replication: state-of-the-art on antiviral research. Biochem Pharmacol. 2012 Jan 15;83(2):185-92.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTS6LBM	Heparan sulfate 6-O-sulfotransferase-2 (HS6ST2)	Q96MM7	H6ST2_HUMAN	.	Heparan-sulfate 6-O-sulfotransferase 2; HS6ST-2	HS6ST2	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.	EC 2.8.2.-	.	MALPACAVREFEPPRQPERGAPVRTTCPRRHSRVEAELAASRPGSVAASVRAGPPRGVSHGFHTRPLLDKPRKASSSLAGAACAPLFALLSRGRRRRMHVLRRRWDLGSLCRALLTRGLAALGHSLKHVLGAIFSKIFGPMASVGNMDEKSNKLLLALVMLFLFAVIVLQYVCPGTECQLLRLQAFSSPVPDPYRSEDESSARFVPRYNFTRGDLLRKVDFDIKGDDLIVFLHIQKTGGTTFGRHLVRNIQLEQPCECRVGQKKCTCHRPGKRETWLFSRFSTGWSCGLHADWTELTSCVPSVVDGKRDARLRPSRNFHYITILRDPVSRYLSEWRHVQRGATWKASLHVCDGRPPTSEELPSCYTGDDWSGCPLKEFMDCPYNLANNRQVRMLSDLTLVGCYNLSVMPEKQRNKVLLESAKSNLKHMAFFGLTEFQRKTQYLFEKTFNMNFISPFTQYNTTRASSVEINEEIQKRIEGLNFLDMELYSYAKDLFLQRYQFMRQKEHQEARRKRQEQRKFLKGRLLQTHFQSQGQGQSQNPNQNQSQNPNPNANQNLTQNLMQNLTQSLSQKENRESPKQNSGKEQNDNTSNGTNDYIGSVEKWR	Literature-reported	Overexpression of heparan sulfate 6-O-sulfotransferase-2 in colorectal cancer. Mol Clin Oncol. 2013 Sep;1(5):845-850.	.	.	.	.	.	.	.	.	.	.	.	hsa00534: Glycosaminoglycan biosynthesis - heparan sulfate / heparin	R-HSA-2022928: HS-GAG biosynthesis	.	Q96MM7
TTN7BL9	Corticosteroid 11-beta-dehydrogenase 1 (HSD11B1)	P28845	DHI1_HUMAN	Short-chain dehydrogenases reductase	HSD11B1; 11beta-HSD1A; 11HSD1; 11-beta-hydroxysteroid dehydrogenase 1; 11-beta-HSD1; 11-DH; 11 beta-hydroxysteroid dehydrogenase type 1	HSD11B1	"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."	EC 1.1.1.146	5QII; 5PGY; 5PGX; 5PGW; 5PGV	MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEECALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK	Clinical trial	Selective inhibition of 11 beta-hydroxysteroid dehydrogenase type 1 improves hepatic insulin sensitivity in hyperglycemic mice strains. Endocrinology. 2003 Nov;144(11):4755-62.	25	.	.	.	.	.	.	.	.	.	.	hsa00140:Steroid hormone biosynthesis; hsa00980:Metabolism of xenobiotics by cytochrome P450; hsa01100:Metabolic pathways; hsa05204:Chemical carcinogenesis	R-HSA-194002:Glucocorticoid biosynthesis	MetaCyc:HS04154-MON	P28845
TT9H85R	Corticosteroid 11-beta-dehydrogenase 2 (HSD11B2)	P80365	DHI2_HUMAN	Short-chain dehydrogenases reductase	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	HSD11B2	"Catalyzes the conversion of cortisol to the inactive metabolite cortisone. modulates intracellular glucocorticoid levels, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids."	EC 1.1.1.-	.	MERWPWPSGGAWLLVAARALLQLLRSDLRLGRPLLAALALLAALDWLCQRLLPPPAALAVLAAAGWIALSRLARPQRLPVATRAVLITGCDSGFGKETAKKLDSMGFTVLATVLELNSPGAIELRTCCSPRLRLLQMDLTKPGDISRVLEFTKAHTTSTGLWGLVNNAGHNEVVADAELSPVATFRSCMEVNFFGALELTKGLLPLLRSSRGRIVTVGSPAGDMPYPCLGAYGTSKAAVALLMDTFSCELLPWGVKVSIIQPGCFKTESVRNVGQWEKRKQLLLANLPQELLQAYGKDYIEHLHGQFLHSLRLAMSDLTPVVDAITDALLAARPRRRYYPGQGLGLMYFIHYYLPEGLRRRFLQAFFISHCLPRALQPGQPGTTPPQDAAQDPNLSPGPSPAVAR	Clinical trial	New Therapeutic Strategies for Type 2 Diabetes: Small Molecule Approaches. 2012. Chapter 5. Page(131).	21	.	.	.	.	.	.	.	.	.	.	hsa00140:Steroid hormone biosynthesis; hsa04960:Aldosterone-regulated sodium reabsorption	R-HSA-194002:Glucocorticoid biosynthesis	MetaCyc:ENSG00000176387-MON	P80365
TTIWB6L	Estradiol 17 beta-dehydrogenase 1 (17-beta-HSD1)	P14061	DHB1_HUMAN	CH-OH donor oxidoreductase	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	HSD17B1	Has 20-alpha-HSD activity. Uses preferentially NADH. Favors the reduction of estrogens and androgens.	EC 1.1.1.62	6MNE; 6MNC; 6DTP; 6CGE; 6CGC	MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRGAVGDPELGDPPAAPQ	Clinical trial	Discovery of nonsteroidal 17beta-hydroxysteroid dehydrogenase 1 inhibitors by pharmacophore-based screening of virtual compound libraries. J Med Chem. 2008 Jul 24;51(14):4188-99.	17	EC:1.1	Short-chain dehydrogenases reductases	short-chain dehydrogenases/reductases (SDR) family.	1.1.1.62	Acting on the CH-OH group of donors	short chain dehydrogenase	PF00106	PF00106; adh_short	.	.	hsa00140:Steroid hormone biosynthesis; hsa01100:Metabolic pathways; hsa04913:Ovarian steroidogenesis	R-HSA-2453902:The canonical retinoid cycle in rods (twilight vision)	.	P14061
TTDJYZR	17-beta-hydroxysteroid dehydrogenase 13 (HSD17B13)	Q7Z5P4	DHB13_HUMAN	.	17-beta-HSD 13; Hepatic retinol/retinal dehydrogenase; Short chain dehydrogenase/reductase family 16C member 3; Short-chain dehydrogenase/reductase 9	HSD17B13	"Plays a pivotal role in hepatic lipid metabolism (PubMed:29562163). In vitro, it catalyzes the oxidation of a variety of lipid substrates, including 17beta-estradiol, retinol, retinal, and leukotriene B4 (PubMed:29562163, PubMed:30415504, PubMed:32973038). {ECO:0000269|PubMed:29562163, ECO:0000269|PubMed:30415504, ECO:0000269|PubMed:32973038}.; [Isoform 2]: Has retinol/retinal dehydrogenase activity in vitro. {ECO:0000269|PubMed:30415504, ECO:0000269|PubMed:32973038}.; [Isoform 1]: Does not have retinol/retinal dehydrogenase activity in vitro. {ECO:0000269|PubMed:30415504}."	EC 1.1.1.-; EC 1.1.1.105; EC 1.1.1.62	.	MNIILEILLLLITIIYSYLESLVKFFIPQRRKSVAGEIVLITGAGHGIGRQTTYEFAKRQSILVLWDINKRGVEETAAECRKLGVTAHAYVVDCSNREEIYRSLNQVKKEVGDVTIVVNNAGTVYPADLLSTKDEEITKTFEVNILGHFWITKALLPSMMERNHGHIVTVASVCGHEGIPYLIPYCSSKFAAVGFHRGLTSELQALGKTGIKTSCLCPVFVNTGFTKNPSTRLWPVLETDEVVRSLIDGILTNKKMIFVPSYINIFLRLQKFLPERASAILNRMQNIQFEAVVGHKIKMK	Clinical trial	"Clinical pipeline report, company report or official report of Arrowhead Pharmaceuticals"	.	.	.	.	.	.	.	.	.	.	.	hsa:345275	R-HSA-8964572;	.	Q7Z5P4;
TT0PT1R	Estradiol 17-beta-dehydrogenase 2	.	DHB2_HUMAN	Single Protein	Microsomal 17-beta-hydroxysteroid dehydrogenase; Short chain dehydrogenase/reductase family 9C member 2; 17-beta-hydroxysteroid dehydrogenase type 2; 17-beta-HSD 2; 20 alpha-hydroxysteroid dehydrogenase; 20-alpha-HSD; E2DH; Testosterone 17-beta-dehydrogenase	HSD17B2	"Capable of catalyzing the interconversion of testosterone and androstenedione, as well as estradiol and estrone. Also has 20-alpha-HSD activity. Uses NADH while EDH17B3 uses NADPH."	.	.	MSTFFSDTAWICLAVPTVLCGTVFCKYKKSSGQLWSWMVCLAGLCAVCLLILSPFWGLILFSVSCFLMYTYLSGQELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRGLWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPAEVQEDYGQDYILAQRNFLLLINSLASKDFSPVLRDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYDYFAKRHFGQDKPMPRALRMPNYKKKAT	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P37059
TTL1WGS	Estradiol 17 beta-dehydrogenase 4 (HSD17B4)	P51659	DHB4_HUMAN	Short-chain dehydrogenases reductase	MFE-2; HSD17B4; DBP; D-bifunctional protein; 17-beta-hydroxysteroid dehydrogenase 4; 17-beta-HSD 4; 17 beta-hydroxysteroid dehydrogenase type 4	HSD17B4	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.	.	1ZBQ; 1S9C; 1IKT	MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWIGKLRWERTLGAIVRQKNHPMTPEAVKANWKKICDFENASKPQSIQESTGSIIEVLSKIDSEGGVSANHTSRATSTATSGFAGAIGQKLPPFSYAYTELEAIMYALGVGASIKDPKDLKFIYEGSSDFSCLPTFGVIIGQKSMMGGGLAEIPGLSINFAKVLHGEQYLELYKPLPRAGKLKCEAVVADVLDKGSGVVIIMDVYSYSEKELICHNQFSLFLVGSGGFGGKRTSDKVKVAVAIPNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNDVSRFKAIKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISNAYVDLAPTSGTSAKTPSEGGKLQSTFVFEEIGRRLKDIGPEVVKKVNAVFEWHITKGGNIGAKWTIDLKSGSGKVYQGPAKGAADTTIILSDEDFMEVVLGKLDPQKAFFSGRLKARGNIMLSQKLQMILKDYAKL	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	hsa00120:Primary bile acid biosynthesis; hsa01100:Metabolic pathways; hsa04146:Peroxisome	R-HSA-193368: Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol; R-HSA-2046106: alpha-linolenic acid (ALA) metabolism; R-HSA-389887: Beta-oxidation of pristanoyl-CoA; R-HSA-390247: Beta-oxidation of very long chain fatty acids; R-HSA-9033241: Peroxisomal protein import; R-HSA-9033500: TYSND1 cleaves peroxisomal proteins	MetaCyc:HS05792-MON	P51659
TTZT9R2	Hydroxysteroid dehydrogenase 3-beta (HSD3B)	P14060; P26439	3BHS1_HUMAN; 3BHS2_HUMAN	Short-chain dehydrogenases reductase	3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase	HSD3B1	"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."	.	.	MTGWSCLVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAVLAANGWNLKNGGTLYTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRALQDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSRWSFPLSLMYWIGFLLEIVSFLLRPIYTYRPPFNRHIVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSLVDRHKETLKSKTQ	Literature-reported	Inhibition of 3 beta-hydroxysteroid-dehydrogenase: an approach for prostate cancer treatment Anticancer Res. 1995 Jul-Aug;15(4):1349-54.	0	.	.	.	.	.	.	.	.	.	.	hsa00140: Steroid hormone biosynthesis; hsa01100: Metabolic pathways; hsa04913: Ovarian steroidogenesis; hsa04925: Aldosterone synthesis and secretion; hsa04927: Cortisol synthesis and secretion; hsa04934: Cushing syndrome	R-HSA-193048: Androgen biosynthesis; R-HSA-193993: Mineralocorticoid biosynthesis; R-HSA-194002: Glucocorticoid biosynthesis	MetaCyc:HS08829-MON	P14060
TTN6STZ	Heat shock factor 1	.	HSF1_HUMAN	Single Protein	Heat shock transcription factor 1; HSF 1; HSTF 1	HSF1	"Functions 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. In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form."	.	.	MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPYSAPSPAYSSSSLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEEPPSPPQSPRVEEASPGRPSSVDTLLSPTALIDSILRESEPAPASVTALTDARGHTDTEGRPPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQTMLSSHGFSVDTSALLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPRPPEAENSSPDSGKQLVHYTAQPLFLLDPGSVDTGSNDLPVLFELGEGSYFSEGDGFAEDPTISLLTGSEPPKAKDPTVS	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q00613
TT78R5H	Heat shock protein 90 alpha (HSP90A)	P07900	HS90A_HUMAN	Heat shock protein	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	HSP90AA1	"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."	.	6GR5; 6GR4; 6GR3; 6GR1; 6GQU	MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPPLEGDDDTSRMEEVD	Successful	Tanespimycin: the opportunities and challenges of targeting heat shock protein 90. Expert Opin Investig Drugs. 2009 Jun;18(6):861-8.	21	Heat shock protein	Heat shock protein	heat shock protein 90 family.	.	.	"Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; Hsp90 protein"	PF02518; PF00183	PF02518; HATPase_c; PF00183; HSP90	.	.	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	"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"	.	P07900
TTH5YN2	Heat shock protein 90 beta (HSP90B)	P08238	HS90B_HUMAN	Heat shock protein	Heat shock 84 kDa; HSP84; HSP 84	HSP90AB1	"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)."	.	5UCJ; 5UCI; 5UCH; 5UC4; 5FWP	MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVAAEEPNAAVPDEIPPLEGDEDASRMEEVD	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	19	.	.	.	.	.	.	.	.	.	.	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	R-HSA-168928: DDX58/IFIH1-mediated induction of interferon-alpha/beta; R-HSA-2029482: Regulation of actin dynamics for phagocytic cup formation; R-HSA-3371497: HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand; R-HSA-3371511: HSF1 activation; R-HSA-3371568: Attenuation phase; R-HSA-3371571: HSF1-dependent transactivation; R-HSA-399954: Sema3A PAK dependent Axon repulsion; R-HSA-5336415: Uptake and function of diphtheria toxin; R-HSA-6798695: Neutrophil degranulation; R-HSA-844456: The NLRP3 inflammasome; R-HSA-8852276: The role of GTSE1 in G2/M progression after G2 checkpoint; R-HSA-8937144: Aryl hydrocarbon receptor signalling; R-HSA-8939211: ESR-mediated signaling; R-HSA-9013418: RHOBTB2 GTPase cycle; R-HSA-9018519: Estrogen-dependent gene expression; R-HSA-9613829: Chaperone Mediated Autophagy; R-HSA-9660826: Purinergic signaling in leishmaniasis infection; R-HSA-9679191: Potential therapeutics for SARS; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses	.	P08238
TTFPKXQ	Endoplasmin (HSP90B1)	P14625	ENPL_HUMAN	Heat shock protein	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	HSP90B1	"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."	.	4NH9	MRALWVLGLCCVLLTFGSVRADDEVDVDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTETVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKKPKTKKVEKTVWDWELMNDIKPIWQRPSKEVEEDEYKAFYKSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRGLFDEYGSKKSDYIKLYVRRVFITDDFHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIADDKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPTDITSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAVEKEFEPLLNWMKDKALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQKKTFEINPRHPLIRDMLRRIKEDEDDKTVLDLAVVLFETATLRSGYLLPDTKAYGDRIERMLRLSLNIDPDAKVEEEPEEEPEETAEDTTEDTEQDEDEEMDVGTDEEEETAKESTAEKDEL	Clinical trial	"Clinical pipeline report, company report or official report of Heat Biologics."	21	Heat shock protein	Heat shock protein	heat shock protein 90 family.	.	.	"Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; Hsp90 protein"	PF02518; PF00183	PF02518; HATPase_c; PF00183; HSP90	.	.	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	R-HSA-1679131:Trafficking and processing of endosomal TLR; R-HSA-3000480:Scavenging by Class A Receptors	.	P14625
TTAI9ZQ	Heat shock protein A 12B (HSPA12B)	Q96MM6	HS12B_HUMAN	Heat shock protein	Heat shock 70 kDa protein 12B; C20orf60	HSPA12B	"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."	.	.	MLAVPEMGLQGLYIGSSPERSPVPSPPGSPRTQESCGIAPLTPSQSPKPEVRAPQQASFSVVVAIDFGTTSSGYAFSFASDPEAIHMMRKWEGGDPGVAHQKTPTCLLLTPEGAFHSFGYTARDYYHDLDPEEARDWLYFEKFKMKIHSATDLTLKTQLEAVNGKTMPALEVFAHALRFFREHALQELREQSPSLPEKDTVRWVLTVPAIWKQPAKQFMREAAYLAGLVSRENAEQLLIALEPEAASVYCRKLRLHQLLDLSGRAPGGGRLGERRSIDSSFRQAREQLRRSRHSRTFLVESGVGELWAEMQAGDRYVVADCGGGTVDLTVHQLEQPHGTLKELYKASGGPYGAVGVDLAFEQLLCRIFGEDFIATFKRQRPAAWVDLTIAFEARKRTAGPHRAGALNISLPFSFIDFYRKQRGHNVETALRRSSVNFVKWSSQGMLRMSCEAMNELFQPTVSGIIQHIEALLARPEVQGVKLLFLVGGFAESAVLQHAVQAALGARGLRVVVPHDVGLTILKGAVLFGQAPGVVRVRRSPLTYGVGVLNRFVPGRHPPEKLLVRDGRRWCTDVFERFVAAEQSVALGEEVRRSYCPARPGQRRVLINLYCCAAEDARFITDPGVRKCGALSLELEPADCGQDTAGAPPGRREIRAAMQFGDTEIKVTAVDVSTNRSVRASIDFLSN	Literature-reported	MiR-4505 aggravates lipopolysaccharide-induced vascular endothelial injury by targeting heat shock protein A12B. Mol Med Rep. 2018 Jan;17(1):1389-1395.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-3371453: Regulation of HSF1-mediated heat shock response	.	Q96MM6
TTHYBIX	Heat shock protein 70 (HSP70)	P0DMV8; P0DMV9	HS71A_HUMAN; HS71B_HUMAN	Heat shock protein	Heat shock 70 kDa protein; HSP72; HSP70	HSPA1A	"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."	.	.	MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD	Clinical trial	Mitogen-activated protein kinase kinase kinase 12 (MAP3K12; DLK); c-jun N-terminal kinase (JNK). SciBX 2(11); doi:10.1038/scibx.2009.462. March 19 2009	21	.	.	HSF family.	.	.	HSF-type DNA-binding; Vertebrate heat shock transcription factor	PF00447; PF06546	PF00447; HSF_DNA-bind; PF06546; Vert_HS_TF	.	.	hsa03040: Spliceosome; hsa04010: MAPK signaling pathway; hsa04141: Protein processing in endoplasmic reticulum; hsa04144: Endocytosis; hsa04213: Longevity regulating pathway - multiple species; hsa04612: Antigen processing and presentation; hsa04915: Estrogen signaling pathway; hsa05020: Prion disease; hsa05134: Legionellosis; hsa05145: Toxoplasmosis; hsa05162: Measles; hsa05417: Lipid and atherosclerosis	R-HSA-168330: Viral RNP Complexes in the Host Cell Nucleus; R-HSA-3371453: Regulation of HSF1-mediated heat shock response; R-HSA-3371497: HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand; R-HSA-3371568: Attenuation phase; R-HSA-3371571: HSF1-dependent transactivation; R-HSA-450408: AUF1 (hnRNP D0) binds and destabilizes mRNA; R-HSA-6798695: Neutrophil degranulation	.	P0DMV8
TTW26OG	Endoplasmic reticulum chaperone BiP (HSPA5)	P11021	BIP_HUMAN	Acid anhydride hydrolase	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	HSPA5	"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."	EC 3.6.4.10	6DFO; 6DFM; 6CZ1; 6ASY; 5F2R	MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAEKDEL	Clinical trial	"NKP-1339, a first-in-class anticancer drug showing mild side effects and activity in patients suffering from advanced refractory cancer. BMC Pharmacol Toxicol. 2012; 13(Suppl 1): A82."	17	EC:3.6	Heat shock protein	heat shock protein 70 family.	3.6.4.10 	Acting on acid anhydrides	Hsp70 protein	PF00012	PF00012; HSP70	1.A.33.1.6	The Cation Channel-forming Heat Shock Protein-70 (Hsp70) Family	hsa03060:Protein export; hsa04141:Protein processing in endoplasmic reticulum; hsa04612:Antigen processing and presentation; hsa04918:Thyroid hormone synthesis; hsa05020:Prion diseases	R-HSA-114608:Platelet degranulation; R-HSA-3371453:Regulation of HSF1-mediated heat shock response	.	P11021
TTMQL3K	Lipopolysaccharide-associated protein 1 (HSPA8)	P11142	HSP7C_HUMAN	Heat shock protein	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	HSPA8	"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."	.	6B1N; 6B1M; 6B1I; 5AQV; 5AQU	MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD	Literature-reported	DrugBank 3.0: a comprehensive resource for 'omics' research on drugs. Nucleic Acids Res. 2011 Jan;39(Database issue):D1035-41.	0	Heat shock protein	Heat shock protein	heat shock protein 70 family.	.	.	Hsp70 protein	PF00012	PF00012; HSP70	.	.	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	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	.	P11142
TTMTPG3	Mortalin (HSPA9)	P38646	GRP75_HUMAN	Heat shock protein	"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"	HSPA9	"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."	.	6NHK; 4KBO; 3N8E	MISASRAAAARLVGAAASRGPTAARHQDSWNGLSHEAFRLVSRRDYASEAIKGAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQKDIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDSSGPKHLNMKLTRAQFEGIVTDLIRRTIAPCQKAMQDAEVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNKLKEEISKMRELLARKDSETGENIRQAASSLQQASLKLFEMAYKKMASEREGSGSSGTGEQKEDQKEEKQ	Clinical trial	Selective toxicity of MKT-077 to cancer cells is mediated by its binding to the hsp70 family protein mot-2 and reactivation of p53 function. Cancer Res. 2000 Dec 15;60(24):6818-21.	21	Heat shock protein	Heat shock protein	heat shock protein 70 family.	.	.	Hsp70 protein	PF00012	PF00012; HSP70	.	.	hsa03018:RNA degradation; hsa05152:Tuberculosis	R-HSA-1268020:Mitochondrial protein import; R-HSA-3371453:Regulation of HSF1-mediated heat shock response	.	P38646
TT9AZWY	HSPB1 messenger RNA (HSPB1 mRNA)	P04792	HSPB1_HUMAN	mRNA target	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)	HSPB1	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.	.	4MJH; 3Q9Q; 3Q9P; 2N3J	MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK	Discontinued	Biphenyl amide p38 kinase inhibitors 4: DFG-in and DFG-out binding modes. Bioorg Med Chem Lett. 2008 Aug 1;18(15):4433-7.	3	mRNA	mRNA target	.	.	.	Hsp20/alpha crystallin family	PF00011	PF00011; HSP20	.	.	hsa04010:MAPK signaling pathway; hsa04370:VEGF signaling pathway; hsa05146:Amoebiasis; hsa05169:Epstein-Barr virus infection	R-HSA-4420097:VEGFA-VEGFR2 Pathway; R-HSA-5687128:MAPK6/MAPK4 signaling	.	P04792
TT5IP87	Heat shock protein 20 (HSP20)	P04792	HSPB1_HUMAN	Heat shock protein	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	HSPB1	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.	.	4MJH; 3Q9Q; 3Q9P; 2N3J	MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK	Clinical trial	"Internalization and intracellular trafficking of a PTD-conjugated anti-fibrotic peptide, AZX100, in human dermal keloid fibroblasts. J Pharm Sci. 2010 Jul;99(7):3100-21."	21	.	.	.	.	.	.	.	.	.	.	hsa04010: MAPK signaling pathway; hsa04370: VEGF signaling pathway; hsa05146: Amoebiasis	R-HSA-4420097: VEGFA-VEGFR2 Pathway; R-HSA-450408: AUF1 (hnRNP D0) binds and destabilizes mRNA; R-HSA-5687128: MAPK6/MAPK4 signaling; R-HSA-9009391: Extra-nuclear estrogen signaling	.	P04792
TTLH8WG	HSP27 messenger RNA (HSPB3 mRNA)	Q12988	HSPB3_HUMAN	mRNA target	Protein 3 (mRNA); HspB3 (mRNA); Heat shock protein beta-3 (mRNA); Heat shock 17 kDa protein (mRNA); HSPL27 (mRNA); HSP 17 (mRNA)	HSPB3	Inhibitor of actin polymerization.	.	6F2R	MAKIILRHLIEIPVRYQEEFEARGLEDCRLDHALYALPGPTIVDLRKTRAAQSPPVDSAAETPPREGKSHFQILLDVVQFLPEDIIIQTFEGWLLIKAQHGTRMDEHGFISRSFTRQYKLPDGVEIKDLSAVLCHDGILVVEVKDPVGTK	Literature-reported	"Heat Shock Protein 27, a Novel Regulator of Transforming Growth Factor Induced Resistance to Cisplatin in A549 Cell. Pharmacology. 2017;100(5-6):283-291."	.	mRNA	mRNA target	.	.	.	Hsp20/alpha crystallin family	PF00011	PF00011; HSP20	.	.	.	.	.	Q12988
TTMG98T	Heat shock protein 27 (HSP27)	Q12988	HSPB3_HUMAN	Heat shock protein	Protein 3; HspB3; Heat shock protein beta3; Heat shock 17 kDa protein; HSP 17	HSPB3	Inhibitor of actin polymerization.	.	6F2R	MAKIILRHLIEIPVRYQEEFEARGLEDCRLDHALYALPGPTIVDLRKTRAAQSPPVDSAAETPPREGKSHFQILLDVVQFLPEDIIIQTFEGWLLIKAQHGTRMDEHGFISRSFTRQYKLPDGVEIKDLSAVLCHDGILVVEVKDPVGTK	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	Q12988
TTY0OJN	Heat shock protein beta-8 (HSPB8)	Q9UJY1	HSPB8_HUMAN	Heat shock protein	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	HSPB8	Displays temperature-dependent chaperone activity.	.	.	MADGQMPFSCHYPSRLRRDPFRDSPLSSRLLDDGFGMDPFPDDLTASWPDWALPRLSSAWPGTLRSGMVPRGPTATARFGVPAEGRTPPPFPGEPWKVCVNVHSFKPEELMVKTKDGYVEVSGKHEEKQQEGGIVSKNFTKKIQLPAEVDPVTVFASLSPEGLLIIEAPQVPPYSTFGESSFNNELPQDSQEVTCT	Literature-reported	HSPB8 Promotes the Fusion of Autophagosome and Lysosome during Autophagy in Diabetic Neurons. Int J Med Sci. 2017 Oct 15;14(13):1335-1341.	.	Heat shock protein	Heat shock protein	small heat shock protein (HSP20) family.	.	.	Hsp20/alpha crystallin family	PF00011	PF00011; HSP20	.	.	.	R-HSA-3371571: HSF1-dependent transactivation	.	Q9UJY1
TT9HL5R	Mitochondrial matrix protein P1 (HSPD1)	P10809	CH60_HUMAN	Chaperonin ATPase	"P60 lymphocyte protein; HuCHA60; Hsp60; Heat shock protein 60; HSP-60; Chaperonin 60; CPN60; 60 kDa heat shock protein, mitochondrial; 60 kDa chaperonin"	HSPD1	"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."	EC 5.6.1.7	4PJ1	MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF	Clinical trial	Therapy with the hsp60 peptide DiaPep277 in C-peptide positive type 1 diabetes patients. Diabetes Metab Res Rev. 2007 May;23(4):269-75.	25	EC:5.6.1	Heat shock protein	chaperonin (HSP60) family.	5.6.1.7 	Isomerases altering macromolecular conformation	TCP-1/cpn60 chaperonin family	PF00118	PF00118; Cpn60_TCP1	.	.	hsa03018:RNA degradation; hsa04940:Type I diabetes mellitus; hsa05134:Legionellosis; hsa05152:Tuberculosis	R-HSA-1268020:Mitochondrial protein import	.	P10809
TTWYMFE	Mitochondrial 10kDa heat shock protein (HSPE1)	P61604	CH10_HUMAN	Heat shock protein	"Hsp10; Earlypregnancy factor; Early-pregnancy factor; EPF; Chaperonin 10; CPN10; 10 kDa heat shock protein, mitochondrial; 10 kDa chaperonin"	HSPE1	"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."	.	4PJ1	MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGSKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD	Clinical trial	"XToll, a recombinant chaperonin 10 as an anti-inflammatory immunomodulator. Curr Opin Investig Drugs. 2008 May;9(5):523-33."	19	Heat shock protein	Heat shock protein	GroES chaperonin family.	.	.	Chaperonin 10 Kd subunit	PF00166	PF00166; Cpn10	.	.	.	R-HSA-9013408: RHOG GTPase cycle	.	P61604
TT5UM29	Perlecan (HSPG)	P98160	PGBM_HUMAN	.	LG3 peptide; Basement membranespecific heparan sulfate proteoglycan coreprotein; Basement membrane-specific heparan sulfate proteoglycan core protein	HSPG2	"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."	.	3SH5; 3SH4	MGWRAAGALLLALLLHGRLLAVTHGLRAYDGLSLPEDIETVTASQMRWTHSYLSDDEDMLADSISGDDLGSGDLGSGDFQMVYFRALVNFTRSIEYSPQLEDAGSREFREVSEAVVDTLESEYLKIPGDQVVSVVFIKELDGWVFVELDVGSEGNADGAQIQEMLLRVISSGSVASYVTSPQGFQFRRLGTVPQFPRACTEAEFACHSYNECVALEYRCDRRPDCRDMSDELNCEEPVLGISPTFSLLVETTSLPPRPETTIMRQPPVTHAPQPLLPGSVRPLPCGPQEAACRNGHCIPRDYLCDGQEDCEDGSDELDCGPPPPCEPNEFPCGNGHCALKLWRCDGDFDCEDRTDEANCPTKRPEEVCGPTQFRCVSTNMCIPASFHCDEESDCPDRSDEFGCMPPQVVTPPRESIQASRGQTVTFTCVAIGVPTPIINWRLNWGHIPSHPRVTVTSEGGRGTLIIRDVKESDQGAYTCEAMNARGMVFGIPDGVLELVPQRGPCPDGHFYLEHSAACLPCFCFGITSVCQSTRRFRDQIRLRFDQPDDFKGVNVTMPAQPGTPPLSSTQLQIDPSLHEFQLVDLSRRFLVHDSFWALPEQFLGNKVDSYGGSLRYNVRYELARGMLEPVQRPDVVLMGAGYRLLSRGHTPTQPGALNQRQVQFSEEHWVHESGRPVQRAELLQVLQSLEAVLIQTVYNTKMASVGLSDIAMDTTVTHATSHGRAHSVEECRCPIGYSGLSCESCDAHFTRVPGGPYLGTCSGCNCNGHASSCDPVYGHCLNCQHNTEGPQCNKCKAGFFGDAMKATATSCRPCPCPYIDASRRFSDTCFLDTDGQATCDACAPGYTGRRCESCAPGYEGNPIQPGGKCRPVNQEIVRCDERGSMGTSGEACRCKNNVVGRLCNECADGSFHLSTRNPDGCLKCFCMGVSRHCTSSSWSRAQLHGASEEPGHFSLTNAASTHTTNEGIFSPTPGELGFSSFHRLLSGPYFWSLPSRFLGDKVTSYGGELRFTVTQRSQPGSTPLHGQPLVVLQGNNIILEHHVAQEPSPGQPSTFIVPFREQAWQRPDGQPATREHLLMALAGIDTLLIRASYAQQPAESRVSGISMDVAVPEETGQDPALEVEQCSCPPGYRGPSCQDCDTGYTRTPSGLYLGTCERCSCHGHSEACEPETGACQGCQHHTEGPRCEQCQPGYYGDAQRGTPQDCQLCPCYGDPAAGQAAHTCFLDTDGHPTCDACSPGHSGRHCERCAPGYYGNPSQGQPCQRDSQVPGPIGCNCDPQGSVSSQCDAAGQCQCKAQVEGLTCSHCRPHHFHLSASNPDGCLPCFCMGITQQCASSAYTRHLISTHFAPGDFQGFALVNPQRNSRLTGEFTVEPVPEGAQLSFGNFAQLGHESFYWQLPETYQGDKVAAYGGKLRYTLSYTAGPQGSPLSDPDVQITGNNIMLVASQPALQGPERRSYEIMFREEFWRRPDGQPATREHLLMALADLDELLIRATFSSVPLAASISAVSLEVAQPGPSNRPRALEVEECRCPPGYIGLSCQDCAPGYTRTGSGLYLGHCELCECNGHSDLCHPETGACSQCQHNAAGEFCELCAPGYYGDATAGTPEDCQPCACPLTNPENMFSRTCESLGAGGYRCTACEPGYTGQYCEQCGPGYVGNPSVQGGQCLPETNQAPLVVEVHPARSIVPQGGSHSLRCQVSGSPPHYFYWSREDGRPVPSGTQQRHQGSELHFPSVQPSDAGVYICTCRNLHQSNTSRAELLVTEAPSKPITVTVEEQRSQSVRPGADVTFICTAKSKSPAYTLVWTRLHNGKLPTRAMDFNGILTIRNVQLSDAGTYVCTGSNMFAMDQGTATLHVQASGTLSAPVVSIHPPQLTVQPGQLAEFRCSATGSPTPTLEWTGGPGGQLPAKAQIHGGILRLPAVEPTDQAQYLCRAHSSAGQQVARAVLHVHGGGGPRVQVSPERTQVHAGRTVRLYCRAAGVPSATITWRKEGGSLPPQARSERTDIATLLIPAITTADAGFYLCVATSPAGTAQARIQVVVLSASDASPPPVKIESSSPSVTEGQTLDLNCVVAGSAHAQVTWYRRGGSLPPHTQVHGSRLRLPQVSPADSGEYVCRVENGSGPKEASITVSVLHGTHSGPSYTPVPGSTRPIRIEPSSSHVAEGQTLDLNCVVPGQAHAQVTWHKRGGSLPARHQTHGSLLRLHQVTPADSGEYVCHVVGTSGPLEASVLVTIEASVIPGPIPPVRIESSSSTVAEGQTLDLSCVVAGQAHAQVTWYKRGGSLPARHQVRGSRLYIFQASPADAGQYVCRASNGMEASITVTVTGTQGANLAYPAGSTQPIRIEPSSSQVAEGQTLDLNCVVPGQSHAQVTWHKRGGSLPVRHQTHGSLLRLYQASPADSGEYVCRVLGSSVPLEASVLVTIEPAGSVPALGVTPTVRIESSSSQVAEGQTLDLNCLVAGQAHAQVTWHKRGGSLPARHQVHGSRLRLLQVTPADSGEYVCRVVGSSGTQEASVLVTIQQRLSGSHSQGVAYPVRIESSSASLANGHTLDLNCLVASQAPHTITWYKRGGSLPSRHQIVGSRLRIPQVTPADSGEYVCHVSNGAGSRETSLIVTIQGSGSSHVPSVSPPIRIESSSPTVVEGQTLDLNCVVARQPQAIITWYKRGGSLPSRHQTHGSHLRLHQMSVADSGEYVCRANNNIDALEASIVISVSPSAGSPSAPGSSMPIRIESSSSHVAEGETLDLNCVVPGQAHAQVTWHKRGGSLPSHHQTRGSRLRLHHVSPADSGEYVCRVMGSSGPLEASVLVTIEASGSSAVHVPAPGGAPPIRIEPSSSRVAEGQTLDLKCVVPGQAHAQVTWHKRGGNLPARHQVHGPLLRLNQVSPADSGEYSCQVTGSSGTLEASVLVTIEPSSPGPIPAPGLAQPIYIEASSSHVTEGQTLDLNCVVPGQAHAQVTWYKRGGSLPARHQTHGSQLRLHLVSPADSGEYVCRAASGPGPEQEASFTVTVPPSEGSSYRLRSPVISIDPPSSTVQQGQDASFKCLIHDGAAPISLEWKTRNQELEDNVHISPNGSIITIVGTRPSNHGTYRCVASNAYGVAQSVVNLSVHGPPTVSVLPEGPVWVKVGKAVTLECVSAGEPRSSARWTRISSTPAKLEQRTYGLMDSHAVLQISSAKPSDAGTYVCLAQNALGTAQKQVEVIVDTGAMAPGAPQVQAEEAELTVEAGHTATLRCSATGSPAPTIHWSKLRSPLPWQHRLEGDTLIIPRVAQQDSGQYICNATSPAGHAEATIILHVESPPYATTVPEHASVQAGETVQLQCLAHGTPPLTFQWSRVGSSLPGRATARNELLHFERAAPEDSGRYRCRVTNKVGSAEAFAQLLVQGPPGSLPATSIPAGSTPTVQVTPQLETKSIGASVEFHCAVPSDRGTQLRWFKEGGQLPPGHSVQDGVLRIQNLDQSCQGTYICQAHGPWGKAQASAQLVIQALPSVLINIRTSVQTVVVGHAVEFECLALGDPKPQVTWSKVGGHLRPGIVQSGGVVRIAHVELADAGQYRCTATNAAGTTQSHVLLLVQALPQISMPQEVRVPAGSAAVFPCIASGYPTPDISWSKLDGSLPPDSRLENNMLMLPSVRPQDAGTYVCTATNRQGKVKAFAHLQVPERVVPYFTQTPYSFLPLPTIKDAYRKFEIKITFRPDSADGMLLYNGQKRVPGSPTNLANRQPDFISFGLVGGRPEFRFDAGSGMATIRHPTPLALGHFHTVTLLRSLTQGSLIVGDLAPVNGTSQGKFQGLDLNEELYLGGYPDYGAIPKAGLSSGFIGCVRELRIQGEEIVFHDLNLTAHGISHCPTCRDRPCQNGGQCHDSESSSYVCVCPAGFTGSRCEHSQALHCHPEACGPDATCVNRPDGRGYTCRCHLGRSGLRCEEGVTVTTPSLSGAGSYLALPALTNTHHELRLDVEFKPLAPDGVLLFSGGKSGPVEDFVSLAMVGGHLEFRYELGSGLAVLRSAEPLALGRWHRVSAERLNKDGSLRVNGGRPVLRSSPGKSQGLNLHTLLYLGGVEPSVPLSPATNMSAHFRGCVGEVSVNGKRLDLTYSFLGSQGIGQCYDSSPCERQPCQHGATCMPAGEYEFQCLCRDGFKGDLCEHEENPCQLREPCLHGGTCQGTRCLCLPGFSGPRCQQGSGHGIAESDWHLEGSGGNDAPGQYGAYFHDDGFLAFPGHVFSRSLPEVPETIELEVRTSTASGLLLWQGVEVGEAGQGKDFISLGLQDGHLVFRYQLGSGEARLVSEDPINDGEWHRVTALREGRRGSIQVDGEELVSGRSPGPNVAVNAKGSVYIGGAPDVATLTGGRFSSGITGCVKNLVLHSARPGAPPPQPLDLQHRAQAGANTRPCPS	Discontinued	A perlecan-inducing compound significantly inhibits smooth muscle cell function and in-stent intimal hyperplasia: novel insights into the diverse biological effects of perlecan. EuroIntervention. 2010 May;6(1):134-40.	3	.	.	.	.	.	EGF-like domain; Immunoglobulin I-set domain; Immunoglobulin domain; Laminin B (Domain IV); Laminin EGF domain; Laminin G domain; Low-density lipoprotein receptor domain class A	PF00008; PF07679; PF13895; PF00052; PF00053; PF00054; PF00057	PF00008; EGF; PF07679; I-set; PF13895; Ig_2; PF00052; Laminin_B; PF00053; Laminin_EGF; PF00054; Laminin_G_1; PF00057; Ldl_recept_a	.	.	hsa04512:ECM-receptor interaction; hsa05161:Hepatitis B; hsa05205:Proteoglycans in cancer	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	.	.
TTQA9C6	Herpes simplex virus E3 ubiquitin-protein ligase ICP0 (HSV ICP0)	P08393	ICP0_HHV11	.	VMW110; Trans-acting transcriptional protein ICP0; RING-type E3 ubiquitin transferase ICP0; Immediate-early protein IE110; E3 ubiquitin-protein ligase ICP0; Alpha-0 protein	HSV ICP0	"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."	EC 2.3.2.27	5C56; 4WPI; 4WPH	MEPRPGASTRRPEGRPQREPAPDVWVFPCDRDLPDSSDSEAETEVGGRGDADHHDDDSASEADSTDTELFETGLLGPQGVDGGAVSGGSPPREEDPGSCGGAPPREDGGSDEGDVCAVCTDEIAPHLRCDTFPCMHRFCIPCMKTWMQLRNTCPLCNAKLVYLIVGVTPSGSFSTIPIVNDPQTRMEAEEAVRAGTAVDFIWTGNQRFAPRYLTLGGHTVRALSPTHPEPTTDEDDDDLDDADYVPPAPRRTPRAPPRRGAAAPPVTGGASHAAPQPAAARTAPPSAPIGPHGSSNTNTTTNSSGGGGSRQSRAAAPRGASGPSGGVGVGVGVVEAEAGRPRGRTGPLVNRPAPLANNRDPIVISDSPPASPHRPPAAPMPGSAPRPGPPASAAASGPARPRAAVAPCVRAPPPGPGPRAPAPGAEPAARPADARRVPQSHSSLAQAANQEQSLCRARATVARGSGGPGVEGGHGPSRGAAPSGAAPLPSAASVEQEAAVRPRKRRGSGQENPSPQSTRPPLAPAGAKRAATHPPSDSGPGGRGQGGPGTPLTSSAASASSSSASSSSAPTPAGAASSAAGAASSSASASSGGAVGALGGRQEETSLGPRAASGPRGPRKCARKTRHAETSGAVPAGGLTRYLPISGVSSVVALSPYVNKTITGDCLPILDMETGNIGAYVVLVDQTGNMATRLRAAVPGWSRRTLLPETAGNHVMPPEYPTAPASEWNSLWMTPVGNMLFDQGTLVGALDFRSLRSRHPWSGEQGASTRDEGKQ	Literature-reported	The herpes simplex virus type 1 alpha protein ICP27 can act as a trans-repressor or a trans-activator in combination with ICP4 and ICP0. J Virol. 1988 Dec;62(12):4510-22.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT51ZGC	Herpes simplex virus DNA polymerase POL (HSV POL)	P04293-P10226	DPOL_HHV21-PAP_HHV11	DNA polymerase type-B family	Complex of DNA polymerase processivity factor and DNA polymerase catalytic subunit	HSV POL	"Synthesize herpes simplex virus DNA from deoxyribonucleotides, the building blocks of DNA."	.	.	MTDSPGGVAPASPVEDASDASLGQPEEGAPCQVVLQGAELNGILQAFAPLRTSLLDSLLVMGDRGILIHNTIFGEQVFLPLEHSQFSRYRWRGPTAAFLSLVDQKRSLLSVFRANQYPDLRRVELAITGQAPFRTLVQRIWTTTSDGEAVELASETLMKRELTSFVVLVPQGTPDVQLRLTRPQLTKVLNATGADSATPTTFELGVNGKFSVFTTSTCVTFAAREEGVSSSTSTQVQILSNALTKAGQAAANAKTVYGENTHRTFSVVVDDCSMRAVLRRLQVGGGTLKFFLTTPVPSLCVTATGPNAVSAVFLLKPQKICLDWLGHSQGSPSAGSSASRASGSEPTDSQDSASDAVSHGDPEDLDGAARAGEAGALHACPMPSSTTRVTPTTKRGRSGGEDARADTALKKPKTGSPTAPPPADPVPLDTEDDSDAADGTAARPAAPDARSGSRYACYFRDLPTGEASPGAFSAFRGGPQTPYGFGFPMFCAAGGPASPGGKSAARAASGFFAPHNPRGATQTAPPPCRRQNFYNPHLAQTGTQPKAPGPAQRHTYYSECDEFRFIAPRSLDEDAPAEQRTGVHDGRLRRAPKVYCGGDERDVLRVGPEGFWPRRLRLWGGADHAPEGFDPTVTVFHVYDILEHVEHAYSMRAAQLHERFMDAITPAGTVITLLGLTPEGHRVAVHVYGTRQYFYMNKAEVDRHLQCRAPRDLCERLAAALRESPGASFRGISADHFEAEVVERADVYYYETRPTLYYRVFVRSGRALAYLCDNFCPAIRKYEGGVDATTRFILDNPGFVTFGWYRLKPGRGNAPAQPRPPTAFGTSSDVEFNCTADNLAVEGAMCDLPAYKLMCFDIECKAGGEDELAFPVAERPEDLVIQISCLLYDLSTTALEHILLFSLGSCDLPESHLSDLASRGLPAPVVLEFDSEFEMLLAFMTFVKQYGPEFVTGYNIINFDWPFVLTKLTEIYKVPLDGYGRMNGRGVFRVWDIGQSHFQKRSKIKVNGMVNIDMYGIITDKVKLSSYKLNAVAEAVLKDKKKDLSYRDIPAYYASGPAQRGVIGEYCVQDSLLVGQLFFKFLPHLELSAVARLAGINITRTIYDGQQIRVFTCLLRLAGQKGFILPDTQGRFRGLDKEAPKRPAVPRGEGERPGDGNGDEDKDDDEDGDEDGDEREEVARETGGRHVGYQGARVLDPTSGFHVDPVVVFDFASLYPSIIQAHNLCFSTLSLRPEAVAHLEADRDYLEIEVGGRRLFFVKAHVRESLLSILLRDWLAMRKQIRSRIPQSPPEEAVLLDKQQAAIKVVCNSVYGFTGVQHGLLPCLHVAATVTTIGREMLLATRAYVHARWAEFDQLLADFPEAAGMRAPGPYSMRIIYGDTDSIFVLCRGLTGEALVAMGDKMASHISRALFLPPIKLECEKTFTKLLLIAKKKYIGVICGGKMLIKGVDLVRKNNCAFINRTSRALVDLLFYDDTVSGAAAALAERPAEEWLARPLPEGLQAFGAVLVDAHRRITDPERDIQDFVLTAELSRHPRAYTNKRLAHLTVYYKLMARRAQVPSIKDRIPYVIVAQTREVEETVARLAALRELDAAAPGDEPAPPAALPSPAKRPRETPSHADPPGGASKPRKLLVSELAEDPGYAIARGVPLNTDYYFSHLLGAACVTFKALFGNNAKITESLLKRFIPETWHPPDDVAARLRAAGFGPAGAGATAEETRRMLHRAFDTLA	Literature-reported	Herpes simplex virus type 1 DNA polymerase. Mechanism of inhibition by acyclovir triphosphate. J Biol Chem. 1989 May 5;264(13):7405-11.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMJX4U	Herpes simplex virus Ribonucleoside-diphosphate reductase (HSV RIR1)	P08543	RIR1_HHV11	CH/CH(2) oxidoreductase	HSV Ribonucleotide reductase; HSV Ribonucleoside diphosphate reductase; HSV RIR1	HSV RIR1	"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."	.	.	MASRPAASSPVEARAPVGGQEAGGPSAATQGEAAGAPLAHGHHVYCQRVNGVMVLSDKTPGSASYRISDNNFVQCGSNCTMIIDGDVVRGRPQDPGAAASPAPFVAVTNIGAGSDGGTAVVAFGGTPRRSAGTSTGTQTADVPTEALGGPPPPPRFTLGGGCCSCRDTRRRSAVFGGEGDPVGPAEFVSDDRSSDSDSDDSEDTDSETLSHASSDVSGGATYDDALDSDSSSDDSLQIDGPVCRPWSNDTAPLDVCPGTPGPGADAGGPSAVDPHAPTPEAGAGLAADPAVARDDAEGLSDPRPRLGTGTAYPVPLELTPENAEAVARFLGDAVNREPALMLEYFCRCAREETKRVPPRTFGSPPRLTEDDFGLLNYALVEMQRLCLDVPPVPPNAYMPYYLREYVTRLVNGFKPLVSRSARLYRILGVLVHLRIRTREASFEEWLRSKEVALDFGLTERLREHEAQLVILAQALDHYDCLIHSTPHTLVERGLQSALKYEEFYLKRFGGHYMESVFQMYTRIAGFLACRATRGMRHIALGREGSWWEMFKFFFHRLYDHQIVPSTPAMLNLGTRNYYTSSCYLVNPQATTNKATLRAITSNVSAILARNGGIGLCVQAFNDSGPGTASVMPALKVLDSLVAAHNKESARPTGACVYLEPWHTDVRAVLRMKGVLAGEEAQRCDNIFSALWMPDLFFKRLIRHLDGEKNVTWTLFDRDTSMSLADFHGEEFEKLYQHLEVMGFGEQIPIQELAYGIVRSAATTGSPFVMFKDAVNRHYIYDTQGAAIAGSNLCTEIVHPASKRSSGVCNLGSVNLARCVSRQTFDFGRLRDAVQACVLMVNIMIDSTLQPTPQCTRGNDNLRSMGIGMQGLHTACLKLGLDLESAEFQDLNKHIAEVMLLSAMKTSNALCVRGARPFNHFKRSMYRAGRFHWERFPDARPRYEGEWEMLRQSMMKHGLRNSQFVALMPTAASAQISDVSEGFAPLFTNLFSKVTRDGETLRPNTLLLKELERTFSGKRLLEVMDSLDAKQWSVAQALPCLEPTHPLRRFKTAFDYDQKLLIDLCADRAPYVDHSQSMTLYVTEKADGTLPASTLVRLLVHAYKRGLKTGMYYCKVRKATNSGVFGGDDNIVCMSCAL	Discontinued	"Clofarabine: past, present, and future. Leuk Lymphoma. 2007 Oct;48(10):1922-30."	34	.	.	.	.	.	.	.	.	.	.	.	R-HSA-5213460: RIPK1-mediated regulated necrosis; R-HSA-9686347: Microbial modulation of RIPK1-mediated regulated necrosis	.	.
TTIU7X1	Herpes simplex virus DNA polymerase UL30 (HSV UL30)	P04293	DPOL_HHV11	DNA polymerase type-B	HSV DNA polymerase catalytic subunit	HSV UL30	"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."	.	.	MFSGGGGPLSPGGKSAARAASGFFAPAGPRGASRGPPPCLRQNFYNPYLAPVGTQQKPTGPTQRHTYYSECDEFRFIAPRVLDEDAPPEKRAGVHDGHLKRAPKVYCGGDERDVLRVGSGGFWPRRSRLWGGVDHAPAGFNPTVTVFHVYDILENVEHAYGMRAAQFHARFMDAITPTGTVITLLGLTPEGHRVAVHVYGTRQYFYMNKEEVDRHLQCRAPRDLCERMAAALRESPGASFRGISADHFEAEVVERTDVYYYETRPALFYRVYVRSGRVLSYLCDNFCPAIKKYEGGVDATTRFILDNPGFVTFGWYRLKPGRNNTLAQPAAPMAFGTSSDVEFNCTADNLAIEGGMSDLPAYKLMCFDIECKAGGEDELAFPVAGHPEDLVIQISCLLYDLSTTALEHVLLFSLGSCDLPESHLNELAARGLPTPVVLEFDSEFEMLLAFMTLVKQYGPEFVTGYNIINFDWPFLLAKLTDIYKVPLDGYGRMNGRGVFRVWDIGQSHFQKRSKIKVNGMVNIDMYGIITDKIKLSSYKLNAVAEAVLKDKKKDLSYRDIPAYYAAGPAQRGVIGEYCIQDSLLVGQLFFKFLPHLELSAVARLAGINITRTIYDGQQIRVFTCLLRLADQKGFILPDTQGRFRGAGGEAPKRPAAAREDEERPEEEGEDEDEREEGGGEREPEGARETAGRHVGYQGARVLDPTSGFHVNPVVVFDFASLYPSIIQAHNLCFSTLSLRADAVAHLEAGKDYLEIEVGGRRLFFVKAHVRESLLSILLRDWLAMRKQIRSRIPQSSPEEAVLLDKQQAAIKVVCNSVYGFTGVQHGLLPCLHVAATVTTIGREMLLATREYVHARWAAFEQLLADFPEAADMRAPGPYSMRIIYGDTDSIFVLCRGLTAAGLTAVGDKMASHISRALFLPPIKLECEKTFTKLLLIAKKKYIGVIYGGKMLIKGVDLVRKNNCAFINRTSRALVDLLFYDDTVSGAAAALAERPAEEWLARPLPEGLQAFGAVLVDAHRRITDPERDIQDFVLTAELSRHPRAYTNKRLAHLTVYYKLMARRAQVPSIKDRIPYVIVAQTREVEETVARLAALRELDAAAPGDEPAPPAALPSPAKRPRETPSPADPPGGASKPRKLLVSELAEDPAYAIAHGVALNTDYYFSHLLGAACVTFKALFGNNAKITESLLKRFIPEVWHPPDDVAARLRTAGFGAVGAGATAEETRRMLHRAFDTLA	Successful	Antimicrobial strategies: inhibition of viral polymerases by 3'-hydroxyl nucleosides. Drugs. 2009;69(2):151-66. 	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT4KCSR	Herpes simplex virus DNA polymerase processivity factor (HSV UL42)	P10226	PAP_HHV11	Herpesviridae DNA polymerase	UL42; Protein UL42; Polymerase accessory protein; HSV PAP; DNA-binding protein UL42	HSV UL42	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.	.	1DML	MTDSPGGVAPASPVEDASDASLGQPEEGAPCQVVLQGAELNGILQAFAPLRTSLLDSLLVMGDRGILIHNTIFGEQVFLPLEHSQFSRYRWRGPTAAFLSLVDQKRSLLSVFRANQYPDLRRVELAITGQAPFRTLVQRIWTTTSDGEAVELASETLMKRELTSFVVLVPQGTPDVQLRLTRPQLTKVLNATGADSATPTTFELGVNGKFSVFTTSTCVTFAAREEGVSSSTSTQVQILSNALTKAGQAAANAKTVYGENTHRTFSVVVDDCSMRAVLRRLQVGGGTLKFFLTTPVPSLCVTATGPNAVSAVFLLKPQKICLDWLGHSQGSPSAGSSASRASGSEPTDSQDSASDAVSHGDPEDLDGAARAGEAGALHACPMPSSTTRVTPTTKRGRSGGEDARADTALKKPKTGSPTAPPPADPVPLDTEDDSDAADGTAARPAAPDARSGSRYACYFRDLPTGEASPGAFSAFRGGPQTPYGFGFP	Literature-reported	Secondary structure and structure-activity relationships of peptides corresponding to the subunit interface of herpes simplex virus DNA polymerase. J Biol Chem. 2000 Jan 7;275(1):472-8.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTKCVJR	Herpes simplex virus Helicase-primase (HSV UL8)	P10192	HEPA_HHV11	Acid anhydrides hydrolase	Primase-associated factor; HEPA; DNA helicase/primase complex-associated protein	HSV UL8	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.	.	.	MDTADIVWVEESVSAITLYAVWLPPRAREYFHALVYFVCRNAAGEGRARFAEVSVTATELRDFYGSADVSVQAVVAAARAATTPAASPLEPLENPTLWRALYACVLAALERQTGPVALFAPLRIGSDPRTGLVVKVERASWGPPAAPRAALLVAEANIDIDPMALAARVAEHPDARLAWARLAAIRDTPQCASAASLTVNITTGTALFAREYQTLAFPPIKKEGAFGDLVEVCEVGLRPRGHPQRVTARVLLPRDYDYFVSAGEKFSAPALVALFRQWHTTVHAAPGALAPVFAFLGPEFEVRGGPVPYFAVLGFPGWPTFTVPATAESARDLVRGAAAAYAALLGAWPAVGARVVLPPRAWPGVASAAAGCLLPAVREAVARWHPATKIIQLLDPPAAVGPVWTARFCFPGLRAQLLAALADLGGSGLADPHGRTGLARLDALVVAAPSEPWAGAVLERLVPDTCNACPALRQLLGGVMAAVCLQIEETASSVKFAVCGGDGGAFWGVFNVDPQDADAASGVIEDARRAIETAVGAVLRANAVRLRHPLCLALEGVYTHAVAWSQAGVWFWNSRDNTDHLGGFPLRGPAYTTAAGVVRDTLRRVLGLTTACVPEEDALTARGLMEDACDRLILDAFNKRLDAEYWSVRVSPFEASDPLPPTAFRGGALLDAEHYWRRVVRVCPGGGESVGVPVDLYPRPLVLPPVDCAHHLREILREIELVFTGVLAGVWGEGGKFVYPFDDKMSFLFA	Clinical trial	Helicase primase: targeting the Achilles heel of herpes simplex viruses. Antivir Chem Chemother. 2004 May;15(3):135-40.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTC6IX5	Oxidoreductase HTATIP2 (HTATIP2)	Q9BUP3	HTAI2_HUMAN	.	HIV-1 TAT-interactive protein 2; 30 kDa HIV-1 TAT-interacting protein	HTATIP2	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.	EC 1.1.1.-	2BKA	MAETEALSKLREDFRMQNKSVFILGASGETGRVLLKEILEQGLFSKVTLIGRRKLTFDEEAYKNVNQEVVDFEKLDDYASAFQGHDVGFCCLGTTRGKAGAEGFVRVDRDYVLKSAELAKAGGCKHFNLLSSKGADKSSNFLYLQVKGEVEAKVEELKFDRYSVFRPGVLLCDRQESRPGEWLVRKFFGSLPDSWASGHSVPVVTVVRAMLNNVVRPRDKQMELLENKAIHDLGKAHGSLKP	Literature-reported	Inhibition of nuclear import by the proapoptotic protein CC3. Mol Cell Biol. 2004 Aug;24(16):7091-101.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9BUP3
TTSQIFT	5-HT 1A receptor (HTR1A)	P08908	5HT1A_HUMAN	GPCR rhodopsin	Serotonin receptor 1A; G-21; ADRBRL1; ADRB2RL1; 5-hydroxytryptamine receptor 1A; 5-HT1A receptor; 5-HT1A; 5-HT-1A	HTR1A	"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)."	.	.	MDVLSPGQGNNTTSPPAPFETGGNTTGISDVTVSYQVITSLLLGTLIFCAVLGNACVVAAIALERSLQNVANYLIGSLAVTDLMVSVLVLPMAALYQVLNKWTLGQVTCDLFIALDVLCCTSSILHLCAIALDRYWAITDPIDYVNKRTPRRAAALISLTWLIGFLISIPPMLGWRTPEDRSDPDACTISKDHGYTIYSTFGAFYIPLLLMLVLYGRIFRAARFRIRKTVKKVEKTGADTRHGASPAPQPKKSVNGESGSRNWRLGVESKAGGALCANGAVRQGDDGAALEVIEVHRVGNSKEHLPLPSEAGPTPCAPASFERKNERNAEAKRKMALARERKTVKTLGIIMGTFILCWLPFFIVALVLPFCESSCHMPTLLGAIINWLGYSNSLLNPVIYAYFNKDFQNAFKKIIKCKFCRQ	Successful	Interactions between corticotropin-releasing hormone and serotonin: implications for the aetiology and treatment of anxiety disorders. Handb Exp Pharmacol. 2005;(169):181-204.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family. 5-hydroxytryptamine receptor subfamily. HTR1A sub-subfamily.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse	R-HSA-390666:Serotonin receptors; R-HSA-418594:G alpha (i) signalling events	.	P08908
TTK8CXU	5-HT 1B receptor (HTR1B)	P28222	5HT1B_HUMAN	GPCR rhodopsin	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	HTR1B	"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)."	.	6G79; 5V54; 4IAR; 4IAQ; 2G1X	MEEPGAQCAPPPPAGSETWVPQANLSSAPSQNCSAKDYIYQDSISLPWKVLLVMLLALITLATTLSNAFVIATVYRTRKLHTPANYLIASLAVTDLLVSILVMPISTMYTVTGRWTLGQVVCDFWLSSDITCCTASILHLCVIALDRYWAITDAVEYSAKRTPKRAAVMIALVWVFSISISLPPFFWRQAKAEEEVSECVVNTDHILYTVYSTVGAFYFPTLLLIALYGRIYVEARSRILKQTPNRTGKRLTRAQLITDSPGSTSSVTSINSRVPDVPSESGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGIILGAFIVCWLPFFIISLVMPICKDACWFHLAIFDFFTWLGYLNSLINPIIYTMSNEDFKQAFHKLIRFKCTS	Successful	Triptans in pregnancy. Ther Drug Monit. 2008 Feb;30(1):5-9.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.3.6	The G-protein-coupled receptor (GPCR) Family	hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse	R-HSA-390666:Serotonin receptors; R-HSA-418594:G alpha (i) signalling events	.	P28222
TT6MSOK	5-HT 1D receptor (HTR1D)	P28221	5HT1D_HUMAN	GPCR rhodopsin	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	HTR1D	"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)."	.	.	MSPLNQSAEGLPQEASNRSLNATETSEAWDPRTLQALKISLAVVLSVITLATVLSNAFVLTTILLTRKLHTPANYLIGSLATTDLLVSILVMPISIAYTITHTWNFGQILCDIWLSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGHAATMIAIVWAISICISIPPLFWRQAKAQEEMSDCLVNTSQISYTIYSTCGAFYIPSVLLIILYGRIYRAARNRILNPPSLYGKRFTTAHLITGSAGSSLCSLNSSLHEGHSHSAGSPLFFNHVKIKLADSALERKRISAARERKATKILGIILGAFIICWLPFFVVSLVLPICRDSCWIHPALFDFFTWLGYLNSLINPIIYTVFNEEFRQAFQKIVPFRKAS	Successful	Irritable bowel syndrome: new agents targeting serotonin receptor subtypes. Drugs. 2001;61(3):317-32.	34	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse	R-HSA-390666:Serotonin receptors; R-HSA-418594:G alpha (i) signalling events	.	P28221
TTCPG9S	5-HT 1E receptor (HTR1E)	P28566	5HT1E_HUMAN	GPCR rhodopsin	Serotonin receptor 1E; S31; 5-hydroxytryptamine receptor 1E; 5-HT1E; 5-HT-1E; 5-HT 1E	HTR1E	"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)."	.	.	MNITNCTTEASMAIRPKTITEKMLICMTLVVITTLTTLLNLAVIMAIGTTKKLHQPANYLICSLAVTDLLVAVLVMPLSIIYIVMDRWKLGYFLCEVWLSVDMTCCTCSILHLCVIALDRYWAITNAIEYARKRTAKRAALMILTVWTISIFISMPPLFWRSHRRLSPPPSQCTIQHDHVIYTIYSTLGAFYIPLTLILILYYRIYHAAKSLYQKRGSSRHLSNRSTDSQNSFASCKLTQTFCVSDFSTSDPTTEFEKFHASIRIPPFDNDLDHPGERQQISSTRERKAARILGLILGAFILSWLPFFIKELIVGLSIYTVSSEVADFLTWLGYVNSLINPLLYTSFNEDFKLAFKKLIRCREHT	Successful	Molecular cloning and pharmacological characterization of the guinea pig 5-HT1E receptor. Eur J Pharmacol. 2004 Jan 26;484(2-3):127-39.	34	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse	R-HSA-390666:Serotonin receptors; R-HSA-418594:G alpha (i) signalling events	.	P28566
TT0MI3F	5-HT 1F receptor (HTR1F)	P30939	5HT1F_HUMAN	GPCR rhodopsin	Serotonin receptor 1F; HTR1EL; 5-hydroxytryptamine receptor 1F; 5-HT1F receptor; 5-HT1F; 5-HT-1F	HTR1F	"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)."	.	.	MDFLNSSDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVVCDIWLSVDITCCTCSILHLSAIALDRYRAITDAVEYARKRTPKHAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLALILILYYKIYRAAKTLYHKRQASRIAKEEVNGQVLLESGEKSTKSVSTSYVLEKSLSDPSTDFDKIHSTVRSLRSEFKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCDKCKISEEMSNFLAWLGYLNSLINPLIYTIFNEDFKKAFQKLVRCRC	Successful	Cloning and characterization of the guinea pig 5-HT1F receptor subtype: a comparison of the pharmacological profile to the human species homolog. Neuropharmacology. 1997 Apr-May;36(4-5):569-76.	34	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse	R-HSA-390666:Serotonin receptors; R-HSA-418594:G alpha (i) signalling events	.	P30939
TTJQOD7	5-HT 2A receptor (HTR2A)	P28223	5HT2A_HUMAN	GPCR rhodopsin	Serotonin receptor 2A; HTR2; 5-hydroxytryptamine receptor 2A; 5-HT-2A; 5-HT-2	HTR2A	"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."	.	6A94; 6A93	MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV	Successful	"Beneficial effects of sarpogrelate hydrochloride, a 5-HT2A receptor antagonist, supplemented with pioglitazone on diabetic model mice. Endocr Res. 2009;34(1-2):18-30."	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04540:Gap junction; hsa04726:Serotonergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels	R-HSA-390666:Serotonin receptors; R-HSA-416476:G alpha (q) signalling events	.	P28223
TT0K1SC	5-HT 2B receptor (HTR2B)	P41595	5HT2B_HUMAN	GPCR rhodopsin	Serotonin receptor 2B; 5-hydroxytryptamine receptor 2B; 5-HT2B; 5-HT-2B; 5-HT 2B	HTR2B	"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)."	.	6DS0; 6DRZ; 6DRY; 6DRX; 5TVN	MALSYRVSELQSTIPEHILQSTFVHVISSNWSGLQTESIPEEMKQIVEEQGNKLHWAALLILMVIIPTIGGNTLVILAVSLEKKLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEAMWPLPLVLCPAWLFLDVLFSTASIMHLCAISVDRYIAIKKPIQANQYNSRATAFIKITVVWLISIGIAIPVPIKGIETDVDNPNNITCVLTKERFGDFMLFGSLAAFFTPLAIMIVTYFLTIHALQKKAYLVKNKPPQRLTWLTVSTVFQRDETPCSSPEKVAMLDGSRKDKALPNSGDETLMRRTSTIGKKSVQTISNEQRASKVLGIVFFLFLLMWCPFFITNITLVLCDSCNQTTLQMLLEIFVWIGYVSSGVNPLVYTLFNKTFRDAFGRYITCNYRATKSVKTLRKRSSKIYFRNPMAENSKFFKKHGIRNGINPAMYQSPMRLRSSTIQSSSIILLDTLLLTENEGDKTEEQVSYV	Successful	Some properties of 5-hydroxytryptamine receptors in the hindquarters of the rat. Br J Pharmacol. 1979 Sep;67(1):79-85.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.3.7	The G-protein-coupled receptor (GPCR) Family	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04540:Gap junction; hsa04726:Serotonergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels	R-HSA-390666:Serotonin receptors; R-HSA-416476:G alpha (q) signalling events	.	P41595
TTWJBZ5	5-HT 2C receptor (HTR2C)	P28335	5HT2C_HUMAN	GPCR rhodopsin	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	HTR2C	"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)."	.	6BQH; 6BQG	MVNLRNAVHSFLVHLIGLLVWQCDISVSPVAAIVTDIFNTSDGGRFKFPDGVQNWPALSIVIIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDEEKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYCLTIYVLRRQALMLLHGHTEEPPGLSLDFLKCCKRNTAEEENSANPNQDQNARRRKKKERRPRGTMQAINNERKASKVLGIVFFVFLIMWCPFFITNILSVLCEKSCNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSNYLRCNYKVEKKPPVRQIPRVAATALSGRELNVNIYRHTNEPVIEKASDNEPGIEMQVENLELPVNPSSVVSERISSV	Successful	Spinal serotonin receptor activation modulates the exercise ventilatory response with increased dead space in goats. Respir Physiol Neurobiol. 2008 May 31;161(3):230-8.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04540:Gap junction; hsa04726:Serotonergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels	R-HSA-390666:Serotonin receptors; R-HSA-416476:G alpha (q) signalling events	.	P28335
TTPC4TU	5-HT 3A receptor (HTR3A)	P46098	5HT3A_HUMAN	GPCR rhodopsin	Serotonin-gated ion channel receptor; Serotonin receptor 3A; HTR3; 5HT3R; 5-hydroxytryptamine receptor 3A; 5-HT3RA; 5-HT3A; 5-HT3-A; 5-HT 3A	HTR3A	"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."	.	.	MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA	Successful	Local anesthetics have different mechanisms and sites of action at recombinant 5-HT3 receptors. Reg Anesth Pain Med. 2007 Nov-Dec;32(6):462-70.	34	PF00001	.	ligand-gated ion channel (TC 1.A.9) family. 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily. HTR3A sub-subfamily. 	.	.	Neurotransmitter-gated ion-channel ligand binding domain; Neurotransmitter-gated ion-channel transmembrane region	PF02931; PF02932	PF02931; Neur_chan_LBD; PF02932; Neur_chan_memb	1.A.9.2.1	"The Neurotransmitter Receptor, Cys loop, Ligand-gated Ion Channel (LIC) Family"	hsa04726:Serotonergic synapse	R-HSA-975298:Ligand-gated ion channel transport	.	P46098
TTR6K75	5-HT 3B receptor (HTR3B)	O95264	5HT3B_HUMAN	GPCR rhodopsin	Serotonin receptor 3B; 5-hydroxytryptamine receptor 3B; 5-HT3B; 5-HT3-B; 5-HT-3B	HTR3B	"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."	.	.	MLSSVMAPLWACILVAAGILATDTHHPQDSALYHLSKQLLQKYHKEVRPVYNWTKATTVYLDLFVHAILDVDAENQILKTSVWYQEVWNDEFLSWNSSMFDEIREISLPLSAIWAPDIIINEFVDIERYPDLPYVYVNSSGTIENYKPIQVVSACSLETYAFPFDVQNCSLTFKSILHTVEDVDLAFLRSPEDIQHDKKAFLNDSEWELLSVSSTYSILQSSAGGFAQIQFNVVMRRHPLVYVVSLLIPSIFLMLVDLGSFYLPPNCRARIVFKTSVLVGYTVFRVNMSNQVPRSVGSTPLIGHFFTICMAFLVLSLAKSIVLVKFLHDEQRGGQEQPFLCLRGDTDADRPRVEPRAQRAVVTESSLYGEHLAQPGTLKEVWSQLQSISNYLQTQDQTDQQEAEWLVLLSRFDRLLFQSYLFMLGIYTITLCSLWALWGGV	Discontinued	"Zatosetron, a potent, selective, and long-acting 5HT3 receptor antagonist: synthesis and structure-activity relationships. J Med Chem. 1992 Jan 24;35(2):310-9."	9	PF00001	.	ligand-gated ion channel (TC 1.A.9) family. 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily. HTR3B sub-subfamily. 	.	.	Neurotransmitter-gated ion-channel ligand binding domain; Neurotransmitter-gated ion-channel transmembrane region	PF02931; PF02932	PF02931; Neur_chan_LBD; PF02932; Neur_chan_memb	.	.	hsa04726:Serotonergic synapse	R-HSA-975298:Ligand-gated ion channel transport	.	O95264
TT07C3Y	5-HT 4 receptor (HTR4)	Q13639	5HT4R_HUMAN	GPCR rhodopsin	Serotonin receptor 4; 5-hydroxytryptamine receptor 4; 5-HT4 receptor; 5-HT4; 5-HT-4	HTR4	"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."	.	5EM9	MDKLDANVSSEEGFGSVEKVVLLTFLSTVILMAILGNLLVMVAVCWDRQLRKIKTNYFIVSLAFADLLVSVLVMPFGAIELVQDIWIYGEVFCLVRTSLDVLLTTASIFHLCCISLDRYYAICCQPLVYRNKMTPLRIALMLGGCWVIPTFISFLPIMQGWNNIGIIDLIEKRKFNQNSNSTYCVFMVNKPYAITCSVVAFYIPFLLMVLAYYRIYVTAKEHAHQIQMLQRAGASSESRPQSADQHSTHRMRTETKAAKTLCIIMGCFCLCWAPFFVTNIVDPFIDYTVPGQVWTAFLWLGYINSGLNPFLYAFLNKSFRRAFLIILCCDDERYRRPSILGQTVPCSTTTINGSTHVLRDAVECGGQWESQCHPPATSPLVAAQPSDT	Successful	Metoclopramide stimulates catecholamine- and granin-derived peptide secretion from pheochromocytoma cells through activation of serotonin type 4 (5... Endocr Relat Cancer. 2009 Mar;16(1):281-90.	34	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse	R-HSA-390666:Serotonin receptors; R-HSA-418555:G alpha (s) signalling events	.	Q13639
TTRUFDT	5-HT 5A receptor (HTR5A)	P47898	5HT5A_HUMAN	GPCR rhodopsin	Serotonin receptor 5A; 5-hydroxytryptamine receptor 5A; 5-HT5A; 5-HT-5A; 5-HT-5; 5-HT 5A	HTR5A	"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."	.	.	MDLPVNLTSFSLSTPSPLETNHSLGKDDLRPSSPLLSVFGVLILTLLGFLVAATFAWNLLVLATILRVRTFHRVPHNLVASMAVSDVLVAALVMPLSLVHELSGRRWQLGRRLCQLWIACDVLCCTASIWNVTAIALDRYWSITRHMEYTLRTRKCVSNVMIALTWALSAVISLAPLLFGWGETYSEGSEECQVSREPSYAVFSTVGAFYLPLCVVLFVYWKIYKAAKFRVGSRKTNSVSPISEAVEVKDSAKQPQMVFTVRHATVTFQPEGDTWREQKEQRAALMVGILIGVFVLCWIPFFLTELISPLCSCDIPAIWKSIFLWLGYSNSFFNPLIYTAFNKNYNSAFKNFFSRQH	Successful	Cloning and characterisation of the human 5-HT5A serotonin receptor. FEBS Lett. 1994 Dec 5;355(3):242-6.	34	PF00001	.	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse	R-HSA-390666:Serotonin receptors; R-HSA-418594:G alpha (i) signalling events	.	P47898
TT9KJ1X	5-HT 5B receptor (HTR5B)	Q9P2D3	HTR5B_HUMAN	GPCR rhodopsin	KIAA1414; HEATR5B; HEAT repeat-containing protein 5B	HTR5B	"endocytic vesicle, membrane, endocytosis, protein localization, retrograde transport, endosome to Golgi."	.	.	MELAHSLLLNEEALAQITEAKRPVFIFEWLRFLDKVLVAANKTDVKEKQKKLVEQLTGLISSSPGPPTRKLLAKNLAALYSIGDTFTVFQTLDKCNDIIRNKDDTAAYLPTKLAAVACVGAFYEKMGRMLGSAFPETVNNLLKSLKSAESQGRSEILMSLQKVLSGLGGAAASSHRDIYKNARSLLTDRSMAVRCAVAKCLLELQNEAVFMWTAELENIATLCFKALENSNYGVRVAVSKLLGTVMATALMPKQATVMRQNVKRATFDEVLELMATGFLRGGSGFLKSGGEMLKVGGSVNREVRVGVTQAYVVFVTTLGGQWLERSFATFLSHVLDLVSHPRATQTHVEAVYSRRCVSFILRATVGSLLGEKAQIAAAKEICQAIGKQMKAVEAVVNDTSGENKSGAADIAASQHVMVCALQELGSLVQSLNATASPLIQEASIGLLEIVTSVLLHPSMAARLAAAWCLRCVAVALPFQLTPFLDRCAERLNNLKTSPEAVSGYSFAMAALLGGVHQCPLGIPHAKGKMVVSIAEDLLRTAAQNSRLSLQRTQAGWLLLGALMTLGPSVVRYHLPKMLLLWRNVFPRSLKELEAEKARGDSFTWQVTLEGRAGALCAMRSFVAHCPELLTEDVIRKLMTPIECAMTMMSHIPSVMKAHGAHLKASAAMVRLRLYDILALLPPKTYEGSFNALLRELVAEFTLTDNSANTTTSLLRSLCHYDDSVLLGSWLQETDHKSIEDQLQPNSASGSGALEHDPSSIYLRIPAGEAVPGPLPLGVSVIDASVALFGVVFPHVSYKHRLQMLDHFAECVKQAKGVRQQAVQLNIFTAVLSALKGLAENKSTLGPEEVRKSALTLVMGPLDNPNPILRCAAGEALGRMAQVVGEATFIARMAQYSFDKLKSARDVVSRTGHSLALGCLHRYVGGIGSGQHLKTSVSILLALAQDGTSPEVQTWSLHSLALIVDSSGPMYRGYVEPTLSLVLTLLLTVPPSHTEVHQCLGRCLGAIITTVGPELQGNGATTSTIRSSCLVGCAITQDHSDSLVQAAAISCLQQLHMFAPRHVNLSSLVPSLCVHLCSSHLLLRRAAVACLRQLAQREAAEVCEYAMSLAKNTGDKESSSANVSPFAPGVSSRTDIHCRHQGVNITETGLEGLLFGMLDRETDRKLCSDIHDTLGHMLSSLAVEKLSHWLMLCKDVLAASSDMSTATLLSSGKDEEAEKKDEMDDDTMFTTLGEEDKSKPFVAPRWATRVFAADCLCRIINLCENADQAHFDLALARSAKLRNPTNDLLVLHLSDLIRMAFMAATDHSNQLRMAGLQALEDIIKKFASVPEPEFPGHVILEQYQANVGAALRPAFSQDTPSDIIAKACQVCSTWIGSGVVSDLNDLRRVHNLLVSSLDKVQAGKGSSSQLYRESATTMEKLAVLKAWAEVYVVAMNIKKEAESKPKRAIKNTDDDDDDCGTIDELPPDSLITLVQPELPTLSRLWLAALKDYALLTLPAEFSSQLPPDGGAFYTPETIDTARLHYRNSWAPILHAVALWLNSTGFTCSESTEAAAISGLQKRSTSVNLNQASGAVGSAKSLPEINKDRMHLILGVSIQFLCSPRPEEPIEHVTACLQALHTLLDSPYARVHIAEDQLIGVELLSVLHRLLLTWNPSSVQLLVTGVVQQIVRAAQDYLQEKRNTLNEDDMEKEACTVLGEGGDSGGLIPGKSLVFATMELLMFILVRHMPHLSTKVSDSPSHIATKTRLSEESARLVAATVTILSDLPSLCSPAGCMTILPTILFLIARILKDTAIKSADNQVPPPVSAALQGIKSIVTLSMAKTEAGVQKQWTALIRSTLACILEYSQPEDSVPTPDEVSMLTAIALFLWSASNEIIGVQSLQNGCMNRFKNALNSCDPWVQAKCYQLLLSVFQHSNRALSTPYIHSLAPIVVEKLKAVERNRPASNIELLAVQEGIKVLETLVALGEEQNRVQLLALLVPTLISYLLDENSFASASSASKDLHEFALQNLMHIGPLYPHAFKTVMGAAPELKVRLETAVRASQASKAKAAARQPAPAIHSAPTIKLKTSFF	Literature-reported	Putative 5-ht5 receptors: localization in the mouse CNS and lack of effect in the inhibition of dural protein extravasation. Ann N Y Acad Sci. 1998 Dec 15;861:85-90.	0	PF00001	.	HEATR5 family.	.	.	.	.	.	.	.	.	.	.	Q9P2D3
TTJS8PY	5-HT 6 receptor (HTR6)	P50406	5HT6R_HUMAN	GPCR rhodopsin	Serotonin receptor 6; 5-hydroxytryptamine receptor 6; 5-HT6 receptor; 5-HT6; 5-HT-6	HTR6	"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."	.	.	MVPEPGPTANSTPAWGAGPPSAPGGSGWVAAALCVVIALTAAANSLLIALICTQPALRNTSNFFLVSLFTSDLMVGLVVMPPAMLNALYGRWVLARGLCLLWTAFDVMCCSASILNLCLISLDRYLLILSPLRYKLRMTPLRALALVLGAWSLAALASFLPLLLGWHELGHARPPVPGQCRLLASLPFVLVASGLTFFLPSGAICFTYCRILLAARKQAVQVASLTTGMASQASETLQVPRTPRPGVESADSRRLATKHSRKALKASLTLGILLGMFFVTWLPFFVANIVQAVCDCISPGLFDVLTWLGYCNSTMNPIIYPLFMRDFKRALGRFLPCPRCPRERQASLASPSLRTSHSGPRPGLSLQQVLPLPLPPDSDSDSDAGSGGSSGLRLTAQLLLPGEATQDPPLPTRAAAAVNFFNIDPAEPELRPHPLGIPTN	Clinical trial	The 5-hydroxytryptamine6 receptor-selective radioligand [3H]Ro 63-0563 labels 5-hydroxytryptamine receptor binding sites in rat and porcine striatum. Mol Pharmacol. 1998 Sep;54(3):577-83.	25	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04020:Calcium signaling pathway; hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse	R-HSA-390666:Serotonin receptors; R-HSA-418555:G alpha (s) signalling events	.	P50406
TTO9X1H	5-HT 7 receptor (HTR7)	P34969	5HT7R_HUMAN	GPCR rhodopsin	Serotonin receptor 7; 5HT7; 5-hydroxytryptamine receptor 7; 5-HT7 receptor; 5-HT7; 5-HT-X; 5-HT-7	HTR7	"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."	.	.	MMDVNSSGRPDLYGHLRSFLLPEVGRGLPDLSPDGGADPVAGSWAPHLLSEVTASPAPTWDAPPDNASGCGEQINYGRVEKVVIGSILTLITLLTIAGNCLVVISVCFVKKLRQPSNYLIVSLALADLSVAVAVMPFVSVTDLIGGKWIFGHFFCNVFIAMDVMCCTASIMTLCVISIDRYLGITRPLTYPVRQNGKCMAKMILSVWLLSASITLPPLFGWAQNVNDDKVCLISQDFGYTIYSTAVAFYIPMSVMLFMYYQIYKAARKSAAKHKFPGFPRVEPDSVIALNGIVKLQKEVEECANLSRLLKHERKNISIFKREQKAATTLGIIVGAFTVCWLPFFLLSTARPFICGTSCSCIPLWVERTFLWLGYANSLINPFIYAFFNRDLRTTYRSLLQCQYRNINRKLSAAGMHEALKLAERPERPEFVLRACTRRVLLRPEKRPPVSVWVLQSPDHHNWLADKMLTTVEKKVMIHD	Clinical trial	Cloning of a novel human serotonin receptor (5-HT7) positively linked to adenylate cyclase. J Biol Chem. 1993 Nov 5;268(31):23422-6.	21	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04014:Ras signaling pathway; hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04726:Serotonergic synapse	R-HSA-390666:Serotonin receptors; R-HSA-418555:G alpha (s) signalling events	.	P34969
TT8POQR	Serine protease HTRA1 (HTRA1)	Q92743	HTRA1_HUMAN	Peptidase	Serine protease 11; L56; High-temperature requirement A serine peptidase 1; HTRA1	HTRA1	"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."	EC 3.4.21.-	3TJQ; 3TJO; 3TJN; 3NZI; 3NWU	MQIPRAALLPLLLLLLAAPASAQLSRAGRSAPLAAGCPDRCEPARCPPQPEHCEGGRARDACGCCEVCGAPEGAACGLQEGPCGEGLQCVVPFGVPASATVRRRAQAGLCVCASSEPVCGSDANTYANLCQLRAASRRSERLHRPPVIVLQRGACGQGQEDPNSLRHKYNFIADVVEKIAPAVVHIELFRKLPFSKREVPVASGSGFIVSEDGLIVTNAHVVTNKHRVKVELKNGATYEAKIKDVDEKADIALIKIDHQGKLPVLLLGRSSELRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTAGISFAIPSDKIKKFLTESHDRQAKGKAITKKKYIGIRMMSLTSSKAKELKDRHRDFPDVISGAYIIEVIPDTPAEAGGLKENDVIISINGQSVVSANDVSDVIKRESTLNMVVRRGNEDIMITVIPEEIDP	Literature-reported	HtrA serine proteases as potential therapeutic targets in cancer. Curr Cancer Drug Targets. 2009 Jun;9(4):451-68.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1474228: Degradation of the extracellular matrix	.	Q92743
TTIWZ0O	Huntingtin messenger RNA (HTT mRNA)	P42858	HD_HUMAN	mRNA target	IT15 (mRNA); Huntington disease protein (mRNA); Huntingtin (mRNA); HD protein (mRNA); HD (mRNA)	HTT	May play a role in microtubule-mediated transport or vesicle function.	.	6N8C; 6EZ8; 4RAV; 4FED; 4FEC	MATLEKLMKAFESLKSFQQQQQQQQQQQQQQQQQQQQQPPPPPPPPPPPQLPQPPPQAQPLLPQPQPPPPPPPPPPGPAVAEEPLHRPKKELSATKKDRVNHCLTICENIVAQSVRNSPEFQKLLGIAMELFLLCSDDAESDVRMVADECLNKVIKALMDSNLPRLQLELYKEIKKNGAPRSLRAALWRFAELAHLVRPQKCRPYLVNLLPCLTRTSKRPEESVQETLAAAVPKIMASFGNFANDNEIKVLLKAFIANLKSSSPTIRRTAAGSAVSICQHSRRTQYFYSWLLNVLLGLLVPVEDEHSTLLILGVLLTLRYLVPLLQQQVKDTSLKGSFGVTRKEMEVSPSAEQLVQVYELTLHHTQHQDHNVVTGALELLQQLFRTPPPELLQTLTAVGGIGQLTAAKEESGGRSRSGSIVELIAGGGSSCSPVLSRKQKGKVLLGEEEALEDDSESRSDVSSSALTASVKDEISGELAASSGVSTPGSAGHDIITEQPRSQHTLQADSVDLASCDLTSSATDGDEEDILSHSSSQVSAVPSDPAMDLNDGTQASSPISDSSQTTTEGPDSAVTPSDSSEIVLDGTDNQYLGLQIGQPQDEDEEATGILPDEASEAFRNSSMALQQAHLLKNMSHCRQPSDSSVDKFVLRDEATEPGDQENKPCRIKGDIGQSTDDDSAPLVHCVRLLSASFLLTGGKNVLVPDRDVRVSVKALALSCVGAAVALHPESFFSKLYKVPLDTTEYPEEQYVSDILNYIDHGDPQVRGATAILCGTLICSILSRSRFHVGDWMGTIRTLTGNTFSLADCIPLLRKTLKDESSVTCKLACTAVRNCVMSLCSSSYSELGLQLIIDVLTLRNSSYWLVRTELLETLAEIDFRLVSFLEAKAENLHRGAHHYTGLLKLQERVLNNVVIHLLGDEDPRVRHVAAASLIRLVPKLFYKCDQGQADPVVAVARDQSSVYLKLLMHETQPPSHFSVSTITRIYRGYNLLPSITDVTMENNLSRVIAAVSHELITSTTRALTFGCCEALCLLSTAFPVCIWSLGWHCGVPPLSASDESRKSCTVGMATMILTLLSSAWFPLDLSAHQDALILAGNLLAASAPKSLRSSWASEEEANPAATKQEEVWPALGDRALVPMVEQLFSHLLKVINICAHVLDDVAPGPAIKAALPSLTNPPSLSPIRRKGKEKEPGEQASVPLSPKKGSEASAASRQSDTSGPVTTSKSSSLGSFYHLPSYLKLHDVLKATHANYKVTLDLQNSTEKFGGFLRSALDVLSQILELATLQDIGKCVEEILGYLKSCFSREPMMATVCVQQLLKTLFGTNLASQFDGLSSNPSKSQGRAQRLGSSSVRPGLYHYCFMAPYTHFTQALADASLRNMVQAEQENDTSGWFDVLQKVSTQLKTNLTSVTKNRADKNAIHNHIRLFEPLVIKALKQYTTTTCVQLQKQVLDLLAQLVQLRVNYCLLDSDQVFIGFVLKQFEYIEVGQFRESEAIIPNIFFFLVLLSYERYHSKQIIGIPKIIQLCDGIMASGRKAVTHAIPALQPIVHDLFVLRGTNKADAGKELETQKEVVVSMLLRLIQYHQVLEMFILVLQQCHKENEDKWKRLSRQIADIILPMLAKQQMHIDSHEALGVLNTLFEILAPSSLRPVDMLLRSMFVTPNTMASVSTVQLWISGILAILRVLISQSTEDIVLSRIQELSFSPYLISCTVINRLRDGDSTSTLEEHSEGKQIKNLPEETFSRFLLQLVGILLEDIVTKQLKVEMSEQQHTFYCQELGTLLMCLIHIFKSGMFRRITAAATRLFRSDGCGGSFYTLDSLNLRARSMITTHPALVLLWCQILLLVNHTDYRWWAEVQQTPKRHSLSSTKLLSPQMSGEEEDSDLAAKLGMCNREIVRRGALILFCDYVCQNLHDSEHLTWLIVNHIQDLISLSHEPPVQDFISAVHRNSAASGLFIQAIQSRCENLSTPTMLKKTLQCLEGIHLSQSGAVLTLYVDRLLCTPFRVLARMVDILACRRVEMLLAANLQSSMAQLPMEELNRIQEYLQSSGLAQRHQRLYSLLDRFRLSTMQDSLSPSPPVSSHPLDGDGHVSLETVSPDKDWYVHLVKSQCWTRSDSALLEGAELVNRIPAEDMNAFMMNSEFNLSLLAPCLSLGMSEISGGQKSALFEAAREVTLARVSGTVQQLPAVHHVFQPELPAEPAAYWSKLNDLFGDAALYQSLPTLARALAQYLVVVSKLPSHLHLPPEKEKDIVKFVVATLEALSWHLIHEQIPLSLDLQAGLDCCCLALQLPGLWSVVSSTEFVTHACSLIYCVHFILEAVAVQPGEQLLSPERRTNTPKAISEEEEEVDPNTQNPKYITAACEMVAEMVESLQSVLALGHKRNSGVPAFLTPLLRNIIISLARLPLVNSYTRVPPLVWKLGWSPKPGGDFGTAFPEIPVEFLQEKEVFKEFIYRINTLGWTSRTQFEETWATLLGVLVTQPLVMEQEESPPEEDTERTQINVLAVQAITSLVLSAMTVPVAGNPAVSCLEQQPRNKPLKALDTRFGRKLSIIRGIVEQEIQAMVSKRENIATHHLYQAWDPVPSLSPATTGALISHEKLLLQINPERELGSMSYKLGQVSIHSVWLGNSITPLREEEWDEEEEEEADAPAPSSPPTSPVNSRKHRAGVDIHSCSQFLLELYSRWILPSSSARRTPAILISEVVRSLLVVSDLFTERNQFELMYVTLTELRRVHPSEDEILAQYLVPATCKAAAVLGMDKAVAEPVSRLLESTLRSSHLPSRVGALHGVLYVLECDLLDDTAKQLIPVISDYLLSNLKGIAHCVNIHSQQHVLVMCATAFYLIENYPLDVGPEFSASIIQMCGVMLSGSEESTPSIIYHCALRGLERLLLSEQLSRLDAESLVKLSVDRVNVHSPHRAMAALGLMLTCMYTGKEKVSPGRTSDPNPAAPDSESVIVAMERVSVLFDRIRKGFPCEARVVARILPQFLDDFFPPQDIMNKVIGEFLSNQQPYPQFMATVVYKVFQTLHSTGQSSMVRDWVMLSLSNFTQRAPVAMATWSLSCFFVSASTSPWVAAILPHVISRMGKLEQVDVNLFCLVATDFYRHQIEEELDRRAFQSVLEVVAAPGSPYHRLLTCLRNVHKVTTC	Literature-reported	Design and development of antisense drugs. Expert Opin. Drug Discov. 2008 3(10):1189-1207.	2.1	mRNA	mRNA target	.	.	.	Huntingtin protein region 	PF12372	PF12372; DUF3652	.	.	hsa05016: Huntington disease; hsa05022: Pathways of neurodegeneration - multiple diseases	R-HSA-9022692: Regulation of MECP2 expression and activity	.	.
TTUKLBM	Huntingtin (HTT)	P42858	HD_HUMAN	.	IT15; Huntington disease protein; HD protein; HD	HTT	May play a role in microtubule-mediated transport or vesicle function.	.	6N8C; 6EZ8; 4RAV; 4FED; 4FEC	MATLEKLMKAFESLKSFQQQQQQQQQQQQQQQQQQQQQPPPPPPPPPPPQLPQPPPQAQPLLPQPQPPPPPPPPPPGPAVAEEPLHRPKKELSATKKDRVNHCLTICENIVAQSVRNSPEFQKLLGIAMELFLLCSDDAESDVRMVADECLNKVIKALMDSNLPRLQLELYKEIKKNGAPRSLRAALWRFAELAHLVRPQKCRPYLVNLLPCLTRTSKRPEESVQETLAAAVPKIMASFGNFANDNEIKVLLKAFIANLKSSSPTIRRTAAGSAVSICQHSRRTQYFYSWLLNVLLGLLVPVEDEHSTLLILGVLLTLRYLVPLLQQQVKDTSLKGSFGVTRKEMEVSPSAEQLVQVYELTLHHTQHQDHNVVTGALELLQQLFRTPPPELLQTLTAVGGIGQLTAAKEESGGRSRSGSIVELIAGGGSSCSPVLSRKQKGKVLLGEEEALEDDSESRSDVSSSALTASVKDEISGELAASSGVSTPGSAGHDIITEQPRSQHTLQADSVDLASCDLTSSATDGDEEDILSHSSSQVSAVPSDPAMDLNDGTQASSPISDSSQTTTEGPDSAVTPSDSSEIVLDGTDNQYLGLQIGQPQDEDEEATGILPDEASEAFRNSSMALQQAHLLKNMSHCRQPSDSSVDKFVLRDEATEPGDQENKPCRIKGDIGQSTDDDSAPLVHCVRLLSASFLLTGGKNVLVPDRDVRVSVKALALSCVGAAVALHPESFFSKLYKVPLDTTEYPEEQYVSDILNYIDHGDPQVRGATAILCGTLICSILSRSRFHVGDWMGTIRTLTGNTFSLADCIPLLRKTLKDESSVTCKLACTAVRNCVMSLCSSSYSELGLQLIIDVLTLRNSSYWLVRTELLETLAEIDFRLVSFLEAKAENLHRGAHHYTGLLKLQERVLNNVVIHLLGDEDPRVRHVAAASLIRLVPKLFYKCDQGQADPVVAVARDQSSVYLKLLMHETQPPSHFSVSTITRIYRGYNLLPSITDVTMENNLSRVIAAVSHELITSTTRALTFGCCEALCLLSTAFPVCIWSLGWHCGVPPLSASDESRKSCTVGMATMILTLLSSAWFPLDLSAHQDALILAGNLLAASAPKSLRSSWASEEEANPAATKQEEVWPALGDRALVPMVEQLFSHLLKVINICAHVLDDVAPGPAIKAALPSLTNPPSLSPIRRKGKEKEPGEQASVPLSPKKGSEASAASRQSDTSGPVTTSKSSSLGSFYHLPSYLKLHDVLKATHANYKVTLDLQNSTEKFGGFLRSALDVLSQILELATLQDIGKCVEEILGYLKSCFSREPMMATVCVQQLLKTLFGTNLASQFDGLSSNPSKSQGRAQRLGSSSVRPGLYHYCFMAPYTHFTQALADASLRNMVQAEQENDTSGWFDVLQKVSTQLKTNLTSVTKNRADKNAIHNHIRLFEPLVIKALKQYTTTTCVQLQKQVLDLLAQLVQLRVNYCLLDSDQVFIGFVLKQFEYIEVGQFRESEAIIPNIFFFLVLLSYERYHSKQIIGIPKIIQLCDGIMASGRKAVTHAIPALQPIVHDLFVLRGTNKADAGKELETQKEVVVSMLLRLIQYHQVLEMFILVLQQCHKENEDKWKRLSRQIADIILPMLAKQQMHIDSHEALGVLNTLFEILAPSSLRPVDMLLRSMFVTPNTMASVSTVQLWISGILAILRVLISQSTEDIVLSRIQELSFSPYLISCTVINRLRDGDSTSTLEEHSEGKQIKNLPEETFSRFLLQLVGILLEDIVTKQLKVEMSEQQHTFYCQELGTLLMCLIHIFKSGMFRRITAAATRLFRSDGCGGSFYTLDSLNLRARSMITTHPALVLLWCQILLLVNHTDYRWWAEVQQTPKRHSLSSTKLLSPQMSGEEEDSDLAAKLGMCNREIVRRGALILFCDYVCQNLHDSEHLTWLIVNHIQDLISLSHEPPVQDFISAVHRNSAASGLFIQAIQSRCENLSTPTMLKKTLQCLEGIHLSQSGAVLTLYVDRLLCTPFRVLARMVDILACRRVEMLLAANLQSSMAQLPMEELNRIQEYLQSSGLAQRHQRLYSLLDRFRLSTMQDSLSPSPPVSSHPLDGDGHVSLETVSPDKDWYVHLVKSQCWTRSDSALLEGAELVNRIPAEDMNAFMMNSEFNLSLLAPCLSLGMSEISGGQKSALFEAAREVTLARVSGTVQQLPAVHHVFQPELPAEPAAYWSKLNDLFGDAALYQSLPTLARALAQYLVVVSKLPSHLHLPPEKEKDIVKFVVATLEALSWHLIHEQIPLSLDLQAGLDCCCLALQLPGLWSVVSSTEFVTHACSLIYCVHFILEAVAVQPGEQLLSPERRTNTPKAISEEEEEVDPNTQNPKYITAACEMVAEMVESLQSVLALGHKRNSGVPAFLTPLLRNIIISLARLPLVNSYTRVPPLVWKLGWSPKPGGDFGTAFPEIPVEFLQEKEVFKEFIYRINTLGWTSRTQFEETWATLLGVLVTQPLVMEQEESPPEEDTERTQINVLAVQAITSLVLSAMTVPVAGNPAVSCLEQQPRNKPLKALDTRFGRKLSIIRGIVEQEIQAMVSKRENIATHHLYQAWDPVPSLSPATTGALISHEKLLLQINPERELGSMSYKLGQVSIHSVWLGNSITPLREEEWDEEEEEEADAPAPSSPPTSPVNSRKHRAGVDIHSCSQFLLELYSRWILPSSSARRTPAILISEVVRSLLVVSDLFTERNQFELMYVTLTELRRVHPSEDEILAQYLVPATCKAAAVLGMDKAVAEPVSRLLESTLRSSHLPSRVGALHGVLYVLECDLLDDTAKQLIPVISDYLLSNLKGIAHCVNIHSQQHVLVMCATAFYLIENYPLDVGPEFSASIIQMCGVMLSGSEESTPSIIYHCALRGLERLLLSEQLSRLDAESLVKLSVDRVNVHSPHRAMAALGLMLTCMYTGKEKVSPGRTSDPNPAAPDSESVIVAMERVSVLFDRIRKGFPCEARVVARILPQFLDDFFPPQDIMNKVIGEFLSNQQPYPQFMATVVYKVFQTLHSTGQSSMVRDWVMLSLSNFTQRAPVAMATWSLSCFFVSASTSPWVAAILPHVISRMGKLEQVDVNLFCLVATDFYRHQIEEELDRRAFQSVLEVVAAPGSPYHRLLTCLRNVHKVTTC	Literature-reported	Huntingtin is a scaffolding protein in the ATM oxidative DNA damage response complex. Hum Mol Genet. 2017 Jan 15;26(2):395-406.	.	.	.	huntingtin family.	.	.	Huntingtin protein region 	PF12372	PF12372; DUF3652	.	.	hsa05016: Huntington disease; hsa05022: Pathways of neurodegeneration - multiple diseases	R-HSA-9022692: Regulation of MECP2 expression and activity	.	.
TTU6FJG	Trichoderma L-Lysine alpha-oxidase (HYPRU LysOX)	A0A0G4DCU0	A0A0G4DCU0_HYPRU	.	L-Lysine alpha-oxidase	HYPRU LysOX	"An antitumor enzyme of Trichoderma harzianum. Inhibit highly infectious viruses INSV and TRSV, Mycoplasma hominis, and tick-borne encephalitis virus."	.	.	MDNVDFAESVRTRWARRLIREKVAKELNILTERLGEVPGIPPPREGRFLGGGYSHDNLPSDPLYSSIKPALLKEAPRAEEELPPRKVCIVGAGVSGLYIAMILDDLKIPNLTYDIFESSSRTGGRLYTHHFTDAKHDYYDIGAMRYPDIPSMKRTFNLFKRTGMPLIKYYLDGENTPQLYNNHFFAKGVVDPYMVSVANGGTVPDDVVDSVGEKLQQAFGYYKEKLAEDFDKGFDELMLVDDMTTREYLKRGGPKGEAPKYDFFAIQWMETQNTGTNLFDQAFSESVIDSFDFDNPTKPEWYCIEGGTSLLVDAMKETLVHKVQNNKRVEAISIDLDAPDDGNMSVKIGGKDYSGYSTVFNTTALGCLDRMDLRGLNLHPTQADAIRCLHYDNSTKVALKFSYPWWIKDCGITCGGAASTDLPLRTCVYPSYNLGDTGEAVLLASYTWSQDATRIGSLVKDAPPQPPKEDELVELILQNLARLHAEHMTYEKIKEAYTGVYHAYCWANDPNVGGAFALFGPGQFSNLYPYLMRPAAGGKFHIVGEASSVHHAWIIGSLESAYTAVYQFLYKYKMWDYLRLLLERWQYGLQELETGKHGTAHLQFILGSLPKEYQVKI	Literature-reported	Antibacterial Activity of L-Lysine--Oxidase from the Trichoderma. Bull Exp Biol Med. 2017 Oct;163(6):777-779.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHN8EM	Islet amyloid polypeptide (IAPP)	P10997	IAPP_HUMAN	.	Insulinoma amyloid peptide; IAPP; Diabetes-associated peptide; Amylin	IAPP	"Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism."	.	5MGQ; 5KO0; 5KNZ; 5K5G; 3HGZ	MGILKLQVFLIVLSVALNHLKATPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYGKRNAVEVLKREPLNYLPL	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04950: Maturity onset diabetes of the young	R-HSA-210745: Regulation of gene expression in beta cells; R-HSA-418555: G alpha (s) signalling events; R-HSA-419812: Calcitonin-like ligand receptors; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production; R-HSA-977225: Amyloid fiber formation	.	P10997
TTYD3AN	Isoleucyl-tRNA synthetase (IARS)	P41252	SYIC_HUMAN	Carbon-oxygen ligase	"Isoleucine--tRNA ligase, cytoplasmic; Isoleucine--tRNA ligase; IleRS; IRS"	IARS	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.	EC 6.1.1.5	.	MLQQVPENINFPAEEEKILEFWTEFNCFQECLKQSKHKPKFTFYDGPPFATGLPHYGHILAGTIKDIVTRYAHQSGFHVDRRFGWDCHGLPVEYEIDKTLGIRGPEDVAKMGITEYNNQCRAIVMRYSAEWKSTVSRLGRWIDFDNDYKTLYPQFMESVWWVFKQLYDKGLVYRGVKVMPFSTACNTPLSNFESHQNYKDVQDPSVFVTFPLEEDETVSLVAWTTTPWTLPSNLAVCVNPEMQYVKIKDVARGRLLILMEARLSALYKLESDYEILERFPGAYLKGKKYRPLFDYFLKCKENGAFTVLVDNYVKEEEGTGVVHQAPYFGAEDYRVCMDFNIIRKDSLPVCPVDASGCFTTEVTDFAGQYVKDADKSIIRTLKEQGRLLVATTFTHSYPFCWRSDTPLIYKAVPSWFVRVENMVDQLLRNNDLCYWVPELVREKRFGNWLKDARDWTISRNRYWGTPIPLWVSDDFEEVVCIGSVAELEELSGAKISDLHRESVDHLTIPSRCGKGSLHRISEVFDCWFESGSMPYAQVHYPFENKREFEDAFPADFIAEGIDQTRGWFYTLLVLATALFGQPPFKNVIVNGLVLASDGQKMSKRKKNYPDPVSIIQKYGADALRLYLINSPVVRAENLRFKEEGVRDVLKDVLLPWYNAYRFLIQNVLRLQKEEEIEFLYNENTVRESPNITDRWILSFMQSLIGFFETEMAAYRLYTVVPRLVKFVDILTNWYVRMNRRRLKGENGMEDCVMALETLFSVLLSLCRLMAPYTPFLTELMYQNLKVLIDPVSVQDKDTLSIHYLMLPRVREELIDKKTESAVSQMQSVIELGRVIRDRKTIPIKYPLKEIVVIHQDPEALKDIKSLEKYIIEELNVRKVTLSTDKNKYGIRLRAEPDHMVLGKRLKGAFKAVMTSIKQLSSEELEQFQKTGTIVVEGHELHDEDIRLMYTFDQATGGTAQFEAHSDAQALVLLDVTPDQSMVDEGMAREVINRIQKLRKKCNLVPTDEITVYYKAKSEGTYLNSVIESHTEFIFTTIKAPLKPYPVSPSDKVLIQEKTQLKGSELEITLTRGSSLPGPACAYVNLNICANGSEQGGVLLLENPKGDNRLDLLKLKSVVTSIFGVKNTELAVFHDETEIQNQTDLLSLSGKTLCVTAGSAPSLINSSSTLLCQYINLQLLNAKPQECLMGTVGTLLLENPLGQNGLTHQGLLYEAAKVFGLRSRKLKLFLNETQTQEITEDIPVKTLNMKTVYVSVLPTTADF	Literature-reported	Synthesis and biological activities of reveromycin A and spirofungin A derivatives. Bioorg Med Chem Lett. 2008 Jul 1;18(13):3756-60.	2	EC:6.1	Carbon-oxygen ligase	class-I aminoacyl-tRNA synthetase family.	6.1.1.5 	Forming carbon-oxygen bonds	"Anticodon-binding domain of tRNA; tRNA synthetases class I (I, L, M and V)"	PF08264; PF00133	PF08264; Anticodon_1; PF00133; tRNA-synt_1	.	.	hsa00970:Aminoacyl-tRNA biosynthesis	R-HSA-2408522: Selenoamino acid metabolism; R-HSA-379716: Cytosolic tRNA aminoacylation	.	P41252
TTMX06B	Islet cell autoantigen p69 (ICA1)	Q05084	ICA69_HUMAN	.	P69; Islet cell autoantigen 1; ICAp69; ICA69; ICA1	ICA1	May play a role in neurotransmitter secretion.	.	.	MSGHKCSYPWDLQDRYAQDKSVVNKMQQKYWETKQAFIKATGKKEDEHVVASDADLDAKLELFHSIQRTCLDLSKAIVLYQKRICFLSQEENELGKFLRSQGFQDKTRAGKMMQATGKALCFSSQQRLALRNPLCRFHQEVETFRHRAISDTWLTVNRMEQCRTEYRGALLWMKDVSQELDPDLYKQMEKFRKVQTQVRLAKKNFDKLKMDVCQKVDLLGASRCNLLSHMLATYQTTLLHFWEKTSHTMAAIHESFKGYQPYEFTTLKSLQDPMKKLVEKEEKKKINQQESTDAAVQEPSQLISLEEENQRKESSSFKTEDGKSILSALDKGSTHTACSGPIDELLDMKSEEGACLGPVAGTPEPEGADKDDLLLLSEIFNASSLEEGEFSKEWAAVFGDGQVKEPVPTMALGEPDPKAQTGSGFLPSQLLDQNMKDLQASLQEPAKAASDLTAWFSLFADLDPLSNPDAVGKTDKEHELLNA	Literature-reported	Sera from patients with IDDM and healthy individuals have antibodies to ICA69 on western blots but do not immunoprecipitate liquid phase antigen. J Autoimmun. 1994 Oct;7(5):665-74.	.	.	.	.	.	.	.	.	.	.	.	hsa04940: Type I diabetes mellitus	.	.	Q05084
TTA1L39	ICAM1 messenger RNA (ICAM1 mRNA)	P05362	ICAM1_HUMAN	mRNA target	Major group rhinovirus receptor (mRNA); Intercellular adhesion molecule 1 (mRNA); ICAM-1 (mRNA); CD54 (mRNA)	ICAM1	"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)."	.	6EIT; 5MZA; 3TCX; 2OZ4; 1Z7Z	MAPSSPRPALPALLVLLGALFPGPGNAQTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQEDSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLTVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPYQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGNDSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEVTVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELRVLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYLCRARSTQGEVTRKVTVNVLSPRYEIVIITVVAAAVIMGTAGLSTYLYNRQRKIKKYRLQQAQKGTPMKPNTQATPP	Successful	"US patent application no. 6,300,491, Oligonucleotide inhibition of cell adhesion."	34	mRNA	mRNA target	.	.	.	"Intercellular adhesion molecule (ICAM), N-terminal domain"	PF03921	PF03921; ICAM_N	.	.	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	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	.	P05362
TTCT6F7	Intercellular adhesion molecule ICAM-1 (ICAM1)	P05362	ICAM1_HUMAN	Immunoglobulin	Major group rhinovirus receptor; Intercellular adhesion molecule 1; ICAM-1; CD54	ICAM1	"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)."	.	6EIT; 5MZA; 3TCX; 2OZ4; 1Z7Z	MAPSSPRPALPALLVLLGALFPGPGNAQTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQEDSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLTVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPYQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGNDSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEVTVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELRVLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYLCRARSTQGEVTRKVTVNVLSPRYEIVIITVVAAAVIMGTAGLSTYLYNRQRKIKKYRLQQAQKGTPMKPNTQATPP	Successful	Discovery and Development of Potent LFA-1/ICAM-1 Antagonist SAR 1118 as an Ophthalmic Solution for Treating Dry Eye. ACS Med Chem Lett. 2012 Jan 31;3(3):203-6.	34	Immunoglobulin	Immunoglobulin	immunoglobulin superfamily. ICAM family.	.	.	"Intercellular adhesion molecule (ICAM), N-terminal domain"	PF03921	PF03921; ICAM_N	.	.	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	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	.	P05362
TTE5VP6	Inducible T-cell costimulator (ICOS)	Q9Y6W8	ICOS_HUMAN	Immunoglobulin	Inducible costimulator; Inducible T-cell co-stimulator; Inducible COSTIMULATOR precursor; CD278; Activation-inducible lymphocyte immunomediatory molecule; AILIM	ICOS	"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."	.	.	MKSGLWYFFLFCLRIKVLTGEINGSANYEMFIFHNGGVQILCKYPDIVQQFKMQLLKGGQILCDLTKTKGSGNTVSIKSLKFCHSQLSNNSVSFFLYNLDHSHANYYFCNLSIFDPPPFKVTLTGGYLHIYESQLCCQLKFWLPIGCAAFVVVCILGCILICWLTKKKYSSSVHDPNGEYMFMRAVNTAKKSRLTDVTL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	Immunoglobulin	Immunoglobulin superfamily	.	.	.	ICOS V-set domain	PF15910	PF15910; V-set_2	.	.	hsa04514:Cell adhesion molecules (CAMs); hsa04660:T cell receptor signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa05340:Primary immunodeficiency	"R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-388841: Costimulation by the CD28 family; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling"	.	Q9Y6W8
TTB9Z8R	B7-related protein 1 (B7RP1)	O75144	ICOSL_HUMAN	Immunoglobulin	KIAA0653; ICOSL; ICOS ligand; CD275; B7related protein 1; B7like protein Gl50; B7RP-1; B7H2; B7-like protein Gl50; B7-H2; B7 homolog 2	ICOSLG	"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."	.	.	MRLGSPGLLFLLFSSLRADTQEKEVRAMVGSDVELSCACPEGSRFDLNDVYVYWQTSESKTVVTYHIPQNSSLENVDSRYRNRALMSPAGMLRGDFSLRLFNVTPQDEQKFHCLVLSQSLGFQEVLSVEVTLHVAANFSVPVVSAPHSPSQDELTFTCTSINGYPRPNVYWINKTDNSLLDQALQNDTVFLNMRGLYDVVSVLRIARTPSVNIGCCIENVLLQQNLTVGSQTGNDIGERDKITENPVSTGEKNAATWSILAVLCLLVVVAVAIGWVCRDRCLQHSYAGAWAVSPETELTGHV	Clinical trial	"Administration Of AMG 557, A Human Anti-B7RP-1 (ICOSL) Antibody, Leads To The Selective Inhibition Of Anti-KLH IgG Responses In Subjects With SLE: Results Of A Phase 1 Randomized, Double-Blind, Placebo-Controlled, Sequential, Rising, Multiple-Dose Study. San Diego, CA October 25-30, 2013"	21	Immunoglobulin	Immunoglobulin superfamily	immunoglobulin superfamily. BTN/MOG family.	.	.	Immunoglobulin V-set domain	PF07686	PF07686; V-set	.	.	hsa04514:Cell adhesion molecules (CAMs); hsa04672:Intestinal immune network for IgA production	R-HSA-388841:Costimulation by the CD28 family	.	O75144
TTBXVDE	ID1 messenger RNA (ID1 mRNA)	P41134	ID1_HUMAN	mRNA target	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)	ID1	"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."	.	.	MKVASGSTATAAAGPSCALKAGKTASGAGEVVRCLSEQSVAISRCAGGAGARLPALLDEQQVNVLLYDMNGCYSRLKELVPTLPQNRKVSKVEILQHVIDYIRDLQLELNSESEVGTPGGRGLPVRAPLSTLNGEISALTAEAACVPADDRILCR	Literature-reported	Suppression of ID1 expression in colon cancer cells increases sensitivity to 5-fluorouracil. Acta Biochim Pol. 2017;64(2):315-322.	.	mRNA	mRNA target	.	.	.	Helix-loop-helix DNA-binding domain	PF00010	PF00010; HLH	.	.	hsa04015: Rap1 signaling pathway; hsa04350: TGF-beta signaling pathway; hsa04390: Hippo signaling pathway; hsa04550: Signaling pathways regulating pluripotency of stem cells	R-HSA-2559585: Oncogene Induced Senescence; R-HSA-9031628: NGF-stimulated transcription	.	P41134
TTW8A5N	DNA-binding protein inhibitor ID-2 (ID2)	Q02363	ID2_HUMAN	.	bHLHb26; Inhibitor of differentiation 2; Inhibitor of DNA binding 2; Id2; Class B basic helix-loop-helix protein 26	ID2	"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."	.	4AYA	MKAFSPVRSVRKNSLSDHSLGISRSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVSKMEILQHVIDYILDLQIALDSHPTIVSLHHQRPGQNQASRTPLTTLNTDISILSLQASEFPSELMSNDSKALCG	Literature-reported	TH2 dominance and defective development of a CD8+ dendritic cell subset in Id2-deficient mice. J Allergy Clin Immunol. 2003 Jan;111(1):136-42.	.	.	.	.	.	.	Helix-loop-helix DNA-binding domain	PF00010	PF00010; HLH	.	.	hsa04350: TGF-beta signaling pathway; hsa04390: Hippo signaling pathway; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa05202: Transcriptional misregulation in cancer	R-HSA-9031628: NGF-stimulated transcription	.	Q02363
TT2EDHU	Insulin-degrading enzyme (IDE)	P14735	IDE_HUMAN	Peptidase	Insulysin; Insulinase; Insulin protease; Abeta-degrading protease	IDE	"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."	EC 3.4.24.56	6MQ3; 6EDS; 6BYZ; 6BFC; 6BF9	MRYRLAWLLHPALPSTFRSVLGARLPPPERLCGFQKKTYSKMNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSCPVVGEFPCQNDINLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHINFMAAKL	Successful	Brain insulin impairs amyloid-beta(1-40) clearance from the brain. J Neurosci. 2004 Oct 27;24(43):9632-7.	34	EC:3.4	.	peptidase M16 family.	3.4.24.56 	Acting on peptide bonds (peptidases)	Insulinase (Peptidase family M16); Peptidase M16 inactive domain; Middle or third domain of peptidase_M16	PF00675; PF05193; PF16187	PF00675; Peptidase_M16; PF05193; Peptidase_M16_C; PF16187; Peptidase_M16_M	.	.	hsa05010:Alzheimer's disease	R-HSA-5689880: Ub-specific processing proteases; R-HSA-9033241: Peroxisomal protein import	.	P14735
TTV2A1R	Oxalosuccinate decarboxylase (IDH1)	O75874	IDHC_HUMAN	Short-chain dehydrogenases reductase	PICD; NADP(+)-specific ICDH; Isocitrate dehydrogenase [NADP] cytoplasmic; IDP; IDH; Cytosolic NADP-isocitrate dehydrogenase	IDH1	Catalyses the NADPH-dependent reduction of alpha-ketoglutarate to R(-)-2-hydroxyglutarate (2HG).	EC 1.1.1.42	6BL2; 6BL1; 6BL0; 6BKZ; 6BKY	MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKIKLAQAKL	Successful	2018 FDA drug approvals.Nat Rev Drug Discov. 2019 Feb;18(2):85-89. 	34	.	.	.	.	.	.	.	.	.	.	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	R-HSA-2978092: Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate; R-HSA-389542: NADPH regeneration; R-HSA-6798695: Neutrophil degranulation; R-HSA-9033241: Peroxisomal protein import; R-HSA-9759194: Nuclear events mediated by NFE2L2	MetaCyc:HS06502-MON	O75874
TTXDKHT	Mutated oxalosuccinate decarboxylase (mIDH1)	O75874 (mutated)	IDHC_HUMAN	Short-chain dehydrogenases reductase	PICD (mutated); Oxalosuccinate decarboxylase (mutated); NADP(+)-specific ICDH (mutated); Isocitrate dehydrogenase [NADP] cytoplasmic (mutated); IDP (mutated); IDH (mutated); Cytosolic NADP-isocitrate dehydrogenase (mutated)	IDH1	Catalyses the NADPH-dependent reduction of alpha-ketoglutarate to R(-)-2-hydroxyglutarate (2HG).	EC 1.1.1.42	6BL2; 6BL1; 6BL0; 6BKZ; 6BKY	MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKIKLAQAKL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	.	.	.	O75874
TTDTWV0	Isocitrate dehydrogenase (IDH)	O75874; P48735; P50213; O43837; P51553	IDHC_HUMAN; IDHP_HUMAN; IDH3A_HUMAN; IDH3B_HUMAN; IDH3G_HUMAN	CH-OH donor oxidoreductase	Isocitrate dehydrogenase [NAD]	IDH1	It may tightly associate or interact with the pyruvate dehydrogenase complex. Plays a role in intermediary metabolism and energy production.	.	.	MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKIKLAQAKL	Successful	2017 FDA drug approvals.Nat Rev Drug Discov. 2018 Feb;17(2):81-85. 	34	EC:1.1	Short-chain dehydrogenases reductases	isocitrate and isopropylmalate dehydrogenases family.	1.1.1.42	Acting on the CH-OH group of donors	Isocitrate/isopropylmalate dehydrogenase	PF00180	PF00180; Iso_dh	.	.	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	R-HSA-2978092: Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate; R-HSA-389542: NADPH regeneration; R-HSA-6798695: Neutrophil degranulation; R-HSA-9033241: Peroxisomal protein import; R-HSA-9759194: Nuclear events mediated by NFE2L2	MetaCyc:HS06502-MON	O75874
TTZJYKH	"Indoleamine 2,3-dioxygenase 1 (IDO1)"	P14902	I23O1_HUMAN	Oxygenase	"Indoleamine-pyrrole 2,3-dioxygenase; INDO; IDO-1; IDO"	IDO1	"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."	EC 1.13.11.52	6MQ6; 6F0A; 6DPR; 6DPQ; 6CXV	MAHAMENSWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG	Successful	"Interactions between nitric oxide and indoleamine 2,3-dioxygenase. Biochemistry. 2006 Jul 18;45(28):8527-38."	34	EC:1.13	Oxidoreductases acting on single donors	"indoleamine 2,3-dioxygenase family."	1.13.11.52 	Acting on single donors with incorporation of molecular oxygen (oxygenases)	"Indoleamine 2,3-dioxygenase"	PF01231	PF01231; IDO	.	.	hsa00380:Tryptophan metabolism; hsa01100:Metabolic pathways; hsa05143:African trypanosomiasis	R-HSA-71240:Tryptophan catabolism	MetaCyc:HS05502-MON	P14902
TTALN9W	"Indoleamine 2,3-dioxygenase 2 (IDO2)"	Q6ZQW0	I23O2_HUMAN	Oxygenase	"Indoleamine-pyrrole 2,3-dioxygenase-like protein 1; Indoleamine 2,3-dioxygenase-like protein 1; INDOL1; IDO-2"	IDO2	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.	EC 1.13.11.-	.	MLHFHYYDTSNKIMEPHRPNVKTAVPLSLESYHISEEYGFLLPDSLKELPDHYRPWMEIANKLPQLIDAHQLQAHVDKMPLLSCQFLKGHREQRLAHLVLSFLTMGYVWQEGEAQPAEVLPRNLALPFVEVSRNLGLPPILVHSDLVLTNWTKKDPDGFLEIGNLETIISFPGGESLHGFILVTALVEKEAVPGIKALVQATNAILQPNQEALLQALQRLRLSIQDITKTLGQMHDYVDPDIFYAGIRIFLSGWKDNPAMPAGLMYEGVSQEPLKYSGGSAAQSTVLHAFDEFLGIRHSKESGDFLYRMRDYMPPSHKAFIEDIHSAPSLRDYILSSGQDHLLTAYNQCVQALAELRSYHITMVTKYLITAAAKAKHGKPNHLPGPPQALKDRGTGGTAVMSFLKSVRDKTLESILHPRG	Patented-recorded	Inhibitors of the kynurenine pathway as neurotherapeutics: a patent review (2012-2015).Expert Opin Ther Pat. 2016 Jul;26(7):815-32.	15.5	EC:1.13	"Indoleamine 2,3-dioxygenase family"	"indoleamine 2,3-dioxygenase family."	1.13.11.- 	Acting on single donors with incorporation of molecular oxygen (oxygenases)	"Indoleamine 2,3-dioxygenase"	PF01231	PF01231; IDO	.	.	hsa00380:Tryptophan metabolism; hsa01100:Metabolic pathways; hsa05143:African trypanosomiasis	R-HSA-71240: Tryptophan catabolism	.	Q6ZQW0
TTNY2AP	Iduronate 2-sulfatase (IDS)	P22304	IDS_HUMAN	Sulfuric ester hydrolase	Idursulfase; Iduronate 2sulfatase 14 kDa chain; IDS; AlphaLiduronate sulfate sulfatase	IDS	Required for the lysosomal degradation ofheparan sulfate and dermatan sulfate.	EC 3.1.6.13	6IOZ; 5FQL	MPPPRTGRGLLWLGLVLSSVCVALGSETQANSTTDALNVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKVFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPEVPDGLPPVAYNPWMDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTASLPEAGEKLFPYLDPFDSASQLMEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCPVPSFHVELCREGKNLLKHFRFRDLEEDPYLPGNPRELIAYSQYPRPSDIPQWNSDKPSLKDIKIMGYSIRTIDYRYTVWVGFNPDEFLANFSDIHAGELYFVDSDPLQDHNMYNDSQGGDLFQLLMP	Successful	2006 drug approvals: finding the niche. Nat Rev Drug Discov. 2007 Feb;6(2):99-101.	34	.	.	.	.	.	.	.	.	.	.	hsa00531:Glycosaminoglycan degradation; hsa01100:Metabolic pathways; hsa04142:Lysosome	R-HSA-2024096:HS-GAG degradation; R-HSA-2024101:CS/DS degradation	MetaCyc:HS00286-MON	P22304
TT0IUKX	Alpha-L-iduronidase (IDUA)	P35475	IDUA_HUMAN	.	.	IDUA	"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"	EC 3.2.1.76	.	MRPLRPRAALLALLASLLAAPPVAPAEAPHLVHVDAARALWPLRRFWRSTGFCPPLPHSQADQYVLSWDQQLNLAYVGAVPHRGIKQVRTHWLLELVTTRGSTGRGLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTDFEDKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEPDHHDFDNVSMTMQGFLNYYDACSEGLRAASPALRLGGPGDSFHTPPRSPLSWGLLRHCHDGTNFFTGEAGVRLDYISLHRKGARSSISILEQEKVVAQQIRQLFPKFADTPIYNDEADPLVGWSLPQPWRADVTYAAMVVKVIAQHQNLLLANTTSAFPYALLSNDNAFLSYHPHPFAQRTLTARFQVNNTRPPHVQLLRKPVLTAMGLLALLDEEQLWAEVSQAGTVLDSNHTVGVLASAHRPQGPADAWRAAVLIYASDDTRAHPNRSVAVTLRLRGVPPGPGLVYVTRYLDNGLCSPDGEWRRLGRPVFPTAEQFRRMRAAEDPVAAAPRPLPAGGRLTLRPALRLPSLLLVHVCARPEKPPGQVTRLRALPLTQGQLVLVWSDEHVGSKCLWTYEIQFSQDGKAYTPVSRKPSTFNLFVFSPDTGAVSGSYRVRALDYWARPGPFSDPVPYLEVPVPRGPPSPGNP	Clinical trial	ClinicalTrials.gov (NCT02702115) Ascending Dose Study of Genome Editing by the Zinc Finger Nuclease (ZFN) Therapeutic SB-318 in Subjects With MPS I. U.S. National Institutes of Health.	.	.	.	.	.	.	.	.	.	.	.	hsa00531: Glycosaminoglycan degradation; hsa01100: Metabolic pathways; hsa04142: Lysosome	R-HSA-2024096: HS-GAG degradation; R-HSA-2024101: CS/DS degradation; R-HSA-2206302: MPS I - Hurler syndrome	MetaCyc:HS05096-MON	P35475
TTSIUJ9	Interferon-alpha 2 (IFNA2)	P01563	IFNA2_HUMAN	Cytokine: interferon	LeIF A; Interferon alphaA; Interferon alpha2; Interferon alpha-A; Interferon alpha-2; IFNalpha2; IFNA2C; IFNA2B; IFNA2A; IFN-alpha-2	IFNA2	"Produced by macrophages, IFN-alpha have antiviral activities."	.	4Z5R; 4YPG; 3SE3; 3S9D; 2LMS	MALTFALLVALLVLSCKSSCSVGCDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	Cytokine	.	alpha/beta interferon family.	.	.	Interferon alpha/beta domain	PF00143	PF00143; Interferon	.	.	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	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	.	P01563
TTLHGSF	Interferon-alpha 5 (IFNA5)	P01569	IFNA5_HUMAN	Cytokine: interferon	LeIF G; Interferon alphaG; Interferon alpha61; Interferon alpha5; Interferon alpha-G; Interferon alpha-61; Interferon alpha-5; IFNalpha5; IFN-alpha-5	IFNA5	"Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. Produced by macrophages, IFN-alpha have antiviral activities."	.	.	MALPFVLLMALVVLNCKSICSLGCDLPQTHSLSNRRTLMIMAQMGRISPFSCLKDRHDFGFPQEEFDGNQFQKAQAISVLHEMIQQTFNLFSTKDSSATWDETLLDKFYTELYQQLNDLEACMMQEVGVEDTPLMNVDSILTVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSFSLSANLQERLRRKE	Clinical trial	Interferons and viral infections. Biofactors. 2009 Jan-Feb;35(1):14-20.	19	Cytokine	.	alpha/beta interferon family.	.	.	Interferon alpha/beta domain	PF00143	PF00143; Interferon	.	.	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	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	.	P01569
TTSYFMA	Interferon alpha/beta receptor 1 (IFNAR1)	P17181	INAR1_HUMAN	Cytokine receptor	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	IFNAR1	"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."	.	4PO6; 3SE4; 3SE3; 3S98	MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTPVIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKTKPGNTSKIWLIVGICIALFALPFVIYAAKVFLRCINYVFFPSLKPSSSIDEYFSEQPLKNLLLSTSEEQIEKCFIIENISTIATVEETNQTDEDHKKYSSQTSQDSGNYSNEDESESKTSEELQQDFV	Clinical trial	Patent EP2766021 A1.	21	Cytokine receptor	Type II cytokine receptor	type II cytokine receptor family.	.	.	"Interferon-alpha/beta receptor, fibronectin type III; Tissue factor"	PF09294; PF01108	PF09294; Interfer-bind; PF01108; Tissue_fac	8.A.47.2.1	The Neuropilin and Tolloid-like (Neto) Family	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	R-HSA-909733:Interferon alpha/beta signaling; R-HSA-912694:Regulation of IFNA signaling	.	P17181
TTMQB37	Interferon alpha/beta receptor 2 (IFNAR2)	P48551	INAR2_HUMAN	Cytokine receptor	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	IFNAR2	"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."	.	3SE4; 3SE3; 3S9D; 3S8W; 2LAG	MLLSQNAFIFRSLNLVLMVYISLVFGISYDSPDYTDESCTFKISLRNFRSILSWELKNHSIVPTHYTLLYTIMSKPEDLKVVKNCANTTRSFCDLTDEWRSTHEAYVTVLEGFSGNTTLFSCSHNFWLAIDMSFEPPEFEIVGFTNHINVMVKFPSIVEEELQFDLSLVIEEQSEGIVKKHKPEIKGNMSGNFTYIIDKLIPNTNYCVSVYLEHSDEQAVIKSPLKCTLLPPGQESESAESAKIGGIITVFLIALVLTSTIVTLKWIGYICLRNSLPKVLNFHNFLAWPFPNLPPLEAMDMVEVIYINRKKKVWDYNYDDESDSDTEAAPRTSGGGYTMHGLTVRPLGQASATSTESQLIDPESEEEPDLPEVDVELPTMPKDSPQQLELLSGPCERRKSPLQDPFPEEDYSSTEGSGGRITFNVDLNSVFLRVLDDEDSDDLEAPLMLSSHLEEMVDPEDPDNVQSNHLLASGEGTQPTFPSPSSEGLWSEDAPSDQSDTSESDVDLGDGYIMR	Successful	"Clinical pipeline report, company report or official report of AstraZeneca (2009)."	34	Cytokine receptor	Cytokine receptor	type II cytokine receptor family.	.	.	"Interferon-alpha/beta receptor, fibronectin type III; Tissue factor"	PF09294; PF01108	PF09294; Interfer-bind; PF01108; Tissue_fac	.	.	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	R-HSA-909733:Interferon alpha/beta signaling; R-HSA-912694:Regulation of IFNA signaling	.	P48551
TT4TZ8J	Interferon-beta (IFNB1)	P01574	IFNB_HUMAN	Cytokine: interferon	Interferon beta; IFNbeta; IFNB; IFN-beta; IFB; Fibroblast interferon	IFNB1	"Has antiviral, antibacterial and anticancer activities."	.	1AU1	MTNKCLLQIALLLCFSTTALSMSYNLLGFLQRSSNFQCQKLLWQLNGRLEYCLKDRMNFDIPEEIKQLQQFQKEDAALTIYEMLQNIFAIFRQDSSSTGWNETIVENLLANVYHQINHLKTVLEEKLEKEDFTRGKLMSSLHLKRYYGRILHYLKAKEYSHCAWTIVRVEILRNFYFINRLTGYLRN	Successful	"Pegylated interferon beta-1a for relapsing-remitting multiple sclerosis (ADVANCE): a randomised, phase 3, double-blind study. Lancet Neurol. 2014 Jul;13(7):657-65."	34	Cytokine	Interferon	alpha/beta interferon family.	.	.	Interferon alpha/beta domain	PF00143	PF00143; Interferon	.	.	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	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	.	P01574
TT93WF5	Interferon-gamma (IFNG)	P01579	IFNG_HUMAN	Cytokine: interferon	Interferon gamma; Immune interferon; IFN-gamma	IFNG	"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."	.	6E3L; 6E3K; 3BES; 1HIG; 1FYH	MKYTSYILAFQLCIVLGSLGCYCQDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAELSPAAKTGKRKRSQMLFRGRRASQ	Successful	2018 FDA drug approvals.Nat Rev Drug Discov. 2019 Feb;18(2):85-89. 	34	Cytokine	Interferon	type II (or gamma) interferon family.	.	.	Interferon gamma	PF00714	PF00714; IFN-gamma	.	.	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	R-HSA-877300:Interferon gamma signaling; R-HSA-877312:Regulation of IFNG signaling	.	P01579
TTR10KI	HUMAN interferon gamma (IFNG)	P01579	IFNG_HUMAN	Cytokine: interferon	Interferon gamma; Immune interferon; IFN-gamma	IFNG	"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."	.	6E3L; 6E3K; 3BES; 1HIG; 1FYH	MKYTSYILAFQLCIVLGSLGCYCQDPYVKEAENLKKYFNAGHSDVADNGTLFLGILKNWKEESDRKIMQSQIVSFYFKLFKNFKDDQSIQKSVETIKEDMNVKFFNSNKKKRDDFEKLTNYSVTDLNVQRKAIHELIQVMAELSPAAKTGKRKRSQMLFRGRRASQ	.	Interferon-beta and interferon-gamma synergistically inhibit the replication of severe acute respiratory syndrome-associated coronavirus (SARS-CoV). Virology. 2004 Nov 10;329(1):11-7. doi: 10.1016/j.virol.2004.08.011.	.	.	.	.	.	.	.	.	.	.	.	hsa03050: Proteasome; hsa04060: Cytokine-cytokine receptor interaction; hsa04066: HIF-1 signaling pathway; hsa04217: Necroptosis; hsa04350: TGF-beta signaling pathway; hsa04380: Osteoclast differentiation; hsa04612: Antigen processing and presentation; hsa04630: JAK-STAT signaling pathway; hsa04650: Natural killer cell mediated cytotoxicity; hsa04657: IL-17 signaling pathway; hsa04658: Th1 and Th2 cell differentiation; hsa04659: Th17 cell differentiation; hsa04660: T cell receptor signaling pathway; hsa04940: Type I diabetes mellitus; hsa05140: Leishmaniasis; hsa05142: Chagas disease; hsa05143: African trypanosomiasis; hsa05144: Malaria; hsa05145: Toxoplasmosis; hsa05146: Amoebiasis; hsa05152: Tuberculosis; hsa05160: Hepatitis C; hsa05164: Influenza A; hsa05168: Herpes simplex virus 1 infection; hsa05200: Pathways in cancer; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer; hsa05321: Inflammatory bowel disease; hsa05322: Systemic lupus erythematosus; hsa05323: Rheumatoid arthritis; hsa05330: Allograft rejection; hsa05332: Graft-versus-host disease; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-877300: Interferon gamma signaling; R-HSA-877312: Regulation of IFNG signaling; R-HSA-8877330: RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs); R-HSA-8950505: Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation	.	P01579
TT13TL0	Interferon gamma receptor (IFNGR2)	P38484	INGR2_HUMAN	Cytokine receptor	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	IFNGR2	"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) (, ,)."	.	6E3L; 6E3K; 5EH1	MRPTLLWSLLLLLGVFAAAAAAPPDPLSQLPAPQHPKIRLYNAEQVLSWEPVALSNSTRPVVYQVQFKYTDSKWFTADIMSIGVNCTQITATECDFTAASPSAGFPMDFNVTLRLRAELGALHSAWVTMPWFQHYRNVTVGPPENIEVTPGEGSLIIRFSSPFDIADTSTAFFCYYVHYWEKGGIQQVKGPFRSNSISLDNLKPSRVYCLQVQAQLLWNKSNIFRVGHLSNISCYETMADASTELQQVILISVGTFSLLSVLAGACFFLVLKYRGLIKYWFHTPPSIPLQIEEYLKDPTQPILEALDKDSSPKDDVWDSVSIISFPEKEQEDVLQTL	Successful	Genetic polymorphisms in the promoter of the interferon gamma receptor 1 gene are associated with atopic cataracts. Invest Ophthalmol Vis Sci. 2007 Feb;48(2):583-9.	34	Cytokine receptor	.	type II cytokine receptor family.	.	.	"Interferon-alpha/beta receptor, fibronectin type III; Tissue factor"	PF09294; PF01108	PF09294; Interfer-bind; PF01108; Tissue_fac	.	.	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)	R-HSA-877300:Interferon gamma signaling; R-HSA-877312:Regulation of IFNG signaling	.	P38484
TTM624L	Interleukin-29 (IL29)	Q8IU54	IFNL1_HUMAN	Cytokine: interleukin	ZCYTO21; Interleukin29; Interferon lambda1; Interferon lambda-1; IL-29; IFNlambda1; IFN-lambda-1; Cytokine Zcyto21	IFNL1	"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."	.	3OG6; 3OG4	MAAAWTVVLVTLVLGLAVAGPVPTSKPTTTGKGCHIGRFKSLSPQELASFKKARDALEESLKLKNWSCSSPVFPGNWDLRLLQVRERPVALEAELALTLKVLEAAAGPALEDVLDQPLHTLHHILSQLQACIQPQPTAGPRPRGRLHHWLHRLQEAPKKESAGCLEASVTFNLFRLLTRDLKYVADGNLCLRTSTHPEST	Clinical trial	Preclinical and clinical development of pegylated interferon-lambda 1 in chronic hepatitis C. J Interferon Cytokine Res. 2010 Aug;30(8):591-5.	25	Cytokine	.	lambda interferon family.	.	.	Interleukin-28A	PF15177	PF15177; IL28A	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway	R-HSA-449836: Other interleukin signaling; R-HSA-8854691: Interleukin-20 family signaling	.	Q8IU54
TTRF4Q2	Interferon-lambda 3 (IFNL3)	Q8IZI9	IFNL3_HUMAN	Cytokine: interferon	ZCYTO22; Interleukin28C; Interleukin28B; Interleukin-28C; Interleukin-28B; Interferon lambda3; Interferon lambda-3; IL28C; IL28B; IL-28C; IL-28B; IFNlambda3; IFN-lambda-3; Cytokine Zcyto22	IFNL3	"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."	.	5T5W; 3HHC	MTGDCMPVLVLMAAVLTVTGAVPVARLRGALPDARGCHIAQFKSLSPQELQAFKRAKDALEESLLLKDCKCRSRLFPRTWDLRQLQVRERPVALEAELALTLKVLEATADTDPALGDVLDQPLHTLHHILSQLRACIQPQPTAGPRTRGRLHHWLHRLQEAPKKESPGCLEASVTFNLFRLLTRDLNCVASGDLCV	Literature-reported	The favorable IFNL3 genotype escapes mRNA decay mediated by AU-rich elements and hepatitis C virus-induced microRNAs. Nat Immunol. 2014 Jan;15(1):72-9.	.	.	.	lambda interferon family.	.	.	Interleukin-28A	PF15177	PF15177; IL28A	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04630: JAK-STAT signaling pathway	R-HSA-8854691: Interleukin-20 family signaling	.	Q8IZI9
TTS2TGF	Interferon-omega (IFNW1)	P05000	IFNW1_HUMAN	Cytokine: interferon	Interferon omega1; Interferon omega-1; Interferon alphaII1; Interferon alpha-II-1	IFNW1	"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."	.	3SE4	MALLFPLLAALVMTSYSPVGSLGCDLPQNHGLLSRNTLVLLHQMRRISPFLCLKDRRDFRFPQEMVKGSQLQKAHVMSVLHEMLQQIFSLFHTERSSAAWNMTLLDQLHTGLHQQLQHLETCLLQVVGEGESAGAISSPALTLRRYFQGIRVYLKEKKYSDCAWEVVRMEIMKSLFLSTNMQERLRSKDRDLGSS	Clinical trial	Interferons and viral infections. Biofactors. 2009 Jan-Feb;35(1):14-20.	21	Cytokine	.	alpha/beta interferon family.	.	.	Interferon alpha/beta domain	PF00143	PF00143; Interferon	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04622:RIG-I-like receptor signaling pathway; hsa04630:Jak-STAT signaling pathway	.	.	P05000
TTT6LOU	Insulin-like growth factor-I (IGF1)	P05019	IGF1_HUMAN	.	SomatomedinC; Somatomedin-C; Mechano growth factor; Insulin-like growth factor I; IGFI; IGF-I	IGF1	"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."	.	6FF3; 5U8Q; 4XSS; 3LRI; 3GF1	MGKISSLPTQLFKCCFCDFLKVKMHTMSSSHLFYLALCLLTFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKTQKYQPPSTNKNTKSQRRKGWPKTHPGGEQKEGTEASLQIRGKKKEQRREIGSRNAECRGKKGK	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	19	.	Insulin family	insulin family.	.	.	Insulin/IGF/Relaxin family	PF00049	PF00049; Insulin	.	.	"hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa01522: Endocrine resistance; hsa04010: MAPK signaling pathway; hsa04014: Ras signaling pathway; hsa04015: Rap1 signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04068: FoxO signaling pathway; hsa04114: Oocyte meiosis; hsa04115: p53 signaling pathway; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04152: AMPK signaling pathway; hsa04211: Longevity regulating pathway; hsa04213: Longevity regulating pathway - multiple species; hsa04510: Focal adhesion; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04730: Long-term depression; hsa04750: Inflammatory mediator regulation of TRP channels; hsa04913: Ovarian steroidogenesis; hsa04914: Progesterone-mediated oocyte maturation; hsa04935: Growth hormone synthesis, secretion and action; hsa04960: Aldosterone-regulated sodium reabsorption; hsa05200: Pathways in cancer; hsa05202: Transcriptional misregulation in cancer; hsa05205: Proteoglycans in cancer; hsa05214: Glioma; hsa05215: Prostate cancer; hsa05218: Melanoma; hsa05224: Breast cancer; hsa05410: Hypertrophic cardiomyopathy; hsa05414: Dilated cardiomyopathy"	"R-HSA-114608: Platelet degranulation; R-HSA-2404192: Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R); R-HSA-2428928: IRS-related events triggered by IGF1R; R-HSA-2428933: SHC-related events triggered by IGF1R; R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-422085: Synthesis, secretion, and deacylation of Ghrelin"	.	P05019
TTQFBMY	IGF1R messenger RNA (IGF1R mRNA)	P08069	IGF1R_HUMAN	mRNA target	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)	IGF1R	"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)."	EC 2.7.10.1	5U8R; 5U8Q; 5HZN; 5FXS; 5FXR	MKSGSGGGSPTSLWGLLFLSAALSLWPTSGEICGPGIDIRNDYQQLKRLENCTVIEGYLHILLISKAEDYRSYRFPKLTVITEYLLLFRVAGLESLGDLFPNLTVIRGWKLFYNYALVIFEMTNLKDIGLYNLRNITRGAIRIEKNADLCYLSTVDWSLILDAVSNNYIVGNKPPKECGDLCPGTMEEKPMCEKTTINNEYNYRCWTTNRCQKMCPSTCGKRACTENNECCHPECLGSCSAPDNDTACVACRHYYYAGVCVPACPPNTYRFEGWRCVDRDFCANILSAESSDSEGFVIHDGECMQECPSGFIRNGSQSMYCIPCEGPCPKVCEEEKKTKTIDSVTSAQMLQGCTIFKGNLLINIRRGNNIASELENFMGLIEVVTGYVKIRHSHALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQLWDWDHRNLTIKAGKMYFAFNPKLCVSEIYRMEEVTGTKGRQSKGDINTRNNGERASCESDVLHFTSTTTSKNRIIITWHRYRPPDYRDLISFTVYYKEAPFKNVTEYDGQDACGSNSWNMVDVDLPPNKDVEPGILLHGLKPWTQYAVYVKAVTLTMVENDHIRGAKSEILYIRTNASVPSIPLDVLSASNSSSQLIVKWNPPSLPNGNLSYYIVRWQRQPQDGYLYRHNYCSKDKIPIRKYADGTIDIEEVTENPKTEVCGGEKGPCCACPKTEAEKQAEKEEAEYRKVFENFLHNSIFVPRPERKRRDVMQVANTTMSSRSRNTTAADTYNITDPEELETEYPFFESRVDNKERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTDPVFFYVQAKTGYENFIHLIIALPVAVLLIVGGLVIMLYVFHRKRNNSRLGNGVLYASVNPEYFSAADVYVPDEWEVAREKITMSRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPEMENNPVLAPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIKEEMEPGFREVSFYYSEENKLPEPEELDLEPENMESVPLDPSASSSSLPLPDRHSGHKAENGPGPGVLVLRASFDERQPYAHMNGGRKNERALPLPQSSTC	Literature-reported	"Clinical pipeline report, company report or official report of Antisense Therapeutics."	2.1	mRNA	mRNA target	.	.	.	Furin-like cysteine rich region; Protein tyrosine kinase; Receptor L domain	PF00757; PF07714; PF01030	PF00757; Furin-like; PF07714; Pkinase_Tyr; PF01030; Recep_L_domain	.	.	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	R-HSA-2428928:IRS-related events triggered by IGF1R; R-HSA-2428933:SHC-related events triggered by IGF1R	.	P08069
TTHRID2	Insulin-like growth factor I receptor (IGF1R)	P08069	IGF1R_HUMAN	Kinase	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	IGF1R	"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)."	EC 2.7.10.1	5U8R; 5U8Q; 5HZN; 5FXS; 5FXR	MKSGSGGGSPTSLWGLLFLSAALSLWPTSGEICGPGIDIRNDYQQLKRLENCTVIEGYLHILLISKAEDYRSYRFPKLTVITEYLLLFRVAGLESLGDLFPNLTVIRGWKLFYNYALVIFEMTNLKDIGLYNLRNITRGAIRIEKNADLCYLSTVDWSLILDAVSNNYIVGNKPPKECGDLCPGTMEEKPMCEKTTINNEYNYRCWTTNRCQKMCPSTCGKRACTENNECCHPECLGSCSAPDNDTACVACRHYYYAGVCVPACPPNTYRFEGWRCVDRDFCANILSAESSDSEGFVIHDGECMQECPSGFIRNGSQSMYCIPCEGPCPKVCEEEKKTKTIDSVTSAQMLQGCTIFKGNLLINIRRGNNIASELENFMGLIEVVTGYVKIRHSHALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQLWDWDHRNLTIKAGKMYFAFNPKLCVSEIYRMEEVTGTKGRQSKGDINTRNNGERASCESDVLHFTSTTTSKNRIIITWHRYRPPDYRDLISFTVYYKEAPFKNVTEYDGQDACGSNSWNMVDVDLPPNKDVEPGILLHGLKPWTQYAVYVKAVTLTMVENDHIRGAKSEILYIRTNASVPSIPLDVLSASNSSSQLIVKWNPPSLPNGNLSYYIVRWQRQPQDGYLYRHNYCSKDKIPIRKYADGTIDIEEVTENPKTEVCGGEKGPCCACPKTEAEKQAEKEEAEYRKVFENFLHNSIFVPRPERKRRDVMQVANTTMSSRSRNTTAADTYNITDPEELETEYPFFESRVDNKERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTDPVFFYVQAKTGYENFIHLIIALPVAVLLIVGGLVIMLYVFHRKRNNSRLGNGVLYASVNPEYFSAADVYVPDEWEVAREKITMSRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPEMENNPVLAPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIKEEMEPGFREVSFYYSEENKLPEPEELDLEPENMESVPLDPSASSSSLPLPDRHSGHKAENGPGPGVLVLRASFDERQPYAHMNGGRKNERALPLPQSSTC	Successful	"IGF-1R, IGF-1 and IGF-2 expression as potential prognostic and predictive markers in colorectal-cancer. Virchows Arch. 2003 Aug;443(2):139-45."	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Furin-like cysteine rich region; Protein tyrosine kinase; Receptor L domain	PF00757; PF07714; PF01030	PF00757; Furin-like; PF07714; Pkinase_Tyr; PF01030; Recep_L_domain	.	.	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	R-HSA-2428928:IRS-related events triggered by IGF1R; R-HSA-2428933:SHC-related events triggered by IGF1R	.	P08069
TTE8WGO	Insulin-like growth factor-II (IGF2)	P01344	IGF2_HUMAN	.	T3M-11-derived growth factor; Somatomedin-A; Somatomedin A; PP1446; Insulin-like growth factor II; Insulin-like growth factor 2; IGF-II	IGF2	"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."	.	5L3N; 5L3M; 5L3L; 3KR3; 3E4Z	MGIPMGKSMLVLLTFLAFASCCIAAYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSTPPTVLPDNFPRYPVGKFFQYDTWKQSTQRLRRGLPALLRARRGHVLAKELEAFREAKRHRPLIALPTQDPAHGGAPPEMASNRK	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	Insulin family	insulin family.	.	.	Insulin-like growth factor II E-peptide; Insulin/IGF/Relaxin family	PF08365; PF00049	PF08365; IGF2_C; PF00049; Insulin	.	.	hsa04010: MAPK signaling pathway; hsa04014: Ras signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05225: Hepatocellular carcinoma	R-HSA-114608: Platelet degranulation; R-HSA-2404192: Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R); R-HSA-2428928: IRS-related events triggered by IGF1R; R-HSA-2428933: SHC-related events triggered by IGF1R; R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)	.	P01344
TTPNE41	CI Man-6-P receptor (IGF2R)	P11717	MPRI_HUMAN	Mannose 6-phosphate receptor	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	IGF2R	"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."	.	5IEI; 2V5P; 2V5O; 2V5N; 2M6T	MGAAAGRSPHLGPAPARRPQRSLLLLQLLLLVAAPGSTQAQAAPFPELCSYTWEAVDTKNNVLYKINICGSVDIVQCGPSSAVCMHDLKTRTYHSVGDSVLRSATRSLLEFNTTVSCDQQGTNHRVQSSIAFLCGKTLGTPEFVTATECVHYFEWRTTAACKKDIFKANKEVPCYVFDEELRKHDLNPLIKLSGAYLVDDSDPDTSLFINVCRDIDTLRDPGSQLRACPPGTAACLVRGHQAFDVGQPRDGLKLVRKDRLVLSYVREEAGKLDFCDGHSPAVTITFVCPSERREGTIPKLTAKSNCRYEIEWITEYACHRDYLESKTCSLSGEQQDVSIDLTPLAQSGGSSYISDGKEYLFYLNVCGETEIQFCNKKQAAVCQVKKSDTSQVKAAGRYHNQTLRYSDGDLTLIYFGGDECSSGFQRMSVINFECNKTAGNDGKGTPVFTGEVDCTYFFTWDTEYACVKEKEDLLCGATDGKKRYDLSALVRHAEPEQNWEAVDGSQTETEKKHFFINICHRVLQEGKARGCPEDAAVCAVDKNGSKNLGKFISSPMKEKGNIQLSYSDGDDCGHGKKIKTNITLVCKPGDLESAPVLRTSGEGGCFYEFEWHTAAACVLSKTEGENCTVFDSQAGFSFDLSPLTKKNGAYKVETKKYDFYINVCGPVSVSPCQPDSGACQVAKSDEKTWNLGLSNAKLSYYDGMIQLNYRGGTPYNNERHTPRATLITFLCDRDAGVGFPEYQEEDNSTYNFRWYTSYACPEEPLECVVTDPSTLEQYDLSSLAKSEGGLGGNWYAMDNSGEHVTWRKYYINVCRPLNPVPGCNRYASACQMKYEKDQGSFTEVVSISNLGMAKTGPVVEDSGSLLLEYVNGSACTTSDGRQTTYTTRIHLVCSRGRLNSHPIFSLNWECVVSFLWNTEAACPIQTTTDTDQACSIRDPNSGFVFNLNPLNSSQGYNVSGIGKIFMFNVCGTMPVCGTILGKPASGCEAETQTEELKNWKPARPVGIEKSLQLSTEGFITLTYKGPLSAKGTADAFIVRFVCNDDVYSGPLKFLHQDIDSGQGIRNTYFEFETALACVPSPVDCQVTDLAGNEYDLTGLSTVRKPWTAVDTSVDGRKRTFYLSVCNPLPYIPGCQGSAVGSCLVSEGNSWNLGVVQMSPQAAANGSLSIMYVNGDKCGNQRFSTRITFECAQISGSPAFQLQDGCEYVFIWRTVEACPVVRVEGDNCEVKDPRHGNLYDLKPLGLNDTIVSAGEYTYYFRVCGKLSSDVCPTSDKSKVVSSCQEKREPQGFHKVAGLLTQKLTYENGLLKMNFTGGDTCHKVYQRSTAIFFYCDRGTQRPVFLKETSDCSYLFEWRTQYACPPFDLTECSFKDGAGNSFDLSSLSRYSDNWEAITGTGDPEHYLINVCKSLAPQAGTEPCPPEAAACLLGGSKPVNLGRVRDGPQWRDGIIVLKYVDGDLCPDGIRKKSTTIRFTCSESQVNSRPMFISAVEDCEYTFAWPTATACPMKSNEHDDCQVTNPSTGHLFDLSSLSGRAGFTAAYSEKGLVYMSICGENENCPPGVGACFGQTRISVGKANKRLRYVDQVLQLVYKDGSPCPSKSGLSYKSVISFVCRPEARPTNRPMLISLDKQTCTLFFSWHTPLACEQATECSVRNGSSIVDLSPLIHRTGGYEAYDESEDDASDTNPDFYINICQPLNPMHGVPCPAGAAVCKVPIDGPPIDIGRVAGPPILNPIANEIYLNFESSTPCLADKHFNYTSLIAFHCKRGVSMGTPKLLRTSECDFVFEWETPVVCPDEVRMDGCTLTDEQLLYSFNLSSLSTSTFKVTRDSRTYSVGVCTFAVGPEQGGCKDGGVCLLSGTKGASFGRLQSMKLDYRHQDEAVVLSYVNGDRCPPETDDGVPCVFPFIFNGKSYEECIIESRAKLWCSTTADYDRDHEWGFCRHSNSYRTSSIIFKCDEDEDIGRPQVFSEVRGCDVTFEWKTKVVCPPKKLECKFVQKHKTYDLRLLSSLTGSWSLVHNGVSYYINLCQKIYKGPLGCSERASICRRTTTGDVQVLGLVHTQKLGVIGDKVVVTYSKGYPCGGNKTASSVIELTCTKTVGRPAFKRFDIDSCTYYFSWDSRAACAVKPQEVQMVNGTITNPINGKSFSLGDIYFKLFRASGDMRTNGDNYLYEIQLSSITSSRNPACSGANICQVKPNDQHFSRKVGTSDKTKYYLQDGDLDVVFASSSKCGKDKTKSVSSTIFFHCDPLVEDGIPEFSHETADCQYLFSWYTSAVCPLGVGFDSENPGDDGQMHKGLSERSQAVGAVLSLLLVALTCCLLALLLYKKERRETVISKLTTCCRRSSNVSYKYSKVNKEEETDENETEWLMEEIQLPPPRQGKEGQENGHITTKSVKALSSLHGDDQDSEDEVLTIPEVKVHSGRGAGAESSHPVRNAQSNALQEREDDRVGLVRGEKARKGKSSSAQQKTVSSTKLVSFHDDSDEDLLHI	Clinical trial	Hypertrophic Scarring and Keloids: Pathomechanisms and Current and Emerging Treatment Strategies. Mol Med. 2011 Jan-Feb; 17(1-2): 113-125.	21	TC=9.B.247	.	MRL1/IGF2R family.	.	.	Cation-independent mannose-6-phosphate receptor repeat; Fibronectin type II domain	PF00878; PF00040	PF00878; CIMR; PF00040; fn2	9.B.247.1.2	The Mannose 6-Phosphate Receptor (M6PR) Family	hsa04142:Lysosome	R-HSA-432722:Golgi Associated Vesicle Biogenesis	.	P11717
TTCJTWF	Insulin-like growth factor-binding protein 1 (IGFBP1)	P08833	IBP1_HUMAN	Insulin-like growth factor binding	Placental protein 12; PP12; KITLG; IGFBP-1; IGF-binding protein 1; IBP1; IBP-1	IGFBP1	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.	.	2DSQ; 1ZT5; 1ZT3	MSEVPVARVWLVLLLLTVQVGVTAGAPWQCAPCSAEKLALCPPVSASCSEVTRSAGCGCCPMCALPLGAACGVATARCARGLSCRALPGEQQPLHALTRGQGACVQESDASAPHAAEAGSPESPESTEITEEELLDNFHLMAPSEEDHSILWDAISTYDGSKALHVTNIKKWKEPCRIELYRVVESLAKAQETSGEEISKFYLPNCNKNGFYHSRQCETSMDGEAGLCWCVYPWNGKRIPGSPEIRGDPNCQIYFNVQN	Literature-reported	The insulin-like growth factor system as a therapeutic target in colorectal cancer. Ann Oncol. 2002 Mar;13(3):349-56.	.	Insulin-like growth factor binding	Insulin-like growth factor binding	.	.	.	Insulin-like growth factor binding protein; Thyroglobulin type-1 repeat	PF00219; PF00086	PF00219; IGFBP; PF00086; Thyroglobulin_1	.	.	.	"R-HSA-380994: ATF4 activates genes in response to endoplasmic reticulum stress; R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation; R-HSA-9615017: FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes"	.	P08833
TTKOBY0	Bone resorption factor (BRF)	P08833; P18065; P17936	IBP1_HUMAN; IBP2_HUMAN; IBP3_HUMAN	.	Insulin-like growth factor-binding protein; IGFBP; IGF-binding protein; IBP	IGFBP1	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.	.	.	MSEVPVARVWLVLLLLTVQVGVTAGAPWQCAPCSAEKLALCPPVSASCSEVTRSAGCGCCPMCALPLGAACGVATARCARGLSCRALPGEQQPLHALTRGQGACVQESDASAPHAAEAGSPESPESTEITEEELLDNFHLMAPSEEDHSILWDAISTYDGSKALHVTNIKKWKEPCRIELYRVVESLAKAQETSGEEISKFYLPNCNKNGFYHSRQCETSMDGEAGLCWCVYPWNGKRIPGSPEIRGDPNCQIYFNVQN	Discontinued	"Disodium 1-hydroxy-3-(1-pyrrolidinyl)-propylidene-1,1-bisphosphonate (EB-1053) is a potent inhibitor of bone resorption in vitro and in vivo. J Bone Miner Res. 1992 Aug;7(8):981-6."	5	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-380994: ATF4 activates genes in response to endoplasmic reticulum stress; R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation; R-HSA-9615017: FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes"	.	P08833
TTU4QSN	IGFBP2 messenger RNA (IGFBP2 mRNA)	P18065	IBP2_HUMAN	mRNA target	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)	IGFBP2	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.	.	2H7T	MLPRVGCPALPLPPPPLLPLLLLLLGASGGGGGARAEVLFRCPPCTPERLAACGPPPVAPPAAVAAVAGGARMPCAELVREPGCGCCSVCARLEGEACGVYTPRCGQGLRCYPHPGSELPLQALVMGEGTCEKRRDAEYGASPEQVADNGDDHSEGGLVENHVDSTMNMLGGGGSAGRKPLKSGMKELAVFREKVTEQHRQMGKGGKHHLGLEEPKKLRPPPARTPCQQELDQVLERISTMRLPDERGPLEHLYSLHIPNCDKHGLYNLKQCKMSLNGQRGECWCVNPNTGKLIQGAPTIRGDPECHLFYNEQQEARGVHTQRMQ	Literature-reported	Modulation of IGFBP2 mRNA expression in white adipose tissue upon aging and obesity. Horm Metab Res. 2010 Oct;42(11):787-91.	.	mRNA	mRNA target	.	.	.	Insulin-like growth factor binding protein; Thyroglobulin type-1 repeat	PF00219; PF00086	PF00219; IGFBP; PF00086; Thyroglobulin_1	.	.	.	R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)	.	P18065
TT8FDB0	Insulin-like growth factor-binding protein 2 (IGFBP2)	P18065	IBP2_HUMAN	Insulin-like growth factor binding	IGFBP-2; IGF-binding protein 2; IBP2; IBP-2; BP2	IGFBP2	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.	.	2H7T	MLPRVGCPALPLPPPPLLPLLLLLLGASGGGGGARAEVLFRCPPCTPERLAACGPPPVAPPAAVAAVAGGARMPCAELVREPGCGCCSVCARLEGEACGVYTPRCGQGLRCYPHPGSELPLQALVMGEGTCEKRRDAEYGASPEQVADNGDDHSEGGLVENHVDSTMNMLGGGGSAGRKPLKSGMKELAVFREKVTEQHRQMGKGGKHHLGLEEPKKLRPPPARTPCQQELDQVLERISTMRLPDERGPLEHLYSLHIPNCDKHGLYNLKQCKMSLNGQRGECWCVNPNTGKLIQGAPTIRGDPECHLFYNEQQEARGVHTQRMQ	Literature-reported	Glioma progression is mediated by an addiction to aberrant IGFBP2 expression and can be blocked using anti-IGFBP2 strategies. J Pathol. 2016 Jul;239(3):355-64.	.	Insulin-like growth factor binding	Insulin-like growth factor binding	.	.	.	Insulin-like growth factor binding protein; Thyroglobulin type-1 repeat	PF00219; PF00086	PF00219; IGFBP; PF00086; Thyroglobulin_1	.	.	.	R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)	.	P18065
TTZHNQA	Insulin-like growth factor-binding protein 3 (IGFBP3)	P17936	IBP3_HUMAN	Insulin-like growth factor binding	IGFBP-3; IGF-binding protein 3; IBP3; IBP-3	IGFBP3	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.	.	.	MQRARPTLWAAALTLLVLLRGPPVARAGASSAGLGPVVRCEPCDARALAQCAPPPAVCAELVREPGCGCCLTCALSEGQPCGIYTERCGSGLRCQPSPDEARPLQALLDGRGLCVNASAVSRLRAYLLPAPPAPGNASESEEDRSAGSVESPSVSSTHRVSDPKFHPLHSKIIIIKKGHAKDSQRYKVDYESQSTDTQNFSSESKRETEYGPCRREMEDTLNHLKFLNVLSPRGVHIPNCDKKGFYKKKQCRPSKGRKRGFCWCVDKYGQPLPGYTTKGKEDVHCYSMQSK	Clinical trial	"Plasma insulin-like growth factors, insulin-like binding protein-3, and outcome in metastatic colorectal cancer: results from intergroup trial N9741. Clin Cancer Res. 2008 Dec 15;14(24):8263-9. "	.	Insulin-like growth factor binding	Insulin-like growth factor binding	.	.	.	Insulin-like growth factor binding protein; Thyroglobulin type-1 repeat	PF00219; PF00086	PF00219; IGFBP; PF00086; Thyroglobulin_1	.	.	"hsa04115: p53 signaling pathway; hsa04218: Cellular senescence; hsa04935: Growth hormone synthesis, secretion and action; hsa05202: Transcriptional misregulation in cancer"	R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-6803211: TP53 Regulates Transcription of Death Receptors and Ligands; R-HSA-8957275: Post-translational protein phosphorylation	.	P17936
TTDWEA8	IGFBP5 messenger RNA (IGFBP5 mRNA)	P24593	IBP5_HUMAN	mRNA target	Insulin-like growth factor-binding protein 5 (mRNA); IGFBP-5 (mRNA); IGF-binding protein 5 (mRNA); IBP5 (mRNA); IBP-5 (mRNA)	IGFBP5	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.	.	1H59; 1BOE	MVLLTAVLLLLAAYAGPAQSLGSFVHCEPCDEKALSMCPPSPLGCELVKEPGCGCCMTCALAEGQSCGVYTERCAQGLRCLPRQDEEKPLHALLHGRGVCLNEKSYREQVKIERDSREHEEPTTSEMAEETYSPKIFRPKHTRISELKAEAVKKDRRKKLTQSKFVGGAENTAHPRIISAPEMRQESEQGPCRRHMEASLQELKASPRMVPRAVYLPNCDRKGFYKRKQCKPSRGRKRGICWCVDKYGMKLPGMEYVDGDFQCHTFDSSNVE	Literature-reported	Correlation between the DNA methylation and gene expression of IGFBP5 in breast cancer. Breast Dis. 2016;36(4):123-131.	.	mRNA	mRNA target	.	.	.	Insulin-like growth factor binding protein; Thyroglobulin type-1 repeat	PF00219; PF00086	PF00219; IGFBP; PF00086; Thyroglobulin_1	.	.	.	R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation	MetaCyc:ENSG00000115461-MON	P24593
TTLAYV8	Insulin-like growth factor-binding protein 6 (IGFBP6)	P24592	IBP6_HUMAN	Insulin-like growth factor binding	IGFBP-6; IGF-binding protein 6; IBP6; IBP-6	IGFBP6	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.	.	1RMJ	MTPHRLLPPLLLLLALLLAASPGGALARCPGCGQGVQAGCPGGCVEEEDGGSPAEGCAEAEGCLRREGQECGVYTPNCAPGLQCHPPKDDEAPLRALLLGRGRCLPARAPAVAEENPKESKPQAGTARPQDVNRRDQQRNPGTSTTPSQPNSAGVQDTEMGPCRRHLDSVLQQLQTEVYRGAQTLYVPNCDHRGFYRKRQCRSSQGQRRGPCWCVDRMGKSLPGSPDGNGSSSCPTGSSG	Literature-reported	Insulin-like growth factor binding protein-6 activates programmed cell death in non-small cell lung cancer cells. Oncogene. 2000 Sep 7;19(38):4432-6.	.	Insulin-like growth factor binding	.	.	.	.	Thyroglobulin type-1 repeat	PF00086	PF00086; Thyroglobulin_1	.	.	.	R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)	.	P24592
TTUQ01B	Insulin-like growth factor-binding protein 7 (IGFBP7)	Q16270	IBP7_HUMAN	Immunoglobulin	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	IGFBP7	Stimulates prostacyclin (PGI2) production. Stimulates cell adhesion. Binds IGF-I and IGF-II with a relatively low affinity.	.	.	MERPSLRALLLGAAGLLLLLLPLSSSSSSDTCGPCEPASCPPLPPLGCLLGETRDACGCCPMCARGEGEPCGGGGAGRGYCAPGMECVKSRKRRKGKAGAAAGGPGVSGVCVCKSRYPVCGSDGTTYPSGCQLRAASQRAESRGEKAITQVSKGTCEQGPSIVTPPKDIWNVTGAQVYLSCEVIGIPTPVLIWNKVKRGHYGVQRTELLPGDRDNLAIQTRGGPEKHEVTGWVLVSPLSKEDAGEYECHASNSQGQASASAKITVVDALHEIPVKKGEGAEL	Literature-reported	Insulin growth factor binding protein 7 is a novel target to treat dementia. Neurobiol Dis. 2014 Feb;62:135-43.	.	Immunoglobulin	.	.	.	.	Immunoglobulin I-set domain; Insulin-like growth factor binding protein; Kazal-type serine protease inhibitor domain	PF07679; PF00219; PF07648	PF07679; I-set; PF00219; IGFBP; PF07648; Kazal_2	.	.	.	R-HSA-2559582: Senescence-Associated Secretory Phenotype (SASP); R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation	.	Q16270
TTCJ4WY	Immunoglobulin heavy variable 5 (IGHV5)	A0A0C4DH38; A0A0J9YXX1	HV551_HUMAN; HV5X1_HUMAN	.	Immunoglobulin heavy variable 5	IGHV5-10-1	"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."	.	.	MGSTAILALLLAVLQGVCAEVQLVQSGAEVKKPGESLKISCKGSGYSFTSYWIGWVRQMPGKGLEWMGIIYPGDSDTRYSPSFQGQVTISADKSISTAYLQWSSLKASDTAMYYCAR	Literature-reported	Human IgE against the major allergen Bet v 1--defining an epitope with limited cross-reactivity between different PR-10 family proteins. Clin Exp Allergy. 2014 Feb;44(2):288-99.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	A0A0C4DH38
TTY2XZ0	IKK complex-associated protein (IKBKAP)	O95163	ELP1_HUMAN	.	IkappaB kinase complexassociated protein; IkappaB kinase complex-associated protein; IKK complexassociated protein; IKAP; Elongator complex protein 1; ELP1	IKBKAP	"May act as a scaffold protein that may assemble active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK)."	.	5CQR	MRNLKLFRTLEFRDIQGPGNPQCFSLRTEQGTVLIGSEHGLIEVDPVSREVKNEVSLVAEGFLPEDGSGRIVGVQDLLDQESVCVATASGDVILCSLSTQQLECVGSVASGISVMSWSPDQELVLLATGQQTLIMMTKDFEPILEQQIHQDDFGESKFITVGWGRKETQFHGSEGRQAAFQMQMHESALPWDDHRPQVTWRGDGQFFAVSVVCPETGARKVRVWNREFALQSTSEPVAGLGPALAWKPSGSLIASTQDKPNQQDIVFFEKNGLLHGHFTLPFLKDEVKVNDLLWNADSSVLAVWLEDLQREESSIPKTCVQLWTVGNYHWYLKQSLSFSTCGKSKIVSLMWDPVTPYRLHVLCQGWHYLAYDWHWTTDRSVGDNSSDLSNVAVIDGNRVLVTVFRQTVVPPPMCTYQLLFPHPVNQVTFLAHPQKSNDLAVLDASNQISVYKCGDCPSADPTVKLGAVGGSGFKVCLRTPHLEKRYKIQFENNEDQDVNPLKLGLLTWIEEDVFLAVSHSEFSPRSVIHHLTAASSEMDEEHGQLNVSSSAAVDGVIISLCCNSKTKSVVLQLADGQIFKYLWESPSLAIKPWKNSGGFPVRFPYPCTQTELAMIGEEECVLGLTDRCRFFINDIEVASNITSFAVYDEFLLLTTHSHTCQCFCLRDASFKTLQAGLSSNHVSHGEVLRKVERGSRIVTVVPQDTKLVLQMPRGNLEVVHHRALVLAQIRKWLDKLMFKEAFECMRKLRINLNLIYDHNPKVFLGNVETFIKQIDSVNHINLFFTELKEEDVTKTMYPAPVTSSVYLSRDPDGNKIDLVCDAMRAVMESINPHKYCLSILTSHVKKTTPELEIVLQKVHELQGNAPSDPDAVSAEEALKYLLHLVDVNELYDHSLGTYDFDLVLMVAEKSQKDPKEYLPFLNTLKKMETNYQRFTIDKYLKRYEKAIGHLSKCGPEYFPECLNLIKDKNLYNEALKLYSPSSQQYQDISIAYGEHLMQEHMYEPAGLMFARCGAHEKALSAFLTCGNWKQALCVAAQLNFTKDQLVGLGRTLAGKLVEQRKHIDAAMVLEECAQDYEEAVLLLLEGAAWEEALRLVYKYNRLDIIETNVKPSILEAQKNYMAFLDSQTATFSRHKKRLLVVRELKEQAQQAGLDDEVPHGQESDLFSETSSVVSGSEMSGKYSHSNSRISARSSKNRRKAERKKHSLKEGSPLEDLALLEALSEVVQNTENLKDEVYHILKVLFLFEFDEQGRELQKAFEDTLQLMERSLPEIWTLTYQQNSATPVLGPNSTANSIMASYQQQKTSVPVLDAELFIPPKINRRTQWKLSLLD	Literature-reported	Kinetin in familial dysautonomia carriers: implications for a new therapeutic strategy targeting mRNA splicing. Pediatr Res. 2009 Mar;65(3):341-6.	.	.	.	ELP1/IKA1 family.	.	.	IKI3 family	PF04762	PF04762; IKI3	.	.	.	R-HSA-3214847: HATs acetylate histones	.	O95163
TTJ3E9X	Inhibitor of nuclear factor kappa-B kinase beta (IKKB)	O14920	IKKB_HUMAN	Kinase	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	IKBKB	"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."	EC 2.7.11.10	4KIK; 4E3C; 3BRV; 3BRT	MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHNQETGEQIAIKQCRQELSPRNRERWCLEIQIMRRLTHPNVVAARDVPEGMQNLAPNDLPLLAMEYCQGGDLRKYLNQFENCCGLREGAILTLLSDIASALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNWQPVQWHSKVRQKSEVDIVVSEDLNGTVKFSSSLPYPNNLNSVLAERLEKWLQLMLMWHPRQRGTDPTYGPNGCFKALDDILNLKLVHILNMVTGTIHTYPVTEDESLQSLKARIQQDTGIPEEDQELLQEAGLALIPDKPATQCISDGKLNEGHTLDMDLVFLFDNSKITYETQISPRPQPESVSCILQEPKRNLAFFQLRKVWGQVWHSIQTLKEDCNRLQQGQRAAMMNLLRNNSCLSKMKNSMASMSQQLKAKLDFFKTSIQIDLEKYSEQTEFGITSDKLLLAWREMEQAVELCGRENEVKLLVERMMALQTDIVDLQRSPMGRKQGGTLDDLEEQARELYRRLREKPRDQRTEGDSQEMVRLLLQAIQSFEKKVRVIYTQLSKTVVCKQKALELLPKVEEVVSLMNEDEKTVVRLQEKRQKELWNLLKIACSKVRGPVSGSPDSMNASRLSQPGQLMSQPSTASNSLPEPAKKSEELVAEAHNLCTLLENAIQDTVREQDQSFTALDWSWLQTEEEEHSCLEQAS	Clinical trial	The NF B pathway: a therapeutic target in glioblastoma. Oncotarget. 2011 August; 2(8): 646-653.	21	EC:2.7	Kinase	protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily.	2.7.11.10	Transferring phosphorus-containing groups	IQBAL scaffold dimerization domain; I-kappa-kinase-beta NEMO binding domain; Protein kinase domain	PF18397; PF12179; PF00069	PF18397; IKBKB_SDD; PF12179; IKKbetaNEMObind; PF00069; Pkinase	.	.	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	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	.	O14920
TTKT5NV	Zinc finger protein Helios (IKZF2)	Q9UKS7	IKZF2_HUMAN	.	Ikaros family zinc finger protein 2	IKZF2	Associates with Ikaros at centromeric heterochromatin.	.	.	METEAIDGYITCDNELSPEREHSNMAIDLTSSTPNGQHASPSHMTSTNSVKLEMQSDEECDRKPLSREDEIRGHDEGSSLEEPLIESSEVADNRKVQELQGEGGIRLPNGKLKCDVCGMVCIGPNVLMVHKRSHTGERPFHCNQCGASFTQKGNLLRHIKLHSGEKPFKCPFCSYACRRRDALTGHLRTHSVGKPHKCNYCGRSYKQRSSLEEHKERCHNYLQNVSMEAAGQVMSHHVPPMEDCKEQEPIMDNNISLVPFERPAVIEKLTGNMGKRKSSTPQKFVGEKLMRFSYPDIHFDMNLTYEKEAELMQSHMMDQAINNAITYLGAEALHPLMQHPPSTIAEVAPVISSAYSQVYHPNRIERPISRETADSHENNMDGPISLIRPKSRPQEREASPSNSCLDSTDSESSHDDHQSYQGHPALNPKRKQSPAYMKEDVKALDTTKAPKGSLKDIYKVFNGEGEQIRAFKCEHCRVLFLDHVMYTIHMGCHGYRDPLECNICGYRSQDRYEFSSHIVRGEHTFH	Clinical trial	Targeted protein degraders crowd into the clinic. Nat Rev Drug Discov. 2021 Apr;20(4):247-250.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9UKS7
TTCZVFZ	Zinc finger protein Aiolos (IKZF3)	Q9UKT9	IKZF3_HUMAN	.	Ikaros family zinc finger protein 3	IKZF3	"Transcription factor that plays an important role in the regulation of lymphocyte differentiation. Plays an essential role in regulation of B-cell differentiation, proliferation and maturation to an effector state. Involved in regulating BCL2 expression and controlling apoptosis in T-cells in an IL2-dependent manner. {ECO:0000269|PubMed:10369681, ECO:0000269|PubMed:34155405}."	.	.	MEDIQTNAELKSTQEQSVPAESAAVLNDYSLTKSHEMENVDSGEGPANEDEDIGDDSMKVKDEYSERDENVLKSEPMGNAEEPEIPYSYSREYNEYENIKLERHVVSFDSSRPTSGKMNCDVCGLSCISFNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHTGEKPFKCHLCNYACQRRDALTGHLRTHSVEKPYKCEFCGRSYKQRSSLEEHKERCRTFLQSTDPGDTASAEARHIKAEMGSERALVLDRLASNVAKRKSSMPQKFIGEKRHCFDVNYNSSYMYEKESELIQTRMMDQAINNAISYLGAEALRPLVQTPPAPTSEMVPVISSMYPIALTRAEMSNGAPQELEKKSIHLPEKSVPSERGLSPNNSGHDSTDTDSNHEERQNHIYQQNHMVLSRARNGMPLLKEVPRSYELLKPPPICPRDSVKVINKEGEVMDVYRCDHCRVLFLDYVMFTIHMGCHGFRDPFECNMCGYRSHDRYEFSSHIARGEHRALLK	Clinical trial	The Evolution of Therapies Targeting Bruton Tyrosine Kinase for the Treatment of Chronic Lymphocytic Leukaemia: Future Perspectives. Cancers (Basel). 2023 May 3;15(9):2596.	.	.	.	.	.	.	.	.	.	.	.	hsa:22806	.	.	Q9UKT9;
TTT0Q1F	Interleukin-10 (IL10)	P22301	IL10_HUMAN	Cytokine: interleukin	IL-10; Cytokine synthesis inhibitory factor; CSIF	IL10	"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."	.	2ILK; 2H24; 1Y6K; 1LK3; 1J7V	MHSSALLCCLVLLTGVRASPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN	Clinical trial	"Preclinical characterization of DEKAVIL (F8-IL10), a novel clinical-stage immunocytokine which inhibits the progression of collagen-induced arthritis. Arthritis Res Ther. 2009;11(5):R142."	21	Cytokine	Cytokine: interleukin	IL-10 family.	.	.	Interleukin 10	PF00726	PF00726; IL10	.	.	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	R-HSA-6783783: Interleukin-10 signaling; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-8950505: Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation; R-HSA-9662834: CD163 mediating an anti-inflammatory response; R-HSA-9664323: FCGR3A-mediated IL10 synthesis	.	P22301
TT4NHTB	HUMAN interleukin-10 (IL10)	P22301	IL10_HUMAN	Cytokine: interleukin	IL-10; Cytokine synthesis inhibitory factor; CSIF	IL10	"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."	.	2ILK; 2H24; 1Y6K; 1LK3; 1J7V	MHSSALLCCLVLLTGVRASPGQGTQSENSCTHFPGNLPNMLRDLRDAFSRVKTFFQMKDQLDNLLLKESLLEDFKGYLGCQALSEMIQFYLEEVMPQAENQDPDIKAHVNSLGENLKTLRLRLRRCHRFLPCENKSKAVEQVKNAFNKLQEKGIYKAMSEFDIFINYIEAYMTMKIRN	.	"ClinicalTrials.gov (NCT04363008) COVID-19 Inflammatory Blood Biomarkers for Clinical Management, Prognosis and Evaluation of Interventions"	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04068: FoxO signaling pathway; hsa04625: C-type lectin receptor signaling pathway; hsa04630: JAK-STAT signaling pathway; hsa04660: T cell receptor signaling pathway; hsa04672: Intestinal immune network for IgA production; hsa05133: Pertussis; hsa05135: Yersinia infection; hsa05140: Leishmaniasis; hsa05142: Chagas disease; hsa05143: African trypanosomiasis; hsa05144: Malaria; hsa05145: Toxoplasmosis; hsa05146: Amoebiasis; hsa05150: Staphylococcus aureus infection; hsa05152: Tuberculosis; hsa05310: Asthma; hsa05320: Autoimmune thyroid disease; hsa05321: Inflammatory bowel disease; hsa05322: Systemic lupus erythematosus; hsa05330: Allograft rejection	R-HSA-6783783: Interleukin-10 signaling; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-8950505: Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation; R-HSA-9662834: CD163 mediating an anti-inflammatory response; R-HSA-9664323: FCGR3A-mediated IL10 synthesis	.	P22301
TTJTRMK	Interleukin 10 receptor (IL10RB)	Q08334	I10R2_HUMAN	Cytokine receptor	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	IL10RB	"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."	.	5T5W; 3LQM	MAWSLGSWLGGCLLVSALGMVPPPENVRMNSVNFKNILQWESPAFAKGNLTFTAQYLSYRIFQDKCMNTTLTECDFSSLSKYGDHTLRVRAEFADEHSDWVNITFCPVDDTIIGPPGMQVEVLADSLHMRFLAPKIENEYETWTMKNVYNSWTYNVQYWKNGTDEKFQITPQYDFEVLRNLEPWTTYCVQVRGFLPDRNKAGEWSEPVCEQTTHDETVPSWMVAVILMASVFMVCLALLGCFALLWCVYKKTKYAFSPRNSLPQHLKEFLGHPHHNTLLFFSFPLSDENDVFDKLSVIAEDSESGKQNPGDSCSLGTPPGQGPQS	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1900).	0	Cytokine receptor	.	type II cytokine receptor family.	.	.	"Interferon-alpha/beta receptor, fibronectin type III; Tissue factor"	PF09294; PF01108	PF09294; Interfer-bind; PF01108; Tissue_fac	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa05145:Toxoplasmosis; hsa05152:Tuberculosis; hsa05169:Epstein-Barr virus infection	R-HSA-449836: Other interleukin signaling; R-HSA-6783783: Interleukin-10 signaling; R-HSA-8854691: Interleukin-20 family signaling	.	Q08334
TTGUYTR	Interleukin-11 (IL11)	P20809	IL11_HUMAN	Cytokine: interleukin	Oprelvekin; IL-11; Adipogenesis inhibitory factor; AGIF	IL11	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.	.	4MHL	MNCVCRLVLVVLSLWPDTAVAPGPPPGPPRVSPDPRAELDSTVLLTRSLLADTRQLAAQLRDKFPADGDHNLDSLPTLAMSAGALGALQLPGVLTRLRADLLSYLRHVQWLRRAGGSSLKTLEPELGTLQARLDRLLRRLQLLMSRLALPQPPPDPPAPPLAPPSSAWGGIRAAHAILGGLHLTLDWAVRGLLLLKTRL	Clinical trial	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800033052)"	25	Cytokine	Cytokine: interleukin	IL-6 superfamily.	.	.	Interleukin 11	PF07400	PF07400; IL11	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa05323:Rheumatoid arthritis	R-HSA-6788467: IL-6-type cytokine receptor ligand interactions	.	P20809
TTZPLJS	Interleukin 11 receptor alpha (IL11RA)	Q14626	I11RA_HUMAN	Cytokine receptor	Interleukin-11 receptor subunit alpha; IL-11RA; IL-11R-alpha; IL-11R subunit alpha; IL-11 receptor subunit alpha	IL11RA	"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."	.	.	MSSSCSGLSRVLVAVATALVSASSPCPQAWGPPGVQYGQPGRSVKLCCPGVTAGDPVSWFRDGEPKLLQGPDSGLGHELVLAQADSTDEGTYICQTLDGALGGTVTLQLGYPPARPVVSCQAADYENFSCTWSPSQISGLPTRYLTSYRKKTVLGADSQRRSPSTGPWPCPQDPLGAARCVVHGAEFWSQYRINVTEVNPLGASTRLLDVSLQSILRPDPPQGLRVESVPGYPRRLRASWTYPASWPCQPHFLLKFRLQYRPAQHPAWSTVEPAGLEEVITDAVAGLPHAVRVSARDFLDAGTWSTWSPEAWGTPSTGTIPKEIPAWGQLHTQPEVEPQVDSPAPPRPSLQPHPRLLDHRDSVEQVAVLASLGILSFLGLVAGALALGLWLRLRRGGKDGSPKPGFLASVIPVDRRPGAPNL	Successful	Oprelvekin: a review of its pharmacology and therapeutic potential in chemotherapy-induced thrombocytopenia. BioDrugs. 1998 Aug;10(2):159-71.	34	Cytokine receptor	.	type I cytokine receptor family. Type 3 subfamily.	.	.	.	.	.	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage	R-HSA-6788467: IL-6-type cytokine receptor ligand interactions	.	Q14626
TTRTK6Y	Interleukin-12 alpha (IL12A)	P29459	IL12A_HUMAN	Cytokine: interleukin	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	IL12A	"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."	.	3HMX; 1F45	MCPARSLLLVATLVLLDHLSLARNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLPLELTKNESCLNSRETSFITNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS	Successful	Hughes B: 2009 FDA drug approvals. Nat Rev Drug Discov. 2010 Feb;9(2):89-92.	34	Cytokine	Interleukin	IL-6 superfamily.	.	.	Interleukin-12 alpha subunit	PF03039	PF03039; IL12	.	.	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	R-HSA-6783783: Interleukin-10 signaling; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-8984722: Interleukin-35 Signalling; R-HSA-9020591: Interleukin-12 signaling	.	P29459
TTGW72V	Interleukin-12 beta (IL12B)	P29460	IL12B_HUMAN	Cytokine: interleukin	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	IL12B	"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."	.	5NJD; 5MZV; 5MXA; 5MJ4; 5MJ3	MCHQQLVISWFSLVFLASPLVAIWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEWASVPCS	Successful	"A phase 1 study of AS1409, a novel antibody-cytokine fusion protein, in patients with malignant melanoma or renal cell carcinoma. Clin Cancer Res. 2011 Apr 1;17(7):1998-2005."	34	Cytokine	Cytokine: interleukin	type I cytokine receptor family. Type 3 subfamily.	.	.	Cytokine interleukin-12p40 C-terminus	PF10420	PF10420; IL12p40_C	.	.	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	R-HSA-6783783: Interleukin-10 signaling; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9020591: Interleukin-12 signaling; R-HSA-9020933: Interleukin-23 signaling	.	P29460
TT4SWR8	Interleukin 12 receptor beta-2 (IL12RB2)	Q99665	I12R2_HUMAN	Cytokine receptor	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	IL12RB2	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.	.	.	MAHTFRGCSLAFMFIITWLLIKAKIDACKRGDVTVKPSHVILLGSTVNITCSLKPRQGCFHYSRRNKLILYKFDRRINFHHGHSLNSQVTGLPLGTTLFVCKLACINSDEIQICGAEIFVGVAPEQPQNLSCIQKGEQGTVACTWERGRDTHLYTEYTLQLSGPKNLTWQKQCKDIYCDYLDFGINLTPESPESNFTAKVTAVNSLGSSSSLPSTFTFLDIVRPLPPWDIRIKFQKASVSRCTLYWRDEGLVLLNRLRYRPSNSRLWNMVNVTKAKGRHDLLDLKPFTEYEFQISSKLHLYKGSWSDWSESLRAQTPEEEPTGMLDVWYMKRHIDYSRQQISLFWKNLSVSEARGKILHYQVTLQELTGGKAMTQNITGHTSWTTVIPRTGNWAVAVSAANSKGSSLPTRINIMNLCEAGLLAPRQVSANSEGMDNILVTWQPPRKDPSAVQEYVVEWRELHPGGDTQVPLNWLRSRPYNVSALISENIKSYICYEIRVYALSGDQGGCSSILGNSKHKAPLSGPHINAITEEKGSILISWNSIPVQEQMGCLLHYRIYWKERDSNSQPQLCEIPYRVSQNSHPINSLQPRVTYVLWMTALTAAGESSHGNEREFCLQGKANWMAFVAPSICIAIIMVGIFSTHYFQQKVFVLLAALRPQWCSREIPDPANSTCAKKYPIAEEKTQLPLDRLLIDWPTPEDPEPLVISEVLHQVTPVFRHPPCSNWPQREKGIQGHQASEKDMMHSASSPPPPRALQAESRQLVDLYKVLESRGSDPKPENPACPWTVLPAGDLPTHDGYLPSNIDDLPSHEAPLADSLEELEPQHISLSVFPSSSLHPLTFSCGDKLTLDQLKMRCDSLML	Literature-reported	Biomarkers for chronic fatigue. Brain Behav Immun. 2012 Nov;26(8):1202-10. 	.	Cytokine receptor	Transmembrane protein	type I cytokine receptor family. Type 2 subfamily.	.	.	Fibronectin type III domain; Ig-like C2-type domain	PF00041; PF06328	PF00041; fn3; PF06328; Lep_receptor_Ig	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04630: JAK-STAT signaling pathway; hsa04658: Th1 and Th2 cell differentiation; hsa05200: Pathways in cancer; hsa05321: Inflammatory bowel disease	R-HSA-8984722: Interleukin-35 Signalling; R-HSA-9020591: Interleukin-12 signaling	.	Q99665
TT0GVCH	Interleukin-13 (IL13)	P35225	IL13_HUMAN	Cytokine: interleukin	NC30; IL-13	IL13	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.	.	5L6Y; 5E4E; 4PS4; 4I77; 3LB6	MHPLLNPLLLALGLMALLLTTVIALTCLGGFASPGPVPPSTALRELIEELVNITQNQKAPLCNGSMVWSINLTAGMYCAALESLINVSGCSAIEKTQRMLSGFCPHKVSAGQFSSLHVRDTKIEVAQFVKDLLLHLKKLFREGRFN	Clinical trial	The potential of biologics for the treatment of asthma. Nat Rev Drug Discov. 2012 Dec;11(12):958-72. 	25	Cytokine	Interleukin	IL-4/IL-13 family.	.	.	Interleukin-13	PF03487	PF03487; IL13	.	.	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)	R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9012546: Interleukin-18 signaling	.	P35225
TTNEAMG	Interleukin 13 receptor alpha-1 (IL13RA1)	P78552	I13R1_HUMAN	Cytokine receptor	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	IL13RA1	"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)."	.	5E4E; 4HWB; 3BPO; 3BPN	MEWPARLCGLWALLLCAGGGGGGGGAAPTETQPPVTNLSVSVENLCTVIWTWNPPEGASSNCSLWYFSHFGDKQDKKIAPETRRSIEVPLNERICLQVGSQCSTNESEKPSILVEKCISPPEGDPESAVTELQCIWHNLSYMKCSWLPGRNTSPDTNYTLYYWHRSLEKIHQCENIFREGQYFGCSFDLTKVKDSSFEQHSVQIMVKDNAGKIKPSFNIVPLTSRVKPDPPHIKNLSFHNDDLYVQWENPQNFISRCLFYEVEVNNSQTETHNVFYVQEAKCENPEFERNVENTSCFMVPGVLPDTLNTVRIRVKTNKLCYEDDKLWSNWSQEMSIGKKRNSTLYITMLLIVPVIVAGAIIVLLLYLKRLKIIIFPPIPDPGKIFKEMFGDQNDDTLHWKKYDIYEKQTKEETDSVVLIENLKKASQ	Literature-reported	Receptor for interleukin 13 is a marker and therapeutic target for human high-grade gliomas. Clin Cancer Res. 1999 May;5(5):985-90.	.	Cytokine receptor	Cytokine receptor	type I cytokine receptor family. Type 5 subfamily.	.	.	"Interleukin-13 receptor subunit alpha Ig-like domain; Interleukin-6 receptor alpha chain, binding"	PF18001; PF09240	PF18001; Il13Ra_Ig; PF09240; IL6Ra-bind	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04630: JAK-STAT signaling pathway; hsa05200: Pathways in cancer	R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling	.	P78552
TTMPZ7V	Interleukin 13 receptor alpha-2 (IL13RA2)	Q14627	I13R2_HUMAN	Cytokine receptor	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	IL13RA2	"Binds as a monomer with high affinity to interleukin-13 (IL13), but not to interleukin-4 (IL4)."	.	3LB6	MAFVCLAIGCLYTFLISTTFGCTSSSDTEIKVNPPQDFEIVDPGYLGYLYLQWQPPLSLDHFKECTVEYELKYRNIGSETWKTIITKNLHYKDGFDLNKGIEAKIHTLLPWQCTNGSEVQSSWAETTYWISPQGIPETKVQDMDCVYYNWQYLLCSWKPGIGVLLDTNYNLFYWYEGLDHALQCVDYIKADGQNIGCRFPYLEASDYKDFYICVNGSSENKPIRSSYFTFQLQNIVKPLPPVYLTFTRESSCEIKLKWSIPLGPIPARCFDYEIEIREDDTTLVTATVENETYTLKTTNETRQLCFVVRSKVNIYCSDDGIWSEWSDKQCWEGEDLSKKTLLRFWLPFGFILILVIFVTGLLLRKPNTYPKMIPEFFCDT	Clinical trial	"Clinical pipeline report, company report or official report of ImmunoCellular Therapeutics."	25	Cytokine receptor	.	type I cytokine receptor family. Type 5 subfamily.	.	.	"Interleukin-6 receptor alpha chain, binding"	PF09240	PF09240; IL6Ra-bind	.	.	hsa04630:Jak-STAT signaling pathway	R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling	.	Q14627
TTJFA35	Interleukin-15 (IL15)	P40933	IL15_HUMAN	Cytokine: interleukin	IL-15	IL15	"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."	.	4GS7; 2Z3R; 2Z3Q; 2XQB	MRISKPHLRSISIQCYLCLLLNSHFLTEAGIHVFILGCFSAGLPKTEANWVNVISDLKKIEDLIQSMHIDATLYTESDVHPSCKVTAMKCFLLELQVISLESGDASIHDTVENLIILANNSLSSNGNVTESGCKECEELEEKNIKEFLQSFVHIVQMFINTS	Clinical trial	Emerging drugs for rheumatoid arthritis. Expert Opin Emerg Drugs. 2008 Mar;13(1):175-96.	21	Cytokine	.	IL-15/IL-21 family.	.	.	Interleukin 15	PF02372	PF02372; IL15	.	.	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	R-HSA-8983432: Interleukin-15 signaling	.	P40933
TTGN89I	Interleukin 15 receptor alpha (IL15RA)	Q13261	I15RA_HUMAN	Cytokine receptor	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	IL15RA	"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."	.	4GS7; 2Z3R; 2Z3Q; 2ERS	MAPRRARGCRTLGLPALLLLLLLRPPATRGITCPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKATNVAHWTTPSLKCIRDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKEPAASSPSSNNTAATTAAIVPGSQLMPSKSPSTGTTEISSHESSHGTPSQTTAKNWELTASASHQPPGVYPQGHSDTTVAISTSTVLLCGLSAVSLLACYLKSRQTPPLASVEMEAMEALPVTWGTSSRDEDLENCSHHL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	Cytokine receptor	.	.	.	.	.	.	.	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa04672:Intestinal immune network for IgA production; hsa05166:HTLV-I infection	R-HSA-8983432: Interleukin-15 signaling	.	Q13261
TTW4R0B	Interleukin-16 (IL16)	Q14005	IL16_HUMAN	Cytokine: interleukin	Prointerleukin16; Pro-interleukin-16; LCF; Interleukin16	IL16	"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."	.	5FB8; 1X6D; 1I16	MESHSRAGKSRKSAKFRSISRSLMLCNAKTSDDGSSPDEKYPDPFEISLAQGKEGIFHSSVQLADTSEAGPSSVPDLALASEAAQLQAAGNDRGKTCRRIFFMKESSTASSREKPGKLEAQSSNFLFPKACHQRARSNSTSVNPYCTREIDFPMTKKSAAPTDRQPYSLCSNRKSLSQQLDCPAGKAAGTSRPTRSLSTAQLVQPSGGLQASVISNIVLMKGQAKGLGFSIVGGKDSIYGPIGIYVKTIFAGGAAAADGRLQEGDEILELNGESMAGLTHQDALQKFKQAKKGLLTLTVRTRLTAPPSLCSHLSPPLCRSLSSSTCITKDSSSFALESPSAPISTAKPNYRIMVEVSLQKEAGVGLGIGLCSVPYFQCISGIFVHTLSPGSVAHLDGRLRCGDEIVEISDSPVHCLTLNEVYTILSHCDPGPVPIIVSRHPDPQVSEQQLKEAVAQAVENTKFGKERHQWSLEGVKRLESSWHGRPTLEKEREKNSAPPHRRAQKVMIRSSSDSSYMSGSPGGSPGSGSAEKPSSDVDISTHSPSLPLAREPVVLSIASSRLPQESPPLPESRDSHPPLRLKKSFEILVRKPMSSKPKPPPRKYFKSDSDPQKSLEERENSSCSSGHTPPTCGQEARELLPLLLPQEDTAGRSPSASAGCPGPGIGPQTKSSTEGEPGWRRASPVTQTSPIKHPLLKRQARMDYSFDTTAEDPWVRISDCIKNLFSPIMSENHGHMPLQPNASLNEEEGTQGHPDGTPPKLDTANGTPKVYKSADSSTVKKGPPVAPKPAWFRQSLKGLRNRASDPRGLPDPALSTQPAPASREHLGSHIRASSSSSSIRQRISSFETFGSSQLPDKGAQRLSLQPSSGEAAKPLGKHEEGRFSGLLGRGAAPTLVPQQPEQVLSSGSPAASEARDPGVSESPPPGRQPNQKTLPPGPDPLLRLLSTQAEESQGPVLKMPSQRARSFPLTRSQSCETKLLDEKTSKLYSISSQVSSAVMKSLLCLPSSISCAQTPCIPKEGASPTSSSNEDSAANGSAETSALDTGFSLNLSELREYTEGLTEAKEDDDGDHSSLQSGQSVISLLSSEELKKLIEEVKVLDEATLKQLDGIHVTILHKEEGAGLGFSLAGGADLENKVITVHRVFPNGLASQEGTIQKGNEVLSINGKSLKGTTHHDALAILRQAREPRQAVIVTRKLTPEAMPDLNSSTDSAASASAASDVSVESTAEATVCTVTLEKMSAGLGFSLEGGKGSLHGDKPLTINRIFKGAASEQSETVQPGDEILQLGGTAMQGLTRFEAWNIIKALPDGPVTIVIRRKSLQSKETTAAGDS	Literature-reported	Biomarkers in bronchopulmonary dysplasia. Paediatr Respir Rev. 2013 Sep;14(3):173-9. 	.	Cytokine	.	.	.	.	PDZ domain	PF00595	PF00595; PDZ	.	.	hsa04060: Cytokine-cytokine receptor interaction	R-HSA-449836: Other interleukin signaling	.	Q14005
TTG0MT6	Interleukin-17 (IL17)	Q16552	IL17_HUMAN	Cytokine: interleukin	Interleukin-17A; IL-17A; IL-17; Cytotoxic T-lymphocyte-associated antigen 8; Cytotoxic T lymphocyte-associated antigen 8; CTLA8; CTLA-8	IL17A	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.	.	5VB9; 5NAN; 5N92; 5N7W; 5HI5	MTPGKTSLVSLLLLLSLEAIVKAGITIPRNPGCPNSEDKNFPRTVMVNLNIHNRNTNTNPKRSSDYYNRSTSPWNLHRNEDPERYPSVIWEAKCRHLGCINADGNVDYHMNSVPIQQEILVLRREPPHCPNSFRLEKILVSVGCTCVTPIVHHVA	Successful	"Brodalumab and ixekizumab, anti-interleukin-17-receptor antibodies for psoriasis: a critical appraisal. Br J Dermatol. 2012 Oct;167(4):710-3; discussion 714-5."	34	Cytokine	Interleukin	IL-17 family.	.	.	Interleukin-17	PF06083	PF06083; IL17	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis	R-HSA-448424: Interleukin-17 signaling; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses	.	Q16552
TTC5LTG	Interleukin-27 (IL27)	Q8TAD2	IL17D_HUMAN	Cytokine: interleukin	UNQ3096/PRO21175; Interleukin27; Interleukin17D; Interleukin-17D; IL-27; IL-17D	IL17D	"Induces expression of IL6, CXCL8/IL8, and CSF2/GM-CSF from endothelial cells."	.	.	MLVAGFLLALPPSWAAGAPRAGRRPARPRGCADRPEELLEQLYGRLAAGVLSAFHHTLQLGPREQARNASCPAGGRPADRRFRPPTNLRSVSPWAYRISYDPARYPRYLPEAYCLCRGCLTGLFGEEDVRFRSAPVYMPTVVLRRTPACAGGRSVYTEAYVTIPVGCTCVPEPEKDADSINSSIDKQGAKLLLGPNDAPAGP	Clinical trial	IL-27-induced modulation of autoimmunity and its therapeutic potential. Autoimmun Rev. 2015 Dec;14(12):1131-1141.	.	Cytokine	.	IL-17 family.	.	.	Interleukin-17	PF06083	PF06083; IL17	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04625: C-type lectin receptor signaling pathway; hsa04630: JAK-STAT signaling pathway; hsa04657: IL-17 signaling pathway	.	.	Q8TAD2
TT2B6PS	Cytokine ML-1 (IL17F)	Q96PD4	IL17F_HUMAN	Cytokine: interleukin	Interleukin-17F; IL-17F	IL17F	"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."	.	5NAN; 5N92; 3JVF; 1JPY	MTVKTLHGPAMVKYLLLSILGLAFLSEAAARKIPKVGHTFFQKPESCPPVPGGSMKLDIGIINENQRVSMSRNIESRSTSPWNYTVTWDPNRYPSEVVQAQCRNLGCINAQGKEDISMNSVPIQQETLVVRRKHQGCSVSFQLEKVLVTVGCTCVTPVIHHVQ	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	Cytokine	.	IL-17 family.	.	.	Interleukin-17	PF06083	PF06083; IL17	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04657:IL-17 signaling pathway; hsa04659:Th17 cell differentiation; hsa05321:Inflammatory bowel disease (IBD)	R-HSA-448424: Interleukin-17 signaling; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses	.	Q96PD4
TT69OHW	Interleukin 17 receptor (IL17R)	Q96F46; Q9NRM6; Q9NRM6; Q8NFM7; Q8NFR9	I17RA_HUMAN; I17RB_HUMAN; I17RC_HUMAN; I17RD_HUMAN; I17RE_HUMAN	Cytokine receptor	Interleukin-17 receptor; IL-17R; IL-17 receptor	IL17RA	"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."	.	.	MGAARSPPSAVPGPLLGLLLLLLGVLAPGGASLRLLDHRALVCSQPGLNCTVKNSTCLDDSWIHPRNLTPSSPKDLQIQLHFAHTQQGDLFPVAHIEWTLQTDASILYLEGAELSVLQLNTNERLCVRFEFLSKLRHHHRRWRFTFSHFVVDPDQEYEVTVHHLPKPIPDGDPNHQSKNFLVPDCEHARMKVTTPCMSSGSLWDPNITVETLEAHQLRVSFTLWNESTHYQILLTSFPHMENHSCFEHMHHIPAPRPEEFHQRSNVTLTLRNLKGCCRHQVQIQPFFSSCLNDCLRHSATVSCPEMPDTPEPIPDYMPLWVYWFITGISILLVGSVILLIVCMTWRLAGPGSEKYSDDTKYTDGLPAADLIPPPLKPRKVWIIYSADHPLYVDVVLKFAQFLLTACGTEVALDLLEEQAISEAGVMTWVGRQKQEMVESNSKIIVLCSRGTRAKWQALLGRGAPVRLRCDHGKPVGDLFTAAMNMILPDFKRPACFGTYVVCYFSEVSCDGDVPDLFGAAPRYPLMDRFEEVYFRIQDLEMFQPGRMHRVGELSGDNYLRSPGGRQLRAALDRFRDWQVRCPDWFECENLYSADDQDAPSLDEEVFEEPLLPPGTGIVKRAPLVREPGSQACLAIDPLVGEEGGAAVAKLEPHLQPRGQPAPQPLHTLVLAAEEGALVAAVEPGPLADGAAVRLALAGEGEACPLLGSPGAGRNSVLFLPVDPEDSPLGSSTPMASPDLLPEDVREHLEGLMLSLFEQSLSCQAQGGCSRPAMVLTDPHTPYEEEQRQSVQSDQGYISRSSPQPPEGLTEMEEEEEEEQDPGKPALPLSPEDLESLRSLQRQLLFRQLQKNSGWDTMGSESEGPSA	Successful	2017 FDA drug approvals.Nat Rev Drug Discov. 2018 Feb;17(2):81-85. 	34	.	.	.	.	.	.	.	.	.	.	hsa04060:Cytokine-cytokine receptor interaction	R-HSA-448424: Interleukin-17 signaling; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses	.	Q96F46
TTRICUF	Interleukin-18 (IL18)	Q14116	IL18_HUMAN	Cytokine: interleukin	Interleukin-1 gamma; Interferon-gamma inducing factor; Interferon gamma-inducing factor; Iboctadekin; IL1F4; IL-18; IL-1 gamma; IGIF; IFN-gamma-inducing factor	IL18	"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."	.	4XFU; 4XFT; 4XFS; 4R6U; 4HJJ	MAAEPVEDNCINFVAMKFIDNTLYFIAEDDENLESDYFGKLESKLSVIRNLNDQVLFIDQGNRPLFEDMTDSDCRDNAPRTIFIISMYKDSQPRGMAVTISVKCEKISTLSCENKIISFKEMNPPDNIKDTKSDIIFFQRSVPGHDNKMQFESSSYEGYFLACEKERDLFKLILKKEDELGDRSIMFTVQNED	Clinical trial	Targeting the IL-1 family members in skin inflammation. Curr Opin Investig Drugs. 2010 November; 11(11): 1211-1220.	21	Cytokine	Interleukin	IL-1 family.	.	.	Interleukin-1 / 18	PF00340	PF00340; IL1	.	.	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	R-HSA-448706:Interleukin-1 processing	.	Q14116
TTZUJVE	Interleukin 18 receptor (IL18RAP)	O95256	I18RA_HUMAN	Cytokine receptor	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	IL18RAP	"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."	.	3WO4	MLCLGWIFLWLVAGERIKGFNISGCSTKKLLWTYSTRSEEEFVLFCDLPEPQKSHFCHRNRLSPKQVPEHLPFMGSNDLSDVQWYQQPSNGDPLEDIRKSYPHIIQDKCTLHFLTPGVNNSGSYICRPKMIKSPYDVACCVKMILEVKPQTNASCEYSASHKQDLLLGSTGSISCPSLSCQSDAQSPAVTWYKNGKLLSVERSNRIVVDEVYDYHQGTYVCDYTQSDTVSSWTVRAVVQVRTIVGDTKLKPDILDPVEDTLEVELGKPLTISCKARFGFERVFNPVIKWYIKDSDLEWEVSVPEAKSIKSTLKDEIIERNIILEKVTQRDLRRKFVCFVQNSIGNTTQSVQLKEKRGVVLLYILLGTIGTLVAVLAASALLYRHWIEIVLLYRTYQSKDQTLGDKKDFDAFVSYAKWSSFPSEATSSLSEEHLALSLFPDVLENKYGYSLCLLERDVAPGGVYAEDIVSIIKRSRRGIFILSPNYVNGPSIFELQAAVNLALDDQTLKLILIKFCYFQEPESLPHLVKKALRVLPTVTWRGLKSVPPNSRFWAKMRYHMPVKNSQGFTWNQLRITSRIFQWKGLSRTETTGRSSQPKEW	Literature-reported	Parasites represent a major selective force for interleukin genes and shape the genetic predisposition to autoimmune conditions. J Exp Med. 2009 Jun 8;206(6):1395-408.	.	Cytokine receptor	.	interleukin-1 receptor family.	.	.	Immunoglobulin domain; Immunoglobulin domain; TIR domain	PF13895; PF18452; PF01582	PF13895; Ig_2; PF18452; Ig_6; PF01582; TIR	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa05321: Inflammatory bowel disease	R-HSA-9012546: Interleukin-18 signaling	.	O95256
TT87RWS	Interleukin-19 (IL19)	Q9UHD0	IL19_HUMAN	Cytokine: interleukin	ZMDA1; NG.1; Melanoma differentiation-associated protein-like protein; IL-19	IL19	Up-regulates IL-6 and TNF-alpha and induces apoptosis. May play some important roles in inflammatory responses.	.	1N1F	MKLQCVSLWLLGTILILCSVDNHGLRRCLISTDMHHIEESFQEIKRAIQAKDTFPNVTILSTLETLQIIKPLDVCCVTKNLLAFYVDRVFKDHQEPNPKILRKISSIANSFLYMQKTLRQCQEQRQCHCRQEATNATRVIHDNYDQLEVHAAAIKSLGELDVFLAWINKNHEVMFSA	Literature-reported	Interleukin-19 contributes as a protective factor in experimental Th2-mediated colitis. Naunyn Schmiedebergs Arch Pharmacol. 2017 Mar;390(3):261-268.	.	Cytokine	.	IL-10 family.	.	.	Interleukin 10	PF00726	PF00726; IL10	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04630: JAK-STAT signaling pathway	R-HSA-8854691: Interleukin-20 family signaling	.	Q9UHD0
TTPM6HI	Interleukin-1 alpha (IL1A)	P01583	IL1A_HUMAN	Cytokine: interleukin	IL1F1; IL-1 alpha; Hematopoietin-1	IL1A	"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."	.	5UC6; 2L5X; 2KKI; 2ILA; 1ITA	MAKVPDMFEDLKNCYSENEEDSSSIDHLSLNQKSFYHVSYGPLHEGCMDQSVSLSISETSKTSKLTFKESMVVVATNGKVLKKRRLSLSQSITDDDLEAIANDSEEEIIKPRSAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAVKFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITGSETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILENQA	Clinical trial	"Generation and characterization of ABT-981, a dual variable domain immunoglobulin (DVD-Ig(TM)) molecule that specifically and potently neutralizes both IL-1alpha and IL-1beta. MAbs. 2015;7(3):605-19."	21	Cytokine	Interleukin	IL-1 family.	.	.	Interleukin-1 / 18; Interleukin-1 propeptide	PF00340; PF02394	PF00340; IL1; PF02394; IL1_propep	1.A.109.1.1	The Interleukin 1 (IL1) Family	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	R-HSA-2559582:Senescence-Associated Secretory Phenotype (SASP); R-HSA-446652:Interleukin-1 signaling; R-HSA-448706:Interleukin-1 processing	.	P01583
TTRYK0X	Interleukin-1 beta (IL1B)	P01584	IL1B_HUMAN	Cytokine: interleukin	IL1F2; IL-1beta; IL-1 beta; Catabolin	IL1B	"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."	.	9ILB; 7I1B; 6I1B; 5MVZ; 5I1B	MAEVPELASEMMAYYSGNEDDLFFEADGPKQMKCSFQDLDLCPLDGGIQLRISDHHYSKGFRQAASVVVAMDKLRKMLVPCPQTFQENDLSTFFPFIFEEEPIFFDTWDNEAYVHDAPVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS	Successful	"Elimination of arthritis pain and inflammation for over 2 years with a single 90 min, topical 14% gallium nitrate treatment: case reports and revie... Med Hypotheses. 2005;65(6):1136-41."	34	Cytokine	Interleukin	IL-1 family.	.	.	Interleukin-1 / 18; Interleukin-1 propeptide	PF00340; PF02394	PF00340; IL1; PF02394; IL1_propep	1.A.109.1.2	The Interleukin 1 (IL1) Family	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	R-HSA-446652:Interleukin-1 signaling; R-HSA-448706:Interleukin-1 processing; R-HSA-5660668:CLEC7A/inflammasome pathway	.	P01584
TTBJZ7D	HUMAN interleukin-1 beta (IL1B)	P01584	IL1B_HUMAN	Cytokine: interleukin	IL1F2; IL-1beta; IL-1 beta; Catabolin	IL1B	"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."	.	9ILB; 7I1B; 6I1B; 5MVZ; 5I1B	MAEVPELASEMMAYYSGNEDDLFFEADGPKQMKCSFQDLDLCPLDGGIQLRISDHHYSKGFRQAASVVVAMDKLRKMLVPCPQTFQENDLSTFFPFIFEEEPIFFDTWDNEAYVHDAPVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS	.	"ClinicalTrials.gov (NCT04363008) COVID-19 Inflammatory Blood Biomarkers for Clinical Management, Prognosis and Evaluation of Interventions"	34	Cytokine	Interleukin	IL-1 family.	.	.	Interleukin-1 / 18; Interleukin-1 propeptide	PF00340; PF02394	PF00340; IL1; PF02394; IL1_propep	1.A.109.1.2	The Interleukin 1 (IL1) Family	hsa01523: Antifolate resistance; hsa04010: MAPK signaling pathway; hsa04060: Cytokine-cytokine receptor interaction; hsa04064: NF-kappa B signaling pathway; hsa04217: Necroptosis; hsa04380: Osteoclast differentiation; hsa04620: Toll-like receptor signaling pathway; hsa04621: NOD-like receptor signaling pathway; hsa04623: Cytosolic DNA-sensing pathway; hsa04625: C-type lectin receptor signaling pathway; hsa04640: Hematopoietic cell lineage; hsa04657: IL-17 signaling pathway; hsa04659: Th17 cell differentiation; hsa04668: TNF signaling pathway; hsa04750: Inflammatory mediator regulation of TRP channels; hsa04932: Non-alcoholic fatty liver disease; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04936: Alcoholic liver disease; hsa04940: Type I diabetes mellitus; hsa05010: Alzheimer disease; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05133: Pertussis; hsa05134: Legionellosis; hsa05135: Yersinia infection; hsa05140: Leishmaniasis; hsa05142: Chagas disease; hsa05143: African trypanosomiasis; hsa05144: Malaria; hsa05146: Amoebiasis; hsa05152: Tuberculosis; hsa05162: Measles; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; hsa05168: Herpes simplex virus 1 infection; hsa05171: Coronavirus disease - COVID-19; hsa05321: Inflammatory bowel disease; hsa05323: Rheumatoid arthritis; hsa05332: Graft-versus-host disease; hsa05417: Lipid and atherosclerosis; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-448706: Interleukin-1 processing; R-HSA-5620971: Pyroptosis; R-HSA-5660668: CLEC7A/inflammasome pathway; R-HSA-6783783: Interleukin-10 signaling; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9020702: Interleukin-1 signaling; R-HSA-9660826: Purinergic signaling in leishmaniasis infection	.	P01584
TTWOTEA	Interleukin 1 receptor type 1 (IL1R1)	P14778	IL1R1_HUMAN	Cytokine receptor	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	IL1R1	"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."	.	4GAF; 4DEP; 1ITB; 1IRA; 1G0Y	MKVLLRLICFIALLISSLEADKCKEREEKIILVSSANEIDVRPCPLNPNEHKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSYCLRIKISAKFVENEPNLCYNAQAIFKQKLPVAGDGGLVCPYMEFFKNENNELPKLQWYKDCKPLLLDNIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLEENKPTRPVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRFYKHPFTCFAKNTHGIDAAYIQLIYPVTNFQKHMIGICVTLTVIIVCSVFIYKIFKIDIVLWYRDSCYDFLPIKASDGKTYDAYILYPKTVGEGSTSDCDIFVFKVLPEVLEKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSWLGGSSEEQIAMYNALVQDGIKVVLLELEKIQDYEKMPESIKFIKQKHGAIRWSGDFTQGPQSAKTRFWKNVRYHMPVQRRSPSSKHQLLSPATKEKLQREAHVPLG	Successful	IL-1 receptor antagonism and muscle gene expression in patients with type 2 diabetes. Eur Cytokine Netw. 2009 Jun 1;20(2):81-87.	34	Cytokine receptor	Immunoglobulin	interleukin-1 receptor family.	.	.	Immunoglobulin domain; Immunoglobulin domain; TIR domain	PF13895; PF18452; PF01582	PF13895; Ig_2; PF18452; Ig_6; PF01582; TIR	8.A.23.1.11	The Basigin (Basigin) Family	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	R-HSA-446652:Interleukin-1 signaling	.	P14778
TTT7FOP	HUMAN interleukin-1 receptor 1 (IL1R1)	P14778	IL1R1_HUMAN	Cytokine receptor	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	IL1R1	"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."	.	4GAF; 4DEP; 1ITB; 1IRA; 1G0Y	MKVLLRLICFIALLISSLEADKCKEREEKIILVSSANEIDVRPCPLNPNEHKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSYCLRIKISAKFVENEPNLCYNAQAIFKQKLPVAGDGGLVCPYMEFFKNENNELPKLQWYKDCKPLLLDNIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLEENKPTRPVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRFYKHPFTCFAKNTHGIDAAYIQLIYPVTNFQKHMIGICVTLTVIIVCSVFIYKIFKIDIVLWYRDSCYDFLPIKASDGKTYDAYILYPKTVGEGSTSDCDIFVFKVLPEVLEKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSWLGGSSEEQIAMYNALVQDGIKVVLLELEKIQDYEKMPESIKFIKQKHGAIRWSGDFTQGPQSAKTRFWKNVRYHMPVQRRSPSSKHQLLSPATKEKLQREAHVPLG	.	FDA Approved Drug Products from FDA Official Website. 2019. Application Number: (BLA) 125166.	.	.	.	.	.	.	.	.	.	.	.	hsa04010: MAPK signaling pathway; hsa04060: Cytokine-cytokine receptor interaction; hsa04064: NF-kappa B signaling pathway; hsa04380: Osteoclast differentiation; hsa04640: Hematopoietic cell lineage; hsa04659: Th17 cell differentiation; hsa04750: Inflammatory mediator regulation of TRP channels; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05146: Amoebiasis; hsa05163: Human cytomegalovirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-6783783: Interleukin-10 signaling; R-HSA-9020702: Interleukin-1 signaling; R-HSA-9679191: Potential therapeutics for SARS	.	P14778
TT5BFT0	Interleukin-1 receptor (IL1R)	P14778; P27930	IL1R1_HUMAN; IL1R2_HUMAN	.	.	IL1R1	.	.	.	.	Clinical trial	"Multicenter Study of a Novel Topical Interleukin-1 Receptor Inhibitor, Isunakinra, in Subjects With Moderate to Severe Dry Eye Disease. Eye Contact Lens. 2017 Sep;43(5):287-296."	.	.	.	.	.	.	.	.	.	.	.	hsa04010: MAPK signaling pathway; hsa04060: Cytokine-cytokine receptor interaction; hsa04064: NF-kappa B signaling pathway; hsa04380: Osteoclast differentiation; hsa04640: Hematopoietic cell lineage; hsa04659: Th17 cell differentiation; hsa04750: Inflammatory mediator regulation of TRP channels; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05146: Amoebiasis; hsa05163: Human cytomegalovirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-6783783: Interleukin-10 signaling; R-HSA-9020702: Interleukin-1 signaling; R-HSA-9679191: Potential therapeutics for SARS	.	P14778
TT51DEV	Interleukin 1 receptor type 2 (IL1R2)	P27930	IL1R2_HUMAN	Cytokine receptor	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	IL1R2	"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."	.	3O4O	MLRLYVLVMGVSAFTLQPAAHTGAARSCRFRGRHYKREFRLEGEPVALRCPQVPYWLWASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMSIELRVFENTDAFLPFISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQYNITRSIELRIKKKKEETIPVIISPLKTISASLGSRLTIPCKVFLGTGTPLTTMLWWTANDTHIESAYPGGRVTEGPRQEYSENNENYIEVPLIFDPVTREDLHMDFKCVVHNTLSFQTLRTTVKEASSTFSWGIVLAPLSLAFLVLGGIWMHRRCKHRTGKADGLTVLWPHHQDFQSYPK	Clinical trial	"WO patent application no. 2013,0077,63, Modulators of the nlrp3 inflammasome il-1ss pathway for the prevention and treatment of acne."	17	Cytokine receptor	.	interleukin-1 receptor family.	.	.	Immunoglobulin domain; Immunoglobulin domain	PF00047; PF18452	PF00047; ig; PF18452; Ig_6	.	.	hsa04010:MAPK signaling pathway; hsa04060:Cytokine-cytokine receptor interaction; hsa04640:Hematopoietic cell lineage; hsa05146:Amoebiasis; hsa05166:HTLV-I infection; hsa05202:Transcriptional misregulation in cancer	R-HSA-446652:Interleukin-1 signaling	.	P27930
TTWS50K	Interleukin 1 receptor accessory protein (IL1RAP)	Q9NPH3	IL1AP_HUMAN	Cytokine receptor	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	IL1RAP	"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."	.	4DEP; 3O4O	MTLLWCVVSLYFYGILQSDASERCDDWGLDTMRQIQVFEDEPARIKCPLFEHFLKFNYSTAHSAGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSPMKLPVHKLYIEYGIQRITCPNVDGYFPSSVKPTITWYMGCYKIQNFNNVIPEGMNLSFLIALISNNGNYTCVVTYPENGRTFHLTRTLTVKVVGSPKNAVPPVIHSPNDHVVYEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDITIDVTINESISHSRTEDETRTQILSIKKVTSEDLKRSYVCHARSAKGEVAKAAKVKQKVPAPRYTVELACGFGATVLLVVILIVVYHVYWLEMVLFYRAHFGTDETILDGKEYDIYVSYARNAEEEEFVLLTLRGVLENEFGYKLCIFDRDSLPGGIVTDETLSFIQKSRRLLVVLSPNYVLQGTQALLELKAGLENMASRGNINVILVQYKAVKETKVKELKRAKTVLTVIKWKGEKSKYPQGRFWKQLQVAMPVKKSPRRSSSDEQGLSYSSLKNV	Clinical trial	Antibodies targeting human IL1RAP (IL1R3) show therapeutic effects in xenograft models of acute myeloid leukemia. Proc Natl Acad Sci U S A. 2015 Aug 25;112(34):10786-91.	.	Cytokine receptor	Interleukin receptor family	interleukin-1 receptor family.	.	.	Immunoglobulin domain; TIR domain	PF18452; PF01582	PF18452; Ig_6; PF01582; TIR	.	.	hsa04010: MAPK signaling pathway; hsa04060: Cytokine-cytokine receptor interaction; hsa04659: Th17 cell differentiation; hsa04750: Inflammatory mediator regulation of TRP channels	"R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-388844: Receptor-type tyrosine-protein phosphatases; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-9014826: Interleukin-36 pathway; R-HSA-9014843: Interleukin-33 signaling; R-HSA-9020702: Interleukin-1 signaling"	.	Q9NPH3
TT4GZA4	Interleukin-1 receptor-like 1 (IL1RL1)	Q01638	ILRL1_HUMAN	.	Protein ST2	IL1RL1	"Receptor for interleukin-33 (IL-33) which plays crucial roles in innate and adaptive immunity, contributing to tissue homeostasis and responses to environmental stresses together with coreceptor IL1RAP (PubMed:35238669). Its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Possibly involved in helper T-cell function (PubMed:16286016) (Probable). Upon tissue injury, induces UCP2-dependent mitochondrial rewiring that attenuates the generation of reactive oxygen species and preserves the integrity of Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages (By similarity). {ECO:0000250|UniProtKB:P14719, ECO:0000269|PubMed:16286016, ECO:0000269|PubMed:35238669, ECO:0000305|PubMed:19836339}.; [Isoform B]: Inhibits IL-33 signaling. {ECO:0000250|UniProtKB:P14719}."	EC 3.2.2.6	4KC3	MGFWILAILTILMYSTAAKFSKQSWGLENEALIVRCPRQGKPSYTVDWYYSQTNKSIPTQERNRVFASGQLLKFLPAAVADSGIYTCIVRSPTFNRTGYANVTIYKKQSDCNVPDYLMYSTVSGSEKNSKIYCPTIDLYNWTAPLEWFKNCQALQGSRYRAHKSFLVIDNVMTEDAGDYTCKFIHNENGANYSVTATRSFTVKDEQGFSLFPVIGAPAQNEIKEVEIGKNANLTCSACFGKGTQFLAAVLWQLNGTKITDFGEPRIQQEEGQNQSFSNGLACLDMVLRIADVKEEDLLLQYDCLALNLHGLRRHTVRLSRKNPIDHHSIYCIIAVCSVFLMLINVLVIILKMFWIEATLLWRDIAKPYKTRNDGKLYDAYVVYPRNYKSSTDGASRVEHFVHQILPDVLENKCGYTLCIYGRDMLPGEDVVTAVETNIRKSRRHIFILTPQITHNKEFAYEQEVALHCALIQNDAKVILIEMEALSELDMLQAEALQDSLQHLMKVQGTIKWREDHIANKRSLNSKFWKHVRYQMPVPSKIPRKASSLTPLAAQKQ	Clinical trial	"Efficacy and safety of GSK3772847 in participants with moderate-to-severe asthma with allergic fungal airway disease: A phase IIa randomized, multicenter, double-blind, sponsor-open, comparative trial. PLoS One. 2023 Feb 3;18(2):e0281205."	.	.	.	.	.	.	.	.	.	.	.	hsa:9173	R-HSA-1257604;R-HSA-6811558;R-HSA-9014843 [Q01638-2];	.	Q01638;
TTUS18T	IL-1 receptor-like 2 (IL1RL2)	Q9HB29	ILRL2_HUMAN	Cytokine receptor	Interleukin-1 receptor-related protein 2; Interleukin-1 receptor-like 2; IL1RRP2; IL1R-rp2; IL-36R; IL-36 receptor; IL-1Rrp2	IL1RL2	"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)."	.	.	MWSLLLCGLSIALPLSVTADGCKDIFMKNEILSASQPFAFNCTFPPITSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIKGRDSCHRIHVNLTVFEKHWCDTSIGGLPNLSDEYKQILHLGKDDSLTCHLHFPKSCVLGPIKWYKDCNEIKGERFTVLETRLLVSNVSAEDRGNYACQAILTHSGKQYEVLNGITVSITERAGYGGSVPKIIYPKNHSIEVQLGTTLIVDCNVTDTKDNTNLRCWRVNNTLVDDYYDESKRIREGVETHVSFREHNLYTVNITFLEVKMEDYGLPFMCHAGVSTAYIILQLPAPDFRAYLIGGLIALVAVAVSVVYIYNIFKIDIVLWYRSAFHSTETIVDGKLYDAYVLYPKPHKESQRHAVDALVLNILPEVLERQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGLLKNLSEEQIAVYSALIQDGMKVILIELEKIEDYTVMPESIQYIKQKHGAIRWHGDFTEQSQCMKTKFWKTVRYHMPPRRCRPFPPVQLLQHTPCYRTAGPELGSRRKKCTLTTG	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	Cytokine receptor	.	interleukin-1 receptor family.	.	.	Immunoglobulin domain; Immunoglobulin domain; TIR domain	PF13895; PF18452; PF01582	PF13895; Ig_2; PF18452; Ig_6; PF01582; TIR	.	.	hsa04060:Cytokine-cytokine receptor interaction	R-HSA-9007892: Interleukin-38 signaling; R-HSA-9014826: Interleukin-36 pathway	.	Q9HB29
TT6GSR3	Interleukin-1 receptor antagonist protein (IL1RN)	P18510	IL1RA_HUMAN	.	IL-1RN; IL-1ra; IRAP; ICIL-1RA; IL1 inhibitor; Anakinra	IL1RN	"Anti-inflammatory antagonist of interleukin-1 family of proinflammatory cytokines such as interleukin-1beta/IL1B and interleukin-1alpha/IL1A. Protects from immune dysregulation and uncontrolled systemic inflammation triggered by IL1 for a range of innate stimulatory agents such as pathogens. {ECO:0000250|UniProtKB:P25085, ECO:0000269|PubMed:7775431}."	.	1ILR;1ILT;1IRA;1IRP;2IRT	MEICRGLRSHLITLLLFLFHSETICRPSGRKSSKMQAFRIWDVNQKTFYLRNNQLVAGYLQGPNVNLEEKIDVVPIEPHALFLGIHGGKMCLSCVKSGDETRLQLEAVNITDLSENRKQDKRFAFIRSDSGPTTSFESAACPGWFLCTAMEADQPVSLTNMPDEGVMVTKFYFQEDE	Clinical trial	"ClinicalTrials.gov (NCT04119687) An Open-Label, Single Ascending Dose Study to Assess the Safety and Tolerability of FX201 in Patients With Osteoarthritis of the Knee. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	hsa:3557	R-HSA-6783783;R-HSA-9020702;	.	P18510;
TTF89GD	Interleukin-2 (IL2)	P60568	IL2_HUMAN	Cytokine: interleukin	TCGF; T-cell growth factor; IL-2; Aldesleukin	IL2	"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."	.	5UTZ; 5M5E; 5LQB; 4NEM; 4NEJ	MYRMQLLSCIALSLALVTNSAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	Cytokine	Interleukin	IL-2 family.	.	.	Interleukin 2	PF00715	PF00715; IL2	.	.	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	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	.	P60568
TTNZMY2	Interleukin-20 (IL20)	Q9NYY1	IL20_HUMAN	Cytokine: interleukin	ZCYTO10; UNQ852/PRO1801; IL-20; Four alpha helix cytokine ZCYTO10; Cytokine Zcyto10	IL20	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.	.	4DOH	MKASSLAFSLLSAAFYLLWTPSTGLKTLNLGSCVIATNLQEIRNGFSEIRGSVQAKDGNIDIRILRRTESLQDTKPANRCCLLRHLLRLYLDRVFKNYQTPDHYTLRKISSLANSFLTIKKDLRLCHAHMTCHCGEEAMKKYSQILSHFEKLEPQAAVVKALGELDILLQWMEETE	Clinical trial	Handbook of Therapeutic Antibodies. 2014. 1. Page(995).	21	Cytokine	.	IL-10 family.	.	.	Interleukin 10	PF00726	PF00726; IL10	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway	R-HSA-8854691: Interleukin-20 family signaling	.	Q9NYY1
TT9QEJ6	Interleukin-21 (IL21)	Q9HBE4	IL21_HUMAN	Cytokine: interleukin	Za11; Interleukin21; IL-21	IL21	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.	.	3TGX; 2OQP	MRSSPGNMERIVICLMVIFLGTLVHKSSSQGQDRHMIRMRQLIDIVDQLKNYVNDLVPEFLPAPEDVETNCEWSAFSCFQKAQLKSANTGNNERIINVSIKKLKRKPPSTNAGRRQKHRLTCPSCDSYEKKPPKEFLERFKSLLQKMIHQHLSSRTHGSEDS	Clinical trial	National Cancer Institute Drug Dictionary (drug id 409696).	21	Cytokine	.	IL-15/IL-21 family.	.	.	Interleukin 15	PF02372	PF02372; IL15	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa05321:Inflammatory bowel disease (IBD)	R-HSA-9020958: Interleukin-21 signaling	.	Q9HBE4
TTZO9B0	Interleukin 21 receptor (IL21R)	Q9HBE5	IL21R_HUMAN	Cytokine receptor	UNQ3121/PRO10273; Novel interleukin receptor; NILR; Interleukin-21 receptor; IL21 receptor; IL-21R; IL-21 receptor; CD360	IL21R	This is a receptor for interleukin-21.	.	4NZD; 3TGX	MPRGWAAPLLLLLLQGGWGCPDLVCYTDYLQTVICILEMWNLHPSTLTLTWQDQYEELKDEATSCSLHRSAHNATHATYTCHMDVFHFMADDIFSVNITDQSGNYSQECGSFLLAESIKPAPPFNVTVTFSGQYNISWRSDYEDPAFYMLKGKLQYELQYRNRGDPWAVSPRRKLISVDSRSVSLLPLEFRKDSSYELQVRAGPMPGSSYQGTWSEWSDPVIFQTQSEELKEGWNPHLLLLLLLVIVFIPAFWSLKTHPLWRLWKKIWAVPSPERFFMPLYKGCSGDFKKWVGAPFTGSSLELGPWSPEVPSTLEVYSCHPPRSPAKRLQLTELQEPAELVESDGVPKPSFWPTAQNSGGSAYSEERDRPYGLVSIDTVTVLDAEGPCTWPCSCEDDGYPALDLDAGLEPSPGLEDPLLDAGTTVLSCGCVSAGSPGLGGPLGSLLDRLKPPLADGEDWAGGLPWGGRSPGGVSESEAGSPLAGLDMDTFDSGFVGSDCSSPVECDFTSPGDEGPPRSYLRQWVVIPPPLSSPGPQAS	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2304).	21	Cytokine receptor	Cytokine receptor	type I cytokine receptor family. Type 4 subfamily.	.	.	.	.	.	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa05321:Inflammatory bowel disease (IBD)	R-HSA-9020958: Interleukin-21 signaling	.	Q9HBE5
TTLDX4N	Interleukin-22 (IL22)	Q9GZX6	IL22_HUMAN	Cytokine: interleukin	ZCYTO18; UNQ3099/PRO10096; Interleukin22; ILTIF; IL10related Tcellderivedinducible factor; IL-TIF; IL-22; IL-10-related T-cell-derived-inducible factor; Cytokine Zcyto18	IL22	Cytokine that contributes to the inflammatory response in vivo.	.	3Q1S; 3G9V; 3DLQ; 3DGC; 1YKB	MAALQKSVSSFLMGTLATSCLLLLALLVQGGAAAPISSHCRLDKSNFQQPYITNRTFMLAKEASLADNNTDVRLIGEKLFHGVSMSERCYLMKQVLNFTLEEVLFPQSDRFQPYMQEVVPFLARLSNRLSTCHIEGDDLHIQRNVQKLKDTVKKLGESGEIKAIGELDLLFMSLRNACI	Clinical trial	Emerging Therapies for the Treatment of Psoriasis. Dermatol Ther (Heidelb) 2012 December; 2(1): 16.	21	Cytokine	.	IL-10 family.	.	.	Interleukin 22 IL-10-related T-cell-derived-inducible factor	PF14565	PF14565; IL22	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04630: JAK-STAT signaling pathway; hsa04659: Th17 cell differentiation; hsa05321: Inflammatory bowel disease	R-HSA-8854691: Interleukin-20 family signaling	.	Q9GZX6
TTC1GLB	Interleukin-23 (IL23)	Q9NPF7	IL23A_HUMAN	Cytokine: interleukin	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	IL23A	"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."	.	5NJD; 5MZV; 5MXA; 5MJ4; 5MJ3	MLGSRAVMLLLLLPWTAQGRAVPGGSSPAWTQCQQLSQKLCTLAWSAHPLVGHMDLREEGDEETTNDVPHIQCGDGCDPQGLRDNSQFCLQRIHQGLIFYEKLLGSDIFTGEPSLLPDSPVGQLHASLLGLSQLLQPEGHHWETQQIPSLSPSQPWQRLLLRFKILRSLQAFVAVAARVFAHGAATLSP	Successful	Interleukin-23 in the pathogenesis and treatment of psoriasis. Skin Therapy Lett. 2015 Mar-Apr;20(2):1-4.	34	Cytokine	Interleukin	IL-6 superfamily.	.	.	Interleukin 23 subunit alpha	PF16649	PF16649; IL23	.	.	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	R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9020933: Interleukin-23 signaling	.	Q9NPF7
TT6H4QR	Interleukin 23 receptor (IL23R)	Q5VWK5	IL23R_HUMAN	Cytokine receptor	Interleukin-23 receptor; IL23 receptor; IL-23R; IL-23 receptor	IL23R	"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."	.	5MZV	MNQVTIQWDAVIALYILFSWCHGGITNINCSGHIWVEPATIFKMGMNISIYCQAAIKNCQPRKLHFYKNGIKERFQITRINKTTARLWYKNFLEPHASMYCTAECPKHFQETLICGKDISSGYPPDIPDEVTCVIYEYSGNMTCTWNAGKLTYIDTKYVVHVKSLETEEEQQYLTSSYINISTDSLQGGKKYLVWVQAANALGMEESKQLQIHLDDIVIPSAAVISRAETINATVPKTIIYWDSQTTIEKVSCEMRYKATTNQTWNVKEFDTNFTYVQQSEFYLEPNIKYVFQVRCQETGKRYWQPWSSLFFHKTPETVPQVTSKAFQHDTWNSGLTVASISTGHLTSDNRGDIGLLLGMIVFAVMLSILSLIGIFNRSFRTGIKRRILLLIPKWLYEDIPNMKNSNVVKMLQENSELMNNNSSEQVLYVDPMITEIKEIFIPEHKPTDYKKENTGPLETRDYPQNSLFDNTTVVYIPDLNTGYKPQISNFLPEGSHLSNNNEITSLTLKPPVDSLDSGNNPRLQKHPNFAFSVSSVNSLSNTIFLGELSLILNQGECSSPDIQNSVEEETTMLLENDSPSETIPEQTLLPDEFVSCLGIVNEELPSINTYFPQNILESHFNRISLLEK	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2293).	25	Cytokine receptor	Cytokine receptor	type I cytokine receptor family. Type 2 subfamily.	.	.	.	.	.	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa05321:Inflammatory bowel disease (IBD)	R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9020933: Interleukin-23 signaling	.	Q5VWK5
TT1EPXZ	Interleukin-24 (IL24)	Q13007	IL24_HUMAN	Cytokine: interleukin	Suppression of tumorigenicity 16 protein; ST16; Melanoma differentiationassociated gene 7 protein; Melanoma differentiation-associated gene 7 protein; MDA7; MDA-7; Interleukin24; IL-24	IL24	Has antiproliferative properties on melanoma cells and may contribute to terminal cell differentiation.	.	6GG1; 6DF3	MNFQQRLQSLWTLARPFCPPLLATASQMQMVVLPCLGFTLLLWSQVSGAQGQEFHFGPCQVKGVVPQKLWEAFWAVKDTMQAQDNITSARLLQQEVLQNVSDAESCYLVHTLLEFYLKTVFKNYHNRTVEVRTLKSFSTLANNFVLIVSQLQPSQENEMFSIRDSAHRRFLLFRRAFKQLDVEAALTKALGEVDILLTWMQKFYKL	Clinical trial	"Intratumoral injection of INGN 241, a nonreplicating adenovector expressing the melanoma-differentiation associated gene-7 (mda-7/IL24): biologic outcome in advanced cancer patients. Mol Ther. 2005 Jan;11(1):160-72."	21	Cytokine	Cytokine: interleukin	IL-10 family.	.	.	.	.	.	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway	R-HSA-8854691: Interleukin-20 family signaling	.	Q13007
TTVMO5W	Interleukin-25 (IL25)	Q9H293	IL25_HUMAN	Cytokine: interleukin	UNQ3120/PRO10272; Interleukin-17E; IL17E; IL-25; IL-17E	IL25	Proinflammatory cytokine favoring Th2-type immune responses. Induces activation of NF-kappa-B and stimulates production of the proinflammatory chemokine IL-8.	.	.	MRERPRLGEDSSLISLFLQVVAFLAMVMGTHTYSHWPSCCPSKGQDTSEELLRWSTVPVPPLEPARPNRHPESCRASEDGPLNSRAISPWRYELDRDLNRLPQDLYHARCLCPHCVSLQTGSHMDPRGNSELLYHNQTVFYRRPCHGEKGTHKGYCLERRLYRVSLACVCVRPRVMG	Clinical trial	Bispecific antibodies rise again. Nat Rev Drug Discov. 2014 Nov;13(11):799-801. 	17	Cytokine	Cytokine: interleukin	IL-17 family.	.	.	Interleukin-17	PF06083	PF06083; IL17	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa05321:Inflammatory bowel disease (IBD); hsa05323:Rheumatoid arthritis	R-HSA-448424: Interleukin-17 signaling	.	Q9H293
TT10Y9E	Interleukin 2 receptor alpha (IL2RA)	P01589	IL2RA_HUMAN	Cytokine receptor	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	IL2RA	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.	.	3NFP; 3IU3; 2ERJ; 2B5I; 1Z92	MDSYLLMWGLLTFIMVPGCQAELCDDDPPEIPHATFKAMAYKEGTMLNCECKRGFRRIKSGSLYMLCTGNSSHSSWDNQCQCTSSATRNTTKQVTPQPEEQKERKTTEMQSPMQPVDQASLPGHCREPPPWENEATERIYHFVVGQMVYYQCVQGYRALHRGPAESVCKMTHGKTRWTQPQLICTGEMETSQFPGEEKPQASPEGRPESETSCLVTTTDFQIQTEMAATMETSIFTTEYQVAVAGCVFLLISVLLLSGLTWQRRQRKSRRTI	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	Cytokine receptor	Cytokine receptor	.	.	.	Sushi repeat (SCR repeat)	PF00084	PF00084; Sushi	.	.	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	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	.	P01589
TT9721Y	Interleukin 2 receptor beta (IL2RB)	P14784	IL2RB_HUMAN	Cytokine receptor	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	IL2RB	"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."	.	6E8K; 5M5E; 4GS7; 3QAZ; 2ERJ	MAAPALSWRLPLLILLLPLATSWASAAVNGTSQFTCFYNSRANISCVWSQDGALQDTSCQVHAWPDRRRWNQTCELLPVSQASWACNLILGAPDSQKLTTVDIVTLRVLCREGVRWRVMAIQDFKPFENLRLMAPISLQVVHVETHRCNISWEISQASHYFERHLEFEARTLSPGHTWEEAPLLTLKQKQEWICLETLTPDTQYEFQVRVKPLQGEFTTWSPWSQPLAFRTKPAALGKDTIPWLGHLLVGLSGAFGFIILVYLLINCRNTGPWLKKVLKCNTPDPSKFFSQLSSEHGGDVQKWLSSPFPSSSFSPGGLAPEISPLEVLERDKVTQLLLQQDKVPEPASLSSNHSLTSCFTNQGYFFFHLPDALEIEACQVYFTYDPYSEEDPDEGVAGAPTGSSPQPLQPLSGEDDAYCTFPSRDDLLLFSPSLLGGPSPPSTAPGGSGAGEERMPPSLQERVPRDWDPQPLGPPTPGVPDLVDFQPPPELVLREAGEEVPDAGPREGVSFPWSRPPGQGEFRALNARLPLNTDAYLSLQELQGQDPTHLV	Clinical trial	Phase II randomized trial of autologous formalin-fixed tumor vaccine for postsurgical recurrence of hepatocellular carcinoma. Clin Cancer Res. 2004 Mar 1;10(5):1574-9.	21	Cytokine receptor	Cytokine receptor	type I cytokine receptor family. Type 4 subfamily.	.	.	Interleukin-2 receptor subunit beta N-terminal domain 1	PF18707	PF18707; IL2RB_N1	9.B.281.1.1	The Interleukin-2 Receptor (IL2R) Family	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	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	.	P14784
TT1RJXK	Interleukin-31 (IL31)	Q6EBC2	IL31_HUMAN	Cytokine: interleukin	Interleukin31; IL-31	IL31	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.	.	.	MASHSGPSTSVLFLFCCLGGWLASHTLPVRLLRPSDDVQKIVEELQSLSKMLLKDVEEEKGVLVSQNYTLPCLSPDAQPPNNIHSPAIRAYLKTIRQLDNKSVIDEIIEHLDKLIFQDAPETNISVPTDTHECKRFILTISQQFSECMDLALKSLTSGAQQATT	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	Cytokine	.	.	.	.	Interleukin 31	PF15209	PF15209; IL31	.	.	hsa04060: Cytokine-cytokine receptor interaction	R-HSA-6788467: IL-6-type cytokine receptor ligand interactions	.	Q6EBC2
TT9HPX0	Interleukin 31 receptor (IL31R)	Q8NI17	IL31R_HUMAN	Cytokine receptor	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	IL31RA	"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."	.	.	MMWTWALWMLPSLCKFSLAALPAKPENISCVYYYRKNLTCTWSPGKETSYTQYTVKRTYAFGEKHDNCTTNSSTSENRASCSFFLPRITIPDNYTIEVEAENGDGVIKSHMTYWRLENIAKTEPPKIFRVKPVLGIKRMIQIEWIKPELAPVSSDLKYTLRFRTVNSTSWMEVNFAKNRKDKNQTYNLTGLQPFTEYVIALRCAVKESKFWSDWSQEKMGMTEEEAPCGLELWRVLKPAEADGRRPVRLLWKKARGAPVLEKTLGYNIWYYPESNTNLTETMNTTNQQLELHLGGESFWVSMISYNSLGKSPVATLRIPAIQEKSFQCIEVMQACVAEDQLVVKWQSSALDVNTWMIEWFPDVDSEPTTLSWESVSQATNWTIQQDKLKPFWCYNISVYPMLHDKVGEPYSIQAYAKEGVPSEGPETKVENIGVKTVTITWKEIPKSERKGIICNYTIFYQAEGGKGFSKTVNSSILQYGLESLKRKTSYIVQVMASTSAGGTNGTSINFKTLSFSVFEIILITSLIGGGLLILIILTVAYGLKKPNKLTHLCWPTVPNPAESSIATWHGDDFKDKLNLKESDDSVNTEDRILKPCSTPSDKLVIDKLVVNFGNVLQEIFTDEARTGQENNLGGEKNGYVTCPFRPDCPLGKSFEELPVSPEIPPRKSQYLRSRMPEGTRPEAKEQLLFSGQSLVPDHLCEEGAPNPYLKNSVTAREFLVSEKLPEHTKGEV	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	Cytokine receptor	.	type I cytokine receptor family. Type 2 subfamily.	.	.	"Fibronectin type III domain; Interleukin-6 receptor alpha chain, binding"	PF00041; PF09240	PF00041; fn3; PF09240; IL6Ra-bind	.	.	hsa04060: Cytokine-cytokine receptor interaction	R-HSA-6788467: IL-6-type cytokine receptor ligand interactions	.	Q8NI17
TTD4G7L	Interleukin-32 (IL32)	P24001	IL32_HUMAN	Cytokine: interleukin	Tumor necrosis factor alpha-inducing factor; TAIF; Natural killer cells protein 4; NK4; IL-32	IL32	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.	.	.	MCFPKVLSDDMKKLKARMVMLLPTSAQGLGAWVSACDTEDTVGHLGPWRDKDPALWCQLCLSSQHQAIERFYDKMQNAESGRGQVMSSLAELEDDFKEGYLETVAAYYEEQHPELTPLLEKERDGLRCRGNRSPVPDVEDPATEEPGESFCDKVMRWFQAMLQRLQTWWHGVLAWVKEKVVALVHAVQALWKQFQSFCCSLSELFMSSFQSYGAPRGDKEELTPQKCSEPQSSK	Literature-reported	Role of interleukin-32 in cancer biology. Oncol Lett. 2018 Jul;16(1):41-47.	.	.	.	.	.	.	Interleukin 32	PF15225	PF15225; IL32	.	.	hsa04060:Cytokine-cytokine receptor interaction	R-HSA-449836: Other interleukin signaling; R-HSA-9013423: RAC3 GTPase cycle	.	P24001
TT5MD4P	Interleukin-33 (IL33)	O95760	IL33_HUMAN	Cytokine: interleukin	Nuclear factor from high endothelial venules; NFHEV; NF-HEV; Interleukin1 family member 11; Interleukin-1 family member 11; IL1F11; IL-33; IL-1F11; C9orf26	IL33	"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."	.	4KC3; 2KLL	MKPKMKYSTNKISTAKWKNTASKALCFKLGKSQQKAKEVCPMYFMKLRSGLMIKKEACYFRRETTKRPSLKTGRKHKRHLVLAACQQQSTVECFAFGISGVQKYTRALHDSSITGISPITEYLASLSTYNDQSITFALEDESYEIYVEDLKKDEKKDKVLLSYYESQHPSNESGDGVDGKMLMVTLSPTKDFWLHANNKEHSVELHKCEKPLPDQAFFVLHNMHSNCVSFECKTDPGVFIGVKDNHLALIKVDSSENLCTENILFKLSET	Clinical trial	"Clinical pipeline report, company report or official report of Amgen."	17	Cytokine	.	IL-1 family. Highly divergent.	.	.	Interleukin 33	PF15095	PF15095; IL33	.	.	hsa04623:Cytosolic DNA-sensing pathway; hsa05164:Influenza A	"R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-5689880: Ub-specific processing proteases; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-9014843: Interleukin-33 signaling"	.	O95760
TT8SLDN	Interleukin-36 gamma (IL36G)	Q9NZH8	IL36G_HUMAN	.	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	IL36G	"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."	.	.	MRGTPGDADGGGRAVYQSMCKPITGTINDLNQQVWTLQGQNLVAVPRSDSVTPVTVAVITCKYPEALEQGRGDPIYLGIQNPEMCLYCEKVGEQPTLQLKEQKIMDLYGQPEPVKPFLFYRAKTGRTSTLESVAFPDWFIASSKRDQPIILTSELGKSYNTAFELNIND	Clinical trial	"Clinical pipeline report, company report or official report of Moderna Therapeutics."	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction	R-HSA-9014826: Interleukin-36 pathway	.	Q9NZH8
TTQTX98	Interleukin-37 (IL37)	Q9NZH6	IL37_HUMAN	Cytokine: interleukin	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	IL37	"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."	.	6NCU; 5HN1	MSFVGENSGVKMGSEDWEKDEPQCCLEDPAGSPLEPGPSLPTMNFVHTSPKVKNLNPKKFSIHDQDHKVLVLDSGNLIAVPDKNYIRPEIFFALASSLSSASAEKGSPILLGVSKGEFCLYCDKDKGQSHPSLQLKKEKLMKLAAQKESARRPFIFYRAQVGSWNMLESAAHPGWFICTSCNCNEPVGVTDKFENRKHIEFSFQPVCKAEMSPSEVSD	Successful	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	34	Cytokine	.	IL-1 family.	.	.	Interleukin-1 / 18	PF00340	PF00340; IL1	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04061:Viral protein interaction with cytokine and cytokine receptor	R-HSA-9008059: Interleukin-37 signaling; R-HSA-9012546: Interleukin-18 signaling	.	Q9NZH6
TTENHJ0	Interleukin 3 receptor alpha (IL3RA)	P26951	IL3RA_HUMAN	Cytokine receptor	Interleukin-3 receptor subunit alpha; IL3R; IL-3RA; IL-3R-alpha; IL-3R subunit alpha; IL-3 receptor subunit alpha; CD123 antigen; CD123	IL3RA	This is a receptor for interleukin-3.	.	5UWC; 5UV8; 4JZJ	MVLLWLTLLLIALPCLLQTKEDPNPPITNLRMKAKAQQLTWDLNRNVTDIECVKDADYSMPAVNNSYCQFGAISLCEVTNYTVRVANPPFSTWILFPENSGKPWAGAENLTCWIHDVDFLSCSWAVGPGAPADVQYDLYLNVANRRQQYECLHYKTDAQGTRIGCRFDDISRLSSGSQSSHILVRGRSAAFGIPCTDKFVVFSQIEILTPPNMTAKCNKTHSFMHWKMRSHFNRKFRYELQIQKRMQPVITEQVRDRTSFQLLNPGTYTVQIRARERVYEFLSAWSTPQRFECDQEEGANTRAWRTSLLIALGTLLALVCVFVICRRYLVMQRLFPRIPHMKDPIGDSFQNDKLVVWEAGKAGLEECLVTEVQVVQKT	Successful	2018 FDA drug approvals.Nat Rev Drug Discov. 2019 Feb;18(2):85-89. 	34	Cytokine receptor	.	type I cytokine receptor family. Type 5 subfamily.	.	.	"IL-3 receptor alpha chain N-terminal domain; Interleukin-6 receptor alpha chain, binding"	PF18611; PF09240	PF18611; IL3Ra_N; PF09240; IL6Ra-bind	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04210:Apoptosis; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage	"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"	.	P26951
TTLGTKB	Interleukin-4 (IL4)	P05112	IL4_HUMAN	Cytokine: interleukin	Pitrakinra; Lymphocyte stimulatory factor 1; IL-4; Binetrakin; BSF-1; B-cell stimulatory factor 1	IL4	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.	.	5FHX; 4YDY; 3QB7; 3BPN; 3BPL	MGLTSQLLPPLFFLLACAGNFVHGHKCDITLQEIIKTLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAATVLRQFYSHHEKDTRCLGATAQQFHRHKQLIRFLKRLDRNLWGLAGLNSCPVKEANQSTLENFLERLKTIMREKYSKCSS	Clinical trial	Efficacy of soluble IL-4 receptor for the treatment of adults with asthma. J Allergy Clin Immunol. 2001 Jun;107(6):963-70.	21	Cytokine	Growth factor	IL-4/IL-13 family.	.	.	Interleukin 4	PF00727	PF00727; IL4	.	.	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	R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9012546: Interleukin-18 signaling	.	P05112
TTDWHC3	Interleukin 4 receptor alpha (IL4R)	P24394	IL4RA_HUMAN	Cytokine receptor	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	IL4R	"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."	.	5E4E; 3BPO; 3BPN; 3BPL; 1ITE	MGWLCSGLLFPVSCLVLLQVASSGNMKVLQEPTCVSDYMSISTCEWKMNGPTNCSTELRLLYQLVFLLSEAHTCIPENNGGAGCVCHLLMDDVVSADNYTLDLWAGQQLLWKGSFKPSEHVKPRAPGNLTVHTNVSDTLLLTWSNPYPPDNYLYNHLTYAVNIWSENDPADFRIYNVTYLEPSLRIAASTLKSGISYRARVRAWAQCYNTTWSEWSPSTKWHNSYREPFEQHLLLGVSVSCIVILAVCLLCYVSITKIKKEWWDQIPNPARSRLVAIIIQDAQGSQWEKRSRGQEPAKCPHWKNCLTKLLPCFLEHNMKRDEDPHKAAKEMPFQGSGKSAWCPVEISKTVLWPESISVVRCVELFEAPVECEEEEEVEEEKGSFCASPESSRDDFQEGREGIVARLTESLFLDLLGEENGGFCQQDMGESCLLPPSGSTSAHMPWDEFPSAGPKEAPPWGKEQPLHLEPSPPASPTQSPDNLTCTETPLVIAGNPAYRSFSNSLSQSPCPRELGPDPLLARHLEEVEPEMPCVPQLSEPTTVPQPEPETWEQILRRNVLQHGAAAAPVSAPTSGYQEFVHAVEQGGTQASAVVGLGPPGEAGYKAFSSLLASSAVSPEKCGFGASSGEEGYKPFQDLIPGCPGDPAPVPVPLFTFGLDREPPRSPQSSHLPSSSPEHLGLEPGEKVEDMPKPPLPQEQATDPLVDSLGSGIVYSALTCHLCGHLKQCHGQEDGGQTPVMASPCCGCCCGDRSSPPTTPLRAPDPSPGGVPLEASLCPASLAPSGISEKSKSSSSFHPAPGNAQSSSQTPKIVNFVSVGPTYMRVS	Successful	Dupilumab in persistent asthma with elevated eosinophil levels. N Engl J Med. 2013 Jun 27;368(26):2455-66.	34	Cytokine receptor	Cytokine receptor	type I cytokine receptor family. Type 4 subfamily.	.	.	"Interleukin-4 receptor alpha chain, N-terminal"	PF09238	PF09238; IL4Ra_N	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage; hsa05321:Inflammatory bowel disease (IBD)	R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling	.	P24394
TTO8F0B	IL4R messenger RNA (IL4R mRNA)	P24394	IL4RA_HUMAN	mRNA target	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)	IL4R	"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."	.	5E4E; 3BPO; 3BPN; 3BPL; 1ITE	MGWLCSGLLFPVSCLVLLQVASSGNMKVLQEPTCVSDYMSISTCEWKMNGPTNCSTELRLLYQLVFLLSEAHTCIPENNGGAGCVCHLLMDDVVSADNYTLDLWAGQQLLWKGSFKPSEHVKPRAPGNLTVHTNVSDTLLLTWSNPYPPDNYLYNHLTYAVNIWSENDPADFRIYNVTYLEPSLRIAASTLKSGISYRARVRAWAQCYNTTWSEWSPSTKWHNSYREPFEQHLLLGVSVSCIVILAVCLLCYVSITKIKKEWWDQIPNPARSRLVAIIIQDAQGSQWEKRSRGQEPAKCPHWKNCLTKLLPCFLEHNMKRDEDPHKAAKEMPFQGSGKSAWCPVEISKTVLWPESISVVRCVELFEAPVECEEEEEVEEEKGSFCASPESSRDDFQEGREGIVARLTESLFLDLLGEENGGFCQQDMGESCLLPPSGSTSAHMPWDEFPSAGPKEAPPWGKEQPLHLEPSPPASPTQSPDNLTCTETPLVIAGNPAYRSFSNSLSQSPCPRELGPDPLLARHLEEVEPEMPCVPQLSEPTTVPQPEPETWEQILRRNVLQHGAAAAPVSAPTSGYQEFVHAVEQGGTQASAVVGLGPPGEAGYKAFSSLLASSAVSPEKCGFGASSGEEGYKPFQDLIPGCPGDPAPVPVPLFTFGLDREPPRSPQSSHLPSSSPEHLGLEPGEKVEDMPKPPLPQEQATDPLVDSLGSGIVYSALTCHLCGHLKQCHGQEDGGQTPVMASPCCGCCCGDRSSPPTTPLRAPDPSPGGVPLEASLCPASLAPSGISEKSKSSSSFHPAPGNAQSSSQTPKIVNFVSVGPTYMRVS	Literature-reported	Common variations in the IL4R gene affect splicing and influence natural expression of the soluble isoform. Hum Mutat. 2006 Oct;27(10):990-8.	.	mRNA	mRNA target	.	.	.	"Interleukin-4 receptor alpha chain, N-terminal"	PF09238	PF09238; IL4Ra_N	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04151: PI3K-Akt signaling pathway; hsa04630: JAK-STAT signaling pathway; hsa04640: Hematopoietic cell lineage; hsa04658: Th1 and Th2 cell differentiation; hsa04659: Th17 cell differentiation; hsa05200: Pathways in cancer; hsa05321: Inflammatory bowel disease	R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling	.	P24394
TTPREZD	Interleukin-5 (IL5)	P05113	IL5_HUMAN	Cytokine: interleukin	TRF protein; T-cell replacing factor; IL-5; Eosinophil differentiation factor; B-cell differentiation factor I; B cell differentiation factor I	IL5	Factor that induces terminal differentiation of late-developing B-cells to immunoglobulin secreting cells.	.	3VA2; 3QT2; 1HUL	MRMLLHLSLLALGAAYVYAIPTEIPTSALVKETLALLSTHRTLLIANETLRIPVPVHKNHQLCTEEIFQGIGTLESQTVQGGTVERLFKNLSLIKKYIDGQKKKCGEERRRVNQFLDYLQEFLGVMNTEWIIES	Successful	Benralizumab a humanized mAb to IL-5R with enhanced antibody-dependent cell-mediated cytotoxicity a novel approach for the treatment of asthma	34	Cytokine	Growth factor	IL-5 family.	.	.	Interleukin 5	PF02025	PF02025; IL5	.	.	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	"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"	.	P05113
TTXH9AD	Interleukin 5 receptor alpha (IL5RA)	Q01344	IL5RA_HUMAN	Cytokine receptor	Interleukin-5 receptor subunit alpha; IL5R; IL-5RA; IL-5R-alpha; IL-5R subunit alpha; IL-5 receptor subunit alpha; CDw125; CD125	IL5RA	The alpha chain binds to IL5. This is the receptor for interleukin-5.	.	6H41; 3VA2; 3QT2; 1OBZ; 1OBX	MIIVAHVLLILLGATEILQADLLPDEKISLLPPVNFTIKVTGLAQVLLQWKPNPDQEQRNVNLEYQVKINAPKEDDYETRITESKCVTILHKGFSASVRTILQNDHSLLASSWASAELHAPPGSPGTSIVNLTCTTNTTEDNYSRLRSYQVSLHCTWLVGTDAPEDTQYFLYYRYGSWTEECQEYSKDTLGRNIACWFPRTFILSKGRDWLAVLVNGSSKHSAIRPFDQLFALHAIDQINPPLNVTAEIEGTRLSIQWEKPVSAFPIHCFDYEVKIHNTRNGYLQIEKLMTNAFISIIDDLSKYDVQVRAAVSSMCREAGLWSEWSQPIYVGNDEHKPLREWFVIVIMATICFILLILSLICKICHLWIKLFPPIPAPKSNIKDLFVTTNYEKAGSSETEIEVICYIEKPGVETLEDSVF	Successful	Benralizumab--a humanized mAb to IL-5R with enhanced antibody-dependent cell-mediated cytotoxicity--a novel approach for the treatment of asthma. Expert Opin Biol Ther. 2012 Jan;12(1):113-8. 	34	Cytokine receptor	.	type I cytokine receptor family. Type 5 subfamily.	.	.	"Interleukin-6 receptor alpha chain, binding"	PF09240	PF09240; IL6Ra-bind	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04630: JAK-STAT signaling pathway; hsa04640: Hematopoietic cell lineage; hsa05200: Pathways in cancer	"R-HSA-512988: Interleukin-3, Interleukin-5 and GM-CSF signaling; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-912526: Interleukin receptor SHC signaling"	.	Q01344
TTT1V78	Interleukin-6 (IL6)	P05231	IL6_HUMAN	Cytokine: interleukin	Interferon beta-2; IL-6; IFNB2; IFN-beta-2; Hybridoma growth factor; CTL differentiation factor; CDF; BSF-2; B-cell stimulatory factor 2	IL6	"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."	.	5FUC; 4ZS7; 4O9H; 4NI9; 4NI7	MNSFSTSAFGPVAFSLGLLLVLPAAFPAPVPPGEDSKDVAAPHRQPLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM	Successful	2014 FDA drug approvals. Nat Rev Drug Discov. 2015 Feb;14(2):77-81.	34	Cytokine	Interleukin	IL-6 superfamily.	.	.	Interleukin-6/G-CSF/MGF family	PF00489	PF00489; IL6	.	.	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)	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)	.	P05231
TTJH4Y5	HUMAN interleukin 6 (IL6)	P05231	IL6_HUMAN	Cytokine: interleukin	Interferon beta-2; IL-6; IFNB2; IFN-beta-2; Hybridoma growth factor; CTL differentiation factor; CDF; BSF-2; B-cell stimulatory factor 2	IL6	"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."	.	5FUC; 4ZS7; 4O9H; 4NI9; 4NI7	MNSFSTSAFGPVAFSLGLLLVLPAAFPAPVPPGEDSKDVAAPHRQPLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM	.	Elevated Interleukin-6 and Severe COVID-19: A Meta-Analysis. J Med Virol. 2020 Apr 28.	34	Cytokine	Interleukin	IL-6 superfamily.	.	.	Interleukin-6/G-CSF/MGF family	PF00489	PF00489; IL6	.	.	hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa01523: Antifolate resistance; hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04066: HIF-1 signaling pathway; hsa04068: FoxO signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04218: Cellular senescence; hsa04620: Toll-like receptor signaling pathway; hsa04621: NOD-like receptor signaling pathway; hsa04623: Cytosolic DNA-sensing pathway; hsa04625: C-type lectin receptor signaling pathway; hsa04630: JAK-STAT signaling pathway; hsa04640: Hematopoietic cell lineage; hsa04657: IL-17 signaling pathway; hsa04659: Th17 cell differentiation; hsa04668: TNF signaling pathway; hsa04672: Intestinal immune network for IgA production; hsa04931: Insulin resistance; hsa04932: Non-alcoholic fatty liver disease; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04936: Alcoholic liver disease; hsa05010: Alzheimer disease; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05130: Pathogenic Escherichia coli infection; hsa05132: Salmonella infection; hsa05133: Pertussis; hsa05134: Legionellosis; hsa05135: Yersinia infection; hsa05142: Chagas disease; hsa05143: African trypanosomiasis; hsa05144: Malaria; hsa05146: Amoebiasis; hsa05152: Tuberculosis; hsa05161: Hepatitis B; hsa05162: Measles; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05202: Transcriptional misregulation in cancer; hsa05321: Inflammatory bowel disease; hsa05323: Rheumatoid arthritis; hsa05332: Graft-versus-host disease; hsa05410: Hypertrophic cardiomyopathy; hsa05417: Lipid and atherosclerosis	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); R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-6783783: Interleukin-10 signaling; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-8853884: Transcriptional Regulation by VENTX; R-HSA-8957275: Post-translational protein phosphorylation; R-HSA-9660821: ADORA2B mediated anti-inflammatory cytokines production; R-HSA-9662834: CD163 mediating an anti-inflammatory response	.	P05231
TT0E5SK	Interleukin 6 receptor (IL6R)	P08887; P40189	IL6RA_HUMAN; IL6RB_HUMAN	Cytokine receptor	Membrane glycoprotein; Interleukin-6 receptor; IL-6R; IL-6 receptor	IL6R	Low concentration of a soluble form of IL6 receptor acts as an agonist of IL6 activity.	.	.	MLAVGCALLAALLAAPGAALAPRRCPAQEVARGVLTSLPGDSVTLTCPGVEPEDNATVHWVLRKPAAGSHPSRWAGMGRRLLLRSVQLHDSGNYSCYRAGRPAGTVHLLVDVPPEEPQLSCFRKSPLSNVVCEWGPRSTPSLTTKAVLLVRKFQNSPAEDFQEPCQYSQESQKFSCQLAVPEGDSSFYIVSMCVASSVGSKFSKTQTFQGCGILQPDPPANITVTAVARNPRWLSVTWQDPHSWNSSFYRLRFELRYRAERSKTFTTWMVKDLQHHCVIHDAWSGLRHVVQLRAQEEFGQGEWSEWSPEAMGTPWTESRSPPAENEVSTPMQALTTNKDDDNILFRDSANATSLPVQDSSSVPLPTFLVAGGSLAFGTLLCIAIVLRFKKTWKLRALKEGKTSMHPPYSLGQLVPERPRPTPVLVPLISPPVSPSSLGSDNTSSHNRPDARDPRSPYDISNTDYFFPR	Successful	Mullard A: 2010 FDA drug approvals. Nat Rev Drug Discov. 2011 Feb;10(2):82-5.	34	Cytokine receptor	.	.	.	.	.	.	.	.	.	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)	R-HSA-110056:MAPK3 (ERK1) activation; R-HSA-112411:MAPK1 (ERK2) activation	.	P08887
TTDVAKP	HUMAN interleukin-6 receptor (IL6R)	P08887; P40189	IL6RA_HUMAN; IL6RB_HUMAN	Cytokine receptor	Membrane glycoprotein; Interleukin-6 receptor; IL-6R; IL-6 receptor	IL6R	Low concentration of a soluble form of IL6 receptor acts as an agonist of IL6 activity.	.	.	MLAVGCALLAALLAAPGAALAPRRCPAQEVARGVLTSLPGDSVTLTCPGVEPEDNATVHWVLRKPAAGSHPSRWAGMGRRLLLRSVQLHDSGNYSCYRAGRPAGTVHLLVDVPPEEPQLSCFRKSPLSNVVCEWGPRSTPSLTTKAVLLVRKFQNSPAEDFQEPCQYSQESQKFSCQLAVPEGDSSFYIVSMCVASSVGSKFSKTQTFQGCGILQPDPPANITVTAVARNPRWLSVTWQDPHSWNSSFYRLRFELRYRAERSKTFTTWMVKDLQHHCVIHDAWSGLRHVVQLRAQEEFGQGEWSEWSPEAMGTPWTESRSPPAENEVSTPMQALTTNKDDDNILFRDSANATSLPVQDSSSVPLPTFLVAGGSLAFGTLLCIAIVLRFKKTWKLRALKEGKTSMHPPYSLGQLVPERPRPTPVLVPLISPPVSPSSLGSDNTSSHNRPDARDPRSPYDISNTDYFFPR	.	"Tocilizumab, an anti-IL6 receptor antibody, to treat Covid-19-related respiratory failure: a case report. Ann Oncol. 2020 Apr 2. pii: S0923-7534(20)36387-0."	.	.	.	.	.	.	.	.	.	.	.	hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa04060: Cytokine-cytokine receptor interaction; hsa04061: Viral protein interaction with cytokine and cytokine receptor; hsa04066: HIF-1 signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04630: JAK-STAT signaling pathway; hsa04640: Hematopoietic cell lineage; hsa04659: Th17 cell differentiation; hsa04932: Non-alcoholic fatty liver disease; hsa05163: Human cytomegalovirus infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer	R-HSA-1059683: Interleukin-6 signaling; R-HSA-110056: MAPK3 (ERK1) activation; R-HSA-112411: MAPK1 (ERK2) activation; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9616222: Transcriptional regulation of granulopoiesis; R-HSA-9679191: Potential therapeutics for SARS	.	P08887
TT8FRMO	Interleukin-7 (IL7)	P13232	IL7_HUMAN	Cytokine: interleukin	Interleukin7; IL-7	IL7	It is important for proliferation during certain stages of B-cell maturation. Hematopoietic growth factor capable of stimulating the proliferation of lymphoid progenitors.	.	3DI3; 3DI2; 1IL7	MFHVSFRYIFGLPPLILVLLPVASSDCDIEGKDGKQYESVLMVSIDQLLDSMKEIGSNCLNNEFNFFKRHICDANKEGMFLFRAARKLRQFLKMNSTGDFDLHLLKVSEGTTILLNCTGQVKGRKPAALGEAQPTKSLEENKSLKEQKKLNDLCFLKRLLQEIKTCWNKILMGTKEH	Clinical trial	ClinicalTrials.gov (NCT02293161) Single Ascending Doses Study of Anti- Interleukin-7 Receptor alpha Monoclonal Antibody (GSK2618960) in Healthy Volunteers. U.S. National Institutes of Health.	17	Cytokine	Interleukin receptor family	IL-7/IL-9 family.	.	.	.	.	.	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04630:Jak-STAT signaling pathway; hsa04640:Hematopoietic cell lineage	R-HSA-1266695:Interleukin-7 signaling	.	P13232
TTAWI51	Interleukin 7 receptor alpha (IL7R)	P16871	IL7RA_HUMAN	Cytokine receptor	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	IL7R	Acts as a receptor for thymic stromal lymphopoietin (TSLP). Receptor for interleukin-7.	.	5J11; 3UP1; 3DI3; 3DI2	MTILGTTFGMVFSLLQVVSGESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNITNLEFEICGALVEVKCLNFRKLQEIYFIETKKFLLIGKSNICVKVGEKSLTCKKIDLTTIVKPEAPFDLSVVYREGANDFVVTFNTSHLQKKYVKVLMHDVAYRQEKDENKWTHVNLSSTKLTLLQRKLQPAAMYEIKVRSIPDHYFKGFWSEWSPSYYFRTPEINNSSGEMDPILLTISILSFFSVALLVILACVLWKKRIKPIVWPSLPDHKKTLEHLCKKPRKNLNVSFNPESFLDCQIHRVDDIQARDEVEGFLQDTFPQQLEESEKQRLGGDVQSPNCPSEDVVITPESFGRDSSLTCLAGNVSACDAPILSSSRSLDCRESGKNGPHVYQDLLLSLGTTNSTLPPPFSLQSGILTLNPVAQGQPILTSLGSNQEEAYVTMSSFYQNQ	Clinical trial	Perspectives on interleukin-7 therapy in HIV infection. Curr Opin HIV AIDS. 2007 May;2(3):228-33.	21	Cytokine receptor	.	type I cytokine receptor family. Type 4 subfamily.	.	.	Fibronectin type III domain; Fibronectin type III domain	PF00041; PF18447	PF00041; fn3; PF18447; FN3_7	.	.	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	R-HSA-1266695:Interleukin-7 signaling	.	P16871
TT0JTFD	Interleukin-9 (IL9)	P15248	IL9_HUMAN	Cytokine: interleukin	T-cell growth factor P40; P40 cytokine; IL-9; Cytokine P40	IL9	Supports IL-2 independent and IL-4 independent growth of helper T-cells.	.	.	MLLAMVLTSALLLCSVAGQGCPTLAGILDINFLINKMQEDPASKCHCSANVTSCLCLGIPSDNCTRPCFSERLSQMTNTTMQTRYPLIFSRVKKSVEVLKNNKCPYFSCEQPCNQTTAGNALTFLKSLLEIFQKEKMRGMRGKI	Clinical trial	"Clinical pipeline report, company report or official report of AstraZeneca (2009)."	21	Cytokine	.	IL-7/IL-9 family.	.	.	.	.	.	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway; hsa05310:Asthma	R-HSA-8985947: Interleukin-9 signaling	.	P15248
TT0R2QD	Ig-like domain-containing receptor 2 (ILDR2)	Q71H61	ILDR2_HUMAN	.	.	ILDR2	May be involved in lipid homeostasis and ER stress pathways.	.	.	MDRVLLRWISLFWLTAMVEGLQVTVPDKKKVAMLFQPTVLRCHFSTSSHQPAVVQWKFKSYCQDRMGESLGMSSTRAQSLSKRNLEWDPYLDCLDSRRTVRVVASKQGSTVTLGDFYRGREITIVHDADLQIGKLMWGDSGLYYCIITTPDDLEGKNEDSVELLVLGRTGLLADLLPSFAVEIMPEWVFVGLVLLGVFLFFVLVGICWCQCCPHSCCCYVRCPCCPDSCCCPQALYEAGKAAKAGYPPSVSGVPGPYSIPSVPLGGAPSSGMLMDKPHPPPLAPSDSTGGSHSVRKGYRIQADKERDSMKVLYYVEKELAQFDPARRMRGRYNNTISELSSLHEEDSNFRQSFHQMRSKQFPVSGDLESNPDYWSGVMGGSSGASRGPSAMEYNKEDRESFRHSQPRSKSEMLSRKNFATGVPAVSMDELAAFADSYGQRPRRADGNSHEARGGSRFERSESRAHSGFYQDDSLEEYYGQRSRSREPLTDADRGWAFSPARRRPAEDAHLPRLVSRTPGTAPKYDHSYLGSARERQARPEGASRGGSLETPSKRSAQLGPRSASYYAWSPPGTYKAGSSQDDQEDASDDALPPYSELELTRGPSYRGRDLPYHSNSEKKRKKEPAKKTNDFPTRMSLVV	Clinical trial	"Characterization of BAY 1905254, an Immune Checkpoint Inhibitor Targeting the Immunoglobulin-Like Domain Containing Receptor 2 (ILDR2). Cancer Immunol Res. 2020 Jul;8(7):895-911."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q71H61
TT7ALZG	Integrin-linked protein kinase 1 (ILK)	Q13418	ILK_HUMAN	Kinase	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	ILK	"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."	EC 2.7.11.1	6MIB; 4HI9; 4HI8; 3REP; 3KMW	MDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIMRGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQVAEDLVANGALVSICNKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTRTRPRNGTLNKHSGIDFKQLNFLTKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPRLRIFSHPNVLPVLGACQSPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDMARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQCPGRMYAPAWVAPEALQKKPEDTNRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHVCKLMKICMNEDPAKRPKFDMIVPILEKMQDK	Patented-recorded	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2041).	0	EC:2.7	Kinase	protein kinase superfamily. TKL Ser/Thr protein kinase family.	2.7.11.1	Transferring phosphorus-containing groups	Protein tyrosine kinase	PF07714	PF07714; Pkinase_Tyr	.	.	hsa03320: PPAR signaling pathway; hsa04360: Axon guidance; hsa04510: Focal adhesion; hsa05100: Bacterial invasion of epithelial cells; hsa05131: Shigellosis; hsa05213: Endometrial cancer	R-HSA-446343:Localization of the PINCH-ILK-PARVIN complex to focal adhesions	.	Q13418
TTEJA2R	U3 snoRNP protein IMP3 (IMP3)	Q9NV31	IMP3_HUMAN	.	U3 small nucleolar ribonucleoprotein protein IMP3; MRPS4; C15orf12; BRMS2	IMP3	Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing.	.	2CQJ	MVRKLKFHEQKLLKQVDFLNWEVTDHNLHELRVLRRYRLQRREDYTRYNQLSRAVRELARRLRDLPERDQFRVRASAALLDKLYALGLVPTRGSLELCDFVTASSFCRRRLPTVLLKLRMAQHLQAAVAFVEQGHVRVGPDVVTDPAFLVTRSMEDFVTWVDSSKIKRHVLEYNEERDDFDLEA	Literature-reported	"L523S, an RNA-binding protein as a potential therapeutic target for lung cancer. Br J Cancer. 2003 Mar 24;88(6):887-94."	.	.	.	.	.	.	.	.	.	.	.	hsa03008: Ribosome biogenesis in eukaryotes	R-HSA-6790901: rRNA modification in the nucleus and cytosol; R-HSA-6791226: Major pathway of rRNA processing in the nucleolus and cytosol	.	Q9NV31
TTXWL6D	Inositol-1(or4)-monophosphatase (IMPA2)	O14732	IMPA2_HUMAN	Phosphoric monoester hydrolase	Myo-inositol-1-phosphate phosphohydrolase; Myo-inositol monophosphatase: IMP.18p; Lithium-sensitive myo-inositol monophosphatase A1; Inositol monophosphatase; IMPase; IMPA2; IMP	IMPA2	"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."	EC 3.1.3.25	2FVZ; 2DDK; 2CZK; 2CZI; 2CZH	MKPSGEDQAALAAGPWEECFQAAVQLALRAGQIIRKALTEEKRVSTKTSAADLVTETDHLVEDLIISELRERFPSHRFIAEEAAASGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEIGPKRDPATLKLFLSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIREAGGIVIDTSGGPLDLMACRVVAASTREMAMLIAQALQTINYGRDDEK	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	hsa00562:Inositol phosphate metabolism; hsa01100:Metabolic pathways; hsa04070:Phosphatidylinositol signaling system	"R-HSA-1855183: Synthesis of IP2, IP, and Ins in the cytosol"	MetaCyc:HS06822-MON	O14732
TT3GRLK	HUMAN inosine-5'-monophosphate dehydrogenase 1 (IMPDH1)	P20839	IMDH1_HUMAN	CH-OH donor oxidoreductase	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	IMPDH1	"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."	EC 1.1.1.205	1JCN	MADYLISGGTGYVPEDGLTAQQLFASADGLTYNDFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY	.	Proteomics of SARS-CoV-2-infected Host Cells Reveals Therapy Targets. Nature. 2020 May 14.  doi: 10.1038/s41586-020-2332-7.	.	.	.	.	.	.	.	.	.	.	.	hsa00230: Purine metabolism; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa01232: Nucleotide metabolism	R-HSA-6798695: Neutrophil degranulation; R-HSA-73817: Purine ribonucleoside monophosphate biosynthesis; R-HSA-9679191: Potential therapeutics for SARS; R-HSA-9748787: Azathioprine ADME	MetaCyc:HS02896-MON	P20839
TTL7C8Q	Inosine-5'-monophosphate dehydrogenase 1 (IMPDH1)	P20839	IMDH1_HUMAN	CH-OH donor oxidoreductase	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	IMPDH1	"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."	EC 1.1.1.205	1JCN	MADYLISGGTGYVPEDGLTAQQLFASADGLTYNDFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY	Successful	Clinical pharmacology and pharmacogenetics of thiopurines. Eur J Clin Pharmacol. 2008 Aug;64(8):753-67.	34	EC:1.1	IMPDH/GMPR family	IMPDH/GMPR family.	1.1.1.205 	Acting on the CH-OH group of donors	CBS domain; IMP dehydrogenase / GMP reductase domain	PF00571; PF00478	PF00571; CBS; PF00478; IMPDH	.	.	hsa00230: Purine metabolism; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa01232: Nucleotide metabolism	R-HSA-6798695: Neutrophil degranulation; R-HSA-73817: Purine ribonucleoside monophosphate biosynthesis; R-HSA-9679191: Potential therapeutics for SARS; R-HSA-9748787: Azathioprine ADME	MetaCyc:HS02896-MON	P20839
TTTB4UP	Inosine-5'-monophosphate dehydrogenase 2 (IMPDH2)	P12268	IMDH2_HUMAN	CH-OH donor oxidoreductase	IMPDH-II; IMPDH 2; IMPD2; IMPD 2; IMP dehydrogenase 2	IMPDH2	"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."	EC 1.1.1.205	6I0O; 6I0M; 1NFB; 1NF7; 1B3O	MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF	Successful	"Clinical pipeline report, company report or official report of Roche (2009)."	34	EC:1.1	Short-chain dehydrogenases reductases	IMPDH/GMPR family.	1.1.1.205 	Acting on the CH-OH group of donors	CBS domain; IMP dehydrogenase / GMP reductase domain	PF00571; PF00478	PF00571; CBS; PF00478; IMPDH	.	.	hsa00230:Purine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways	R-HSA-73817:Purine ribonucleoside monophosphate biosynthesis	MetaCyc:HS11242-MON	P12268
TTTU6X1	HUMAN inosine-5'-monophosphate dehydrogenase 2 (IMPDH2)	P12268	IMDH2_HUMAN	CH-OH donor oxidoreductase	IMPDH-II; IMPDH 2; IMPD2; IMPD 2; IMP dehydrogenase 2	IMPDH2	"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."	EC 1.1.1.205	6I0O; 6I0M; 1NFB; 1NF7; 1B3O	MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF	.	"The IMPDH inhibitor merimepodib suppresses SARS-CoV-2 replication in vitro. April 09, 2020. doi: https://doi.org/10.1101/2020.04.07.028589"	.	.	.	.	.	.	.	.	.	.	.	hsa00230: Purine metabolism; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa01232: Nucleotide metabolism	R-HSA-6798695: Neutrophil degranulation; R-HSA-73817: Purine ribonucleoside monophosphate biosynthesis; R-HSA-9679191: Potential therapeutics for SARS; R-HSA-9748787: Azathioprine ADME	MetaCyc:HS11242-MON	P12268
TTASGP0	Influenza Env messenger RNA (Influ Env mRNA)	O70902	ENV_HV190	mRNA target	HIV-1 90CF056 envelope glycoprotein gp160 (mRNA); HIV-1 90CF056 env polyprotein (mRNA)	Influ Env mRNA	"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."	.	.	METQRNYPSLWRWGTLILGMLLICSAAQNLWVTVYYGVPVWKEAKTTLFCASDAKAYETEKHNVWATHACVPTDPNPQEMVMENVTESFNMWENNMVEQMHTDIISLWDQSLKPCVKLTPLCVTLNCTNVRNNTSNSTSSMEAGGELTNCSFNVTTVLRDKQQKVHALFYRLDVVPIDNNSTQYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGLCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEQIIIRTKNISDNTKNIIVQLKTPVNITCTRPNNNTRTSIHLGPGRAFYATGDIIGDIRQAHCNISRTDWNKTLHQVVTQLGIHLNNRTISFKPNSGGDMEVRTHSFNCRGEFFYCNTSGLFNSSWEMHTNYTSNDTKGNENITLPCRIKQIVNMWQRVGRAMYAPPIQGNIMCVSNITGLILTIDEGNASAENYTFRPGGGDMRDNWRSELYKYKVVKIEPLGIAPTKTRRRVVEREKRAVGMGASFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQSNLLRAIQARQHMLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTNVPWNSSWSNKSQSEIWDNMTWMEWDKQISNYTEEIYRLLEVSQTQQEKNEQDLLALDKWASLWTWFDISHWLWYIKIFIMIVGGLIGLRIIFAVLSIVNRVRQGYSPLSFQTLVPNPRGPDRPEGTEEGGGEQDRDRSVRLVNGFLPVVWDDLRSLSLFSYRLLRDLLLIVVRTVELLGRRGREALKYLWNLLQYWGQELKNSAIDLLNTTAIAVAEGTDGIIVIVQRAWRAILHIPRRIRQGFERSLL	Literature-reported	Codon-substitution models for heterogeneous selection pressure at amino acid sites. Genetics. 2000 May;155(1):431-49.	.	mRNA	mRNA target	.	.	.	Envelope glycoprotein GP120; Retroviral envelope protein	PF00516; PF00517	PF00516; GP120; PF00517; GP41	.	.	.	.	.	.
TTF4CAM	Influenza Hemagglutinin (Influ HA)	P03452	HEMA_I34A1	Influenza viruses hemagglutinin	Hemagglutinin	Influ HA	"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."	.	1RVZ; 1RVX; 1RU7	MKANLLVLLCALAAADADTICIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDSHNGKLCRLKGIAPLQLGKCNIAGWLLGNPECDPLLPVRSWSYIVETPNSENGICYPGDFIDYEELREQLSSVSSFERFEIFPKESSWPNHNTNGVTAACSHEGKSSFYRNLLWLTEKEGSYPKLKNSYVNKKGKEVLVLWGIHHPPNSKEQQNLYQNENAYVSVVTSNYNRRFTPEIAERPKVRDQAGRMNYYWTLLKPGDTIIFEANGNLIAPMYAFALSRGFGSGIITSNASMHECNTKCQTPLGAINSSLPYQNIHPVTIGECPKYVRSAKLRMVTGLRNIPSIQSRGLFGAIAGFIEGGWTGMIDGWYGYHHQNEQGSGYAADQKSTQNAINGITNKVNTVIEKMNIQFTAVGKEFNKLEKRMENLNKKVDDGFLDIWTYNAELLVLLENERTLDFHDSNVKNLYEKVKSQLKNNAKEIGNGCFEFYHKCDNECMESVRNGTYDYPKYSEESKLNREKVDGVKLESMGIYQILAIYSTVASSLVLLVSLGAISFWMCSNGSLQCRICI	Successful	"Pharmacokinetic properties and bioequivalence of two formulations of arbidol: an open-label, single-dose, randomized-sequence, two-period crossover study in healthy Chinese male volunteers. Clin Ther. 2009 Apr;31(4):784-92."	34	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-168255: Influenza Infection; R-HSA-168275: Entry of Influenza Virion into Host Cell via Endocytosis; R-HSA-168288: Fusion of the Influenza Virion to the Host Cell Endosome; R-HSA-168298: Release; R-HSA-168302: Budding; R-HSA-168303: Packaging of Eight RNA Segments; R-HSA-168316: Assembly of Viral Components at the Budding Site; R-HSA-168336: Uncoating of the Influenza Virion; R-HSA-168874: Transport of HA trimer, NA tetramer and M2 tetramer from the endoplasmic reticulum to the Golgi Apparatus; R-HSA-192823: Viral mRNA Translation; R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell"	.	.
TTZSY8Q	Influenza HA messenger RNA (Influ HA mRNA)	O56140	HEMA_I97A1	mRNA target	Hemagglutinin (mRNA); HA of influenza (mRNA)	Influ HA mRNA	"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."	.	.	MEKTVLLLATVSLVKSDQICIGYHANNSTEQVDTIMEKNVTVTHAQDILERTHNGKLCDLNGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIVEKASPANDLCYPGNFNDYEELKHLLSRINHFEKIQIIPKSSWSNHDASSGVSSACPYLGRSSFFRNVVWLIKKNSAYPTIKRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYQNPTTYISVGTSTLNQRLVPEIATRPKVNGQSGRMEFFWTILKPNDAINFESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNTPQRERRRKKRGLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIINKMNTQFEAVGREFNNLERRIENLNKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVKNGTYDYPQYSEEARLNREEISGVKLESMGTYQILSIYSTVASSLALAIMVAGLSLWMCSNGSLQCRICI	Literature-reported	"US patent application no. 5,580,767, Inhibition of influenza viruses by antisense oligonucleotides."	0	mRNA	mRNA target	.	.	.	Haemagglutinin	PF00509	PF00509; Hemagglutinin	.	.	.	.	.	.
TTXT3PU	Influenza M2 protein (Influ M)	P06821	M2_I34A1	Influenza viruses matrix protein	Matrix protein M2; M2 proton channel; M	Influ M	"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."	.	5DLM	MSLLTEVETPIRNEWGCRCNGSSDPLAIAANIIGILHLILWILDRLFFKCIYRRFKYGLKGGPSTEGVPKSMREEYRKEQQSAVDADDGHFVSIELE	Successful	Antiviral resistance of influenza A (H3N2) strains isolated in northern Greece between 2004 and 2007. Euro Surveill. 2009 Jan 29;14(4). pii: 19104.	34	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-168255: Influenza Infection; R-HSA-168275: Entry of Influenza Virion into Host Cell via Endocytosis; R-HSA-168288: Fusion of the Influenza Virion to the Host Cell Endosome; R-HSA-168298: Release; R-HSA-168302: Budding; R-HSA-168303: Packaging of Eight RNA Segments; R-HSA-168316: Assembly of Viral Components at the Budding Site; R-HSA-168336: Uncoating of the Influenza Virion; R-HSA-168874: Transport of HA trimer, NA tetramer and M2 tetramer from the endoplasmic reticulum to the Golgi Apparatus; R-HSA-192823: Viral mRNA Translation"	.	.
TT50QJ3	Influenza Neuraminidase (Influ NA)	P03470	NRAM_I33A0	Glycosylase	STNA; NEU1; NANase; N-acylneuraminate glycohydrolase; Influ Sialidase	Influ NA	"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."	EC 3.2.1.18	.	MNPNQKIITIGSICMVVGIISLILQIGNIISIWISHSIQTGNQNHTGICNQGIITYNVVAGQDSTSVILTGNSSLCPIRGWAIHSKDNGIRIGSKGDVFVIREPFISCSHLECRTFFLTQGALLNDKHSNGTVKDRSPYRALMSCPVGEAPSPYNSRFESVAWSASACHDGMGWLTIGISGPDNGAVAVLKYNGIITETIKSWRKKILRTQESECTCVNGSCFTIMTDGPSNGLASYKIFKIEKGKVTKSIELNAPNSHYEECSCYPDTGKVMCVCRDNWHGSNRPWVSFDQNLDYQIGYICSGVFGDNPRPKDGPGSCGPVSADGANGVKGFSYRYGNGVWIGRTKSDSSRHGFEMIWDPNGWTETDSRFSVRQDVVAMTDRSGYSGSFVQHPELTGLDCMRPCFWVELIRGRPEEETIWTSGSIISFCGVNSDTVDWSWPDGAELPFTIDK	Successful	Developing new antiviral agents for influenza treatment: what does the future hold Clin Infect Dis. 2009 Jan 1;48 Suppl 1:S3-13.	34	.	.	.	.	.	.	.	.	.	.	stm00511:Other glycan degradation	.	.	.
TTQI726	Influenza Nucleoprotein (Influ NP)	P03466	NCAP_I34A1	.	Influ Protein N; Influ Nucleoprotein; Influ Nucleocapsid protein	Influ NP	"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."	.	5V5O; 5NQ3; 5NPZ; 4ZDU; 4NQV	MASQGTKRSYEQMETDGERQNATEIRASVGKMIGGIGRFYIQMCTELKLSDYEGRLIQNSLTIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRVNGKWMRELILYDKEEIRRIWRQANNGDDATAGLTHMMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELVRMIKRGINDRNFWRGENGRKTRIAYERMCNILKGKFQTAAQKAMMDQVRESRNPGNAEFEDLTFLARSALILRGSVAHKSCLPACVYGPAVASGYDFEREGYSLVGIDPFRLLQNSQVYSLIRPNENPAHKSQLVWMACHSAAFEDLRVLSFIKGTKVLPRGKLSTRGVQIASNENMETMESSTLELRSRYWAIRTRSGGNTNQQRASAGQISIQPTFSVQRNLPFDRTTIMAAFNGNTEGRTSDMRTEIIRMMESARPEDVSFQGRGVFELSDEKAASPIVPSFDMSNEGSYFFGDNAEEYDN	Literature-reported	Influenza A Virus Nucleoprotein: A Highly Conserved Multi-Functional Viral Protein as a Hot Antiviral Drug Target. Curr Top Med Chem. 2017;17(20):2271-2285.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-168255: Influenza Infection; R-HSA-168271: Transport of Ribonucleoproteins into the Host Nucleus; R-HSA-168275: Entry of Influenza Virion into Host Cell via Endocytosis; R-HSA-168288: Fusion of the Influenza Virion to the Host Cell Endosome; R-HSA-168298: Release; R-HSA-168302: Budding; R-HSA-168303: Packaging of Eight RNA Segments; R-HSA-168316: Assembly of Viral Components at the Budding Site; R-HSA-168325: Viral Messenger RNA Synthesis; R-HSA-168330: Viral RNP Complexes in the Host Cell Nucleus; R-HSA-168333: NEP/NS2 Interacts with the Cellular Export Machinery; R-HSA-168336: Uncoating of the Influenza Virion; R-HSA-192814: vRNA Synthesis; R-HSA-192823: Viral mRNA Translation; R-HSA-192869: cRNA Synthesis; R-HSA-192905: vRNP Assembly	.	.
TTRG72O	Influenza NP messenger RNA (Influ NP mRNA)	O92784	NCAP_I97A1	mRNA target	Influenza nucleoprotein (mRNA); Influenza nucleocapsid protein (mRNA)	Influ NP mRNA	"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."	.	.	MASQGTKRSYEQMETGGERQNATEIRASVGRMVGGIGRFYIQMCTELKLSDQEGRLIQNSITIERMVLSAFDERRNRYLEEHPSAGKDPKKTGGPIYRRRDGKWVRELILYDKEEIRRIWRQANNGEDATAGLTHMMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAIKGVGTMVMELIRMIKRGINDRNFWRGENGRRTRIAYERMCNILKGKFQTAAQKAMMDQVRESRNPGNAEIEDLIFLARSALILRGSVAHKSCLPACVYGPAVASGYDFEREGYSLVGIDPFRLLQNSQVFSLIRPKENPAHKSQLVWMACHSAAFEDLRVSSFIRGTRVIPRGQLSTRGVQIASNENVEAMDSTTLELRSRYWAIRTRSGGNTNQQRASAGQISVQPTFSVQRNLPFERVTIMAAFKGNTEGRTSDMRTEIIRMMESARPEDVSFQGRGVFELSDEKATNPIVPSFDMSNEGSYFFGDNAEEYDN	Literature-reported	"US patent application no. 5,580,767, Inhibition of influenza viruses by antisense oligonucleotides."	0	mRNA	mRNA target	.	.	.	Influenza virus nucleoprotein	PF00506	PF00506; Flu_NP	.	.	.	.	.	.
TTWORX6	Influenza Polymerase acidic endonuclease (Influ PA)	P03433	PA_I34A1	.	RNA-directed RNA polymerase subunit P2; Polymerase acidic protein	Influ PA	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.	EC 3.1.-.-	5JHV; 5JHT; 5I13; 5FDG; 5FDD	MEDFVRQCFNPMIVELAEKTMKEYGEDLKIETNKFAAICTHLEVCFMYSDFHFINEQGESIIVELGDPNALLKHRFEIIEGRDRTMAWTVVNSICNTTGAEKPKFLPDLYDYKENRFIEIGVTRREVHIYYLEKANKIKSEKTHIHIFSFTGEEMATKADYTLDEESRARIKTRLFTIRQEMASRGLWDSFRQSERGEETIEERFEITGTMRKLADQSLPPNFSSLENFRAYVDGFEPNGYIEGKLSQMSKEVNARIEPFLKTTPRPLRLPNGPPCSQRSKFLLMDALKLSIEDPSHEGEGIPLYDAIKCMRTFFGWKEPNVVKPHEKGINPNYLLSWKQVLAELQDIENEEKIPKTKNMKKTSQLKWALGENMAPEKVDFDDCKDVGDLKQYDSDEPELRSLASWIQNEFNKACELTDSSWIELDEIGEDVAPIEHIASMRRNYFTSEVSHCRATEYIMKGVYINTALLNASCAAMDDFQLIPMISKCRTKEGRRKTNLYGFIIKGRSHLRNDTDVVNFVSMEFSLTDPRLEPHKWEKYCVLEIGDMLIRSAIGQVSRPMFLYVRTNGTSKIKMKWGMEMRRCLLQSLQQIESMIEAESSVKEKDMTKEFFENKSETWPIGESPKGVEESSIGKVCRTLLAKSVFNSLYASPQLEGFSAESRKLLLIVQALRDNLEPGTFDLGGLYEAIEECLINDPWVLLNASWFNSFLTHALS	Successful	2018 FDA drug approvals.Nat Rev Drug Discov. 2019 Feb;18(2):85-89. 	34	.	.	.	.	.	.	.	.	.	.	.	R-HSA-168255: Influenza Infection; R-HSA-168271: Transport of Ribonucleoproteins into the Host Nucleus; R-HSA-168275: Entry of Influenza Virion into Host Cell via Endocytosis; R-HSA-168288: Fusion of the Influenza Virion to the Host Cell Endosome; R-HSA-168298: Release; R-HSA-168302: Budding; R-HSA-168303: Packaging of Eight RNA Segments; R-HSA-168325: Viral Messenger RNA Synthesis; R-HSA-168330: Viral RNP Complexes in the Host Cell Nucleus; R-HSA-168333: NEP/NS2 Interacts with the Cellular Export Machinery; R-HSA-168336: Uncoating of the Influenza Virion; R-HSA-192814: vRNA Synthesis; R-HSA-192823: Viral mRNA Translation; R-HSA-192869: cRNA Synthesis; R-HSA-192905: vRNP Assembly	.	.
TT6HV2K	Influenza PB1 messenger RNA (Influ PB1 mRNA)	Q9WLS3	RDRP_I97A1	mRNA target	RNA-directed RNA polymerase subunit P1 (mRNA); RNA-directed RNA polymerase catalytic subunit (mRNA); Polymerase basic protein 1 (mRNA)	Influ PB1 mRNA	"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."	EC 2.7.7.48	3CM8	MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSEKGRWTTNTETGAPQLNPIDGPLPEDNEPSGYAQTDCVLEAMAFLEESHPGLFENSCLETMEVVQQTRMDKLTQGRQTYDWTLNRNQPAATALANTIEVFRSNGLTANESGRLIDFLKDVMESMDKEEMEITTHFQRKRRVRDNMTKKMVTQRTIGKKKQRLTKKSYLIRALTLNTMTKDAERGKLKRRAIATPGMQIRGFVHFVEALARSICEKLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTELSFTVTGDNTKWNENQNPRIFLAMITYITRNQPEWFRNVLSIAPIMFSNKMARLGKGYMFESKSMKLRTQIPAEMLANIDLKYFNESTRKKIEKIRPLLVEGTASLSPGMMMGMFNMLSTVLGVSILNLGQKRYTKTTYWWDGLQSSDDFALIVNAPNHEGIQAGVDRFYRTCKLVGINMSKKKSYINRTGTFEFTSFFYRYGFVANFSMELPSFGVSGINESADMSIGVTVIKNNMINNDLGPATAQMALQLFIKDYRYTYRCHRGDTQIQTRRSFELKKLWEQTRSKAGLLVSDGGPNLYNIRNLHIPEVGLKWELMDEDYQGRLCNPLNPFVSHKEVESVNNAVVMPAHGPAKSMEYDAVATTHSWIPKRNRSILNTSQRGILEDEQMYQKCCTLFEKFFPSSSYRRPVGISSMMEAMVSRARIDARIDFESGRIKKEEFAEILKICSTIEELGRQGK	Literature-reported	"US patent application no. 5,580,767, Inhibition of influenza viruses by antisense oligonucleotides."	0	mRNA	mRNA target	.	.	.	Influenza RNA-dependent RNA polymerase subunit PB1	PF00602	PF00602; Flu_PB1	.	.	.	.	.	.
TT62KQV	Influenza Polymerase basic protein 2 (Influ PB2)	P03428	PB2_I34A1	.	RNA-directed RNA polymerase subunit P3; Polymerase basic protein 2	Influ PB2	"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."	.	4U6O; 4J2R; 4ENF; 3WI1; 3WI0	MERIKELRNLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRITEMIPERNEQGQTLWSKMNDAGSDRVMVSPLAVTWWNRNGPITNTVHYPKIYKTYFERVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKKEELQDCKISPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVDQSLIIAARNIVRRAAVSADPLASLLEMCHSTQIGGIRMVDILRQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTSGSSVKREEEVLTGNLQTLKIRVHEGYEEFTMVGRRATAILRKATRRLIQLIVSGRDEQSIAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQNWGVEPIDNVMGMIGILPDMTPSIEMSMRGVRISKMGVDEYSSTERVVVSIDRFLRIRDQRGNVLLSPEEVSETQGTEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQNPTMLYNKMEFEPFQSLVPKAIRGQYSGFVRTLFQQMRDVLGTFDTAQIIKLLPFAAAPPKQSRMQFSSFTVNVRGSGMRILVRGNSPVFNYNKATKRLTVLGKDAGTLTEDPDEGTAGVESAVLRGFLILGKEDKRYGPALSINELSNLAKGEKANVLIGQGDVVLVMKRKRDSSILTDSQTATKRIRMAIN	Clinical trial	"Discovery of a novel, first-in-class, orally bioavailable azaindole inhibitor (VX-787) of influenza PB2. J Med Chem. 2014 Aug 14;57(15):6668-78."	21	.	.	.	.	.	.	.	.	.	.	.	R-HSA-168255: Influenza Infection; R-HSA-168271: Transport of Ribonucleoproteins into the Host Nucleus; R-HSA-168275: Entry of Influenza Virion into Host Cell via Endocytosis; R-HSA-168288: Fusion of the Influenza Virion to the Host Cell Endosome; R-HSA-168298: Release; R-HSA-168302: Budding; R-HSA-168303: Packaging of Eight RNA Segments; R-HSA-168325: Viral Messenger RNA Synthesis; R-HSA-168330: Viral RNP Complexes in the Host Cell Nucleus; R-HSA-168333: NEP/NS2 Interacts with the Cellular Export Machinery; R-HSA-168336: Uncoating of the Influenza Virion; R-HSA-192814: vRNA Synthesis; R-HSA-192823: Viral mRNA Translation; R-HSA-192869: cRNA Synthesis; R-HSA-192905: vRNP Assembly	.	.
TTSC4OM	Influenza PB2 messenger RNA (Influ PB2 mRNA)	O56266	PB2_I97A1	mRNA target	RNA-directed RNA polymerase subunit P3 (mRNA); Polymerase basic protein 2 (mRNA); PB2 (mRNA)	Influ PB2 mRNA	"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."	.	.	MERIKELRDLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRIMEMIPERNEQGQTLWSKTNDAGSDRVMVSPLAVTWWNRNGPTTSTVHYPKVYKTYFEKVERLKHGTFGPVHFRNQVKIRRRVDMNPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKREELKNCNISPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVDQSLIIAARNIVRRATVSADPLASLLEMCHSTQIGGVRMVDILKQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTKGFSVKREEEVLTGNLQTLKIKVHEGYEEFTMVGRRATAILRKATRRMIQLIVSGRDEQSIAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQNWGIEPIDNVMGMIGILPDMTPSTEMSLRGVRVSKMGVDEYSSTERVVVSIDRFLRVRDQQGNVLLSPEEVSETQGMEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQEPTMLYNKMEFEPFQSLVPKAARSQYSGFVRTLFQQMRDVLGTFDTVQIIKLLPFAAAPPEQSRMQFSSLTVNVRGSGMRILVRGNSPAFNYNKTTKRLTILGKDAGALTEDPDEGTAGVESAVLRGFLILGKEDKRYGPALSINELSNLTKGEKANVLIRQGDVVLVMKRKRDSSILTDSQTATKRIRMAIN	Literature-reported	"US patent application no. 5,580,767, Inhibition of influenza viruses by antisense oligonucleotides."	0	mRNA	mRNA target	.	.	.	Influenza RNA-dependent RNA polymerase subunit PB2	PF00604	PF00604; Flu_PB2	.	.	.	.	.	.
TTXAUJ8	Influenza M messenger RNA (Influenza M mRNA)	O70632	M2_I97A1	mRNA target	Proton channel protein M2 (mRNA); Matrix protein 2 (mRNA); M (mRNA)	Influenza M mRNA	"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."	.	6MPN; 6MPM; 6MPL; 4RWC; 4RWB	MSLLTEVETLTRNGWGCRCSDSSDPLVVAASIIGILHLILWILDRLFFKCIYRRFKYGLKRGPSTEGVPESMREEYRQEQQNAVDVDDGHFVNIELE	Literature-reported	"US patent application no. 5,580,767, Inhibition of influenza viruses by antisense oligonucleotides."	0	mRNA	mRNA target	.	.	.	Influenza Matrix protein (M2)	PF00599	PF00599; Flu_M2	.	.	.	.	.	.
TTM27B5	Influenza NA messenger RNA (Influenza NA mRNA)	Q9W7Y7	NRAM_I97A1	mRNA target	Neuraminidase (mRNA); NA of influenza (mRNA)	Influenza NA mRNA	"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."	EC 3.2.1.18	.	MNPNQKIITIGSICMVVGIISLMLQIGNIISVWVSHIIQTWHPNQPEPCNQSINFYTEQAAASVTLAGNSSLCPISGWAIYSKDNSIRIGSKGDVFVIREPFISCSHLECRTFFLTQGALLNDKHSNGTVKDRSPYRTLMSCPVGEAPSPYNSRFESVAWSASACHDGISWLTIGISGPDNGAVAVLKYNGIITDTIKSWRNNILRTQESECACVNGSCFTVMTDGPSNEQASYKIFKIEKGRVVKSVELNAPNYHYEECSCYPDAGEITCVCRDNWHGSNRPWVSFNQNLEYQIGYICSGVFGDSPRPNDGTGSCGPVSLNGAYGVKGFSFKYGNGVWIGRTKSTSSRSGFEMIWDPNGWTETDSSFSLKQDIIAITDWSGYSGSFIQHPELTGLNCMRPCFWVELIRGRPKEKTIWTSGSSISFCGVNSDTVGWSWPDGADLPFTIDK	Literature-reported	Respiratory viral diseases: access to RNA interference therapy. Drug Discov Today Ther Strateg. 2007; 4(4): 273-276.	2.1	mRNA	mRNA target	.	.	.	Neuraminidase	PF00064	PF00064; Neur	.	.	.	.	.	.
TTVB30D	Inhibin beta A chain (INHBA)	P08476	INHBA_HUMAN	.	Activin beta-A chain; Erythroid differentiation protein; EDF	INHBA	"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."	.	1NYS;1NYU;1S4Y;2ARP;2ARV;2B0U;2P6A;3B4V;4MID;5HLY;5HLZ;6Y6N;6Y6O;7OLY;7U5P	MPLLWLRGFLLASCWIIVRSSPTPGSEGHSAAPDCPSCALAALPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGEEAEEVGLKGERSELLLSEKVVDARKSTWHVFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGKKKKKEEEGEGKKKGGGEGGAGADEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS	Clinical trial	Pharmacokinetics and Pharmacodynamics of Garetosmab (Anti-Activin A): Results From a First-in-Human Phase 1 Study. J Clin Pharmacol. 2020 Nov;60(11):1424-1431.	.	.	.	.	.	.	.	.	.	.	.	hsa:3624	R-HSA-1502540;R-HSA-201451;R-HSA-209822;R-HSA-2473224;	.	P08476;
TT9RV4P	Activin (ACT)	P08476; P09529; P55103; P58166	INHBA_HUMAN; INHBB_HUMAN; INHBC_HUMAN; INHBE_HUMAN	.	Inhibin beta; Activin beta	INHBA	"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."	.	.	MPLLWLRGFLLASCWIIVRSSPTPGSEGHSAAPDCPSCALAALPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGEEAEEVGLKGERSELLLSEKVVDARKSTWHVFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGKKKKKEEEGEGKKKGGGEGGAGADEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04350: TGF-beta signaling pathway; hsa04550: Signaling pathways regulating pluripotency of stem cells	R-HSA-1502540: Signaling by Activin; R-HSA-209822: Glycoprotein hormones; R-HSA-2473224: Antagonism of Activin by Follistatin	.	P08476
TTW0PHM	Inositol polyphosphate 1-phosphatase (INPP1)	P49441	INPP_HUMAN	Phosphoric monoester hydrolase	IPPase; IPP	INPP1	"Removes the phosphate group at position 1 of the inositol ring from the polyphosphates inositol 1,4-bisphosphate and inositol 1,3,4-trisphophosphate."	EC 3.1.3.57	.	MSDILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEVIKQNMENKFPGLEKNIFGEESNEFTNDWGEKITLRLCSTEEETAELLSKVLNGNKVASEALARVVHQDVAFTDPTLDSTEINVPQDILGIWVDPIDSTYQYIKGSADIKSNQGIFPCGLQCVTILIGVYDIQTGVPLMGVINQPFVSRDPNTLRWKGQCYWGLSYMGTNMHSLQLTISRRNGSETHTGNTGSEAAFSPSFSAVISTSEKETIKAALSRVCGDRIFGAAGAGYKSLCVVQGLVDIYIFSEDTTFKWDSCAAHAILRAMGGGIVDLKECLERNPETGLDLPQLVYHVENEGAAGVDRWANKGGLIAYRSRKRLETFLSLLVQNLAPAETHT	Literature-reported	Crystal structure of an enzyme displaying both inositol-polyphosphate-1-phosphatase and 3'-phosphoadenosine-5'-phosphate phosphatase activities: a ... J Mol Biol. 2002 Jan 25;315(4):677-85.	.	.	.	.	.	.	.	.	.	.	.	hsa00562: Inositol phosphate metabolism; hsa01100: Metabolic pathways; hsa04070: Phosphatidylinositol signaling system	"R-HSA-1855183: Synthesis of IP2, IP, and Ins in the cytosol"	MetaCyc:HS07761-MON	P49441
TTTP2Z1	SH2 domain inositol 5'-phosphatase 1 (INPP5D)	Q92835	SHIP1_HUMAN	Phosphoric monoester hydrolase	"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"	INPP5D	"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."	EC 3.1.3.86	6IBD; 2YSX	MVPCWNHGNITRSKAEELLSRTGKDGSFLVRASESISRAYALCVLYRNCVYTYRILPNEDDKFTVQASEGVSMRFFTKLDQLIEFYKKENMGLVTHLQYPVPLEEEDTGDDPEEDTVESVVSPPELPPRNIPLTASSCEAKEVPFSNENPRATETSRPSLSETLFQRLQSMDTSGLPEEHLKAIQDYLSTQLAQDSEFVKTGSSSLPHLKKLTTLLCKELYGEVIRTLPSLESLQRLFDQQLSPGLRPRPQVPGEANPINMVSKLSQLTSLLSSIEDKVKALLHEGPESPHRPSLIPPVTFEVKAESLGIPQKMQLKVDVESGKLIIKKSKDGSEDKFYSHKKILQLIKSQKFLNKLVILVETEKEKILRKEYVFADSKKREGFCQLLQQMKNKHSEQPEPDMITIFIGTWNMGNAPPPKKITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLSEKEWLEILKHSLQEITSVTFKTVAIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNSHLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWFGDLNYRVDLPTWEAETIIQKIKQQQYADLLSHDQLLTERREQKVFLHFEEEEITFAPTYRFERLTRDKYAYTKQKATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKNGPGTVDSQGQIEFLRCYATLKTKSQTKFYLEFHSSCLESFVKSQEGENEEGSEGELVVKFGETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLEATETQLPIYTPLTHHGELTGHFQGEIKLQTSQGKTREKLYDFVKTERDESSGPKTLKSLTSHDPMKQWEVTSRAPPCSGSSITEIINPNYMGVGPFGPPMPLHVKQTLSPDQQPTAWSYDQPPKDSPLGPCRGESPPTPPGQPPISPKKFLPSTANRGLPPRTQESRPSDLGKNAGDTLPQEDLPLTKPEMFENPLYGSLSSFPKPAPRKDQESPKMPRKEPPPCPEPGILSPSIVLTKAQEADRGEGPGKQVPAPRLRSFTCSSSAEGRAAGGDKSQGKPKTPVSSQAPVPAKRPIKPSRSEINQQTPPTPTPRPPLPVKSPAVLHLQHSKGRDYRDNTELPHHGKHRPEEGPPGPLGRTAMQ	Clinical trial	"Characterization of AQX-1125, a small-molecule SHIP1 activator: Part 2. Efficacy studies in allergic and pulmonary inflammation models in vivo. Br J Pharmacol. 2013 Mar;168(6):1519-29."	21	EC:3.1.3	Phosphoric monoester hydrolases	"inositol 1,4,5-trisphosphate 5-phosphatase family."	3.1.3.86	Acting on ester bonds	Endonuclease/Exonuclease/phosphatase family; SH2 domain	PF03372; PF00017	PF03372; Exo_endo_phos; PF00017; SH2	.	.	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	R-HSA-210990:PECAM1 interactions; R-HSA-912526:Interleukin receptor SHC signaling	MetaCyc:HS09849-MON	Q92835
TTZOPHG	Insulin (INS)	P01308	INS_HUMAN	.	Insulin	INS	"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."	.	6HN5; 6CK2; 6CEB; 6CE9; 6CE7	MALWMRLLPLLALLALWGPDPAAAFVNQHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYCN	Successful	"2005 approvals: Safety first. Nature Reviews Drug Discovery 5, 92-93 (February 2006)."	34	.	Insulin family	insulin family.	.	.	Insulin/IGF/Relaxin family	PF00049	PF00049; Insulin	.	.	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	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	MetaCyc:MON-16190	P01308
TTCBFJO	Insulin receptor (INSR)	P06213	INSR_HUMAN	Kinase	IR; CD220 antigen; CD220	INSR	"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."	EC 2.7.10.1	6HN5; 6HN4; 5U1M; 5KQV; 5J3H	MATGGRRGAAAAPLLVAVAALLLGAAGHLYPGEVCPGMDIRNNLTRLHELENCSVIEGHLQILLMFKTRPEDFRDLSFPKLIMITDYLLLFRVYGLESLKDLFPNLTVIRGSRLFFNYALVIFEMVHLKELGLYNLMNITRGSVRIEKNNELCYLATIDWSRILDSVEDNYIVLNKDDNEECGDICPGTAKGKTNCPATVINGQFVERCWTHSHCQKVCPTICKSHGCTAEGLCCHSECLGNCSQPDDPTKCVACRNFYLDGRCVETCPPPYYHFQDWRCVNFSFCQDLHHKCKNSRRQGCHQYVIHNNKCIPECPSGYTMNSSNLLCTPCLGPCPKVCHLLEGEKTIDSVTSAQELRGCTVINGSLIINIRGGNNLAAELEANLGLIEEISGYLKIRRSYALVSLSFFRKLRLIRGETLEIGNYSFYALDNQNLRQLWDWSKHNLTITQGKLFFHYNPKLCLSEIHKMEEVSGTKGRQERNDIALKTNGDQASCENELLKFSYIRTSFDKILLRWEPYWPPDFRDLLGFMLFYKEAPYQNVTEFDGQDACGSNSWTVVDIDPPLRSNDPKSQNHPGWLMRGLKPWTQYAIFVKTLVTFSDERRTYGAKSDIIYVQTDATNPSVPLDPISVSNSSSQIILKWKPPSDPNGNITHYLVFWERQAEDSELFELDYCLKGLKLPSRTWSPPFESEDSQKHNQSEYEDSAGECCSCPKTDSQILKELEESSFRKTFEDYLHNVVFVPRKTSSGTGAEDPRPSRKRRSLGDVGNVTVAVPTVAAFPNTSSTSVPTSPEEHRPFEKVVNKESLVISGLRHFTGYRIELQACNQDTPEERCSVAAYVSARTMPEAKADDIVGPVTHEIFENNVVHLMWQEPKEPNGLIVLYEVSYRRYGDEELHLCVSRKHFALERGCRLRGLSPGNYSVRIRATSLAGNGSWTEPTYFYVTDYLDVPSNIAKIIIGPLIFVFLFSVVIGSIYLFLRKRQPDGPLGPLYASSNPEYLSASDVFPCSVYVPDEWEVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELMAHGDLKSYLRSLRPEAENNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLHPSFPEVSFFHSEENKAPESEELEMEFEDMENVPLDRSSHCQREEAGGRDGGSSLGFKRSYEEHIPYTHMNGGKKNGRILTLPRSNPS	Successful	New drugs for type 2 diabetes mellitus: what is their place in therapy Drugs. 2008;68(15):2131-62.	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Furin-like cysteine rich region; Insulin receptor trans-membrane segment; Protein tyrosine kinase; Receptor L domain	PF00757; PF17870; PF07714; PF01030	PF00757; Furin-like; PF17870; Insulin_TMD; PF07714; Pkinase_Tyr; PF01030; Recep_L_domain	.	.	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	R-HSA-74713:IRS activation; R-HSA-74749:Signal attenuation; R-HSA-74751:Insulin receptor signalling cascade; R-HSA-77387:Insulin receptor recycling	.	P06213
TTXAJWN	IL-1 receptor-associated kinase 1 (IRAK1)	P51617	IRAK1_HUMAN	Kinase	Interleukin-1 receptor-associated kinase 1; IRAK-1; IRAK	IRAK1	"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."	EC 2.7.11.1	6BFN	MAGGPGPGEPAAPGAQHFLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSGQRTASVLWPWINRNARVADLVHILTHLQLLRARDIITAWHPPAPLPSPGTTAPRPSSIPAPAEAEAWSPRKLPSSASTFLSPAFPGSQTHSGPELGLVPSPASLWPPPPSPAPSSTKPGPESSVSLLQGARPFPFCWPLCEISRGTHNFSEELKIGEGGFGCVYRAVMRNTVYAVKRLKENADLEWTAVKQSFLTEVEQLSRFRHPNIVDFAGYCAQNGFYCLVYGFLPNGSLEDRLHCQTQACPPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLTPKLGDFGLARFSRFAGSSPSQSSMVARTQTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVVLETLAGQRAVKTHGARTKYLKDLVEEEAEEAGVALRSTQSTLQAGLAADAWAAPIAMQIYKKHLDPRPGPCPPELGLGLGQLACCCLHRRAKRRPPMTQVYERLEKLQAVVAGVPGHSEAASCIPPSPQENSYVSSTGRAHSGAAPWQPLAAPSGASAQAAEQLQRGPNQPVESDESLGGLSAALRSWHLTPSCPLDPAPLREAGCPQGDTAGESSWGSGPGSRPTAVEGLALGSSASSSSEPPQIIINPARQKMVQKLALYEDGALDSLQLLSSSSLPGLGLEQDRQGPEESDEFQS	Patented-recorded	Inhibitors of interleukin-1 receptor-associated kinase 4 (IRAK4): a patent review (2012-2015).Expert Opin Ther Pat. 2016 Aug;26(8):917-32.	15.5	EC:2.7	.	protein kinase superfamily. TKL Ser/Thr protein kinase family. Pelle subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Death domain; Protein kinase domain	PF00531; PF00069	PF00531; Death; PF00069; Pkinase	.	.	hsa04010: MAPK signaling pathway; hsa04064: NF-kappa B signaling pathway; hsa04620: Toll-like receptor signaling pathway; hsa04722: Neurotrophin signaling pathway; hsa04936: Alcoholic liver disease; hsa05130: Pathogenic Escherichia coli infection; hsa05132: Salmonella infection; hsa05133: Pertussis; hsa05135: Yersinia infection; hsa05140: Leishmaniasis; hsa05142: Chagas disease; hsa05145: Toxoplasmosis; hsa05152: Tuberculosis; hsa05161: Hepatitis B; hsa05162: Measles; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05171: Coronavirus disease - COVID-19; hsa05417: Lipid and atherosclerosis	"R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-166058: MyD88:MAL(TIRAP) cascade initiated on plasma membrane; R-HSA-168638: NOD1/2 Signaling Pathway; R-HSA-209543: p75NTR recruits signalling complexes; R-HSA-209560: NF-kB is activated and signals survival; R-HSA-445989: TAK1-dependent IKK and NF-kappa-B activation; 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-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-8986944: Transcriptional Regulation by MECP2; R-HSA-9020702: Interleukin-1 signaling; R-HSA-937039: IRAK1 recruits IKK complex; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses; 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-975144: IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation; R-HSA-975155: MyD88 dependent cascade initiated on endosome; R-HSA-975871: MyD88 cascade initiated on plasma membrane"	.	P51617
TTBPJOK	IL-1 receptor-associated kinase 3 (IRAK3)	Q9Y616	IRAK3_HUMAN	Kinase	Interleukin-1 receptor-associated kinase 3; IRAK-M; IRAK-3; IL-1 receptor-associated kinase M	IRAK3	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.	EC 2.7.11.1	5UKE	MAGNCGARGALSAHTLLFDLPPALLGELCAVLDSCDGALGWRGLAERLSSSWLDVRHIEKYVDQGKSGTRELLWSWAQKNKTIGDLLQVLQEMGHRRAIHLITNYGAVLSPSEKSYQEGGFPNILFKETANVTVDNVLIPEHNEKGILLKSSISFQNIIEGTRNFHKDFLIGEGEIFEVYRVEIQNLTYAVKLFKQEKKMQCKKHWKRFLSELEVLLLFHHPNILELAAYFTETEKFCLIYPYMRNGTLFDRLQCVGDTAPLPWHIRIGILIGISKAIHYLHNVQPCSVICGSISSANILLDDQFQPKLTDFAMAHFRSHLEHQSCTINMTSSSSKHLWYMPEEYIRQGKLSIKTDVYSFGIVIMEVLTGCRVVLDDPKHIQLRDLLRELMEKRGLDSCLSFLDKKVPPCPRNFSAKLFCLAGRCAATRAKLRPSMDEVLNTLESTQASLYFAEDPPTSLKSFRCPSPLFLENVPSIPVEDDESQNNNLLPSDEGLRIDRMTQKTPFECSQSEVMFLSLDKKPESKRNEEACNMPSSSCEESWFPKYIVPSQDLRPYKVNIDPSSEAPGHSCRSRPVESSCSSKFSWDEYEQYKKE	Literature-reported	"Improvement in oral bioavailability of 2,4-diaminopyrimidine c-Met inhibitors by incorporation of a 3-amidobenzazepin-2-one group. Bioorg Med Chem. 2011 Nov 1;19(21):6274-84."	0	EC:2.7	.	protein kinase superfamily. TKL Ser/Thr protein kinase family. Pelle subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Death domain; Protein kinase domain	PF00531; PF00069	PF00531; Death; PF00069; Pkinase	.	.	hsa04722: Neurotrophin signaling pathway	R-HSA-166058: MyD88:MAL(TIRAP) cascade initiated on plasma membrane; R-HSA-9020702: Interleukin-1 signaling	.	Q9Y616
TTILUKB	IRAK4 messenger RNA (IRAK4 mRNA)	Q9NWZ3	IRAK4_HUMAN	mRNA target	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)	IRAK4	"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."	EC 2.7.11.1	6O9D; 6O95; 6O94; 6O8U; 6N8G	MNKPITPSTYVRCLNVGLIRKLSDFIDPQEGWKKLAVAIKKPSGDDRYNQFHIRRFEALLQTGKSPTSELLFDWGTTNCTVGDLVDLLIQNEFFAPASLLLPDAVPKTANTLPSKEAITVQQKQMPFCDKDRTLMTPVQNLEQSYMPPDSSSPENKSLEVSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIKVMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANILLDEAFTAKISDFGLARASEKFAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQLLLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS	Literature-reported	"US patent application no. 6,692,959, Antisense modulation of IL-1 receptor-associated kinase-4 expression."	0	mRNA	mRNA target	.	.	.	Protein tyrosine kinase	PF07714	PF07714; Pkinase_Tyr	.	.	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	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	.	Q9NWZ3
TTKFVXR	Renal carcinoma antigen NY-REN-64 (IRAK-4)	Q9NWZ3	IRAK4_HUMAN	Kinase	Interleukin-1 receptor-associated kinase 4; IRAK-4	IRAK4	"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."	EC 2.7.11.1	6O9D; 6O95; 6O94; 6O8U; 6N8G	MNKPITPSTYVRCLNVGLIRKLSDFIDPQEGWKKLAVAIKKPSGDDRYNQFHIRRFEALLQTGKSPTSELLFDWGTTNCTVGDLVDLLIQNEFFAPASLLLPDAVPKTANTLPSKEAITVQQKQMPFCDKDRTLMTPVQNLEQSYMPPDSSSPENKSLEVSDTRFHSFSFYELKNVTNNFDERPISVGGNKMGEGGFGVVYKGYVNNTTVAVKKLAAMVDITTEELKQQFDQEIKVMAKCQHENLVELLGFSSDGDDLCLVYVYMPNGSLLDRLSCLDGTPPLSWHMRCKIAQGAANGINFLHENHHIHRDIKSANILLDEAFTAKISDFGLARASEKFAQTVMTSRIVGTTAYMAPEALRGEITPKSDIYSFGVVLLEIITGLPAVDEHREPQLLLDIKEEIEDEEKTIEDYIDKKMNDADSTSVEAMYSVASQCLHEKKNKRPDIKKVQQLLQEMTAS	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	EC:2.7	Kinase	protein kinase superfamily. TKL Ser/Thr protein kinase family. Pelle subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein tyrosine kinase	PF07714	PF07714; Pkinase_Tyr	.	.	hsa04010: MAPK signaling pathway; hsa04064: NF-kappa B signaling pathway; hsa04620: Toll-like receptor signaling pathway; hsa04621: NOD-like receptor signaling pathway; hsa04722: Neurotrophin signaling pathway; hsa04936: Alcoholic liver disease; hsa05130: Pathogenic Escherichia coli infection; hsa05132: Salmonella infection; hsa05133: Pertussis; hsa05135: Yersinia infection; hsa05140: Leishmaniasis; hsa05142: Chagas disease; hsa05145: Toxoplasmosis; hsa05152: Tuberculosis; hsa05161: Hepatitis B; hsa05162: Measles; hsa05164: Influenza A; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05171: Coronavirus disease - COVID-19; hsa05417: Lipid and atherosclerosis	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	.	Q9NWZ3
TT4TU3L	Interferon regulatory factor 1 (IRF1)	P10914	IRF1_HUMAN	.	IRF-1	IRF1	"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."	.	.	MPITRMRMRPWLEMQINSNQIPGLIWINKEEMIFQIPWKHAAKHGWDINKDACLFRSWAIHTGRYKAGEKEPDPKTWKANFRCAMNSLPDIEEVKDQSRNKGSSAVRVYRMLPPLTKNQRKERKSKSSRDAKSKAKRKSCGDSSPDTFSDGLSSSTLPDDHSSYTVPGYMQDLEVEQALTPALSPCAVSSTLPDWHIPVEVVPDSTSDLYNFQVSPMPSTSEATTDEDEEGKLPEDIMKLLEQSEWQPTNVDGKGYLLNEPGVQPTSVYGDFSCKEEPEIDSPGGDIGLSLQRVFTDLKNMDATWLDSLLTPVRLPSIQAIPCAP	Literature-reported	The transcription factor interferon regulatory factor 1 is expressed after cerebral ischemia and contributes to ischemic brain injury. J Exp Med. 1999 Feb 15;189(4):719-27.	.	.	.	IRF family.	.	.	Interferon regulatory factor transcription factor	PF00605	PF00605; IRF	.	.	hsa04625: C-type lectin receptor signaling pathway; hsa04668: TNF signaling pathway; hsa04917: Prolactin signaling pathway; hsa05133: Pertussis; hsa05165: Human papillomavirus infection	R-HSA-5620971: Pyroptosis; R-HSA-877300: Interferon gamma signaling; R-HSA-909733: Interferon alpha/beta signaling; R-HSA-983231: Factors involved in megakaryocyte development and platelet production	.	P10914
TTYR7OH	Interferon regulatory factor 3 (IRF3)	Q14653	IRF3_HUMAN	.	IRF-3	IRF3	"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."	.	5JER; 5JEO; 5JEM; 5JEL; 5JEK	MGTPKPRILPWLVSQLDLGQLEGVAWVNKSRTRFRIPWKHGLRQDAQQEDFGIFQAWAEATGAYVPGRDKPDLPTWKRNFRSALNRKEGLRLAEDRSKDPHDPHKIYEFVNSGVGDFSQPDTSPDTNGGGSTSDTQEDILDELLGNMVLAPLPDPGPPSLAVAPEPCPQPLRSPSLDNPTPFPNLGPSENPLKRLLVPGEEWEFEVTAFYRGRQVFQQTISCPEGLRLVGSEVGDRTLPGWPVTLPDPGMSLTDRGVMSYVRHVLSCLGGGLALWRAGQWLWAQRLGHCHTYWAVSEELLPNSGHGPDGEVPKDKEGGVFDLGPFIVDLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMVKVVPTCLRALVEMARVGGASSLENTVDLHISNSHPLSLTSDQYKAYLQDLVEGMDFQGPGES	Literature-reported	Inhibition of lipopolysaccharide-induced interferon regulatory factor 3 activation and protection from septic shock by hydroxystilbenes. Shock. 2004 May;21(5):470-5.	0	.	.	IRF family.	.	.	Interferon regulatory factor transcription factor; Interferon-regulatory factor 3	PF00605; PF10401	PF00605; IRF; PF10401; IRF-3	.	.	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	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	.	Q14653
TTHUBNK	Interferon consensus sequence binding protein (IRF8)	Q02556	IRF8_HUMAN	.	Interferon regulatory factor 8; Interferon consensus sequence-binding protein; IRF-8; ICSBP1; ICSBP; H-ICSBP	IRF8	"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."	.	.	MCDRNGGRRLRQWLIEQIDSSMYPGLIWENEEKSMFRIPWKHAGKQDYNQEVDASIFKAWAVFKGKFKEGDKAEPATWKTRLRCALNKSPDFEEVTDRSQLDISEPYKVYRIVPEEEQKCKLGVATAGCVNEVTEMECGRSEIDELIKEPSVDDYMGMIKRSPSPPEACRSQLLPDWWAQQPSTGVPLVTGYTTYDAHHSAFSQMVISFYYGGKLVGQATTTCPEGCRLSLSQPGLPGTKLYGPEGLELVRFPPADAIPSERQRQVTRKLFGHLERGVLLHSSRQGVFVKRLCQGRVFCSGNAVVCKGRPNKLERDEVVQVFDTSQFFRELQQFYNSQGRLPDGRVVLCFGEEFPDMAPLRSKLILVQIEQLYVRQLAEEAGKSCGAGSVMQAPEEPPPDQVFRMFPDICASHQRSFFRENQQITV	Literature-reported	Interferon consensus sequence binding protein (ICSBP; IRF-8) antagonizes BCR/ABL and down-regulates bcl-2. Blood. 2004 May 1;103(9):3480-9.	.	.	.	IRF family.	.	.	Interferon regulatory factor transcription factor; Interferon-regulatory factor 3	PF00605; PF10401	PF00605; IRF; PF10401; IRF-3	.	.	hsa05133: Pertussis	R-HSA-877300: Interferon gamma signaling; R-HSA-909733: Interferon alpha/beta signaling	.	Q02556
TTAJSQ0	IRS1 messenger RNA (IRS1 mRNA)	P35568	IRS1_HUMAN	mRNA target	Insulin receptor substrate 1 (mRNA); IRS-1 (mRNA)	IRS1	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.	.	6BNT; 5U1M; 2Z8C; 1QQG; 1K3A	MASPPESDGFSDVRKVGYLRKPKSMHKRFFVLRAASEAGGPARLEYYENEKKWRHKSSAPKRSIPLESCFNINKRADSKNKHLVALYTRDEHFAIAADSEAEQDSWYQALLQLHNRAKGHHDGAAALGAGGGGGSCSGSSGLGEAGEDLSYGDVPPGPAFKEVWQVILKPKGLGQTKNLIGIYRLCLTSKTISFVKLNSEAAAVVLQLMNIRRCGHSENFFFIEVGRSAVTGPGEFWMQVDDSVVAQNMHETILEAMRAMSDEFRPRSKSQSSSNCSNPISVPLRRHHLNNPPPSQVGLTRRSRTESITATSPASMVGGKPGSFRVRASSDGEGTMSRPASVDGSPVSPSTNRTHAHRHRGSARLHPPLNHSRSIPMPASRCSPSATSPVSLSSSSTSGHGSTSDCLFPRRSSASVSGSPSDGGFISSDEYGSSPCDFRSSFRSVTPDSLGHTPPARGEEELSNYICMGGKGPSTLTAPNGHYILSRGGNGHRCTPGTGLGTSPALAGDEAASAADLDNRFRKRTHSAGTSPTITHQKTPSQSSVASIEEYTEMMPAYPPGGGSGGRLPGHRHSAFVPTRSYPEEGLEMHPLERRGGHHRPDSSTLHTDDGYMPMSPGVAPVPSGRKGSGDYMPMSPKSVSAPQQIINPIRRHPQRVDPNGYMMMSPSGGCSPDIGGGPSSSSSSSNAVPSGTSYGKLWTNGVGGHHSHVLPHPKPPVESSGGKLLPCTGDYMNMSPVGDSNTSSPSDCYYGPEDPQHKPVLSYYSLPRSFKHTQRPGEPEEGARHQHLRLSTSSGRLLYAATADDSSSSTSSDSLGGGYCGARLEPSLPHPHHQVLQPHLPRKVDTAAQTNSRLARPTRLSLGDPKASTLPRAREQQQQQQPLLHPPEPKSPGEYVNIEFGSDQSGYLSGPVAFHSSPSVRCPSQLQPAPREEETGTEEYMKMDLGPGRRAAWQESTGVEMGRLGPAPPGAASICRPTRAVPSSRGDYMTMQMSCPRQSYVDTSPAAPVSYADMRTGIAAEEVSLPRATMAAASSSSAASASPTGPQGAAELAAHSSLLGGPQGPGGMSAFTRVNLSPNRNQSAKVIRADPQGCRRRHSSETFSSTPSATRVGNTVPFGAGAAVGGGGGSSSSSEDVKRHSSASFENVWLRPGELGGAPKEPAKLCGAAGGLENGLNYIDLDLVKDFKQCPQECTPEPQPPPPPPPHQPLGSGESSSTRRSSEDLSAYASISFQKQPEDRQ	Literature-reported	Neutrophil elastase-mediated degradation of IRS-1 accelerates lung tumor growth. Nat Med. 2010 Feb;16(2):219-23.	.	mRNA	mRNA target	.	.	.	PTB domain (IRS-1 type); PH domain	PF02174; PF00169	PF02174; IRS; PF00169; PH	.	.	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	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	.	P35568
TTADRX7	Insulin receptor substrate-1 (IRS1)	P35568	IRS1_HUMAN	.	Insulin receptor substrate 1; IRS-1	IRS1	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.	.	6BNT; 5U1M; 2Z8C; 1QQG; 1K3A	MASPPESDGFSDVRKVGYLRKPKSMHKRFFVLRAASEAGGPARLEYYENEKKWRHKSSAPKRSIPLESCFNINKRADSKNKHLVALYTRDEHFAIAADSEAEQDSWYQALLQLHNRAKGHHDGAAALGAGGGGGSCSGSSGLGEAGEDLSYGDVPPGPAFKEVWQVILKPKGLGQTKNLIGIYRLCLTSKTISFVKLNSEAAAVVLQLMNIRRCGHSENFFFIEVGRSAVTGPGEFWMQVDDSVVAQNMHETILEAMRAMSDEFRPRSKSQSSSNCSNPISVPLRRHHLNNPPPSQVGLTRRSRTESITATSPASMVGGKPGSFRVRASSDGEGTMSRPASVDGSPVSPSTNRTHAHRHRGSARLHPPLNHSRSIPMPASRCSPSATSPVSLSSSSTSGHGSTSDCLFPRRSSASVSGSPSDGGFISSDEYGSSPCDFRSSFRSVTPDSLGHTPPARGEEELSNYICMGGKGPSTLTAPNGHYILSRGGNGHRCTPGTGLGTSPALAGDEAASAADLDNRFRKRTHSAGTSPTITHQKTPSQSSVASIEEYTEMMPAYPPGGGSGGRLPGHRHSAFVPTRSYPEEGLEMHPLERRGGHHRPDSSTLHTDDGYMPMSPGVAPVPSGRKGSGDYMPMSPKSVSAPQQIINPIRRHPQRVDPNGYMMMSPSGGCSPDIGGGPSSSSSSSNAVPSGTSYGKLWTNGVGGHHSHVLPHPKPPVESSGGKLLPCTGDYMNMSPVGDSNTSSPSDCYYGPEDPQHKPVLSYYSLPRSFKHTQRPGEPEEGARHQHLRLSTSSGRLLYAATADDSSSSTSSDSLGGGYCGARLEPSLPHPHHQVLQPHLPRKVDTAAQTNSRLARPTRLSLGDPKASTLPRAREQQQQQQPLLHPPEPKSPGEYVNIEFGSDQSGYLSGPVAFHSSPSVRCPSQLQPAPREEETGTEEYMKMDLGPGRRAAWQESTGVEMGRLGPAPPGAASICRPTRAVPSSRGDYMTMQMSCPRQSYVDTSPAAPVSYADMRTGIAAEEVSLPRATMAAASSSSAASASPTGPQGAAELAAHSSLLGGPQGPGGMSAFTRVNLSPNRNQSAKVIRADPQGCRRRHSSETFSSTPSATRVGNTVPFGAGAAVGGGGGSSSSSEDVKRHSSASFENVWLRPGELGGAPKEPAKLCGAAGGLENGLNYIDLDLVKDFKQCPQECTPEPQPPPPPPPHQPLGSGESSSTRRSSEDLSAYASISFQKQPEDRQ	Clinical trial	MicroRNA-145 Negatively Regulates Cell Proliferation Through Targeting IRS1 in Isolated Ovarian Granulosa Cells From Patients With Polycystic Ovary... Reprod Sci. 2017 Jun;24(6):902-910.	.	.	.	.	.	.	PTB domain (IRS-1 type); PH domain	PF02174; PF00169	PF02174; IRS; PF00169; PH	.	.	"hsa04022: cGMP-PKG signaling pathway; hsa04068: FoxO signaling pathway; hsa04140: Autophagy - animal; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04152: AMPK signaling pathway; hsa04211: Longevity regulating pathway; hsa04213: Longevity regulating pathway - multiple species; hsa04722: Neurotrophin signaling pathway; hsa04910: Insulin signaling pathway; hsa04920: Adipocytokine signaling pathway; hsa04923: Regulation of lipolysis in adipocytes; hsa04930: Type II diabetes mellitus; hsa04931: Insulin resistance; hsa04932: Non-alcoholic fatty liver disease; hsa04935: Growth hormone synthesis, secretion and action; hsa04960: Aldosterone-regulated sodium reabsorption; hsa05010: Alzheimer disease; hsa05206: MicroRNAs in cancer; hsa05415: Diabetic cardiomyopathy"	"R-HSA-109704: PI3K Cascade; R-HSA-112399: IRS-mediated signalling; R-HSA-112412: SOS-mediated signalling; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1266695: Interleukin-7 signaling; R-HSA-198203: PI3K/AKT activation; R-HSA-201556: Signaling by ALK; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-2428928: IRS-related events triggered by IGF1R; R-HSA-2586552: Signaling by Leptin; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-74713: IRS activation; R-HSA-74749: Signal attenuation; R-HSA-9603381: Activated NTRK3 signals through PI3K; R-HSA-9725370: Signaling by ALK fusions and activated point mutants; R-HSA-982772: Growth hormone receptor signaling"	.	P35568
TTF95B8	Insulin receptor substrate 2 (IRS2)	Q9Y4H2	IRS2_HUMAN	.	IRS-2	IRS2	May mediate the control of various cellular processes by insulin.	.	.	MASPPRHGPPGPASGDGPNLNNNNNNNNHSVRKCGYLRKQKHGHKRFFVLRGPGAGGDEATAGGGSAPQPPRLEYYESEKKWRSKAGAPKRVIALDCCLNINKRADAKHKYLIALYTKDEYFAVAAENEQEQEGWYRALTDLVSEGRAAAGDAPPAAAPAASCSASLPGALGGSAGAAGAEDSYGLVAPATAAYREVWQVNLKPKGLGQSKNLTGVYRLCLSARTIGFVKLNCEQPSVTLQLMNIRRCGHSDSFFFIEVGRSAVTGPGELWMQADDSVVAQNIHETILEAMKALKELFEFRPRSKSQSSGSSATHPISVPGARRHHHLVNLPPSQTGLVRRSRTDSLAATPPAAKCSSCRVRTASEGDGGAAAGAAAAGARPVSVAGSPLSPGPVRAPLSRSHTLSGGCGGRGSKVALLPAGGALQHSRSMSMPVAHSPPAATSPGSLSSSSGHGSGSYPPPPGPHPPLPHPLHHGPGQRPSSGSASASGSPSDPGFMSLDEYGSSPGDLRAFCSHRSNTPESIAETPPARDGGGGGEFYGYMTMDRPLSHCGRSYRRVSGDAAQDLDRGLRKRTYSLTTPARQRPVPQPSSASLDEYTLMRATFSGSAGRLCPSCPASSPKVAYHPYPEDYGDIEIGSHRSSSSNLGADDGYMPMTPGAALAGSGSGSCRSDDYMPMSPASVSAPKQILQPRAAAAAAAAVPSAGPAGPAPTSAAGRTFPASGGGYKASSPAESSPEDSGYMRMWCGSKLSMEHADGKLLPNGDYLNVSPSDAVTTGTPPDFFSAALHPGGEPLRGVPGCCYSSLPRSYKAPYTCGGDSDQYVLMSSPVGRILEEERLEPQATPGPSQAASAFGAGPTQPPHPVVPSPVRPSGGRPEGFLGQRGRAVRPTRLSLEGLPSLPSMHEYPLPPEPKSPGEYINIDFGEPGARLSPPAPPLLASAASSSSLLSASSPASSLGSGTPGTSSDSRQRSPLSDYMNLDFSSPKSPKPGAPSGHPVGSLDGLLSPEASSPYPPLPPRPSASPSSSLQPPPPPPAPGELYRLPPASAVATAQGPGAASSLSSDTGDNGDYTEMAFGVAATPPQPIAAPPKPEAARVASPTSGVKRLSLMEQVSGVEAFLQASQPPDPHRGAKVIRADPQGGRRRHSSETFSSTTTVTPVSPSFAHNPKRHNSASVENVSLRKSSEGGVGVGPGGGDEPPTSPRQLQPAPPLAPQGRPWTPGQPGGLVGCPGSGGSPMRRETSAGFQNGLNYIAIDVREEPGLPPQPQPPPPPLPQPGDKSSWGRTRSLGGLISAVGVGSTGGGCGGPGPGALPPANTYASIDFLSHHLKEATIVKE	Clinical trial	"Clinical pipeline report, company report or official report of Purple Biotech."	.	.	.	.	.	.	.	.	.	.	.	"hsa04022: cGMP-PKG signaling pathway; hsa04068: FoxO signaling pathway; hsa04140: Autophagy - animal; hsa04152: AMPK signaling pathway; hsa04211: Longevity regulating pathway; hsa04213: Longevity regulating pathway - multiple species; hsa04910: Insulin signaling pathway; hsa04920: Adipocytokine signaling pathway; hsa04923: Regulation of lipolysis in adipocytes; hsa04930: Type II diabetes mellitus; hsa04931: Insulin resistance; hsa04932: Non-alcoholic fatty liver disease; hsa04935: Growth hormone synthesis, secretion and action; hsa05010: Alzheimer disease; hsa05206: MicroRNAs in cancer"	"R-HSA-109704: PI3K Cascade; R-HSA-112399: IRS-mediated signalling; R-HSA-112412: SOS-mediated signalling; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1266695: Interleukin-7 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-2586552: Signaling by Leptin; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-74713: IRS activation; R-HSA-74749: Signal attenuation; R-HSA-8853659: RET signaling; R-HSA-9006335: Signaling by Erythropoietin; R-HSA-9027276: Erythropoietin activates Phosphoinositide-3-kinase (PI3K); R-HSA-9027277: Erythropoietin activates Phospholipase C gamma (PLCG); R-HSA-9027283: Erythropoietin activates STAT5; R-HSA-9027284: Erythropoietin activates RAS; R-HSA-982772: Growth hormone receptor signaling"	.	Q9Y4H2
TTVOH3T	ISG15 messenger RNA (ISG15 mRNA)	P05161	ISG15_HUMAN	mRNA target	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)	ISG15	"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."	.	6FFA; 6BI8; 5W8U; 5W8T; 5TL6	MGWDLTVKMLAGNEFQVSLSSSMSVSELKAQITQKIGVHAFQQRLAVHPSGVALQDRVPLASQGLGPGSTVLLVVDKCDEPLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDDLFWLTFEGKPLEDQLPLGEYGLKPLSTVFMNLRLRGGGTEPGGRS	Literature-reported	Prognostic value of ISG15 mRNA level in drinkers with esophageal squamous cell cancers. Int J Clin Exp Pathol. 2015 Sep 1;8(9):10975-84.	.	mRNA	mRNA target	.	.	.	Ubiquitin family	PF00240	PF00240; ubiquitin	.	.	hsa04622: RIG-I-like receptor signaling pathway; hsa05165: Human papillomavirus infection; hsa05169: Epstein-Barr virus infection; hsa05171: Coronavirus disease - COVID-19	R-HSA-1169408: ISG15 antiviral mechanism; R-HSA-168276: NS1 Mediated Effects on Host Pathways; R-HSA-168928: DDX58/IFIH1-mediated induction of interferon-alpha/beta; R-HSA-5656169: Termination of translesion DNA synthesis; R-HSA-909733: Interferon alpha/beta signaling; R-HSA-936440: Negative regulators of DDX58/IFIH1 signaling; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses	.	P05161
TT5SEWD	E3 ubiquitin protein ligase Itchy (ITCH)	Q96J02	ITCH_HUMAN	Acyltransferase	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	ITCH	"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."	EC 2.3.2.26	5SXP; 5DZD; 5DWS; 5CQ2; 5C7M	MSDSGSQLGSMGSLTMKSQLQITVISAKLKENKKNWFGPSPYVEVTVDGQSKKTEKCNNTNSPKWKQPLTVIVTPVSKLHFRVWSHQTLKSDVLLGTAALDIYETLKSNNMKLEEVVVTLQLGGDKEPTETIGDLSICLDGLQLESEVVTNGETTCSENGVSLCLPRLECNSAISAHCNLCLPGLSDSPISASRVAGFTGASQNDDGSRSKDETRVSTNGSDDPEDAGAGENRRVSGNNSPSLSNGGFKPSRPPRPSRPPPPTPRRPASVNGSPSATSESDGSSTGSLPPTNTNTNTSEGATSGLIIPLTISGGSGPRPLNPVTQAPLPPGWEQRVDQHGRVYYVDHVEKRTTWDRPEPLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLESVRNYEQWQLQRSQLQGAMQQFNQRFIYGNQDLFATSQSKEFDPLGPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRSQGQLNEKPLPEGWEMRFTVDGIPYFVDHNRRTTTYIDPRTGKSALDNGPQIAYVRDFKAKVQYFRFWCQQLAMPQHIKITVTRKTLFEDSFQQIMSFSPQDLRRRLWVIFPGEEGLDYGGVAREWFFLLSHEVLNPMYCLFEYAGKDNYCLQINPASYINPDHLKYFRFIGRFIAMALFHGKFIDTGFSLPFYKRILNKPVGLKDLESIDPEFYNSLIWVKENNIEECDLEMYFSVDKEILGEIKSHDLKPNGGNILVTEENKEEYIRMVAEWRLSRGVEEQTQAFFEGFNEILPQQYLQYFDAKELEVLLCGMQEIDLNDWQRHAIYRHYARTSKQIMWFWQFVKEIDNEKRMRLLQFVTGTCRLPVGGFADLMGSNGPQKFCIEKVGKENWLPRSHTCFNRLDLPPYKSYEQLKEKLLFAIEETEGFGQE	Literature-reported	The anti-HER3 (ErbB3) therapeutic antibody 9F7-F11 induces HER3 ubiquitination and degradation in tumors through JNK1/2- dependent ITCH/AIP4 activa... Oncotarget. 2016 Jun 14;7(24):37013-37029.	.	EC:2.3	Carbon-nitrogen ligase	.	2.3.2.26 	Acyltransferases	C2 domain; HECT-domain (ubiquitin-transferase); WW domain	PF00168; PF00632; PF00397	PF00168; C2; PF00632; HECT; PF00397; WW	.	.	hsa04120: Ubiquitin mediated proteolysis; hsa04144: Endocytosis; hsa04668: TNF signaling pathway; hsa04932: Non-alcoholic fatty liver disease	R-HSA-1253288: Downregulation of ERBB4 signaling; R-HSA-168638: NOD1/2 Signaling Pathway; R-HSA-2122948: Activated NOTCH1 Transmits Signal to the Nucleus; R-HSA-5610780: Degradation of GLI1 by the proteasome; R-HSA-5632684: Hedgehog 'on' state; R-HSA-8939236: RUNX1 regulates transcription of genes involved in differentiation of HSCs; R-HSA-936440: Negative regulators of DDX58/IFIH1 signaling; R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	Q96J02
TTPERWV	Integrin alpha-1 (VLA-1)	P56199	ITA1_HUMAN	Integrin	Laminin and collagen receptor; Integrin alpha1; ITGA1; CD49a; CD49 antigenlike family member A	ITGA1	"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."	.	5HGJ; 4A0Q; 2M32; 2L8S; 1QCY	MAPRPRARPGVAVACCWLLTVVLRCCVSFNVDVKNSMTFSGPVEDMFGYTVQQYENEEGKWVLIGSPLVGQPKNRTGDVYKCPVGRGESLPCVKLDLPVNTSIPNVTEVKENMTFGSTLVTNPNGGFLACGPLYAYRCGHLHYTTGICSDVSPTFQVVNSIAPVQECSTQLDIVIVLDGSNSIYPWDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQTMTALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNHRLKKVIQDCEDENIQRFSIAILGSYNRGNLSTEKFVEEIKSIASEPTEKHFFNVSDELALVTIVKTLGERIFALEATADQSAASFEMEMSQTGFSAHYSQDWVMLGAVGAYDWNGTVVMQKASQIIIPRNTTFNVESTKKNEPLASYLGYTVNSATASSGDVLYIAGQPRYNHTGQVIIYRMEDGNIKILQTLSGEQIGSYFGSILTTTDIDKDSNTDILLVGAPMYMGTEKEEQGKVYVYALNQTRFEYQMSLEPIKQTCCSSRQHNSCTTENKNEPCGARFGTAIAAVKDLNLDGFNDIVIGAPLEDDHGGAVYIYHGSGKTIRKEYAQRIPSGGDGKTLKFFGQSIHGEMDLNGDGLTDVTIGGLGGAALFWSRDVAVVKVTMNFEPNKVNIQKKNCHMEGKETVCINATVCFDVKLKSKEDTIYEADLQYRVTLDSLRQISRSFFSGTQERKVQRNITVRKSECTKHSFYMLDKHDFQDSVRITLDFNLTDPENGPVLDDSLPNSVHEYIPFAKDCGNKEKCISDLSLHVATTEKDLLIVRSQNDKFNVSLTVKNTKDSAYNTRTIVHYSPNLVFSGIEAIQKDSCESNHNITCKVGYPFLRRGEMVTFKILFQFNTSYLMENVTIYLSATSDSEEPPETLSDNVVNISIPVKYEVGLQFYSSASEYHISIAANETVPEVINSTEDIGNEINIFYLIRKSGSFPMPELKLSISFPNMTSNGYPVLYPTGLSSSENANCRPHIFEDPFSINSGKKMTTSTDHLKRGTILDCNTCKFATITCNLTSSDISQVNVSLILWKPTFIKSYFSSLNLTIRGELRSENASLVLSSSNQKRELAIQISKDGLPGRVPLWVILLSAFAGLLLLMLLILALWKIGFFKRPLKKKMEK	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	hsa04151: PI3K-Akt signaling pathway; hsa04510: Focal adhesion; hsa04512: ECM-receptor interaction; hsa04640: Hematopoietic cell lineage; hsa04810: Regulation of actin cytoskeleton; hsa05165: Human papillomavirus infection; hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy	R-HSA-216083: Integrin cell surface interactions; R-HSA-3000157: Laminin interactions; R-HSA-416700: Other semaphorin interactions; R-HSA-445355: Smooth Muscle Contraction; R-HSA-447041: CHL1 interactions; R-HSA-75892: Platelet Adhesion to exposed collagen	.	P56199
TTANXZ7	Integrin alpha-11 (ITGA11)	Q9UKX5	ITA11_HUMAN	Integrin	MSTP018	ITGA11	Integrin alpha-11/beta-1 is a receptor for collagen.	.	.	MDLPRGLVVAWALSLWPGFTDTFNMDTRKPRVIPGSRTAFFGYTVQQHDISGNKWLVVGAPLETNGYQKTGDVYKCPVIHGNCTKLNLGRVTLSNVSERKDNMRLGLSLATNPKDNSFLACSPLWSHECGSSYYTTGMCSRVNSNFRFSKTVAPALQRCQTYMDIVIVLDGSNSIYPWVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTETRTAFGIEFARSEAFQKGGRKGAKKVMIVITDGESHDSPDLEKVIQQSERDNVTRYAVAVLGYYNRRGINPETFLNEIKYIASDPDDKHFFNVTDEAALKDIVDALGDRIFSLEGTNKNETSFGLEMSQTGFSSHVVEDGVLLGAVGAYDWNGAVLKETSAGKVIPLRESYLKEFPEELKNHGAYLGYTVTSVVSSRQGRVYVAGAPRFNHTGKVILFTMHNNRSLTIHQAMRGQQIGSYFGSEITSVDIDGDGVTDVLLVGAPMYFNEGRERGKVYVYELRQNLFVYNGTLKDSHSYQNARFGSSIASVRDLNQDSYNDVVVGAPLEDNHAGAIYIFHGFRGSILKTPKQRITASELATGLQYFGCSIHGQLDLNEDGLIDLAVGALGNAVILWSRPVVQINASLHFEPSKINIFHRDCKRSGRDATCLAAFLCFTPIFLAPHFQTTTVGIRYNATMDERRYTPRAHLDEGGDRFTNRAVLLSSGQELCERINFHVLDTADYVKPVTFSVEYSLEDPDHGPMLDDGWPTTLRVSVPFWNGCNEDEHCVPDLVLDARSDLPTAMEYCQRVLRKPAQDCSAYTLSFDTTVFIIESTRQRVAVEATLENRGENAYSTVLNISQSANLQFASLIQKEDSDGSIECVNEERRLQKQVCNVSYPFFRAKAKVAFRLDFEFSKSIFLHHLEIELAAGSDSNERDSTKEDNVAPLRFHLKYEADVLFTRSSSLSHYEVKPNSSLERYDGIGPPFSCIFRIQNLGLFPIHGMMMKITIPIATRSGNRLLKLRDFLTDEANTSCNIWGNSTEYRPTPVEEDLRRAPQLNHSNSDVVSINCNIRLVPNQEINFHLLGNLWLRSLKALKYKSMKIMVNAALQRQFHSPFIFREEDPSRQIVFEISKQEDWQVPIWIIVGSTLGGLLLLALLVLALWKLGFFRSARRRREPGLDPTPKVLE	Literature-reported	Integrin alpha 11 in the regulation of the myofibroblast phenotype: implications for fibrotic diseases. Exp Mol Med. 2017 Nov 17;49(11):e396.	.	TC=8.A.54	Integrin	integrin alpha chain family.	.	.	FG-GAP repeat; Integrin alpha; von Willebrand factor type A domain	PF01839; PF08441; PF00092	PF01839; FG-GAP; PF08441; Integrin_alpha2; PF00092; VWA	.	.	hsa04151: PI3K-Akt signaling pathway; hsa04510: Focal adhesion; hsa04512: ECM-receptor interaction; hsa04810: Regulation of actin cytoskeleton; hsa05165: Human papillomavirus infection; hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy	R-HSA-216083: Integrin cell surface interactions	.	Q9UKX5
TT6NV8L	Integrin alpha-1/beta-1 (ITGA1/B1)	P56199-P05556	ITA1_HUMAN-ITB1_HUMAN	Integrin	alpha(1)beta(1) integrin; Alpha 1 beta 1 integrin	ITGA1-ITGB1	"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."	.	.	MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGKMAPRPRARPGVAVACCWLLTVVLRCCVSFNVDVKNSMTFSGPVEDMFGYTVQQYENEEGKWVLIGSPLVGQPKNRTGDVYKCPVGRGESLPCVKLDLPVNTSIPNVTEVKENMTFGSTLVTNPNGGFLACGPLYAYRCGHLHYTTGICSDVSPTFQVVNSIAPVQECSTQLDIVIVLDGSNSIYPWDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQTMTALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNHRLKKVIQDCEDENIQRFSIAILGSYNRGNLSTEKFVEEIKSIASEPTEKHFFNVSDELALVTIVKTLGERIFALEATADQSAASFEMEMSQTGFSAHYSQDWVMLGAVGAYDWNGTVVMQKASQIIIPRNTTFNVESTKKNEPLASYLGYTVNSATASSGDVLYIAGQPRYNHTGQVIIYRMEDGNIKILQTLSGEQIGSYFGSILTTTDIDKDSNTDILLVGAPMYMGTEKEEQGKVYVYALNQTRFEYQMSLEPIKQTCCSSRQHNSCTTENKNEPCGARFGTAIAAVKDLNLDGFNDIVIGAPLEDDHGGAVYIYHGSGKTIRKEYAQRIPSGGDGKTLKFFGQSIHGEMDLNGDGLTDVTIGGLGGAALFWSRDVAVVKVTMNFEPNKVNIQKKNCHMEGKETVCINATVCFDVKLKSKEDTIYEADLQYRVTLDSLRQISRSFFSGTQERKVQRNITVRKSECTKHSFYMLDKHDFQDSVRITLDFNLTDPENGPVLDDSLPNSVHEYIPFAKDCGNKEKCISDLSLHVATTEKDLLIVRSQNDKFNVSLTVKNTKDSAYNTRTIVHYSPNLVFSGIEAIQKDSCESNHNITCKVGYPFLRRGEMVTFKILFQFNTSYLMENVTIYLSATSDSEEPPETLSDNVVNISIPVKYEVGLQFYSSASEYHISIAANETVPEVINSTEDIGNEINIFYLIRKSGSFPMPELKLSISFPNMTSNGYPVLYPTGLSSSENANCRPHIFEDPFSINSGKKMTTSTDHLKRGTILDCNTCKFATITCNLTSSDISQVNVSLILWKPTFIKSYFSSLNLTIRGELRSENASLVLSSSNQKRELAIQISKDGLPGRVPLWVILLSAFAGLLLLMLLILALWKIGFFKRPLKKKMEK	Literature-reported	Involvement of beta(1) integrin in betaAP-induced apoptosis in human neuroblastoma cells. Mol Cell Neurosci. 2004 Jan;25(1):1-8.	.	TC=8.A.54	.	.	.	.	.	.	.	.	.	.	.	.	P56199
TTKPR4W	Integrin alpha-1/beta-3 (ITGA1/B3)	P56199-P05106	ITA1_HUMAN-ITB3_HUMAN	Integrin	alpha(1)beta(3) integrin; Alpha 1 beta 3 integrin	ITGA1-ITGB3	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.	.	.	MRARPRPRPLWATVLALGALAGVGVGGPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPDILVVLLSVMGAILLIGLAALLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGTMAPRPRARPGVAVACCWLLTVVLRCCVSFNVDVKNSMTFSGPVEDMFGYTVQQYENEEGKWVLIGSPLVGQPKNRTGDVYKCPVGRGESLPCVKLDLPVNTSIPNVTEVKENMTFGSTLVTNPNGGFLACGPLYAYRCGHLHYTTGICSDVSPTFQVVNSIAPVQECSTQLDIVIVLDGSNSIYPWDSVTAFLNDLLERMDIGPKQTQVGIVQYGENVTHEFNLNKYSSTEEVLVAAKKIVQRGGRQTMTALGIDTARKEAFTEARGARRGVKKVMVIVTDGESHDNHRLKKVIQDCEDENIQRFSIAILGSYNRGNLSTEKFVEEIKSIASEPTEKHFFNVSDELALVTIVKTLGERIFALEATADQSAASFEMEMSQTGFSAHYSQDWVMLGAVGAYDWNGTVVMQKASQIIIPRNTTFNVESTKKNEPLASYLGYTVNSATASSGDVLYIAGQPRYNHTGQVIIYRMEDGNIKILQTLSGEQIGSYFGSILTTTDIDKDSNTDILLVGAPMYMGTEKEEQGKVYVYALNQTRFEYQMSLEPIKQTCCSSRQHNSCTTENKNEPCGARFGTAIAAVKDLNLDGFNDIVIGAPLEDDHGGAVYIYHGSGKTIRKEYAQRIPSGGDGKTLKFFGQSIHGEMDLNGDGLTDVTIGGLGGAALFWSRDVAVVKVTMNFEPNKVNIQKKNCHMEGKETVCINATVCFDVKLKSKEDTIYEADLQYRVTLDSLRQISRSFFSGTQERKVQRNITVRKSECTKHSFYMLDKHDFQDSVRITLDFNLTDPENGPVLDDSLPNSVHEYIPFAKDCGNKEKCISDLSLHVATTEKDLLIVRSQNDKFNVSLTVKNTKDSAYNTRTIVHYSPNLVFSGIEAIQKDSCESNHNITCKVGYPFLRRGEMVTFKILFQFNTSYLMENVTIYLSATSDSEEPPETLSDNVVNISIPVKYEVGLQFYSSASEYHISIAANETVPEVINSTEDIGNEINIFYLIRKSGSFPMPELKLSISFPNMTSNGYPVLYPTGLSSSENANCRPHIFEDPFSINSGKKMTTSTDHLKRGTILDCNTCKFATITCNLTSSDISQVNVSLILWKPTFIKSYFSSLNLTIRGELRSENASLVLSSSNQKRELAIQISKDGLPGRVPLWVILLSAFAGLLLLMLLILALWKIGFFKRPLKKKMEK	Literature-reported	Expression of alpha 1 and beta 3 integrins subunits in the endometrium of patients with tubal phimosis or hydrosalpinx. Fertil Steril. 2006 Jan;85(1):188-92.	.	TC=8.A.54	.	.	.	.	.	.	.	.	.	.	.	.	P56199
TTSJ542	Integrin alpha-2 (ITGA2)	P17301	ITA2_HUMAN	Integrin	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	ITGA2	"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."	.	6NDH; 6NDG; 6NDF; 6NDE; 6NDD	MGPERTGAAPLPLLLVLALSQGILNCCLAYNVGLPEAKIFSGPSSEQFGYAVQQFINPKGNWLLVGSPWSGFPENRMGDVYKCPVDLSTATCEKLNLQTSTSIPNVTEMKTNMSLGLILTRNMGTGGFLTCGPLWAQQCGNQYYTTGVCSDISPDFQLSASFSPATQPCPSLIDVVVVCDESNSIYPWDAVKNFLEKFVQGLDIGPTKTQVGLIQYANNPRVVFNLNTYKTKEEMIVATSQTSQYGGDLTNTFGAIQYARKYAYSAASGGRRSATKVMVVVTDGESHDGSMLKAVIDQCNHDNILRFGIAVLGYLNRNALDTKNLIKEIKAIASIPTERYFFNVSDEAALLEKAGTLGEQIFSIEGTVQGGDNFQMEMSQVGFSADYSSQNDILMLGAVGAFGWSGTIVQKTSHGHLIFPKQAFDQILQDRNHSSYLGYSVAAISTGESTHFVAGAPRANYTGQIVLYSVNENGNITVIQAHRGDQIGSYFGSVLCSVDVDKDTITDVLLVGAPMYMSDLKKEEGRVYLFTIKKGILGQHQFLEGPEGIENTRFGSAIAALSDINMDGFNDVIVGSPLENQNSGAVYIYNGHQGTIRTKYSQKILGSDGAFRSHLQYFGRSLDGYGDLNGDSITDVSIGAFGQVVQLWSQSIADVAIEASFTPEKITLVNKNAQIILKLCFSAKFRPTKQNNQVAIVYNITLDADGFSSRVTSRGLFKENNERCLQKNMVVNQAQSCPEHIIYIQEPSDVVNSLDLRVDISLENPGTSPALEAYSETAKVFSIPFHKDCGEDGLCISDLVLDVRQIPAAQEQPFIVSNQNKRLTFSVTLKNKRESAYNTGIVVDFSENLFFASFSLPVDGTEVTCQVAASQKSVACDVGYPALKREQQVTFTINFDFNLQNLQNQASLSFQALSESQEENKADNLVNLKIPLLYDAEIHLTRSTNINFYEISSDGNVPSIVHSFEDVGPKFIFSLKVTTGSVPVSMATVIIHIPQYTKEKNPLMYLTGVQTDKAGDISCNADINPLKIGQTSSSVSFKSENFRHTKELNCRTASCSNVTCWLKDVHMKGEYFVNVTTRIWNGTFASSTFQTVQLTAAAEINTYNPEIYVIEDNTVTIPLMIMKPDEKAEVPTGVIIGSIIAGILLLLALVAILWKLGFFKRKYEKMTKNPDEIDETTELSS	Clinical trial	"Phase I study of E7820, an oral inhibitor of integrin alpha-2 expression with antiangiogenic properties, in patients with advanced malignancies. Clin Cancer Res. 2011 Jan 1;17(1):193-200."	21	TC=8.A.54	Integrin	integrin alpha chain family.	.	.	FG-GAP repeat; Integrin alpha; von Willebrand factor type A domain	PF01839; PF08441; PF00092	PF01839; FG-GAP; PF08441; Integrin_alpha2; PF00092; VWA	.	.	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	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	.	P17301
TT38RM1	Glycoprotein IIb/IIIa receptor (GPIIb/IIIa)	P08514; P05106	ITA2B_HUMAN; ITB3_HUMAN	.	Platelet membrane glycoprotein IIb; Platelet membrane glycoprotein IIIa; GP	ITGA2B	"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."	.	.	MARALCPLQALWLLEWVLLLLGPCAAPPAWALNLDPVQLTFYAGPNGSQFGFSLDFHKDSHGRVAIVVGAPRTLGPSQEETGGVFLCPWRAEGGQCPSLLFDLRDETRNVGSQTLQTFKARQGLGASVVSWSDVIVACAPWQHWNVLEKTEEAEKTPVGSCFLAQPESGRRAEYSPCRGNTLSRIYVENDFSWDKRYCEAGFSSVVTQAGELVLGAPGGYYFLGLLAQAPVADIFSSYRPGILLWHVSSQSLSFDSSNPEYFDGYWGYSVAVGEFDGDLNTTEYVVGAPTWSWTLGAVEILDSYYQRLHRLRGEQMASYFGHSVAVTDVNGDGRHDLLVGAPLYMESRADRKLAEVGRVYLFLQPRGPHALGAPSLLLTGTQLYGRFGSAIAPLGDLDRDGYNDIAVAAPYGGPSGRGQVLVFLGQSEGLRSRPSQVLDSPFPTGSAFGFSLRGAVDIDDNGYPDLIVGAYGANQVAVYRAQPVVKASVQLLVQDSLNPAVKSCVLPQTKTPVSCFNIQMCVGATGHNIPQKLSLNAELQLDRQKPRQGRRVLLLGSQQAGTTLNLDLGGKHSPICHTTMAFLRDEADFRDKLSPIVLSLNVSLPPTEAGMAPAVVLHGDTHVQEQTRIVLDCGEDDVCVPQLQLTASVTGSPLLVGADNVLELQMDAANEGEGAYEAELAVHLPQGAHYMRALSNVEGFERLICNQKKENETRVVLCELGNPMKKNAQIGIAMLVSVGNLEEAGESVSFQLQIRSKNSQNPNSKIVLLDVPVRAEAQVELRGNSFPASLVVAAEEGEREQNSLDSWGPKVEHTYELHNNGPGTVNGLHLSIHLPGQSQPSDLLYILDIQPQGGLQCFPQPPVNPLKVDWGLPIPSPSPIHPAHHKRDRRQIFLPEPEQPSRLQDPVLVSCDSAPCTVVQCDLQEMARGQRAMVTVLAFLWLPSLYQRPLDQFVLQSHAWFNVSSLPYAVPPLSLPRGEAQVWTQLLRALEERAIPIWWVLVGVLGGLLLLTILVLAMWKVGFFKRNRPPLEEDDEEGE	Successful	"Accutin, a new disintegrin, inhibits angiogenesis in vitro and in vivo by acting as integrin alphavbeta3 antagonist and inducing apoptosis. Blood. 1998 Nov 1;92(9):3268-76."	34	.	.	.	.	.	.	.	.	.	.	hsa04015: Rap1 signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04510: Focal adhesion; hsa04512: ECM-receptor interaction; hsa04611: Platelet activation; hsa04613: Neutrophil extracellular trap formation; hsa04640: Hematopoietic cell lineage; hsa04810: Regulation of actin cytoskeleton; hsa05165: Human papillomavirus infection; hsa05200: Pathways in cancer; hsa05222: Small cell lung cancer; hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy; hsa05418: Fluid shear stress and atherosclerosis	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	.	P08514
TTMSB0A	Integrin alpha-2/beta-1 (ITGA2/B1)	P17301-P05556	ITA2_HUMAN-ITB1_HUMAN	Integrin	alpha(2)beta(1) integrin; Integrin alpha(2)beta(1); Alpha 2 beta 1 integrin	ITGA2-ITGB1	"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."	.	.	MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGKMGPERTGAAPLPLLLVLALSQGILNCCLAYNVGLPEAKIFSGPSSEQFGYAVQQFINPKGNWLLVGSPWSGFPENRMGDVYKCPVDLSTATCEKLNLQTSTSIPNVTEMKTNMSLGLILTRNMGTGGFLTCGPLWAQQCGNQYYTTGVCSDISPDFQLSASFSPATQPCPSLIDVVVVCDESNSIYPWDAVKNFLEKFVQGLDIGPTKTQVGLIQYANNPRVVFNLNTYKTKEEMIVATSQTSQYGGDLTNTFGAIQYARKYAYSAASGGRRSATKVMVVVTDGESHDGSMLKAVIDQCNHDNILRFGIAVLGYLNRNALDTKNLIKEIKAIASIPTERYFFNVSDEAALLEKAGTLGEQIFSIEGTVQGGDNFQMEMSQVGFSADYSSQNDILMLGAVGAFGWSGTIVQKTSHGHLIFPKQAFDQILQDRNHSSYLGYSVAAISTGESTHFVAGAPRANYTGQIVLYSVNENGNITVIQAHRGDQIGSYFGSVLCSVDVDKDTITDVLLVGAPMYMSDLKKEEGRVYLFTIKKGILGQHQFLEGPEGIENTRFGSAIAALSDINMDGFNDVIVGSPLENQNSGAVYIYNGHQGTIRTKYSQKILGSDGAFRSHLQYFGRSLDGYGDLNGDSITDVSIGAFGQVVQLWSQSIADVAIEASFTPEKITLVNKNAQIILKLCFSAKFRPTKQNNQVAIVYNITLDADGFSSRVTSRGLFKENNERCLQKNMVVNQAQSCPEHIIYIQEPSDVVNSLDLRVDISLENPGTSPALEAYSETAKVFSIPFHKDCGEDGLCISDLVLDVRQIPAAQEQPFIVSNQNKRLTFSVTLKNKRESAYNTGIVVDFSENLFFASFSLPVDGTEVTCQVAASQKSVACDVGYPALKREQQVTFTINFDFNLQNLQNQASLSFQALSESQEENKADNLVNLKIPLLYDAEIHLTRSTNINFYEISSDGNVPSIVHSFEDVGPKFIFSLKVTTGSVPVSMATVIIHIPQYTKEKNPLMYLTGVQTDKAGDISCNADINPLKIGQTSSSVSFKSENFRHTKELNCRTASCSNVTCWLKDVHMKGEYFVNVTTRIWNGTFASSTFQTVQLTAAAEINTYNPEIYVIEDNTVTIPLMIMKPDEKAEVPTGVIIGSIIAGILLLLALVAILWKLGFFKRKYEKMTKNPDEIDETTELSS	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2578).	21	TC=8.A.54	.	.	.	.	.	.	.	.	.	.	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	.	P17301
TTJMF9P	ITGA4 messenger RNA (ITGA4 mRNA)	P13612	ITA4_HUMAN	mRNA target	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)	ITGA4	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.	.	5FPI; 5C7Z; 4HKC; 3V4V; 3V4P	MAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNAMETNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQEDDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQSISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASLSHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYIVLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSREANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHVISKRSTEEFPPLQPILQQKKEKDIMKKTINFARFCAHENCSADLQVSAKIGFLKPHENKTYLAVGSMKTLMLNVSLFNAGDDAYETTLHVKLPVGLYFIKILELEEKQINCEVTDNSGVVQLDCSIGYIYVDHLSRIDISFLLDVSSLSRAEEDLSITVHATCENEEEMDNLKHSRVTVAIPLKYEVKLTVHGFVNPTSFVYGSNDENEPETCMVEKMNLTFHVINTGNSMAPNVSVEIMVPNSFSPQTDKLFNILDVQTTTGECHFENYQRVCALEQQKSAMQTLKGIVRFLSKTDKRLLYCIKADPHCLNFLCNFGKMESGKEASVHIQLEGRPSILEMDETSALKFEIRATGFPEPNPRVIELNKDENVAHVLLEGLHHQRPKRYFTIVIISSSLLLGLIVLLLISYVMWKAGFFKRQYKSILQEENRRDSWSYINSKSNDD	Clinical trial	CD49d antisense drug ATL1102 reduces disease activity in patients with relapsing-remitting MS.Neurology.2014 Nov 11;83(20):1780-8.	21	mRNA	mRNA target	.	.	.	FG-GAP repeat; Integrin alpha	PF01839; PF08441	PF01839; FG-GAP; PF08441; Integrin_alpha2	.	.	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	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	.	P13612
TT4BT06	Integrin alpha-4 (ITGA4)	P13612	ITA4_HUMAN	Integrin	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	ITGA4	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.	.	5FPI; 5C7Z; 4HKC; 3V4V; 3V4P	MAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNAMETNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQEDDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQSISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASLSHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYIVLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSREANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHVISKRSTEEFPPLQPILQQKKEKDIMKKTINFARFCAHENCSADLQVSAKIGFLKPHENKTYLAVGSMKTLMLNVSLFNAGDDAYETTLHVKLPVGLYFIKILELEEKQINCEVTDNSGVVQLDCSIGYIYVDHLSRIDISFLLDVSSLSRAEEDLSITVHATCENEEEMDNLKHSRVTVAIPLKYEVKLTVHGFVNPTSFVYGSNDENEPETCMVEKMNLTFHVINTGNSMAPNVSVEIMVPNSFSPQTDKLFNILDVQTTTGECHFENYQRVCALEQQKSAMQTLKGIVRFLSKTDKRLLYCIKADPHCLNFLCNFGKMESGKEASVHIQLEGRPSILEMDETSALKFEIRATGFPEPNPRVIELNKDENVAHVLLEGLHHQRPKRYFTIVIISSSLLLGLIVLLLISYVMWKAGFFKRQYKSILQEENRRDSWSYINSKSNDD	Successful	"Clinical pipeline report, company report or official report of Takeda (2009)."	34	TC=8.A.54	.	integrin alpha chain family.	.	.	FG-GAP repeat; Integrin alpha	PF01839; PF08441	PF01839; FG-GAP; PF08441; Integrin_alpha2	.	.	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	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	.	P13612
TTH52YN	VLA-4 messenger RNA (VLA-4 mRNA)	P13612-P05556	ITA4_HUMAN-ITB1_HUMAN	mRNA target	VLA-4 (mRNA); Integrin alpha-4/beta-1 (mRNA)	ITGA4-ITGB1	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.	.	.	MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGKMAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNAMETNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQEDDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQSISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASLSHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYIVLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSREANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHVISKRSTEEFPPLQPILQQKKEKDIMKKTINFARFCAHENCSADLQVSAKIGFLKPHENKTYLAVGSMKTLMLNVSLFNAGDDAYETTLHVKLPVGLYFIKILELEEKQINCEVTDNSGVVQLDCSIGYIYVDHLSRIDISFLLDVSSLSRAEEDLSITVHATCENEEEMDNLKHSRVTVAIPLKYEVKLTVHGFVNPTSFVYGSNDENEPETCMVEKMNLTFHVINTGNSMAPNVSVEIMVPNSFSPQTDKLFNILDVQTTTGECHFENYQRVCALEQQKSAMQTLKGIVRFLSKTDKRLLYCIKADPHCLNFLCNFGKMESGKEASVHIQLEGRPSILEMDETSALKFEIRATGFPEPNPRVIELNKDENVAHVLLEGLHHQRPKRYFTIVIISSSLLLGLIVLLLISYVMWKAGFFKRQYKSILQEENRRDSWSYINSKSNDD	Literature-reported	NCBI GEO: archive for functional genomics data sets--update. Nucleic Acids Res. 2013 Jan;41(Database issue):D991-5.	.	mRNA	mRNA target	.	.	.	FG-GAP repeat; Integrin alpha	PF01839; PF08441	PF01839; FG-GAP; PF08441; Integrin_alpha2	.	.	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	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	.	P13612
TT6S84X	Integrin alpha-4/beta-1 (ITGA4/B1)	P13612-P05556	ITA4_HUMAN-ITB1_HUMAN	Integrin	alpha(4)beta(1) integrin; Alpha 4 beta 1 integrin	ITGA4-ITGB1	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.	.	.	MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGKMAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNAMETNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQEDDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQSISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASLSHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYIVLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSREANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHVISKRSTEEFPPLQPILQQKKEKDIMKKTINFARFCAHENCSADLQVSAKIGFLKPHENKTYLAVGSMKTLMLNVSLFNAGDDAYETTLHVKLPVGLYFIKILELEEKQINCEVTDNSGVVQLDCSIGYIYVDHLSRIDISFLLDVSSLSRAEEDLSITVHATCENEEEMDNLKHSRVTVAIPLKYEVKLTVHGFVNPTSFVYGSNDENEPETCMVEKMNLTFHVINTGNSMAPNVSVEIMVPNSFSPQTDKLFNILDVQTTTGECHFENYQRVCALEQQKSAMQTLKGIVRFLSKTDKRLLYCIKADPHCLNFLCNFGKMESGKEASVHIQLEGRPSILEMDETSALKFEIRATGFPEPNPRVIELNKDENVAHVLLEGLHHQRPKRYFTIVIISSSLLLGLIVLLLISYVMWKAGFFKRQYKSILQEENRRDSWSYINSKSNDD	Clinical trial	"Oral treatment with a novel small molecule alpha 4 integrin antagonist, AJM300, prevents the development of experimental colitis in mice. J Crohns Colitis. 2013 Dec;7(11):e533-42."	25	TC=8.A.54	.	.	.	.	.	.	.	.	.	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	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	.	P13612
TT0LHGI	Integrin alpha-4/beta-4 (ITGA4/B4)	P13612-P16144	ITA4_HUMAN-ITB4_HUMAN	Integrin	alpha(4)beta(4) integrin; Alpha 4 beta 4 integrin	ITGA4-ITGB4	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.	.	.	MAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNAMETNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQEDDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQSISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASLSHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYIVLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSREANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHVISKRSTEEFPPLQPILQQKKEKDIMKKTINFARFCAHENCSADLQVSAKIGFLKPHENKTYLAVGSMKTLMLNVSLFNAGDDAYETTLHVKLPVGLYFIKILELEEKQINCEVTDNSGVVQLDCSIGYIYVDHLSRIDISFLLDVSSLSRAEEDLSITVHATCENEEEMDNLKHSRVTVAIPLKYEVKLTVHGFVNPTSFVYGSNDENEPETCMVEKMNLTFHVINTGNSMAPNVSVEIMVPNSFSPQTDKLFNILDVQTTTGECHFENYQRVCALEQQKSAMQTLKGIVRFLSKTDKRLLYCIKADPHCLNFLCNFGKMESGKEASVHIQLEGRPSILEMDETSALKFEIRATGFPEPNPRVIELNKDENVAHVLLEGLHHQRPKRYFTIVIISSSLLLGLIVLLLISYVMWKAGFFKRQYKSILQEENRRDSWSYINSKSNDDMAGPRPSPWARLLLAALISVSLSGTLANRCKKAPVKSCTECVRVDKDCAYCTDEMFRDRRCNTQAELLAAGCQRESIVVMESSFQITEETQIDTTLRRSQMSPQGLRVRLRPGEERHFELEVFEPLESPVDLYILMDFSNSMSDDLDNLKKMGQNLARVLSQLTSDYTIGFGKFVDKVSVPQTDMRPEKLKEPWPNSDPPFSFKNVISLTEDVDEFRNKLQGERISGNLDAPEGGFDAILQTAVCTRDIGWRPDSTHLLVFSTESAFHYEADGANVLAGIMSRNDERCHLDTTGTYTQYRTQDYPSVPTLVRLLAKHNIIPIFAVTNYSYSYYEKLHTYFPVSSLGVLQEDSSNIVELLEEAFNRIRSNLDIRALDSPRGLRTEVTSKMFQKTRTGSFHIRRGEVGIYQVQLRALEHVDGTHVCQLPEDQKGNIHLKPSFSDGLKMDAGIICDVCTCELQKEVRSARCSFNGDFVCGQCVCSEGWSGQTCNCSTGSLSDIQPCLREGEDKPCSGRGECQCGHCVCYGEGRYEGQFCEYDNFQCPRTSGFLCNDRGRCSMGQCVCEPGWTGPSCDCPLSNATCIDSNGGICNGRGHCECGRCHCHQQSLYTDTICEINYSAIHPGLCEDLRSCVQCQAWGTGEKKGRTCEECNFKVKMVDELKRAEEVVVRCSFRDEDDDCTYSYTMEGDGAPGPNSTVLVHKKKDCPPGSFWWLIPLLLLLLPLLALLLLLCWKYCACCKACLALLPCCNRGHMVGFKEDHYMLRENLMASDHLDTPMLRSGNLKGRDVVRWKVTNNMQRPGFATHAASINPTELVPYGLSLRLARLCTENLLKPDTRECAQLRQEVEENLNEVYRQISGVHKLQQTKFRQQPNAGKKQDHTIVDTVLMAPRSAKPALLKLTEKQVEQRAFHDLKVAPGYYTLTADQDARGMVEFQEGVELVDVRVPLFIRPEDDDEKQLLVEAIDVPAGTATLGRRLVNITIIKEQARDVVSFEQPEFSVSRGDQVARIPVIRRVLDGGKSQVSYRTQDGTAQGNRDYIPVEGELLFQPGEAWKELQVKLLELQEVDSLLRGRQVRRFHVQLSNPKFGAHLGQPHSTTIIIRDPDELDRSFTSQMLSSQPPPHGDLGAPQNPNAKAAGSRKIHFNWLPPSGKPMGYRVKYWIQGDSESEAHLLDSKVPSVELTNLYPYCDYEMKVCAYGAQGEGPYSSLVSCRTHQEVPSEPGRLAFNVVSSTVTQLSWAEPAETNGEITAYEVCYGLVNDDNRPIGPMKKVLVDNPKNRMLLIENLRESQPYRYTVKARNGAGWGPEREAIINLATQPKRPMSIPIIPDIPIVDAQSGEDYDSFLMYSDDVLRSPSGSQRPSVSDDTGCGWKFEPLLGEELDLRRVTWRLPPELIPRLSASSGRSSDAEAPHGPPDDGGAGGKGGSLPRSATPGPPGEHLVNGRMDFAFPGSTNSLHRMTTTSAAAYGTHLSPHVPHRVLSTSSTLTRDYNSLTRSEHSHSTTLPRDYSTLTSVSSHDSRLTAGVPDTPTRLVFSALGPTSLRVSWQEPRCERPLQGYSVEYQLLNGGELHRLNIPNPAQTSVVVEDLLPNHSYVFRVRAQSQEGWGREREGVITIESQVHPQSPLCPLPGSAFTLSTPSAPGPLVFTALSPDSLQLSWERPRRPNGDIVGYLVTCEMAQGGGPATAFRVDGDSPESRLTVPGLSENVPYKFKVQARTTEGFGPEREGIITIESQDGGPFPQLGSRAGLFQHPLQSEYSSITTTHTSATEPFLVDGLTLGAQHLEAGGSLTRHVTQEFVSRTLTTSGTLSTHMDQQFFQT	Literature-reported	Epigenetic regulation of miR-21 in colorectal cancer: ITGB4 as a novel miR-21 target and a three-gene network (miR-21-ITG4-PDCD4) as predictor of ... Epigenetics. 2014 Jan;9(1):129-41.	.	TC=8.A.54	Integrin	.	.	.	.	.	.	.	.	.	.	.	P13612
TT7ZMI1	Integrin alpha-4/beta-7 (ITGA4/B7)	P13612-P26010	ITA4_HUMAN-ITB7_HUMAN	Integrin	alpha(4)beta(7) integrin; Alpha 4 beta 7 integrin	ITGA4-ITGB7	"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."	.	.	MVALPMVLVLLLVLSRGESELDAKIPSTGDATEWRNPHLSMLGSCQPAPSCQKCILSHPSCAWCKQLNFTASGEAEARRCARREELLARGCPLEELEEPRGQQEVLQDQPLSQGARGEGATQLAPQRVRVTLRPGEPQQLQVRFLRAEGYPVDLYYLMDLSYSMKDDLERVRQLGHALLVRLQEVTHSVRIGFGSFVDKTVLPFVSTVPSKLRHPCPTRLERCQSPFSFHHVLSLTGDAQAFEREVGRQSVSGNLDSPEGGFDAILQAALCQEQIGWRNVSRLLVFTSDDTFHTAGDGKLGGIFMPSDGHCHLDSNGLYSRSTEFDYPSVGQVAQALSAANIQPIFAVTSAALPVYQELSKLIPKSAVGELSEDSSNVVQLIMDAYNSLSSTVTLEHSSLPPGVHISYESQCEGPEKREGKAEDRGQCNHVRINQTVTFWVSLQATHCLPEPHLLRLRALGFSEELIVELHTLCDCNCSDTQPQAPHCSDGQGHLQCGVCSCAPGRLGRLCECSVAELSSPDLESGCRAPNGTGPLCSGKGHCQCGRCSCSGQSSGHLCECDDASCERHEGILCGGFGRCQCGVCHCHANRTGRACECSGDMDSCISPEGGLCSGHGRCKCNRCQCLDGYYGALCDQCPGCKTPCERHRDCAECGAFRTGPLATNCSTACAHTNVTLALAPILDDGWCKERTLDNQLFFFLVEDDARGTVVLRVRPQEKGADHTQAIVLGCVGGIVAVGLGLVLAYRLSVEIYDRREYSRFEKEQQQLNWKQDSNPLYKSAITTTINPRFQEADSPTLMAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGSGAVMNAMETNLVGSDKYAARFGESIVNLGDIDNDGFEDVAIGAPQEDDLQGAIYIYNGRADGISSTFSQRIEGLQISKSLSMFGQSISGQIDADNNGYVDVAVGAFRSDSAVLLRTRPVVIVDASLSHPESVNRTKFDCVENGWPSVCIDLTLCFSYKGKEVPGYIVLFYNMSLDVNRKAESPPRFYFSSNGTSDVITGSIQVSSREANCRTHQAFMRKDVRDILTPIQIEAAYHLGPHVISKRSTEEFPPLQPILQQKKEKDIMKKTINFARFCAHENCSADLQVSAKIGFLKPHENKTYLAVGSMKTLMLNVSLFNAGDDAYETTLHVKLPVGLYFIKILELEEKQINCEVTDNSGVVQLDCSIGYIYVDHLSRIDISFLLDVSSLSRAEEDLSITVHATCENEEEMDNLKHSRVTVAIPLKYEVKLTVHGFVNPTSFVYGSNDENEPETCMVEKMNLTFHVINTGNSMAPNVSVEIMVPNSFSPQTDKLFNILDVQTTTGECHFENYQRVCALEQQKSAMQTLKGIVRFLSKTDKRLLYCIKADPHCLNFLCNFGKMESGKEASVHIQLEGRPSILEMDETSALKFEIRATGFPEPNPRVIELNKDENVAHVLLEGLHHQRPKRYFTIVIISSSLLLGLIVLLLISYVMWKAGFFKRQYKSILQEENRRDSWSYINSKSNDD	Successful	2014 FDA drug approvals. Nat Rev Drug Discov. 2015 Feb;14(2):77-81.	34	TC=8.A.54	.	.	.	.	.	.	.	.	.	.	.	.	P13612
TTHIZP9	Integrin alpha-5 (ITGA5)	P08648	ITA5_HUMAN	Integrin	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	ITGA5	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.	.	4WK4; 4WK2; 4WK0; 4WJK; 3VI4	MGSRTPESPLHAVQLRWGPRRRPPLLPLLLLLLPPPPRVGGFNLDAEAPAVLSGPPGSFFGFSVEFYRPGTDGVSVLVGAPKANTSQPGVLQGGAVYLCPWGASPTQCTPIEFDSKGSRLLESSLSSSEGEEPVEYKSLQWFGATVRAHGSSILACAPLYSWRTEKEPLSDPVGTCYLSTDNFTRILEYAPCRSDFSWAAGQGYCQGGFSAEFTKTGRVVLGGPGSYFWQGQILSATQEQIAESYYPEYLINLVQGQLQTRQASSIYDDSYLGYSVAVGEFSGDDTEDFVAGVPKGNLTYGYVTILNGSDIRSLYNFSGEQMASYFGYAVAATDVNGDGLDDLLVGAPLLMDRTPDGRPQEVGRVYVYLQHPAGIEPTPTLTLTGHDEFGRFGSSLTPLGDLDQDGYNDVAIGAPFGGETQQGVVFVFPGGPGGLGSKPSQVLQPLWAASHTPDFFGSALRGGRDLDGNGYPDLIVGSFGVDKAVVYRGRPIVSASASLTIFPAMFNPEERSCSLEGNPVACINLSFCLNASGKHVADSIGFTVELQLDWQKQKGGVRRALFLASRQATLTQTLLIQNGAREDCREMKIYLRNESEFRDKLSPIHIALNFSLDPQAPVDSHGLRPALHYQSKSRIEDKAQILLDCGEDNICVPDLQLEVFGEQNHVYLGDKNALNLTFHAQNVGEGGAYEAELRVTAPPEAEYSGLVRHPGNFSSLSCDYFAVNQSRLLVCDLGNPMKAGASLWGGLRFTVPHLRDTKKTIQFDFQILSKNLNNSQSDVVSFRLSVEAQAQVTLNGVSKPEAVLFPVSDWHPRDQPQKEEDLGPAVHHVYELINQGPSSISQGVLELSCPQALEGQQLLYVTRVTGLNCTTNHPINPKGLELDPEGSLHHQQKREAPSRSSASSGPQILKCPEAECFRLRCELGPLHQQESQSLQLHFRVWAKTFLQREHQPFSLQCEAVYKALKMPYRILPRQLPQKERQVATAVQWTKAEGSYGVPLWIIILAILFGLLLLGLLIYILYKLGFFKRSLPYGTAMEKAQLKPPATSDA	Clinical trial	An alpha5beta1 integrin inhibitor attenuates glioma growth. Mol Cell Neurosci. 2008 Dec;39(4):579-85.	17	TC=8.A.54	Integrin	integrin alpha chain family.	.	.	FG-GAP repeat; Integrin alpha	PF01839; PF08441	PF01839; FG-GAP; PF08441; Integrin_alpha2	.	.	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	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	.	P08648
TTH4QIS	Integrin alpha-5/beta-1 (ITGA5/B1)	P08648-P05556	ITA5_HUMAN-ITB1_HUMAN	Integrin	alpha(5)beta(1) integrin; Alpha 5 beta 1 integrin	ITGA5-ITGB1	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.	.	.	MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGKMGSRTPESPLHAVQLRWGPRRRPPLLPLLLLLLPPPPRVGGFNLDAEAPAVLSGPPGSFFGFSVEFYRPGTDGVSVLVGAPKANTSQPGVLQGGAVYLCPWGASPTQCTPIEFDSKGSRLLESSLSSSEGEEPVEYKSLQWFGATVRAHGSSILACAPLYSWRTEKEPLSDPVGTCYLSTDNFTRILEYAPCRSDFSWAAGQGYCQGGFSAEFTKTGRVVLGGPGSYFWQGQILSATQEQIAESYYPEYLINLVQGQLQTRQASSIYDDSYLGYSVAVGEFSGDDTEDFVAGVPKGNLTYGYVTILNGSDIRSLYNFSGEQMASYFGYAVAATDVNGDGLDDLLVGAPLLMDRTPDGRPQEVGRVYVYLQHPAGIEPTPTLTLTGHDEFGRFGSSLTPLGDLDQDGYNDVAIGAPFGGETQQGVVFVFPGGPGGLGSKPSQVLQPLWAASHTPDFFGSALRGGRDLDGNGYPDLIVGSFGVDKAVVYRGRPIVSASASLTIFPAMFNPEERSCSLEGNPVACINLSFCLNASGKHVADSIGFTVELQLDWQKQKGGVRRALFLASRQATLTQTLLIQNGAREDCREMKIYLRNESEFRDKLSPIHIALNFSLDPQAPVDSHGLRPALHYQSKSRIEDKAQILLDCGEDNICVPDLQLEVFGEQNHVYLGDKNALNLTFHAQNVGEGGAYEAELRVTAPPEAEYSGLVRHPGNFSSLSCDYFAVNQSRLLVCDLGNPMKAGASLWGGLRFTVPHLRDTKKTIQFDFQILSKNLNNSQSDVVSFRLSVEAQAQVTLNGVSKPEAVLFPVSDWHPRDQPQKEEDLGPAVHHVYELINQGPSSISQGVLELSCPQALEGQQLLYVTRVTGLNCTTNHPINPKGLELDPEGSLHHQQKREAPSRSSASSGPQILKCPEAECFRLRCELGPLHQQESQSLQLHFRVWAKTFLQREHQPFSLQCEAVYKALKMPYRILPRQLPQKERQVATAVQWTKAEGSYGVPLWIIILAILFGLLLLGLLIYILYKLGFFKRSLPYGTAMEKAQLKPPATSDA	Clinical trial	A non-RGD-based integrin binding peptide (ATN-161) blocks breast cancer growth and metastasis in vivo. Mol Cancer Ther. 2006 Sep;5(9):2271-80.	21	TC=8.A.54	.	.	.	.	.	.	.	.	.	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	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	.	P08648
TT165T3	Integrin alpha-6 (ITGA6)	P23229	ITA6_HUMAN	Integrin	VLA-6 integrin; VLA-6; CD49f; CD49 antigen-like family member F; Alpha6 beta1 integrin	ITGA6	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.	.	.	MAAAGQLCLLYLSAGLLSRLGAAFNLDTREDNVIRKYGDPGSLFGFSLAMHWQLQPEDKRLLLVGAPRAEALPLQRANRTGGLYSCDITARGPCTRIEFDNDADPTSESKEDQWMGVTVQSQGPGGKVVTCAHRYEKRQHVNTKQESRDIFGRCYVLSQNLRIEDDMDGGDWSFCDGRLRGHEKFGSCQQGVAATFTKDFHYIVFGAPGTYNWKGIVRVEQKNNTFFDMNIFEDGPYEVGGETEHDESLVPVPANSYLGLLFLTSVSYTDPDQFVYKTRPPREQPDTFPDVMMNSYLGFSLDSGKGIVSKDEITFVSGAPRANHSGAVVLLKRDMKSAHLLPEHIFDGEGLASSFGYDVAVVDLNKDGWQDIVIGAPQYFDRDGEVGGAVYVYMNQQGRWNNVKPIRLNGTKDSMFGIAVKNIGDINQDGYPDIAVGAPYDDLGKVFIYHGSANGINTKPTQVLKGISPYFGYSIAGNMDLDRNSYPDVAVGSLSDSVTIFRSRPVINIQKTITVTPNRIDLRQKTACGAPSGICLQVKSCFEYTANPAGYNPSISIVGTLEAEKERRKSGLSSRVQFRNQGSEPKYTQELTLKRQKQKVCMEETLWLQDNIRDKLRPIPITASVEIQEPSSRRRVNSLPEVLPILNSDEPKTAHIDVHFLKEGCGDDNVCNSNLKLEYKFCTREGNQDKFSYLPIQKGVPELVLKDQKDIALEITVTNSPSNPRNPTKDGDDAHEAKLIATFPDTLTYSAYRELRAFPEKQLSCVANQNGSQADCELGNPFKRNSNVTFYLVLSTTEVTFDTPDLDINLKLETTSNQDNLAPITAKAKVVIELLLSVSGVAKPSQVYFGGTVVGEQAMKSEDEVGSLIEYEFRVINLGKPLTNLGTATLNIQWPKEISNGKWLLYLVKVESKGLEKVTCEPQKEINSLNLTESHNSRKKREITEKQIDDNRKFSLFAERKYQTLNCSVNVNCVNIRCPLRGLDSKASLILRSRLWNSTFLEEYSKLNYLDILMRAFIDVTAAAENIRLPNAGTQVRVTVFPSKTVAQYSGVPWWIILVAILAGILMLALLVFILWKCGFFKRSRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS	Literature-reported	Abrogation of lung metastasis of human fibrosarcoma cells by ribozyme-mediated suppression of integrin alpha6 subunit expression. Int J Cancer. 1996 Feb 8;65(4):519-24.	.	TC=8.A.54	Integrin	integrin alpha chain family.	.	.	FG-GAP repeat; Integrin alpha	PF01839; PF08441	PF01839; FG-GAP; PF08441; Integrin_alpha2	8.A.54.1.2	The Integrin (Integrin) Family	hsa04151: PI3K-Akt signaling pathway; hsa04510: Focal adhesion; hsa04512: ECM-receptor interaction; hsa04514: Cell adhesion molecules; hsa04640: Hematopoietic cell lineage; hsa04810: Regulation of actin cytoskeleton; hsa05145: Toxoplasmosis; hsa05165: Human papillomavirus infection; hsa05200: Pathways in cancer; hsa05222: Small cell lung cancer; hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy	R-HSA-2022090: Assembly of collagen fibrils and other multimeric structures; R-HSA-210991: Basigin interactions; R-HSA-216083: Integrin cell surface interactions; R-HSA-3000157: Laminin interactions; R-HSA-3000170: Syndecan interactions; R-HSA-446107: Type I hemidesmosome assembly	.	P23229
TT1FW8B	Integrin alpha-8 (ITGA8)	P53708	ITA8_HUMAN	Integrin	Integrin alpha-8 light chain; Integrin alpha-8 heavy chain	ITGA8	"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."	.	.	MSPGASRGPRGSQAPLIAPLCCAAAALGMLLWSPACQAFNLDVEKLTVYSGPKGSYFGYAVDFHIPDARTASVLVGAPKANTSQPDIVEGGAVYYCPWPAEGSAQCRQIPFDTTNNRKIRVNGTKEPIEFKSNQWFGATVKAHKGKVVACAPLYHWRTLKPTPEKDPVGTCYVAIQNFSAYAEFSPCRNSNADPEGQGYCQAGFSLDFYKNGDLIVGGPGSFYWQGQVITASVADIIANYSFKDILRKLAGEKQTEVAPASYDDSYLGYSVAAGEFTGDSQQELVAGIPRGAQNFGYVSIINSTDMTFIQNFTGEQMASYFGYTVVVSDVNSDGLDDVLVGAPLFMEREFESNPREVGQIYLYLQVSSLLFRDPQILTGTETFGRFGSAMAHLGDLNQDGYNDIAIGVPFAGKDQRGKVLIYNGNKDGLNTKPSQVLQGVWASHAVPSGFGFTLRGDSDIDKNDYPDLIVGAFGTGKVAVYRARPVVTVDAQLLLHPMIINLENKTCQVPDSMTSAACFSLRVCASVTGQSIANTIVLMAEVQLDSLKQKGAIKRTLFLDNHQAHRVFPLVIKRQKSHQCQDFIVYLRDETEFRDKLSPINISLNYSLDESTFKEGLEVKPILNYYRENIVSEQAHILVDCGEDNLCVPDLKLSARPDKHQVIIGDENHLMLIINARNEGEGAYEAELFVMIPEEADYVGIERNNKGFRPLSCEYKMENVTRMVVCDLGNPMVSGTNYSLGLRFAVPRLEKTNMSINFDLQIRSSNKDNPDSNFVSLQINITAVAQVEIRGVSHPPQIVLPIHNWEPEEEPHKEEEVGPLVEHIYELHNIGPSTISDTILEVGWPFSARDEFLLYIFHIQTLGPLQCQPNPNINPQDIKPAASPEDTPELSAFLRNSTIPHLVRKRDVHVVEFHRQSPAKILNCTNIECLQISCAVGRLEGGESAVLKVRSRLWAHTFLQRKNDPYALASLVSFEVKKMPYTDQPAKLPEGSIVIKTSVIWATPNVSFSIPLWVIILAILLGLLVLAILTLALWKCGFFDRARPPQEDMTDREQLTNDKTPEA	Literature-reported	Highly Expressed Integrin-8 Induces Epithelial to Mesenchymal Transition-Like Features in Multiple Myeloma with Early Relapse. Mol Cells. 2016 Dec;39(12):898-908.	.	TC=8.A.54	.	integrin alpha chain family.	.	.	FG-GAP repeat; Integrin alpha cytoplasmic region; Integrin alpha	PF01839; PF00357; PF08441	PF01839; FG-GAP; PF00357; Integrin_alpha; PF08441; Integrin_alpha2	.	.	hsa04151: PI3K-Akt signaling pathway; hsa04510: Focal adhesion; hsa04512: ECM-receptor interaction; hsa04514: Cell adhesion molecules; hsa04810: Regulation of actin cytoskeleton; hsa05165: Human papillomavirus infection; hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy	R-HSA-2129379: Molecules associated with elastic fibres; R-HSA-216083: Integrin cell surface interactions; R-HSA-2173789: TGF-beta receptor signaling activates SMADs; R-HSA-3000178: ECM proteoglycans	.	P53708
TTH0Z37	Integrin alpha-E (ITGAE)	P38570	ITAE_HUMAN	Integrin	Mucosal lymphocyte 1 antigen; Integrin alphaIEL; Integrin alphaE heavy chain; Integrin alpha-IEL; HML1 antigen; HML-1 antigen; CD103	ITGAE	It mediates adhesion of intra-epithelial T-lymphocytes to epithelial cell monolayers. Integrin alpha-E/beta-7 is a receptor for E-cadherin.	.	.	MWLFHTLLCIASLALLAAFNVDVARPWLTPKGGAPFVLSSLLHQDPSTNQTWLLVTSPRTKRTPGPLHRCSLVQDEILCHPVEHVPIPKGRHRGVTVVRSHHGVLICIQVLVRRPHSLSSELTGTCSLLGPDLRPQAQANFFDLENLLDPDARVDTGDCYSNKEGGGEDDVNTARQRRALEKEEEEDKEEEEDEEEEEAGTEIAIILDGSGSIDPPDFQRAKDFISNMMRNFYEKCFECNFALVQYGGVIQTEFDLRDSQDVMASLARVQNITQVGSVTKTASAMQHVLDSIFTSSHGSRRKASKVMVVLTDGGIFEDPLNLTTVINSPKMQGVERFAIGVGEEFKSARTARELNLIASDPDETHAFKVTNYMALDGLLSKLRYNIISMEGTVGDALHYQLAQIGFSAQILDERQVLLGAVGAFDWSGGALLYDTRSRRGRFLNQTAAAAADAEAAQYSYLGYAVAVLHKTCSLSYIAGAPRYKHHGAVFELQKEGREASFLPVLEGEQMGSYFGSELCPVDIDMDGSTDFLLVAAPFYHVHGEEGRVYVYRLSEQDGSFSLARILSGHPGFTNARFGFAMAAMGDLSQDKLTDVAIGAPLEGFGADDGASFGSVYIYNGHWDGLSASPSQRIRASTVAPGLQYFGMSMAGGFDISGDGLADITVGTLGQAVVFRSRPVVRLKVSMAFTPSALPIGFNGVVNVRLCFEISSVTTASESGLREALLNFTLDVDVGKQRRRLQCSDVRSCLGCLREWSSGSQLCEDLLLMPTEGELCEEDCFSNASVKVSYQLQTPEGQTDHPQPILDRYTEPFAIFQLPYEKACKNKLFCVAELQLATTVSQQELVVGLTKELTLNINLTNSGEDSYMTSMALNYPRNLQLKRMQKPPSPNIQCDDPQPVASVLIMNCRIGHPVLKRSSAHVSVVWQLEENAFPNRTADITVTVTNSNERRSLANETHTLQFRHGFVAVLSKPSIMYVNTGQGLSHHKEFLFHVHGENLFGAEYQLQICVPTKLRGLQVVAVKKLTRTQASTVCTWSQERACAYSSVQHVEEWHSVSCVIASDKENVTVAAEISWDHSEELLKDVTELQILGEISFNKSLYEGLNAENHRTKITVVFLKDEKYHSLPIIIKGSVGGLLVLIVILVILFKCGFFKRKYQQLNLESIRKAQLKSENLLEEEN	Literature-reported	CD103+ tumor-infiltrating lymphocytes are tumor-reactive intraepithelial CD8+ T cells associated with prognostic benefit and therapy response in ce... Oncoimmunology. 2017 Jul 24;6(9):e1338230.	.	TC=8.A.54	.	integrin alpha chain family.	.	.	FG-GAP repeat; Integrin alpha cytoplasmic region; Integrin alpha; von Willebrand factor type A domain	PF01839; PF00357; PF08441; PF00092	PF01839; FG-GAP; PF00357; Integrin_alpha; PF08441; Integrin_alpha2; PF00092; VWA	.	.	hsa04810: Regulation of actin cytoskeleton	R-HSA-216083: Integrin cell surface interactions	.	P38570
TT48WR6	Integrin alpha-L (ITGAL)	P20701	ITAL_HUMAN	Integrin	"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"	ITGAL	"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."	.	6CKB; 6BXJ; 6BXF; 6BXB; 5E6U	MKDSCITVMAMALLSGFFFFAPASSYNLDVRGARSFSPPRAGRHFGYRVLQVGNGVIVGAPGEGNSTGSLYQCQSGTGHCLPVTLRGSNYTSKYLGMTLATDPTDGSILACDPGLSRTCDQNTYLSGLCYLFRQNLQGPMLQGRPGFQECIKGNVDLVFLFDGSMSLQPDEFQKILDFMKDVMKKLSNTSYQFAAVQFSTSYKTEFDFSDYVKRKDPDALLKHVKHMLLLTNTFGAINYVATEVFREELGARPDATKVLIIITDGEATDSGNIDAAKDIIRYIIGIGKHFQTKESQETLHKFASKPASEFVKILDTFEKLKDLFTELQKKIYVIEGTSKQDLTSFNMELSSSGISADLSRGHAVVGAVGAKDWAGGFLDLKADLQDDTFIGNEPLTPEVRAGYLGYTVTWLPSRQKTSLLASGAPRYQHMGRVLLFQEPQGGGHWSQVQTIHGTQIGSYFGGELCGVDVDQDGETELLLIGAPLFYGEQRGGRVFIYQRRQLGFEEVSELQGDPGYPLGRFGEAITALTDINGDGLVDVAVGAPLEEQGAVYIFNGRHGGLSPQPSQRIEGTQVLSGIQWFGRSIHGVKDLEGDGLADVAVGAESQMIVLSSRPVVDMVTLMSFSPAEIPVHEVECSYSTSNKMKEGVNITICFQIKSLIPQFQGRLVANLTYTLQLDGHRTRRRGLFPGGRHELRRNIAVTTSMSCTDFSFHFPVCVQDLISPINVSLNFSLWEEEGTPRDQRAQGKDIPPILRPSLHSETWEIPFEKNCGEDKKCEANLRVSFSPARSRALRLTAFASLSVELSLSNLEEDAYWVQLDLHFPPGLSFRKVEMLKPHSQIPVSCEELPEESRLLSRALSCNVSSPIFKAGHSVALQMMFNTLVNSSWGDSVELHANVTCNNEDSDLLEDNSATTIIPILYPINILIQDQEDSTLYVSFTPKGPKIHQVKHMYQVRIQPSIHDHNIPTLEAVVGVPQPPSEGPITHQWSVQMEPPVPCHYEDLERLPDAAEPCLPGALFRCPVVFRQEILVQVIGTLELVGEIEASSMFSLCSSLSISFNSSKHFHLYGSNASLAQVVMKVDVVYEKQMLYLYVLSGIGGLLLLLLIFIVLYKVGFFKRNLKEKMEAGRGVPNGIPAEDSEQLASGQEAGDPGCLKPLHEKDSESGGGKD	Successful	"Corneal inflammation is inhibited by the LFA-1 antagonist, lifitegrast (SAR 1118). J Ocul Pharmacol Ther. 2013 May;29(4):395-402."	34	TC=8.A.54	Integrin	integrin alpha chain family.	.	.	FG-GAP repeat; Integrin alpha cytoplasmic region; Integrin alpha; von Willebrand factor type A domain	PF01839; PF00357; PF08441; PF00092	PF01839; FG-GAP; PF00357; Integrin_alpha; PF08441; Integrin_alpha2; PF00092; VWA	.	.	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	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	.	P20701
TTB69FJ	Integrin alpha-M (ITGAM)	P11215	ITAM_HUMAN	Integrin	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	ITGAM	"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."	.	4XW2; 4M76; 3QA3; 3Q3G; 2LKJ	MALRVLLLTALTLCHGFNLDTENAMTFQENARGFGQSVVQLQGSRVVVGAPQEIVAANQRGSLYQCDYSTGSCEPIRLQVPVEAVNMSLGLSLAATTSPPQLLACGPTVHQTCSENTYVKGLCFLFGSNLRQQPQKFPEALRGCPQEDSDIAFLIDGSGSIIPHDFRRMKEFVSTVMEQLKKSKTLFSLMQYSEEFRIHFTFKEFQNNPNPRSLVKPITQLLGRTHTATGIRKVVRELFNITNGARKNAFKILVVITDGEKFGDPLGYEDVIPEADREGVIRYVIGVGDAFRSEKSRQELNTIASKPPRDHVFQVNNFEALKTIQNQLREKIFAIEGTQTGSSSSFEHEMSQEGFSAAITSNGPLLSTVGSYDWAGGVFLYTSKEKSTFINMTRVDSDMNDAYLGYAAAIILRNRVQSLVLGAPRYQHIGLVAMFRQNTGMWESNANVKGTQIGAYFGASLCSVDVDSNGSTDLVLIGAPHYYEQTRGGQVSVCPLPRGRARWQCDAVLYGEQGQPWGRFGAALTVLGDVNGDKLTDVAIGAPGEEDNRGAVYLFHGTSGSGISPSHSQRIAGSKLSPRLQYFGQSLSGGQDLTMDGLVDLTVGAQGHVLLLRSQPVLRVKAIMEFNPREVARNVFECNDQVVKGKEAGEVRVCLHVQKSTRDRLREGQIQSVVTYDLALDSGRPHSRAVFNETKNSTRRQTQVLGLTQTCETLKLQLPNCIEDPVSPIVLRLNFSLVGTPLSAFGNLRPVLAEDAQRLFTALFPFEKNCGNDNICQDDLSITFSFMSLDCLVVGGPREFNVTVTVRNDGEDSYRTQVTFFFPLDLSYRKVSTLQNQRSQRSWRLACESASSTEVSGALKSTSCSINHPIFPENSEVTFNITFDVDSKASLGNKLLLKANVTSENNMPRTNKTEFQLELPVKYAVYMVVTSHGVSTKYLNFTASENTSRVMQHQYQVSNLGQRSLPISLVFLVPVRLNQTVIWDRPQVTFSENLSSTCHTKERLPSHSDFLAELRKAPVVNCSIAVCQRIQCDIPFFGIQEEFNATLKGNLSFDWYIKTSHNHLLIVSTAEILFNDSVFTLLPGQGAFVRSQTETKVEPFEVPNPLPLIVGSSVGGLLLLALITAALYKLGFFKRQYKDMMSEGGPPGAEPQ	Clinical trial	Biomarkers of eosinophil involvement in allergic and eosinophilic diseases: review of phenotypic and serum markers including a novel assay to quantify levels of soluble Siglec-8. J Immunol Methods. 2012 Sep 28;383(1-2):39-46. 	.	TC=8.A.54	.	integrin alpha chain family.	.	.	FG-GAP repeat; Integrin alpha cytoplasmic region; Integrin alpha; von Willebrand factor type A domain	PF01839; PF00357; PF08441; PF00092	PF01839; FG-GAP; PF00357; Integrin_alpha; PF08441; Integrin_alpha2; PF00092; VWA	.	.	hsa04015: Rap1 signaling pathway; hsa04145: Phagosome; hsa04514: Cell adhesion molecules; hsa04610: Complement and coagulation cascades; hsa04613: Neutrophil extracellular trap formation; hsa04640: Hematopoietic cell lineage; hsa04670: Leukocyte transendothelial migration; hsa04810: Regulation of actin cytoskeleton; hsa05133: Pertussis; hsa05134: Legionellosis; hsa05140: Leishmaniasis; hsa05146: Amoebiasis; hsa05150: Staphylococcus aureus infection; hsa05152: Tuberculosis; hsa05202: Transcriptional misregulation in cancer; hsa05221: Acute myeloid leukemia	R-HSA-166016: Toll Like Receptor 4 (TLR4) Cascade; R-HSA-202733: Cell surface interactions at the vascular wall; R-HSA-216083: Integrin cell surface interactions; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6798695: Neutrophil degranulation	.	P11215
TTT1R2L	Integrin alpha-V (ITGAV)	P06756	ITAV_HUMAN	Integrin	Vitronectin receptor subunit alpha; Vitronectin receptor alpha subunit; Vitronectin receptor; VTNR; VNRA; MSK8; CD51 antigen; CD51	ITGAV	"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."	.	6DJP; 6AVU; 6AVR; 6AVQ; 5NEU	MAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET	Clinical trial	Abituzumab combined with cetuximab plus irinotecan versus cetuximab plus irinotecan alone for patients with KRAS wild-type metastatic colorectal cancer: the randomised phase I/II POSEIDON trial. Ann Oncol. 2015 Jan;26(1):132-40.	21	TC=8.A.54	Integrin	integrin alpha chain family.	.	.	FG-GAP repeat; Integrin alpha cytoplasmic region; Integrin alpha	PF01839; PF00357; PF08441	PF01839; FG-GAP; PF00357; Integrin_alpha; PF08441; Integrin_alpha2	8.A.54.1.4	The Integrin (Integrin) Family	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	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	.	P06756
TT2VIZQ	ITGAV messenger RNA (ITGAV mRNA)	P06756	ITAV_HUMAN	mRNA target	Vitronectin receptor subunit alpha (mRNA); Vitronectin receptor alpha subunit (mRNA); Vitronectin receptor (mRNA); VTNR (mRNA); VNRA (mRNA); MSK8 (mRNA); CD51 antigen (mRNA); CD51 (mRNA)	ITGAV	"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."	.	6DJP; 6AVU; 6AVR; 6AVQ; 5NEU	MAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET	Clinical trial	Design and development of antisense drugs. Expert Opin. Drug Discov. 2008 3(10):1189-1207.	21	mRNA	mRNA target	.	.	.	FG-GAP repeat; Integrin alpha cytoplasmic region; Integrin alpha	PF01839; PF00357; PF08441	PF01839; FG-GAP; PF00357; Integrin_alpha; PF08441; Integrin_alpha2	.	.	hsa04145: Phagosome; hsa04151: PI3K-Akt signaling pathway; hsa04510: Focal adhesion; hsa04512: ECM-receptor interaction; hsa04514: Cell adhesion molecules; hsa04810: Regulation of actin cytoskeleton; hsa04919: Thyroid hormone signaling pathway; hsa05163: Human cytomegalovirus infection; hsa05165: Human papillomavirus infection; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05222: Small cell lung cancer; hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy; hsa05418: Fluid shear stress and atherosclerosis	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-2173789: TGF-beta receptor signaling activates SMADs; R-HSA-3000157: Laminin interactions; R-HSA-3000170: Syndecan interactions; R-HSA-3000178: ECM proteoglycans; R-HSA-4420097: VEGFA-VEGFR2 Pathway; R-HSA-445144: Signal transduction by L1; R-HSA-6798695: Neutrophil degranulation	.	P06756
TT69TQN	Integrin alpha-V/beta-3 (ITGAV/B3)	P06756-P05106	ITAV_HUMAN-ITB3_HUMAN	Integrin	Integrin alphaVbeta3; Integrin alpha-v beta-3; Integrin alpha V beta 3; Alpha(v)beta(3) Integrin; Alpha v beta 3 integrin	ITGAV-ITGB3	"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."	.	.	MRARPRPRPLWATVLALGALAGVGVGGPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPDILVVLLSVMGAILLIGLAALLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGTMAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET	Clinical trial	A non-RGD-based integrin binding peptide (ATN-161) blocks breast cancer growth and metastasis in vivo. Mol Cancer Ther. 2006 Sep;5(9):2271-80.	21	TC=8.A.54	Integrin	.	.	.	.	.	.	.	.	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	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	.	P06756
TTPRDH7	Integrin alpha-V/beta-5 (ITGAV/B5)	P06756-P18084	ITAV_HUMAN-ITB5_HUMAN	Integrin	Integrin; Vitronectin receptor	ITGAV-ITGB5	"Binds to matrix macromolecules and proteinases and thereby stimulates angiogenesis. However, it inhibits angiogenesis."	.	.	MPRAPAPLYACLLGLCALLPRLAGLNICTSGSATSCEECLLIHPKCAWCSKEDFGSPRSITSRCDLRANLVKNGCGGEIESPASSFHVLRSLPLSSKGSGSAGWDVIQMTPQEIAVNLRPGDKTTFQLQVRQVEDYPVDLYYLMDLSLSMKDDLDNIRSLGTKLAEEMRKLTSNFRLGFGSFVDKDISPFSYTAPRYQTNPCIGYKLFPNCVPSFGFRHLLPLTDRVDSFNEEVRKQRVSRNRDAPEGGFDAVLQAAVCKEKIGWRKDALHLLVFTTDDVPHIALDGKLGGLVQPHDGQCHLNEANEYTASNQMDYPSLALLGEKLAENNINLIFAVTKNHYMLYKNFTALIPGTTVEILDGDSKNIIQLIINAYNSIRSKVELSVWDQPEDLNLFFTATCQDGVSYPGQRKCEGLKIGDTASFEVSLEARSCPSRHTEHVFALRPVGFRDSLEVGVTYNCTCGCSVGLEPNSARCNGSGTYVCGLCECSPGYLGTRCECQDGENQSVYQNLCREAEGKPLCSGRGDCSCNQCSCFESEFGKIYGPFCECDNFSCARNKGVLCSGHGECHCGECKCHAGYIGDNCNCSTDISTCRGRDGQICSERGHCLCGQCQCTEPGAFGEMCEKCPTCPDACSTKRDCVECLLLHSGKPDNQTCHSLCRDEVITWVDTIVKDDQEAVLCFYKTAKDCVMMFTYVELPSGKSNLTVLREPECGNTPNAMTILLAVVGSILLVGLALLAIWKLLVTIHDRREFAKFQSERSRARYEMASNPLYRKPISTHTVDFTFNKFNKSYNGTVDMAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET	Discontinued	"SB-267268, a nonpeptidic antagonist of alpha(v)beta3 and alpha(v)beta5 integrins, reduces angiogenesis and VEGF expression in a mouse model of retinopathy of prematurity. Invest Ophthalmol Vis Sci. 2006 Apr;47(4):1600-5."	3	TC=8.A.54	Integrin	.	.	.	.	.	.	.	.	.	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	.	P06756
TTIQSVM	Integrin alpha-V/beta-6 (ITGAV/B6)	P06756-P18564	ITAV_HUMAN-ITB6_HUMAN	Integrin	alpha(V)beta(6) integrin; Alpha V beta 6 integrin	ITGAV-ITGB6	"It is expressed exclusively on subsets of epithelial cells, especially during development, after injury or inflammation, or on many carcinomas."	.	.	MGIELLCLFFLFLGRNDHVQGGCALGGAETCEDCLLIGPQCAWCAQENFTHPSGVGERCDTPANLLAKGCQLNFIENPVSQVEILKNKPLSVGRQKNSSDIVQIAPQSLILKLRPGGAQTLQVHVRQTEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKPVSPFVKTTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVIPNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENYAKLIPGATVGLLQKDSGNILQLIISAYEELRSEVELEVLGDTEGLNLSFTAICNNGTLFQHQKKCSHMKVGDTASFSVTVNIPHCERRSRHIIIKPVGLGDALELLVSPECNCDCQKEVEVNSSKCHHGNGSFQCGVCACHPGHMGPRCECGEDMLSTDSCKEAPDHPSCSGRGDCYCGQCICHLSPYGNIYGPYCQCDNFSCVRHKGLLCGGNGDCDCGECVCRSGWTGEYCNCTTSTDSCVSEDGVLCSGRGDCVCGKCVCTNPGASGPTCERCPTCGDPCNSKRSCIECHLSAAGQAREECVDKCKLAGATISEEEDFSKDGSVSCSLQGENECLITFLITTDNEGKTIIHSINEKDCPKPPNIPMIMLGVSLAILLIGVVLLCIWKLLVSFHDRKEVAKFEAERSKAKWQTGTNPLYRGSTSTFKNVTYKHREKQKVDLSTDCMAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET	Clinical trial	"Integrin-mediated regulation of TGFbeta in fibrosis. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease Volume 1832, Issue 7, July 2013, Pages 891-896."	21	TC=8.A.54	.	.	.	.	.	.	.	.	.	.	.	.	P06756
TT7B3HE	Integrin alpha-V/beta-8 (ITGAV/B8)	P06756-P26012	ITAV_HUMAN-ITB8_HUMAN	.	.	ITGAV-ITGB8	.	.	.	.	Clinical trial	ClinicalTrials.gov (NCT04152018) Study of PF-06940434 in Patients With Advanced or Metastatic Solid Tumors.. U.S. National Institutes of Health.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P06756
TTBVIQC	Integrin beta-1 (ITGB1)	P05556	ITB1_HUMAN	Integrin	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	ITGB1	"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."	.	4WK4; 4WK2; 4WK0; 4WJK; 4DX9	MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK	Clinical trial	Radretumab radioimmunotherapy in patients with brain metastasis: a 124I-L19SIP dosimetric PET study. Cancer Immunol Res. 2013 Aug;1(2):134-43.	19	TC=8.A.54	Integrin	integrin beta chain family.	.	.	EGF-like domain; Integrin beta epidermal growth factor like domain 1; Integrin beta cytoplasmic domain; Integrin beta tail domain; Integrin beta chain VWA domain; Integrin plexin domain	PF07974; PF18372; PF08725; PF07965; PF00362; PF17205	PF07974; EGF_2; PF18372; I-EGF_1; PF08725; Integrin_b_cyt; PF07965; Integrin_B_tail; PF00362; Integrin_beta; PF17205; PSI_integrin	9.B.87.1.8	The Selenoprotein P Receptor (SelP-Receptor) Family	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	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	.	P05556
TTIJWR7	Integrin beta-2 (ITGB2)	P05107	ITB2_HUMAN	Integrin	"MFI7; Integrin alpha-M/beta-2; Complement receptor C3 subunit beta; Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta; CD18"	ITGB2	"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."	.	5ZAZ; 5XR1; 5ES4; 5E6X; 5E6W	MLGLRPPLLALVGLLSLGCVLSQECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELSEDSSNVVQLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFCSNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSFVIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHGKGFLECGICRCDTGYIGKNCECQTQGRSSQELEGSCRKDNNSIICSGLGDCVCGQCLCHTSDVPGKLIYGQYCECDTINCERYNGQVCGGPGRGLCFCGKCRCHPGFEGSACQCERTTEGCLNPRRVECSGRGRCRCNVCECHSGYQLPLCQECPGCPSPCGKYISCAECLKFEKGPFGKNCSAACPGLQLSNNPVKGRTCKERDSEGCWVAYTLEQQDGMDRYLIYVDESRECVAGPNIAAIVGGTVAGIVLIGILLLVIWKALIHLSDLREYRRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES	Clinical trial	Advances in ischemic stroke treatment: neuroprotective and combination therapies. Expert Opin Emerg Drugs. 2007 Mar;12(1):97-112.	5	TC=8.A.54	Integrin	integrin beta chain family.	.	.	Integrin beta cytoplasmic domain; Integrin beta tail domain; Integrin beta chain VWA domain; Integrin plexin domain	PF08725; PF07965; PF00362; PF17205	PF08725; Integrin_b_cyt; PF07965; Integrin_B_tail; PF00362; Integrin_beta; PF17205; PSI_integrin	.	.	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	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	.	P05107
TTJA1ZO	ITGB3 messenger RNA (ITGB3 mRNA)	P05106	ITB3_HUMAN	mRNA target	Platelet membrane glycoprotein IIIa (mRNA); Integrin beta-3 (mRNA); GPIIIa (mRNA); GP3A (mRNA); CD61 (mRNA)	ITGB3	"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."	.	6CKB; 6BXJ; 6BXF; 6BXB; 6AVU	MRARPRPRPLWATVLALGALAGVGVGGPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPDILVVLLSVMGAILLIGLAALLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGT	Discontinued	"Potent, orally active GPIIb/IIIa antagonists containing a nipecotic acid subunit. Structure-activity studies leading to the discovery of RWJ-53308. J Med Chem. 1999 Dec 16;42(25):5254-65."	9	mRNA	mRNA target	.	.	.	EGF-like domain; Integrin beta epidermal growth factor like domain 1; Integrin beta cytoplasmic domain; Integrin beta tail domain; Integrin beta chain VWA domain; Integrin plexin domain	PF07974; PF18372; PF08725; PF07965; PF00362; PF17205	PF07974; EGF_2; PF18372; I-EGF_1; PF08725; Integrin_b_cyt; PF07965; Integrin_B_tail; PF00362; Integrin_beta; PF17205; PSI_integrin	.	.	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	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	.	P05106
TT8NBXR	Integrin beta-3 (ITGB3)	P05106	ITB3_HUMAN	Integrin	GPIIIa; GP3A; CD61	ITGB3	"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."	.	6CKB; 6BXJ; 6BXF; 6BXB; 6AVU	MRARPRPRPLWATVLALGALAGVGVGGPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPDILVVLLSVMGAILLIGLAALLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGT	Literature-reported	The mammary progenitor marker CD61/beta3 integrin identifies cancer stem cells in mouse models of mammary tumorigenesis. Cancer Res. 2008 Oct 1;68(19):7711-7.	.	TC=8.A.54	Integrin	integrin beta chain family.	.	.	EGF-like domain; Integrin beta epidermal growth factor like domain 1; Integrin beta cytoplasmic domain; Integrin beta tail domain; Integrin beta chain VWA domain; Integrin plexin domain	PF07974; PF18372; PF08725; PF07965; PF00362; PF17205	PF07974; EGF_2; PF18372; I-EGF_1; PF08725; Integrin_b_cyt; PF07965; Integrin_B_tail; PF00362; Integrin_beta; PF17205; PSI_integrin	.	.	hsa04015: Rap1 signaling pathway; hsa04145: Phagosome; hsa04151: PI3K-Akt signaling pathway; hsa04380: Osteoclast differentiation; hsa04510: Focal adhesion; hsa04512: ECM-receptor interaction; hsa04611: Platelet activation; hsa04613: Neutrophil extracellular trap formation; hsa04640: Hematopoietic cell lineage; hsa04810: Regulation of actin cytoskeleton; hsa04919: Thyroid hormone signaling pathway; hsa05163: Human cytomegalovirus infection; hsa05165: Human papillomavirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05205: Proteoglycans in cancer; hsa05206: MicroRNAs in cancer; hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy; hsa05418: Fluid shear stress and atherosclerosis	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-2173789: TGF-beta receptor signaling activates SMADs; R-HSA-3000170: Syndecan interactions; R-HSA-3000178: ECM proteoglycans; R-HSA-354192: Integrin 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-445144: Signal transduction by L1; R-HSA-5674135: MAP2K and MAPK activation; R-HSA-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants	.	P05106
TTKQSXZ	Integrin beta-6 (ITGB6)	P18564	ITB6_HUMAN	.	.	ITGB6	"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."	.	.	MGIELLCLFFLFLGRNDHVQGGCALGGAETCEDCLLIGPQCAWCAQENFTHPSGVGERCDTPANLLAKGCQLNFIENPVSQVEILKNKPLSVGRQKNSSDIVQIAPQSLILKLRPGGAQTLQVHVRQTEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKPVSPFVKTTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVIPNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENYAKLIPGATVGLLQKDSGNILQLIISAYEELRSEVELEVLGDTEGLNLSFTAICNNGTLFQHQKKCSHMKVGDTASFSVTVNIPHCERRSRHIIIKPVGLGDALELLVSPECNCDCQKEVEVNSSKCHHGNGSFQCGVCACHPGHMGPRCECGEDMLSTDSCKEAPDHPSCSGRGDCYCGQCICHLSPYGNIYGPYCQCDNFSCVRHKGLLCGGNGDCDCGECVCRSGWTGEYCNCTTSTDSCVSEDGVLCSGRGDCVCGKCVCTNPGASGPTCERCPTCGDPCNSKRSCIECHLSAAGQAREECVDKCKLAGATISEEEDFSKDGSVSCSLQGENECLITFLITTDNEGKTIIHSINEKDCPKPPNIPMIMLGVSLAILLIGVVLLCIWKLLVSFHDRKEVAKFEAERSKAKWQTGTNPLYRGSTSTFKNVTYKHREKQKVDLSTDC	Clinical trial	"Clinical pipeline report, company report or official report of Seagen."	.	.	.	.	.	.	.	.	.	.	.	hsa04151: PI3K-Akt signaling pathway; hsa04510: Focal adhesion; hsa04512: ECM-receptor interaction; hsa04810: Regulation of actin cytoskeleton; hsa05165: Human papillomavirus infection; hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy	R-HSA-1566948: Elastic fibre formation; R-HSA-2129379: Molecules associated with elastic fibres; R-HSA-216083: Integrin cell surface interactions; R-HSA-2173789: TGF-beta receptor signaling activates SMADs; R-HSA-3000178: ECM proteoglycans	.	P18564
TTLT9XQ	Integrin beta-7 (ITGB7)	P26010	ITB7_HUMAN	Integrin	Gut homing receptor beta subunit	ITGB7	"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)."	.	3V4V; 3V4P; 2BRQ	MVALPMVLVLLLVLSRGESELDAKIPSTGDATEWRNPHLSMLGSCQPAPSCQKCILSHPSCAWCKQLNFTASGEAEARRCARREELLARGCPLEELEEPRGQQEVLQDQPLSQGARGEGATQLAPQRVRVTLRPGEPQQLQVRFLRAEGYPVDLYYLMDLSYSMKDDLERVRQLGHALLVRLQEVTHSVRIGFGSFVDKTVLPFVSTVPSKLRHPCPTRLERCQSPFSFHHVLSLTGDAQAFEREVGRQSVSGNLDSPEGGFDAILQAALCQEQIGWRNVSRLLVFTSDDTFHTAGDGKLGGIFMPSDGHCHLDSNGLYSRSTEFDYPSVGQVAQALSAANIQPIFAVTSAALPVYQELSKLIPKSAVGELSEDSSNVVQLIMDAYNSLSSTVTLEHSSLPPGVHISYESQCEGPEKREGKAEDRGQCNHVRINQTVTFWVSLQATHCLPEPHLLRLRALGFSEELIVELHTLCDCNCSDTQPQAPHCSDGQGHLQCGVCSCAPGRLGRLCECSVAELSSPDLESGCRAPNGTGPLCSGKGHCQCGRCSCSGQSSGHLCECDDASCERHEGILCGGFGRCQCGVCHCHANRTGRACECSGDMDSCISPEGGLCSGHGRCKCNRCQCLDGYYGALCDQCPGCKTPCERHRDCAECGAFRTGPLATNCSTACAHTNVTLALAPILDDGWCKERTLDNQLFFFLVEDDARGTVVLRVRPQEKGADHTQAIVLGCVGGIVAVGLGLVLAYRLSVEIYDRREYSRFEKEQQQLNWKQDSNPLYKSAITTTINPRFQEADSPTL	Successful	"Clinical pipeline report, company report or official report of Takeda (2009)."	34	TC=8.A.54	.	integrin beta chain family.	.	.	EGF-like domain; Integrin beta cytoplasmic domain; Integrin beta chain VWA domain; Integrin plexin domain	PF07974; PF08725; PF00362; PF17205	PF07974; EGF_2; PF08725; Integrin_b_cyt; PF00362; Integrin_beta; PF17205; PSI_integrin	.	.	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	R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-216083:Integrin cell surface interactions	.	P26010
TTIF29E	Integrin beta-8 (ITGB8)	P26012	ITB8_HUMAN	Integrin	Integrin subunit beta 8	ITGB8	"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."	.	6DJP	MCGSALAFFTAAFVCLQNDRRGPASFLWAAWVFSLVLGLGQGEDNRCASSNAASCARCLALGPECGWCVQEDFISGGSRSERCDIVSNLISKGCSVDSIEYPSVHVIIPTENEINTQVTPGEVSIQLRPGAEANFMLKVHPLKKYPVDLYYLVDVSASMHNNIEKLNSVGNDLSRKMAFFSRDFRLGFGSYVDKTVSPYISIHPERIHNQCSDYNLDCMPPHGYIHVLSLTENITEFEKAVHRQKISGNIDTPEGGFDAMLQAAVCESHIGWRKEAKRLLLVMTDQTSHLALDSKLAGIVVPNDGNCHLKNNVYVKSTTMEHPSLGQLSEKLIDNNINVIFAVQGKQFHWYKDLLPLLPGTIAGEIESKAANLNNLVVEAYQKLISEVKVQVENQVQGIYFNITAICPDGSRKPGMEGCRNVTSNDEVLFNVTVTMKKCDVTGGKNYAIIKPIGFNETAKIHIHRNCSCQCEDNRGPKGKCVDETFLDSKCFQCDENKCHFDEDQFSSESCKSHKDQPVCSGRGVCVCGKCSCHKIKLGKVYGKYCEKDDFSCPYHHGNLCAGHGECEAGRCQCFSGWEGDRCQCPSAAAQHCVNSKGQVCSGRGTCVCGRCECTDPRSIGRFCEHCPTCYTACKENWNCMQCLHPHNLSQAILDQCKTSCALMEQQHYVDQTSECFSSPSYLRIFFIIFIVTFLIGLLKVLIIRQVILQWNSNKIKSSSDYRVSASKKDKLILQSVCTRAVTYRREKPEEIKMDISKLNAHETFRCNF	Patented-recorded	"miR-93 Promotes the Growth and Invasion of Prostate Cancer by Upregulating Its Target Genes TGFBR2, ITGB8, and LATS2. Mol Ther Oncolytics. 2018 Aug 16;11:14-19."	.	TC=8.A.54	Integrin	integrin beta chain family.	.	.	EGF-like domain; Integrin beta chain VWA domain; Integrin plexin domain	PF07974; PF00362; PF17205	PF07974; EGF_2; PF00362; Integrin_beta; PF17205; PSI_integrin	.	.	hsa04151: PI3K-Akt signaling pathway; hsa04510: Focal adhesion; hsa04512: ECM-receptor interaction; hsa04514: Cell adhesion molecules; hsa04810: Regulation of actin cytoskeleton; hsa05165: Human papillomavirus infection; hsa05410: Hypertrophic cardiomyopathy; hsa05412: Arrhythmogenic right ventricular cardiomyopathy; hsa05414: Dilated cardiomyopathy	R-HSA-2129379: Molecules associated with elastic fibres; R-HSA-216083: Integrin cell surface interactions; R-HSA-2173789: TGF-beta receptor signaling activates SMADs	.	P26012
TT3C80U	T-cell-specific kinase (ITK)	Q08881	ITK_HUMAN	Kinase	Tyrosine kinase ITK; Inducible T cell kinase; EMT	ITK	"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."	EC 2.7.10.2	4RFM; 4QD6; 4PQN; 4PPC; 4PPB	MNNFILLEEQLIKKSQQKRRTSPSNFKVRFFVLTKASLAYFEDRHGKKRTLKGSIELSRIKCVEIVKSDISIPCHYKYPFQVVHDNYLLYVFAPDRESRQRWVLALKEETRNNNSLVPKYHPNFWMDGKWRCCSQLEKLATGCAQYDPTKNASKKPLPPTPEDNRRPLWEPEETVVIALYDYQTNDPQELALRRNEEYCLLDSSEIHWWRVQDRNGHEGYVPSSYLVEKSPNNLETYEWYNKSISRDKAEKLLLDTGKEGAFMVRDSRTAGTYTVSVFTKAVVSENNPCIKHYHIKETNDNPKRYYVAEKYVFDSIPLLINYHQHNGGGLVTRLRYPVCFGRQKAPVTAGLRYGKWVIDPSELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRGLFAAETLLGMCLDVCEGMAYLEEACVIHRDLAARNCLVGENQVIKVSDFGMTRFVLDDQYTSSTGTKFPVKWASPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDISTGFRLYKPRLASTHVYQIMNHCWKERPEDRPAFSRLLRQLAEIAESGL	Clinical trial	Characterisation of a K390R ITK Kinase Dead Transgenic Mouse - Implications for ITK as a Therapeutic Target. PLoS One. 2014; 9(9): e107490.	21	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. TEC subfamily.	2.7.10.2	Transferring phosphorus-containing groups	BTK motif; PH domain; Protein tyrosine kinase; SH2 domain; SH3 domain	PF00779; PF00169; PF07714; PF00017; PF00018	PF00779; BTK; PF00169; PH; PF07714; Pkinase_Tyr; PF00017; SH2; PF00018; SH3_1	.	.	hsa04062:Chemokine signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04670:Leukocyte transendothelial migration	R-HSA-202433:Generation of second messenger molecules; R-HSA-2871809:FCERI mediated Ca+2 mobilization	.	Q08881
TTNHIXL	Tyrosine-protein kinase ITK (ITK)	Q08881	ITK_HUMAN	.	Tyrosine-protein kinase Lyk; Tyrosine-protein kinase ITK/TSK; LYK; Kinase EMT; Interleukin-2-inducible T-cell kinase; IL-2-inducible T-cell kinase	ITK	"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)."	EC 2.7.10.2	4RFM; 4QD6; 4PQN; 4PPC; 4PPB	MNNFILLEEQLIKKSQQKRRTSPSNFKVRFFVLTKASLAYFEDRHGKKRTLKGSIELSRIKCVEIVKSDISIPCHYKYPFQVVHDNYLLYVFAPDRESRQRWVLALKEETRNNNSLVPKYHPNFWMDGKWRCCSQLEKLATGCAQYDPTKNASKKPLPPTPEDNRRPLWEPEETVVIALYDYQTNDPQELALRRNEEYCLLDSSEIHWWRVQDRNGHEGYVPSSYLVEKSPNNLETYEWYNKSISRDKAEKLLLDTGKEGAFMVRDSRTAGTYTVSVFTKAVVSENNPCIKHYHIKETNDNPKRYYVAEKYVFDSIPLLINYHQHNGGGLVTRLRYPVCFGRQKAPVTAGLRYGKWVIDPSELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRGLFAAETLLGMCLDVCEGMAYLEEACVIHRDLAARNCLVGENQVIKVSDFGMTRFVLDDQYTSSTGTKFPVKWASPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDISTGFRLYKPRLASTHVYQIMNHCWKERPEDRPAFSRLLRQLAEIAESGL	Literature-reported	Ibrutinib is an irreversible molecular inhibitor of ITK driving a Th1-selective pressure in T lymphocytes. Blood. 2013 Oct 10;122(15):2539-49.	.	.	.	.	.	.	.	.	.	.	.	hsa04062: Chemokine signaling pathway; hsa04660: T cell receptor signaling pathway; hsa04670: Leukocyte transendothelial migration	R-HSA-202433: Generation of second messenger molecules; R-HSA-2871809: FCERI mediated Ca+2 mobilization	.	Q08881
TT5HWAT	IP3 receptor isoform 1 (ITPR1)	Q14643	ITPR1_HUMAN	Ryanodine-inositol triphosphate calcium channel	"Type 1 inositol 1,4,5-trisphosphate receptor; Type 1 InsP3 receptor; InsP3R1; Inositol 1,4,5-trisphosphate receptor type 1; IP3R 1"	ITPR1	"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."	.	.	MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPETGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPVKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMAKGEENKGNNDVEKLKSSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQTSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDETMDGASGENEHKKTEEGNNKPQKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHSIVQKTAMNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKLISIDELDNAELPPAPDSENATEELEPSPPLRQLEDHKRGEALRQVLVNRYYGNVRPSGRRESLTSFGNGPLSAGGPGKPGGGGGGSGSSSMSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQPGEGTQATADKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQSMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLVICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVDRLPNETAVPETGESLASEFLFSDVCRVESGENCSSPAPREELVPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIKERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 743).	0	TC=1.A.3	.	InsP3 receptor family.	.	.	"Inositol 1,4,5-trisphosphate/ryanodine receptor; Ion transport protein; MIR domain; RyR and IP3R Homology associated; RIH domain"	PF08709; PF00520; PF02815; PF08454; PF01365	PF08709; Ins145_P3_rec; PF00520; Ion_trans; PF02815; MIR; PF08454; RIH_assoc; PF01365; RYDR_ITPR	1.A.3.2.6	"The Ryanodine-Inositol 1,4,5-triphosphate Receptor Ca<sup>2+</sup> Channel (RIR-CaC) Family"	"hsa04020: Calcium signaling pathway; hsa04022: cGMP-PKG signaling pathway; hsa04070: Phosphatidylinositol signaling system; hsa04114: Oocyte meiosis; hsa04140: Autophagy - animal; hsa04210: Apoptosis; hsa04218: Cellular senescence; hsa04270: Vascular smooth muscle contraction; hsa04371: Apelin signaling pathway; hsa04540: Gap junction; hsa04611: Platelet activation; hsa04621: NOD-like receptor signaling pathway; hsa04625: C-type lectin receptor signaling pathway; hsa04713: Circadian entrainment; hsa04720: Long-term potentiation; hsa04723: Retrograde endocannabinoid signaling; hsa04724: Glutamatergic synapse; hsa04725: Cholinergic synapse; hsa04726: Serotonergic synapse; hsa04728: Dopaminergic synapse; hsa04730: Long-term depression; hsa04750: Inflammatory mediator regulation of TRP channels; hsa04912: GnRH signaling pathway; hsa04915: Estrogen signaling pathway; hsa04918: Thyroid hormone synthesis; hsa04921: Oxytocin signaling pathway; hsa04922: Glucagon signaling pathway; hsa04924: Renin secretion; hsa04925: Aldosterone synthesis and secretion; hsa04927: Cortisol synthesis and secretion; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04929: GnRH secretion; hsa04934: Cushing syndrome; hsa04935: Growth hormone synthesis, secretion and action; hsa04970: Salivary secretion; hsa04971: Gastric acid secretion; hsa04972: Pancreatic secretion; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05016: Huntington disease; hsa05017: Spinocerebellar ataxia; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05131: Shigellosis; hsa05163: Human cytomegalovirus infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05205: Proteoglycans in cancer; hsa05417: Lipid and atherosclerosis"	R-HSA-112043: PLC beta mediated events; R-HSA-114508: Effects of PIP2 hydrolysis; R-HSA-139853: Elevation of cytosolic Ca2+ levels; R-HSA-1489509: DAG and IP3 signaling; R-HSA-2029485: Role of phospholipids in phagocytosis; R-HSA-2871809: FCERI mediated Ca+2 mobilization; R-HSA-381676: Glucagon-like Peptide-1 (GLP1) regulates insulin secretion; R-HSA-4086398: Ca2+ pathway; R-HSA-418457: cGMP effects; R-HSA-422356: Regulation of insulin secretion; R-HSA-5218921: VEGFR2 mediated cell proliferation; R-HSA-5578775: Ion homeostasis; R-HSA-5607763: CLEC7A (Dectin-1) induces NFAT activation; R-HSA-9664323: FCGR3A-mediated IL10 synthesis; R-HSA-983695: Antigen activates B Cell Receptor (BCR) leading to generation of second messengers	.	.
TTC9IZL	"Inositol 1,4,5-trisphosphate receptor (ITPR)"	Q14643; Q14571; Q14573	ITPR1_HUMAN; ITPR2_HUMAN; ITPR3_HUMAN	.	InsP3R; InsP3 receptor; IP3R; IP3 receptor	ITPR1	"Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate."	.	.	MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPETGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPVKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMAKGEENKGNNDVEKLKSSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQTSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDETMDGASGENEHKKTEEGNNKPQKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHSIVQKTAMNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKLISIDELDNAELPPAPDSENATEELEPSPPLRQLEDHKRGEALRQVLVNRYYGNVRPSGRRESLTSFGNGPLSAGGPGKPGGGGGGSGSSSMSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQPGEGTQATADKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQSMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLVICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVDRLPNETAVPETGESLASEFLFSDVCRVESGENCSSPAPREELVPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIKERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA	Successful	"Prostacyclin and sodium nitroprusside inhibit the activity of the platelet inositol 1,4,5-trisphosphate receptor and promote its phosphorylation. J Biol Chem. 1996 Mar 8;271(10):5545-51."	34	.	.	.	.	.	.	.	.	.	.	"hsa04020: Calcium signaling pathway; hsa04022: cGMP-PKG signaling pathway; hsa04070: Phosphatidylinositol signaling system; hsa04114: Oocyte meiosis; hsa04140: Autophagy - animal; hsa04210: Apoptosis; hsa04218: Cellular senescence; hsa04270: Vascular smooth muscle contraction; hsa04371: Apelin signaling pathway; hsa04540: Gap junction; hsa04611: Platelet activation; hsa04621: NOD-like receptor signaling pathway; hsa04625: C-type lectin receptor signaling pathway; hsa04713: Circadian entrainment; hsa04720: Long-term potentiation; hsa04723: Retrograde endocannabinoid signaling; hsa04724: Glutamatergic synapse; hsa04725: Cholinergic synapse; hsa04726: Serotonergic synapse; hsa04728: Dopaminergic synapse; hsa04730: Long-term depression; hsa04750: Inflammatory mediator regulation of TRP channels; hsa04912: GnRH signaling pathway; hsa04915: Estrogen signaling pathway; hsa04918: Thyroid hormone synthesis; hsa04921: Oxytocin signaling pathway; hsa04922: Glucagon signaling pathway; hsa04924: Renin secretion; hsa04925: Aldosterone synthesis and secretion; hsa04927: Cortisol synthesis and secretion; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04929: GnRH secretion; hsa04934: Cushing syndrome; hsa04935: Growth hormone synthesis, secretion and action; hsa04970: Salivary secretion; hsa04971: Gastric acid secretion; hsa04972: Pancreatic secretion; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05016: Huntington disease; hsa05017: Spinocerebellar ataxia; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05131: Shigellosis; hsa05163: Human cytomegalovirus infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05205: Proteoglycans in cancer; hsa05417: Lipid and atherosclerosis"	R-HSA-112043: PLC beta mediated events; R-HSA-114508: Effects of PIP2 hydrolysis; R-HSA-139853: Elevation of cytosolic Ca2+ levels; R-HSA-1489509: DAG and IP3 signaling; R-HSA-2029485: Role of phospholipids in phagocytosis; R-HSA-2871809: FCERI mediated Ca+2 mobilization; R-HSA-381676: Glucagon-like Peptide-1 (GLP1) regulates insulin secretion; R-HSA-4086398: Ca2+ pathway; R-HSA-418457: cGMP effects; R-HSA-422356: Regulation of insulin secretion; R-HSA-5218921: VEGFR2 mediated cell proliferation; R-HSA-5578775: Ion homeostasis; R-HSA-5607763: CLEC7A (Dectin-1) induces NFAT activation; R-HSA-9664323: FCGR3A-mediated IL10 synthesis; R-HSA-983695: Antigen activates B Cell Receptor (BCR) leading to generation of second messengers	.	.
TTK9OV3	IP3 receptor isoform 2 (IP3R2)	Q14571	ITPR2_HUMAN	.	"Type 2 inositol 1,4,5-trisphosphate receptor; Type 2 InsP3 receptor; InsP3R2; Inositol 1,4,5-trisphosphate receptor type 2; IP3R 2"	ITPR2	"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)."	.	.	MTEKMSSFLYIGDIVSLYAEGSVNGFISTLGLVDDRCVVHPEAGDLANPPKKFRDCLFKVCPMNRYSAQKQYWKAKQAKQGNHTEAALLKKLQHAAELEQKQNESENKKLLGEIVKYSNVIQLLHIKSNKYLTVNKRLPALLEKNAMRVSLDAAGNEGSWFYIHPFWKLRSEGDNIVVGDKVVLMPVNAGQPLHASNIELLDNPGCKEVNAVNCNTSWKITLFMKYSSYREDVLKGGDVVRLFHAEQEKFLTCDEYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWNSLFRFKHLATGNYLAAELNPDYRDAQNEGKNVRDGVPPTSKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVPRNSYVRLRHLCTNTWVTSTSIPIDTDEERPVMLKIGTCQTKEDKEAFAIVSVPLSEVRDLDFANDANKVLATTVKKLENGTITQNERRFVTKLLEDLIFFVADVPNNGQEVLDVVITKPNRERQKLMREQNILAQVFGILKAPFKEKAGEGSMLRLEDLGDQRYAPYKYMLRLCYRVLRHSQQDYRKNQEYIAKNFCVMQSQIGYDILAEDTITALLHNNRKLLEKHITAKEIETFVSLLRRNREPRFLDYLSDLCVSNTTAIPVTQELICKFMLSPGNADILIQTKVVSMQADNPMESSILSDDIDDEEVWLYWIDSNKEPHGKAIRHLAQEAKEGTKADLEVLTYYRYQLNLFARMCLDRQYLAINQISTQLSVDLILRCVSDESLPFDLRASFCRLMLHMHVDRDPQESVVPVRYARLWTEIPTKITIHEYDSITDSSRNDMKRKFALTMEFVEEYLKEVVNQPFPFGDKEKNKLTFEVVHLARNLIYFGFYSFSELLRLTRTLLAILDIVQAPMSSYFERLSKFQDGGNNVMRTIHGVGEMMTQMVLSRGSIFPMSVPDVPPSIHPSKQGSPTEHEDVTVMDTKLKIIEILQFILSVRLDYRISYMLSIYKKEFGEDNDNAETSASGSPDTLLPSAIVPDIDEIAAQAETMFAGRKEKNPVQLDDEGGRTFLRVLIHLIMHDYPPLLSGALQLLFKHFSQRAEVLQAFKQVQLLVSNQDVDNYKQIKADLDQLRLTVEKSELWVEKSSNYENGEIGESQVKGGEEPIEESNILSPVQDGTKKPQIDSNKSNNYRIVKEILIRLSKLCVQNKKCRNQHQRLLKNMGAHSVVLDLLQIPYEKNDEKMNEVMNLAHTFLQNFCRGNPQNQVLLHKHLNLFLTPGLLEAETMRHIFMNNYHLCNEISERVVQHFVHCIETHGRHVEYLRFLQTIVKADGKYVKKCQDMVMTELINGGEDVLIFYNDRASFPILLHMMCSERDRGDESGPLAYHITLVELLAACTEGKNVYTEIKCNSLLPLDDIVRVVTHDDCIPEVKIAYVNFVNHCYVDTEVEMKEIYTSNHIWKLFENFLVDMARVCNTTTDRKHADIFLEKCVTESIMNIVSGFFNSPFSDNSTSLQTHQPVFIQLLQSAFRIYNCTWPNPAQKASVESCIRTLAEVAKNRGIAIPVDLDSQVNTLFMKSHSNMVQRAAMGWRLSARSGPRFKEALGGPAWDYRNIIEKLQDVVASLEHQFSPMMQAEFSVLVDVLYSPELLFPEGSDARIRCGAFMSKLINHTKKLMEKEEKLCIKILQTLREMLEKKDSFVEEGNTLRKILLNRYFKGDYSIGVNGHLSGAYSKTAQVGGSFSGQDSDKMGISMSDIQCLLDKEGASELVIDVIVNTKNDRIFSEGIFLGIALLEGGNTQTQYSFYQQLHEQKKSEKFFKVLYDRMKAAQKEIRSTVTVNTIDLGNKKRDDDNELMTSGPRMRVRDSTLHLKEGMKGQLTEASSATSKAYCVYRREMDPEIDIMCTGPEAGNTEEKSAEEVTMSPAIAIMQPILRFLQLLCENHNRELQNFLRNQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALVNQNLESLTEYCQGPCHENQTCIATHESNGIDIIIALILNDINPLGKYRMDLVLQLKNNASKLLLAIMESRHDSENAERILFNMRPRELVDVMKNAYNQGLECDHGDDEGGDDGVSPKDVGHNIYILAHQLARHNKLLQQMLKPGSDPDEGDEALKYYANHTAQIEIVRHDRTMEQIVFPVPNICEYLTRESKCRVFNTTERDEQGSKVNDFFQQTEDLYNEMKWQKKIRNNPALFWFSRHISLWGSISFNLAVFINLAVALFYPFGDDGDEGTLSPLFSVLLWIAVAICTSMLFFFSKPVGIRPFLVSIMLRSIYTIGLGPTLILLGAANLCNKIVFLVSFVGNRGTFTRGYRAVILDMAFLYHVAYVLVCMLGLFVHEFFYSFLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIIGFLFLKDDFTMEVDRLKNRTPVTGSHQVPTMTLTTMMEACAKENCSPTIPASNTADEEYEDGIERTCDTLLMCIVTVLNQGLRNGGGVGDVLRRPSKDEPLFAARVVYDLLFYFIVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVSFEEHIKSEHNMWHYLYFIVLVKVKDPTEYTGPESYVAQMIVEKNLDWFPRMRAMSLVSNEGDSEQNEIRSLQEKLESTMSLVKQLSGQLAELKEQMTEQRKNKQRLGFLGSNTPHVNHHMPPH	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 744).	0	.	.	.	.	.	.	.	.	.	.	"hsa04020: Calcium signaling pathway; hsa04022: cGMP-PKG signaling pathway; hsa04070: Phosphatidylinositol signaling system; hsa04114: Oocyte meiosis; hsa04210: Apoptosis; hsa04218: Cellular senescence; hsa04270: Vascular smooth muscle contraction; hsa04371: Apelin signaling pathway; hsa04540: Gap junction; hsa04611: Platelet activation; hsa04621: NOD-like receptor signaling pathway; hsa04625: C-type lectin receptor signaling pathway; hsa04720: Long-term potentiation; hsa04723: Retrograde endocannabinoid signaling; hsa04724: Glutamatergic synapse; hsa04725: Cholinergic synapse; hsa04726: Serotonergic synapse; hsa04728: Dopaminergic synapse; hsa04730: Long-term depression; hsa04750: Inflammatory mediator regulation of TRP channels; hsa04912: GnRH signaling pathway; hsa04915: Estrogen signaling pathway; hsa04918: Thyroid hormone synthesis; hsa04921: Oxytocin signaling pathway; hsa04922: Glucagon signaling pathway; hsa04924: Renin secretion; hsa04925: Aldosterone synthesis and secretion; hsa04927: Cortisol synthesis and secretion; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04929: GnRH secretion; hsa04934: Cushing syndrome; hsa04935: Growth hormone synthesis, secretion and action; hsa04970: Salivary secretion; hsa04971: Gastric acid secretion; hsa04972: Pancreatic secretion; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05017: Spinocerebellar ataxia; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05131: Shigellosis; hsa05163: Human cytomegalovirus infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05205: Proteoglycans in cancer"	R-HSA-112043: PLC beta mediated events; R-HSA-114508: Effects of PIP2 hydrolysis; R-HSA-139853: Elevation of cytosolic Ca2+ levels; R-HSA-1489509: DAG and IP3 signaling; R-HSA-2029485: Role of phospholipids in phagocytosis; R-HSA-2871809: FCERI mediated Ca+2 mobilization; R-HSA-381676: Glucagon-like Peptide-1 (GLP1) regulates insulin secretion; R-HSA-4086398: Ca2+ pathway; R-HSA-422356: Regulation of insulin secretion; R-HSA-5218921: VEGFR2 mediated cell proliferation; R-HSA-5578775: Ion homeostasis; R-HSA-5607763: CLEC7A (Dectin-1) induces NFAT activation; R-HSA-9664323: FCGR3A-mediated IL10 synthesis; R-HSA-983695: Antigen activates B Cell Receptor (BCR) leading to generation of second messengers	.	.
TTH1769	IP3 receptor isoform 3 (ITPR3)	Q14573	ITPR3_HUMAN	Ryanodine-inositol triphosphate calcium channel	"Type 3 inositol 1,4,5-trisphosphate receptor; Type 3 InsP3 receptor; InsP3R3; Inositol 1,4,5-trisphosphate receptor type 3; IP3R 3"	ITPR3	"Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium."	.	6DRC; 6DRA; 6DR2; 6DR0; 6DQZ	MSEMSSFLHIGDIVSLYAEGSVNGFISTLGLVDDRCVVEPAAGDLDNPPKKFRDCLFKVCPMNRYSAQKQYWKAKQTKQDKEKIADVVLLQKLQHAAQMEQKQNDTENKKVHGDVVKYGSVIQLLHMKSNKYLTVNKRLPALLEKNAMRVTLDATGNEGSWLFIQPFWKLRSNGDNVVVGDKVILNPVNAGQPLHASNYELSDNAGCKEVNSVNCNTSWKINLFMQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLYRFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQGRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRNSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEIRDLDFANDASSMLASAVEKLNEGFISQNDRRFVIQLLEDLVFFVSDVPNNGQNVLDIMVTKPNRERQKLMREQNILKQVFGILKAPFREKGGEGPLVRLEELSDQKNAPYQHMFRLCYRVLRHSQEDYRKNQEHIAKQFGMMQSQIGYDILAEDTITALLHNNRKLLEKHITKTEVETFVSLVRKNREPRFLDYLSDLCVSNHIAIPVTQELICKCVLDPKNSDILIRTELRPVKEMAQSHEYLSIEYSEEEVWLTWTDKNNEHHEKSVRQLAQEARAGNAHDENVLSYYRYQLKLFARMCLDRQYLAIDEISQQLGVDLIFLCMADEMLPFDLRASFCHLMLHVHVDRDPQELVTPVKFARLWTEIPTAITIKDYDSNLNASRDDKKNKFANTMEFVEDYLNNVVSEAVPFANEEKNKLTFEVVSLAHNLIYFGFYSFSELLRLTRTLLGIIDCVQGPPAMLQAYEDPGGKNVRRSIQGVGHMMSTMVLSRKQSVFSAPSLSAGASAAEPLDRSKFEENEDIVVMETKLKILEILQFILNVRLDYRISYLLSVFKKEFVEVFPMQDSGADGTAPAFDSTTANMNLDRIGEQAEAMFGVGKTSSMLEVDDEGGRMFLRVLIHLTMHDYAPLVSGALQLLFKHFSQRQEAMHTFKQVQLLISAQDVENYKVIKSELDRLRTMVEKSELWVDKKGSGKGEEVEAGAAKDKKERPTDEEGFLHPPGEKSSENYQIVKGILERLNKMCGVGEQMRKKQQRLLKNMDAHKVMLDLLQIPYDKGDAKMMEILRYTHQFLQKFCAGNPGNQALLHKHLHLFLTPGLLEAETMQHIFLNNYQLCSEISEPVLQHFVHLLATHGRHVQYLDFLHTVIKAEGKYVKKCQDMIMTELTNAGDDVVVFYNDKASLAHLLDMMKAARDGVEDHSPLMYHISLVDLLAACAEGKNVYTEIKCTSLLPLEDVVSVVTHEDCITEVKMAYVNFVNHCYVDTEVEMKEIYTSNHIWTLFENFTLDMARVCSKREKRVADPTLEKYVLSVVLDTINAFFSSPFSENSTSLQTHQTIVVQLLQSTTRLLECPWLQQQHKGSVEACIRTLAMVAKGRAILLPMDLDAHISSMLSSGASCAAAAQRNASSYKATTRAFPRVTPTANQWDYKNIIEKLQDIITALEERLKPLVQAELSVLVDVLHWPELLFLEGSEAYQRCESGGFLSKLIQHTKDLMESEEKLCIKVLRTLQQMLLKKTKYGDRGNQLRKMLLQNYLQNRKSTSRGDLPDPIGTGLDPDWSAIAATQCRLDKEGATKLVCDLITSTKNEKIFQESIGLAIHLLDGGNTEIQKSFHNLMMSDKKSERFFKVLHDRMKRAQQETKSTVAVNMNDLGSQPHEDREPVDPTTKGRVASFSIPGSSSRYSLGPSLRRGHEVSERVQSSEMGTSVLIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDIMCGSTTGGLGLLGLYINEDNVGLVIQTLETLTEYCQGPCHENQTCIVTHESNGIDIITALILNDISPLCKYRMDLVLQLKDNASKLLLALMESRHDSENAERILISLRPQELVDVIKKAYLQEEERENSEVSPREVGHNIYILALQLSRHNKQLQHLLKPVKRIQEEEAEGISSMLSLNNKQLSQMLKSSAPAQEEEEDPLAYYENHTSQIEIVRQDRSMEQIVFPVPGICQFLTEETKHRLFTTTEQDEQGSKVSDFFDQSSFLHNEMEWQRKLRSMPLIYWFSRRMTLWGSISFNLAVFINIIIAFFYPYMEGASTGVLDSPLISLLFWILICFSIAALFTKRYSIRPLIVALILRSIYYLGIGPTLNILGALNLTNKIVFVVSFVGNRGTFIRGYKAMVMDMEFLYHVGYILTSVLGLFAHELFYSILLFDLIYREETLFNVIKSVTRNGRSILLTALLALILVYLFSIVGFLFLKDDFILEVDRLPNNHSTASPLGMPHGAAAFVDTCSGDKMDCVSGLSVPEVLEEDRELDSTERACDTLLMCIVTVMNHGLRNGGGVGDILRKPSKDESLFPARVVYDLLFFFIVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVSFEEHIKLEHNMWNYLYFIVLVRVKNKTDYTGPESYVAQMIKNKNLDWFPRMRAMSLVSNEGEGEQNEIRILQDKLNSTMKLVSHLTAQLNELKEQMTEQRKRRQRLGFVDVQNCISR	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 745).	0	TC=1.A.3	.	InsP3 receptor family.	.	.	"Inositol 1,4,5-trisphosphate/ryanodine receptor; Ion transport protein; MIR domain; RyR and IP3R Homology associated; RIH domain"	PF08709; PF00520; PF02815; PF08454; PF01365	PF08709; Ins145_P3_rec; PF00520; Ion_trans; PF02815; MIR; PF08454; RIH_assoc; PF01365; RYDR_ITPR	.	.	"hsa04020: Calcium signaling pathway; hsa04022: cGMP-PKG signaling pathway; hsa04070: Phosphatidylinositol signaling system; hsa04114: Oocyte meiosis; hsa04210: Apoptosis; hsa04218: Cellular senescence; hsa04270: Vascular smooth muscle contraction; hsa04371: Apelin signaling pathway; hsa04540: Gap junction; hsa04611: Platelet activation; hsa04621: NOD-like receptor signaling pathway; hsa04625: C-type lectin receptor signaling pathway; hsa04713: Circadian entrainment; hsa04720: Long-term potentiation; hsa04723: Retrograde endocannabinoid signaling; hsa04724: Glutamatergic synapse; hsa04725: Cholinergic synapse; hsa04726: Serotonergic synapse; hsa04728: Dopaminergic synapse; hsa04730: Long-term depression; hsa04742: Taste transduction; hsa04750: Inflammatory mediator regulation of TRP channels; hsa04911: Insulin secretion; hsa04912: GnRH signaling pathway; hsa04915: Estrogen signaling pathway; hsa04918: Thyroid hormone synthesis; hsa04921: Oxytocin signaling pathway; hsa04922: Glucagon signaling pathway; hsa04924: Renin secretion; hsa04925: Aldosterone synthesis and secretion; hsa04927: Cortisol synthesis and secretion; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04929: GnRH secretion; hsa04934: Cushing syndrome; hsa04935: Growth hormone synthesis, secretion and action; hsa04970: Salivary secretion; hsa04971: Gastric acid secretion; hsa04972: Pancreatic secretion; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05014: Amyotrophic lateral sclerosis; hsa05017: Spinocerebellar ataxia; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05131: Shigellosis; hsa05163: Human cytomegalovirus infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05205: Proteoglycans in cancer"	"R-HSA-112043: PLC beta mediated events; R-HSA-114508: Effects of PIP2 hydrolysis; R-HSA-139853: Elevation of cytosolic Ca2+ levels; R-HSA-1489509: DAG and IP3 signaling; R-HSA-2029485: Role of phospholipids in phagocytosis; R-HSA-2871809: FCERI mediated Ca+2 mobilization; R-HSA-381676: Glucagon-like Peptide-1 (GLP1) regulates insulin secretion; R-HSA-4086398: Ca2+ pathway; R-HSA-422356: Regulation of insulin secretion; R-HSA-5218921: VEGFR2 mediated cell proliferation; R-HSA-5578775: Ion homeostasis; R-HSA-5607763: CLEC7A (Dectin-1) induces NFAT activation; R-HSA-9664323: FCGR3A-mediated IL10 synthesis; R-HSA-9717207: Sensory perception of sweet, bitter, and umami (glutamate) taste; R-HSA-983695: Antigen activates B Cell Receptor (BCR) leading to generation of second messengers"	.	Q14573
TTOJY1B	Jagged2 messenger RNA (JAG2 mRNA)	Q9Y219	JAG2_HUMAN	mRNA target	hJ2 (mRNA); Protein jagged-2 (mRNA); Jagged2 (mRNA)	JAG2	Involved in limb development. Putative Notch ligand involved in the mediation of Notch signaling.	.	5MWF; 5MW7; 5MW5	MRAQGRGRLPRRLLLLLALWVQAARPMGYFELQLSALRNVNGELLSGACCDGDGRTTRAGGCGHDECDTYVRVCLKEYQAKVTPTGPCSYGHGATPVLGGNSFYLPPAGAAGDRARARARAGGDQDPGLVVIPFQFAWPRSFTLIVEAWDWDNDTTPNEELLIERVSHAGMINPEDRWKSLHFSGHVAHLELQIRVRCDENYYSATCNKFCRPRNDFFGHYTCDQYGNKACMDGWMGKECKEAVCKQGCNLLHGGCTVPGECRCSYGWQGRFCDECVPYPGCVHGSCVEPWQCNCETNWGGLLCDKDLNYCGSHHPCTNGGTCINAEPDQYRCTCPDGYSGRNCEKAEHACTSNPCANGGSCHEVPSGFECHCPSGWSGPTCALDIDECASNPCAAGGTCVDQVDGFECICPEQWVGATCQLDANECEGKPCLNAFSCKNLIGGYYCDCIPGWKGINCHINVNDCRGQCQHGGTCKDLVNGYQCVCPRGFGGRHCELERDECASSPCHSGGLCEDLADGFHCHCPQGFSGPLCEVDVDLCEPSPCRNGARCYNLEGDYYCACPDDFGGKNCSVPREPCPGGACRVIDGCGSDAGPGMPGTAASGVCGPHGRCVSQPGGNFSCICDSGFTGTYCHENIDDCLGQPCRNGGTCIDEVDAFRCFCPSGWEGELCDTNPNDCLPDPCHSRGRCYDLVNDFYCACDDGWKGKTCHSREFQCDAYTCSNGGTCYDSGDTFRCACPPGWKGSTCAVAKNSSCLPNPCVNGGTCVGSGASFSCICRDGWEGRTCTHNTNDCNPLPCYNGGICVDGVNWFRCECAPGFAGPDCRINIDECQSSPCAYGATCVDEINGYRCSCPPGRAGPRCQEVIGFGRSCWSRGTPFPHGSSWVEDCNSCRCLDGRRDCSKVWCGWKPCLLAGQPEALSAQCPLGQRCLEKAPGQCLRPPCEAWGECGAEEPPSTPCLPRSGHLDNNCARLTLHFNRDHVPQGTTVGAICSGIRSLPATRAVARDRLLVLLCDRASSGASAVEVAVSFSPARDLPDSSLIQGAAHAIVAAITQRGNSSLLLAVTEVKVETVVTGGSSTGLLVPVLCGAFSVLWLACVVLCVWWTRKRRKERERSRLPREESANNQWAPLNPIRNPIERPGGHKDVLYQCKNFTPPPRRADEALPGPAGHAAVREDEEDEDLGRGEEDSLEAEKFLSHKFTKDPGRSPGRPAHWASGPKVDNRAVRSINEARYAGKE	Literature-reported	"US patent application no. 7,425,545, Modulation of C-reactive protein expression."	0	mRNA	mRNA target	.	.	.	Delta serrate ligand; EGF-like domain; Calcium-binding EGF domain; Human growth factor-like EGF; N terminus of Notch ligand	PF01414; PF00008; PF07645; PF12661; PF07657	PF01414; DSL; PF00008; EGF; PF07645; EGF_CA; PF12661; hEGF; PF07657; MNNL	.	.	hsa04330:Notch signaling pathway	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	.	Q9Y219
TTUBIOW	Jagged-2 protein (JAG2)	Q9Y219	JAG2_HUMAN	.	hJ2; Protein jagged-2; Jagged2	JAG2	Involved in limb development. Putative Notch ligand involved in the mediation of Notch signaling.	.	5MWF; 5MW7; 5MW5	MRAQGRGRLPRRLLLLLALWVQAARPMGYFELQLSALRNVNGELLSGACCDGDGRTTRAGGCGHDECDTYVRVCLKEYQAKVTPTGPCSYGHGATPVLGGNSFYLPPAGAAGDRARARARAGGDQDPGLVVIPFQFAWPRSFTLIVEAWDWDNDTTPNEELLIERVSHAGMINPEDRWKSLHFSGHVAHLELQIRVRCDENYYSATCNKFCRPRNDFFGHYTCDQYGNKACMDGWMGKECKEAVCKQGCNLLHGGCTVPGECRCSYGWQGRFCDECVPYPGCVHGSCVEPWQCNCETNWGGLLCDKDLNYCGSHHPCTNGGTCINAEPDQYRCTCPDGYSGRNCEKAEHACTSNPCANGGSCHEVPSGFECHCPSGWSGPTCALDIDECASNPCAAGGTCVDQVDGFECICPEQWVGATCQLDANECEGKPCLNAFSCKNLIGGYYCDCIPGWKGINCHINVNDCRGQCQHGGTCKDLVNGYQCVCPRGFGGRHCELERDECASSPCHSGGLCEDLADGFHCHCPQGFSGPLCEVDVDLCEPSPCRNGARCYNLEGDYYCACPDDFGGKNCSVPREPCPGGACRVIDGCGSDAGPGMPGTAASGVCGPHGRCVSQPGGNFSCICDSGFTGTYCHENIDDCLGQPCRNGGTCIDEVDAFRCFCPSGWEGELCDTNPNDCLPDPCHSRGRCYDLVNDFYCACDDGWKGKTCHSREFQCDAYTCSNGGTCYDSGDTFRCACPPGWKGSTCAVAKNSSCLPNPCVNGGTCVGSGASFSCICRDGWEGRTCTHNTNDCNPLPCYNGGICVDGVNWFRCECAPGFAGPDCRINIDECQSSPCAYGATCVDEINGYRCSCPPGRAGPRCQEVIGFGRSCWSRGTPFPHGSSWVEDCNSCRCLDGRRDCSKVWCGWKPCLLAGQPEALSAQCPLGQRCLEKAPGQCLRPPCEAWGECGAEEPPSTPCLPRSGHLDNNCARLTLHFNRDHVPQGTTVGAICSGIRSLPATRAVARDRLLVLLCDRASSGASAVEVAVSFSPARDLPDSSLIQGAAHAIVAAITQRGNSSLLLAVTEVKVETVVTGGSSTGLLVPVLCGAFSVLWLACVVLCVWWTRKRRKERERSRLPREESANNQWAPLNPIRNPIERPGGHKDVLYQCKNFTPPPRRADEALPGPAGHAAVREDEEDEDLGRGEEDSLEAEKFLSHKFTKDPGRSPGRPAHWASGPKVDNRAVRSINEARYAGKE	Literature-reported	A microRNA-1280/JAG2 network comprises a novel biological target in high-risk medulloblastoma. Oncotarget. 2015 Feb 20;6(5):2709-24.	.	.	.	.	.	.	Delta serrate ligand; EGF-like domain; Calcium-binding EGF domain; Human growth factor-like EGF; N terminus of Notch ligand	PF01414; PF00008; PF07645; PF12661; PF07657	PF01414; DSL; PF00008; EGF; PF07645; EGF_CA; PF12661; hEGF; PF07657; MNNL	.	.	hsa01522: Endocrine resistance; hsa04330: Notch signaling pathway; hsa04658: Th1 and Th2 cell differentiation; hsa05200: Pathways in cancer; hsa05224: Breast cancer	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-9013507: NOTCH3 Activation and Transmission of Signal to the Nucleus	.	Q9Y219
TT6DM01	Janus kinase 1 (JAK-1)	P23458	JAK1_HUMAN	Kinase	Tyrosine-protein kinase JAK1; JAK1B; JAK1A	JAK1	"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."	EC 2.7.10.2	6N7D; 6N7C; 6N7B; 6N7A; 6N79	MQYLNIKEDCNAMAFCAKMRSSKKTEVNLEAPEPGVEVIFYLSDREPLRLGSGEYTAEELCIRAAQACRISPLCHNLFALYDENTKLWYAPNRTITVDDKMSLRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKKIPDATPLLDASSLEYLFAQGQYDLVKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETLTKHYGAEIFETSMLLISSENEMNWFHSNDGGNVLYYEVMVTGNLGIQWRHKPNVVSVEKEKNKLKRKKLENKHKKDEEKNKIREEWNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTDVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEQVQGAQKQFKNFQIEVQKGRYSLHGSDRSFPSLGDLMSHLKKQILRTDNISFMLKRCCQPKPREISNLLVATKKAQEWQPVYPMSQLSFDRILKKDLVQGEHLGRGTRTHIYSGTLMDYKDDEGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECGPFIKLSDPGIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDIVSEKKPATEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK	Successful	2011 FDA drug approvals. Nat Rev Drug Discov. 2012 Feb 1;11(2):91-4.	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. JAK subfamily.	2.7.10.2 	Transferring phosphorus-containing groups	FERM F1 ubiquitin-like domain; FERM F2 acyl-CoA binding protein-like domain; Jak1 pleckstrin homology-like domain; Protein tyrosine kinase	PF18379; PF18377; PF17887; PF07714	PF18379; FERM_F1; PF18377; FERM_F2; PF17887; Jak1_Phl; PF07714; Pkinase_Tyr	.	.	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	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	.	P23458
TTWKB01	HUMAN janus kinase 1 (JAK-1)	P23458	JAK1_HUMAN	Kinase	Tyrosine-protein kinase JAK1; JAK1B; JAK1A	JAK1	"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."	EC 2.7.10.2	6N7D; 6N7C; 6N7B; 6N7A; 6N79	MQYLNIKEDCNAMAFCAKMRSSKKTEVNLEAPEPGVEVIFYLSDREPLRLGSGEYTAEELCIRAAQACRISPLCHNLFALYDENTKLWYAPNRTITVDDKMSLRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKKIPDATPLLDASSLEYLFAQGQYDLVKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETLTKHYGAEIFETSMLLISSENEMNWFHSNDGGNVLYYEVMVTGNLGIQWRHKPNVVSVEKEKNKLKRKKLENKHKKDEEKNKIREEWNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTDVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEQVQGAQKQFKNFQIEVQKGRYSLHGSDRSFPSLGDLMSHLKKQILRTDNISFMLKRCCQPKPREISNLLVATKKAQEWQPVYPMSQLSFDRILKKDLVQGEHLGRGTRTHIYSGTLMDYKDDEGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECGPFIKLSDPGIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDIVSEKKPATEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK	.	The Use of Anti-Inflammatory Drugs in the Treatment of People With Severe Coronavirus Disease 2019 (COVID-19): The Perspectives of Clinical Immunologists From China. Clin Immunol. 2020 May;214:108393.	.	.	.	.	.	.	.	.	.	.	.	hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa04151: PI3K-Akt signaling pathway; hsa04217: Necroptosis; hsa04380: Osteoclast differentiation; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04621: NOD-like receptor signaling pathway; hsa04630: JAK-STAT signaling pathway; hsa04658: Th1 and Th2 cell differentiation; hsa04659: Th17 cell differentiation; hsa05140: Leishmaniasis; hsa05145: Toxoplasmosis; hsa05152: Tuberculosis; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05162: Measles; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; hsa05165: Human papillomavirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05203: Viral carcinogenesis; hsa05212: Pancreatic cancer; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer	R-HSA-1059683: Interleukin-6 signaling; R-HSA-110056: MAPK3 (ERK1) activation; R-HSA-112411: MAPK1 (ERK2) activation; R-HSA-1169408: ISG15 antiviral mechanism; R-HSA-1266695: Interleukin-7 signaling; R-HSA-449836: Other interleukin signaling; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6783783: Interleukin-10 signaling; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6788467: IL-6-type cytokine receptor ligand interactions; R-HSA-877300: Interferon gamma signaling; R-HSA-877312: Regulation of IFNG signaling; R-HSA-8854691: Interleukin-20 family signaling; R-HSA-8983432: Interleukin-15 signaling; R-HSA-8984722: Interleukin-35 Signalling; R-HSA-8985947: Interleukin-9 signaling; R-HSA-9020558: Interleukin-2 signaling; R-HSA-9020591: Interleukin-12 signaling; R-HSA-9020956: Interleukin-27 signaling; R-HSA-9020958: Interleukin-21 signaling; R-HSA-909733: Interferon alpha/beta signaling; R-HSA-912526: Interleukin receptor SHC signaling; R-HSA-912694: Regulation of IFNA/IFNB signaling; R-HSA-9674555: Signaling by CSF3 (G-CSF); R-HSA-9679191: Potential therapeutics for SARS; R-HSA-9705462: Inactivation of CSF3 (G-CSF) signaling; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses	.	P23458
TTRMX3V	Janus kinase 2 (JAK-2)	O60674	JAK2_HUMAN	Kinase	Tyrosine-protein kinase JAK2	JAK2	"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."	EC 2.7.10.2	6M9H; 6E2Q; 6E2P; 6DRW; 6BSS	MGMACLTMTEMEGTSTSSIYQNGDISGNANSMKQIDPVLQVYLYHSLGKSEADYLTFPSGEYVAEEICIAASKACGITPVYHNMFALMSETERIWYPPNHVFHIDESTRHNVLYRIRFYFPRWYCSGSNRAYRHGISRGAEAPLLDDFVMSYLFAQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKENDQTPLAIYNSISYKTFLPKCIRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEKFEVKEPGSGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDLQLYCDFPNIIDVSIKQANQEGSNESRVVTIHKQDGKNLEIELSSLREALSFVSLIDGYYRLTADAHHYLCKEVAPPAVLENIQSNCHGPISMDFAISKLKKAGNQTGLYVLRCSPKDFNKYFLTFAVERENVIEYKHCLITKNENEEYNLSGTKKNFSSLKDLLNCYQMETVRSDNIIFQFTKCCPPKPKDKSNLLVFRTNGVSDVPTSPTLQRPTHMNQMVFHKIRNEDLIFNESLGQGTFTKIFKGVRREVGDYGQLHETEVLLKVLDKAHRNYSESFFEAASMMSKLSHKHLVLNYGVCVCGDENILVQEFVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEENTLIHGNVCAKNILLIREEDRKTGNPPFIKLSDPGISITVLPKDILQERIPWVPPECIENPKNLNLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPKWAELANLINNCMDYEPDFRPSFRAIIRDLNSLFTPDYELLTENDMLPNMRIGALGFSGAFEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAG	Successful	2011 FDA drug approvals. Nat Rev Drug Discov. 2012 Feb 1;11(2):91-4.	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. JAK subfamily.	2.7.10.2 	Transferring phosphorus-containing groups	FERM F1 ubiquitin-like domain; FERM F2 acyl-CoA binding protein-like domain; Jak1 pleckstrin homology-like domain; Protein tyrosine kinase; SH2 domain	PF18379; PF18377; PF17887; PF07714; PF00017	PF18379; FERM_F1; PF18377; FERM_F2; PF17887; Jak1_Phl; PF07714; Pkinase_Tyr; PF00017; SH2	.	.	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	"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"	.	O60674
TT0F5HE	HUMAN janus kinase 2 (JAK-2)	O60674	JAK2_HUMAN	Kinase	Tyrosine-protein kinase JAK2	JAK2	"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."	EC 2.7.10.2	6M9H; 6E2Q; 6E2P; 6DRW; 6BSS	MGMACLTMTEMEGTSTSSIYQNGDISGNANSMKQIDPVLQVYLYHSLGKSEADYLTFPSGEYVAEEICIAASKACGITPVYHNMFALMSETERIWYPPNHVFHIDESTRHNVLYRIRFYFPRWYCSGSNRAYRHGISRGAEAPLLDDFVMSYLFAQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKENDQTPLAIYNSISYKTFLPKCIRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEKFEVKEPGSGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDLQLYCDFPNIIDVSIKQANQEGSNESRVVTIHKQDGKNLEIELSSLREALSFVSLIDGYYRLTADAHHYLCKEVAPPAVLENIQSNCHGPISMDFAISKLKKAGNQTGLYVLRCSPKDFNKYFLTFAVERENVIEYKHCLITKNENEEYNLSGTKKNFSSLKDLLNCYQMETVRSDNIIFQFTKCCPPKPKDKSNLLVFRTNGVSDVPTSPTLQRPTHMNQMVFHKIRNEDLIFNESLGQGTFTKIFKGVRREVGDYGQLHETEVLLKVLDKAHRNYSESFFEAASMMSKLSHKHLVLNYGVCVCGDENILVQEFVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEENTLIHGNVCAKNILLIREEDRKTGNPPFIKLSDPGISITVLPKDILQERIPWVPPECIENPKNLNLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPKWAELANLINNCMDYEPDFRPSFRAIIRDLNSLFTPDYELLTENDMLPNMRIGALGFSGAFEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAG	.	TH17 responses in cytokine storm of COVID-19: An emerging target of JAK2 inhibitor Fedratinib. J Microbiol Immunol Infect. 2020 Mar 11. pii: S1684-1182(20)30065-7.	.	.	.	.	.	.	.	.	.	.	.	"hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa04062: Chemokine signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04217: Necroptosis; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04630: JAK-STAT signaling pathway; hsa04658: Th1 and Th2 cell differentiation; hsa04659: Th17 cell differentiation; hsa04725: Cholinergic synapse; hsa04917: Prolactin signaling pathway; hsa04920: Adipocytokine signaling pathway; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04935: Growth hormone synthesis, secretion and action; hsa05140: Leishmaniasis; hsa05145: Toxoplasmosis; hsa05152: Tuberculosis; hsa05161: Hepatitis B; hsa05164: Influenza A; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05200: Pathways in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer; hsa05417: Lipid and atherosclerosis"	"R-HSA-1059683: Interleukin-6 signaling; R-HSA-110056: MAPK3 (ERK1) activation; R-HSA-112411: MAPK1 (ERK2) activation; R-HSA-1170546: Prolactin receptor signaling; R-HSA-1433557: Signaling by SCF-KIT; R-HSA-2586552: Signaling by Leptin; R-HSA-3214858: RMTs methylate histone arginines; R-HSA-512988: Interleukin-3, Interleukin-5 and GM-CSF signaling; R-HSA-5673000: RAF activation; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6788467: IL-6-type cytokine receptor ligand interactions; R-HSA-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-69231: Cyclin D associated events in G1; R-HSA-877300: Interferon gamma signaling; R-HSA-877312: Regulation of IFNG signaling; R-HSA-8854691: Interleukin-20 family signaling; R-HSA-8984722: Interleukin-35 Signalling; R-HSA-9006335: Signaling by Erythropoietin; R-HSA-9020591: Interleukin-12 signaling; R-HSA-9020933: Interleukin-23 signaling; R-HSA-9020956: Interleukin-27 signaling; R-HSA-9027276: Erythropoietin activates Phosphoinositide-3-kinase (PI3K); R-HSA-9027277: Erythropoietin activates Phospholipase C gamma (PLCG); R-HSA-9027283: Erythropoietin activates STAT5; R-HSA-9027284: Erythropoietin activates RAS; R-HSA-912526: Interleukin receptor SHC signaling; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants; R-HSA-9670439: Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants; R-HSA-9674555: Signaling by CSF3 (G-CSF); R-HSA-9679191: Potential therapeutics for SARS; R-HSA-9705462: Inactivation of CSF3 (G-CSF) signaling; R-HSA-982772: Growth hormone receptor signaling; R-HSA-983231: Factors involved in megakaryocyte development and platelet production"	.	O60674
TTT7PJU	Janus kinase 3 (JAK-3)	P52333	JAK3_HUMAN	Kinase	Tyrosine-protein kinase JAK3; Leukocyte janus kinase; L-JAK	JAK3	"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."	EC 2.7.10.2	6NY4; 6GLB; 6GLA; 6GL9; 6DUD	MAPPSEETPLIPQRSCSLLSTEAGALHVLLPARGPGPPQRLSFSFGDHLAEDLCVQAAKASGILPVYHSLFALATEDLSCWFPPSHIFSVEDASTQVLLYRIRFYFPNWFGLEKCHRFGLRKDLASAILDLPVLEHLFAQHRSDLVSGRLPVGLSLKEQGECLSLAVLDLARMAREQAQRPGELLKTVSYKACLPPSLRDLIQGLSFVTRRRIRRTVRRALRRVAACQADRHSLMAKYIMDLERLDPAGAAETFHVGLPGALGGHDGLGLLRVAGDGGIAWTQGEQEVLQPFCDFPEIVDISIKQAPRVGPAGEHRLVTVTRTDNQILEAEFPGLPEALSFVALVDGYFRLTTDSQHFFCKEVAPPRLLEEVAEQCHGPITLDFAINKLKTGGSRPGSYVLRRSPQDFDSFLLTVCVQNPLGPDYKGCLIRRSPTGTFLLVGLSRPHSSLRELLATCWDGGLHVDGVAVTLTSCCIPRPKEKSNLIVVQRGHSPPTSSLVQPQSQYQLSQMTFHKIPADSLEWHENLGHGSFTKIYRGCRHEVVDGEARKTEVLLKVMDAKHKNCMESFLEAASLMSQVSYRHLVLLHGVCMAGDSTMVQEFVHLGAIDMYLRKRGHLVPASWKLQVVKQLAYALNYLEDKGLPHGNVSARKVLLAREGADGSPPFIKLSDPGVSPAVLSLEMLTDRIPWVAPECLREAQTLSLEADKWGFGATVWEVFSGVTMPISALDPAKKLQFYEDRQQLPAPKWTELALLIQQCMAYEPVQRPSFRAVIRDLNSLISSDYELLSDPTPGALAPRDGLWNGAQLYACQDPTIFEERHLKYISQLGKGNFGSVELCRYDPLGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRQSLRLVMEYLPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKSCSPSAEFLRMMGCERDVPALCRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDMLWSGSRGCETHAFTAHPEGKHHSLSFS	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. 2015	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. JAK subfamily.	2.7.10.2	Transferring phosphorus-containing groups	FERM F1 ubiquitin-like domain; FERM F2 acyl-CoA binding protein-like domain; Jak1 pleckstrin homology-like domain; Protein tyrosine kinase	PF18379; PF18377; PF17887; PF07714	PF18379; FERM_F1; PF18377; FERM_F2; PF17887; Jak1_Phl; PF07714; Pkinase_Tyr	.	.	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	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	.	P52333
TTBISK4	Jumonji domain-containing protein 1C (JMJD1C)	Q15652	JHD2C_HUMAN	.	Thyroid receptor-interacting protein 8; TRIP8; TRIP-8; TR-interacting protein 8; Probable JmjC domain-containing histone demethylation protein 2C; KIAA1380; JHDM2C	JMJD1C	"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)."	EC 1.14.11.-	5FZO; 2YPD	MAVETRAELVGKRFLCVAVGDEARSERWESGRGWRSWRAGVIRAVSHRDSRNPDLAVYVEFDDLEWDKREWVKVYEDFSTFLVEYHLIWAKRNDPSQTQGSKSKQIQWPALTFKPLVERNIPSSVTAVEFLVDKQLDFLTEDSAFQPYQDDIDSLNPVLRDNPQLHEEVKVWVKEQKVQEIFMQGPYSLNGYRVRVYRQDSATQWFTGIITHHDLFTRTMIVMNDQVLEPQNVDPSMVQMTFLDDVVHSLLKGENIGITSRRRSRANQNVNAVHSHYTRAQANSPRPAMNSQAAVPKQNTHQQQQQRSIRPNKRKGSDSSIPDEEKMKEEKYDYISRGENPKGKNKHLMNKRRKPEEDEKKLNMKRLRTDNVSDFSESSDSENSNKRIIDNSSEQKPENELKNKNTSKINGEEGKPHNNEKAGEETLKNSQPPWDQIQEDKKHEEAEKRKSVDTQLQEDMIIHSSEQSTVSDHNSNDLLPQECNMDKTHTMELLPKEKFVSRPPTPKCVIDITNDTNLEKVAQENSSTFGLQTLQKMDPNVSDSKHSIANAKFLETAKKDSDQSWVSDVVKVDLTQSSVTNASSGNDHLNMEKEKYVSYISPLSAVSVMEDKLHKRSPPPETIKSKLNTSVDTHKIKSSPSPEVVKPKITHSPDSVKSKATYVNSQATGERRLANKIEHELSRCSFHPIPTRSSTLETTKSPLIIDKNEHFTVYRDPALIGSETGANHISPFLSQHPFPLHSSSHRTCLNPGTHHPALTPAPHLLAGSSSQTPLPTINTHPLTSGPHHAVHHPHLLPTVLPGVPTASLLGGHPRLESAHASSLSHLALAHQQQQQLLQHQSPHLLGQAHPSASYNQLGLYPIIWQYPNGTHAYSGLGLPSSKWVHPENAVNAEASLRRNSPSPWLHQPTPVTSADGIGLLSHIPVRPSSAEPHRPLKITAHSSPPLTKTLVDHHKEELERKAFMEPLRSVASTSAKNDLDLNRSQTGKDCHLHRHFVDPVLNQLQRPPQETGERLNKYKEEHRRILQESIDVAPFTTKIKGLEGERENYSRVASSSSSPKSHIIKQDMDVERSVSDLYKMKHSVPQSLPQSNYFTTLSNSVVNEPPRSYPSKEVSNIYGDKQSNALAAAAANPQTLTSFITSLSKPPPLIKHQPESEGLVGKIPEHLPHQIASHSVTTFRNDCRSPTHLTVSSTNTLRSMPALHRAPVFHPPIHHSLERKEGSYSSLSPPTLTPVMPVNAGGKVQESQKPPTLIPEPKDSQANFKSSSEQSLTEMWRPNNNLSKEKTEWHVEKSSGKLQAAMASVIVRPSSSTKTDSMPAMQLASKDRVSERSSAGAHKTDCLKLAEAGETGRIILPNVNSDSVHTKSEKNFQAVSQGSVPSSVMSAVNTMCNTKTDVITSAADTTSVSSWGGSEVISSLSNTILASTSSECVSSKSVSQPVAQKQECKVSTTAPVTLASSKTGSVVQPSSGFSGTTDFIHLKKHKAALAAAQYKSSNASETEPNAIKNQTLSASLPLDSTVICSTINKANSVGNGQASQTSQPNYHTKLKKAWLTRHSEEDKNTNKMENSGNSVSEIIKPCSVNLIASTSSDIQNSVDSKIIVDKYVKDDKVNRRKAKRTYESGSESGDSDESESKSEQRTKRQPKPTYKKKQNDLQKRKGEIEEDLKPNGVLSRSAKERSKLKLQSNSNTGIPRSVLKDWRKVKKLKQTGESFLQDDSCCEIGPNLQKCRECRLIRSKKGEEPAHSPVFCRFYYFRRLSFSKNGVVRIDGFSSPDQYDDEAMSLWTHENFEDDELDIETSKYILDIIGDKFCQLVTSEKTALSWVKKDAKIAWKRAVRGVREMCDACEATLFNIHWVCQKCGFVVCLDCYKAKERKSSRDKELYAWMKCVKGQPHDHKHLMPTQIIPGSVLTDLLDAMHTLREKYGIKSHCHCTNKQNLQVGNFPTMNGVSQVLQNVLNHSNKISLCMPESQQQNTPPKSEKNGGSSPESDVGTDNKLTPPESQSPLHWLADLAEQKAREEKKENKELTLENQIKEEREQDNSESPNGRTSPLVSQNNEQGSTLRDLLTTTAGKLRVGSTDAGIAFAPVYSMGAPSSKSGRTMPNILDDIIASVVENKIPPSKTSKINVKPELKEEPEESIISAVDENNKLYSDIPHSWICEKHILWLKDYKNSSNWKLFKECWKQGQPAVVSGVHKKMNISLWKAESISLDFGDHQADLLNCKDSIISNANVKEFWDGFEEVSKRQKNKSGETVVLKLKDWPSGEDFKTMMPARYEDLLKSLPLPEYCNPEGKFNLASHLPGFFVRPDLGPRLCSAYGVVAAKDHDIGTTNLHIEVSDVVNILVYVGIAKGNGILSKAGILKKFEEEDLDDILRKRLKDSSEIPGALWHIYAGKDVDKIREFLQKISKEQGLEVLPEHDPIRDQSWYVNKKLRQRLLEEYGVRTCTLIQFLGDAIVLPAGALHQVQNFHSCIQVTEDFVSPEHLVESFHLTQELRLLKEEINYDDKLQVKNILYHAVKEMVRALKIHEDEVEDMEEN	Literature-reported	Cooperative demethylation by JMJD2C and LSD1 promotes androgen receptor-dependent gene expression. Nat Cell Biol. 2007 Mar;9(3):347-53.	.	.	.	.	.	.	.	.	.	.	.	hsa05202: Transcriptional misregulation in cancer	R-HSA-983231: Factors involved in megakaryocyte development and platelet production	MetaCyc:ENSG00000171988-MON	Q15652
TTS7IR5	c-Jun messenger RNA (c-Jun mRNA)	P05412	JUN_HUMAN	mRNA target	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)	JUN	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'.	.	5T01; 5FV8; 1T2K; 1S9K; 1JNM	MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF	Literature-reported	"US patent application no. 6,312,900, Antisense oligonucleotide compositions and methods for the modulation of activating protein 1."	0	mRNA	mRNA target	.	.	.	bZIP transcription factor; Jun-like transcription factor	PF00170; PF03957	PF00170; bZIP_1; PF03957; Jun	.	.	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	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	.	P05412
TTN3GBV	Transcription factor AP-1 (JUN)	P05412	JUN_HUMAN	Basic leucine zipper bZIP	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	JUN	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'.	.	5T01; 5FV8; 1T2K; 1S9K; 1JNM	MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF	Discontinued	CenterWatch. Drugs in Clinical Trials Database. CenterWatch. 2008.	5	bZIP	.	bZIP family. Jun subfamily.	.	.	bZIP transcription factor; Jun-like transcription factor	PF00170; PF03957	PF00170; bZIP_1; PF03957; Jun	.	.	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	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	.	P05412
TTREN0G	Junction plakoglobin (JUP)	P14923	PLAK_HUMAN	Beta-catenin	Plakoglobin; Desmoplakin-3; Desmoplakin III; DP3; Catenin gamma; CTNNG	JUP	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.	.	3IFQ	MEVMNLMEQPIKVTEWQQTYTYDSGIHSGANTCVPSVSSKGIMEEDEACGRQYTLKKTTTYTQGVPPSQGDLEYQMSTTARAKRVREAMCPGVSGEDSSLLLATQVEGQATNLQRLAEPSQLLKSAIVHLINYQDDAELATRALPELTKLLNDEDPVVVTKAAMIVNQLSKKEASRRALMGSPQLVAAVVRTMQNTSDLDTARCTTSILHNLSHHREGLLAIFKSGGIPALVRMLSSPVESVLFYAITTLHNLLLYQEGAKMAVRLADGLQKMVPLLNKNNPKFLAITTDCLQLLAYGNQESKLIILANGGPQALVQIMRNYSYEKLLWTTSRVLKVLSVCPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSDVATKQEGLESVLKILVNQLSVDDVNVLTCATGTLSNLTCNNSKNKTLVTQNSGVEALIHAILRAGDKDDITEPAVCALRHLTSRHPEAEMAQNSVRLNYGIPAIVKLLNQPNQWPLVKATIGLIRNLALCPANHAPLQEAAVIPRLVQLLVKAHQDAQRHVAAGTQQPYTDGVRMEEIVEGCTGALHILARDPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELAQDKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNPDYRKRVSVELTNSLFKHDPAAWEAAQSMIPINEPYGDDMDATYRPMYSSDVPLDPLEMHMDMDGDYPIDTYSDGLRPPYPTADHMLA	Literature-reported	Plakoglobin is a new target gene of histone deacetylase in human fibrosarcoma HT1080 cells. Oncogene. 2004 Mar 4;23(9):1704-11.	.	Beta-catenin	.	beta-catenin family.	.	.	Armadillo/beta-catenin-like repeat	PF00514	PF00514; Arm	.	.	hsa05200: Pathways in cancer; hsa05202: Transcriptional misregulation in cancer; hsa05221: Acute myeloid leukemia; hsa05226: Gastric cancer; hsa05412: Arrhythmogenic right ventricular cardiomyopathy	R-HSA-418990: Adherens junctions interactions; R-HSA-5218920: VEGFR2 mediated vascular permeability; R-HSA-6798695: Neutrophil degranulation; R-HSA-6805567: Keratinization; R-HSA-6809371: Formation of the cornified envelope; R-HSA-8980692: RHOA GTPase cycle; R-HSA-9013026: RHOB GTPase cycle; R-HSA-9013106: RHOC GTPase cycle; R-HSA-9013148: CDC42 GTPase cycle; R-HSA-9013406: RHOQ GTPase cycle; R-HSA-9013407: RHOH GTPase cycle; R-HSA-9013409: RHOJ GTPase cycle	.	P14923
TTLWKP4	Kidney associated antigen 1 (KAAG1)	Q9UBP8	KAAG1_HUMAN	.	RU2AS; RU2 antisense gene protein; Kidney-associated antigen 1	KAAG1	Invovled in immune response.	.	.	MDDDAAPRVEGVPVAVHKHALHDGLRQVAGPGAAAAHLPRWPPPQLAASRREAPPLSQRPHRTQGAGSPPETNEKLTNPQVKEK	Literature-reported	Strong genetic evidence of DCDC2 as a susceptibility gene for dyslexia. Am J Hum Genet. 2006 Jan;78(1):52-62.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9UBP8
TTVK7SB	Histone acetyltransferase KAT2B (KAT2B)	Q92831	KAT2B_HUMAN	Acyltransferase	Spermidine acetyltransferase KAT2B; PCAF; P300/CBP-associated factor; P/CAF; Lysine acetyltransferase 2B; Histone acetyltransferase PCAF; Histone acetylase PCAF	KAT2B	"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."	EC 2.3.1.48	6J3O; 5MKX; 5LVR; 5LVQ; 5FE9	MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKERQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSGLEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHDILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK	Literature-reported	Specific inhibition of p300-HAT alters global gene expression and represses HIV replication. Chem Biol. 2007 Jun;14(6):645-57.	0	EC:2.3	Acyltransferase	acetyltransferase family. GCN5 subfamily.	2.3.1.48 	Acyltransferases	Acetyltransferase (GNAT) family; Bromodomain; PCAF (P300/CBP-associated factor) N-terminal domain	PF00583; PF00439; PF06466	PF00583; Acetyltransf_1; PF00439; Bromodomain; PF06466; PCAF_N	.	.	hsa03250: Viral life cycle - HIV-1; hsa04330: Notch signaling pathway; hsa04919: Thyroid hormone signaling pathway; hsa05166: Human T-cell leukemia virus 1 infection; hsa05203: Viral carcinogenesis	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	.	Q92831
TT6O1J0	Histone acetyltransferase KAT6A (KAT6A)	Q92794	KAT6A_HUMAN	.	"MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3; MYST-3; Monocytic leukemia zinc finger protein; Runt-related transcription factor-binding protein 2; Zinc finger protein 220"	KAT6A	"Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML. {ECO:0000269|PubMed:11742995, ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:12771199, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:17925393, ECO:0000269|PubMed:23431171}."	EC 2.3.1.48	1M36;2LN0;2OZU;2RC4;3V43;4LJN;4LK9;4LKA;4LLB;5B75;5B76;5B77;5B78;6LSB;7Y43;8DD5;8H7A	MVKLANPLYTEWILEAIKKVKKQKQRPSEERICNAVSSSHGLDRKTVLEQLELSVKDGTILKVSNKGLNSYKDPDNPGRIALPKPRNHGKLDNKQNVDWNKLIKRAVEGLAESGGSTLKSIERFLKGQKDVSALFGGSAASGFHQQLRLAIKRAIGHGRLLKDGPLYRLNTKATNVDGKESCESLSCLPPVSLLPHEKDKPVAEPIPICSFCLGTKEQNREKKPEELISCADCGNSGHPSCLKFSPELTVRVKALRWQCIECKTCSSCRDQGKNADNMLFCDSCDRGFHMECCDPPLTRMPKGMWICQICRPRKKGRKLLQKKAAQIKRRYTNPIGRPKNRLKKQNTVSKGPFSKVRTGPGRGRKRKITLSSQSASSSSEEGYLERIDGLDFCRDSNVSLKFNKKTKGLIDGLTKFFTPSPDGRKARGEVVDYSEQYRIRKRGNRKSSTSDWPTDNQDGWDGKQENEERLFGSQEIMTEKDMELFRDIQEQALQKVGVTGPPDPQVRCPSVIEFGKYEIHTWYSSPYPQEYSRLPKLYLCEFCLKYMKSRTILQQHMKKCGWFHPPANEIYRKNNISVFEVDGNVSTIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTQNDVKGCHLVGYFSKEKHCQQKYNVSCIMILPQYQRKGYGRFLIDFSYLLSKREGQAGSPEKPLSDLGRLSYMAYWKSVILECLYHQNDKQISIKKLSKLTGICPQDITSTLHHLRMLDFRSDQFVIIRREKLIQDHMAKLQLNLRPVDVDPECLRWTPVIVSNSVVSEEEEEEAEEGENEEPQCQERELEISVGKSVSHENKEQDSYSVESEKKPEVMAPVSSTRLSKQVLPHDSLPANSQPSRRGRWGRKNRKTQERFGDKDSKLLLEETSSAPQEQYGECGEKSEATQEQYTESEEQLVASEEQPSQDGKPDLPKRRLSEGVEPWRGQLKKSPEALKCRLTEGSERLPRRYSEGDRAVLRGFSESSEEEEEPESPRSSSPPILTKPTLKRKKPFLHRRRRVRKRKHHNSSVVTETISETTEVLDEPFEDSDSERPMPRLEPTFEIDEEEEEEDENELFPREYFRRLSSQDVLRCQSSSKRKSKDEEEDEESDDADDTPILKPVSLLRKRDVKNSPLEPDTSTPLKKKKGWPKGKSRKPIHWKKRPGRKPGFKLSREIMPVSTQACVIEPIVSIPKAGRKPKIQESEETVEPKEDMPLPEERKEEEEMQAEAEEAEEGEEEDAASSEVPAASPADSSNSPETETKEPEVEEEEEKPRVSEEQRQSEEEQQELEEPEPEEEEDAAAETAQNDDHDADDEDDGHLESTKKKELEEQPTREDVKEEPGVQESFLDANMQKSREKIKDKEETELDSEEEQPSHDTSVVSEQMAGSEDDHEEDSHTKEELIELKEEEEIPHSELDLETVQAVQSLTQEESSEHEGAYQDCEETLAACQTLQSYTQADEDPQMSMVEDCHASEHNSPISSVQSHPSQSVRSVSSPNVPALESGYTQISPEQGSLSAPSMQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNSSSQSSCSYGGLSSSSSLTQSSCVVTQQMASMGSSCSMMQQSSVQPAANCSIKSPQSCVVERPPSNQQQQPPPPPPQQPQPPPPQPQPAPQPPPPQQQPQQQPQPQPQQPPPPPPPQQQPPLSQCSMNNSFTPAPMIMEIPESGSTGNISIYERIPGDFGAGSYSQPSATFSLAKLQQLTNTIMDPHAMPYSHSPAVTSYATSVSLSNTGLAQLAPSHPLAGTPQAQATMTPPPNLASTTMNLTSPLLQCNMSATNIGIPHTQRLQGQMPVKGHISIRSKSAPLPSAAAHQQQLYGRSPSAVAMQAGPRALAVQRGMNMGVNLMPTPAYNVNSMNMNTLNAMNSYRMTQPMMNSSYHSNPAYMNQTAQYPMQMQMGMMGSQAYTQQPMQPNPHGNMMYTGPSHHSYMNAAGVPKQSLNGPYMRR	Clinical trial	"Clinical pipeline report, company report or official report of Pfzer"	.	.	.	.	.	.	.	.	.	.	.	hsa:7994	R-HSA-3214847;R-HSA-6804758;	.	Q92794;
TTH4VJL	Histone acetyltransferase KAT6B (KAT6B)	Q8WYB5	KAT6B_HUMAN	Acyltransferase	KAT6B	KAT6B	"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."	EC 2.3.1.48	5U2J	MVKLANPLYTEWILEAIQKIKKQKQRPSEERICHAVSTSHGLDKKTVSEQLELSVQDGSVLKVTNKGLASYKDPDNPGRFSSVKPGTFPKSAKGSRGSCNDLRNVDWNKLLRRAIEGLEEPNGSSLKNIEKYLRSQSDLTSTTNNPAFQQRLRLGAKRAVNNGRLLKDGPQYRVNYGSLDGKGAPQYPSAFPSSLPPVSLLPHEKDQPRADPIPICSFCLGTKESNREKKPEELLSCADCGSSGHPSCLKFCPELTTNVKALRWQCIECKTCSACRVQGRNADNMLFCDSCDRGFHMECCDPPLSRMPKGMWICQVCRPKKKGRKLLHEKAAQIKRRYAKPIGRPKNKLKQRLLSVTSDEGSMNAFTGRGSPGRGQKTKVCTTPSSGHAASGKDSSSRLAVTDPTRPGATTKITTTSTYISASTLKVNKKTKGLIDGLTKFFTPSPDGRRSRGEIIDFSKHYRPRKKVSQKQSCTSHVLATGTTQKLKPPPSSLPPPTPISGQSPSSQKSSTATSSPSPQSSSSQCSVPSLSSLTTNSQLKALFDGLSHIYTTQGQSRKKGHPSYAPPKRMRRKTELSSTAKSKAHFFGKRDIRSRFISHSSSSSWGMARGSIFKAIAHFKRTTFLKKHRMLGRLKYKVTPQMGTPSPGKGSLTDGRIKPDQDDDTEIKINIKQESADVNVIGNKDVVTEEDLDVFKQAQELSWEKIECESGVEDCGRYPSVIEFGKYEIQTWYSSPYPQEYARLPKLYLCEFCLKYMKSKNILLRHSKKCGWFHPPANEIYRRKDLSVFEVDGNMSKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTKNDEKGCHLVGYFSKEKLCQQKYNVSCIMIMPQHQRQGFGRFLIDFSYLLSRREGQAGSPEKPLSDLGRLSYLAYWKSVILEYLYHHHERHISIKAISRATGMCPHDIATTLQHLHMIDKRDGRFVIIRREKLILSHMEKLKTCSRANELDPDSLRWTPILISNAAVSEEEREAEKEAERLMEQASCWEKEEQEILSTRANSRQSPAKVQSKNKYLHSPESRPVTGERGQLLELSKESSEEEEEEEDEEEEEEEEEEEEDEEEEEEEEEEEEEENIQSSPPRLTKPQSVAIKRKRPFVLKKKRGRKRRRINSSVTTETISETTEVLNEPFDNSDEERPMPQLEPTCEIEVEEDGRKPVLRKAFQHQPGKKRQTEEEEGKDNHCFKNADPCRNNMNDDSSNLKEGSKDNPEPLKCKQVWPKGTKRGLSKWRQNKERKTGFKLNLYTPPETPMEPDEQVTVEEQKETSEGKTSPSPIRIEEEVKETGEALLPQEENRREETCAPVSPNTSPGEKPEDDLIKPEEEEEEEEEEEEEEEEEEGEEEEGGGNVEKDPDGAKSQEKEEPEISTEKEDSARLDDHEEEEEEDEEPSHNEDHDADDEDDSHMESAEVEKEELPRESFKEVLENQETFLDLNVQPGHSNPEVLMDCGVDLTASCNSEPKELAGDPEAVPESDEEPPPGEQAQKQDQKNSKEVDTEFKEGNPATMEIDSETVQAVQSLTQESSEQDDTFQDCAETQEACRSLQNYTRADQSPQIATTLDDCQQSDHSSPVSSVHSHPGQSVRSVNSPSVPALENSYAQISPDQSAISVPSLQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNGSSQNSCSYSNLTSSSLTQSSCAVTQQMSNISGSCSMLQQTSISSPPTCSVKSPQGCVVERPPSSSQQLAQCSMAANFTPPMQLAEIPETSNANIGLYERMGQSDFGAGHYPQPSATFSLAKLQQLTNTLIDHSLPYSHSAAVTSYANSASLSTPLSNTGLVQLSQSPHSVPGGPQAQATMTPPPNLTPPPMNLPPPLLQRNMAASNIGISHSQRLQTQIASKGHISMRTKSASLSPAAATHQSQIYGRSQTVAMQGPARTLTMQRGMNMSVNLMPAPAYNVNSVNMNMNTLNAMNGYSMSQPMMNSGYHSNHGYMNQTPQYPMQMQMGMMGTQPYAQQPMQTPPHGNMMYTAPGHHGYMNTGMSKQSLNGSYMRR	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2735).	0	.	.	.	.	.	.	.	.	.	.	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	"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"	.	Q8WYB5
TTS3DIK	Voltage-gated potassium channel Kv1.1 (KCNA1)	Q09470	KCNA1_HUMAN	Voltage-gated ion channel	Voltagegated potassium channel subunit Kv1.1; Voltagegated potassium channel HBK1; Voltagegated K(+) channel HuKI; Potassium voltagegated channel subfamily A member 1; KCNA1	KCNA1	"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)."	.	2AFL	MTVMSGENVDEASAAPGHPQDGSYPRQADHDDHECCERVVINISGLRFETQLKTLAQFPNTLLGNPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDMFSEEIKFYELGEEAMEKFREDEGFIKEEERPLPEKEYQRQVWLLFEYPESSGPARVIAIVSVMVILISIVIFCLETLPELKDDKDFTGTVHRIDNTTVIYNSNIFTDPFFIVETLCIIWFSFELVVRFFACPSKTDFFKNIMNFIDIVAIIPYFITLGTEIAEQEGNQKGEQATSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEAEEAESHFSSIPDAFWWAVVSMTTVGYGDMYPVTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQAQLLHVSSPNLASDSDLSRRSSSTMSKSEYMEIEEDMNNSIAHYRQVNIRTANCTTANQNCVNKSKLLTDV	Literature-reported	"Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. Mol Pharmacol. 1994 Jun;45(6):1227-34."	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1296072:Voltage gated Potassium channels	.	Q09470
TTT4Y0X	Voltage-gated potassium channel Kv1.8 (KCNA10)	Q16322	KCA10_HUMAN	Voltage-gated ion channel	Voltage-gated potassium channel subunit Kv1.8; Potassium voltage-gated channel subfamily A member 10	KCNA10	"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."	.	.	MDVCGWKEMEVALVNFDNSDEIQEEPGYATDFDSTSPKGRPGGSSFSNGKILISESTNHETAFSKLPGDYADPPGPEPVVLNEGNQRVIINIAGLRFETQLRTLSQFPETLLGDREKRMQFFDSMRNEYFFDRNRPSFDGILYYYQSGGKIRRPANVPIDIFADEISFYELGSEAMDQFREDEGFIKDPETLLPTNDIHRQFWLLFEYPESSSAARAVAVVSVLVVVISITIFCLETLPEFREDRELKVVRDPNLNMSKTVLSQTMFTDPFFMVESTCIVWFTFELVLRFVVCPSKTDFFRNIMNIIDIISIIPYFATLITELVQETEPSAQQNMSLAILRIIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEVDEPESHFSSIPDGFWWAVVTMTTVGYGDMCPTTPGGKIVGTLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEKQNIPGEIERILNSVGSRMGSTDSLNKTNGGCSTEKSRK	Literature-reported	KCNA10: a novel ion channel functionally related to both voltage-gated potassium and CNG cation channels. Am J Physiol Renal Physiol. 2000 Jun;278(6):F1013-21.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1296072: Voltage gated Potassium channels	.	Q16322
TTVFB0O	Voltage-gated potassium channel Kv1.2 (KCNA2)	P16389	KCNA2_HUMAN	Voltage-gated ion channel	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	KCNA2	"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."	.	.	MTVATGDPADEAAALPGHPQDTYDPEADHECCERVVINISGLRFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFSEEIRFYELGEEAMEMFREDEGYIKEEERPLPENEFQRQVWLLFEYPESSGPARIIAIVSVMVILISIVSFCLETLPIFRDENEDMHGSGVTFHTYSNSTIGYQQSTSFTDPFFIVETLCIIWFSFEFLVRFFACPSKAGFFTNIMNIIDIVAIIPYFITLGTELAEKPEDAQQGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEADERESQFPSIPDAFWWAVVSMTTVGYGDMVPTTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQAQYLQVTSCPKIPSSPDLKKSRSASTISKSDYMEIQEGVNNSNEDFREENLKTANCTLANTNYVNITKMLTDV	Literature-reported	"Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. Mol Pharmacol. 1994 Jun;45(6):1227-34."	0	TC=1.A.1	.	potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.2/KCNA2 sub-subfamily. 	.	.	BTB/POZ domain; Ion transport protein	PF02214; PF00520	PF02214; BTB_2; PF00520; Ion_trans	1.A.1.2.10	The Voltage-gated Ion Channel (VIC) Superfamily 	.	R-HSA-1296072: Voltage gated Potassium channels	.	P16389
TTY3UE6	Voltage-gated potassium channel Kv1.3 (KCNA3)	P22001	KCNA3_HUMAN	Voltage-gated ion channel	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	KCNA3	"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."	.	4BGC	MDERLSLLRSPPPPSARHRAHPPQRPASSGGAHTLVNHGYAEPAAGRELPPDMTVVPGDHLLEPEVADGGGAPPQGGCGGGGCDRYEPLPPSLPAAGEQDCCGERVVINISGLRFETQLKTLCQFPETLLGDPKRRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRIRRPVNVPIDIFSEEIRFYQLGEEAMEKFREDEGFLREEERPLPRRDFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPEFRDEKDYPASTSQDSFEAAGNSTSGSRAGASSFSDPFFVVETLCIIWFSFELLVRFFACPSKATFSRNIMNLIDIVAIIPYFITLGTELAERQGNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEADDPTSGFSSIPDAFWWAVVTMTTVGYGDMHPVTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQSQYMHVGSCQHLSSSAEELRKARSNSTLSKSEYMVIEEGGMNHSAFPQTPFKTGNSTATCTTNNNPNSCVNIKKIFTDV	Clinical trial	"Durable Pharmacological Responses from the Peptide ShK-186, a Specific Kv1.3 Channel Inhibitor That Suppresses T Cell Mediators of Autoimmune Disease. J Pharmacol Exp Ther. 2012 September; 342(3): 642-653."	20	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1296072:Voltage gated Potassium channels	.	P22001
TTL213V	Voltage-gated A-type potassium channel (A-KC)	P22459; Q03721; Q9NSA2; Q9NZV8; Q9UK17	KCNA4_HUMAN; KCNC4_HUMAN; KCND1_HUMAN; KCND2_HUMAN; KCND3_HUMAN	Voltage-gated ion channel	Potassium voltage-gated channel	KCNA4	"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."	.	.	MEVAMVSAESSGCNSHMPYGYAAQARARERERLAHSRAAAAAAVAAATAAVEGSGGSGGGSHHHHQSRGACTSHDPQSSRGSRRRRRQRSEKKKAHYRQSSFPHCSDLMPSGSEEKILRELSEEEEDEEEEEEEEEEGRFYYSEDDHGDECSYTDLLPQDEGGGGYSSVRYSDCCERVVINVSGLRFETQMKTLAQFPETLLGDPEKRTQYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLKRPVNVPFDIFTEEVKFYQLGEEALLKFREDEGFVREEEDRALPENEFKKQIWLLFEYPESSSPARGIAIVSVLVILISIVIFCLETLPEFRDDRDLVMALSAGGHGGLLNDTSAPHLENSGHTIFNDPFFIVETVCIVWFSFEFVVRCFACPSQALFFKNIMNIIDIVSILPYFITLGTDLAQQQGGGNGQQQQAMSFAILRIIRLVRVFRIFKLSRHSKGLQILGHTLRASMRELGLLIFFLFIGVILFSSAVYFAEADEPTTHFQSIPDAFWWAVVTMTTVGYGDMKPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEQTQLTQNAVSCPYLPSNLLKKFRSSTSSSLGDKSEYLEMEEGVKESLCAKEEKCQGKGDDSETDKNNCSNAKAVETDV	Literature-reported	Inhibition of A-Type K+ Channels by Urotensin-II Induces Sensory Neuronal Hyperexcitability Through the PKC-ERK Pathway. Endocrinology. 2018 May 1;159(5):2253-2263.	.	.	.	.	.	.	.	.	.	.	.	hsa04927: Cortisol synthesis and secretion; hsa04934: Cushing syndrome	R-HSA-1296072: Voltage gated Potassium channels	.	P22459
TTW0CMT	Voltage-gated potassium channel Kv1.5 (KCNA5)	P22460	KCNA5_HUMAN	Voltage-gated ion channel	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	KCNA5	"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."	.	.	MEIALVPLENGGAMTVRGGDEARAGCGQATGGELQCPPTAGLSDGPKEPAPKGRGAQRDADSGVRPLPPLPDPGVRPLPPLPEELPRPRRPPPEDEEEEGDPGLGTVEDQALGTASLHHQRVHINISGLRFETQLGTLAQFPNTLLGDPAKRLRYFDPLRNEYFFDRNRPSFDGILYYYQSGGRLRRPVNVSLDVFADEIRFYQLGDEAMERFREDEGFIKEEEKPLPRNEFQRQVWLIFEYPESSGSARAIAIVSVLVILISIITFCLETLPEFRDERELLRHPPAPHQPPAPAPGANGSGVMAPPSGPTVAPLLPRTLADPFFIVETTCVIWFTFELLVRFFACPSKAGFSRNIMNIIDVVAIFPYFITLGTELAEQQPGGGGGGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADNQGTHFSSIPDAFWWAVVTMTTVGYGDMRPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDHEEPAVLKEEQGTQSQGPGLDRGVQRKVSGSRGSFCKAGGTLENADSARRGSCPLEKCNVKAKSNVDLRRSLYALCLDTSRETDL	Successful	New antiarrhythmic agents for atrial fibrillation and atrial flutter. Expert Opin Emerg Drugs. 2005 May;10(2):311-22.	34	TC=1.A.1	Voltage gated ion channel	potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.5/KCNA5 sub-subfamily. 	.	.	BTB/POZ domain; Ion transport protein	PF02214; PF00520	PF02214; BTB_2; PF00520; Ion_trans	1.A.1.2.4	The Voltage-gated Ion Channel (VIC) Superfamily 	.	R-HSA-1296072:Voltage gated Potassium channels	.	P22460
TTJ2W69	Voltage-gated potassium channel Kv1.6 (KCNA6)	P17658	KCNA6_HUMAN	Voltage-gated ion channel	Voltage-gated potassium channel subunit Kv1.6; Voltage-gated potassium channel HBK2; Potassium voltage-gated channel subfamily A member 6	KCNA6	"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."	.	.	MRSEKSLTLAAPGEVRGPEGEQQDAGDFPEAGGGGGCCSSERLVINISGLRFETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFLEEIRFYQLGDEALAAFREDEGCLPEGGEDEKPLPSQPFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPQFRVDGRGGNNGGVSRVSPVSRGSQEEEEDEDDSYTFHHGITPGEMGTGGSSSLSTLGGSFFTDPFFLVETLCIVWFTFELLVRFSACPSKPAFFRNIMNIIDLVAIFPYFITLGTELVQQQEQQPASGGGGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADDDDSLFPSIPDAFWWAVVTMTTVGYGDMYPMTVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEQEEQGQYTHVTCGQPAPDLRATDNGLGKPDFPEANRERRPSYLPTPHRAYAEKRMLTEV	Literature-reported	Cloning and expression of a human voltage-gated potassium channel. A novel member of the RCK potassium channel family. EMBO J. 1990 Jun;9(6):1749-56.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1296072: Voltage gated Potassium channels	.	P17658
TTCVBT7	Voltage-gated potassium channel Kv1.7 (KCNA7)	Q96RP8	KCNA7_HUMAN	Voltage-gated ion channel	Voltage-gated potassium channel subunit Kv1.7; Potassium voltage-gated channel subfamily A member 7	KCNA7	"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)."	.	.	MEPRCPPPCGCCERLVLNVAGLRFETRARTLGRFPDTLLGDPARRGRFYDDARREYFFDRHRPSFDAVLYYYQSGGRLRRPAHVPLDVFLEEVAFYGLGAAALARLREDEGCPVPPERPLPRRAFARQLWLLFEFPESSQAARVLAVVSVLVILVSIVVFCLETLPDFRDDRDGTGLAAAAAAGPFPAPLNGSSQMPGNPPRLPFNDPFFVVETLCICWFSFELLVRLLVCPSKAIFFKNVMNLIDFVAILPYFVALGTELARQRGVGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLRASMRELGLLIFFLFIGVVLFSSAVYFAEVDRVDSHFTSIPESFWWAVVTMTTVGYGDMAPVTVGGKIVGSLCAIAGVLTISLPVPVIVSNFSYFYHRETEGEEAGMFSHVDMQPCGPLEGKANGGLVDGEVPELPPPLWAPPGKHLVTEV	Literature-reported	"Genomic organization, chromosomal localization, tissue distribution, and biophysical characterization of a novel mammalian Shaker-related voltage-gated potassium channel, Kv1.7. J Biol Chem. 1998 Mar6;273(10):5851-7."	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1296072: Voltage gated Potassium channels	.	Q96RP8
TT5OEKU	Voltage-gated potassium channel Kv2.1 (KCNB1)	Q14721	KCNB1_HUMAN	Voltage-gated ion channel	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	KCNB1	"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."	.	.	MPAGMTKHGSRSTSSLPPEPMEIVRSKACSRRVRLNVGGLAHEVLWRTLDRLPRTRLGKLRDCNTHDSLLEVCDDYSLDDNEYFFDRHPGAFTSILNFYRTGRLHMMEEMCALSFSQELDYWGIDEIYLESCCQARYHQKKEQMNEELKREAETLREREGEEFDNTCCAEKRKKLWDLLEKPNSSVAAKILAIISIMFIVLSTIALSLNTLPELQSLDEFGQSTDNPQLAHVEAVCIAWFTMEYLLRFLSSPKKWKFFKGPLNAIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDDTKFKSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNMKDAFARSIEMMDIVVEKNGENMGKKDKVQDNHLSPNKWKWTKRTLSETSSSKSFETKEQGSPEKARSSSSPQHLNVQQLEDMYNKMAKTQSQPILNTKESAAQSKPKEELEMESIPSPVAPLPTRTEGVIDMRSMSSIDSFISCATDFPEATRFSHSPLTSLPSKTGGSTAPEVGWRGALGASGGRFVEANPSPDASQHSSFFIESPKSSMKTNNPLKLRALKVNFMEGDPSPLLPVLGMYHDPLRNRGSAAAAVAGLECATLLDKAVLSPESSIYTTASAKTPPRSPEKHTAIAFNFEAGVHQYIDADTDDEGQLLYSVDSSPPKSLPGSTSPKFSTGTRSEKNHFESSPLPTSPKFLRQNCIYSTEALTGKGPSGQEKCKLENHISPDVRVLPGGGAHGSTRDQSI	Literature-reported	Identification of novel and selective Kv2 channel inhibitors. Mol Pharmacol. 2011 Dec;80(6):959-64.	0	TC=1.A.1	Voltage-gated ion channel	potassium channel family. B (Shab) (TC 1.A.1.2) subfamily. Kv2.1/KCNB1 sub-subfamily. 	.	.	BTB/POZ domain; Ion transport protein; Kv2 voltage-gated K+ channel	PF02214; PF00520; PF03521	PF02214; BTB_2; PF00520; Ion_trans; PF03521; Kv2channel	1.A.1.2.11	The Voltage-gated Ion Channel (VIC) Superfamily 	.	R-HSA-1296072:Voltage gated Potassium channels; R-HSA-381676:Glucagon-like Peptide-1 (GLP1) regulates insulin secretion	.	Q14721
TT5PFNG	Voltage-gated potassium channel Kv2.2 (KCNB2)	Q92953	KCNB2_HUMAN	Voltage-gated ion channel	Voltage-gated potassium channel subunit Kv2.2; Potassium voltage-gated channel subfamily B member 2	KCNB2	"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."	.	.	MAEKAPPGLNRKTSRSTLSLPPEPVDIIRSKTCSRRVKINVGGLNHEVLWRTLDRLPRTRLGKLRDCNTHESLLEVCDDYNLNENEYFFDRHPGAFTSILNFYRTGKLHMMEEMCALSFGQELDYWGIDEIYLESCCQARYHQKKEQMNEELRREAETMREREGEEFDNTCCPDKRKKLWDLLEKPNSSVAAKILAIVSILFIVLSTIALSLNTLPELQETDEFGQLNDNRQLAHVEAVCIAWFTMEYLLRFLSSPNKWKFFKGPLNVIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDATKFTSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNLKDAFARSMELIDVAVEKAGESANTKDSADDNHLSPSRWKWARKALSETSSNKSFENKYQEVSQKDSHEQLNNTSSSSPQHLSAQKLEMLYNEITKTQPHSHPNPDCQEKPERPSAYEEEIEMEEVVCPQEQLAVAQTEVIVDMKSTSSIDSFTSCATDFTETERSPLPPPSASHLQMKFPTDLPGTEEHQRARGPPFLTLSREKGPAARDGTLEYAPVDITVNLDASGSQCGLHSPLQSDNATDSPKSSLKGSNPLKSRSLKVNFKENRGSAPQTPPSTARPLPVTTADFSLTTPQHISTILLEETPSQGDRPLLGTEVSAPCQGPSKGLSPRFPKQKLFPFSSRERRSFTEIDTGDDEDFLELPGAREEKQVDSSPNCFADKPSDGRDPLREEGSVGSSSPQDTGHNCRQDIYHAVSEVKKDSSQEGCKMENHLFAPEIHSNPGDTGYCPTRETSM	Literature-reported	Identification of novel and selective Kv2 channel inhibitors. Mol Pharmacol. 2011 Dec;80(6):959-64.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1296072: Voltage gated Potassium channels	.	Q92953
TTVUWHQ	Voltage-gated potassium channel Kv3.1 (KCNC1)	P48547	KCNC1_HUMAN	Voltage-gated ion channel	Voltage-gated potassium channel subunit Kv4; Voltage-gated potassium channel subunit Kv3.1; Potassium voltage-gated channel subfamily C member 1; NGK2	KCNC1	"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."	.	.	MGQGDESERIVINVGGTRHQTYRSTLRTLPGTRLAWLAEPDAHSHFDYDPRADEFFFDRHPGVFAHILNYYRTGKLHCPADVCGPLYEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDSFGGAPLDNSADDADADGPGDSGDGEDELEMTKRLALSDSPDGRPGGFWRRWQPRIWALFEDPYSSRYARYVAFASLFFILVSITTFCLETHERFNPIVNKTEIENVRNGTQVRYYREAETEAFLTYIEGVCVVWFTFEFLMRVIFCPNKVEFIKNSLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGAQPNDPSASEHTHFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKKKKHIPRPPQLGSPNYCKSVVNSPHHSTQSDTCPLAQEEILEINRAGRKPLRGMSI	Literature-reported	"Effects of norfluoxetine, the major metabolite of fluoxetine, on the cloned neuronal potassium channel Kv3.1. Neuropharmacology. 2001 Sep;41(4):443-53."	0	TC=1.A.1	.	potassium channel family. C (Shaw) (TC 1.A.1.2) subfamily. Kv3.1/KCNC1 sub-subfamily. 	.	.	BTB/POZ domain; Ion transport protein	PF02214; PF00520	PF02214; BTB_2; PF00520; Ion_trans	1.A.1.2.24	The Voltage-gated Ion Channel (VIC) Superfamily 	.	R-HSA-1296072: Voltage gated Potassium channels	.	P48547
TTGK3ZO	Voltage-gated potassium channel Kv3.2 (KCNC2)	Q96PR1	KCNC2_HUMAN	Voltage-gated ion channel	Shaw-like potassium channel; Potassium voltage-gated channel subfamily C member 2	KCNC2	"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)."	.	.	MGKIENNERVILNVGGTRHETYRSTLKTLPGTRLALLASSEPPGDCLTTAGDKLQPSPPPLSPPPRAPPLSPGPGGCFEGGAGNCSSRGGRASDHPGGGREFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDIFETPDLIGGDPGDDEDLAAKRLGIEDAAGLGGPDGKSGRWRRLQPRMWALFEDPYSSRAARFIAFASLFFILVSITTFCLETHEAFNIVKNKTEPVINGTSVVLQYEIETDPALTYVEGVCVVWFTFEFLVRIVFSPNKLEFIKNLLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERVGAQPNDPSASEHTQFKNIPIGFWWAVVTMTTLGYGDMYPQTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPRKRKKHIPPAPQASSPTFCKTELNMACNSTQSDTCLGKDNRLLEHNRSVLSGDDSTGSEPPLSPPERLPIRRSSTRDKNRRGETCFLLTTGDYTCASDGGIRKGYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL	Literature-reported	"Gating, modulation and subunit composition of voltage-gated K(+) channels in dendritic inhibitory interneurones of rat hippocampus. J Physiol. 2002 Jan 15;538(Pt 2):405-19."	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1296072: Voltage gated Potassium channels; R-HSA-381676: Glucagon-like Peptide-1 (GLP1) regulates insulin secretion	.	Q96PR1
TTALSY9	Voltage-gated potassium channel Kv3.3 (KCNC3)	Q14003	KCNC3_HUMAN	Voltage-gated ion channel	Voltage-gated potassium channel subunit Kv3.3; Potassium voltage-gated channel subfamily C member 3; KSHIIID	KCNC3	"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."	.	.	MLSSVCVSSFRGRQGASKQQPAPPPQPPESPPPPPLPPQQQQPAQPGPAASPAGPPAPRGPGDRRAEPCPGLPAAAMGRHGGGGGDSGKIVINVGGVRHETYRSTLRTLPGTRLAGLTEPEAAARFDYDPGADEFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELGFWGIDETDVEACCWMTYRQHRDAEEALDSFEAPDPAGAANAANAAGAHDGGLDDEAGAGGGGLDGAGGELKRLCFQDAGGGAGGPPGGAGGAGGTWWRRWQPRVWALFEDPYSSRAARYVAFASLFFILISITTFCLETHEGFIHISNKTVTQASPIPGAPPENITNVEVETEPFLTYVEGVCVVWFTFEFLMRITFCPDKVEFLKSSLNIIDCVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGADPDDILGSNHTYFKNIPIGFWWAVVTMTTLGYGDMYPKTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKKNKHIPRPPQPGSPNYCKPDPPPPPPPHPHHGSGGISPPPPITPPSMGVTVAGAYPAGPHTHPGLLRGGAGGLGIMGLPPLPAPGEPCPLAQEEVIEINRADPRPNGDPAAAALAHEDCPAIDQPAMSPEDKSPITPGSRGRYSRDRACFLLTDYAPSPDGSIRKATGAPPLPPQDWRKPGPPSFLPDLNANAAAWISP	Literature-reported	"Cloning of ShIII (Shaw-like) cDNAs encoding a novel high-voltage-activating, TEA-sensitive, type-A K+ channel. Proc Biol Sci. 1992 Apr 22;248(1321):9-18."	0	.	.	.	.	.	.	.	.	.	.	hsa05017: Spinocerebellar ataxia	R-HSA-1296072: Voltage gated Potassium channels	.	Q14003
TTODZF1	Voltage-gated potassium channel Kv3.4 (KCNC4)	Q03721	KCNC4_HUMAN	Voltage-gated ion channel	Voltage-gated potassium channel subunit Kv3.4; Potassium voltage-gated channel subfamily C member 4; KSHIIIC; C1orf30	KCNC4	"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."	.	1ZTN; 1B4I; 1B4G	MISSVCVSSYRGRKSGNKPPSKTCLKEEMAKGEASEKIIINVGGTRHETYRSTLRTLPGTRLAWLADPDGGGRPETDGGGVGSSGSSGGGGCEFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELTFWGIDETDVEPCCWMTYRQHRDAEEALDIFESPDGGGSGAGPSDEAGDDERELALQRLGPHEGGAGHGAGSGGCRGWQPRMWALFEDPYSSRAARVVAFASLFFILVSITTFCLETHEAFNIDRNVTEILRVGNITSVHFRREVETEPILTYIEGVCVLWFTLEFLVRIVCCPDTLDFVKNLLNIIDFVAILPFYLEVGLSGLSSKAARDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGARPSDPRGNDHTDFKNIPIGFWWAVVTMTTLGYGDMYPKTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKRKKHVPRPAQLESPMYCKSEETSPRDSTCSDTSPPAREEGMIERKRADSKQNGDANAVLSDEEGAGLTQPLASSPTPEERRALRRSTTRDRNKKAAACFLLSTGDYACADGSVRKGTFVLRDLPLQHSPEAACPPTAGTLFLPH	Literature-reported	Characterization of a Shaw-related potassium channel family in rat brain. EMBO J. 1992 Jul;11(7):2473-86.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1296072: Voltage gated Potassium channels	.	Q03721
TT4DI0J	Voltage-gated potassium channel Kv4.1 (KCND1)	Q9NSA2	KCND1_HUMAN	Voltage-gated ion channel	Voltage-gated potassium channel subunit Kv4.1; Potassium voltage-gated channel subfamily D member 1	KCND1	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.	.	.	MAAGLATWLPFARAAAVGWLPLAQQPLPPAPGVKASRGDEVLVVNVSGRRFETWKNTLDRYPDTLLGSSEKEFFYDADSGEYFFDRDPDMFRHVLNFYRTGRLHCPRQECIQAFDEELAFYGLVPELVGDCCLEEYRDRKKENAERLAEDEEAEQAGDGPALPAGSSLRQRLWRAFENPHTSTAALVFYYVTGFFIAVSVIANVVETIPCRGSARRSSREQPCGERFPQAFFCMDTACVLIFTGEYLLRLFAAPSRCRFLRSVMSLIDVVAILPYYIGLLVPKNDDVSGAFVTLRVFRVFRIFKFSRHSQGLRILGYTLKSCASELGFLLFSLTMAIIIFATVMFYAEKGTNKTNFTSIPAAFWYTIVTMTTLGYGDMVPSTIAGKIFGSICSLSGVLVIALPVPVIVSNFSRIYHQNQRADKRRAQQKVRLARIRLAKSGTTNAFLQYKQNGGLEDSGSGEEQALCVRNRSAFEQQHHHLLHCLEKTTCHEFTDELTFSEALGAVSPGGRTSRSTSVSSQPVGPGSLLSSCCPRRAKRRAIRLANSTASVSRGSMQELDMLAGLRRSHAPQSRSSLNAKPHDSLDLNCDSRDFVAAIISIPTPPANTPDESQPSSPGGGGRAGSTLRNSSLGTPCLFPETVKISSL	Literature-reported	Endogenous Kv channels in human embryonic kidney (HEK-293) cells. Mol Cell Biochem. 2002 Sep;238(1-2):69-79.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1296072: Voltage gated Potassium channels; R-HSA-5576894: Phase 1 - inactivation of fast Na+ channels	.	Q9NSA2
TTPLQO0	Voltage-gated potassium channel Kv4.3 (KCND3)	Q9UK17	KCND3_HUMAN	Voltage-gated ion channel	Voltage-gated potassium channel subunit Kv4.3; KCND3	KCND3	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.	.	2NZ0; 1S1G	MAAGVAAWLPFARAAAIGWMPVANCPMPLAPADKNKRQDELIVLNVSGRRFQTWRTTLERYPDTLLGSTEKEFFFNEDTKEYFFDRDPEVFRCVLNFYRTGKLHYPRYECISAYDDELAFYGILPEIIGDCCYEEYKDRKRENAERLMDDNDSENNQESMPSLSFRQTMWRAFENPHTSTLALVFYYVTGFFIAVSVITNVVETVPCGTVPGSKELPCGERYSVAFFCLDTACVMIFTVEYLLRLFAAPSRYRFIRSVMSIIDVVAIMPYYIGLVMTNNEDVSGAFVTLRVFRVFRIFKFSRHSQGLRILGYTLKSCASELGFLLFSLTMAIIIFATVMFYAEKGSSASKFTSIPASFWYTIVTMTTLGYGDMVPKTIAGKIFGSICSLSGVLVIALPVPVIVSNFSRIYHQNQRADKRRAQKKARLARIRVAKTGSSNAYLHSKRNGLLNEALELTGTPEEEHMGKTTSLIESQHHHLLHCLEKTTGLSYLVDDPLLSVRTSTIKNHEFIDEQMFEQNCMESSMQNYPSTRSPSLSSHPGLTTTCCSRRSKKTTHLPNSNLPATRLRSMQELSTIHIQGSEQPSLTTSRSSLNLKADDGLRPNCKTSQITTAIISIPTPPALTPEGESRPPPASPGPNTNIPSIASNVVKVSAL	Successful	Management of cocaine-induced cardiac arrhythmias due to cardiac ion channel dysfunction. Clin Toxicol (Phila). 2009 Jan;47(1):14-23.	34	.	.	.	.	.	.	.	.	.	.	hsa05017: Spinocerebellar ataxia	R-HSA-1296072:Voltage gated Potassium channels	.	Q9UK17
TT9XKUC	Voltage-gated potassium channel Kv10.1 (KCNH1)	O95259	KCNH1_HUMAN	Voltage-gated ion channel	hEAG1; h-eag; Voltage-gated potassium channel subunit Kv10.1; Potassium voltage-gated channel subfamily H member 1; EAG1; EAG channel 1; EAG	KCNH1	"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."	.	5J7E	MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTIEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTSSRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSAFMGDPGKIGFADQIPPPLEGRESQGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSIGDYEIFDEDTKTIRNNSWLYQLAMDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGKGDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEERMKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGNVLTEHASANHSLVKASVVTVRESPATPVSFQAASTSGVPDHAKLQAPGSECLGPKGGGGDCAKRKSWARFKDACGKSEDWNKVSKAESMETLPERTKASGEATLKKTDSCDSGITKSDLRLDNVGEARSPQDRSPILAEVKHSFYPIPEQTLQATVLEVRHELKEDIKALNAKMTNIEKQLSEILRILTSRRSSQSPQELFEISRPQSPESERDIFGAS	Literature-reported	ICA-105574 interacts with a common binding site to elicit opposite effects on inactivation gating of EAG and ERG potassium channels. Mol Pharmacol. 2013 Apr;83(4):805-13.	0	TC=1.A.1	.	potassium channel family. H (Eag) (TC 1.A.1.20) subfamily. Kv10.1/KCNH1 sub-subfamily. 	.	.	Cyclic nucleotide-binding domain; Ion transport protein; PAS domain	PF00027; PF00520; PF13426	PF00027; cNMP_binding; PF00520; Ion_trans; PF13426; PAS_9	1.I.1.1.3	The Eukaryotic Nuclear Pore Complex (E-NPC) Family	.	R-HSA-1296072: Voltage gated Potassium channels	.	O95259
TTQ6VDM	Voltage-gated potassium channel Kv11.1 (KCNH2)	Q12809	KCNH2_HUMAN	Voltage-gated ion channel	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	KCNH2	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.	.	5VA3; 5VA2; 5VA1; 4HQA; 4HP9	MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVMQRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDGAVIMFILNFEVVMEKDMVGSPAHDTNHRGPPTSWLAPGRAKTFRLKLPALLALTARESSVRSGGAGGAGAPGAVVVDVDLTPAAPSSESLALDEVTAMDNHVAGLGPAEERRALVGPGSPPRSAPGQLPSPRAHSLNPDASGSSCSLARTRSRESCASVRRASSADDIEAMRAGVLPPPPRHASTGAMHPLRSGLLNSTSDSDLVRYRTISKIPQITLNFVDLKGDPFLASPTSDREIIAPKIKERTHNVTEKVTQVLSLGADVLPEYKLQAPRIHRWTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLKETEEGPPATECGYACQPLAVVDLIVDIMFIVDILINFRTTYVNANEEVVSHPGRIAVHYFKGWFLIDMVAAIPFDLLIFGSGSEELIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNMEQPHMDSRIGWLHNLGDQIGKPYNSSGLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGFPECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGDVVVAILGKNDIFGEPLNLYARPGKSNGDVRALTYCDLHKIHRDDLLEVLDMYPEFSDHFWSSLEITFNLRDTNMIPGSPGSTELEGGFSRQRKRKLSFRRRTDKDTEQPGEVSALGPGRAGAGPSSRGRPGGPWGESPSSGPSSPESSEDEGPGRSSSPLRLVPFSSPRPPGEPPGGEPLMEDCEKSSDTCNPLSGAFSGVSNIFSFWGDSRGRQYQELPRCPAPTPSLLNIPLSSPGRRPRGDVESRLDALQRQLNRLETRLSADMATVLQLLQRQMTLVPPAYSAVTTPGPGPTSTSPLLPVSPLPTLTLDSLSQVSQFMACEELPPGAPELPQEGPTRRLSLPGQLGALTSQPLHRHGSDPGS	Successful	Prediction of hERG potassium channel affinity by traditional and hologram qSAR methods. Bioorg Med Chem Lett. 2003 Aug 18;13(16):2773-5.	34	TC=1.A.1	Voltage gated ion channel	potassium channel family. H (Eag) (TC 1.A.1.20) subfamily. Kv11.1/KCNH2 sub-subfamily. 	.	.	Cyclic nucleotide-binding domain; Ion transport protein; PAS domain	PF00027; PF00520; PF13426	PF00027; cNMP_binding; PF00520; Ion_trans; PF13426; PAS_9	1.A.1.20.1	The Voltage-gated Ion Channel (VIC) Superfamily 	.	R-HSA-1296072:Voltage gated Potassium channels	.	Q12809
TTZ4MTQ	Voltage-gated potassium channel Kv12.2 (KCNH3)	Q9ULD8	KCNH3_HUMAN	Voltage-gated ion channel	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	KCNH3	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.	.	.	MPAMRGLLAPQNTFLDTIATRFDGTHSNFVLGNAQVAGLFPVVYCSDGFCDLTGFSRAEVMQRGCACSFLYGPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEKGEVALFLVSHKDISETKNRGGPDRWKETGGGRRRYGRARSKGFNANRRRSRAVLYHLSGHLQKQPKGKHKLNKGVFGEKPNLPEYKVAAIRKSPFILLHCGALRATWDGFILLATLYVAVTVPYSVCVSTAREPSAARGPPSVCDLAVEVLFILDIVLNFRTTFVSKSGQVVFAPKSICLHYVTTWFLLDVIAALPFDLLHAFKVNVYFGAHLLKTVRLLRLLRLLPRLDRYSQYSAVVLTLLMAVFALLAHWVACVWFYIGQREIESSESELPEIGWLQELARRLETPYYLVGRRPAGGNSSGQSDNCSSSSEANGTGLELLGGPSLRSAYITSLYFALSSLTSVGFGNVSANTDTEKIFSICTMLIGALMHAVVFGNVTAIIQRMYARRFLYHSRTRDLRDYIRIHRIPKPLKQRMLEYFQATWAVNNGIDTTELLQSLPDELRADIAMHLHKEVLQLPLFEAASRGCLRALSLALRPAFCTPGEYLIHQGDALQALYFVCSGSMEVLKGGTVLAILGKGDLIGCELPRREQVVKANADVKGLTYCVLQCLQLAGLHDSLALYPEFAPRFSRGLRGELSYNLGAGGGSAEVDTSSLSGDNTLMSTLEEKETDGEQGPTVSPAPADEPSSPLLSPGCTSSSSAAKLLSPRRTAPRPRLGGRGRPGRAGALKAEAGPSAPPRALEGLRLPPMPWNVPPDLSPRVVDGIEDGCGSDQPKFSFRVGQSGPECSSSPSPGPESGLLTVPHGPSEARNTDTLDKLRQAVTELSEQVLQMREGLQSLRQAVQLVLAPHREGPCPRASGEGPCPASTSGLLQPLCVDTGASSYCLQPPAGSVLSGTWPHPRPGPPPLMAPWPWGPPASQSSPWPRATAFWTSTSDSEPPASGDLCSEPSTPASPPPSEEGARTGPAEPVSQAEATSTGEPPPGSGGLALPWDPHSLEMVLIGCHGSGTVQWTQEEGTGV	Literature-reported	Deletion of the potassium channel Kv12.2 causes hippocampal hyperexcitability and epilepsy. Nat Neurosci. 2010 Sep;13(9):1056-8.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1296072: Voltage gated Potassium channels	.	Q9ULD8
TTX8LQ0	Voltage-gated potassium channel Kv10.2 (KCNH5)	Q8NCM2	KCNH5_HUMAN	Voltage-gated ion channel	hEAG2; Voltage-gated potassium channel subunit Kv10.2; Potassium voltage-gated channel subfamily H member 5; Ether-a-go-go potassium channel 2; EAG2	KCNH5	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.	.	.	MPGGKRGLVAPQNTFLENIVRRSSESSFLLGNAQIVDWPVVYSNDGFCKLSGYHRADVMQKSSTCSFMYGELTDKKTIEKVRQTFDNYESNCFEVLLYKKNRTPVWFYMQIAPIRNEHEKVVLFLCTFKDITLFKQPIEDDSTKGWTKFARLTRALTNSRSVLQQLTPMNKTEVVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCAFKTTWDWVILILTFYTAIMVPYNVSFKTKQNNIAWLVLDSVVDVIFLVDIVLNFHTTFVGPGGEVISDPKLIRMNYLKTWFVIDLLSCLPYDIINAFENVDEGISSLFSSLKVVRLLRLGRVARKLDHYLEYGAAVLVLLVCVFGLVAHWLACIWYSIGDYEVIDEVTNTIQIDSWLYQLALSIGTPYRYNTSAGIWEGGPSKDSLYVSSLYFTMTSLTTIGFGNIAPTTDVEKMFSVAMMMVGSLLYATIFGNVTTIFQQMYANTNRYHEMLNNVRDFLKLYQVPKGLSERVMDYIVSTWSMSKGIDTEKVLSICPKDMRADICVHLNRKVFNEHPAFRLASDGCLRALAVEFQTIHCAPGDLIYHAGESVDALCFVVSGSLEVIQDDEVVAILGKGDVFGDIFWKETTLAHACANVRALTYCDLHIIKREALLKVLDFYTAFANSFSRNLTLTCNLRKRIIFRKISDVKKEEEERLRQKNEVTLSIPVDHPVRKLFQKFKQQKELRNQGSTQGDPERNQLQVESRSLQNGASITGTSVVTVSQITPIQTSLAYVKTSESLKQNNRDAMELKPNGGADQKCLKVNSPIRMKNGNGKGWLRLKNNMGAHEEKKEDWNNVTKAESMGLLSEDPKSSDSENSVTKNPLRKTDSCDSGITKSDLRLDKAGEARSPLEHSPIQADAKHPFYPIPEQALQTTLQEVKHELKEDIQLLSCRMTALEKQVAEILKILSEKSVPQASSPKSQMPLQVPPQIPCQDIFSVSRPESPESDKDEIHF	Literature-reported	Molecular determinants for high-affinity block of human EAG potassium channels by antiarrhythmic agents. Mol Pharmacol. 2004 May;65(5):1120-9.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1296072: Voltage gated Potassium channels	.	Q8NCM2
TTJ13ST	Inward rectifier potassium channel Kir1.1 (KCNJ1)	P48048	KCNJ1_HUMAN	Inward rectifier potassium channel	"ROMK1; Potassium channel, inwardly rectifying subfamily J member 1; Inward rectifier K(+) channel Kir1.1; ATP-sensitive inward rectifier potassium channel 1"	KCNJ1	"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."	.	.	MNASSRNVFDTLIRVLTESMFKHLRKWVVTRFFGHSRQRARLVSKDGRCNIEFGNVEAQSRFIFFVDIWTTVLDLKWRYKMTIFITAFLGSWFFFGLLWYAVAYIHKDLPEFHPSANHTPCVENINGLTSAFLFSLETQVTIGYGFRCVTEQCATAIFLLIFQSILGVIINSFMCGAILAKISRPKKRAKTITFSKNAVISKRGGKLCLLIRVANLRKSLLIGSHIYGKLLKTTVTPEGETIILDQININFVVDAGNENLFFISPLTIYHVIDHNSPFFHMAAETLLQQDFELVVFLDGTVESTSATCQVRTSYVPEEVLWGYRFAPIVSKTKEGKYRVDFHNFSKTVEVETPHCAMCLYNEKDVRARMKRGYDNPNFILSEVNETDDTKM	Patented-recorded	Inhibitors of the renal outer medullary potassium channel: a patent review.Expert Opin Ther Pat. 2015;25(9):1035-51.	15.5	TC=1.A.2	.	inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ1 subfamily. 	.	.	Inward rectifier potassium channel transmembrane domain; Inward rectifier potassium channel C-terminal domain	PF01007; PF17655	PF01007; IRK; PF17655; IRK_C	.	.	hsa04960: Aldosterone-regulated sodium reabsorption; hsa04971: Gastric acid secretion	R-HSA-1296067: Potassium transport channels	.	P48048
TTG140O	Inward rectifier potassium channel Kir1.2 (KCNJ10)	P78508	KCJ10_HUMAN	Inward rectifier potassium channel	"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"	KCNJ10	"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."	.	.	MTSVAKVYYSQTTQTESRPLMGPGIRRRRVLTKDGRSNVRMEHIADKRFLYLKDLWTTFIDMQWRYKLLLFSATFAGTWFLFGVVWYLVAVAHGDLLELDPPANHTPCVVQVHTLTGAFLFSLESQTTIGYGFRYISEECPLAIVLLIAQLVLTTILEIFITGTFLAKIARPKKRAETIRFSQHAVVASHNGKPCLMIRVANMRKSLLIGCQVTGKLLQTHQTKEGENIRLNQVNVTFQVDTASDSPFLILPLTFYHVVDETSPLKDLPLRSGEGDFELVLILSGTVESTSATCQVRTSYLPEEILWGYEFTPAISLSASGKYIADFSLFDQVVKVASPSGLRDSTVRYGDPEKLKLEESLREQAEKEGSALSVRISNV	Successful	Carboxyl-glucuronidation of mitiglinide by human UDP-glucuronosyltransferases. Biochem Pharmacol. 2007 Jun 1;73(11):1842-51.	34	TC=1.A.2	Inward rectifier K(+) channel	inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ10 subfamily. 	.	.	Inward rectifier potassium channel transmembrane domain; Inward rectifier potassium channel C-terminal domain	PF01007; PF17655	PF01007; IRK; PF17655; IRK_C	.	.	hsa04971:Gastric acid secretion	R-HSA-1296041:Activation of G protein gated Potassium channels; R-HSA-997272:Inhibition  of voltage gated Ca2+ channels via Gbeta/gamma subunits	.	P78508
TT329V4	Inward rectifier potassium channel Kir6.2 (KCNJ11)	Q14654	KCJ11_HUMAN	Inward rectifier potassium channel	"Potassium channel, inwardly rectifying, subfamily J, member 11; KCNJ11; KATP channel (Kir6.2/SUR2A); Inward rectifier K+ channel Kir6.2; IKATP"	KCNJ11	"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."	.	6C3P; 6C3O	MLSRKGIIPEEYVLTRLAEDPAEPRYRARQRRARFVSKKGNCNVAHKNIREQGRFLQDVFTTLVDLKWPHTLLIFTMSFLCSWLLFAMAWWLIAFAHGDLAPSEGTAEPCVTSIHSFSSAFLFSIEVQVTIGFGGRMVTEECPLAILILIVQNIVGLMINAIMLGCIFMKTAQAHRRAETLIFSKHAVIALRHGRLCFMLRVGDLRKSMIISATIHMQVVRKTTSPEGEVVPLHQVDIPMENGVGGNSIFLVAPLIIYHVIDANSPLYDLAPSDLHHHQDLEIIVILEGVVETTGITTQARTSYLADEILWGQRFVPIVAEEDGRYSVDYSKFGNTIKVPTPLCTARQLDEDHSLLEALTLASARGPLRKRSVPMAKAKPKFSISPDSLS	Literature-reported	Cardioselective K(ATP) channel blockers derived from a new series of m-anisamidoethylbenzenesulfonylthioureas. J Med Chem. 2001 Mar 29;44(7):1085-98.	0	.	.	.	.	.	.	.	.	.	.	hsa04911:Insulin secretion; hsa04930:Type II diabetes mellitus	R-HSA-382556:ABC-family proteins mediated transport; R-HSA-422356:Regulation of insulin secretion	.	Q14654
TTVW8QH	Inward rectifier potassium channel Kir2.6 (KCNJ18)	B7U540	KCJ18_HUMAN	Inward rectifier potassium channel	"Potassium channel, inwardly rectifying subfamily J member 18; KCNJ18; Inward rectifier potassium channel 18; Inward rectifier K(+) channel Kir2.6"	KCNJ18	"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."	.	.	MTAASRANPYSIVSLEEDGLHLVTMSGANGFGNGKVHTRRRCRNRFVKKNGQCNIAFANMDEKSQRYLADMFTTCVDIRWRYMLLIFSLAFLASWLLFGVIFWVIAVAHGDLEPAEGHGRTPCVMQVHGFMAAFLFSIETQTTIGYGLRCVTEECLVAVFMVVAQSIVGCIIDSFMIGAIMAKMARPKKRAQTLLFSHNAVVALRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRVTEEGEYIPLDQIDIDVGFDKGLDRIFLVSPITILHEIDEASPLFGISRQDLETDDFEIVVILEGMVEATAMTTQARSSYLANEILWGHRFEPVLFEEKNQYKIDYSHFHKTYEVPSTPRCSAKDLVENKFLLPSANSFCYENELAFLSRDEEDEADGDQDGRSRDGLSPQARHDFDRLQAGGGVLEQRPYRRGSEI	Literature-reported	Down-regulation of Kir2.6 channel by c-termini mutation D252N and its association with the susceptibility to Thyrotoxic Periodic Paralysis. Neuroscience. 2017 Mar 27;346:197-202.	.	.	.	.	.	.	.	.	.	.	.	hsa04725: Cholinergic synapse; hsa04921: Oxytocin signaling pathway	.	.	B7U540
TTH7UO3	Inward rectifier potassium channel Kir2.1 (KCNJ2)	P63252	KCNJ2_HUMAN	Inward rectifier potassium channel	"hIRK1; Potassium channel, inwardly rectifying subfamily J member 2; Inward rectifier K(+) channel Kir2.1; IRK1; IRK-1; Cardiac inward rectifier potassium channel"	KCNJ2	"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."	.	.	MGSVRTNRYSIVSSEEDGMKLATMAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFINVGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDASKEGKACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPIAVFMVVFQSIVGCIIDAFIIGAVMAKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEGEYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDIDNADFEIVVILEGMVEATAMTTQCRSSYLANEILWGHRYEPVLFEEKHYYKVDYSRFHKTYEVPNTPLCSARDLAEKKYILSNANSFCYENEVALTSKEEDDSENGVPESTSTDTPPDIDLHNQASVPLEPRPLRRESEI	Literature-reported	Cytoplasmic accumulation of long-chain coenzyme A esters activates KATP and inhibits Kir2.1 channels. J Physiol. 2006 Sep 1;575(Pt 2):433-42.	0	TC=1.A.2	.	inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ2 subfamily. 	.	.	Inward rectifier potassium channel transmembrane domain; Inward rectifier potassium channel C-terminal domain; Inward rectifier potassium channel N-terminal	PF01007; PF17655; PF08466	PF01007; IRK; PF17655; IRK_C; PF08466; IRK_N	1.A.2.1.2	The Inward Rectifier K<sup>+</sup> Channel (IRK-C) Family	hsa04725: Cholinergic synapse; hsa04921: Oxytocin signaling pathway; hsa04924: Renin secretion; hsa04971: Gastric acid secretion	R-HSA-1296041: Activation of G protein gated Potassium channels; R-HSA-1296053: Classical Kir channels; R-HSA-5576886: Phase 4 - resting membrane potential; R-HSA-9729555: Sensory perception of sour taste; R-HSA-997272: Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits	.	P63252
TTGM19J	Inward rectifier potassium channel Kir3.1 (KCNJ3)	P48549	KCNJ3_HUMAN	Inward rectifier potassium channel	"Potassium channel, inwardly rectifying subfamily J member 3; KCNJ3; Inward rectifier K(+) channel Kir3.1; GIRK1; G proteinactivated inward rectifier potassium channel 1"	KCNJ3	"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."	.	.	MSALRRKFGDDYQVVTTSSSGSGLQPQGPGQDPQQQLVPKKKRQRFVDKNGRCNVQHGNLGSETSRYLSDLFTTLVDLKWRWNLFIFILTYTVAWLFMASMWWVIAYTRGDLNKAHVGNYTPCVANVYNFPSAFLFFIETEATIGYGYRYITDKCPEGIILFLFQSILGSIVDAFLIGCMFIKMSQPKKRAETLMFSEHAVISMRDGKLTLMFRVGNLRNSHMVSAQIRCKLLKSRQTPEGEFLPLDQLELDVGFSTGADQLFLVSPLTICHVIDAKSPFYDLSQRSMQTEQFEIVVILEGIVETTGMTCQARTSYTEDEVLWGHRFFPVISLEEGFFKVDYSQFHATFEVPTPPYSVKEQEEMLLMSSPLIAPAITNSKERHNSVECLDGLDDITTKLPSKLQKITGREDFPKKLLRMSSTTSEKAYSLGDLPMKLQRISSVPGNSEEKLVSKTTKMLSDPMSQSVADLPPKLQKMAGGAARMEGNLPAKLRKMNSDRFT	Literature-reported	Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gbetagamma. Nature. 1998 Feb 19;391(6669):803-6.	0	.	.	.	.	.	.	.	.	.	.	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	R-HSA-1296041:Activation of G protein gated Potassium channels; R-HSA-997272:Inhibition  of voltage gated Ca2+ channels via Gbeta/gamma subunits	.	P48549
TTXF0ZW	Inward rectifier potassium channel Kir2.3 (KCNJ4)	P48050	KCNJ4_HUMAN	Inward rectifier potassium channel	"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"	KCNJ4	"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)."	.	3GJ9	MHGHSRNGQAHVPRRKRRNRFVKKNGQCNVYFANLSNKSQRYMADIFTTCVDTRWRYMLMIFSAAFLVSWLFFGLLFWCIAFFHGDLEASPGVPAAGGPAAGGGGAAPVAPKPCIMHVNGFLGAFLFSVETQTTIGYGFRCVTEECPLAVIAVVVQSIVGCVIDSFMIGTIMAKMARPKKRAQTLLFSHHAVISVRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPYMTQEGEYLPLDQRDLNVGYDIGLDRIFLVSPIIIVHEIDEDSPLYGMGKEELESEDFEIVVILEGMVEATAMTTQARSSYLASEILWGHRFEPVVFEEKSHYKVDYSRFHKTYEVAGTPCCSARELQESKITVLPAPPPPPSAFCYENELALMSQEEEEMEEEAAAAAAVAAGLGLEAGSKEEAGIIRMLEFGSHLDLERMQASLPLDNISYRRESAI	Literature-reported	Susceptibility of cloned K+ channels to reactive oxygen species. Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11796-800.	0	.	.	.	.	.	.	.	.	.	.	hsa04725: Cholinergic synapse; hsa04921: Oxytocin signaling pathway	R-HSA-1296041: Activation of G protein gated Potassium channels; R-HSA-1296053: Classical Kir channels; R-HSA-5576886: Phase 4 - resting membrane potential; R-HSA-997272: Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits	.	P48050
TTEO25X	Inward rectifier potassium channel Kir3.4 (KCNJ5)	P48544	KCNJ5_HUMAN	Inward rectifier potassium channel	"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"	KCNJ5	"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."	.	.	MAGDSRNAMNQDMEIGVTPWDPKKIPKQARDYVPIATDRTRLLAEGKKPRQRYMEKSGKCNVHHGNVQETYRYLSDLFTTLVDLKWRFNLLVFTMVYTVTWLFFGFIWWLIAYIRGDLDHVGDQEWIPCVENLSGFVSAFLFSIETETTIGYGFRVITEKCPEGIILLLVQAILGSIVNAFMVGCMFVKISQPKKRAETLMFSNNAVISMRDEKLCLMFRVGDLRNSHIVEASIRAKLIKSRQTKEGEFIPLNQTDINVGFDTGDDRLFLVSPLIISHEINQKSPFWEMSQAQLHQEEFEVVVILEGMVEATGMTCQARSSYMDTEVLWGHRFTPVLTLEKGFYEVDYNTFHDTYETNTPSCCAKELAEMKREGRLLQYLPSPPLLGGCAEAGLDAEAEQNEEDEPKGLGGSREARGSV	Clinical trial	Molecular basis for the inhibition of G protein-coupled inward rectifier K(+) channels by protein kinase C. Proc Natl Acad Sci U S A. 2004 Jan 27;101(4):1087-92.	21	.	.	.	.	.	.	.	.	.	.	hsa04713:Circadian entrainment; hsa04723:Retrograde endocannabinoid signaling; hsa04726:Serotonergic synapse; hsa04728:Dopaminergic synapse; hsa04915:Estrogen signaling pathway; hsa04921:Oxytocin signaling pathway; hsa05032:Morphine addiction	R-HSA-1296041:Activation of G protein gated Potassium channels; R-HSA-997272:Inhibition  of voltage gated Ca2+ channels via Gbeta/gamma subunits	.	P48544
TTTIBVP	Inward rectifier potassium channel Kir3.2 (KCNJ6)	P48051	KCNJ6_HUMAN	Inward rectifier potassium channel	"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"	KCNJ6	"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."	.	.	MAKLTESMTNVLEGDSMDQDVESPVAIHQPKLPKQARDDLPRHISRDRTKRKIQRYVRKDGKCNVHHGNVRETYRYLTDIFTTLVDLKWRFNLLIFVMVYTVTWLFFGMIWWLIAYIRGDMDHIEDPSWTPCVTNLNGFVSAFLFSIETETTIGYGYRVITDKCPEGIILLLIQSVLGSIVNAFMVGCMFVKISQPKKRAETLVFSTHAVISMRDGKLCLMFRVGDLRNSHIVEASIRAKLIKSKQTSEGEFIPLNQTDINVGYYTGDDRLFLVSPLIISHEINQQSPFWEISKAQLPKEELEIVVILEGMVEATGMTCQARSSYITSEILWGYRFTPVLTLEDGFYEVDYNSFHETYETSTPSLSAKELAELASRAELPLSWSVSSKLNQHAELETEEEEKNLEEQTERNGDVANLENESKV	Literature-reported	Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gbetagamma. Nature. 1998 Feb 19;391(6669):803-6.	0	.	.	.	.	.	.	.	.	.	.	hsa04713: Circadian entrainment; hsa04723: Retrograde endocannabinoid signaling; hsa04725: Cholinergic synapse; hsa04726: Serotonergic synapse; hsa04727: GABAergic synapse; hsa04728: Dopaminergic synapse; hsa04915: Estrogen signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04929: GnRH secretion; hsa05032: Morphine addiction	R-HSA-1296041: Activation of G protein gated Potassium channels; R-HSA-997272: Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits	.	P48051
TT4VHL6	Inward rectifier potassium channel Kir3.3 (KCNJ9)	Q92806	KCNJ9_HUMAN	Inward rectifier potassium channel	"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"	KCNJ9	"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)."	.	.	MAQENAAFSPGQEEPPRRRGRQRYVEKDGRCNVQQGNVRETYRYLTDLFTTLVDLQWRLSLLFFVLAYALTWLFFGAIWWLIAYGRGDLEHLEDTAWTPCVNNLNGFVAAFLFSIETETTIGYGHRVITDQCPEGIVLLLLQAILGSMVNAFMVGCMFVKISQPNKRAATLVFSSHAVVSLRDGRLCLMFRVGDLRSSHIVEASIRAKLIRSRQTLEGEFIPLHQTDLSVGFDTGDDRLFLVSPLVISHEIDAASPFWEASRRALERDDFEIVVILEGMVEATGMTCQARSSYLVDEVLWGHRFTSVLTLEDGFYEVDYASFHETFEVPTPSCSARELAEAAARLDAHLYWSIPSRLDEKVEEEGAGEGAGGEAGADKEQNGCLPPPESESKV	Literature-reported	"Regulation of cardiac Na+,Ca2+ exchange and KATP potassium channels by PIP2. Science. 1996 Aug 16;273(5277):956-9."	0	.	.	.	.	.	.	.	.	.	.	hsa04713: Circadian entrainment; hsa04723: Retrograde endocannabinoid signaling; hsa04726: Serotonergic synapse; hsa04728: Dopaminergic synapse; hsa04915: Estrogen signaling pathway; hsa04921: Oxytocin signaling pathway; hsa04929: GnRH secretion; hsa05032: Morphine addiction	R-HSA-1296041: Activation of G protein gated Potassium channels; R-HSA-997272: Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits	.	Q92806
TTHT87J	TWIK-related spinal cord potassium channel (TRESK)	Q7Z418	KCNKI_HUMAN	.	TWIK-related individual potassium channel; TRIK; TRESK; Potassium channel subfamily K member 18	KCNK18	"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)."	.	.	MEVSGHPQARRCCPEALGKLFPGLCFLCFLVTYALVGAVVFSAIEDGQVLVAADDGEFEKFLEELCRILNCSETVVEDRKQDLQGHLQKVKPQWFNRTTHWSFLSSLFFCCTVFSTVGYGYIYPVTRLGKYLCMLYALFGIPLMFLVLTDTGDILATILSTSYNRFRKFPFFTRPLLSKWCPKSLFKKKPDPKPADEAVPQIIISAEELPGPKLGTCPSRPSCSMELFERSHALEKQNTLQLPPQAMERSNSCPELVLGRLSYSIISNLDEVGQQVERLDIPLPIIALIVFAYISCAAAILPFWETQLDFENAFYFCFVTLTTIGFGDTVLEHPNFFLFFSIYIIVGMEIVFIAFKLVQNRLIDIYKNVMLFFAKGKFYHLVKK	Literature-reported	TRESK channel as a potential target to treat T-cell mediated immune dysfunction. Biochem Biophys Res Commun. 2009 Dec 25;390(4):1102-5.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1299344: TWIK-related spinal cord K+ channel (TRESK); R-HSA-5576886: Phase 4 - resting membrane potential	.	Q7Z418
TTGR91N	TWIK-related acid-sensitive potassium channel 1 (TASK1)	O14649	KCNK3_HUMAN	.	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	KCNK3	"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."	.	.	MKRQNVRTLALIVCTFTYLLVGAAVFDALESEPELIERQRLELRQQELRARYNLSQGGYEELERVVLRLKPHKAGVQWRFAGSFYFAITVITTIGYGHAAPSTDGGKVFCMFYALLGIPLTLVMFQSLGERINTLVRYLLHRAKKGLGMRRADVSMANMVLIGFFSCISTLCIGAAAFSHYEHWTFFQAYYYCFITLTTIGFGDYVALQKDQALQTQPQYVAFSFVYILTGLTVIGAFLNLVVLRFMTMNAEDEKRDAEHRALLTRNGQAGGGGGGGSAHTTDTASSTAAAGGGGFRNVYAEVLHFQSMCSCLWYKSREKLQYSIPMIIPRDLSTSDTCVEQSHSSPGGGGRYSDTPSRRCLCSGAPRSAISSVSTGLHSLSTFRGLMKRRSSV	Clinical trial	Antibodies and venom peptides: new modalities for ion channels. Nat Rev Drug Discov. 2019 May;18(5):339-357.	21	.	.	.	.	.	.	.	.	.	.	hsa04925:Aldosterone synthesis and secretion; hsa04927:Cortisol synthesis and secretion; hsa04934:Cushing syndrome	R-HSA-1299316: TWIK-releated acid-sensitive K+ channel (TASK); R-HSA-5576886: Phase 4 - resting membrane potential	.	O14649
TTL4FMB	TWIK-related acid-sensitive potassium channel 3 (TASK3)	Q9NPC2	KCNK9_HUMAN	.	Two pore potassium channel KT3.2; TWIK-related acid-sensitive K+ channel 3; KCNK9; Acid-sensitive potassium channel protein TASK-3	KCNK9	"pH-dependent, voltage-insensitive, background potassium channel protein."	.	6GHP; 4FR3; 3UX0; 3SPR; 3SP5	MKRQNVRTLSLIVCTFTYLLVGAAVFDALESDHEMREEEKLKAEEIRIKGKYNISSEDYRQLELVILQSEPHRAGVQWKFAGSFYFAITVITTIGYGHAAPGTDAGKAFCMFYAVLGIPLTLVMFQSLGERMNTFVRYLLKRIKKCCGMRNTDVSMENMVTVGFFSCMGTLCIGAAAFSQCEEWSFFHAYYYCFITLTTIGFGDYVALQTKGALQKKPLYVAFSFMYILVGLTVIGAFLNLVVLRFLTMNSEDERRDAEERASLAGNRNSMVIHIPEEPRPSRPRYKADVPDLQSVCSCTCYRSQDYGGRSVAPQNSFSAKLAPHYFHSISYKIEEISPSTLKNSLFPSPISSISPGLHSFTDHQRLMKRRKSV	Literature-reported	Oncogenic potential of TASK3 (Kcnk9) depends on K+ channel function. Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7803-7.	.	.	.	.	.	.	.	.	.	.	.	hsa04925: Aldosterone synthesis and secretion	R-HSA-1299316: TWIK-releated acid-sensitive K+ channel (TASK); R-HSA-5576886: Phase 4 - resting membrane potential	.	Q9NPC2
TTE87WJ	Calcium-activated potassium channel KCa1.1 (KCNMA1)	Q12791	KCMA1_HUMAN	Voltage-gated ion channel	"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"	KCNMA1	"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)."	.	3NAF; 3MT5; 2K44	MANGGGGGGGSSGGGGGGGGSSLRMSSNIHANHLSLDASSSSSSSSSSSSSSSSSSSSSSVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKTKEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRPKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERAFPLSSVSVNDCSTSFRAFEDEQPSTLSPKKKQRNGGMRNSPNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRQNRPKSRESRDKQKYVQEERL	Literature-reported	KCa1.1 channels regulate 1-integrin function and cell adhesion in rheumatoid arthritis fibroblast-like synoviocytes. FASEB J. 2017 Aug;31(8):3309-3320.	.	TC=1.A.1	Ligand gated ion channel	potassium channel family. Calcium-activated (TC 1.A.1.3) subfamily. KCa1.1/KCNMA1 sub-subfamily. 	.	.	Calcium-activated BK potassium channel alpha subunit; Ion transport protein	PF03493; PF00520	PF03493; BK_channel_a; PF00520; Ion_trans	.	.	hsa04022:cGMP-PKG signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04911:Insulin secretion; hsa04970:Salivary secretion; hsa04972:Pancreatic secretion	R-HSA-418457:cGMP effects	.	Q12791
TT1AQ50	Charybdotoxin receptor beta-4 (BKbeta4)	Q86W47	KCMB4_HUMAN	.	KCNMB4; Calcium activated potassium KCNMA1 (maxiK) channel	KCNMB4	"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."	.	5Y7L	MAKLRVAYEYTEAEDKSIRLGLFLIISGVVSLFIFGFCWLSPALQDLQATEANCTVLSVQQIGEVFECTFTCGADCRGTSQYPCVQVYVNNSESNSRALLHSDEHQLLTNPKCSYIPPCKRENQKNLESVMNWQQYWKDEIGSQPFTCYFNQHQRPDDVLLHRTHDEIVLLHCFLWPLVTFVVGVLIVVLTICAKSLAVKAEAMKKRKFS	Clinical trial	"Effect of 4-(5-chloro-2-hydroxyphenyl)-3-(2-hydroxyethyl)-6-(trifluoromethyl)-quinolin-2(1H)-one (BMS-223131), a novel opener of large conductance ... J Pharmacol Exp Ther. 2005 May;313(2):840-7."	21	.	.	.	.	.	.	.	.	.	.	hsa04022:cGMP-PKG signaling pathway; hsa04270:Vascular smooth muscle contraction; hsa04911:Insulin secretion; hsa04970:Salivary secretion; hsa04972:Pancreatic secretion	R-HSA-418457:cGMP effects	.	Q86W47
TT9R6BE	Calcium-activated potassium channel KCa2.1 (KCNN1)	Q92952	KCNN1_HUMAN	Voltage-gated ion channel	Small conductance calcium-activated potassium channel protein 1; SKCa1; SKCa 1; SK1; SK; KCa2.1	KCNN1	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).	.	.	MNSHSYNGSVGRPLGSGPGALGRDPPDPEAGHPPQPPHSPGLQVVVAKSEPARPSPGSPRGQPQDQDDDEDDEEDEAGRQRASGKPSNVGHRLGHRRALFEKRKRLSDYALIFGMFGIVVMVTETELSWGVYTKESLYSFALKCLISLSTAILLGLVVLYHAREIQLFMVDNGADDWRIAMTCERVFLISLELAVCAIHPVPGHYRFTWTARLAFTYAPSVAEADVDVLLSIPMFLRLYLLGRVMLLHSKIFTDASSRSIGALNKITFNTRFVMKTLMTICPGTVLLVFSISSWIIAAWTVRVCERYHDKQEVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLELTKAEKHVHNFMMDTQLTKRVKNAAANVLRETWLIYKHTRLVKKPDQARVRKHQRKFLQAIHQAQKLRSVKIEQGKLNDQANTLTDLAKTQTVMYDLVSELHAQHEELEARLATLESRLDALGASLQALPGLIAQAIRPPPPPLPPRPGPGPQDQAARSSPCRWTPVAPSDCG	Clinical trial	Pharmacological characterization of small-conductance Ca(2+)-activated K(+) channels stably expressed in HEK 293 cells. Br J Pharmacol. 2000 Mar;129(5):991-9.	16	.	.	.	.	.	.	.	.	.	.	hsa04911: Insulin secretion; hsa04929: GnRH secretion	R-HSA-1296052: Ca2+ activated K+ channels	.	Q92952
TT2T5M0	Calcium-activated potassium channel KCa2.2 (KCNN2)	Q9H2S1	KCNN2_HUMAN	Voltage-gated ion channel	Small conductance calcium-activated potassium channel protein 2; SKCa2; SKCa 2; SK2; KCa2.2	KCNN2	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.	.	6ALE; 5WC5; 5WBX; 5V02	MSSCRYNGGVMRPLSNLSASRRNLHEMDSEAQPLQPPASVGGGGGASSPSAAAAAAAAVSSSAPEIVVSKPEHNNSNNLALYGTGGGGSTGGGGGGGGSGHGSSSGTKSSKKKNQNIGYKLGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSWGAYDKASLYSLALKCLISLSTIILLGLIIVYHAREIQLFMVDNGADDWRIAMTYERIFFICLEILVCAIHPIPGNYTFTWTARLAFSYAPSTTTADVDIILSIPMFLRLYLIARVMLLHSKLFTDASSRSIGALNKINFNTRFVMKTLMTICPGTVLLVFSISLWIIAAWTVRACERYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPNTYCGKGVCLLTGIMGAGCTALVVAVVARKLELTKAEKHVHNFMMDTQLTKRVKNAAANVLRETWLIYKNTKLVKKIDHAKVRKHQRKFLQAIHQLRSVKMEQRKLNDQANTLVDLAKTQNIMYDMISDLNERSEDFEKRIVTLETKLETLIGSIHALPGLISQTIRQQQRDFIEAQMESYDKHVTYNAERSRSSSRRRRSSSTAPPTSSESS	Clinical trial	Block of rat brain recombinant SK channels by tricyclic antidepressants and related compounds. Eur J Pharmacol. 2000 Jul 28;401(1):1-7.	16	.	.	.	.	.	.	.	.	.	.	hsa04726: Serotonergic synapse; hsa04911: Insulin secretion; hsa04929: GnRH secretion; hsa04976: Bile secretion	R-HSA-1296052: Ca2+ activated K+ channels; R-HSA-9667769: Acetylcholine inhibits contraction of outer hair cells	.	Q9H2S1
TT9JH25	Calcium-activated potassium channel KCa2.3 (KCNN3)	Q9UGI6	KCNN3_HUMAN	Voltage-gated ion channel	Small conductance calcium-activated potassium channel protein 3; SKCa3; SKCa 3; SK3; KCa2.3; K3	KCNN3	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.	.	.	MDTSGHFHDSGVGDLDEDPKCPCPSSGDEQQQQQQQQQQQQPPPPAPPAAPQQPLGPSLQPQPPQLQQQQQQQQQQQQQQPPHPLSQLAQLQSQPVHPGLLHSSPTAFRAPPSSNSTAILHPSSRQGSQLNLNDHLLGHSPSSTATSGPGGGSRHRQASPLVHRRDSNPFTEIAMSSCKYSGGVMKPLSRLSASRRNLIEAETEGQPLQLFSPSNPPEIVISSREDNHAHQTLLHHPNATHNHQHAGTTASSTTFPKANKRKNQNIGYKLGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSWGLYSKDSMFSLALKCLISLSTIILLGLIIAYHTREVQLFVIDNGADDWRIAMTYERILYISLEMLVCAIHPIPGEYKFFWTARLAFSYTPSRAEADVDIILSIPMFLRLYLIARVMLLHSKLFTDASSRSIGALNKINFNTRFVMKTLMTICPGTVLLVFSISLWIIAAWTVRVCERYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLELTKAEKHVHNFMMDTQLTKRIKNAAANVLRETWLIYKHTKLLKKIDHAKVRKHQRKFLQAIHQLRSVKMEQRKLSDQANTLVDLSKMQNVMYDLITELNDRSEDLEKQIGSLESKLEHLTASFNSLPLLIADTLRQQQQQLLSAIIEARGVSVAVGTTHTPISDSPIGVSSTSFPTPYTSSSSC	Clinical trial	Pharmacological characterisation of the human small conductance calcium-activated potassium channel hSK3 reveals sensitivity to tricyclic antidepressants and antipsychotic phenothiazines. Neuropharmacology. 2001 May;40(6):772-83.	16	.	.	.	.	.	.	.	.	.	.	hsa04911: Insulin secretion; hsa04929: GnRH secretion	R-HSA-1296052: Ca2+ activated K+ channels	.	Q9UGI6
TT7M9I6	Calcium-activated potassium channel KCa3.1 (KCNN4)	O15554	KCNN4_HUMAN	Voltage-gated ion channel	SKCa4; SKCa 4; SK4; Putative Gardos channel; KCa4; KCa3.1; Intermediate conductance calcium-activated potassium channel protein 4; IKCa1; IK1	KCNN4	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.	.	6D42; 6CNO; 6CNN; 6CNM	MGGDLVLGLGALRRRKRLLEQEKSLAGWALVLAGTGIGLMVLHAEMLWFGGCSWALYLFLVKCTISISTFLLLCLIVAFHAKEVQLFMTDNGLRDWRVALTGRQAAQIVLELVVCGLHPAPVRGPPCVQDLGAPLTSPQPWPGFLGQGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYRSIGALNQVRFRHWFVAKLYMNTHPGRLLLGLTLGLWLTTAWVLSVAERQAVNATGHLSDTLWLIPITFLTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHNFMMDIQYTKEMKESAARVLQEAWMFYKHTRRKESHAARRHQRKLLAAINAFRQVRLKHRKLREQVNSMVDISKMHMILYDLQQNLSSSHRALEKQIDTLAGKLDALTELLSTALGPRQLPEPSQQSK	Clinical trial	Senicapoc (ICA-17043): a potential therapy for the prevention and treatment of hemolysis-associated complications in sickle cell anemia.Expert Opin Investig Drugs.2009 Feb;18(2):231-9.	21	TC=1.A.1	.	potassium channel KCNN family. KCa3.1/KCNN4 subfamily.	.	.	Calmodulin binding domain; Ion channel; Calcium-activated SK potassium channel	PF02888; PF07885; PF03530	PF02888; CaMBD; PF07885; Ion_trans_2; PF03530; SK_channel	1.A.1.16.2	The Voltage-gated Ion Channel (VIC) Superfamily 	hsa04911: Insulin secretion; hsa04929: GnRH secretion; hsa04970: Salivary secretion; hsa04974: Protein digestion and absorption	R-HSA-1296052: Ca2+ activated K+ channels	.	O15554
TT846HF	Voltage-gated potassium channel Kv7.1 (KCNQ1)	P51787	KCNQ1_HUMAN	Voltage-gated ion channel	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	KCNQ1	"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."	.	4V0C; 4UMO; 3HFE; 3HFC; 3BJ4	MAAASSPPRAERKRWGWGRLPGARRGSAGLAKKCPFSLELAEGGPAGGALYAPIAPGAPGPAPPASPAAPAAPPVASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGWKCFVYHFAVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGLWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKKKKFKLDKDNGVTPGEKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFMRTNSFAEDLDLEGETLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVTQLDQRLALITDMLHQLLSLHGGSTPGSGGPPREGGAHITQPCGSGGSVDPELFLPSNTLPTYEQLTVPRRGPDEGS	Successful	Indapamide induces apoptosis of GH3 pituitary cells independently of its inhibition of voltage-dependent K+ currents. Eur J Pharmacol. 2006 Apr 24;536(1-2):78-84.	34	TC=1.A.1	Voltage gated ion channel	potassium channel family. KQT (TC 1.A.1.15) subfamily. Kv7.1/KCNQ1 sub-subfamily. 	.	.	Ion transport protein; KCNQ voltage-gated potassium channel	PF00520; PF03520	PF00520; Ion_trans; PF03520; KCNQ_channel	1.A.1.15.6	The Voltage-gated Ion Channel (VIC) Superfamily 	hsa04261:Adrenergic signaling in cardiomyocytes; hsa04725:Cholinergic synapse; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04974:Protein digestion and absorption; hsa05110:Vibrio cholerae infection	R-HSA-1296072:Voltage gated Potassium channels	.	P51787
TTPXI3S	Voltage-gated potassium channel Kv7.2 (KCNQ2)	O43526	KCNQ2_HUMAN	Voltage-gated ion channel	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	KCNQ2	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.	.	6FEH; 6FEG; 5J03	MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQYYERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSKGSPCRGPLCGCCPGRSSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYFGAKEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQPQSHPRQGHGTSPVGDHGSLVRIPPPPAHERSLSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALNSCYAAVAPCAKVRPYIAEGESDTDSDLCTPCGPPPRSATGEGPFGDVGWAGPRK	Literature-reported	Voltage-gated Potassium Channels as Therapeutic Drug Targets	2.1	.	.	.	.	.	.	.	.	.	.	hsa04725:Cholinergic synapse	R-HSA-1296072:Voltage gated Potassium channels; R-HSA-445095:Interaction between L1 and Ankyrins	.	O43526
TTIVDM3	Voltage-gated potassium channel Kv7.3 (KCNQ3)	O43525	KCNQ3_HUMAN	Voltage-gated ion channel	Voltage-gated potassium channel subunit Kv7.3; Potassium channel alpha subunit KvLQT3; Potassium channel KQT-like 3; KQT-like 3; KCNQ3; K+ channel KCNQ3	KCNQ3	"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."	.	5J03	MGLKARRAAGAAGGGGDGGGGGGGAANPAGGDAAAAGDEERKVGLAPGDVEQVTLALGAGADKDGTLLLEGGGRDEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRGWALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEVDAQGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQEQHRQKHFEKRRKPAAELIQAAWRYYATNPNRIDLVATWRFYESVVSFPFFRKEQLEAASSQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKAYAFWQSSEDAGTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRPYDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTFPSQQSPRNEPYVARPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERLQVQVTEYYPTKGTSSPAEAEKKEDNRYSDLKTIICNYSETGPPEPPYSFHQVTIDKVSPYGFFAHDPVNLPRGGPSSGKVQATPPSSATTYVERPTVLPILTLLDSRVSCHSQADLQGPYSDRISPRQRRSITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPNGGSSWMREKRYLAEGETDTDTDPFTPSGSMPLSSTGDGISDSVWTPSNKPI	Clinical trial	The M-channel blocker linopirdine is an agonist of the capsaicin receptor TRPV1. J Pharmacol Sci. 2010;114(3):332-40.	25	.	.	.	.	.	.	.	.	.	.	hsa04725:Cholinergic synapse	R-HSA-1296072:Voltage gated Potassium channels; R-HSA-445095:Interaction between L1 and Ankyrins	.	O43525
TT8HGRW	Voltage-gated potassium channel Kv7.4 (KCNQ4)	P56696	KCNQ4_HUMAN	Voltage-gated ion channel	Voltage-gated potassium channel subunit Kv7.4; Potassium channel alpha subunit KvLQT4; KQT-like 4; KCNQ4	KCNQ4	"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."	.	6N5W; 4GOW; 2OVC	MAEAPPRRLGLGPPPGDAPRAELVALTAVQSEQGEAGGGGSPRRLGLLGSPLPPGAPLPGPGSGSGSACGQRSSAAHKRYRRLQNWVYNVLERPRGWAFVYHVFIFLLVFSCLVLSVLSTIQEHQELANECLLILEFVMIVVFGLEYIVRVWSAGCCCRYRGWQGRFRFARKPFCVIDFIVFVASVAVIAAGTQGNIFATSALRSMRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFASFLVYLAEKDANSDFSSYADSLWWGTITLTTIGYGDKTPHTWLGRVLAAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRMPAANLIQAAWRLYSTDMSRAYLTATWYYYDSILPSFRELALLFEHVQRARNGGLRPLEVRRAPVPDGAPSRYPPVATCHRPGSTSFCPGESSRMGIKDRIRMGSSQRRTGPSKQHLAPPTMPTSPSSEQVGEATSPTKVQKSWSFNDRTRFRASLRLKPRTSAEDAPSEEVAEEKSYQCELTVDDIMPAVKTVIRSIRILKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLGRIKSLQTRVDQIVGRGPGDRKAREKGDKGPSDAEVVDEISMMGRVVKVEKQVQSIEHKLDLLLGFYSRCLRSGTSASLGAVQVPLFDPDITSDYHSPVDHEDISVSAQTLSISRSVSTNMD	Literature-reported	Identification of novel KCNQ4 openers by a high-throughput fluorescence-based thallium flux assay. Anal Biochem. 2011 Nov 1;418(1):66-72.	0	.	.	.	.	.	.	.	.	.	.	hsa04725:Cholinergic synapse	R-HSA-1296072:Voltage gated Potassium channels	.	P56696
TTWVL5Q	Voltage-gated potassium channel Kv7.5 (KCNQ5)	Q9NR82	KCNQ5_HUMAN	Voltage-gated ion channel	Voltage-gated potassium channel subunit Kv7.5; Potassium voltage-gated channel subfamily KQT member 5; Potassium channel subunit alpha KvLQT5; KQT-like 5	KCNQ5	"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."	.	6B8Q	MPRHHAGGEEGGAAGLWVKSGAAAAAAGGGRLGSGMKDVESGRGRVLLNSAAARGDGLLLLGTRAATLGGGGGGLRESRRGKQGARMSLLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFIYHAFVFLLVFGCLILSVFSTIPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTIVLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTPLTWLGRLLSAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAANLIQCVWRSYAADEKSVSIATWKPHLKALHTCSPTKKEQGEASSSQKLSFKERVRMASPRGQSIKSRQASVGDRRSPSTDITAEGSPTKVQKSWSFNDRTRFRPSLRLKSSQPKPVIDADTALGTDDVYDEKGCQCDVSVEDLTPPLKTVIRAIRIMKFHVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQILGKGQITSDKKSREKITAEHETTDDLSMLGRVVKVEKQVQSIESKLDCLLDIYQQVLRKGSASALALASFQIPPFECEQTSDYQSPVDSKDLSGSAQNSGCLSRSTSANISRGLQFILTPNEFSAQTFYALSPTMHSQATQVPISQSDGSAVAATNTIANQINTAPKPAAPTTLQIPPPLPAIKHLPRPETLHPNPAGLQESISDVTTCLVASKENVQVAQSNLTKDRSMRKSFDMGGETLLSVCPMVPKDLGKSLSVQNLIRSTEELNIQLSGSESSGSRGSQDFYPKWRESKLFITDEEVGPEETETDTFDAAPQPAREAAFASDSLRTGRSRSSQSICKAGESTDALSLPHVKLK	Literature-reported	"KCNQ5, a novel potassium channel broadly expressed in brain, mediates M-type currents. J Biol Chem. 2000 Aug 4;275(31):24089-95."	0	TC=1.A.1	.	potassium channel family. KQT (TC 1.A.1.15) subfamily. Kv7.5/KCNQ5 sub-subfamily. 	.	.	Ion transport protein; KCNQ voltage-gated potassium channel	PF00520; PF03520	PF00520; Ion_trans; PF03520; KCNQ_channel	.	.	hsa04725: Cholinergic synapse	R-HSA-1296072: Voltage gated Potassium channels	.	Q9NR82
TTGJFK1	Calcium-activated potassium channel KCa4.1 (KCNT1)	Q5JUK3	KCNT1_HUMAN	Voltage-gated ion channel	Potassium channel subfamily T member 1; KIAA1422; KCa4.1	KCNT1	"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)."	.	.	MARAKLPRSPSEGKAGPGGAPAGAAAPEEPHGLSPLLPARGGGSVGSDVGQRLPVEDFSLDSSLSQVQVEFYVNENTFKERLKLFFIKNQRSSLRIRLFNFSLKLLTCLLYIVRVLLDDPALGIGCWGCPKQNYSFNDSSSEINWAPILWVERKMTLWAIQVIVAIISFLETMLLIYLSYKGNIWEQIFRVSFVLEMINTLPFIITIFWPPLRNLFIPVFLNCWLAKHALENMINDFHRAILRTQSAMFNQVLILFCTLLCLVFTGTCGIQHLERAGENLSLLTSFYFCIVTFSTVGYGDVTPKIWPSQLLVVIMICVALVVLPLQFEELVYLWMERQKSGGNYSRHRAQTEKHVVLCVSSLKIDLLMDFLNEFYAHPRLQDYYVVILCPTEMDVQVRRVLQIPLWSQRVIYLQGSALKDQDLMRAKMDNGEACFILSSRNEVDRTAADHQTILRAWAVKDFAPNCPLYVQILKPENKFHVKFADHVVCEEECKYAMLALNCICPATSTLITLLVHTSRGQEGQESPEQWQRMYGRCSGNEVYHIRMGDSKFFREYEGKSFTYAAFHAHKKYGVCLIGLKREDNKSILLNPGPRHILAASDTCFYINITKEENSAFIFKQEEKRKKRAFSGQGLHEGPARLPVHSIIASMGTVAMDLQGTEHRPTQSGGGGGGSKLALPTENGSGSRRPSIAPVLELADSSALLPCDLLSDQSEDEVTPSDDEGLSVVEYVKGYPPNSPYIGSSPTLCHLLPVKAPFCCLRLDKGCKHNSYEDAKAYGFKNKLIIVSAETAGNGLYNFIVPLRAYYRSRKELNPIVLLLDNKPDHHFLEAICCFPMVYYMEGSVDNLDSLLQCGIIYADNLVVVDKESTMSAEEDYMADAKTIVNVQTMFRLFPSLSITTELTHPSNMRFMQFRAKDSYSLALSKLEKRERENGSNLAFMFRLPFAAGRVFSISMLDTLLYQSFVKDYMITITRLLLGLDTTPGSGYLCAMKITEGDLWIRTYGRLFQKLCSSSAEIPIGIYRTESHVFSTSESQISVNVEDCEDTREVKGPWGSRAGTGGSSQGRHTGGGDPAEHPLLRRKSLQWARRLSRKAPKQAGRAAAAEWISQQRLSLYRRSERQELSELVKNRMKHLGLPTTGYEDVANLTASDVMNRVNLGYLQDEMNDHQNTLSYVLINPPPDTRLEPSDIVYLIRSDPLAHVASSSQSRKSSCSHKLSSCNPETRDETQL	Clinical trial	Opposite regulation of Slick and Slack K+ channels by neuromodulators. J Neurosci. 2006 May 10;26(19):5059-68.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	Q5JUK3
TTLU5FO	Calcium-activated potassium channel KCa4.2 (KCNT2)	Q6UVM3	KCNT2_HUMAN	Voltage-gated ion channel	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	KCNT2	"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."	.	.	MVDLESEVPPLPPRYRFRDLLLGDQGWQNDDRVQVEFYMNENTFKERLKLFFIKNQRSSLRIRLFNFSLKLLSCLLYIIRVLLENPSQGNEWSHIFWVNRSLPLWGLQVSVALISLFETILLGYLSYKGNIWEQILRIPFILEIINAVPFIISIFWPSLRNLFVPVFLNCWLAKHALENMINDLHRAIQRTQSAMFNQVLILISTLLCLIFTCICGIQHLERIGKKLNLFDSLYFCIVTFSTVGFGDVTPETWSSKLFVVAMICVALVVLPIQFEQLAYLWMERQKSGGNYSRHRAQTEKHVVLCVSSLKIDLLMDFLNEFYAHPRLQDYYVVILCPTEMDVQVRRVLQIPMWSQRVIYLQGSALKDQDLLRAKMDDAEACFILSSRCEVDRTSSDHQTILRAWAVKDFAPNCPLYVQILKPENKFHIKFADHVVCEEEFKYAMLALNCICPATSTLITLLVHTSRGQEGQQSPEQWQKMYGRCSGNEVYHIVLEESTFFAEYEGKSFTYASFHAHKKFGVCLIGVRREDNKNILLNPGPRYIMNSTDICFYINITKEENSAFKNQDQQRKSNVSRSFYHGPSRLPVHSIIASMGTVAIDLQDTSCRSASGPTLSLPTEGSKEIRRPSIAPVLEVADTSSIQTCDLLSDQSEDETTPDEEMSSNLEYAKGYPPYSPYIGSSPTFCHLLHEKVPFCCLRLDKSCQHNYYEDAKAYGFKNKLIIVAAETAGNGLYNFIVPLRAYYRPKKELNPIVLLLDNPPDMHFLDAICWFPMVYYMVGSIDNLDDLLRCGVTFAANMVVVDKESTMSAEEDYMADAKTIVNVQTLFRLFSSLSIITELTHPANMRFMQFRAKDCYSLALSKLEKKERERGSNLAFMFRLPFAAGRVFSISMLDTLLYQSFVKDYMISITRLLLGLDTTPGSGFLCSMKITADDLWIRTYARLYQKLCSSTGDVPIGIYRTESQKLTTSESQISISVEEWEDTKDSKEQGHHRSNHRNSTSSDQSDHPLLRRKSMQWARRLSRKGPKHSGKTAEKITQQRLNLYRRSERQELAELVKNRMKHLGLSTVGYDEMNDHQSTLSYILINPSPDTRIELNDVVYLIRPDPLAYLPNSEPSRRNSICNVTGQDSREETQL	Clinical trial	Opposite regulation of Slick and Slack K+ channels by neuromodulators. J Neurosci. 2006 May 10;26(19):5059-68.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	Q6UVM3
TTI9XK6	Calcium-activated potassium channel KCa5.1 (KCNU1)	A8MYU2	KCNU1_HUMAN	Voltage-gated ion channel	"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"	KCNU1	"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."	.	4HPF	MFQTKLRNETWEDLPKMSCTTEIQAAFILSSFVTFFSGLIILLIFRLIWRSVKKWQIIKGTGIILELFTSGTIARSHVRSLHFQGQFRDHIEMLLSAQTFVGQVLVILVFVLSIGSLIIYFINSADPVGSCSSYEDKTIPIDLVFNAFFSFYFGLRFMAADDKIKFWLEMNSIVDIFTIPPTFISYYLKSNWLGLRFLRALRLLELPQILQILRAIKTSNSVKFSKLLSIILSTWFTAAGFIHLVENSGDPWLKGRNSQNISYFESIYLVMATTSTVGFGDVVAKTSLGRTFIMFFTLGSLILFANYIPEMVELFANKRKYTSSYEALKGKKFIVVCGNITVDSVTAFLRNFLRDKSGEINTEIVFLGETPPSLELETIFKCYLAYTTFISGSAMKWEDLRRVAVESAEACLIIANPLCSDSHAEDISNIMRVLSIKNYDSTTRIIIQILQSHNKVYLPKIPSWNWDTGDNIICFAELKLGFIAQGCLVPGLCTFLTSLFVEQNKKVMPKQTWKKHFLNSMKNKILTQRLSDDFAGMSFPEVARLCFLKMHLLLIAIEYKSLFTDGFCGLILNPPPQVRIRKNTLGFFIAETPKDVRRALFYCSVCHDDVFIPELITNCGCKSRSRQHITVPSVKRMKKCLKGISSRISGQDSPPRVSASTSSISNFTTRTLQHDVEQDSDQLDSSGMFHWCKPTSLDKVTLKRTGKSKYKFRNHIVACVFGDAHSAPMGLRNFVMPLRASNYTRKELKDIVFIGSLDYLQREWRFLWNFPQIYILPGCALYSGDLHAANIEQCSMCAVLSPPPQPSSNQTLVDTEAIMATLTIGSLQIDSSSDPSPSVSEETPGYTNGHNEKSNCRKVPILTELKNPSNIHFIEQLGGLEGSLQETNLHLSTAFSTGTVFSGSFLDSLLATAFYNYHVLELLQMLVTGGVSSQLEQHLDKDKVYGVADSCTSLLSGRNRCKLGLLSLHETILSDVNPRNTFGQLFCGSLDLFGILCVGLYRIIDEEELNPENKRFVITRPANEFKLLPSDLVFCAIPFSTACYKRNEEFSLQKSYEIVNKASQTTETHSDTNCPPTIDSVTETLYSPVYSYQPRTNSLSFPKQIAWNQSRTNSIISSQIPLGDNAKENERKTSDEVYDEDPFAYSEPL	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 387).	0	.	.	.	.	.	.	.	.	.	.	hsa04022: cGMP-PKG signaling pathway; hsa04270: Vascular smooth muscle contraction; hsa04911: Insulin secretion	R-HSA-1300642: Sperm Motility And Taxes	.	A8MYU2
TTNR0UQ	Lysine-specific histone demethylase 1 (LSD)	O60341	KDM1A_HUMAN	CH-NH(2) donor oxidoreductase	Lysine-specific histone demethylase 1A; LSD1; KIAA0601; KDM1; Flavin-containing amine oxidase domain-containing protein 2; BRAF35-HDAC complex protein BHC110; AOF2	KDM1A	"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."	EC 1.-.-.-	6NQU; 6NQM; 5YJB; 5X60; 5LHI	MLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	EC:1.4	Paired donor oxidoreductase	flavin monoamine oxidase family.	1.-.-.-	Oxidoreductases	Flavin containing amine oxidoreductase; SWIRM domain	PF01593; PF04433	PF01593; Amino_oxidase; PF04433; SWIRM	.	.	hsa04714: Thermogenesis	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	MetaCyc:ENSG00000004487-MON	O60341
TT8VP2T	Lysine-specific histone demethylase 1B (KDM1B)	Q8NB78	KDM1B_HUMAN	CH-NH(2) donor oxidoreductase	Lysine-specific histone demethylase 2; LSD2; Flavin-containing amine oxidase domain-containing protein 1; C6orf193; AOF1	KDM1B	"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."	EC 1.-.-.-	6R25; 6R1U; 4HSU; 4GUU; 4GUT	MATPRGRTKKKASFDHSPDSLPLRSSGRQAKKKATETTDEDEDGGSEKKYRKCEKAGCTATCPVCFASASERCAKNGYTSRWYHLSCGEHFCNECFDHYYRSHKDGYDKYTTWKKIWTSNGKTEPSPKAFMADQQLPYWVQCTKPECRKWRQLTKEIQLTPQIAKTYRCGMKPNTAIKPETSDHCSLPEDLRVLEVSNHWWYSMLILPPLLKDSVAAPLLSAYYPDCVGMSPSCTSTNRAAATGNASPGKLEHSKAALSVHVPGMNRYFQPFYQPNECGKALCVRPDVMELDELYEFPEYSRDPTMYLALRNLILALWYTNCKEALTPQKCIPHIIVRGLVRIRCVQEVERILYFMTRKGLINTGVLSVGADQYLLPKDYHNKSVIIIGAGPAGLAAARQLHNFGIKVTVLEAKDRIGGRVWDDKSFKGVTVGRGAQIVNGCINNPVALMCEQLGISMHKFGERCDLIQEGGRITDPTIDKRMDFHFNALLDVVSEWRKDKTQLQDVPLGEKIEEIYKAFIKESGIQFSELEGQVLQFHLSNLEYACGSNLHQVSARSWDHNEFFAQFAGDHTLLTPGYSVIIEKLAEGLDIQLKSPVQCIDYSGDEVQVTTTDGTGYSAQKVLVTVPLALLQKGAIQFNPPLSEKKMKAINSLGAGIIEKIALQFPYRFWDSKVQGADFFGHVPPSASKRGLFAVFYDMDPQKKHSVLMSVIAGEAVASVRTLDDKQVLQQCMATLRELFKEQEVPDPTKYFVTRWSTDPWIQMAYSFVKTGGSGEAYDIIAEDIQGTVFFAGEATNRHFPQTVTGAYLSGVREASKIAAF	Patented-recorded	LSD1 inhibitors: a patent review (2010-2015).Expert Opin Ther Pat. 2016 May;26(5):565-80.	15.5	EC:1.4	Flavin monoamine oxidase family	flavin monoamine oxidase family.	1.-.-.-	Oxidoreductases	Flavin containing amine oxidoreductase; SWIRM domain; CW-type Zinc Finger	PF01593; PF04433; PF07496	PF01593; Amino_oxidase; PF04433; SWIRM; PF07496; zf-CW	.	.	.	R-HSA-3214842: HDMs demethylate histones; R-HSA-5689603: UCH proteinases; R-HSA-9029569: NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux	MetaCyc:ENSG00000165097-MON	Q8NB78
TT8XTY2	Lysine-specific demethylase 2A (KDM2A)	Q9Y2K7	KDM2A_HUMAN	.	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	KDM2A	"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."	EC 1.14.11.27	6C16; 6BYH; 4BBQ; 2YU2; 2YU1	MEPEEERIRYSQRLRGTMRRRYEDDGISDDEIEGKRTFDLEEKLHTNKYNANFVTFMEGKDFNVEYIQRGGLRDPLIFKNSDGLGIKMPDPDFTVNDVKMCVGSRRMVDVMDVNTQKGIEMTMAQWTRYYETPEEEREKLYNVISLEFSHTRLENMVQRPSTVDFIDWVDNMWPRHLKESQTESTNAILEMQYPKVQKYCLMSVRGCYTDFHVDFGGTSVWYHIHQGGKVFWLIPPTAHNLELYENWLLSGKQGDIFLGDRVSDCQRIELKQGYTFVIPSGWIHAVYTPTDTLVFGGNFLHSFNIPMQLKIYNIEDRTRVPNKFRYPFYYEMCWYVLERYVYCITNRSHLTKEFQKESLSMDLELNGLESGNGDEEAVDREPRRLSSRRSVLTSPVANGVNLDYDGLGKTCRSLPSLKKTLAGDSSSDCSRGSHNGQVWDPQCAPRKDRQVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEELANSDPKLALTGVPIVQWPKRDKLKFPTRPKVRVPTIPITKPHTMKPAPRLTPVRPAAASPIVSGARRRRVRCRKCKACVQGECGVCHYCRDMKKFGGPGRMKQSCVLRQCLAPRLPHSVTCSLCGEVDQNEETQDFEKKLMECCICNEIVHPGCLQMDGEGLLNEELPNCWECPKCYQEDSSEKAQKRKMEESDEEAVQAKVLRPLRSCDEPLTPPPHSPTSMLQLIHDPVSPRGMVTRSSPGAGPSDHHSASRDERFKRRQLLRLQATERTMVREKENNPSGKKELSEVEKAKIRGSYLTVTLQRPTKELHGTSIVPKLQAITASSANLRHSPRVLVQHCPARTPQRGDEEGLGGEEEEEEEEEEEDDSAEEGGAARLNGRGSWAQDGDESWMQREVWMSVFRYLSRRELCECMRVCKTWYKWCCDKRLWTKIDLSRCKAIVPQALSGIIKRQPVSLDLSWTNISKKQLTWLVNRLPGLKDLLLAGCSWSAVSALSTSSCPLLRTLDLRWAVGIKDPQIRDLLTPPADKPGQDNRSKLRNMTDFRLAGLDITDATLRLIIRHMPLLSRLDLSHCSHLTDQSSNLLTAVGSSTRYSLTELNMAGCNKLTDQTLIYLRRIANVTLIDLRGCKQITRKACEHFISDLSINSLYCLSDEKLIQKIS	Literature-reported	Selective small molecule probes for the hypoxia inducible factor (HIF) prolyl hydroxylases. ACS Chem Biol. 2013 Jul 19;8(7):1488-96.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-3214842: HDMs demethylate histones	MetaCyc:HS10620-MON	Q9Y2K7
TTKXS4A	Lysine-specific demethylase 3A (KDM3A)	Q9Y4C1	KDM3A_HUMAN	Paired donor oxygen oxidoreductase	TSGA; KIAA0742; Jumonji domain-containing protein 1A; JmjC domain-containing histone demethylation protein 2A; JMJD1A; JMJD1; JHDM2A	KDM3A	"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."	EC 1.14.11.-	.	MVLTLGESWPVLVGRRFLSLSAADGSDGSHDSWDVERVAEWPWLSGTIRAVSHTDVTKKDLKVCVEFDGESWRKRRWIEVYSLLRRAFLVEHNLVLAERKSPEISERIVQWPAITYKPLLDKAGLGSITSVRFLGDQQRVFLSKDLLKPIQDVNSLRLSLTDNQIVSKEFQALIVKHLDESHLLKGDKNLVGSEVKIYSLDPSTQWFSATVINGNPASKTLQVNCEEIPALKIVDPSLIHVEVVHDNLVTCGNSARIGAVKRKSSENNGTLVSKQAKSCSEASPSMCPVQSVPTTVFKEILLGCTAATPPSKDPRQQSTPQAANSPPNLGAKIPQGCHKQSLPEEISSCLNTKSEALRTKPDVCKAGLLSKSSQIGTGDLKILTEPKGSCTQPKTNTDQENRLESVPQALTGLPKECLPTKASSKAELEIANPPELQKHLEHAPSPSDVSNAPEVKAGVNSDSPNNCSGKKVEPSALACRSQNLKESSVKVDNESCCSRSNNKIQNAPSRKSVLTDPAKLKKLQQSGEAFVQDDSCVNIVAQLPKCRECRLDSLRKDKEQQKDSPVFCRFFHFRRLQFNKHGVLRVEGFLTPNKYDNEAIGLWLPLTKNVVGIDLDTAKYILANIGDHFCQMVISEKEAMSTIEPHRQVAWKRAVKGVREMCDVCDTTIFNLHWVCPRCGFGVCVDCYRMKRKNCQQGAAYKTFSWLKCVKSQIHEPENLMPTQIIPGKALYDVGDIVHSVRAKWGIKANCPCSNRQFKLFSKPASKEDLKQTSLAGEKPTLGAVLQQNPSVLEPAAVGGEAASKPAGSMKPACPASTSPLNWLADLTSGNVNKENKEKQPTMPILKNEIKCLPPLPPLSKSSTVLHTFNSTILTPVSNNNSGFLRNLLNSSTGKTENGLKNTPKILDDIFASLVQNKTTSDLSKRPQGLTIKPSILGFDTPHYWLCDNRLLCLQDPNNKSNWNVFRECWKQGQPVMVSGVHHKLNSELWKPESFRKEFGEQEVDLVNCRTNEIITGATVGDFWDGFEDVPNRLKNEKEPMVLKLKDWPPGEDFRDMMPSRFDDLMANIPLPEYTRRDGKLNLASRLPNYFVRPDLGPKMYNAYGLITPEDRKYGTTNLHLDVSDAANVMVYVGIPKGQCEQEEEVLKTIQDGDSDELTIKRFIEGKEKPGALWHIYAAKDTEKIREFLKKVSEEQGQENPADHDPIHDQSWYLDRSLRKRLHQEYGVQGWAIVQFLGDVVFIPAGAPHQVHNLYSCIKVAEDFVSPEHVKHCFWLTQEFRYLSQTHTNHEDKLQVKNVIYHAVKDAVAMLKASESSFGKP	Literature-reported	A cell-permeable ester derivative of the JmjC histone demethylase inhibitor IOX1. ChemMedChem. 2014 Mar;9(3):566-71.	0	EC:1.14	.	JHDM2 histone demethylase family.	1.14.11.-	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	"JmjC domain, hydroxylase"	PF02373	PF02373; JmjC	.	.	hsa04714: Thermogenesis	R-HSA-3214842: HDMs demethylate histones; R-HSA-9029569: NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux	MetaCyc:ENSG00000115548-MON	Q9Y4C1
TTZHPB8	Lysine-specific demethylase 4A (KDM4A)	O75164	KDM4A_HUMAN	Paired donor oxygen oxidoreductase	KIAA0677; Jumonji domain-containing protein 2A; JmjC domain-containing histone demethylation protein 3A; JMJD2A; JMJD2; JHDM3A	KDM4A	"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."	EC 1.14.11.-	6H8P; 6G5X; 6G5W; 6CG2; 6CG1	MASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKNLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRKFQPERYKLWKAGKDNTVIDHTLPTPEAAEFLKESELPPRAGNEEECPEEDMEGVEDGEEGDLKTSLAKHRIGTKRHRVCLEIPQEVSQSELFPKEDLSSEQYEMTECPAALAPVRPTHSSVRQVEDGLTFPDYSDSTEVKFEELKNVKLEEEDEEEEQAAAALDLSVNPASVGGRLVFSGSKKKSSSSLGSGSSRDSISSDSETSEPLSCRAQGQTGVLTVHSYAKGDGRVTVGEPCTRKKGSAARSFSERELAEVADEYMFSLEENKKSKGRRQPLSKLPRHHPLVLQECVSDDETSEQLTPEEEAEETEAWAKPLSQLWQNRPPNFEAEKEFNETMAQQAPHCAVCMIFQTYHQVEFGGFNQNCGNASDLAPQKQRTKPLIPEMCFTSTGCSTDINLSTPYLEEDGTSILVSCKKCSVRVHASCYGVPPAKASEDWMCSRCSANALEEDCCLCSLRGGALQRANDDRWVHVSCAVAILEARFVNIAERSPVDVSKIPLPRFKLKCIFCKKRRKRTAGCCVQCSHGRCPTAFHVSCAQAAGVMMQPDDWPFVVFITCFRHKIPNLERAKGALQSITAGQKVISKHKNGRFYQCEVVRLTTETFYEVNFDDGSFSDNLYPEDIVSQDCLQFGPPAEGEVVQVRWTDGQVYGAKFVASHPIQMYQVEFEDGSQLVVKRDDVYTLDEELPKRVKSRLSVASDMRFNEIFTEKEVKQEKKRQRVINSRYREDYIEPALYRAIME	Patented-recorded	KDM4 histone demethylase inhibitors for anti-cancer agents: a patent review.Expert Opin Ther Pat. 2015 Feb;25(2):135-44.	15.5	EC:1.14	JHDM3 histone demethylase family	JHDM3 histone demethylase family.	1.14.11.-	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	"JmjC domain, hydroxylase; jmjN domain; Jumonji domain-containing protein 2A Tudor domain"	PF02373; PF02375; PF18104	PF02373; JmjC; PF02375; JmjN; PF18104; Tudor_2	.	.	.	R-HSA-3214842: HDMs demethylate histones; R-HSA-5693565: Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks; R-HSA-9029569: NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux	MetaCyc:ENSG00000066135-MON	O75164
TTV8CRH	Lysine-specific demethylase 4C (KDM4C)	Q9H3R0	KDM4C_HUMAN	Paired donor oxygen oxidoreductase	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	KDM4C	"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."	EC 1.14.11.-	5KR7; 5FJK; 5FJH; 4XDP; 4XDO	MEVAEVESPLNPSCKIMTFRPSMEEFREFNKYLAYMESKGAHRAGLAKVIPPKEWKPRQCYDDIDNLLIPAPIQQMVTGQSGLFTQYNIQKKAMTVKEFRQLANSGKYCTPRYLDYEDLERKYWKNLTFVAPIYGADINGSIYDEGVDEWNIARLNTVLDVVEEECGISIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAQGFFPSSSQGCDAFLRHKMTLISPSVLKKYGIPFDKITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATVRWIDYGKVAKLCTCRKDMVKISMDIFVRKFQPDRYQLWKQGKDIYTIDHTKPTPASTPEVKAWLQRRRKVRKASRSFQCARSTSKRPKADEEEEVSDEVDGAEVPNPDSVTDDLKVSEKSEAAVKLRNTEASSEEESSASRMQVEQNLSDHIKLSGNSCLSTSVTEDIKTEDDKAYAYRSVPSISSEADDSIPLSSGYEKPEKSDPSELSWPKSPESCSSVAESNGVLTEGEESDVESHGNGLEPGEIPAVPSGERNSFKVPSIAEGENKTSKSWRHPLSRPPARSPMTLVKQQAPSDEELPEVLSIEEEVEETESWAKPLIHLWQTKSPNFAAEQEYNATVARMKPHCAICTLLMPYHKPDSSNEENDARWETKLDEVVTSEGKTKPLIPEMCFIYSEENIEYSPPNAFLEEDGTSLLISCAKCCVRVHASCYGIPSHEICDGWLCARCKRNAWTAECCLCNLRGGALKQTKNNKWAHVMCAVAVPEVRFTNVPERTQIDVGRIPLQRLKLKCIFCRHRVKRVSGACIQCSYGRCPASFHVTCAHAAGVLMEPDDWPYVVNITCFRHKVNPNVKSKACEKVISVGQTVITKHRNTRYYSCRVMAVTSQTFYEVMFDDGSFSRDTFPEDIVSRDCLKLGPPAEGEVVQVKWPDGKLYGAKYFGSNIAHMYQVEFEDGSQIAMKREDIYTLDEELPKRVKARFSTASDMRFEDTFYGADIIQGERKRQRVLSSRFKNEYVADPVYRTFLKSSFQKKCQKRQ	Patented-recorded	KDM4 histone demethylase inhibitors for anti-cancer agents: a patent review.Expert Opin Ther Pat. 2015 Feb;25(2):135-44.	15.5	EC:1.14	.	JHDM3 histone demethylase family.	1.14.11.-	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	"JmjC domain, hydroxylase; jmjN domain; Jumonji domain-containing protein 2A Tudor domain"	PF02373; PF02375; PF18104	PF02373; JmjC; PF02375; JmjN; PF18104; Tudor_2	.	.	.	R-HSA-3214842: HDMs demethylate histones; R-HSA-5625886: Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3	MetaCyc:ENSG00000107077-MON	Q9H3R0
TTWAQBO	Lysine-specific demethylase 4E (KDM4E)	B2RXH2	KDM4E_HUMAN	Paired donor oxygen oxidoreductase	Lysine-specific demethylase 4D-like; KDM4DL; KDM4D-like protein	KDM4E	"Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code."	EC 1.14.11.-	2W2I	MKSVHSSPQNTSHTIMTFYPTMEEFADFNTYVAYMESQGAHQAGLAKVIPPKEWKARQMYDDIEDILIATPLQQVTSGQGGVFTQYHKKKKAMRVGQYRRLANSKKYQTPPHQNFADLEQRYWKSHPGNPPIYGADISGSLFEESTKQWNLGHLGTILDLLEQECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKTWYVVPPEHGQHLERLARELFPDISRGCEAFLRHKVALISPTVLKENGIPFNCMTQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGESTVTFSMDPFVRIVQPESYELWKHRQDLAIVEHTEPRVAESQELSNWRDDIVLRRAALGLRLLPNLTAQCPTQPVSSGHCYNPKGCGTDAVPGSAFQSSAYHTQTQSLTLGMSARVLLPSTGSWGSGRGRGRGQGQGRGCSRGRGHGCCTRELGTEEPTVQPASKRRLLMGTRSRAQGHRPQLPLANDLMTNLSL	Patented-recorded	KDM4 histone demethylase inhibitors for anti-cancer agents: a patent review.Expert Opin Ther Pat. 2015 Feb;25(2):135-44.	15.5	EC:1.14	JHDM3 histone demethylase family	JHDM3 histone demethylase family.	1.14.11.-	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	"JmjC domain, hydroxylase; jmjN domain"	PF02373; PF02375	PF02373; JmjC; PF02375; JmjN	.	.	.	.	MetaCyc:MON66-43206	B2RXH2
TTIG67W	Lysine-specific demethylase 5A (KDM5A)	P29375	KDM5A_HUMAN	Paired donor oxygen oxidoreductase	Retinoblastoma-binding protein 2; RBP2; RBBP2; RBBP-2; Jumonji/ARID domain-containing protein 1A; JARID1A; Histone demethylase JARID1A	KDM5A	"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."	EC 1.14.11.-	6DQB; 6DQA; 6DQ9; 6DQ8; 6DQ6	MAGVGPGGYAAEFVPPPECPVFEPSWEEFTDPLSFIGRIRPLAEKTGICKIRPPKDWQPPFACEVKSFRFTPRVQRLNELEAMTRVRLDFLDQLAKFWELQGSTLKIPVVERKILDLYALSKIVASKGGFEMVTKEKKWSKVGSRLGYLPGKGTGSLLKSHYERILYPYELFQSGVSLMGVQMPNLDLKEKVEPEVLSTDTQTSPEPGTRMNILPKRTRRVKTQSESGDVSRNTELKKLQIFGAGPKVVGLAMGTKDKEDEVTRRRKVTNRSDAFNMQMRQRKGTLSVNFVDLYVCMFCGRGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKCVAEECSKPREAFGFEQAVREYTLQSFGEMADNFKSDYFNMPVHMVPTELVEKEFWRLVSSIEEDVIVEYGADISSKDFGSGFPVKDGRRKILPEEEEYALSGWNLNNMPVLEQSVLAHINVDISGMKVPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPSHAAEQLEEVMRELAPELFESQPDLLHQLVTIMNPNVLMEHGVPVYRTNQCAGEFVVTFPRAYHSGFNQGYNFAEAVNFCTADWLPIGRQCVNHYRRLRRHCVFSHEELIFKMAADPECLDVGLAAMVCKELTLMTEEETRLRESVVQMGVLMSEEEVFELVPDDERQCSACRTTCFLSALTCSCNPERLVCLYHPTDLCPCPMQKKCLRYRYPLEDLPSLLYGVKVRAQSYDTWVSRVTEALSANFNHKKDLIELRVMLEDAEDRKYPENDLFRKLRDAVKEAETCASVAQLLLSKKQKHRQSPDSGRTRTKLTVEELKAFVQQLFSLPCVISQARQVKNLLDDVEEFHERAQEAMMDETPDSSKLQMLIDMGSSLYVELPELPRLKQELQQARWLDEVRLTLSDPQQVTLDVMKKLIDSGVGLAPHHAVEKAMAELQELLTVSERWEEKAKVCLQARPRHSVASLESIVNEAKNIPAFLPNVLSLKEALQKAREWTAKVEAIQSGSNYAYLEQLESLSAKGRPIPVRLEALPQVESQVAAARAWRERTGRTFLKKNSSHTLLQVLSPRTDIGVYGSGKNRRKKVKELIEKEKEKDLDLEPLSDLEEGLEETRDTAMVVAVFKEREQKEIEAMHSLRAANLAKMTMVDRIEEVKFCICRKTASGFMLQCELCKDWFHNSCVPLPKSSSQKKGSSWQAKEVKFLCPLCMRSRRPRLETILSLLVSLQKLPVRLPEGEALQCLTERAMSWQDRARQALATDELSSALAKLSVLSQRMVEQAAREKTEKIISAELQKAAANPDLQGHLPSFQQSAFNRVVSSVSSSPRQTMDYDDEETDSDEDIRETYGYDMKDTASVKSSSSLEPNLFCDEEIPIKSEEVVTHMWTAPSFCAEHAYSSASKSCSQGSSTPRKQPRKSPLVPRSLEPPVLELSPGAKAQLEELMMVGDLLEVSLDETQHIWRILQATHPPSEDRFLHIMEDDSMEEKPLKVKGKDSSEKKRKRKLEKVEQLFGEGKQKSKELKKMDKPRKKKLKLGADKSKELNKLAKKLAKEEERKKKKEKAAAAKVELVKESTEKKREKKVLDIPSKYDWSGAEESDDENAVCAAQNCQRPCKDKVDWVQCDGGCDEWFHQVCVGVSPEMAENEDYICINCAKKQGPVSPGPAPPPSFIMSYKLPMEDLKETS	Patented-recorded	Identification of small molecule inhibitors of Jumonji AT-rich interactive domain 1B (JARID1B) histone demethylase by a sensitive high throughput screen. J Biol Chem. 2013 Mar 29;288(13):9408-17.	0	EC:1.14	Oxidoreductases acting on paired donors	JARID1 histone demethylase family.	1.14.11.-	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	"ARID/BRIGHT DNA binding domain; JmjC domain, hydroxylase; jmjN domain; PHD-finger; PLU-1-like protein; C5HC2 zinc finger"	PF01388; PF02373; PF02375; PF00628; PF08429; PF02928	PF01388; ARID; PF02373; JmjC; PF02375; JmjN; PF00628; PHD; PF08429; PLU-1; PF02928; zf-C5HC2	.	.	.	R-HSA-3214842: HDMs demethylate histones	MetaCyc:ENSG00000073614-MON	P29375
TTCLI75	Lysine-specific demethylase 5B (KDM5B)	Q9UGL1	KDM5B_HUMAN	Paired donor oxygen oxidoreductase	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	KDM5B	"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."	EC 1.14.11.-	6EK6; 6EJ1; 6EJ0; 6EIY; 6EIU	MEAATTLHPGPRPALPLGGPGPLGEFLPPPECPVFEPSWEEFADPFAFIHKIRPIAEQTGICKVRPPPDWQPPFACDVDKLHFTPRIQRLNELEAQTRVKLNFLDQIAKYWELQGSTLKIPHVERKILDLFQLNKLVAEEGGFAVVCKDRKWTKIATKMGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTTDTKDKEYKPHDIPQRQSVQPSETCPPARRAKRMRAEAMNIKIEPEETTEARTHNLRRRMGCPTPKCENEKEMKSSIKQEPIERKDYIVENEKEKPKSRSKKATNAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKCLAQECSKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKLSPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCVKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYKLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQNQLTVNELRQFVTQLYALPCVLSQTPLLKDLLNRVEDFQQHSQKLLSEETPSAAELQDLLDVSFEFDVELPQLAEMRIRLEQARWLEEVQQACLDPSSLTLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLKARPRHSLNSLATAVKEIEEIPAYLPNGAALKDSVQRARDWLQDVEGLQAGGRVPVLDTLIELVTRGRSIPVHLNSLPRLETLVAEVQAWKECAVNTFLTENSPYSLLEVLCPRCDIGLLGLKRKQRKLKEPLPNGKKKSTKLESLSDLERALTESKETASAMATLGEARLREMEALQSLRLANEGKLLSPLQDVDIKICLCQKAPAAPMIQCELCRDAFHTSCVAVPSISQGLRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKFVQDRVGSGLLYSRWQASAGQVSDTNKVSQPPGTTSFSLPDDWDNRTSYLHSPFSTGRSCIPLHGVSPEVNELLMEAQLLQVSLPEIQELYQTLLAKPSPAQQTDRSSPVRPSSEKNDCCRGKRDGINSLERKLKRRLEREGLSSERWERVKKMRTPKKKKIKLSHPKDMNNFKLERERSYELVRSAETHSLPSDTSYSEQEDSEDEDAICPAVSCLQPEGDEVDWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTVKDAPSRK	Literature-reported	Identification of small molecule inhibitors of Jumonji AT-rich interactive domain 1B (JARID1B) histone demethylase by a sensitive high throughput screen. J Biol Chem. 2013 Mar 29;288(13):9408-17.	0	EC:1.14	Oxidoreductases acting on paired donors	JARID1 histone demethylase family.	1.14.11.-	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	"ARID/BRIGHT DNA binding domain; JmjC domain, hydroxylase; jmjN domain; PHD-finger; PLU-1-like protein; C5HC2 zinc finger"	PF01388; PF02373; PF02375; PF00628; PF08429; PF02928	PF01388; ARID; PF02373; JmjC; PF02375; JmjN; PF00628; PHD; PF08429; PLU-1; PF02928; zf-C5HC2	.	.	.	R-HSA-3214842: HDMs demethylate histones; R-HSA-8866911: TFAP2 (AP-2) family regulates transcription of cell cycle factors	MetaCyc:ENSG00000117139-MON	Q9UGL1
TT94UCF	Lysine-specific demethylase 5C (KDM5C)	P41229	KDM5C_HUMAN	Paired donor oxygen oxidoreductase	XE169; SMCX; Protein Xe169; Protein SmcX; Jumonji/ARID domain-containing protein 1C; JARID1C; Histone demethylase JARID1C; DXS1272E	KDM5C	"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."	EC 1.14.11.-	5FWJ; 2JRZ	MEPGSDDFLPPPECPVFEPSWAEFRDPLGYIAKIRPIAEKSGICKIRPPADWQPPFAVEVDNFRFTPRIQRLNELEAQTRVKLNYLDQIAKFWEIQGSSLKIPNVERRILDLYSLSKIVVEEGGYEAICKDRRWARVAQRLNYPPGKNIGSLLRSHYERIVYPYEMYQSGANLVQCNTRPFDNEEKDKEYKPHSIPLRQSVQPSKFNSYGRRAKRLQPDPEPTEEDIEKNPELKKLQIYGAGPKMMGLGLMAKDKTLRKKDKEGPECPPTVVVKEELGGDVKVESTSPKTFLESKEELSHSPEPCTKMTMRLRRNHSNAQFIESYVCRMCSRGDEDDKLLLCDGCDDNYHIFCLLPPLPEIPKGVWRCPKCVMAECKRPPEAFGFEQATREYTLQSFGEMADSFKADYFNMPVHMVPTELVEKEFWRLVNSIEEDVTVEYGADIHSKEFGSGFPVSDSKRHLTPEEEEYATSGWNLNVMPVLEQSVLCHINADISGMKVPWLYVGMVFSAFCWHIEDHWSYSINYLHWGEPKTWYGVPSLAAEHLEEVMKKLTPELFDSQPDLLHQLVTLMNPNTLMSHGVPVVRTNQCAGEFVITFPRAYHSGFNQGYNFAEAVNFCTADWLPAGRQCIEHYRRLRRYCVFSHEELICKMAACPEKLDLNLAAAVHKEMFIMVQEERRLRKALLEKGITEAEREAFELLPDDERQCIKCKTTCFLSALACYDCPDGLVCLSHINDLCKCSSSRQYLRYRYTLDELPAMLHKLKVRAESFDTWANKVRVALEVEDGRKRSLEELRALESEARERRFPNSELLQQLKNCLSEAEACVSRALGLVSGQEAGPHRVAGLQMTLTELRAFLDQMNNLPCAMHQIGDVKGVLEQVEAYQAEAREALASLPSSPGLLQSLLERGRQLGVEVPEAQQLQRQVEQARWLDEVKRTLAPSARRGTLAVMRGLLVAGASVAPSPAVDKAQAELQELLTIAERWEEKAHLCLEARQKHPPATLEAIIREAENIPVHLPNIQALKEALAKARAWIADVDEIQNGDHYPCLDDLEGLVAVGRDLPVGLEELRQLELQVLTAHSWREKASKTFLKKNSCYTLLEVLCPCADAGSDSTKRSRWMEKELGLYKSDTELLGLSAQDLRDPGSVIVAFKEGEQKEKEGILQLRRTNSAKPSPLASSSTASSTTSICVCGQVLAGAGALQCDLCQDWFHGRCVSVPRLLSSPRPNPTSSPLLAWWEWDTKFLCPLCMRSRRPRLETILALLVALQRLPVRLPEGEALQCLTERAISWQGRARQALASEDVTALLGRLAELRQRLQAEPRPEEPPNYPAAPASDPLREGSGKDMPKVQGLLENGDSVTSPEKVAPEEGSGKRDLELLSSLLPQLTGPVLELPEATRAPLEELMMEGDLLEVTLDENHSIWQLLQAGQPPDLERIRTLLELEKAERHGSRARGRALERRRRRKVDRGGEGDDPAREELEPKRVRSSGPEAEEVQEEEELEEETGGEGPPAPIPTTGSPSTQENQNGLEPAEGTTSGPSAPFSTLTPRLHLPCPQQPPQQQL	Literature-reported	Selective small molecule probes for the hypoxia inducible factor (HIF) prolyl hydroxylases. ACS Chem Biol. 2013 Jul 19;8(7):1488-96.	0	EC:1.14	.	JARID1 histone demethylase family.	1.14.11.-	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	"ARID/BRIGHT DNA binding domain; JmjC domain, hydroxylase; jmjN domain; PHD-finger; PLU-1-like protein; C5HC2 zinc finger"	PF01388; PF02373; PF02375; PF00628; PF08429; PF02928	PF01388; ARID; PF02373; JmjC; PF02375; JmjN; PF00628; PHD; PF08429; PLU-1; PF02928; zf-C5HC2	.	.	.	R-HSA-3214842: HDMs demethylate histones	MetaCyc:ENSG00000126012-MON	P41229
TTDIJUQ	Lysine-specific demethylase 6B (KDM6B)	O15054	KDM6B_HUMAN	.	Lysine demethylase 6B; KIAA0346; Jumonji domain-containing protein 3; JmjC domain-containing protein 3; JMJD3	KDM6B	"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)."	EC 1.14.11.-	6F6D; 5OY3; 5FP3; 4ASK; 2XXZ	MHRAVDPPGARAAREAFALGGLSCAGAWSSCPPHPPPRSAWLPGGRCSASIGQPPLPAPLPPSHGSSSGHPSKPYYAPGAPTPRPLHGKLESLHGCVQALLREPAQPGLWEQLGQLYESEHDSEEATRCYHSALRYGGSFAELGPRIGRLQQAQLWNFHTGSCQHRAKVLPPLEQVWNLLHLEHKRNYGAKRGGPPVKRAAEPPVVQPVPPAALSGPSGEEGLSPGGKRRRGCNSEQTGLPPGLPLPPPPLPPPPPPPPPPPPPLPGLATSPPFQLTKPGLWSTLHGDAWGPERKGSAPPERQEQRHSLPHPYPYPAPAYTAHPPGHRLVPAAPPGPGPRPPGAESHGCLPATRPPGSDLRESRVQRSRMDSSVSPAATTACVPYAPSRPPGLPGTTTSSSSSSSSNTGLRGVEPNPGIPGADHYQTPALEVSHHGRLGPSAHSSRKPFLGAPAATPHLSLPPGPSSPPPPPCPRLLRPPPPPAWLKGPACRAAREDGEILEELFFGTEGPPRPAPPPLPHREGFLGPPASRFSVGTQDSHTPPTPPTPTTSSSNSNSGSHSSSPAGPVSFPPPPYLARSIDPLPRPPSPAQNPQDPPLVPLTLALPPAPPSSCHQNTSGSFRRPESPRPRVSFPKTPEVGPGPPPGPLSKAPQPVPPGVGELPARGPRLFDFPPTPLEDQFEEPAEFKILPDGLANIMKMLDESIRKEEEQQQHEAGVAPQPPLKEPFASLQSPFPTDTAPTTTAPAVAVTTTTTTTTTTTATQEEEKKPPPALPPPPPLAKFPPPSQPQPPPPPPPSPASLLKSLASVLEGQKYCYRGTGAAVSTRPGPLPTTQYSPGPPSGATALPPTSAAPSAQGSPQPSASSSSQFSTSGGPWARERRAGEEPVPGPMTPTQPPPPLSLPPARSESEVLEEISRACETLVERVGRSATDPADPVDTAEPADSGTERLLPPAQAKEEAGGVAAVSGSCKRRQKEHQKEHRRHRRACKDSVGRRPREGRAKAKAKVPKEKSRRVLGNLDLQSEEIQGREKSRPDLGGASKAKPPTAPAPPSAPAPSAQPTPPSASVPGKKAREEAPGPPGVSRADMLKLRSLSEGPPKELKIRLIKVESGDKETFIASEVEERRLRMADLTISHCAADVVRASRNAKVKGKFRESYLSPAQSVKPKINTEEKLPREKLNPPTPSIYLESKRDAFSPVLLQFCTDPRNPITVIRGLAGSLRLNLGLFSTKTLVEASGEHTVEVRTQVQQPSDENWDLTGTRQIWPCESSRSHTTIAKYAQYQASSFQESLQEEKESEDEESEEPDSTTGTPPSSAPDPKNHHIIKFGTNIDLSDAKRWKPQLQELLKLPAFMRVTSTGNMLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFAVHEHYWETISAFCDRHGVDYLTGSWWPILDDLYASNIPVYRFVQRPGDLVWINAGTVHWVQATGWCNNIAWNVGPLTAYQYQLALERYEWNEVKNVKSIVPMIHVSWNVARTVKISDPDLFKMIKFCLLQSMKHCQVQRESLVRAGKKIAYQGRVKDEPAYYCNECDVEVFNILFVTSENGSRNTYLVHCEGCARRRSAGLQGVVVLEQYRTEELAQAYDAFTLAPASTSR	Literature-reported	A cell-permeable ester derivative of the JmjC histone demethylase inhibitor IOX1. ChemMedChem. 2014 Mar;9(3):566-71.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2559580: Oxidative Stress Induced Senescence; R-HSA-3214842: HDMs demethylate histones	MetaCyc:ENSG00000132510-MON	O15054
TT0NYMP	Lysine-specific demethylase 7A (KDM7A)	Q6ZMT4	KDM7A_HUMAN	.	Lysine-specific demethylase 7; KIAA1718; KDM7; JmjC domain-containing histone demethylation protein 1D; JHDM1D	KDM7A	"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."	EC 1.14.11.-	3U78; 3KVB; 3KVA; 3KV9; 3KV6	MAGAAAAVAAGAAAGAAAAAVSVAAPGRASAPPPPPPVYCVCRQPYDVNRFMIECDICKDWFHGSCVGVEEHHAVDIDLYHCPNCAVLHGSSLMKKRRNWHRHDYTEIDDGSKPVQAGTRTFIKELRSRVFPSADEIIIKMHGSQLTQRYLEKHGFDVPIMVPKLDDLGLRLPSPTFSVMDVERYVGGDKVIDVIDVARQADSKMTLHNYVKYFMNPNRPKVLNVISLEFSDTKMSELVEVPDIAKKLSWVENYWPDDSVFPKPFVQKYCLMGVQDSYTDFHIDFGGTSVWYHVLWGEKIFYLIKPTDENLARYESWSSSVTQSEVFFGDKVDKCYKCVVKQGHTLFVPTGWIHAVLTSQDCMAFGGNFLHNLNIGMQLRCYEMEKRLKTPDLFKFPFFEAICWFVAKNLLETLKELREDGFQPQTYLVQGVKALHTALKLWMKKELVSEHAFEIPDNVRPGHLIKELSKVIRAIEEENGKPVKSQGIPIVCPVSRSSNEATSPYHSRRKMRKLRDHNVRTPSNLDILELHTREVLKRLEMCPWEEDILSSKLNGKFNKHLQPSSTVPEWRAKDNDLRLLLTNGRIIKDERQPFADQSLYTADSENEEDKRRTKKAKMKIEESSGVEGVEHEESQKPLNGFFTRVKSELRSRSSGYSDISESEDSGPECTALKSIFTTEESESSGDEKKQEITSNFKEESNVMRNFLQKSQKPSRSEIPIKRECPTSTSTEEEAIQGMLSMAGLHYSTCLQRQIQSTDCSGERNSLQDPSSCHGSNHEVRQLYRYDKPVECGYHVKTEDPDLRTSSWIKQFDTSRFHPQDLSRSQKCIRKEGSSEISQRVQSRNYVDSSGSSLQNGKYMQNSNLTSGACQISNGSLSPERPVGETSFSVPLHPTKRPASNPPPISNQATKGKRPKKGMATAKQRLGKILKLNRNGHARFFV	Literature-reported	Plant growth regulator daminozide is a selective inhibitor of human KDM2/7 histone demethylases. J Med Chem. 2012 Jul 26;55(14):6639-43.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-3214842: HDMs demethylate histones; R-HSA-6802952: Signaling by BRAF and RAF1 fusions	MetaCyc:ENSG00000006459-MON	Q6ZMT4
TTUTJGQ	Vascular endothelial growth factor receptor 2 (KDR)	P35968	VGFR2_HUMAN	Kinase	VEGFR2; VEGFR-2; VEGF-2 receptor; Protein-tyrosine kinase receptor flk-1; Kinase insert domain receptor; Fetal liver kinase 1; FLK1; FLK-1; CD309	KDR	"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."	EC 2.7.10.1	6GQQ; 6GQP; 6GQO; 5OYJ; 5EW3	MQSKVLLAVALWLCVETRAASVGLPSVSLDLPRLSIQKDILTIKANTTLQITCRGQRDLDWLWPNNQSGSEQRVEVTECSDGLFCKTLTIPKVIGNDTGAYKCFYRETDLASVIYVYVQDYRSPFIASVSDQHGVVYITENKNKTVVIPCLGSISNLNVSLCARYPEKRFVPDGNRISWDSKKGFTIPSYMISYAGMVFCEAKINDESYQSIMYIVVVVGYRIYDVVLSPSHGIELSVGEKLVLNCTARTELNVGIDFNWEYPSSKHQHKKLVNRDLKTQSGSEMKKFLSTLTIDGVTRSDQGLYTCAASSGLMTKKNSTFVRVHEKPFVAFGSGMESLVEATVGERVRIPAKYLGYPPPEIKWYKNGIPLESNHTIKAGHVLTIMEVSERDTGNYTVILTNPISKEKQSHVVSLVVYVPPQIGEKSLISPVDSYQYGTTQTLTCTVYAIPPPHHIHWYWQLEEECANEPSQAVSVTNPYPCEEWRSVEDFQGGNKIEVNKNQFALIEGKNKTVSTLVIQAANVSALYKCEAVNKVGRGERVISFHVTRGPEITLQPDMQPTEQESVSLWCTADRSTFENLTWYKLGPQPLPIHVGELPTPVCKNLDTLWKLNATMFSNSTNDILIMELKNASLQDQGDYVCLAQDRKTKKRHCVVRQLTVLERVAPTITGNLENQTTSIGESIEVSCTASGNPPPQIMWFKDNETLVEDSGIVLKDGNRNLTIRRVRKEDEGLYTCQACSVLGCAKVEAFFIIEGAQEKTNLEIIILVGTAVIAMFFWLLLVIILRTVKRANGGELKTGYLSIVMDPDELPLDEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLSTYLRSKRNEFVPYKTKGARFRQGKDYVGAIPVDLKRRLDSITSSQSSASSGFVEEKSLSDVEEEEAPEDLYKDFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQANAQQDGKDYIVLPISETLSMEEDSGLSLPTSPVSCMEEEEVCDPKFHYDNTAGISQYLQNSKRKSRPVSVKTFEDIPLEEPEVKVIPDDNQTDSGMVLASEELKTLEDRTKLSPSFGGMVPSKSRESVASEGSNQTSGYQSGYHSDDTDTTVYSSEEAELLKLIEIGVQTGSTAQILQPDSGTTLSSPPV	Successful	Emerging drugs for ovarian cancer. Expert Opin Emerg Drugs. 2008 Sep;13(3):523-36.	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Immunoglobulin I-set domain; Immunoglobulin domain; Protein tyrosine kinase; VEGFR-2 Transmembrane domain	PF07679; PF00047; PF07714; PF17988	PF07679; I-set; PF00047; ig; PF07714; Pkinase_Tyr; PF17988; VEGFR-2_TMD	.	.	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	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	.	P35968
TTPFN62	VEGFR2 messenger RNA (VEGFR2 mRNA)	P35968	VGFR2_HUMAN	mRNA target	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)	KDR	"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."	EC 2.7.10.1	6GQQ; 6GQP; 6GQO; 5OYJ; 5EW3	MQSKVLLAVALWLCVETRAASVGLPSVSLDLPRLSIQKDILTIKANTTLQITCRGQRDLDWLWPNNQSGSEQRVEVTECSDGLFCKTLTIPKVIGNDTGAYKCFYRETDLASVIYVYVQDYRSPFIASVSDQHGVVYITENKNKTVVIPCLGSISNLNVSLCARYPEKRFVPDGNRISWDSKKGFTIPSYMISYAGMVFCEAKINDESYQSIMYIVVVVGYRIYDVVLSPSHGIELSVGEKLVLNCTARTELNVGIDFNWEYPSSKHQHKKLVNRDLKTQSGSEMKKFLSTLTIDGVTRSDQGLYTCAASSGLMTKKNSTFVRVHEKPFVAFGSGMESLVEATVGERVRIPAKYLGYPPPEIKWYKNGIPLESNHTIKAGHVLTIMEVSERDTGNYTVILTNPISKEKQSHVVSLVVYVPPQIGEKSLISPVDSYQYGTTQTLTCTVYAIPPPHHIHWYWQLEEECANEPSQAVSVTNPYPCEEWRSVEDFQGGNKIEVNKNQFALIEGKNKTVSTLVIQAANVSALYKCEAVNKVGRGERVISFHVTRGPEITLQPDMQPTEQESVSLWCTADRSTFENLTWYKLGPQPLPIHVGELPTPVCKNLDTLWKLNATMFSNSTNDILIMELKNASLQDQGDYVCLAQDRKTKKRHCVVRQLTVLERVAPTITGNLENQTTSIGESIEVSCTASGNPPPQIMWFKDNETLVEDSGIVLKDGNRNLTIRRVRKEDEGLYTCQACSVLGCAKVEAFFIIEGAQEKTNLEIIILVGTAVIAMFFWLLLVIILRTVKRANGGELKTGYLSIVMDPDELPLDEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLSTYLRSKRNEFVPYKTKGARFRQGKDYVGAIPVDLKRRLDSITSSQSSASSGFVEEKSLSDVEEEEAPEDLYKDFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQANAQQDGKDYIVLPISETLSMEEDSGLSLPTSPVSCMEEEEVCDPKFHYDNTAGISQYLQNSKRKSRPVSVKTFEDIPLEEPEVKVIPDDNQTDSGMVLASEELKTLEDRTKLSPSFGGMVPSKSRESVASEGSNQTSGYQSGYHSDDTDTTVYSSEEAELLKLIEIGVQTGSTAQILQPDSGTTLSSPPV	Discontinued	Teaming up to tackle RNAi delivery challenge. Nat Rev Drug Discov. 2009 Jul;8(7):525-6.	5	mRNA	mRNA target	.	.	.	Immunoglobulin I-set domain; Immunoglobulin domain; Protein tyrosine kinase; VEGFR-2 Transmembrane domain	PF07679; PF00047; PF07714; PF17988	PF07679; I-set; PF00047; ig; PF07714; Pkinase_Tyr; PF17988; VEGFR-2_TMD	.	.	hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa04010: MAPK signaling pathway; hsa04014: Ras signaling pathway; hsa04015: Rap1 signaling pathway; hsa04020: Calcium signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04370: VEGF signaling pathway; hsa04510: Focal adhesion; hsa05205: Proteoglycans in cancer; hsa05418: Fluid shear stress and atherosclerosis	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-4420097: VEGFA-VEGFR2 Pathway; R-HSA-5218921: VEGFR2 mediated cell proliferation; R-HSA-9673768: Signaling by membrane-tethered fusions of PDGFRA or PDGFRB	.	P35968
TT3Z6Y9	Cysteines of Keap1 (KEAP1 Cysteines)	Q14145	KEAP1_HUMAN	.	Kelch-like protein 19-Cysteines; Kelch-like ECH-associated protein 1-Cysteines; KLHL19-Cysteines; KIAA0132-Cysteines; INrf2-Cysteines; Cytosolic inhibitor of Nrf2-Cysteines	KEAP1	"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."	.	6FMQ; 6FMP; 6FFM; 5X54; 5WIY	MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGEVAKQEEFFNLSHCQLVTLISRDDLNVRCESEVFHACINWVKYDCEQRRFYVQALLRAVRCHSLTPNFLQMQLQKCEILQSDSRCKDYLVKIFEELTLHKPTQVMPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSDGTWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAPMSVPRNRIGVGVIDGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDTDTWSEVTRMTSGRSGVGVAVTMEPCRKQIDQQNCTC	Clinical trial	Recent progress in the development of small molecule Nrf2 modulators: a patent review (2012-2016).Expert Opin Ther Pat. 2017 Jul;27(7):763-785.	15.5	.	.	.	.	.	BTB And C-terminal Kelch; BTB/POZ domain; Kelch motif	PF07707; PF00651; PF01344	PF07707; BACK; PF00651; BTB; PF01344; Kelch_1	.	.	hsa04120: Ubiquitin mediated proteolysis; hsa05012: Parkinson disease; hsa05200: Pathways in cancer; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05225: Hepatocellular carcinoma; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-5689880: Ub-specific processing proteases; R-HSA-8951664: Neddylation; R-HSA-9679191: Potential therapeutics for SARS; R-HSA-9755511: KEAP1-NFE2L2 pathway; R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	Q14145
TTGIZLN	Keap1-Nrf2[dual DLG and ETGE] PPI (KEAP1-Nrf2 DLG and ETGE)	Q14145-Q16236	KEAP1_HUMAN-NF2L2_HUMAN	.	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]	KEAP1-NFE2L2	"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."	.	.	MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGEVAKQEEFFNLSHCQLVTLISRDDLNVRCESEVFHACINWVKYDCEQRRFYVQALLRAVRCHSLTPNFLQMQLQKCEILQSDSRCKDYLVKIFEELTLHKPTQVMPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSDGTWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAPMSVPRNRIGVGVIDGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDTDTWSEVTRMTSGRSGVGVAVTMEPCRKQIDQQNCTCMMDLELPPPGLPSQQDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN	Patented-recorded	Recent progress in the development of small molecule Nrf2 modulators: a patent review (2012-2016).Expert Opin Ther Pat. 2017 Jul;27(7):763-785.	15.5	.	.	.	.	.	BTB And C-terminal Kelch; BTB/POZ domain; Kelch motif	PF07707; PF00651; PF01344	PF07707; BACK; PF00651; BTB; PF01344; Kelch_1	.	.	.	.	.	Q14145
TTHQJI6	Keap1-Nrf2[ETGE] PPI (KEAP1-Nrf2 ETGE)	Q14145-Q16236	KEAP1_HUMAN-NF2L2_HUMAN	.	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]	KEAP1-NFE2L2	"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."	.	.	MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGEVAKQEEFFNLSHCQLVTLISRDDLNVRCESEVFHACINWVKYDCEQRRFYVQALLRAVRCHSLTPNFLQMQLQKCEILQSDSRCKDYLVKIFEELTLHKPTQVMPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSDGTWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAPMSVPRNRIGVGVIDGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDTDTWSEVTRMTSGRSGVGVAVTMEPCRKQIDQQNCTCMMDLELPPPGLPSQQDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN	Patented-recorded	Recent progress in the development of small molecule Nrf2 modulators: a patent review (2012-2016).Expert Opin Ther Pat. 2017 Jul;27(7):763-785.	15.5	.	.	.	.	.	BTB And C-terminal Kelch; BTB/POZ domain; Kelch motif	PF07707; PF00651; PF01344	PF07707; BACK; PF00651; BTB; PF01344; Kelch_1	.	.	.	.	.	Q14145
TT956B0	Keap1-Nrf2[DLG] PPI (KEAP1-Nrf2 DLG)	Q14145-Q16236	KEAP1_HUMAN-NF2L2_HUMAN	.	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]	KEAP1-NFE2L2	"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."	.	.	MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGEVAKQEEFFNLSHCQLVTLISRDDLNVRCESEVFHACINWVKYDCEQRRFYVQALLRAVRCHSLTPNFLQMQLQKCEILQSDSRCKDYLVKIFEELTLHKPTQVMPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSDGTWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAPMSVPRNRIGVGVIDGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDTDTWSEVTRMTSGRSGVGVAVTMEPCRKQIDQQNCTCMMDLELPPPGLPSQQDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN	Patented-recorded	Recent progress in the development of small molecule Nrf2 modulators: a patent review (2012-2016).Expert Opin Ther Pat. 2017 Jul;27(7):763-785.	15.5	.	.	.	.	.	BTB And C-terminal Kelch; BTB/POZ domain; Kelch motif	PF07707; PF00651; PF01344	PF07707; BACK; PF00651; BTB; PF01344; Kelch_1	.	.	.	.	.	Q14145
TTAT6C7	GAP-associated tyrosine phosphoprotein p62 (KHDRBS1)	Q07666	KHDR1_HUMAN	.	"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"	KHDRBS1	"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."	.	3QHE; 2XA6	MQRRDDPAARMSRSSGRSGSMDPSGAHPSVRQTPSRQPPLPHRSRGGGGGSRGGARASPATQPPPLLPPSATGPDATVGGPAPTPLLPPSATASVKMEPENKYLPELMAEKDSLDPSFTHAMQLLTAEIEKIQKGDSKKDDEENYLDLFSHKNMKLKERVLIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKAKEEELRKGGDPKYAHLNMDLHVFIEVFGPPCEAYALMAHAMEEVKKFLVPDMMDDICQEQFLELSYLNGVPEPSRGRGVPVRGRGAAPPPPPVPRGRGVGPPRGALVRGTPVRGAITRGATVTRGVPPPPTVRGAPAPRARTAGIQRIPLPPPPAPETYEEYGYDDTYAEQSYEGYEGYYSQSQGDSEYYDYGHGEVQDSYEAYGQDDWNGTRPSLKAPPARPVKGAYREHPYGRY	Literature-reported	Clinical significance and effect of Sam68 expression in gastric cancer. Oncol Lett. 2018 Apr;15(4):4745-4752.	.	.	.	KHDRBS family.Sequence analysisKeywords - DomainiSH3-binding	.	.	KH domain; Qua1 domain; Tyrosine-rich domain of Sam68	PF00013; PF16274; PF16568	PF00013; KH_1; PF16274; Qua1; PF16568; Sam68-YY	.	.	.	R-HSA-8849468: PTK6 Regulates Proteins Involved in RNA Processing	.	Q07666
TTPAFR9	Ketohexokinase (KHK)	P50053	KHK_HUMAN	Kinase	Hepatic fructokinase	KHK	Catalyzes the phosphorylation of the ketose sugar fructose to fructose-1-phosphate.	EC 2.7.1.3	5WBZ; 5WBR; 5WBQ; 5WBP; 5WBO	MEEKQILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVDVSQVAWQSKGDTPSSCCIINNSNGNRTIVLHDTSLPDVSATDFEKVDLTQFKWIHIEGRNASEQVKMLQRIDAHNTRQPPEQKIRVSVEVEKPREELFQLFGYGDVVFVSKDVAKHLGFQSAEEALRGLYGRVRKGAVLVCAWAEEGADALGPDGKLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGLQGFDGIV	Literature-reported	Discovery of Fragment-Derived Small Molecules for in Vivo Inhibition of Ketohexokinase (KHK). J Med Chem. 2017 Sep 28;60(18):7835-7849.	.	.	.	.	.	.	.	.	.	.	.	hsa00051: Fructose and mannose metabolism; hsa01100: Metabolic pathways	R-HSA-5657562: Essential fructosuria; R-HSA-70350: Fructose catabolism	MetaCyc:HS06437-MON	P50053
TTBGTCW	Kinesin spindle messenger RNA (KIF11 mRNA)	P52732	KIF11_HUMAN	mRNA target	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)	KIF11	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.	.	6G6Z; 6G6Y; 5ZO9; 5ZO8; 5ZO7	MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADKSSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSPNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSERLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFSVTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNILNKPEVNQKLTKKALIKEYTEEIERLKRDLAAAREKNGVYISEENFRVMSGKLTVQEEQIVELIEKIGAVEEELNRVTELFMDNKNELDQCKSDLQNKTQELETTQKHLQETKLQLVKEEYITSALESTEEKLHDAASKLLNTVEETTKDVSGLHSKLDRKKAVDQHNAEAQDIFGKNLNSLFNNMEELIKDGSSKQKAMLEVHKTLFGNLLSSSVSALDTITTVALGSLTSIPENVSTHVSQIFNMILKEQSLAAESKTVLQELINVLKTDLLSSLEMILSPTVVSILKINSQLKHIFKTSLTVADKIEDQKKELDGFLSILCNNLHELQENTICSLVESQKQCGNLTEDLKTIKQTHSQELCKLMNLWTERFCALEEKCENIQKPLSSVQENIQQKSKDIVNKMTFHSQKFCADSDGFSQELRNFNQEGTKLVEESVKHSDKLNGNLEKISQETEQRCESLNTRTVYFSEQWVSSLNEREQELHNLLEVVSQCCEASSSDITEKSDGRKAAHEKQHNIFLDQMTIDEDKLIAQNLELNETIKIGLTKLNCFLEQDLKLDIPTGTTPQRKSYLYPSTLVRTEPREHLLDQLKRKQPELLMMLNCSENNKEETIPDVDVEEAVLGQYTEEPLSQEPSVDAGVDCSSIGGVPFFQHKKSHGKDKENRGINTLERSKVEETTEHLVTKSRLPLRAQINL	Clinical trial	"Clinical pipeline report, company report or official report of Alnylam Pharmaceuticals, Inc (2011)."	17	mRNA	mRNA target	.	.	.	Kinesin motor domain; Kinesin-associated microtubule-binding	PF00225; PF13931	PF00225; Kinesin; PF13931; Microtub_bind	.	.	.	R-HSA-2132295:MHC class II antigen presentation; R-HSA-983189:Kinesins	.	P52732
TTTRP0H	Kinesin-like protein KIF11 (KIF11)	P52732	KIF11_HUMAN	Kinesin-like protein family	Thyroid receptor interacting protein 5; TRIP5; Kinesin-related motor protein Eg5; Kinesin-like spindle protein HKSP; Kinesin-like protein 1; KIF11; Eg5	KIF11	Motor protein required for establishing a bipolar spindle. Blocking of KIF11 prevents centrosome migration and arrest cells in mitosis with monoastral microtubule arrays.	.	6G6Z; 6G6Y; 5ZO9; 5ZO8; 5ZO7	MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADKSSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSPNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSERLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFSVTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNILNKPEVNQKLTKKALIKEYTEEIERLKRDLAAAREKNGVYISEENFRVMSGKLTVQEEQIVELIEKIGAVEEELNRVTELFMDNKNELDQCKSDLQNKTQELETTQKHLQETKLQLVKEEYITSALESTEEKLHDAASKLLNTVEETTKDVSGLHSKLDRKKAVDQHNAEAQDIFGKNLNSLFNNMEELIKDGSSKQKAMLEVHKTLFGNLLSSSVSALDTITTVALGSLTSIPENVSTHVSQIFNMILKEQSLAAESKTVLQELINVLKTDLLSSLEMILSPTVVSILKINSQLKHIFKTSLTVADKIEDQKKELDGFLSILCNNLHELQENTICSLVESQKQCGNLTEDLKTIKQTHSQELCKLMNLWTERFCALEEKCENIQKPLSSVQENIQQKSKDIVNKMTFHSQKFCADSDGFSQELRNFNQEGTKLVEESVKHSDKLNGNLEKISQETEQRCESLNTRTVYFSEQWVSSLNEREQELHNLLEVVSQCCEASSSDITEKSDGRKAAHEKQHNIFLDQMTIDEDKLIAQNLELNETIKIGLTKLNCFLEQDLKLDIPTGTTPQRKSYLYPSTLVRTEPREHLLDQLKRKQPELLMMLNCSENNKEETIPDVDVEEAVLGQYTEEPLSQEPSVDAGVDCSSIGGVPFFQHKKSHGKDKENRGINTLERSKVEETTEHLVTKSRLPLRAQINL	Clinical trial	Inhibition of KSP by ARRY-520 induces cell cycle block and cell death via the mitochondrial pathway in AML cells. Leukemia. 2009 Oct;23(10):1755-62.	21	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2132295:MHC class II antigen presentation; R-HSA-983189:Kinesins	.	P52732
TTQECT2	Kinesin-like protein KIF20B (MPHOSPH1)	Q96Q89	KI20B_HUMAN	Myosin-kinesin ATPase	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	KIF20B	"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."	.	.	MESNFNQEGVPRPSYVFSADPIARPSEINFDGIKLDLSHEFSLVAPNTEANSFESKDYLQVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQCILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLYTKMNLKPHRSREYLRLSSEQEKEEIASKSALLRQIKEVTVHNDSDDTLYGSLTNSLNISEFEESIKDYEQANLNMANSIKFSVWVSFFEIYNEYIYDLFVPVSSKFQKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSKFQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFSAIAQKVCVPDTLNSSQEKLFGPVKSSQDVSLDSNSNSKILNVKRATISWENSLEDLMEDEDLVEELENAEETQNVETKLLDEDLDKTLEENKAFISHEEKRKLLDLIEDLKKKLINEKKEKLTLEFKIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREEAAKDICATKVETEETHNYVGFEDIIDSLQDNVADIKKQAEIAHLYIASLPDPQEATACLELKFNQIKAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNLKSHMENTFKCNDKADTSSLIINNKLICNETVEVPKDSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVRPNIAEIEDIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRTLDSVSQISNIDLLNLRDLSNGSEEDNLPNTQLDLLGNDYLVSKQVKEYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPDKLQTEPLSTSFEISRNKIEDGSVVLDSCEVSTENDQSTRFPKPELEIQFTPLQPNKMAVKHPGCTTPVTVKIPKARKRKSNEMEEDLVKCENKKNATPRTNLKFPISDDRNSSVKKEQKVAIRPSSKKTYSLRSQASIIGVNLATKKKEGTLQKFGDFLQHSPSILQSKAKKIIETMSSSKLSNVEASKENVSQPKRAKRKLYTSEISSPIDISGQVILMDQKMKESDHQIIKRRLRTKTAK	Literature-reported	MPHOSPH1: a potential therapeutic target for hepatocellular carcinoma. Cancer Res. 2014 Nov 15;74(22):6623-34.	.	Myosin-kinesin ATPase	Kinesin-like protein family	TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.	.	.	Kinesin motor domain	PF00225	PF00225; Kinesin	.	.	.	R-HSA-6811434: COPI-dependent Golgi-to-ER retrograde traffic; R-HSA-983189: Kinesins	.	Q96Q89
TTQWICZ	Kinesin-like protein KIF26B (KIF26B)	Q2KJY2	KI26B_HUMAN	Myosin-kinesin ATPase	Kinesinlike protein KIF26B	KIF26B	"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."	.	.	MNSVAGNKERLAVSTRGKKYGVNEVCSPTKPAAPFSPESWYRKAYEESRAGSRPTPEGAGSALGSSGTPSPGSGTSSPSSFTGSPGPASPGIGTSSPGSLGGSPGFGTGSPGSGSGGGSSPGSDRGVWCENCNARLVELKRQALRLLLPGPFPGKDPAFSAVIHDKLQVPNTIRKAWNDRDNRCDICATHLNQLKQEAIQMVLTLEQAAGSEHYDASPCSPPPLSNIPTLVGSRHVGGLQQPRDWAFVPAPCATSNYTGFANKHGSKPSSLGVSNGAEKKSGSPTHQAKVSLQMATSPSNGNILNSVAIQAHQYLDGTWSLSRTNGVTLYPYQISQLMTESSREGLTEAVLNRYNADKPSACSVPASQGSCVASETSTGTSVAASFFARAAQKLNLSSKKKKHRPSTSSAAEPPLFATSFSGILQTSPPPAPPCLLRAVNKVKDTPGLGKVKVMLRICSTLARDTSESSSFLKVDPRKKQITLYDPLTCGGQNAFQKRGNQVPPKMFAFDAVFPQDASQAEVCAGTVAEVIQSVVNGADGCVFCFGHAKLGKSYTMIGKDDSMQNLGIIPCAISWLFKLINERKEKTGARFSVRVSAVEVWGKEENLRDLLSEVATGSLQDGQSPGVYLCEDPICGTQLQNQSELRAPTAEKAAFFLDAAIASRRSHQQDCDEDDHRNSHVFFTLHIYQYRMEKSGKGGMSGGRSRLHLIDLGSCVKALSKNREGGSGLCLSLSALGNVILALVNGSKHIPYKESKLAMLLRESLGNMNCRTTMIAHISAAVGSYAETLSTIQIASRVLRMKKKKTKYTSSSSGGESSCEEGRMRRPTQLRPFHTRATVDPDFPIAHLSSDPDYSSSSEQSCDTVIYIGPNGTALSDKELTDNEGPPDFVPIVPALQKTRGDSRPAEAGEAAAGKSERDCLKCNTFAELQERLDCIDGSEEPSSFPFEELPAQFGPEQASRGPRLSQAAGASPLSESDKEDNGSEGQLTNREGPELPASKMQRSHSPVPAAAPAHSPSPASPRSVPGSSSQHSASPLVQSPSLQSSRESLNSCGFVEGKPRPMGSPRLGIASLSKTSEYKPPSSPSQRCKVYTQKGVLPSPAPLPPSSKDSGVASRESLLQPEVRTPPVGMSPQVLKKSMSAGSEGFPETPVDDEQQAATPSESKKEILSTTMVTVQQPLELNGEDELVFTLVEELTISGVLDSGRPTSIISFNSDCSARALASGSRPVSIISSISEDLECYSSTAPVSEVSITQFLPLPKMSLDEKAQDAGSRRSSISSWLSEMSAGSEGEQSCHSFIAQTCFGHGEAMAEPVASEFVSSLQNTAVVCREKPKASPDNLLILSEMGDDSFNKAAPIKGCKISTVSKAMVTISNTANLSSCEGYIPMKTNITVYPCIAMSPRNIQEPEAPTATPKAGPTLAQSRESKENSAKKEMKFEDPWLKREEEVKKETAHPNEEGMMRCETATGPSNAETRAEQEQDGKPSPGDRLSSSSGEVSASPVTDNFRRVVDGCEMALPGLATQSPVHPNKSVKSSSLPRAFQKASRQEEPDSLSYYCAAETNGVGAASGTPPSKATLEGKVASPKHCVLARPKGTPPLPPVRKSSLDQKNRASPQHSASGSGTSSPLNQPAAFPAGLPDEPSGKTKDASSSSKLFSAKLEQLASRSNSLGRATVSHYECLSLERAESLSSVSSRLHAGKDGTMPRAGRSLGRSAGTSPPSSGASPKAGQSKISAVSRLLLASPRARGPSASTTKTLSFSTKSLPQAVGQGSSSPPGGKHTPWSTQSLSRNRSSGLASKLPLRAVSGRISELLQGGAGARGLQLRAGPEAEARGGALAEDEPAAAHLLPSPYSKITPPRRPHRCSSGHGSDNSSVLSGELPPAMGKTALFYHSGGSSGYESVMRDSEATGSASSAQDSTSENSSSVGGRCRSLKTPKKRSNPGSQRRRLIPALSLDTSSPVRKPPNSTGVRWVDGPLRSSPRGLGEPFEIKVYEIDDVERLQRRRGGASKEAMCFNAKLKILEHRQQRIAEVRAKYEWLMKELEATKQYLMLDPNKWLSEFDLEQVWELDSLEYLEALECVTERLESRVNFCKAHLMMITCFDITSRRR	Literature-reported	"KIF26B, a novel oncogene, promotes proliferation and metastasis by activating the VEGF pathway in gastric cancer. Oncogene. 2017 Oct 5;36(40):5609-5619."	.	Myosin-kinesin ATPase	Kinesin-like protein family	TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIF26 subfamily.	.	.	Kinesin motor domain	PF00225	PF00225; Kinesin	.	.	.	R-HSA-6811434: COPI-dependent Golgi-to-ER retrograde traffic; R-HSA-983189: Kinesins	.	Q2KJY2
TTCJPAH	Kinesin heavy chain neuron-specific 1 (KIF5A)	Q12840	KIF5A_HUMAN	Kinesin-like protein family	NKHC; Kinesin heavy chain isoform 5A; KIF5A	KIF5A	"Microtubule-dependent motor required for slow axonal transport of neurofilament proteins (NFH, NFM and NFL)."	.	4UY0; 4UXY; 4UXT	MAETNNECSIKVLCRFRPLNQAEILRGDKFIPIFQGDDSVVIGGKPYVFDRVFPPNTTQEQVYHACAMQIVKDVLAGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIARDIFNHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVTKTNLSVHEDKNRVPFVKGCTERFVSSPEEILDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENMETEQKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKSYVPYRDSKMTRILQDSLGGNCRTTMFICCSPSSYNDAETKSTLMFGQRAKTIKNTASVNLELTAEQWKKKYEKEKEKTKAQKETIAKLEAELSRWRNGENVPETERLAGEEAALGAELCEETPVNDNSSIVVRIAPEERQKYEEEIRRLYKQLDDKDDEINQQSQLIEKLKQQMLDQEELLVSTRGDNEKVQRELSHLQSENDAAKDEVKEVLQALEELAVNYDQKSQEVEEKSQQNQLLVDELSQKVATMLSLESELQRLQEVSGHQRKRIAEVLNGLMKDLSEFSVIVGNGEIKLPVEISGAIEEEFTVARLYISKIKSEVKSVVKRCRQLENLQVECHRKMEVTGRELSSCQLLISQHEAKIRSLTEYMQSVELKKRHLEESYDSLSDELAKLQAQETVHEVALKDKEPDTQDADEVKKALELQMESHREAHHRQLARLRDEINEKQKTIDELKDLNQKLQLELEKLQADYEKLKSEEHEKSTKLQELTFLYERHEQSKQDLKGLEETVARELQTLHNLRKLFVQDVTTRVKKSAEMEPEDSGGIHSQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALEGALKEAKEGAMKDKRRYQQEVDRIKEAVRYKSSGKRGHSAQIAKPVRPGHYPASSPTNPYGTRSPECISYTNSLFQNYQNLYLQATPSSTSDMYFANSCTSSGATSSGGPLASYQKANMDNGNATDINDNRSDLPCGYEAEDQAKLFPLHQETAAS	Literature-reported	Axonal transport in neurological disease. Ann Neurol. 1988 Jan;23(1):3-13.	.	.	.	.	.	.	.	.	.	.	.	hsa04144: Endocytosis; hsa04728: Dopaminergic synapse; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05014: Amyotrophic lateral sclerosis; hsa05016: Huntington disease; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05132: Salmonella infection; hsa05223: Non-small cell lung cancer	R-HSA-2132295: MHC class II antigen presentation; R-HSA-264876: Insulin processing; R-HSA-5625970: RHO GTPases activate KTN1; R-HSA-6811434: COPI-dependent Golgi-to-ER retrograde traffic; R-HSA-983189: Kinesins	.	Q12840
TT4UXPE	MHC class I NK cell receptor 2DL1 (CD158A)	P43626	KI2L1_HUMAN	Immunoglobulin	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	KIR2DL1	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.	.	1NKR; 1IM9	MSLLVVSMACVGFFLLQGAWPHEGVHRKPSLLAHPGPLVKSEETVILQCWSDVMFEHFLLHREGMFNDTLRLIGEHHDGVSKANFSISRMTQDLAGTYRCYGSVTHSPYQVSAPSDPLDIVIIGLYEKPSLSAQPGPTVLAGENVTLSCSSRSSYDMYHLSREGEAHERRLPAGPKVNGTFQADFPLGPATHGGTYRCFGSFHDSPYEWSKSSDPLLVSVTGNPSNSWPSPTEPSSKTGNPRHLHILIGTSVVIILFILLFFLLHRWCSNKKNAAVMDQESAGNRTANSEDSDEQDPQEVTYTQLNHCVFTQRKITRPSQRPKTPPTDIIVYTELPNAESRSKVVSCP	Clinical trial	Daratumumab-mediated lysis of primary multiple myeloma cells is enhanced in combination with the human anti-KIR antibody IPH2102 and lenalidomide. Haematologica. 2015 Feb;100(2):263-8.	21	Immunoglobulin	Immunoglobulin	immunoglobulin superfamily.	.	.	Immunoglobulin domain	PF00047	PF00047; ig	.	.	hsa04612:Antigen processing and presentation; hsa04650:Natural killer cell mediated cytotoxicity; hsa05332:Graft-versus-host disease	R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	P43626
TTU0P73	MHC class I NK cell receptor 2DL2 (CD158b1)	P43627	KI2L2_HUMAN	Immunoglobulin	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	KIR2DL2	"Receptor on natural killer (NK) cells for HLA-Cw1, 3, 7, and 8 allotypes. Inhibits the activity of NK cells thus preventing cell lysis."	.	2DLI; 2DL2; 1EFX	MSLMVVSMACVGFFLLQGAWPHEGVHRKPSLLAHPGRLVKSEETVILQCWSDVRFEHFLLHREGKFKDTLHLIGEHHDGVSKANFSIGPMMQDLAGTYRCYGSVTHSPYQLSAPSDPLDIVITGLYEKPSLSAQPGPTVLAGESVTLSCSSRSSYDMYHLSREGEAHECRFSAGPKVNGTFQADFPLGPATHGGTYRCFGSFRDSPYEWSNSSDPLLVSVIGNPSNSWPSPTEPSSKTGNPRHLHILIGTSVVIILFILLFFLLHRWCSNKKNAAVMDQESAGNRTANSEDSDEQDPQEVTYTQLNHCVFTQRKITRPSQRPKTPPTDIIVYAELPNAESRSKVVSCP	Clinical trial	Daratumumab-mediated lysis of primary multiple myeloma cells is enhanced in combination with the human anti-KIR antibody IPH2102 and lenalidomide. Haematologica. 2015 Feb;100(2):263-8.	21	Immunoglobulin	.	immunoglobulin superfamily.	.	.	Immunoglobulin domain	PF00047	PF00047; ig	.	.	hsa04612:Antigen processing and presentation; hsa04650:Natural killer cell mediated cytotoxicity; hsa05332:Graft-versus-host disease	R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	P43627
TTEX3SI	MHC class I NK cell receptor 2DL3 (CD158b2)	P43628	KI2L3_HUMAN	Immunoglobulin	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	KIR2DL3	"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."	.	1B6U	MSLMVVSMVCVGFFLLQGAWPHEGVHRKPSLLAHPGPLVKSEETVILQCWSDVRFQHFLLHREGKFKDTLHLIGEHHDGVSKANFSIGPMMQDLAGTYRCYGSVTHSPYQLSAPSDPLDIVITGLYEKPSLSAQPGPTVLAGESVTLSCSSRSSYDMYHLSREGEAHERRFSAGPKVNGTFQADFPLGPATHGGTYRCFGSFRDSPYEWSNSSDPLLVSVTGNPSNSWPSPTEPSSETGNPRHLHVLIGTSVVIILFILLLFFLLHRWCCNKKNAVVMDQEPAGNRTVNREDSDEQDPQEVTYAQLNHCVFTQRKITRPSQRPKTPPTDIIVYTELPNAEP	Clinical trial	Daratumumab-mediated lysis of primary multiple myeloma cells is enhanced in combination with the human anti-KIR antibody IPH2102 and lenalidomide. Haematologica. 2015 Feb;100(2):263-8.	21	.	.	.	.	.	.	.	.	.	.	hsa04612:Antigen processing and presentation; hsa04650:Natural killer cell mediated cytotoxicity; hsa05332:Graft-versus-host disease	R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	P43628
TTVWAGF	MHC class I NK cell receptor 2DS1 (CD158h)	Q14954	KI2S1_HUMAN	Immunoglobulin	MHC class I NK cell receptor Eb6 ActI; Killer cell immunoglobulin-like receptor 2DS1; CD158h; CD158 antigen-like family member H	KIR2DS1	Receptor on natural killer (NK) cells for some HLA-C alleles such as w6. Does not inhibit the activity of NK cells.	.	.	MSLTVVSMACVGFFLLQGAWPHEGVHRKPSLLAHPGRLVKSEETVILQCWSDVMFEHFLLHREGMFNDTLRLIGEHHDGVSKANFSISRMKQDLAGTYRCYGSVTHSPYQLSAPSDPLDIVIIGLYEKPSLSAQPGPTVLAGENVTLSCSSRSSYDMYHLSREGEAHERRLPAGTKVNGTFQANFPLGPATHGGTYRCFGSFRDSPYEWSKSSDPLLVSVTGNPSNSWPSPTEPSSETGNPRHLHVLIGTSVVKIPFTILLFFLLHRWCSDKKNAAVMDQEPAGNRTVNSEDSDEQDHQEVSYA	Clinical trial	Daratumumab-mediated lysis of primary multiple myeloma cells is enhanced in combination with the human anti-KIR antibody IPH2102 and lenalidomide. Haematologica. 2015 Feb;100(2):263-8.	21	.	.	.	.	.	.	.	.	.	.	hsa04612: Antigen processing and presentation; hsa04650: Natural killer cell mediated cytotoxicity	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-2172127: DAP12 interactions	.	Q14954
TTV3CFI	MHC class I NK cell receptor 2DS2 (CD158j)	P43631	KI2S2_HUMAN	Immunoglobulin	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	KIR2DS2	Receptor on natural killer (NK) cells for HLA-C alleles. Does not inhibit the activity of NK cells.	.	4N8V; 1M4K	MSLMVVSMACVGFFLLQGAWPHEGVHRKPSLLAHPGPLVKSEETVILQCWSDVRFEHFLLHREGKYKDTLHLIGEHHDGVSKANFSIGPMMQDLAGTYRCYGSVTHSPYQLSAPSDPLDIVITGLYEKPSLSAQPGPTVLAGESVTLSCSSRSSYDMYHLSREGEAHERRFSAGPKVNGTFQADFPLGPATHGGTYRCFGSFRDSPYEWSNSSDPLLVSVTGNPSNSWPSPTEPSSKTGNPRHLHVLIGTSVVKIPFTILLFFLLHRWCSNKKNAAVMDQEPAGNRTVNSEDSDEQDHQEVSYA	Clinical trial	Daratumumab-mediated lysis of primary multiple myeloma cells is enhanced in combination with the human anti-KIR antibody IPH2102 and lenalidomide. Haematologica. 2015 Feb;100(2):263-8.	21	.	.	.	.	.	.	.	.	.	.	hsa04612: Antigen processing and presentation; hsa04650: Natural killer cell mediated cytotoxicity	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-2172127: DAP12 interactions	.	P43631
TTQH3N0	MHC class I NK cell receptor 3DL2 (CD158k)	P43630	KI3L2_HUMAN	Immunoglobulin	p70 natural killer cell receptor clone CL5; p70 NK receptor CL5; Natural killerassociated transcript 4; NKAT4; KIR3DL2; CD158k; CD158 antigenlike family member K	KIR3DL2	Receptor on natural killer (NK) cells for HLA-A alleles. Inhibits the activity of NK cells thus preventing cell lysis.	.	.	MSLTVVSMACVGFFLLQGAWPLMGGQDKPFLSARPSTVVPRGGHVALQCHYRRGFNNFMLYKEDRSHVPIFHGRIFQESFIMGPVTPAHAGTYRCRGSRPHSLTGWSAPSNPLVIMVTGNHRKPSLLAHPGPLLKSGETVILQCWSDVMFEHFFLHREGISEDPSRLVGQIHDGVSKANFSIGPLMPVLAGTYRCYGSVPHSPYQLSAPSDPLDIVITGLYEKPSLSAQPGPTVQAGENVTLSCSSWSSYDIYHLSREGEAHERRLRAVPKVNRTFQADFPLGPATHGGTYRCFGSFRALPCVWSNSSDPLLVSVTGNPSSSWPSPTEPSSKSGICRHLHVLIGTSVVIFLFILLLFFLLYRWCSNKKNAAVMDQEPAGDRTVNRQDSDEQDPQEVTYAQLDHCVFIQRKISRPSQRPKTPLTDTSVYTELPNAEPRSKVVSCPRAPQSGLEGVF	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	hsa04612: Antigen processing and presentation; hsa04650: Natural killer cell mediated cytotoxicity; hsa05332: Graft-versus-host disease	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	P43630
TTU2O6T	Metastasis-suppressor KiSS-1 (KISS1)	Q15726	KISS1_HUMAN	.	KiSS-1; KISS1	KISS1	"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."	.	.	MNSLVSWQLLLFLCATHFGEPLEKVASVGNSRPTGQQLESLGLLAPGEQSLPCTERKPAATARLSRRGTSLSPPPESSGSPQQPGLSAPHSRQIPAPQGAVLVQREKDLPNYNWNSFGLRFGKREAAPGNHGRSAGRG	Clinical trial	"Pharmacologic profiles of investigational kisspeptin/metastin analogues, TAK-448 and TAK-683, in adult male rats in comparison to the GnRH analogue leuprolide.Eur J Pharmacol.2014 Jul 15;735:77-85."	21	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04929: GnRH secretion	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-416476: G alpha (q) signalling events	.	Q15726
TT3KBZY	G-protein coupled receptor 54 (KISS1R)	Q969F8	KISSR_HUMAN	GPCR rhodopsin	KiSS-1 receptor GPR54; KISS1R; GPR54	KISS1R	"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."	.	.	MHTVATSGPNASWGAPANASGCPGCGANASDGPVPSPRAVDAWLVPLFFAALMLLGLVGNSLVIYVICRHKPMRTVTNFYIANLAATDVTFLLCCVPFTALLYPLPGWVLGDFMCKFVNYIQQVSVQATCATLTAMSVDRWYVTVFPLRALHRRTPRLALAVSLSIWVGSAAVSAPVLALHRLSPGPRAYCSEAFPSRALERAFALYNLLALYLLPLLATCACYAAMLRHLGRVAVRPAPADSALQGQVLAERAGAVRAKVSRLVAAVVLLFAACWGPIQLFLVLQALGPAGSWHPRSYAAYALKTWAHCMSYSNSALNPLLYAFLGSHFRQAFRRVCPCAPRRPRRPRRPGPSDPAAPHAELLRLGSHPAPARAQKPGSSGLAARGLCVLGEDNAPL	Discontinued	"Clinical pipeline report, company report or official report of Takeda (2009)."	3	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events	.	Q969F8
TTX41N9	Tyrosine-protein kinase Kit (KIT)	P10721	KIT_HUMAN	Kinase	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	KIT	"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."	EC 2.7.10.1	6GQM; 6GQL; 6GQK; 6GQJ; 4U0I	MRGARGAWDFLCVLLLLLRVQTGSSQPSVSPGEPSPPSIHPGKSDLIVRVGDEIRLLCTDPGFVKWTFEILDETNENKQNEWITEKAEATNTGKYTCTNKHGLSNSIYVFVRDPAKLFLVDRSLYGKEDNDTLVRCPLTDPEVTNYSLKGCQGKPLPKDLRFIPDPKAGIMIKSVKRAYHRLCLHCSVDQEGKSVLSEKFILKVRPAFKAVPVVSVSKASYLLREGEEFTVTCTIKDVSSSVYSTWKRENSQTKLQEKYNSWHHGDFNYERQATLTISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFPMINTTVFVNDGENVDLIVEYEAFPKPEHQQWIYMNRTFTDKWEDYPKSENESNIRYVSELHLTRLKGTEGGTYTFLVSNSDVNAAIAFNVYVNTKPEILTYDRLVNGMLQCVAAGFPEPTIDWYFCPGTEQRCSASVLPVDVQTLNSSGPPFGKLVVQSSIDSSAFKHNGTVECKAYNDVGKTSAYFNFAFKGNNKEQIHPHTLFTPLLIGFVIVAGMMCIIVMILTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYKNLLHSKESSCSDSTNEYMDMKPGVSYVVPTKADKRRSVRIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISESTNHIYSNLANCSPNRQKPVVDHSVRINSVGSTASSSQPLLVHDDV	Successful	A comparison of physicochemical property profiles of marketed oral drugs and orally bioavailable anti-cancer protein kinase inhibitors in clinical development. Curr Top Med Chem. 2007;7(14):1408-22.	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Immunoglobulin domain; Protein tyrosine kinase	PF00047; PF07714	PF00047; ig; PF07714; Pkinase_Tyr	.	.	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	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	.	P10721
TT3IFEZ	Mutated tyrosine-protein kinase Kit (mKIT)	P10721 (mutated)	KIT_HUMAN	Kinase	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)	KIT	"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."	EC 2.7.10.1	6GQM; 6GQL; 6GQK; 6GQJ; 4U0I	MRGARGAWDFLCVLLLLLRVQTGSSQPSVSPGEPSPPSIHPGKSDLIVRVGDEIRLLCTDPGFVKWTFEILDETNENKQNEWITEKAEATNTGKYTCTNKHGLSNSIYVFVRDPAKLFLVDRSLYGKEDNDTLVRCPLTDPEVTNYSLKGCQGKPLPKDLRFIPDPKAGIMIKSVKRAYHRLCLHCSVDQEGKSVLSEKFILKVRPAFKAVPVVSVSKASYLLREGEEFTVTCTIKDVSSSVYSTWKRENSQTKLQEKYNSWHHGDFNYERQATLTISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFPMINTTVFVNDGENVDLIVEYEAFPKPEHQQWIYMNRTFTDKWEDYPKSENESNIRYVSELHLTRLKGTEGGTYTFLVSNSDVNAAIAFNVYVNTKPEILTYDRLVNGMLQCVAAGFPEPTIDWYFCPGTEQRCSASVLPVDVQTLNSSGPPFGKLVVQSSIDSSAFKHNGTVECKAYNDVGKTSAYFNFAFKGNNKEQIHPHTLFTPLLIGFVIVAGMMCIIVMILTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYKNLLHSKESSCSDSTNEYMDMKPGVSYVVPTKADKRRSVRIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISESTNHIYSNLANCSPNRQKPVVDHSVRINSVGSTASSSQPLLVHDDV	Literature-reported	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	.	.	.	P10721
TTGTJB2	KIT D816V mutant (KIT D816V)	P10721	KIT_HUMAN	Kinase	SCFR; Piebald trait protein; PBT; Proto-oncogene c-Kit; Tyrosine-protein kinase Kit; p145 c-kit; v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog; CD117	KIT	"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. {ECO:0000269|PubMed:10397721, ECO:0000269|PubMed:12444928, ECO:0000269|PubMed:12511554, ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:17904548, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:21640708, ECO:0000269|PubMed:7520444, ECO:0000269|PubMed:9528781}."	EC 2.7.10.1	1PKG;1T45;1T46;2E9W;2EC8;2IUH;2VIF;3G0E;3G0F;4HVS;4K94;4K9E;4PGZ;4U0I;6GQJ;6GQK;6GQL;6GQM;6HH1;6ITT;6ITV;6KLA;6MOB;6XV9;6XVA;6XVB;7KHG;7KHJ;7KHK;7ZW8;8DFM;8DFP;8DFQ	MRGARGAWDFLCVLLLLLRVQTGSSQPSVSPGEPSPPSIHPGKSDLIVRVGDEIRLLCTDPGFVKWTFEILDETNENKQNEWITEKAEATNTGKYTCTNKHGLSNSIYVFVRDPAKLFLVDRSLYGKEDNDTLVRCPLTDPEVTNYSLKGCQGKPLPKDLRFIPDPKAGIMIKSVKRAYHRLCLHCSVDQEGKSVLSEKFILKVRPAFKAVPVVSVSKASYLLREGEEFTVTCTIKDVSSSVYSTWKRENSQTKLQEKYNSWHHGDFNYERQATLTISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFPMINTTVFVNDGENVDLIVEYEAFPKPEHQQWIYMNRTFTDKWEDYPKSENESNIRYVSELHLTRLKGTEGGTYTFLVSNSDVNAAIAFNVYVNTKPEILTYDRLVNGMLQCVAAGFPEPTIDWYFCPGTEQRCSASVLPVDVQTLNSSGPPFGKLVVQSSIDSSAFKHNGTVECKAYNDVGKTSAYFNFAFKGNNKEQIHPHTLFTPLLIGFVIVAGMMCIIVMILTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYKNLLHSKESSCSDSTNEYMDMKPGVSYVVPTKADKRRSVRIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISESTNHIYSNLANCSPNRQKPVVDHSVRINSVGSTASSSQPLLVHDDV	Clinical trial	"Clinical pipeline report, company report or official report of Cogent Biosciences"	.	.	.	.	.	.	.	.	.	.	.	hsa:3815	R-HSA-1257604;R-HSA-1433557;R-HSA-1433559;R-HSA-2219530;R-HSA-5673001;R-HSA-6811558;R-HSA-8866910;R-HSA-9669914;R-HSA-9669917;R-HSA-9669921;R-HSA-9669924;R-HSA-9669926;R-HSA-9669929;R-HSA-9669933;R-HSA-9669934;R-HSA-9669935;R-HSA-9669936;R-HSA-9670439;R-HSA-9680187;	.	P10721;
TTDJ51N	Mast cell growth factor (MGF)	P21583	SCF_HUMAN	.	sKITLG; cKit ligand; c-Kit ligand; Stem cell factor; Soluble KIT ligand; SCF; Kit ligand	KITLG	"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."	.	2E9W; 1SCF; 1EXZ	MKKTQTWILTCIYLQLLLFNPLVKTEGICRNRVTNNVKDVTKLVANLPKDYMITLKYVPGMDVLPSHCWISEMVVQLSDSLTDLLDKFSNISEGLSNYSIIDKLVNIVDDLVECVKENSSKDLKKSFKSPEPRLFTPEEFFRIFNRSIDAFKDFVVASETSDCVVSSTLSPEKDSRVSVTKPFMLPPVAASSLRNDSSSSNRKAKNPPGDSSLHWAAMALPALFSLIIGFAFGALYWKKRQPSLTRAVENIQINEEDNEISMLQEKEREFQEV	Literature-reported	KITLG is a novel target of miR-34c that is associated with the inhibition of growth and invasion in colorectal cancer cells. J Cell Mol Med. 2014 Oct;18(10):2092-102.	.	.	.	SCF family.	.	.	Stem cell factor	PF02404	PF02404; SCF	.	.	hsa04010: MAPK signaling pathway; hsa04014: Ras signaling pathway; hsa04015: Rap1 signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04640: Hematopoietic cell lineage; hsa04916: Melanogenesis; hsa05200: Pathways in cancer	"R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1433557: Signaling by SCF-KIT; R-HSA-1433559: Regulation of KIT signaling; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling"	.	P21583
TTARBVH	Beta-klotho (KLB)	Q86Z14	KLOTB_HUMAN	Glycosylase	Klotho beta-like protein; BetaKlotho; BKL	KLB	"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."	.	6NFJ; 5WI9; 5VAQ; 5VAN; 5VAK	MKPGCAAGSPGNEWIFFSTDEITTRYRNTMSNGGLQRSVILSALILLRAVTGFSGDGRAIWSKNPNFTPVNESQLFLYDTFPKNFFWGIGTGALQVEGSWKKDGKGPSIWDHFIHTHLKNVSSTNGSSDSYIFLEKDLSALDFIGVSFYQFSISWPRLFPDGIVTVANAKGLQYYSTLLDALVLRNIEPIVTLYHWDLPLALQEKYGGWKNDTIIDIFNDYATYCFQMFGDRVKYWITIHNPYLVAWHGYGTGMHAPGEKGNLAAVYTVGHNLIKAHSKVWHNYNTHFRPHQKGWLSITLGSHWIEPNRSENTMDIFKCQQSMVSVLGWFANPIHGDGDYPEGMRKKLFSVLPIFSEAEKHEMRGTADFFAFSFGPNNFKPLNTMAKMGQNVSLNLREALNWIKLEYNNPRILIAENGWFTDSRVKTEDTTAIYMMKNFLSQVLQAIRLDEIRVFGYTAWSLLDGFEWQDAYTIRRGLFYVDFNSKQKERKPKSSAHYYKQIIRENGFSLKESTPDVQGQFPCDFSWGVTESVLKPESVASSPQFSDPHLYVWNATGNRLLHRVEGVRLKTRPAQCTDFVNIKKQLEMLARMKVTHYRFALDWASVLPTGNLSAVNRQALRYYRCVVSEGLKLGISAMVTLYYPTHAHLGLPEPLLHADGWLNPSTAEAFQAYAGLCFQELGDLVKLWITINEPNRLSDIYNRSGNDTYGAAHNLLVAHALAWRLYDRQFRPSQRGAVSLSLHADWAEPANPYADSHWRAAERFLQFEIAWFAEPLFKTGDYPAAMREYIASKHRRGLSSSALPRLTEAERRLLKGTVDFCALNHFTTRFVMHEQLAGSRYDSDRDIQFLQDITRLSSPTRLAVIPWGVRKLLRWVRRNYGDMDIYITASGIDDQALEDDRLRKYYLGKYLQEVLKAYLIDKVRIKGYYAFKLAEEKSKPRFGFFTSDFKAKSSIQFYNKVISSRGFPFENSSSRCSQTQENTECTVCLFLVQKKPLIFLGCCFFSTLVLLLSIAIFQRQKRRKFWKAKNLQHIPLKKGKRVVS	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	EC:3.2	Glycosyl hydrolase family	glycosyl hydrolase 1 family. Klotho subfamily.	.	.	Glycosyl hydrolase family 1	PF00232	PF00232; Glyco_hydro_1	8.A.49.1.2	The Klotho Auxiliary Protein (Klotho) Family	hsa04714: Thermogenesis	"R-HSA-109704: PI3K Cascade; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1307965: betaKlotho-mediated ligand binding; R-HSA-2219530: Constitutive Signaling by Aberrant PI3K in Cancer; R-HSA-5654228: Phospholipase C-mediated cascade, FGFR4; 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; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling"	.	Q86Z14
TTHDS05	Klebsiella Fimbrial subunit type 3 (Klebsiella mrkA)	P12267	FM3_KLEPN	.	.	Klebsiella mrkA	.	.	.	MKKVLLSAAMATAFFGMAAANAADTNVGGGQVNFFGKVTDVSCTVSVNGQGSDANVYLSPVTLTEVKAAAADTYLKPKSFTIDVSDCQAADGTKQDDVSKLGVNWTGGNLLAGATAKQQGYLANTEAAGAQNIQLVLSTDNATALTNKIIPGDSTQPKAAGDASAVQDGARFTYYVGYATSTPTTVTTGVVNSYATYEITYQ	Preclinical	Anti-MrkA Monoclonal Antibodies Reveal Distinct Structural and Antigenic Features of MrkA. PLoS One. 2017 Jan 20;12(1):e0170529.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P12267
TTTI53X	Kruppel like factor 4 (KLF4)	O43474	KLF4_HUMAN	.	Krueppellike factor 4; Krueppel-like factor 4; Gutenriched krueppellike factor; Gut-enriched krueppel-like factor; GKLF; Epithelial zinc finger protein EZF; EZF	KLF4	"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."	.	.	MRQPPGESDMAVSDALLPSFSTFASGPAGREKTLRQAGAPNNRWREELSHMKRLPPVLPGRPYDLAAATVATDLESGGAGAACGGSNLAPLPRRETEEFNDLLDLDFILSNSLTHPPESVAATVSSSASASSSSSPSSSGPASAPSTCSFTYPIRAGNDPGVAPGGTGGGLLYGRESAPPPTAPFNLADINDVSPSGGFVAELLRPELDPVYIPPQQPQPPGGGLMGKFVLKASLSAPGSEYGSPSVISVSKGSPDGSHPVVVAPYNGGPPRTCPKIKQEAVSSCTHLGAGPPLSNGHRPAAHDFPLGRQLPSRTTPTLGLEEVLSSRDCHPALPLPPGFHPHPGPNYPSFLPDQMQPQVPPLHYQGQSRGFVARAGEPCVCWPHFGTHGMMLTPPSSPLELMPPGSCMPEEPKPKRGRRSWPRKRTATHTCDYAGCGKTYTKSSHLKAHLRTHTGEKPYHCDWDGCGWKFARSDELTRHYRKHTGHRPFQCQKCDRAFSRSDHLALHMKRHF	Clinical trial	"Phase 1 study of APTO-253 HCl, an inducer of KLF4, in patients with advanced or metastatic solid tumors. Invest New Drugs. 2015 Oct;33(5):1086-92."	17	.	.	krueppel C2H2-type zinc-finger protein family.	.	.	"Zinc finger, C2H2 type"	PF00096	PF00096; zf-C2H2	.	.	hsa04550:Signaling pathways regulating pluripotency of stem cells	R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-452723:Transcriptional regulation of pluripotent stem cells	.	O43474
TT5T3P6	Tissue kallikrein (KLK1)	P06870	KLK1_HUMAN	Peptidase	Kidney/pancreas/salivary gland kallikrein; Kallikrein1; Kallikrein-1	KLK1	Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.	EC 3.4.21.35	1SPJ	MWFLVLCLALSLGGTGAAPPIQSRIVGGWECEQHSQPWQAALYHFSTFQCGGILVHRQWVLTAAHCISDNYQLWLGRHNLFDDENTAQFVHVSESFPHPGFNMSLLENHTRQADEDYSHDLMLLRLTEPADTITDAVKVVELPTEEPEVGSTCLASGWGSIEPENFSFPDDLQCVDLKILPNDECKKAHVQKVTDFMLCVGHLEGGKDTCVGDSGGPLMCDGVLQGVTSWGYVPCGTPNKPSVAVRVLSYVKWIEDTIAENS	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2865).	0	EC:3.4	.	peptidase S1 family. Kallikrein subfamily.	3.4.21.35	Acting on peptide bonds (peptidases)	Trypsin	PF00089	PF00089; Trypsin	.	.	hsa04961:Endocrine and other factor-regulated calcium reabsorption	R-HSA-381426:Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)	.	P06870
TTDA81R	Kallikrein-14 (KLK14)	Q9P0G3	KLK14_HUMAN	Peptidase	hK14; Kallikrein-like protein 6; KLKL6; KLK-L6	KLK14	"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."	EC 3.4.21.-	.	MSLRVLGSGTWPSAPKMFLLLTALQVLAIAMTQSQEDENKIIGGHTCTRSSQPWQAALLAGPRRRFLCGGALLSGQWVITAAHCGRPILQVALGKHNLRRWEATQQVLRVVRQVTHPNYNSRTHDNDLMLLQLQQPARIGRAVRPIEVTQACASPGTSCRVSGWGTISSPIARYPASLQCVNINISPDEVCQKAYPRTITPGMVCAGVPQGGKDSCQGDSGGPLVCRGQLQGLVSWGMERCALPGYPGVYTNLCKYRSWIEETMRDK	Patented-recorded	"1,2,4-Triazole derivatives as transient inactivators of kallikreins involved in skin diseases. Bioorg Med Chem Lett. 2013 Aug 15;23(16):4547-51."	0	EC:3.4	.	peptidase S1 family. Kallikrein subfamily.	3.4.21.-	Acting on peptide bonds (peptidases)	Trypsin	PF00089	PF00089; Trypsin	.	.	.	R-HSA-6809371: Formation of the cornified envelope	.	Q9P0G3
TTJLNAW	Tissue kallikrein (KLK2)	P20151	KLK2_HUMAN	Peptidase	hGK-1; Tissue kallikrein-2; Kallikrein-2; Glandular kallikrein-1	KLK2	Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.	EC 3.4.21.35	4NFF; 4NFE	MWDLVLSIALSVGCTGAVPLIQSRIVGGWECEKHSQPWQVAVYSHGWAHCGGVLVHPQWVLTAAHCLKKNSQVWLGRHNLFEPEDTGQRVPVSHSFPHPLYNMSLLKHQSLRPDEDSSHDLMLLRLSEPAKITDVVKVLGLPTQEPALGTTCYASGWGSIEPEEFLRPRSLQCVSLHLLSNDMCARAYSEKVTEFMLCAGLWTGGKDTCGGDSGGPLVCNGVLQGITSWGPEPCALPEKPAVYTKVVHYRKWIKDTIAANP	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	24	EC:3.4	Peptidase	peptidase S1 family. Kallikrein subfamily.	3.4.21.35	Acting on peptide bonds (peptidases)	Trypsin	PF00089	PF00089; Trypsin	.	.	hsa04961:Endocrine and other factor-regulated calcium reabsorption	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	.	P20151
TTS78AZ	Prostate specific antigen (KLK3)	P07288	KLK3_HUMAN	Peptidase	Seminin; Semenogelase; Prostate-specific antigen; PSA; P-30 antigen; Kallikrein-3; Gamma-seminoprotein; APS	KLK3	Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum.	EC 3.4.21.77	3QUM; 2ZCL; 2ZCK; 2ZCH; 2PSA	MWVPVVFLTLSVTWIGAAPLILSRIVGGWECEKHSQPWQVLVASRGRAVCGGVLVHPQWVLTAAHCIRNKSVILLGRHSLFHPEDTGQVFQVSHSFPHPLYDMSLLKNRFLRPGDDSSHDLMLLRLSEPAELTDAVKVMDLPTQEPALGTTCYASGWGSIEPEEFLTPKKLQCVDLHVISNDVCAQVHPQKVTKFMLCAGRWTGGKSTCSGDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKVVHYRKWIKDTIVANP	Clinical trial	Motexafin lutetium-photodynamic therapy of prostate cancer: short- and long-term effects on prostate-specific antigen. Clin Cancer Res. 2008 Aug 1;14(15):4869-76.	25	EC:3.4	Peptidase	peptidase S1 family. Kallikrein subfamily.	3.4.21.77	Acting on peptide bonds (peptidases)	Trypsin	PF00089	PF00089; Trypsin	.	.	hsa05200:Pathways in cancer; hsa05215:Prostate cancer	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	.	P07288
TT4319X	Kallikrein-4 (KLK4)	Q9Y5K2	KLK4_HUMAN	Peptidase	Serine protease 17; Prostase; PSTS; PRSS17; Kallikreinlike protein 1; Kallikrein4; Kallikrein-like protein 1; KLKL1; KLK-L1; Enamel matrix serine proteinase 1; EMSP1	KLK4	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.	EC 3.4.21.-	4KGA; 4KEL; 4K8Y; 4K1E; 2BDI	MATAGNPWGWFLGYLILGVAGSLVSGSCSQIINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNSYTIGLGLHSLEADQEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESDTIRSISIASQCPTAGNSCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSKLYDPLYHPSMFCAGGGHDQKDSCNGDSGGPLICNGYLQGLVSFGKAPCGQVGVPGVYTNLCKFTEWIEKTVQAS	Patented-recorded	Serine protease inhibitors to treat inflammation: a patent review (2011-2016).Expert Opin Ther Pat. 2018 Feb;28(2):93-110.	15.5	EC:3.4	Peptidase	peptidase S1 family. Kallikrein subfamily.	3.4.21.-	Acting on peptide bonds (peptidases)	Trypsin	PF00089	PF00089; Trypsin	.	.	.	.	.	Q9Y5K2
TTULSEW	Kallikrein-5 (KLK5)	Q9Y337	KLK5_HUMAN	Peptidase	UNQ570/PRO1132; Stratum corneum tryptic enzyme; SCTE; Kallikrein-like protein 2; KLK-L2	KLK5	May be involved in desquamation.	EC 3.4.21.-	6QFE; 2PSY; 2PSX	MATARPPWMWVLCALITALLLGVTEHVLANNDVSCDHPSNTVPSGSNQDLGAGAGEDARSDDSSSRIINGSDCDMHTQPWQAALLLRPNQLYCGAVLVHPQWLLTAAHCRKKVFRVRLGHYSLSPVYESGQQMFQGVKSIPHPGYSHPGHSNDLMLIKLNRRIRPTKDVRPINVSSHCPSAGTKCLVSGWGTTKSPQVHFPKVLQCLNISVLSQKRCEDAYPRQIDDTMFCAGDKAGRDSCQGDSGGPVVCNGSLQGLVSWGDYPCARPNRPGVYTNLCKFTKWIQETIQANS	Patented-recorded	"1,2,4-Triazole derivatives as transient inactivators of kallikreins involved in skin diseases. Bioorg Med Chem Lett. 2013 Aug 15;23(16):4547-51."	0	EC:3.4	.	peptidase S1 family. Kallikrein subfamily.	3.4.21.-	Acting on peptide bonds (peptidases)	Trypsin	PF00089	PF00089; Trypsin	.	.	.	R-HSA-6809371: Formation of the cornified envelope	.	Q9Y337
TTLPF4X	Kallikrein-6 (KLK6)	Q92876	KLK6_HUMAN	Peptidase	Zyme; Serine protease 9; Serine protease 18; SP59; Protease M; PRSS9; PRSS18; Neurosin; MSP; K6	KLK6	"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."	EC 3.4.21.-	6QHC; 6QHB; 6QHA; 6QH9; 6QFH	MKKLMVVLSLIAAAWAEEQNKLVHGGPCDKTSHPYQAALYTSGHLLCGGVLIHPLWVLTAAHCKKPNLQVFLGKHNLRQRESSQEQSSVVRAVIHPDYDAASHDQDIMLLRLARPAKLSELIQPLPLERDCSANTTSCHILGWGKTADGDFPDTIQCAYIHLVSREECEHAYPGQITQNMLCAGDEKYGKDSCQGDSGGPLVCGDHLRGLVSWGNIPCGSKEKPGVYTNVCRYTNWIQKTIQAK	Literature-reported	Virtual Screening and X-ray Crystallography for Human Kallikrein 6 Inhibitors with an Amidinothiophene P1 Group. ACS Med Chem Lett. 2012 Jan 11;3(2):159-64.	0	EC:3.4	.	peptidase S1 family. Kallikrein subfamily.	3.4.21.-	Acting on peptide bonds (peptidases)	Trypsin	PF00089	PF00089; Trypsin	.	.	.	.	.	Q92876
TTE6GTB	Kallikrein-7 (KLK7)	P49862	KLK7_HUMAN	Peptidase	hK7; Stratum corneum chymotryptic enzyme; Serine protease 6; SCCE; PRSS6; HSCCE	KLK7	"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."	EC 3.4.21.117	5YJK; 5Y9L; 5FAH; 3BSQ; 2QXJ	MARSLLLPLQILLLSLALETAGEEAQGDKIIDGAPCARGSHPWQVALLSGNQLHCGGVLVNERWVLTAAHCKMNEYTVHLGSDTLGDRRAQRIKASKSFRHPGYSTQTHVNDLMLVKLNSQARLSSMVKKVRLPSRCEPPGTTCTVSGWGTTTSPDVTFPSDLMCVDVKLISPQDCTKVYKDLLENSMLCAGIPDSKKNACNGDSGGPLVCRGTLQGLVSWGTFPCGQPNDPGVYTQVCKFTKWINDTMKKHR	Patented-recorded	"1,2,4-Triazole derivatives as transient inactivators of kallikreins involved in skin diseases. Bioorg Med Chem Lett. 2013 Aug 15;23(16):4547-51."	0	EC:3.4	Peptidase	peptidase S1 family. Kallikrein subfamily.	3.4.21.117	Acting on peptide bonds (peptidases)	Trypsin	PF00089	PF00089; Trypsin	.	.	.	R-HSA-1474228:Degradation of the extracellular matrix	.	P49862
TTH5MRS	Neuropsin (KLK8)	O60259	KLK8_HUMAN	Peptidase	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)	KLK8	"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."	EC 3.4.21.118	5MS4; 5MS3	MGRPRPRAAKTWMFLLLLGGAWAGHSRAQEDKVLGGHECQPHSQPWQAALFQGQQLLCGGVLVGGNWVLTAAHCKKPKYTVRLGDHSLQNKDGPEQEIPVVQSIPHPCYNSSDVEDHNHDLMLLQLRDQASLGSKVKPISLADHCTQPGQKCTVSGWGTVTSPRENFPDTLNCAEVKIFPQKKCEDAYPGQITDGMVCAGSSKGADTCQGDSGGPLVCDGALQGITSWGSDPCGRSDKPGVYTNICRYLDWIKKIIGSKG	Literature-reported	The human KLK8 (neuropsin/ovasin) gene: identification of two novel splice variants and its prognostic value in ovarian cancer. Clin Cancer Res. 2001 Apr;7(4):806-11.	.	EC:3.4	.	peptidase S1 family. Kallikrein subfamily.	3.4.21.118	Acting on peptide bonds (peptidases)	Trypsin	PF00089	PF00089; Trypsin	.	.	.	R-HSA-6809371: Formation of the cornified envelope	.	O60259
TTN0PCX	Plasma kallikrein messenger RNA (KLKB1 mRNA)	P03952	KLKB1_HUMAN	mRNA target	Plasma prekallikrein (mRNA); Plasma kallikrein light chain (mRNA); Plasma kallikrein heavy chain (mRNA); PKK (mRNA); Kininogenin (mRNA); KLK3 (mRNA); Fletcher factor (mRNA)	KLKB1	"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."	EC 3.4.21.34	6O1S; 6O1G; 6I44; 5TJX; 5F8Z	MILFKQATYFISLFATVSCGCLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPASSINDMEKRFGCFLKDSVTGTLPKVHRTGAVSGHSLKQCGHQISACHRDIYKGVDMRGVNFNVSKVSSVEECQKRCTNNIRCQFFSYATQTFHKAEYRNNCLLKYSPGGTPTAIKVLSNVESGFSLKPCALSEIGCHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNVWKIESQRNVCLLKTSESGTPSSSTPQENTISGYSLLTCKRTLPEPCHSKIYPGVDFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSLLPEDCKEEKCKCFLRLSMDGSPTRIAYGTQGSSGYSLRLCNTGDNSVCTTKTSTRIVGGTNSSWGEWPWQVSLQVKLTAQRHLCGGSLIGHQWVLTAAHCFDGLPLQDVWRIYSGILNLSDITKDTPFSQIKEIIIHQNYKVSEGNHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKEKGEIQNILQKVNIPLVTNEECQKRYQDYKITQRMVCAGYKEGGKDACKGDSGGPLVCKHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWILEKTQSSDGKAQMQSPA	Clinical trial	"Clinical pipeline report, company report or official report of ISIS Pharmaceuticals."	25	mRNA	mRNA target	.	.	.	PAN domain; Trypsin	PF00024; PF00089	PF00024; PAN_1; PF00089; Trypsin	.	.	hsa04610:Complement and coagulation cascades	R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-1592389:Activation of Matrix Metalloproteinases	.	P03952
TTMF8H9	Plasma kallikrein (KLKB1)	P03952	KLKB1_HUMAN	Peptidase	Plasma prekallikrein; Plasma kallikrein light chain; Plasma kallikrein heavy chain; PKK; Kininogenin; KLK3; Fletcher factor	KLKB1	"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."	EC 3.4.21.34	6O1S; 6O1G; 6I44; 5TJX; 5F8Z	MILFKQATYFISLFATVSCGCLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPASSINDMEKRFGCFLKDSVTGTLPKVHRTGAVSGHSLKQCGHQISACHRDIYKGVDMRGVNFNVSKVSSVEECQKRCTNNIRCQFFSYATQTFHKAEYRNNCLLKYSPGGTPTAIKVLSNVESGFSLKPCALSEIGCHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNVWKIESQRNVCLLKTSESGTPSSSTPQENTISGYSLLTCKRTLPEPCHSKIYPGVDFGGEELNVTFVKGVNVCQETCTKMIRCQFFTYSLLPEDCKEEKCKCFLRLSMDGSPTRIAYGTQGSSGYSLRLCNTGDNSVCTTKTSTRIVGGTNSSWGEWPWQVSLQVKLTAQRHLCGGSLIGHQWVLTAAHCFDGLPLQDVWRIYSGILNLSDITKDTPFSQIKEIIIHQNYKVSEGNHDIALIKLQAPLNYTEFQKPICLPSKGDTSTIYTNCWVTGWGFSKEKGEIQNILQKVNIPLVTNEECQKRYQDYKITQRMVCAGYKEGGKDACKGDSGGPLVCKHNGMWRLVGITSWGEGCARREQPGVYTKVAEYMDWILEKTQSSDGKAQMQSPA	Successful	"Ecallantide (DX-88), a plasma kallikrein inhibitor for the treatment of hereditary angioedema and the prevention of blood loss in on-pump cardiothoracic surgery. Expert Opin Biol Ther. 2008 Aug;8(8):1187-99."	34	EC:3.4	.	peptidase S1 family. Plasma kallikrein subfamily.	3.4.21.34	Acting on peptide bonds (peptidases)	PAN domain; Trypsin	PF00024; PF00089	PF00024; PAN_1; PF00089; Trypsin	.	.	hsa04610:Complement and coagulation cascades	R-HSA-140837:Intrinsic Pathway of Fibrin Clot Formation; R-HSA-1592389:Activation of Matrix Metalloproteinases	.	P03952
TTC4IMS	NKG2-A/B-activating NK receptor (NKG2A)	P26715	NKG2A_HUMAN	.	NKG2A/NKG2B type II integral membrane protein; NKG2A/Bactivating NK receptor; NK cell receptor A; KLRC1; CD159a; CD159 antigenlike family member A	KLRC1	Plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells.	.	3CII; 3CDG; 3BDW; 2YU7; 2RMX	MDNQGVIYSDLNLPPNPKRQQRKPKGNKNSILATEQEITYAELNLQKASQDFQGNDKTYHCKDLPSAPEKLIVGILGIICLILMASVVTIVVIPSTLIQRHNNSSLNTRTQKARHCGHCPEEWITYSNSCYYIGKERRTWEESLLACTSKNSSLLSIDNEEEMKFLSIISPSSWIGVFRNSSHHPWVTMNGLAFKHEIKDSDNAELNCAVLQVNRLKSAQCGSSIIYHCKHKL	Clinical trial	Handbook of Therapeutic Antibodies. 2014. 1. Page(1098).	21	.	.	.	.	.	.	.	.	.	.	hsa04612:Antigen processing and presentation; hsa04650:Natural killer cell mediated cytotoxicity; hsa05332:Graft-versus-host disease	R-HSA-198933:Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	P26715
TT299E6	Killer cell lectin-like receptor subfamily G member 1 (KLRG1)	Q96E93	KLRG1_HUMAN	.	C-type lectin domain family 15 member A; ITIM-containing receptor MAFA-L; MAFA-like receptor; Mast cell function-associated antigen	KLRG1	"Plays an inhibitory role on natural killer (NK) cells and T-cell functions upon binding to their non-MHC ligands. May mediate missing self recognition by binding to a highly conserved site on classical cadherins, enabling it to monitor expression of E-cadherin/CDH1, N-cadherin/CDH2 and R-cadherin/CDH4 on target cells. {ECO:0000269|PubMed:19604491}."	.	3FF7	MTDSVIYSMLELPTATQAQNDYGPQQKSSSSRPSCSCLVAIALGLLTAVLLSVLLYQWILCQGSNYSTCASCPSCPDRWMKYGNHCYYFSVEEKDWNSSLEFCLARDSHLLVITDNQEMSLLQVFLSEAFCWIGLRNNSGWRWEDGSPLNFSRISSNSFVQTCGAINKNGLQASSCEVPLHWVCKKCPFADQALF	Clinical trial	"Clinical pipeline report, company report or official report of Abcuro"	.	.	.	.	.	.	.	.	.	.	.	hsa:10219	R-HSA-198933;	.	Q96E93;
TTLRN4A	NKG2 D activating NK receptor (KLRK1)	P26718	NKG2D_HUMAN	.	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	KLRK1	"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."	.	4S0U; 4PDC; 1MPU; 1KCG; 1HYR	MGWIRGRRSRHSWEMSEFHNYNLDLKKSDFSTRWQKQRCPVVKSKCRENASPFFFCCFIAVAMGIRFIIMVAIWSAVFLNSLFNQEVQIPLTESYCGPCPKNWICYKNNCYQFFDESKNWYESQASCMSQNASLLKVYSKEDQDLLKLVKSYHWMGLVHIPTNGSWQWEDGSILSPNLLTIIEMQKGDCALYASSFKGYIENCSTPNTYICMQRTV	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	Lectin C-type domain	PF00059	PF00059; Lectin_C	1.C.111.1.13	The RegIII&#947; (RegIII&#947;) Family	hsa04650: Natural killer cell mediated cytotoxicity; hsa05144: Malaria	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-2172127: DAP12 interactions; R-HSA-2424491: DAP12 signaling	.	P26718
TTG53PQ	NKG2D-NKG2D ligand interaction (NKG2D-NKG2DL PPI)	P26718-Q9BZM6/Q9BZM5/Q9BZM4	NKG2D_HUMAN-ULBP1_HUMAN/ULBP2_HUMAN/ULBP3_HUMAN	.	NK cell receptor D-NKG2D ligand interaction	KLRK1-ULBP1/ULBP2/ULBP3	Inhibits the outgrowth of naturally arising low-grade B cell lymphoma In vivo.	.	.	MGWIRGRRSRHSWEMSEFHNYNLDLKKSDFSTRWQKQRCPVVKSKCRENASPFFFCCFIAVAMGIRFIIMVAIWSAVFLNSLFNQEVQIPLTESYCGPCPKNWICYKNNCYQFFDESKNWYESQASCMSQNASLLKVYSKEDQDLLKLVKSYHWMGLVHIPTNGSWQWEDGSILSPNLLTIIEMQKGDCALYASSFKGYIENCSTPNTYICMQRTVMAAAASPAFLLCLPLLHLLSGWSRAGWVDTHCLCYDFIITPKSRPEPQWCEVQGLVDERPFLHYDCVNHKAKAFASLGKKVNVTKTWEEQTETLRDVVDFLKGQLLDIQVENLIPIEPLTLQARMSCEHEAHGHGRGSWQFLFNGQKFLLFDSNNRKWTALHPGAKKMTEKWEKNRDVTMFFQKISLGDCKMWLEEFLMYWEQMLDPTKPPSLAPGTTQPKAMATTLSPWSLLIIFLCFILAGR	Literature-reported	Role of NKG2D in cytokine-induced killer cells against lung cancer. Oncol Lett. 2017 May;13(5):3139-3143.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P26718
TTIY56R	Kynurenine 3-hydroxylase (KMO)	O15229	KMO_HUMAN	Paired donor oxygen oxidoreductase	Kynurenine 3monooxygenase; Kynurenine 3-monooxygenase	KMO	"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)."	EC 1.14.13.9	5X68	MDSSVIQRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVATFTRGRSINLALSHRGRQALKAVGLEDQIVSQGIPMRARMIHSLSGKKSAIPYGTKSQYILSVSRENLNKDLLTAAEKYPNVKMHFNHRLLKCNPEEGMITVLGSDKVPKDVTCDLIVGCDGAYSTVRSHLMKKPRFDYSQQYIPHGYMELTIPPKNGDYAMEPNYLHIWPRNTFMMIALPNMNKSFTCTLFMPFEEFEKLLTSNDVVDFFQKYFPDAIPLIGEKLLVQDFFLLPAQPMISVKCSSFHFKSHCVLLGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFSNDLSLCLPVFSRLRIPDDHAISDLSMYNYIEMRAHVNSSWFIFQKNMERFLHAIMPSTFIPLYTMVTFSRIRYHEAVQRWHWQKKVINKGLFFLGSLIAISSTYLLIHYMSPRSFLRLRRPWNWIAHFRNTTCFPAKAVDSLEQISNLISR	Clinical trial	Inhibitors of the kynurenine pathway as neurotherapeutics: a patent review (2012-2015).Expert Opin Ther Pat. 2016 Jul;26(7):815-32.	15.5	EC:1.14	Oxidoreductases acting on paired donors	aromatic-ring hydroxylase family. KMO subfamily.	1.14.13.9 	"Acting on paired donors, with incorporation or reduction of molecular oxygen"	FAD binding domain	PF01494	PF01494; FAD_binding_3	.	.	hsa00380: Tryptophan metabolism; hsa01100: Metabolic pathways; hsa01240: Biosynthesis of cofactors	R-HSA-71240: Tryptophan catabolism	MetaCyc:HS04082-MON	O15229
TT1GNDM	Mixed-lineage leukemia protein (MLL)	Q03164	KMT2A_HUMAN	Methyltransferase	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	KMT2A	"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."	EC 2.1.1.43	6EMQ; 5SVH; 5F6L; 5F5E; 4NW3	MAHSCRWRFPARPGTTGGGGGGGRRGLGGAPRQRVPALLLPPGPPVGGGGPGAPPSPPAVAAAAAAAGSSGAGVPGGAAAASAASSSSASSSSSSSSSASSGPALLRVGPGFDAALQVSAAIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRSPTRSPSVKTSPRKPRGRPRSGSDRNSAILSDPSVFSPLNKSETKSGDKIKKKDSKSIEKKRGRPPTFPGVKIKITHGKDISELPKGNKEDSLKKIKRTPSATFQQATKIKKLRAGKLSPLKSKFKTGKLQIGRKGVQIVRRRGRPPSTERIKTPSGLLINSELEKPQKVRKDKEGTPPLTKEDKTVVRQSPRRIKPVRIIPSSKRTDATIAKQLLQRAKKGAQKKIEKEAAQLQGRKVKTQVKNIRQFIMPVVSAISSRIIKTPRRFIEDEDYDPPIKIARLESTPNSRFSAPSCGSSEKSSAASQHSSQMSSDSSRSSSPSVDTSTDSQASEEIQVLPEERSDTPEVHPPLPISQSPENESNDRRSRRYSVSERSFGSRTTKKLSTLQSAPQQQTSSSPPPPLLTPPPPLQPASSISDHTPWLMPPTIPLASPFLPASTAPMQGKRKSILREPTFRWTSLKHSRSEPQYFSSAKYAKEGLIRKPIFDNFRPPPLTPEDVGFASGFSASGTAASARLFSPLHSGTRFDMHKRSPLLRAPRFTPSEAHSRIFESVTLPSNRTSAGTSSSGVSNRKRKRKVFSPIRSEPRSPSHSMRTRSGRLSSSELSPLTPPSSVSSSLSISVSPLATSALNPTFTFPSHSLTQSGESAEKNQRPRKQTSAPAEPFSSSSPTPLFPWFTPGSQTERGRNKDKAPEELSKDRDADKSVEKDKSRERDREREKENKRESRKEKRKKGSEIQSSSALYPVGRVSKEKVVGEDVATSSSAKKATGRKKSSSHDSGTDITSVTLGDTTAVKTKILIKKGRGNLEKTNLDLGPTAPSLEKEKTLCLSTPSSSTVKHSTSSIGSMLAQADKLPMTDKRVASLLKKAKAQLCKIEKSKSLKQTDQPKAQGQESDSSETSVRGPRIKHVCRRAAVALGRKRAVFPDDMPTLSALPWEEREKILSSMGNDDKSSIAGSEDAEPLAPPIKPIKPVTRNKAPQEPPVKKGRRSRRCGQCPGCQVPEDCGVCTNCLDKPKFGGRNIKKQCCKMRKCQNLQWMPSKAYLQKQAKAVKKKEKKSKTSEKKDSKESSVVKNVVDSSQKPTPSAREDPAPKKSSSEPPPRKPVEEKSEEGNVSAPGPESKQATTPASRKSSKQVSQPALVIPPQPPTTGPPRKEVPKTTPSEPKKKQPPPPESGPEQSKQKKVAPRPSIPVKQKPKEKEKPPPVNKQENAGTLNILSTLSNGNSSKQKIPADGVHRIRVDFKEDCEAENVWEMGGLGILTSVPITPRVVCFLCASSGHVEFVYCQVCCEPFHKFCLEENERPLEDQLENWCCRRCKFCHVCGRQHQATKQLLECNKCRNSYHPECLGPNYPTKPTKKKKVWICTKCVRCKSCGSTTPGKGWDAQWSHDFSLCHDCAKLFAKGNFCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCVNCTERHPAEWRLALEKELQISLKQVLTALLNSRTTSHLLRYRQAAKPPDLNPETEESIPSRSSPEGPDPPVLTEVSKQDDQQPLDLEGVKRKMDQGNYTSVLEFSDDIVKIIQAAINSDGGQPEIKKANSMVKSFFIRQMERVFPWFSVKKSRFWEPNKVSSNSGMLPNAVLPPSLDHNYAQWQEREENSHTEQPPLMKKIIPAPKPKGPGEPDSPTPLHPPTPPILSTDRSREDSPELNPPPGIEDNRQCALCLTYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFLDDKKVYCQRHRDLIKGEVVPENGFEVFRRVFVDFEGISLRRKFLNGLEPENIHMMIGSMTIDCLGILNDLSDCEDKLFPIGYQCSRVYWSTTDARKRCVYTCKIVECRPPVVEPDINSTVEHDENRTIAHSPTSFTESSSKESQNTAEIISPPSPDRPPHSQTSGSCYYHVISKVPRIRTPSYSPTQRSPGCRPLPSAGSPTPTTHEIVTVGDPLLSSGLRSIGSRRHSTSSLSPQRSKLRIMSPMRTGNTYSRNNVSSVSTTGTATDLESSAKVVDHVLGPLNSSTSLGQNTSTSSNLQRTVVTVGNKNSHLDGSSSSEMKQSSASDLVSKSSSLKGEKTKVLSSKSSEGSAHNVAYPGIPKLAPQVHNTTSRELNVSKIGSFAEPSSVSFSSKEALSFPHLHLRGQRNDRDQHTDSTQSANSSPDEDTEVKTLKLSGMSNRSSIINEHMGSSSRDRRQKGKKSCKETFKEKHSSKSFLEPGQVTTGEEGNLKPEFMDEVLTPEYMGQRPCNNVSSDKIGDKGLSMPGVPKAPPMQVEGSAKELQAPRKRTVKVTLTPLKMENESQSKNALKESSPASPLQIESTSPTEPISASENPGDGPVAQPSPNNTSCQDSQSNNYQNLPVQDRNLMLPDGPKPQEDGSFKRRYPRRSARARSNMFFGLTPLYGVRSYGEEDIPFYSSSTGKKRGKRSAEGQVDGADDLSTSDEDDLYYYNFTRTVISSGGEERLASHNLFREEEQCDLPKISQLDGVDDGTESDTSVTATTRKSSQIPKRNGKENGTENLKIDRPEDAGEKEHVTKSSVGHKNEPKMDNCHSVSRVKTQGQDSLEAQLSSLESSRRVHTSTPSDKNLLDTYNTELLKSDSDNNNSDDCGNILPSDIMDFVLKNTPSMQALGESPESSSSELLNLGEGLGLDSNREKDMGLFEVFSQQLPTTEPVDSSVSSSISAEEQFELPLELPSDLSVLTTRSPTVPSQNPSRLAVISDSGEKRVTITEKSVASSESDPALLSPGVDPTPEGHMTPDHFIQGHMDADHISSPPCGSVEQGHGNNQDLTRNSSTPGLQVPVSPTVPIQNQKYVPNSTDSPGPSQISNAAVQTTPPHLKPATEKLIVVNQNMQPLYVLQTLPNGVTQKIQLTSSVSSTPSVMETNTSVLGPMGGGLTLTTGLNPSLPTSQSLFPSASKGLLPMSHHQHLHSFPAATQSSFPPNISNPPSGLLIGVQPPPDPQLLVSESSQRTDLSTTVATPSSGLKKRPISRLQTRKNKKLAPSSTPSNIAPSDVVSNMTLINFTPSQLPNHPSLLDLGSLNTSSHRTVPNIIKRSKSSIMYFEPAPLLPQSVGGTAATAAGTSTISQDTSHLTSGSVSGLASSSSVLNVVSMQTTTTPTSSASVPGHVTLTNPRLLGTPDIGSISNLLIKASQQSLGIQDQPVALPPSSGMFPQLGTSQTPSTAAITAASSICVLPSTQTTGITAASPSGEADEHYQLQHVNQLLASKTGIHSSQRDLDSASGPQVSNFTQTVDAPNSMGLEQNKALSSAVQASPTSPGGSPSSPSSGQRSASPSVPGPTKPKPKTKRFQLPLDKGNGKKHKVSHLRTSSSEAHIPDQETTSLTSGTGTPGAEAEQQDTASVEQSSQKECGQPAGQVAVLPEVQVTQNPANEQESAEPKTVEEEESNFSSPLMLWLQQEQKRKESITEKKPKKGLVFEISSDDGFQICAESIEDAWKSLTDKVQEARSNARLKQLSFAGVNGLRMLGILHDAVVFLIEQLSGAKHCRNYKFRFHKPEEANEPPLNPHGSARAEVHLRKSAFDMFNFLASKHRQPPEYNPNDEEEEEVQLKSARRATSMDLPMPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGNVIRSIQTDKREKYYDSKGIGCYMFRIDDSEVVDATMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN	Literature-reported	Therapeutic Targeting of MLL Degradation Pathways in MLL-Rearranged Leukemia. Cell. 2017 Jan 12;168(1-2):59-72.e13.	.	EC:2.1	Methyltransferase superfamily	class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.	2.1.1.43 	Transferring one-carbon groups	F/Y rich C-terminus; F/Y-rich N-terminus; PHD-finger; SET domain; CXXC zinc finger domain	PF05965; PF05964; PF00628; PF00856; PF02008	PF05965; FYRC; PF05964; FYRN; PF00628; PHD; PF00856; SET; PF02008; zf-CXXC	.	.	hsa00310: Lysine degradation; hsa01100: Metabolic pathways; hsa04934: Cushing syndrome; hsa05202: Transcriptional misregulation in cancer	R-HSA-3214841: PKMTs methylate histone lysines; R-HSA-8936459: RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function; R-HSA-8939236: RUNX1 regulates transcription of genes involved in differentiation of HSCs; R-HSA-9616222: Transcriptional regulation of granulopoiesis	MetaCyc:HS04188-MON	.
TTGC95K	SET domain containing 8 (KMT5A)	Q9NQR1	KMT5A_HUMAN	Methyltransferase	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	KMT5A	"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."	EC 2.1.1.-	6BOZ; 5W1Y; 5V2N; 5TH7; 5TEG	MGEGGAAAALVAAAAAAAAAAAAVVAGQRRRRLGRRARCHGPGRAAGGKMSKPCAVEAAAAAVAATAPGPEMVERRGPGRPRTDGENVFTGQSKIYSYMSPNKCSGMRFPLQEENSVTHHEVKCQGKPLAGIYRKREEKRNAGNAVRSAMKSEEQKIKDARKGPLVPFPNQKSEAAEPPKTPPSSCDSTNAAIAKQALKKPIKGKQAPRKKAQGKTQQNRKLTDFYPVRRSSRKSKAELQSEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGDFVVEYHGDLIEITDAKKREALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHSKCGNCQTKLHDIDGVPHLILIASRDIAAGEELLYDYGDRSKASIEAHPWLKH	Preclinical	Nahuoic acid A produced by a Streptomyces sp. isolated from a marine sediment is a selective SAM-competitive inhibitor of the histone methyltransferase SETD8. Org Lett. 2013 Jan 18;15(2):414-7.	0	EC:2.1	.	class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. PR/SET subfamily.	2.1.1.-	Transferring one-carbon groups	SET domain	PF00856	PF00856; SET	.	.	hsa00310: Lysine degradation; hsa01100: Metabolic pathways	R-HSA-2299718: Condensation of Prophase Chromosomes; R-HSA-3214841: PKMTs methylate histone lysines; R-HSA-6804760: Regulation of TP53 Activity through Methylation	MetaCyc:HS11381-MON	Q9NQR1
TTJGV7F	Histone-lysine N-methyltransferase KMT5B (KMT5B)	Q4FZB7	KMT5B_HUMAN	.	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	KMT5B	"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)."	EC 2.1.1.361	.	MKWLGESKNMVVNGRRNGGKLSNDHQQNQSKLQHTGKDTLKAGKNAVERRSNRCNGNSGFEGQSRYVPSSGMSAKELCENDDLATSLVLDPYLGFQTHKMNTSAFPSRSSRHFSKSDSFSHNNPVRFRPIKGRQEELKEVIERFKKDEHLEKAFKCLTSGEWARHYFLNKNKMQEKLFKEHVFIYLRMFATDSGFEILPCNRYSSEQNGAKIVATKEWKRNDKIELLVGCIAELSEIEENMLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKALRDIEPGEEISCYYGDGFFGENNEFCECYTCERRGTGAFKSRVGLPAPAPVINSKYGLRETDKRLNRLKKLGDSSKNSDSQSVSSNTDADTTQEKNNATSNRKSSVGVKKNSKSRTLTRQSMSRIPASSNSTSSKLTHINNSRVPKKLKKPAKPLLSKIKLRNHCKRLEQKNASRKLEMGNLVLKEPKVVLYKNLPIKKDKEPEGPAQAAVASGCLTRHAAREHRQNPVRGAHSQGESSPCTYITRRSVRTRTNLKEASDIKLEPNTLNGYKSSVTEPCPDSGEQLQPAPVLQEEELAHETAQKGEAKCHKSDTGMSKKKSRQGKLVKQFAKIEESTPVHDSPGKDDAVPDLMGPHSDQGEHSGTVGVPVSYTDCAPSPVGCSVVTSDSFKTKDSFRTAKSKKKRRITRYDAQLILENNSGIPKLTLRRRHDSSSKTNDQENDGMNSSKISIKLSKDHDNDNNLYVAKLNNGFNSGSGSSSTKLKIQLKRDEENRGSYTEGLHENGVCCSDPLSLLESRMEVDDYSQYEEESTDDSSSSEGDEEEDDYDDDFEDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA	Preclinical	The SUV4-20 inhibitor A-196 verifies a role for epigenetics in genomic integrity. Nat Chem Biol. 2017 Mar;13(3):317-324.	.	.	.	.	.	.	.	.	.	.	.	hsa00310: Lysine degradation; hsa01100: Metabolic pathways	R-HSA-3214841: PKMTs methylate histone lysines	MetaCyc:HS12712-MON	Q4FZB7
TT7H3YM	Histone-lysine N-methyltransferase KMT5C (KMT5C)	Q86Y97	KMT5C_HUMAN	.	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	KMT5C	"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)."	EC 2.1.1.361	.	MGPDRVTARELCENDDLATSLVLDPYLGFRTHKMNVSPVPPLRRQQHLRSALETFLRQRDLEAAYRALTLGGWTARYFQSRGPRQEAALKTHVYRYLRAFLPESGFTILPCTRYSMETNGAKIVSTRAWKKNEKLELLVGCIAELREADEGLLRAGENDFSIMYSTRKRSAQLWLGPAAFINHDCKPNCKFVPADGNAACVKVLRDIEPGDEVTCFYGEGFFGEKNEHCECHTCERKGEGAFRTRPREPALPPRPLDKYQLRETKRRLQQGLDSGSRQGLLGPRACVHPSPLRRDPFCAACQPLRLPACSARPDTSPLWLQWLPQPQPRVRPRKRRRPRPRRAPVLSTHHAARVSLHRWGGCGPHCRLRGEALVALGQPPHARWAPQQDWHWARRYGLPYVVRVDLRRLAPAPPATPAPAGTPGPILIPKQALAFAPFSPPKRLRLVVSHGSIDLDVGGEEL	Preclinical	The SUV4-20 inhibitor A-196 verifies a role for epigenetics in genomic integrity. Nat Chem Biol. 2017 Mar;13(3):317-324.	.	.	.	.	.	.	.	.	.	.	.	hsa00310: Lysine degradation; hsa01100: Metabolic pathways	R-HSA-3214841: PKMTs methylate histone lysines	MetaCyc:HS13469-MON	Q86Y97
TTDJ4MY	Kininogen (KNG1)	P01042	KNG1_HUMAN	.	KNG1; Bradykinin	KNG1	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.	.	6F3Y; 6F3X; 6F3W; 6F3V; 6F27	MKLITILFLCSRLLLSLTQESQSEEIDCNDKDLFKAVDAALKKYNSQNQSNNQFVLYRITEATKTVGSDTFYSFKYEIKEGDCPVQSGKTWQDCEYKDAAKAATGECTATVGKRSSTKFSVATQTCQITPAEGPVVTAQYDCLGCVHPISTQSPDLEPILRHGIQYFNNNTQHSSLFMLNEVKRAQRQVVAGLNFRITYSIVQTNCSKENFLFLTPDCKSLWNGDTGECTDNAYIDIQLRIASFSQNCDIYPGKDFVQPPTKICVGCPRDIPTNSPELEETLTHTITKLNAENNATFYFKIDNVKKARVQVVAGKKYFIDFVARETTCSKESNEELTESCETKKLGQSLDCNAEVYVVPWEKKIYPTVNCQPLGMISLMKRPPGFSPFRSSRIGEIKEETTVSPPHTSMAPAQDEERDSGKEQGHTRRHDWGHEKQRKHNLGHGHKHERDQGHGHQRGHGLGHGHEQQHGLGHGHKFKLDDDLEHQGGHVLDHGHKHKHGHGHGKHKNKGKKNGKHNGWKTEHLASSSEDSTTPSAQTQEKTEGPTPIPSLAKPGVTVTFSDFQDSDLIATMMPPISPAPIQSDDDWIPDIQIDPNGLSFNPISDFPDTTSPKCPGRPWKSVSEINPTTQMKESYYFDLTDGLS	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	24	.	.	.	.	.	.	.	.	.	.	hsa04610:Complement and coagulation cascades	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	.	P01042
TTHOJ5F	Importin beta (KPNB1)	Q14974	IMB1_HUMAN	Eukaryotic nuclear pore complex	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	KPNB1	"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."	.	6N89; 6N88; 3W5K; 3LWW; 2QNA	MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQIKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEIPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQGMRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQNLVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDPSVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEAAYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSAKDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKNYAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDIALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA	Literature-reported	Identification of KPNB1 as a Cellular Target of Aminothiazole Derivatives with Anticancer Activity. ChemMedChem. 2016 Jul 5;11(13):1406-9.	.	TC=1.I.1	.	importin beta family. Importin beta-1 subfamily.	.	.	Importin-beta N-terminal domain	PF03810	PF03810; IBN_N	1.I.1.1.3	The Eukaryotic Nuclear Pore Complex (E-NPC) Family	hsa03013: Nucleocytoplasmic transport; hsa05207: Chemical carcinogenesis - receptor activation	R-HSA-1169408: ISG15 antiviral mechanism; R-HSA-140342: Apoptosis induced DNA fragmentation; R-HSA-1655829: Regulation of cholesterol biosynthesis by SREBP (SREBF); R-HSA-168271: Transport of Ribonucleoproteins into the Host Nucleus; R-HSA-168276: NS1 Mediated Effects on Host Pathways; R-HSA-180746: Nuclear import of Rev protein; R-HSA-2995383: Initiation of Nuclear Envelope (NE) Reformation; R-HSA-6798695: Neutrophil degranulation; R-HSA-68616: Assembly of the ORC complex at the origin of replication; R-HSA-909733: Interferon alpha/beta signaling; R-HSA-9615933: Postmitotic nuclear pore complex (NPC) reformation; R-HSA-9636249: Inhibition of nitric oxide production	.	Q14974
TTM8FR7	KRAS messenger RNA (KRAS mRNA)	P01116	RASK_HUMAN	mRNA target	c-Ki-ras (mRNA); c-K-ras (mRNA); RASK2 (mRNA); Ki-Ras (mRNA); KRAS2 (mRNA); K-Ras 2 (mRNA); GTPase KRas (mRNA)	KRAS	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.	.	6N2K; 6N2J; 6H47; 6H46; 6GQY	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2824).	0	mRNA	mRNA target	.	.	.	Ras family	PF00071	PF00071; Ras	.	.	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	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	.	P01116
TTB1RA4	GTPase KRas (KRAS)	P01116	RASK_HUMAN	Small GTPase	c-Ki-ras; c-K-ras; RASK2; Ki-Ras; KRAS2; K-Ras 2	KRAS	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.	.	6N2K; 6N2J; 6H47; 6H46; 6GQY	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	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	"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-1433557: Signaling by SCF-KIT; R-HSA-167044: Signalling to RAS; R-HSA-171007: p38MAPK events; R-HSA-179812: GRB2 events in EGFR signaling; R-HSA-180336: SHC1 events in EGFR signaling; R-HSA-186763: Downstream signal transduction; 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-4086398: Ca2+ pathway; R-HSA-442982: Ras activation upon Ca2+ influx 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-5655253: Signaling by FGFR2 in disease; R-HSA-5655291: Signaling by FGFR4 in disease; R-HSA-5655302: Signaling by FGFR1 in disease; R-HSA-5655332: Signaling by FGFR3 in disease; 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-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802953: RAS signaling downstream of NF1 loss-of-function variants; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-74751: Insulin receptor signalling cascade; R-HSA-8849471: PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases; R-HSA-8851805: MET activates RAS signaling; R-HSA-8951936: RUNX3 regulates p14-ARF; R-HSA-9026519: Activated NTRK2 signals through RAS; R-HSA-9027284: Erythropoietin activates RAS; R-HSA-9028731: Activated NTRK2 signals through FRS2 and FRS3; R-HSA-9034864: Activated NTRK3 signals through RAS; R-HSA-9607240: FLT3 Signaling; R-HSA-9634285: Constitutive Signaling by Overexpressed ERBB2; R-HSA-9634635: Estrogen-stimulated signaling through PRKCZ; R-HSA-9648002: RAS processing; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665348: Signaling by ERBB2 ECD mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants; R-HSA-9670439: Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants; R-HSA-9673767: Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants; R-HSA-9673770: Signaling by PDGFRA extracellular domain mutants; R-HSA-9674555: Signaling by CSF3 (G-CSF); R-HSA-9703465: Signaling by FLT3 fusion proteins; R-HSA-9703648: Signaling by FLT3 ITD and TKD mutants; R-HSA-9753510: Signaling by RAS GAP mutants; R-HSA-9753512: Signaling by RAS GTPase mutants"	.	P01116
TTRHMTC	Mutated KRAS (mKRAS)	P01116 (mutated)	RASK_HUMAN	.	c-Ki-ras (mutated); c-K-ras (mutated); RASK2 (mutated); Ki-Ras (mutated); KRAS2 (mutated); K-Ras 2 (mutated); GTPase KRas (mutated)	KRAS	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.	.	6N2K; 6N2J; 6H47; 6H46; 6GQY	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM	Clinical trial	"Clinical pipeline report, company report or official report of GlobeImmune."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	P01116
TT9TVNM	KRAS G12D mutant messenger RNA (KRAS mRNA)	P01116	RASK_HUMAN	.	K-Ras 2; Ki-Ras; c-K-ras; c-Ki-ras	KRAS	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.	EC 3.6.5.2	.	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM	Clinical trial	"Clinical pipeline report, company report or official report of Silenseed."	.	.	.	.	.	.	.	.	.	.	.	"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; hsa04929: GnRH secretion; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04935: Growth hormone synthesis, secretion and action; hsa04960: Aldosterone-regulated sodium reabsorption; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; 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; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; 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; hsa05417: Lipid and atherosclerosis"	"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-1433557: Signaling by SCF-KIT; R-HSA-167044: Signalling to RAS; R-HSA-171007: p38MAPK events; R-HSA-179812: GRB2 events in EGFR signaling; R-HSA-180336: SHC1 events in EGFR signaling; R-HSA-186763: Downstream signal transduction; 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-4086398: Ca2+ pathway; R-HSA-442982: Ras activation upon Ca2+ influx 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-5655253: Signaling by FGFR2 in disease; R-HSA-5655291: Signaling by FGFR4 in disease; R-HSA-5655302: Signaling by FGFR1 in disease; R-HSA-5655332: Signaling by FGFR3 in disease; 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-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802953: RAS signaling downstream of NF1 loss-of-function variants; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-74751: Insulin receptor signalling cascade; R-HSA-8849471: PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases; R-HSA-8851805: MET activates RAS signaling; R-HSA-8951936: RUNX3 regulates p14-ARF; R-HSA-9026519: Activated NTRK2 signals through RAS; R-HSA-9027284: Erythropoietin activates RAS; R-HSA-9028731: Activated NTRK2 signals through FRS2 and FRS3; R-HSA-9034864: Activated NTRK3 signals through RAS; R-HSA-9607240: FLT3 Signaling; R-HSA-9634285: Constitutive Signaling by Overexpressed ERBB2; R-HSA-9634635: Estrogen-stimulated signaling through PRKCZ; R-HSA-9648002: RAS processing; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665348: Signaling by ERBB2 ECD mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants; R-HSA-9670439: Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants; R-HSA-9673767: Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants; R-HSA-9673770: Signaling by PDGFRA extracellular domain mutants; R-HSA-9674555: Signaling by CSF3 (G-CSF); R-HSA-9703465: Signaling by FLT3 fusion proteins; R-HSA-9703648: Signaling by FLT3 ITD and TKD mutants; R-HSA-9753510: Signaling by RAS GAP mutants; R-HSA-9753512: Signaling by RAS GTPase mutants"	.	P01116
TT3LH46	KRAS G12C mutant (KRAS G12C)	P01116	RASK_HUMAN	.	.	KRAS	.	.	.	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM	Clinical trial	"Clinical pipeline report, company report or official report of Amgen."	.	.	.	.	.	.	.	.	.	.	.	"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; hsa04929: GnRH secretion; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04935: Growth hormone synthesis, secretion and action; hsa04960: Aldosterone-regulated sodium reabsorption; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; 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; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; 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; hsa05417: Lipid and atherosclerosis"	"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-1433557: Signaling by SCF-KIT; R-HSA-167044: Signalling to RAS; R-HSA-171007: p38MAPK events; R-HSA-179812: GRB2 events in EGFR signaling; R-HSA-180336: SHC1 events in EGFR signaling; R-HSA-186763: Downstream signal transduction; 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-4086398: Ca2+ pathway; R-HSA-442982: Ras activation upon Ca2+ influx 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-5655253: Signaling by FGFR2 in disease; R-HSA-5655291: Signaling by FGFR4 in disease; R-HSA-5655302: Signaling by FGFR1 in disease; R-HSA-5655332: Signaling by FGFR3 in disease; 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-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802953: RAS signaling downstream of NF1 loss-of-function variants; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-74751: Insulin receptor signalling cascade; R-HSA-8849471: PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases; R-HSA-8851805: MET activates RAS signaling; R-HSA-8951936: RUNX3 regulates p14-ARF; R-HSA-9026519: Activated NTRK2 signals through RAS; R-HSA-9027284: Erythropoietin activates RAS; R-HSA-9028731: Activated NTRK2 signals through FRS2 and FRS3; R-HSA-9034864: Activated NTRK3 signals through RAS; R-HSA-9607240: FLT3 Signaling; R-HSA-9634285: Constitutive Signaling by Overexpressed ERBB2; R-HSA-9634635: Estrogen-stimulated signaling through PRKCZ; R-HSA-9648002: RAS processing; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants; R-HSA-9664565: Signaling by ERBB2 KD Mutants; R-HSA-9665348: Signaling by ERBB2 ECD mutants; R-HSA-9665686: Signaling by ERBB2 TMD/JMD mutants; R-HSA-9670439: Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants; R-HSA-9673767: Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants; R-HSA-9673770: Signaling by PDGFRA extracellular domain mutants; R-HSA-9674555: Signaling by CSF3 (G-CSF); R-HSA-9703465: Signaling by FLT3 fusion proteins; R-HSA-9703648: Signaling by FLT3 ITD and TKD mutants; R-HSA-9753510: Signaling by RAS GAP mutants; R-HSA-9753512: Signaling by RAS GTPase mutants"	.	P01116
TTLJX8E	KRas D816V mutant (KRAS D816V)	P01116	RASK_HUMAN	.	K-Ras 2; Ki-Ras; c-K-ras; c-Ki-ras	KRAS	"Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:20949621). Plays an important role in the regulation of cell proliferation (PubMed:23698361, PubMed:22711838). 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 (PubMed:24623306). {ECO:0000269|PubMed:20949621, ECO:0000269|PubMed:22711838, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:24623306, ECO:0000305}."	EC 3.6.5.2	1D8D;1D8E;1KZO;1KZP;1N4P;1N4Q;1N4R;1N4S;3GFT;4DSN;4DSO;4EPR;4EPT;4EPV;4EPW;4EPX;4EPY;4L8G;4LDJ;4LPK;4LRW;4LUC;4LV6;4LYF;4LYH;4LYJ;4M1O;4M1S;4M1T;4M1W;4M1Y;4M21;4M22;4NMM;4OBE;4PZY;4PZZ;4Q01;4Q02;4Q03;4QL3;4TQ9;4TQA;4WA7;5F2E;5KYK;5MLA;5MLB;5O2S;5O2T;5OCG;5OCO;5OCT;5TAR;5TB5;5UFE;5UFQ;5UK9;5UQW;5US4;5USJ;5V6S;5V6V;5V71;5V9L;5V9O;5V9U;5VBM;5VP7;5VPI;5VPY;5VPZ;5VQ0;5VQ1;5VQ2;5VQ6;5VQ8;5W22;5WHA;5WHB;5WHD;5WHE;5WLB;5WPM;5XCO;5YXZ;5YY1;6ARK;6ASA;6ASE;6B0V;6B0Y;6BOF;6BP1;6CC9;6CCH;6CCX;6CU6;6E6F;6E6G;6EPL;6EPM;6EPN;6EPO;6EPP;6F76;6FA1;6FA2;6FA3;6FA4;6GJ5;6GJ6;6GJ7;6GJ8;6GOD;6GOE;6GOF;6GOG;6GOM;6GQT;6GQW;6GQX;6GQY;6H46;6H47;6JTN;6JTO;6JTP;6M9W;6MBQ;6MBT;6MBU;6MNX;6MQG;6MQN;6MS9;6MTA;6N2J;6N2K;6O36;6O46;6O4Y;6O4Z;6O51;6O53;6OB2;6OB3;6OIM;6P0Z;6P8W;6P8X;6P8Y;6P8Z;6PGO;6PGP;6PQ3;6PTS;6PTW;6QUU;6QUV;6QUW;6QUX;6T5B;6T5U;6T5V;6TAM;6TAN;6USX;6USZ;6UT0;6V5L;6V65;6V6F;6VC8;6VJJ;6W4E;6W4F;6WGN;6WS2;6WS4;6XGU;6XGV;6XHA;6XHB;6YR8;6YXW;6ZL5;6ZLI;7A1W;7A1X;7A1Y;7A47;7ACA;7ACF;7ACH;7ACQ;7C40;7C41;7EW9;7EWA;7EWB;7EYX;7F0W;7KFZ;7KMR;7KYZ;7LC1;7LC2;7LGI;7LZ5;7MDP;7MQU;7NY8;7O70;7OK3;7OK4;7OO7;7Q9U;7R0M;7R0N;7R0Q;7ROV;7RP2;7RP3;7RP4;7RPZ;7RSC;7RSE;7RT1;7RT2;7RT3;7RT4;7RT5;7SCW;7SCX;7T1F;7T47;7TLE;7TLG;7TLK;7U8H;7VVB;7W5R;7YCC;7YCE;8AFB;8AFC;8AFD;8AQ5;8AQ7;8AZR;8AZV;8AZX;8AZY;8AZZ;8B00;8B6I;8B78;8CX5;8DNI;8DNJ;8DNK;8EPW;8EZG;8ONV	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM	Clinical trial	Protein degraders enter the clinic - a new approach to cancer therapy. Nat Rev Clin Oncol. 2023 Apr;20(4):265-278.	.	.	.	.	.	.	.	.	.	.	.	hsa:3845	R-HSA-112412;R-HSA-1169092;R-HSA-1236382;R-HSA-1250196;R-HSA-1250347;R-HSA-1433557;R-HSA-167044;R-HSA-171007;R-HSA-179812;R-HSA-180336;R-HSA-186763;R-HSA-1963640;R-HSA-210993;R-HSA-2179392;R-HSA-2424491;R-HSA-2428933;R-HSA-2871796;R-HSA-375165;R-HSA-4086398 [P01116-2];R-HSA-442982;R-HSA-5218921;R-HSA-5621575;R-HSA-5637810;R-HSA-5654688;R-HSA-5654693;R-HSA-5654699;R-HSA-5654700;R-HSA-5654704;R-HSA-5654706;R-HSA-5654712;R-HSA-5654719;R-HSA-5655253;R-HSA-5655291;R-HSA-5655302;R-HSA-5655332;R-HSA-5658442;R-HSA-5673000;R-HSA-5673001;R-HSA-5674135;R-HSA-5675221;R-HSA-6802946;R-HSA-6802948;R-HSA-6802952;R-HSA-6802953;R-HSA-6802955;R-HSA-74751;R-HSA-8849471;R-HSA-8851805;R-HSA-8951936;R-HSA-9026519;R-HSA-9027284;R-HSA-9028731;R-HSA-9034864;R-HSA-9607240;R-HSA-9634285;R-HSA-9634635;R-HSA-9648002;R-HSA-9649948;R-HSA-9656223;R-HSA-9664565;R-HSA-9665348;R-HSA-9665686;R-HSA-9670439;R-HSA-9673767;R-HSA-9673770;R-HSA-9674555;R-HSA-9680350;R-HSA-9703465;R-HSA-9703648;R-HSA-9753510;R-HSA-9753512;	.	P01116;
TTKV0EC	Keratin type I cytoskeletal 17 (KRT17)	Q04695	K1C17_HUMAN	Intermediate filament family	Keratin-17; KRT17; K17; Cytokeratin-17; CK-17	KRT17	"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."	.	.	MTTSIRQFTSSSSIKGSSGLGGGSSRTSCRLSGGLGAGSCRLGSAGGLGSTLGGSSYSSCYSFGSGGGYGSSFGGVDGLLAGGEKATMQNLNDRLASYLDKVRALEEANTELEVKIRDWYQRQAPGPARDYSQYYRTIEELQNKILTATVDNANILLQIDNARLAADDFRTKFETEQALRLSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVGGEINVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGNLAETENRYCVQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLTQYKKEPVTTRQVRTIVEEVQDGKVISSREQVHQTTR	Literature-reported	Knockdown of KRT17 by siRNA induces antitumoral effects on gastric cancer cells. Gastric Cancer. 2017 Nov;20(6):948-959.	.	.	.	.	.	.	.	.	.	.	.	hsa04915: Estrogen signaling pathway; hsa05150: Staphylococcus aureus infection	R-HSA-6805567: Keratinization; R-HSA-6809371: Formation of the cornified envelope	.	Q04695
TT3JF9E	Keratin type I cytoskeletal 19 (KRT19)	P08727	K1C19_HUMAN	Intermediate filament family	"Keratin19; Keratin, type I cytoskeletal 19; KRT19; K19; Cytokeratin19; CK19"	KRT19	"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}."	.	.	MTSYSYRQSSATSSFGGLGGGSVRFGPGVAFRAPSIHGGSGGRGVSVSSARFVSSSSSGAYGGGYGGVLTASDGLLAGNEKLTMQNLNDRLASYLDKVRALEAANGELEVKIRDWYQKQGPGPSRDYSHYYTTIQDLRDKILGATIENSRIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEEEISTLRGQVGGQVSVEVDSAPGTDLAKILSDMRSQYEVMAEQNRKDAEAWFTSRTEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAALEDTLAETEARFGAQLAHIQALISGIEAQLGDVRADSERQNQEYQRLMDIKSRLEQEIATYRSLLEGQEDHYNNLSASKVL	Literature-reported	"Keratin 19, a Cancer Stem Cell Marker in Human Hepatocellular Carcinoma. Clin Cancer Res. 2015 Jul 1;21(13):3081-91."	.	.	.	.	.	.	.	.	.	.	.	hsa04915: Estrogen signaling pathway; hsa05150: Staphylococcus aureus infection	R-HSA-6805567: Keratinization; R-HSA-6809371: Formation of the cornified envelope	.	P08727
TT2FX8W	Keratin 6A messenger RNA (KRT6A mRNA)	P02538	K2C6A_HUMAN	mRNA target	"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)"	KRT6A	"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."	.	5KI0	MASTSTTIRSHSSSRRGFSANSARLPGVSRSGFSSVSVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISIGGGSCAISGGYGSRAGGSYGFGGAGSGFGFGGGAGIGFGLGGGAGLAGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPTIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGQVNISVVQSTVSSGYGGASGVGSGLGLGGGSSYSYGSGLGVGGGFSSSSGRAIGGGLSSVGGGSSTIKYTTTSSSSRKSYKH	Clinical trial	First-in-human mutation-targeted siRNA phase Ib trial of an inherited skin disorder. Mol Ther. 2010 Feb;18(2):442-6.	21	mRNA	mRNA target	.	.	.	Intermediate filament protein; Keratin type II head	PF00038; PF16208	PF00038; Filament; PF16208; Keratin_2_head	.	.	.	R-HSA-6805567: Keratinization; R-HSA-6809371: Formation of the cornified envelope	.	P02538
TT9TENM	Herpesvirus G-protein coupled receptor (KSHV vGPCR)	Q98146	VGPCR_HHV8P	.	viral G-protein coupled receptor; vGPCR; Protein ORF74	KSHV vGPCR	"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."	.	.	MAAEDFLTIFLDDDESWNETLNMSGYDYSGNFSLEVSVCEMTTVVPYTWNVGILSLIFLINVLGNGLVTYIFCKHRSRAGAIDILLLGICLNSLCLSISLLAEVLMFLFPNIISTGLCRLEIFFYYLYVYLDIFSVVCVSLVRYLLVAYSTRSWPKKQSLGWVLTSAALLIALVLSGDACRHRSRVVDPVSKQAMCYENAGNMTADWRLHVRTVSVTAGFLLPLALLILFYALTWCVVRRTKLQARRKVRGVIVAVVLLFFVFCFPYHVLNLLDTLLRRRWIRDSCYTRGLINVGLAVTSLLQALYSAVVPLIYSCLGSLFRQRMYGLFQSLRQSFMSGATT	Literature-reported	The KSHV G protein-coupled receptor signals via multiple pathways to induce transcription factor activation in primary effusion lymphoma cells. Oncogene. 2004 Jan 15;23(2):514-23.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHL1TV	Kinase suppressor of Ras-1 (KSR1)	Q13476	KSR1_HUMAN	Kinase	Kinase suppressor of Ras 1; KSR	KSR1	"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."	.	5VYK	MDRAALRAAAMGEKKEGGGGGDAAAAEGGAGAAASRALQQCGQLQKLIDISIGSLRGLRTKCAVSNDLTQQEIRTLEAKLVRYICKQRQCKLSVAPGERTPELNSYPRFSDWLYTFNVRPEVVQEIPRDLTLDALLEMNEAKVKETLRRCGASGDECGRLQYALTCLRKVTGLGGEHKEDSSWSSLDARRESGSGPSTDTLSAASLPWPPGSSQLGRAGNSAQGPRSISVSALPASDSPTPSFSEGLSDTCIPLHASGRLTPRALHSFITPPTTPQLRRHTKLKPPRTPPPPSRKVFQLLPSFPTLTRSKSHESQLGNRIDDVSSMRFDLSHGSPQMVRRDIGLSVTHRFSTKSWLSQVCHVCQKSMIFGVKCKHCRLKCHNKCTKEAPACRISFLPLTRLRRTESVPSDINNPVDRAAEPHFGTLPKALTKKEHPPAMNHLDSSSNPSSTTSSTPSSPAPFPTSSNPSSATTPPNPSPGQRDSRFNFPAAYFIHHRQQFIFPVPSAGHCWKCLLIAESLKENAFNISAFAHAAPLPEAADGTRLDDQPKADVLEAHEAEAEEPEAGKSEAEDDEDEVDDLPSSRRPWRGPISRKASQTSVYLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREGRRENQLKLSHDWLCYLAPEIVREMTPGKDEDQLPFSKAADVYAFGTVWYELQARDWPLKNQAAEASIWQIGSGEGMKRVLTSVSLGKEVSEILSACWAFDLQERPSFSLLMDMLEKLPKLNRRLSHPGHFWKSADINSSKVVPRFERFGLGVLESSNPKM	Literature-reported	Deficiency of kinase suppressor of Ras1 prevents oncogenic ras signaling in mice. Cancer Res. 2003 Jul 15;63(14):4232-8.	.	EC:2.7	.	protein kinase superfamily. TKL Ser/Thr protein kinase family.	.	.	Protein tyrosine kinase; SAM like domain present in kinase suppressor RAS 1	PF07714; PF13543	PF07714; Pkinase_Tyr; PF13543; SAM_KSR1	.	.	.	.	.	Q8IVT5
TTWQM3J	Kynureninase (KYNU)	Q16719	KYNU_HUMAN	Carbon-carbon bonds hydrolase	L-kynurenine hydrolase; KYNU	KYNU	"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."	EC 3.7.1.3	3E9K; 2HZP	MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLSLVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLMKDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHGLNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAGQAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKPALVGWFGHELSTRFKMDNKLQLIPGVCGFRISNPPILLVCSLHASLEIFKQATMKALRKKSVLLTGYLEYLIKHNYGKDKAATKKPVVNIITPSHVEERGCQLTITFSVPNKDVFQELEKRGVVCDKRNPNGIRVAPVPLYNSFHDVYKFTNLLTSILDSAETKN	Preclinical	Comparative inhibition by substrate analogues 3-methoxy- and 3-hydroxydesaminokynurenine and an improved 3 step purification of recombinant human kynureninase. BMC Biochem. 2003 Sep 24;4:13.	0	.	.	.	.	.	.	.	.	.	.	hsa00380:Tryptophan metabolism; hsa01100:Metabolic pathways	R-HSA-71240:Tryptophan catabolism	MetaCyc:HS03952-MON	Q16719
TTC9D3K	Neural cell adhesion molecule L1 (L1CAM)	P32004	L1CAM_HUMAN	Immunoglobulin	SPG1; S10; NCAM-L1; N-CAML1; N-CAM-L1; MIC5; MASA; L1 cell adhesion molecule; HSAS1; HSAS; CD171; CAML1	L1CAM	"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."	.	.	MVVALRYVWPLLLCSPCLLIQIPEEYEGHHVMEPPVITEQSPRRLVVFPTDDISLKCEASGKPEVQFRWTRDGVHFKPKEELGVTVYQSPHSGSFTITGNNSNFAQRFQGIYRCFASNKLGTAMSHEIRLMAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAEPLRIYWMNSKILHIKQDERVTMGQNGNLYFANVLTSDNHSDYICHAHFPGTRTIIQKEPIDLRVKATNSMIDRKPRLLFPTNSSSHLVALQGQPLVLECIAEGFPTPTIKWLRPSGPMPADRVTYQNHNKTLQLLKVGEEDDGEYRCLAENSLGSARHAYYVTVEAAPYWLHKPQSHLYGPGETARLDCQVQGRPQPEVTWRINGIPVEELAKDQKYRIQRGALILSNVQPSDTMVTQCEARNRHGLLLANAYIYVVQLPAKILTADNQTYMAVQGSTAYLLCKAFGAPVPSVQWLDEDGTTVLQDERFFPYANGTLGIRDLQANDTGRYFCLAANDQNNVTIMANLKVKDATQITQGPRSTIEKKGSRVTFTCQASFDPSLQPSITWRGDGRDLQELGDSDKYFIEDGRLVIHSLDYSDQGNYSCVASTELDVVESRAQLLVVGSPGPVPRLVLSDLHLLTQSQVRVSWSPAEDHNAPIEKYDIEFEDKEMAPEKWYSLGKVPGNQTSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETVVTPEAAPEKNPVDVKGEGNETTNMVITWKPLRWMDWNAPQVQYRVQWRPQGTRGPWQEQIVSDPFLVVSNTSTFVPYEIKVQAVNSQGKGPEPQVTIGYSGEDYPQAIPELEGIEILNSSAVLVKWRPVDLAQVKGHLRGYNVTYWREGSQRKHSKRHIHKDHVVVPANTTSVILSGLRPYSSYHLEVQAFNGRGSGPASEFTFSTPEGVPGHPEALHLECQSNTSLLLRWQPPLSHNGVLTGYVLSYHPLDEGGKGQLSFNLRDPELRTHNLTDLSPHLRYRFQLQATTKEGPGEAIVREGGTMALSGISDFGNISATAGENYSVVSWVPKEGQCNFRFHILFKALGEEKGGASLSPQYVSYNQSSYTQWDLQPDTDYEIHLFKERMFRHQMAVKTNGTGRVRLPPAGFATEGWFIGFVSAIILLLLVLLILCFIKRSKGGKYSVKDKEDTQVDSEARPMKDETFGEYRSLESDNEEKAFGSSQPSLNGDIKPLGSDDSLADYGGSVDVQFNEDGSFIGQYSGKKEKEAAGGNDSSGATSPINPAVALE	Clinical trial	ClinicalTrials.gov (NCT02311621) Engineered Neuroblastoma Cellular Immunotherapy (ENCIT)-01	17	Immunoglobulin	.	immunoglobulin superfamily. L1/neurofascin/NgCAM family.	.	.	Bravo-like intracellular region; Fibronectin type III domain; Immunoglobulin I-set domain	PF13882; PF00041; PF07679	PF13882; Bravo_FIGEY; PF00041; fn3; PF07679; I-set	.	.	hsa04360:Axon guidance; hsa04514:Cell adhesion molecules (CAMs)	R-HSA-210991: Basigin interactions; R-HSA-373760: L1CAM interactions; R-HSA-437239: Recycling pathway of L1; R-HSA-445095: Interaction between L1 and Ankyrins; R-HSA-445144: Signal transduction by L1	.	P32004
TTQDMJN	Lethal(3)malignant brain tumor-like 3 (L3MBTL3)	Q96JM7	LMBL3_HUMAN	.	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	L3MBTL3	"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)."	.	4L59; 4FL6; 3UT1; 1WJS; 1WJQ	MTESASSTSGQEFDVFSVMDWKDGVGTLPGSDLKFRVNEFGALEVITDENEMENVKKATATTTWMVPTAQEAPTSPPSSRPVFPPAYWTSPPGCPTVFSEKTGMPFRLKDPVKVEGLQFCENCCQYGNVDECLSGGNYCSQNCARHIKDKDQKEERDVEEDNEEEDPKCSRKKKPKLSLKADTKEDGEERDDEMENKQDVRILRGSQRARRKRRGDSAVLKQGLPPKGKKAWCWASYLEEEKAVAVPAKLFKEHQSFPYNKNGFKVGMKLEGVDPEHQSVYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLHPPKGYKEEEFNWQTYLKTCKAQAAPKSLFENQNITVIPSGFRVGMKLEAVDKKNPSFICVATVTDMVDNRFLVHFDNWDESYDYWCEASSPHIHPVGWCKEHRRTLITPPGYPNVKHFSWDKYLEETNSLPAPARAFKVKPPHGFQKKMKLEVVDKRNPMFIRVATVADTDDHRVKVHFDGWNNCYDYWIDADSPDIHPVGWCSKTGHPLQPPLSPLELMEASEHGGCSTPGCKGIGHFKRARHLGPHSAANCPYSEINLNKDRIFPDRLSGEMPPASPSFPRNKRTDANESSSSPEIRDQHADDVKEDFEERTESEMRTSHEARGAREEPTVQQAQRRSAVFLSFKSPIPCLPLRWEQQSKLLPTVAGIPASKVSKWSTDEVSEFIQSLPGCEEHGKVFKDEQIDGEAFLLMTQTDIVKIMSIKLGPALKIFNSILMFKAAEKNSHNEL	Literature-reported	Discovery of a chemical probe for the L3MBTL3 methyllysine reader domain. Nat Chem Biol. 2013 Mar;9(3):184-91.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q96JM7
TTNVXAW	Lymphocyte activation gene 3 protein (LAG3)	P18627	LAG3_HUMAN	Immunoglobulin	Protein FDC; LAG-3; FDC; CD223	LAG3	"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."	.	.	MWEAQFLGLLFLQPLWVAPVKPLQPGAEVPVVWAQEGAPAQLPCSPTIPLQDLSLLRRAGVTWQHQPDSGPPAAAPGHPLAPGPHPAAPSSWGPRPRRYTVLSVGPGGLRSGRLPLQPRVQLDERGRQRGDFSLWLRPARRADAGEYRAAVHLRDRALSCRLRLRLGQASMTASPPGSLRASDWVILNCSFSRPDRPASVHWFRNRGQGRVPVRESPHHHLAESFLFLPQVSPMDSGPWGCILTYRDGFNVSIMYNLTVLGLEPPTPLTVYAGAGSRVGLPCRLPAGVGTRSFLTAKWTPPGGGPDLLVTGDNGDFTLRLEDVSQAQAGTYTCHIHLQEQQLNATVTLAIITVTPKSFGSPGSLGKLLCEVTPVSGQERFVWSSLDTPSQRSFSGPWLEAQEAQLLSQPWQCQLYQGERLLGAAVYFTELSSPGAQRSGRAPGALPAGHLLLFLILGVLSLLLLVTGAFGFHLWRRQWRPRRFSALEQGIHPPQAQSKIEELEQEPEPEPEPEPEPEPEPEPEQL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	Immunoglobulin	Immunoglobulin superfamily	LAG3 family.	.	.	.	.	.	.	.	.	R-HSA-2132295: MHC class II antigen presentation	.	P18627
TTSI7A8	Leukocyte-associated Ig-like receptor 1 (LAIR1)	Q6GTX8	LAIR1_HUMAN	.	LAIR-1; hLAIR1; DE   AltName: CD_antigen=CD305	LAIR1	"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."	.	.	MSPHPTALLGLVLCLAQTIHTQEEDLPRPSISAEPGTVIPLGSHVTFVCRGPVGVQTFRLERESRSTYNDTEDVSQASPSESEARFRIDSVSEGNAGPYRCIYYKPPKWSEQSDYLELLVKETSGGPDSPDTEPGSSAGPTQRPSDNSHNEHAPASQGLKAEHLYILIGVSVVFLFCLLLLVLFCLHRQNQIKQGPPRSKDEEQKPQQRPDLAVDVLERTADKATVNGLPEKDRETDTSALAAGSSQEVTYAQLDHWALTQRTARAVSPQSTKPMAESITYAAVARH	Clinical trial	"Clinical pipeline report, company report or official report of NextCure."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-6798695: Neutrophil degranulation	.	Q6GTX8
TTBRLU3	Lactalbumin alpha (LALBA)	P00709	LALBA_HUMAN	.	Lysozyme-like protein 7; Lactose synthase B protein; LYZL7; Alpha-lactalbumin	LALBA	"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."	.	4L41; 3B0O; 3B0I; 1HML; 1CB3	MRFFVPLFLVGILFPAILAKQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAIVENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEKL	Literature-reported	HAMLET - A protein-lipid complex with broad tumoricidal activity. Biochem Biophys Res Commun. 2017 Jan 15;482(3):454-458.	.	.	.	.	.	.	.	.	.	.	.	hsa00052: Galactose metabolism; hsa01100: Metabolic pathways	R-HSA-5653890: Lactose synthesis	MetaCyc:HS09571-MON	P00709
TT2WOUQ	Laminin beta-3 chain (LAMB3)	Q13751	LAMB3_HUMAN	.	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	LAMB3	"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."	.	.	MRPFFLLCFALPGLLHAQQACSRGACYPPVGDLLVGRTRFLRASSTCGLTKPETYCTQYGEWQMKCCKCDSRQPHNYYSHRVENVASSSGPMRWWQSQNDVNPVSLQLDLDRRFQLQEVMMEFQGPMPAGMLIERSSDFGKTWRVYQYLAADCTSTFPRVRQGRPQSWQDVRCQSLPQRPNARLNGGKVQLNLMDLVSGIPATQSQKIQEVGEITNLRVNFTRLAPVPQRGYHPPSAYYAVSQLRLQGSCFCHGHADRCAPKPGASAGPSTAVQVHDVCVCQHNTAGPNCERCAPFYNNRPWRPAEGQDAHECQRCDCNGHSETCHFDPAVFAASQGAYGGVCDNCRDHTEGKNCERCQLHYFRNRRPGASIQETCISCECDPDGAVPGAPCDPVTGQCVCKEHVQGERCDLCKPGFTGLTYANPQGCHRCDCNILGSRRDMPCDEESGRCLCLPNVVGPKCDQCAPYHWKLASGQGCEPCACDPHNSLSPQCNQFTGQCPCREGFGGLMCSAAAIRQCPDRTYGDVATGCRACDCDFRGTEGPGCDKASGRCLCRPGLTGPRCDQCQRGYCNRYPVCVACHPCFQTYDADLREQALRFGRLRNATASLWSGPGLEDRGLASRILDAKSKIEQIRAVLSSPAVTEQEVAQVASAILSLRRTLQGLQLDLPLEEETLSLPRDLESLDRSFNGLLTMYQRKREQFEKISSADPSGAFRMLSTAYEQSAQAAQQVSDSSRLLDQLRDSRREAERLVRQAGGGGGTGSPKLVALRLEMSSLPDLTPTFNKLCGNSRQMACTPISCPGELCPQDNGTACGSRCRGVLPRAGGAFLMAGQVAEQLRGFNAQLQRTRQMIRAAEESASQIQSSAQRLETQVSASRSQMEEDVRRTRLLIQQVRDFLTDPDTDAATIQEVSEAVLALWLPTDSATVLQKMNEIQAIAARLPNVDLVLSQTKQDIARARRLQAEAEEARSRAHAVEGQVEDVVGNLRQGTVALQEAQDTMQGTSRSLRLIQDRVAEVQQVLRPAEKLVTSMTKQLGDFWTRMEELRHQARQQGAEAVQAQQLAEGASEQALSAQEGFERIKQKYAELKDRLGQSSMLGEQGARIQSVKTEAEELFGETMEMMDRMKDMELELLRGSQAIMLRSADLTGLEKRVEQIRDHINGRVLYYATCK	Clinical trial	Correction of junctional epidermolysis bullosa by transplantation of genetically modified epidermal stem cells. Nat Med. 2006 Dec;12(12):1397-402.	17	.	.	.	.	.	Laminin EGF domain; Laminin N-terminal (Domain VI)	PF00053; PF00055	PF00053; Laminin_EGF; PF00055; Laminin_N	.	.	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	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	.	Q13751
TTNS7H3	Laminin gamma-2 subunit (LAMC2)	Q13753	LAMC2_HUMAN	.	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	LAMC2	"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."	.	.	MPALWLGCCLCFSLLLPAARATSRREVCDCNGKSRQCIFDRELHRQTGNGFRCLNCNDNTDGIHCEKCKNGFYRHRERDRCLPCNCNSKGSLSARCDNSGRCSCKPGVTGARCDRCLPGFHMLTDAGCTQDQRLLDSKCDCDPAGIAGPCDAGRCVCKPAVTGERCDRCRSGYYNLDGGNPEGCTQCFCYGHSASCRSSAEYSVHKITSTFHQDVDGWKAVQRNGSPAKLQWSQRHQDVFSSAQRLDPVYFVAPAKFLGNQQVSYGQSLSFDYRVDRGGRHPSAHDVILEGAGLRITAPLMPLGKTLPCGLTKTYTFRLNEHPSNNWSPQLSYFEYRRLLRNLTALRIRATYGEYSTGYIDNVTLISARPVSGAPAPWVEQCICPVGYKGQFCQDCASGYKRDSARLGPFGTCIPCNCQGGGACDPDTGDCYSGDENPDIECADCPIGFYNDPHDPRSCKPCPCHNGFSCSVMPETEEVVCNNCPPGVTGARCELCADGYFGDPFGEHGPVRPCQPCQCNNNVDPSASGNCDRLTGRCLKCIHNTAGIYCDQCKAGYFGDPLAPNPADKCRACNCNPMGSEPVGCRSDGTCVCKPGFGGPNCEHGAFSCPACYNQVKIQMDQFMQQLQRMEALISKAQGGDGVVPDTELEGRMQQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNRVRDTHRLITQMQLSLAESEASLGNTNIPASDHYVGPNGFKSLAQEATRLAESHVESASNMEQLTRETEDYSKQALSLVRKALHEGVGSGSGSPDGAVVQGLVEKLEKTKSLAQQLTREATQAEIEADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAKRIKQKADSLSSLVTRHMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVESILKNLREFDLQVDNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAGVTIQDTLNTLDGLLHLMDQPLSVDEEGLVLLEQKLSRAKTQINSQLRPMMSELEERARQQRGHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALEQQ	Literature-reported	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800019225)"	2.1	.	.	.	.	.	Laminin B (Domain IV); Laminin EGF domain	PF00052; PF00053	PF00052; Laminin_B; PF00053; Laminin_EGF	.	.	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	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	.	Q13753
TTC214J	Lysosome-associated membrane glycoprotein 1 (CD107a)	P11279	LAMP1_HUMAN	Lysosomal protein import	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	LAMP1	Implicated in tumor cell metastasis. Presents carbohydrate ligands to selectins.	.	.	MAAPGSARRPLLLLLLLLLLGLMHCASAAMFMVKNGNGTACIMANFSAAFSVNYDTKSGPKNMTFDLPSDATVVLNRSSCGKENTSDPSLVIAFGRGHTLTLNFTRNATRYSVQLMSFVYNLSDTHLFPNASSKEIKTVESITDIRADIDKKYRCVSGTQVHMNNVTVTLHDATIQAYLSNSSFSRGETRCEQDRPSPTTAPPAPPSPSPSPVPKSPSVDKYNVSGTNGTCLLASMGLQLNLTYERKDNTTVTRLLNINPNKTSASGSCGAHLVTLELHSEGTTVLLFQFGMNASSSRFFLQGIQLNTILPDARDPAFKAANGSLRALQATVGNSYKCNAEEHVRVTKAFSVNIFKVWVQAFKVEGGQFGSVEECLLDENSMLIPIAVGGALAGLVLIVLIAYLVGRKRSHAGYQTI	Literature-reported	Lysosome-associated membrane glycoprotein 1 predicts fratricide amongst T cell receptor transgenic CD8+ T cells directed against tumor-associated a... Oncotarget. 2016 Aug 30;7(35):56584-56597.	.	TC=9.A.16	Lysosomal protein import	LAMP family.	.	.	Lysosome-associated membrane glycoprotein (Lamp)	PF01299	PF01299; Lamp	9.A.16.1.1	The Lysosomal Protein Import (LPI) Family	hsa04140: Autophagy - animal; hsa04142: Lysosome; hsa04145: Phagosome; hsa05152: Tuberculosis	R-HSA-6798695: Neutrophil degranulation	.	P11279
TTULDG7	Lysosome-associated membrane glycoprotein 2 (LAMP2)	P13473	LAMP2_HUMAN	.	LAMP-2; Lysosome-associated membrane protein 2; CD107 antigen-like family member B; LGP-96; DE   AltName: CD_antigen=CD107b	LAMP2	"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."	.	.	MVCFRLFPVPGSGLVLVCLVLGAVRSYALELNLTDSENATCLYAKWQMNFTVRYETTNKTYKTVTISDHGTVTYNGSICGDDQNGPKIAVQFGPGFSWIANFTKAASTYSIDSVSFSYNTGDNTTFPDAEDKGILTVDELLAIRIPLNDLFRCNSLSTLEKNDVVQHYWDVLVQAFVQNGTVSTNEFLCDKDKTSTVAPTIHTTVPSPTTTPTPKEKPEAGTYSVNNGNDTCLLATMGLQLNITQDKVASVININPNTTHSTGSCRSHTALLRLNSSTIKYLDFVFAVKNENRFYLKEVNISMYLVNGSVFSIANNNLSYWDAPLGSSYMCNKEQTVSVSGAFQINTFDLRVQPFNVTQGKYSTAQDCSADDDNFLVPIAVGAALAGVLILVLLAYFIGLKHHHAGYEQF	Clinical trial	ClinicalTrials.gov (NCT03882437) Gene Therapy for Male Patients With Danon Disease (DD) Using RP-A501; AAV9.LAMP2B. U.S. National Institutes of Health.	.	.	.	.	.	.	.	.	.	.	.	hsa04140: Autophagy - animal; hsa04142: Lysosome; hsa04145: Phagosome; hsa05152: Tuberculosis	R-HSA-114608: Platelet degranulation; R-HSA-6798695: Neutrophil degranulation; R-HSA-9613829: Chaperone Mediated Autophagy	.	P13473
TTZW8NS	Glutathione S-transferase LANCL1 (LANCL1)	O43813	LANC1_HUMAN	.	p40; LanC-like protein 1; GPR69A; 40 kDa erythrocyte membrane protein	LANCL1	"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."	EC 2.5.1.18	3E6U; 3.00E+73	MAQRAFPNPYADYNKSLAEGYFDAAGRLTPEFSQRLTNKIRELLQQMERGLKSADPRDGTGYTGWAGIAVLYLHLYDVFGDPAYLQLAHGYVKQSLNCLTKRSITFLCGDAGPLAVAAVLYHKMNNEKQAEDCITRLIHLNKIDPHAPNEMLYGRIGYIYALLFVNKNFGVEKIPQSHIQQICETILTSGENLARKRNFTAKSPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLQVSQGKLHSLVKPSVDYVCQLKFPSGNYPPCIGDNRDLLVHWCHGAPGVIYMLIQAYKVFREEKYLCDAYQCADVIWQYGLLKKGYGLCHGSAGNAYAFLTLYNLTQDMKYLYRACKFAEWCLEYGEHGCRTPDTPFSLFEGMAGTIYFLADLLVPTKARFPAFEL	Literature-reported	Lanthionine synthetase component C-like protein 2: a new drug target for inflammatory diseases and diabetes. Curr Drug Targets. 2014 Jun;15(6):565-72.	.	.	.	.	.	.	.	.	.	.	.	hsa00480: Glutathione metabolism; hsa01100: Metabolic pathways	.	.	O43813
TTMK3EX	LanC-like protein 2 (LANCL2)	Q9NS86	LANC2_HUMAN	.	Testis-specific adriamycin sensitivity protein	LANCL2	Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes. {ECO:0000269|PubMed:19667068}.	.	6WQ1	MGETMSKRLKLHLGGEAEMEERAFVNPFPDYEAAAGALLASGAAEETGCVRPPATTDEPGLPFHQDGKIIHNFIRRIQTKIKDLLQQMEEGLKTADPHDCSAYTGWTGIALLYLQLYRVTCDQTYLLRSLDYVKRTLRNLNGRRVTFLCGDAGPLAVGAVIYHKLRSDCESQECVTKLLQLQRSVVCQESDLPDELLYGRAGYLYALLYLNTEIGPGTVCESAIKEVVNAIIESGKTLSREERKTERCPLLYQWHRKQYVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVRHKKFRSGNYPSSLSNETDRLVHWCHGAPGVIHMLMQAYKVFKEEKYLKEAMECSDVIWQRGLLRKGYGICHGTAGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYGAHGCRIPDRPYSLFEGMAGAIHFLSDVLGPETSRFPAFELDSSKRD	Clinical trial	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2023. Adis Insight"	.	.	.	.	.	.	.	.	.	.	.	hsa:55915	.	.	Q9NS86;
TTEJQT0	Lysosome-associated transmembrane 4b-35 protein (LAPTM4B)	Q86VI4	LAP4B_HUMAN	.	Lysosome-associated transmembrane protein 4-beta; Lysosomal-associated transmembrane protein 4B	LAPTM4B	"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."	.	.	MTSRTRVTWPSPPRPLPVPAAAAVAFGAKGTDPAEARSSRGIEEAGPRAHGRAGREPERRRSRQQRRGGLQARRSTLLKTCARARATAPGAMKMVAPWTRFYSNSCCLCCHVRTGTILLGVWYLIINAVVLLILLSALADPDQYNFSSSELGGDFEFMDDANMCIAIAISLLMILICAMATYGAYKQRAAWIIPFFCYQIFDFALNMLVAITVLIYPNSIQEYIRQLPPNFPYRDDVMSVNPTCLVLIILLFISIILTFKGYLISCVWNCYRYINGRNSSDVLVYVTSNDTTVLLPPYDDATVNGAAKEPPPPYVSA	Literature-reported	LAPTM4B-35 protein as a potential therapeutic target in gastric cancer. Tumour Biol. 2014 Dec;35(12):12737-42.	.	.	.	.	.	.	.	.	.	.	.	hsa04142: Lysosome	.	.	Q86VI4
TTSN1YP	HUMAN la-related protein 1 (LARP1)	Q6PKG0	LARP1_HUMAN	LARP family	La ribonucleoprotein domain family member 1	LARP1	"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."	.	4ZC4; 5C0V; 5V4R; 5V7C; 5V87	MATQVEPLLPGGATLLQAEEHGGLVRKKPPPAPEGKGEPGPNDVRGGEPDGSARRPRPPCAKPHKEGTGQQERESPRPLQLPGAEGPAISDGEEGGGEPGAGGGAAGAAGAGRRDFVEAPPPKVNPWTKNALPPVLTTVNGQSPPEHSAPAKVVRAAVPKQRKGSKVGDFGDAINWPTPGEIAHKSVQPQSHKPQPTRKLPPKKDMKEQEKGEGSDSKESPKTKSDESGEEKNGDEDCQRGGQKKKGNKHKWVPLQIDMKPEVPREKLASRPTRPPEPRHIPANRGEIKGSESATYVPVAPPTPAWQPEIKPEPAWHDQDETSSVKSDGAGGARASFRGRGRGRGRGRGRGRGGTRTHFDYQFGYRKFDGVEGPRTPKYMNNITYYFDNVSSTELYSVDQELLKDYIKRQIEYYFSVDNLERDFFLRRKMDADGFLPITLIASFHRVQALTTDISLIFAALKDSKVVEIVDEKVRRREEPEKWPLPPIVDYSQTDFSQLLNCPEFVPRQHYQKETESAPGSPRAVTPVPTKTEEVSNLKTLPKGLSASLPDLDSENWIEVKKRPRPSPARPKKSEESRFSHLTSLPQQLPSQQLMSKDQDEQEELDFLFDEEMEQMDGRKNTFTAWSDEESDYEIDDRDVNKILIVTQTPHYMRRHPGGDRTGNHTSRAKMSAELAKVINDGLFYYEQDLWAEKFEPEYSQIKQEVENFKKVNMISREQFDTLTPEPPVDPNQEVPPGPPRFQQVPTDALANKLFGAPEPSTIARSLPTTVPESPNYRNTRTPRTPRTPQLKDSSQTSRFYPVVKEGRTLDAKMPRKRKTRHSSNPPLESHVGWVMDSREHRPRTASISSSPSEGTPTVGSYGCTPQSLPKFQHPSHELLKENGFTQHVYHKYRRRCLNERKRLGIGQSQEMNTLFRFWSFFLRDHFNKKMYEEFKQLALEDAKEGYRYGLECLFRYYSYGLEKKFRLDIFKDFQEETVKDYEAGQLYGLEKFWAFLKYSKAKNLDIDPKLQEYLGKFRRLEDFRVDPPMGEEGNHKRHSVVAGGGGGEGRKRCPSQSSSRPAAMISQPPTPPTGQPVREDAKWTSQHSNTQTLGK	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses	.	Q6PKG0
TTZJA87	LIM and SH3 domain protein 1 (LASP1)	Q14847	LASP1_HUMAN	.	Metastatic lymph node gene 50 protein; MLN50; MLN 50; LASP-1	LASP1	"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."	.	3I35	MNPNCARCGKIVYPTEKVNCLDKFWHKACFHCETCKMTLNMKNYKGYEKKPYCNAHYPKQSFTMVADTPENLRLKQQSELQSQVRYKEEFEKNKGKGFSVVADTPELQRIKKTQDQISNIKYHEEFEKSRMGPSGGEGMEPERRDSQDGSSYRRPLEQQQPHHIPTSAPVYQQPQQQPVAQSYGGYKEPAAPVSIQRSAPGGGGKRYRAVYDYSAADEDEVSFQDGDTIVNVQQIDDGWMYGTVERTGDTGMLPANYVEAI	Literature-reported	The role of LIM and SH3 protein-1 in bladder cancer metastasis. Oncol Lett. 2017 Oct;14(4):4829-4834.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q14847
TTD2IK3	Lassa virus Pre-glycoprotein polyprotein GP complex (LASV GPC)	P17332	GLYC_LASSG	.	Pre-GP-C	LASV GPC	.	.	.	MGQIVTFFQEVPHVIEEVMNIVLIALSILAILKGLYNVATCGLIGLVTFLLLSGRSCSLIYKGTYELQTLELNMETLNMTMPLSCTKNNSHHYIRVGNETGLELTLTNTSILNHKFCNLSDAHKRNLYDHSLMSIISTFHLSIPNFNQYEAMSCDFNGGKITVQYNLSHSFAVDAAGHCGTLANGVLQTFMRMAWGGSYIALDSGRGNWDCIMTSYQYLIIQNTTWDDHCQFSRPSPIGYLGLLSQRTRDIYISRRLLGTFTWTLSDSEGNETPGGYCLTRWMLIEAELKCFGNTAVAKCNEKHDEEFCDMLRLFDFNKQAIRRLKTEAQMSIQLINKAVNALINDQLIMKNHLRDIMGIPYCNYSRYWYLNHTSTGKTSLPRCWLISNGSYLNETKFSDDIEQQADNMITEMLQKEYIDRQGKTPLGLVDLFVFSTSFYLISIFLHLVKIPTHRHIVGKPCPKPHRLNHMGICSCGLYKQPGVPVRWKR	Clinical trial	A potent Lassa virus antiviral targets an arenavirus virulence determinant. PLoS Pathog. 2018 Dec 21;14(12):e1007439.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTML7FG	Large tumor suppressor homolog 2 (LATS2)	Q9NRM7	LATS2_HUMAN	Kinase	Warts-like kinase; Serine/threonine-protein kinase kpm; Serine/threonine-protein kinase LATS2; Kinase phosphorylated during mitosis protein; KPM	LATS2	"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."	EC 2.7.11.1	4ZRI	MRPKTFPATTYSGNSRQRLQEIREGLKQPSKSSVQGLPAGPNSDTSLDAKVLGSKDATRQQQQMRATPKFGPYQKALREIRYSLLPFANESGTSAAAEVNRQMLQELVNAGCDQEMAGRALKQTGSRSIEAALEYISKMGYLDPRNEQIVRVIKQTSPGKGLMPTPVTRRPSFEGTGDSFASYHQLSGTPYEGPSFGADGPTALEEMPRPYVDYLFPGVGPHGPGHQHQHPPKGYGASVEAAGAHFPLQGAHYGRPHLLVPGEPLGYGVQRSPSFQSKTPPETGGYASLPTKGQGGPPGAGLAFPPPAAGLYVPHPHHKQAGPAAHQLHVLGSRSQVFASDSPPQSLLTPSRNSLNVDLYELGSTSVQQWPAATLARRDSLQKPGLEAPPRAHVAFRPDCPVPSRTNSFNSHQPRPGPPGKAEPSLPAPNTVTAVTAAHILHPVKSVRVLRPEPQTAVGPSHPAWVPAPAPAPAPAPAPAAEGLDAKEEHALALGGAGAFPLDVEYGGPDRRCPPPPYPKHLLLRSKSEQYDLDSLCAGMEQSLRAGPNEPEGGDKSRKSAKGDKGGKDKKQIQTSPVPVRKNSRDEEKRESRIKSYSPYAFKFFMEQHVENVIKTYQQKVNRRLQLEQEMAKAGLCEAEQEQMRKILYQKESNYNRLKRAKMDKSMFVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDSLYFVMDYIPGGDMMSLLIRMEVFPEHLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFRWTHNSKYYQKGSHVRQDSMEPSDLWDDVSNCRCGDRLKTLEQRARKQHQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQPPFLAPTPTETQLKVINWENTLHIPAQVKLSPEARDLITKLCCSADHRLGRNGADDLKAHPFFSAIDFSSDIRKQPAPYVPTISHPMDTSNFDPVDEESPWNDASEGSTKAWDTLTSPNNKHPEHAFYEFTFRRFFDDNGYPFRCPKPSGAEASQAESSDLESSDLVDQTEGCQPVYV	Literature-reported	Tetrahydroisoquinoline derivatives as highly selective and potent Rho kinase inhibitors. J Med Chem. 2010 Aug 12;53(15):5727-37.	0	EC:2.7	Kinase	protein kinase superfamily. AGC Ser/Thr protein kinase family.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain; Protein kinase C terminal domain	PF00069; PF00433	PF00069; Pkinase; PF00433; Pkinase_C	.	.	hsa04390: Hippo signaling pathway; hsa04392: Hippo signaling pathway - multiple species	R-HSA-2028269: Signaling by Hippo	.	Q9NRM7
TTVQJLY	Lipopolysaccharide-binding protein (LBP)	P18428	LBP_HUMAN	Bactericidal permeability increasing protein	LBP	LBP	"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."	.	.	MGALARALPSILLALLLTSTPEALGANPGLVARITDKGLQYAAQEGLLALQSELLRITLPDFTGDLRIPHVGRGRYEFHSLNIHSCELLHSALRPVPGQGLSLSISDSSIRVQGRWKVRKSFFKLQGSFDVSVKGISISVNLLLGSESSGRPTVTASSCSSDIADVEVDMSGDLGWLLNLFHNQIESKFQKVLESRICEMIQKSVSSDLQPYLQTLPVTTEIDSFADIDYSLVEAPRATAQMLEVMFKGEIFHRNHRSPVTLLAAVMSLPEEHNKMVYFAISDYVFNTASLVYHEEGYLNFSITDDMIPPDSNIRLTTKSFRPFVPRLARLYPNMNLELQGSVPSAPLLNFSPGNLSVDPYMEIDAFVLLPSSSKEPVFRLSVATNVSATLTFNTSKITGFLKPGKVKVELKESKVGLFNAELLEALLNYYILNTFYPKFNDKLAEGFPLPLLKRVQLYDLGLQIHKDFLFLGANVQYMRV	Literature-reported	Toll-like receptor 2 pathway drives streptococcal cell wall-induced joint inflammation: critical role of myeloid differentiation factor 88. J Immunol. 2003 Dec 1;171(11):6145-53.	.	.	.	.	.	.	.	.	.	.	.	hsa04064: NF-kappa B signaling pathway; hsa04620: Toll-like receptor signaling pathway; hsa04936: Alcoholic liver disease; hsa05152: Tuberculosis; hsa05417: Lipid and atherosclerosis	R-HSA-166016: Toll Like Receptor 4 (TLR4) Cascade; R-HSA-166020: Transfer of LPS from LBP carrier to CD14; R-HSA-5686938: Regulation of TLR by endogenous ligand; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling	.	P18428
TTGZ91P	Lecithin-cholesterol acyltransferase (LCAT)	P04180	LCAT_HUMAN	Acyltransferase	Phospholipidcholesterolacyltransferase; Phospholipid-cholesterol acyltransferase; Phosphatidylcholinesterol acyltransferase; Phosphatidylcholine-sterol acyltransferase	LCAT	"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."	EC 2.3.1.43	6MVD; 5TXF; 5BV7; 4XX1; 4XWG	MGPPGSPWQWVTLLLGLLLPPAAPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQLEAKLDKPDVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGVQIRVPGFGKTYSVEYLDSSKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEYYRKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLRQPQAWKDRFIDGFISLGAPWGGSIKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSRMAWPEDHVFISTPSFNYTGRDFQRFFADLHFEEGWYMWLQSRDLLAGLPAPGVEVYCLYGVGLPTPRTYIYDHGFPYTDPVGVLYEDGDDTVATRSTELCGLWQGRQPQPVHLLPLHGIQHLNMVFSNLTLEHINAILLGAYRQGPPASPTASPEPPPPE	Clinical trial	Familial lecithin-cholesterol acyltransferase (LCAT) deficiency; a differential of proteinuria. J Nephropathol. 2015 January; 4(1): 25-28.	21	EC:2.3	Acyltransferase	AB hydrolase superfamily. Lipase family.	2.3.1.43 	Acyltransferases	Lecithin:cholesterol acyltransferase	PF02450	PF02450; LCAT	.	.	hsa00564:Glycerophospholipid metabolism	R-HSA-194223:HDL-mediated lipid transport	.	P04180
TT860QF	LCK tyrosine protein kinase (LCK)	P06239	LCK_HUMAN	Kinase	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	LCK	"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."	EC 2.7.10.2	6H6A; 5MTN; 5MTM; 4D8K; 4C3F	MGCGCSSHPEDDWMENIDVCENCHYPIVPLDGKGTLLIRNGSEVRDPLVTYEGSNPPASPLQDNLVIALHSYEPSHDGDLGFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVAKANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQTQKPQKPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMVRPDNCPEELYQLMRLCWKERPEDRPTFDYLRSVLEDFFTATEGQYQPQP	Successful	A comparison of physicochemical property profiles of marketed oral drugs and orally bioavailable anti-cancer protein kinase inhibitors in clinical development. Curr Top Med Chem. 2007;7(14):1408-22.	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. SRC subfamily.	2.7.10.2	Transferring phosphorus-containing groups	Protein tyrosine kinase; SH2 domain; SH3 domain	PF07714; PF00017; PF00018	PF07714; Pkinase_Tyr; PF00017; SH2; PF00018; SH3_1	.	.	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	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	.	P06239
TTKTLAI	Neutrophil gelatinase-associated lipocalin (LCN2)	P80188	NGAL_HUMAN	Calycin family	p25; Siderocalin LCN2; Oncogene 24p3; NGAL; Lipocalin-2; LCN2; 25 kDa alpha-2-microglobulin-related subunit of MMP-9	LCN2	"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. ."	.	6GR0; 6GQZ; 5NKN; 5N48; 5N47	MPLGLLWLGLALLGALHAQAQDSTSDLIPAPPLSKVPLQQNFQDNQFQGKWYVVGLAGNAILREDKDPQKMYATIYELKEDKSYNVTSVLFRKKKCDYWIRTFVPGCQPGEFTLGNIKSYPGLTSYLVRVVSTNYNQHAMVFFKKVSQNREYFKITLYGRTKELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG	Literature-reported	"Biomarkers of diabetic nephropathy, the present and the future. Curr Diabetes Rev. 2012 Sep;8(5):317-28."	.	.	.	.	.	.	.	.	.	.	.	hsa04657: IL-17 signaling pathway	R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6798695: Neutrophil degranulation; R-HSA-6799990: Metal sequestration by antimicrobial proteins; R-HSA-917937: Iron uptake and transport	.	P80188
TTA0OSE	Lactase-phlorizin hydrolase (LCT)	P09848	LPH_HUMAN	Glycosylase	Lactase-glycosylceramidase; LCT; Glycosyl-hydrolase	LCT	LPH splits lactose in the small intestine.	.	.	MELSWHVVFIALLSFSCWGSDWESDRNFISTAGPLTNDLLHNLSGLLGDQSSNFVAGDKDMYVCHQPLPTFLPEYFSSLHASQITHYKVFLSWAQLLPAGSTQNPDEKTVQCYRRLLKALKTARLQPMVILHHQTLPASTLRRTEAFADLFADYATFAFHSFGDLVGIWFTFSDLEEVIKELPHQESRASQLQTLSDAHRKAYEIYHESYAFQGGKLSVVLRAEDIPELLLEPPISALAQDTVDFLSLDLSYECQNEASLRQKLSKLQTIEPKVKVFIFNLKLPDCPSTMKNPASLLFSLFEAINKDQVLTIGFDINEFLSCSSSSKKSMSCSLTGSLALQPDQQQDHETTDSSPASAYQRIWEAFANQSRAERDAFLQDTFPEGFLWGASTGAFNVEGGWAEGGRGVSIWDPRRPLNTTEGQATLEVASDSYHKVASDVALLCGLRAQVYKFSISWSRIFPMGHGSSPSLPGVAYYNKLIDRLQDAGIEPMATLFHWDLPQALQDHGGWQNESVVDAFLDYAAFCFSTFGDRVKLWVTFHEPWVMSYAGYGTGQHPPGISDPGVASFKVAHLVLKAHARTWHHYNSHHRPQQQGHVGIVLNSDWAEPLSPERPEDLRASERFLHFMLGWFAHPVFVDGDYPATLRTQIQQMNRQCSHPVAQLPEFTEAEKQLLKGSADFLGLSHYTSRLISNAPQNTCIPSYDTIGGFSQHVNHVWPQTSSSWIRVVPWGIRRLLQFVSLEYTRGKVPIYLAGNGMPIGESENLFDDSLRVDYFNQYINEVLKAIKEDSVDVRSYIARSLIDGFEGPSGYSQRFGLHHVNFSDSSKSRTPRKSAYFFTSIIEKNGFLTKGAKRLLPPNTVNLPSKVRAFTFPSEVPSKAKVVWEKFSSQPKFERDLFYHGTFRDDFLWGVSSSAYQIEGAWDADGKGPSIWDNFTHTPGSNVKDNATGDIACDSYHQLDADLNMLRALKVKAYRFSISWSRIFPTGRNSSINSHGVDYYNRLINGLVASNIFPMVTLFHWDLPQALQDIGGWENPALIDLFDSYADFCFQTFGDRVKFWMTFNEPMYLAWLGYGSGEFPPGVKDPGWAPYRIAHAVIKAHARVYHTYDEKYRQEQKGVISLSLSTHWAEPKSPGVPRDVEAADRMLQFSLGWFAHPIFRNGDYPDTMKWKVGNRSELQHLATSRLPSFTEEEKRFIRATADVFCLNTYYSRIVQHKTPRLNPPSYEDDQEMAEEEDPSWPSTAMNRAAPWGTRRLLNWIKEEYGDIPIYITENGVGLTNPNTEDTDRIFYHKTYINEALKAYRLDGIDLRGYVAWSLMDNFEWLNGYTVKFGLYHVDFNNTNRPRTARASARYYTEVITNNGMPLAREDEFLYGRFPEGFIWSAASAAYQIEGAWRADGKGLSIWDTFSHTPLRVENDAIGDVACDSYHKIAEDLVTLQNLGVSHYRFSISWSRILPDGTTRYINEAGLNYYVRLIDTLLAASIQPQVTIYHWDLPQTLQDVGGWENETIVQRFKEYADVLFQRLGDKVKFWITLNEPFVIAYQGYGYGTAAPGVSNRPGTAPYIVGHNLIKAHAEAWHLYNDVYRASQGGVISITISSDWAEPRDPSNQEDVEAARRYVQFMGGWFAHPIFKNGDYNEVMKTRIRDRSLAAGLNKSRLPEFTESEKRRINGTYDFFGFNHYTTVLAYNLNYATAISSFDADRGVASIADRSWPDSGSFWLKMTPFGFRRILNWLKEEYNDPPIYVTENGVSQREETDLNDTARIYYLRTYINEALKAVQDKVDLRGYTVWSAMDNFEWATGFSERFGLHFVNYSDPSLPRIPKASAKFYASVVRCNGFPDPATGPHACLHQPDAGPTISPVRQEEVQFLGLMLGTTEAQTALYVLFSLVLLGVCGLAFLSYKYCKRSKQGKTQRSQQELSPVSSF	Literature-reported	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	0	.	.	.	.	.	.	.	.	.	.	hsa00052:Galactose metabolism; hsa01100:Metabolic pathways; hsa04973:Carbohydrate digestion and absorption	R-HSA-189085: Digestion of dietary carbohydrate; R-HSA-5659898: Intestinal saccharidase deficiencies	MetaCyc:HS03945-MON	P09848
TTW76JE	LDHA messenger RNA (LDHA mRNA)	P00338	LDHA_HUMAN	.	LDH-A; Cell proliferation-inducing gene 19 protein; LDH muscle subunit; LDH-M; Renal carcinoma antigen NY-REN-59	LDHA	.	EC 1.1.1.27	.	MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF	Clinical trial	Hepatic Lactate Dehydrogenase A: An RNA Interference Target for the Treatment of All Known Types of Primary Hyperoxaluria. Kidney Int Rep. 2021 Feb 3;6(4):1088-1098.	.	.	.	.	.	.	.	.	.	.	.	hsa00010: Glycolysis / Gluconeogenesis; hsa00270: Cysteine and methionine metabolism; hsa00620: Pyruvate metabolism; hsa00640: Propanoate metabolism; hsa01100: Metabolic pathways; hsa04066: HIF-1 signaling pathway; hsa04922: Glucagon signaling pathway; hsa05230: Central carbon metabolism in cancer	R-HSA-70268: Pyruvate metabolism	.	P00338
TTNFMAL	Lactate dehydrogenase A (LDHA)	P00338	LDHA_HUMAN	CH-OH donor oxidoreductase	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	LDHA	"Cadherin binding, L-lactate dehydrogenase activity, glycolytic process, pyruvate metabolic process, substantia nigra development."	EC 1.1.1.27	6BB3; 6BB2; 6BB1; 6BB0; 6BAZ	MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF	Literature-reported	Lactate dehydrogenase A in cancer: a promising target for diagnosis and therapy. IUBMB Life. 2013 Nov;65(11):904-10.	.	EC:1.1	Short-chain dehydrogenases reductases	LDH/MDH superfamily. LDH family.	1.1.1.27	Acting on the CH-OH group of donors	"lactate/malate dehydrogenase, alpha/beta C-terminal domain; lactate/malate dehydrogenase, NAD binding domain"	PF02866; PF00056	PF02866; Ldh_1_C; PF00056; Ldh_1_N	.	.	hsa00010: Glycolysis / Gluconeogenesis; hsa00270: Cysteine and methionine metabolism; hsa00620: Pyruvate metabolism; hsa00640: Propanoate metabolism; hsa01100: Metabolic pathways; hsa04066: HIF-1 signaling pathway; hsa04922: Glucagon signaling pathway; hsa05230: Central carbon metabolism in cancer	R-HSA-70268: Pyruvate metabolism	.	P00338
TTAZHU0	L-lactate dehydrogenase (LDH)	P00338; P07195; P07864	LDHA_HUMAN; LDHB_HUMAN; LDHC_HUMAN	Short-chain dehydrogenases reductase	Renal carcinoma antigen NY-REN; LDH	LDHA	"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"	.	.	MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	hsa00010: Glycolysis / Gluconeogenesis; hsa00270: Cysteine and methionine metabolism; hsa00620: Pyruvate metabolism; hsa00640: Propanoate metabolism; hsa01100: Metabolic pathways; hsa04066: HIF-1 signaling pathway; hsa04922: Glucagon signaling pathway; hsa05230: Central carbon metabolism in cancer	R-HSA-70268: Pyruvate metabolism	.	P00338
TTQTSFR	HUMAN l-lactate dehydrogenase (LDH)	P00338; P07195; P07864	LDHA_HUMAN; LDHB_HUMAN; LDHC_HUMAN	Short-chain dehydrogenases reductase	Renal carcinoma antigen NY-REN; LDH	LDHA	"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"	.	.	MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF	.	Hematological Findings and Complications of COVID-19. Am J Hematol. 2020 Apr 13. doi: 10.1002/ajh.25829.	.	.	.	.	.	.	.	.	.	.	.	hsa00010: Glycolysis / Gluconeogenesis; hsa00270: Cysteine and methionine metabolism; hsa00620: Pyruvate metabolism; hsa00640: Propanoate metabolism; hsa01100: Metabolic pathways; hsa04066: HIF-1 signaling pathway; hsa04922: Glucagon signaling pathway; hsa05230: Central carbon metabolism in cancer	R-HSA-70268: Pyruvate metabolism	.	P00338
TTH0DUS	Low-density lipoprotein receptor (LDL-R)	P01130	LDLR_HUMAN	Low density lipoprotein receptor	LDL receptor	LDLR	"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."	.	5OYL; 5OY9; 4NE9; 3SO6; 3P5C	MGPWGWKLRWTVALLLAAAGTAVGDRCERNEFQCQDGKCISYKWVCDGSAECQDGSDESQETCLSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCPPKTCSQDEFRCHDGKCISRQFVCDSDRDCLDGSDEASCPVLTCGPASFQCNSSTCIPQLWACDNDPDCEDGSDEWPQRCRGLYVFQGDSSPCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCAVATCRPDEFQCSDGNCIHGSRQCDREYDCKDMSDEVGCVNVTLCEGPNKFKCHSGECITLDKVCNMARDCRDWSDEPIKECGTNECLDNNGGCSHVCNDLKIGYECLCPDGFQLVAQRRCEDIDECQDPDTCSQLCVNLEGGYKCQCEEGFQLDPHTKACKAVGSIAYLFFTNRHEVRKMTLDRSEYTSLIPNLRNVVALDTEVASNRIYWSDLSQRMICSTQLDRAHGVSSYDTVISRDIQAPDGLAVDWIHSNIYWTDSVLGTVSVADTKGVKRKTLFRENGSKPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIYSLVTENIQWPNGITLDLLSGRLYWVDSKLHSISSIDVNGGNRKTILEDEKRLAHPFSLAVFEDKVFWTDIINEAIFSANRLTGSDVNLLAENLLSPEDMVLFHNLTQPRGVNWCERTTLSNGGCQYLCLPAPQINPHSPKFTCACPDGMLLARDMRSCLTEAEAAVATQETSTVRLKVSSTAVRTQHTTTRPVPDTSRLPGATPGLTTVEIVTMSHQALGDVAGRGNEKKPSSVRALSIVLPIVLLVFLCLGVFLLWKNWRLKNINSINFDNPVYQKTTEDEVHICHNQDGYSYPSRQMVSLEDDVA	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	Low density lipoprotein receptor	.	LDLR family.	.	.	Calcium-binding EGF domain; Low-density lipoprotein receptor domain class A; Low-density lipoprotein receptor repeat class B	PF07645; PF00057; PF00058	PF07645; EGF_CA; PF00057; Ldl_recept_a; PF00058; Ldl_recept_b	.	.	hsa04144:Endocytosis; hsa04913:Ovarian steroidogenesis; hsa04976:Bile secretion; hsa05145:Toxoplasmosis; hsa05160:Hepatitis C	R-HSA-171052:LDL-mediated lipid transport; R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-975634:Retinoid metabolism and transport	.	P01130
TT5XOKS	Leishmania Carbamoyl-phosphate synthase (Leishm CPS)	E9BCR2	E9BCR2_LEIDB	Carbon-nitrogen ligase	"Carbamoyl-phosphate synthase, putative"	Leishm CPS	"Catalyses the formation of carbamoyl phosphate from L-glutamine, bicarbonate, and 2 moles of MgATP. "	.	.	MEHYAKAELVLHGGERFEGYSFGYEESVAGEVVFATGMVGYPESLSDPSYHGQILVLTSPMVGNYGVPRVEEDLFGVTKYFESTDGQIHVSAVVVQEYCDQPDHWEMYETLGTWLRKNKVPGMMMVDTRSIVLKLRDMGTALGKVLVAGNDVPFMDPNTRNLVAEVSTKTRVTHGHGTLRILVIDMGVKLNTLRCLLKHDVTLIVVPHDWDITTEVYDGLFITNGPGNPQICTSTIRSVRWALQQDKPIFGICMGNQMLCLAAGGTTYKMKYGHRGQNQPCKCNIDGRVVITTQNHGFAVDFKTLPSGEWEEYFTNSNDGSNEGLWHKTKPFCSVQFHPEGRCGPQDTEYLFSEYVCRVKESKVREVAKFKPRKVLVLGAGGIVIAQAGEFDYSGSQCLKSLREEGMETVLINPNIATVQTDDEMADHIYFVPLTVEAVERVIEKERPDGILLGWGGQTALNCGVKLDELGVLKKYNVQVLGTPVSVIAVTEDRELFRDTLLQINEQVAKSAAVMSVEEAVAASKDIGFPMMVRAAYCLGGQGSGIVENMEELRHKVEVALAASPQVLLEESVAGWKEIEYEVVRDIYDNCITVCNMENFDPMGVHTGESIVVAPSQTLSNDEFHMLRSASIKIIRHLGIVGECNIQYGLDPFSHRYVVIEVNARLSRSSALASKATGYPLAHVATKIALGKGLFEITNGVTKTTMACFEPSMDYIAVKMPRWDLHKFNMVSEEIGSMMKSVGEVMSIGRTFEEALQKAIRMVDPSYTGFSLPDRFAGVDFDYMEHIRHPTPYRLFALCRALLDGHSAEELYQMTKITRFFLYKLEKLVRLSKATSTLYANKLTEMPRENLLNMKAHGFSDRQLAQLLNSTAADVRARRVELNVMPLIKQIDTVAGEYPAAQCCYLYSTYNAQRDDVPFTERMYAVLGCGVYRIGNSVEFDYGGVLVARELRRLGNKVILINYNPETVSTDYDECDRLYFDEVSEETVLDILTKERVRGVVISLGGQIVQNMALSLKKSGLPILGTDPANIDMAEDRNKFSKMCDELGVPQPEWISATSVEQVHEFCDTVGYPALVRPSYVLSGSAMAVIANKEDVTRYLKEASFVSGEHPVVVSKYYEAATEYDVDIVAHHGRVLCYAICEHVENAGVHSGDATMFLPPQNTDKDTMKRIYDSVNRIAEKLDVVGPMNVQFLLTAEGQLRVIEANVRSSRSVPFVSKTLGISFPSVMVSAFLARKDQNLVPIKRAKMTHIGCKASMFSFNRLAGADPILGVEMASTGEIGVFGRDKHEVFLKAMLCQNFKIPQKGVFFSSDVDSQTEALCPYIQHLVRRGLKVYGTTKTAAVLHEYGIQCEVLLQRGELPSGDASESNRLAVYDEEVAKKEKFDLVIQLRDKRRDFVLRRCTRETAPPDYWVRRLAVDYNIPLLTEPSIVKMFCECMDLPASSIEIEPFRHYVPKIYHKVENNNCAMLRCHKVGLMITNNNDSKVLALRLSQEGLNITCFHAYLGGSDIDHFEQAFQSLNVPVEVVDLRSEIANSAFDLIMCQSADERHNWHLSKLSWYIFGKYLIPVMRQRRMSVVAQTSKQNKKEAGFEKYVQSNCPEMGVYNAWRDARLMEDFETVADQISFLRKHGIKATVKSNVQVHSSVCGSTYYGDDMRSLPAPSLVKPVRECSVTPEFVSLTFRGARCVNINGIDVTPLLALQMANEIAGRNGVGITRTREGAMYETPGMNLLSVGLQFLYDVSFDRCAADLFRIYSRHVSQNIGAGQLSEKHTQSAIEAVRFLTSDVSGVVELELHQGEIIFLKLSHVQNPVDRRVAPQLVTEEELEEVFQPGNGSFSDVQW	Discontinued	Acivicin: a highly active potential chemotherapeutic agent against visceral leishmaniasis. Biochem Biophys Res Commun. 1990 Jul 31;170(2):426-32.	9	.	.	.	.	.	.	.	.	.	.	"ldo00240: Pyrimidine metabolism; ldo00250: Alanine, aspartate and glutamate metabolism; ldo01100: Metabolic pathways; ldo01240: Biosynthesis of cofactors"	.	.	.
TT3ETNF	Leishmania Elongation factor 1-alpha (Leishm EF1A)	Q95VF2	Q95VF2_LEIDO	.	Leishmania Elongation factor 1A	Leishm EF1A	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.	.	.	MGKDKVHMNLVVVGHVDAGKSTATGHLIYKCGGIDKRTIEKFEKEAAEIGKASFKYAWVLDKLKAERERGITIDIALWKFESPKSVFTIIDAPGHRDFIKNMITGTSQADAAILMIDSTHGGFEAGISKDGQTREHALLAFTLGVKQMVVCCNKMDDKTVTYAQSRYDEISKEVGAYLKRVGYNPEKVRFIPISGWQGDNMIERSDNMPWYKGPTLLDALDMLEPPVRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGIMKPGDVVTFAPANVTTEVKSIEMHHEQLAEAQPGDNVGFNVKNVSVKDIRRGNVCGNSKNDPPKEAADFTAQVIVLNHPGQISNGYAPVLDCHTSHIACRFAEIESKIDRRSGKELEKNPKAIKSGDAAIVKMVPQKPMCVEVFNDYAPLGRFAVRDMRQTVAVGIIKGVNKKEGSGGKVTKAAAKAAKK	Literature-reported	The Eukaryotic Elongation Factor 1 Alpha (eEF1) from the Parasite Leishmania infantum Is Modified with the Immunomodulatory Substituent Phosphoryl... Molecules. 2017 Nov 29;22(12). pii: E2094.	.	.	.	.	.	.	.	.	.	.	.	ldo03013: Nucleocytoplasmic transport	.	.	.
TTVFA2D	Leishmania GDP-mannose pyrophosphorylase (Leishm exgmp)	Q9BLW4	Q9BLW4_LEIME	Transferases of phosphorus-containing groups	GDP-mannose pyrophosphorylase	Leishm exgmp	Assembles as a hexamer of 240 kDa in several Leishmania species. Critical for cell integrity and survival.	EC 2.7.7.22	.	MSASDGQGMRAVILVGGFGTRLRPLTLTTPKPLVPFCNKPMIIHQIEALKAVGVTEVILAVAYRPEAMKEQMDEWSRKLGVSFVFSVEEDPLGTAGPLALARDILMQDDKPFFVLNSDVTCMFPLQELLDFHKARGGEGTIMVSQVTQWEKYGVVVYSQQSYQIERFVEKPSSFLGDRVNAGIYIFNKSILDRIPPCRTSIEKEIFPAMAAEGELYAFNLEGFWMDVGQPKDYILGMTKFIPSLLDGDRKTEQLHTEATEHQHGGRFTVVGASLIDPSAKIGDGAVIGPCASIGANCVIGESCRIDNAAILENSKVGKGTMVSRSIVGWNNRIGSWCHIEDISVLGDDVEVKDGVVLIGTKVLPNKDVGEHHFQAGIIM	Literature-reported	"Properties of GDP-mannose pyrophosphorylase, a critical enzyme and drug target in Leishmania mexicana. J Biol Chem. 2004 Mar 26;279(13):12462-8."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTT1LHV	Leishmania Glutathionylspermidine synthase (Leishm GSP)	E9BI04	E9BI04_LEIDB	Carbon-nitrogen ligase	GspS; Glutathionylspermidine synthetase; Glutathione:spermidine ligase [ADP-forming]; GSP synthetase; GSP	Leishm GSP	"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."	.	.	MLSLPRDHHYHTHHRGTELVPFDQVIGITPDGVPVISNGNEFHFTNLESVTPFYQALCSFDRKAPVTVSYKKLGVKWQCVEFARRYLASRKAVWTASMPIAADMWRAETPFVRVQDGTPVEFTRIANRSHGPAPAMSDIIVWGQSEETPFGHVAVVTEVLPEAVRVAEQNQGFERWPQGMLYSREIPVQRSSAGTVELVDEDPVLGWVTLHCPYYDFRDGDLADKFRIVTGPGCIVRQPFPKHVELPWLQPEERCDFYLKRSLAIGGNVGDDARAKECDVPSAFYFLDYNIWCRLGRAAHSLHRIAMTATAQVLDDADSAYLLEHYFGLPPEIHPLLRRSWEMMPPMSGRFDFGYDGNKVAMLEYNCDSSGALLECCNTQEKMANYYGVSQGMSTGSFLGAKCVSHFARLMSNEKVCPKHKLIHFMIDDDDEERYTAMCMMNFAEKAGFRTKLCVKLIDFRYRDGAPANAAPLSVTCDHPIIVDSDGDEVLLVWKTWSWDTVLREYHRQCSATDSVSSPTLSDILLNNNICVIEPLWKAVTGSKALLPFMHALAPDHEHLLAADFVPTKDIISHHYVSKPINGRAGQNIMMFDPVTDAAELNAAPQEMLSESSSQLFSIKPPAASCSALQSQSIDRTNECSTGTFFDSAVVYQKRFFLKKFEGKYFPIFCGWMIDDEFGGVVVREDTSKITKLDSIVIPARVVRENVSLGGAYTDEGET	Literature-reported	Glutathione-like tripeptides as inhibitors of glutathionylspermidine synthetase. Part 2: substitution of the glycine part. Bioorg Med Chem Lett. 2002 Oct 7;12(19):2703-5.	.	.	.	.	.	.	.	.	.	.	.	ldo00480: Glutathione metabolism; ldo01100: Metabolic pathways	.	.	.
TTOUZG8	Leishmania Guanine nucleotide-binding protein (Leishm LACK)	Q25306	GBLP_LEIMA	.	Guanine nucleotide-binding protein subunit beta-like protein; Antigen LACK	Leishm LACK	Involved as modulators or transducers in various transmembrane signaling systems.	.	.	MNYEGHLKGHRGWVTSLACPQQAGSYIKVVSTSRDGTVISWKANPDRHSVDSDYGLPNHRLEGHTGFVSCVSLAHATDYALTASWDRSIRMWDLRNGQCQRKFLKHTKDVLAVAFSPDDRLIVSAGRDNVIRVWNVAGECMHEFLRDGHEDWVSSICFSPSLEHPIVVSGSWDNTIKVWNVNGGKCERTLKGHSNYVSTVTVSPDGSLCASGGKDGAALLWDLSTGEQLFKINVESPINQIGFSPNRFWMCVATERSLSVYDLESKAVIAELTPDGAKPSECISIAWSADGNTLYSGHKDNLIRVWSISDAE	Literature-reported	Leishmania major LACK antigen is required for efficient vertebrate parasitization. J Exp Med. 2003 Dec 1;198(11):1689-98.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q25306
TTZ840V	Leishmania 65kD membrane-associated NADH-fumarate reductase (Leishm nfr65)	Q8ITL2	Q8ITL2_9TRYP	CH-CH donor oxidoreductase	NADH-dependent fumarate reductase	Leishm nfr65	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.	.	.	MVDGRSSASIVAVDPERAARERDAAARALLQDSPLHTTMQYATSGLELTVPYALKVVASADTFDRAKEVADEVLRCAWQLADTVLNSFNPNSEVSLVGRLPVGQKHQMSAPLKRVMACCQRVYNSSAGCFDPSTAPVAKALREIALGKERNNACLEALTQACTLPNSFVIDFEAGTISRKHEHASLDLGGVSKGYIVDYVIDNINAAGFQNVFFDWGGDCRASGMNARNTPWVVGITRPPSLDMLPNPPKEASYISVISLDNEALATSGDYENLIYTADDKPLTCTYDWKGKELMKPSQSNIAQVSVKCYSAMYADALATACFIKRDPAKVRQLLDGWRYVRDTVRDYRVYVRENERVAKMFEIATEDAEMRKRRISNTLPARVIVVGGGLAGLSAAIEAAGCGAQVVLMEKEAKLGGNSAKATSGINGWGTRAQAKASIVDGGKYFERDTYKSGIGGNTDPALVKTLSMKSADAIGWLTSLGVPLTVLSQLGGHSRKRTHRAPDKKDGTPLPIGFTIMKTLEDHVRGNLSGRITIMENCSVTSLLSETKERPDGTKQIRVTGVEFTQAGSGKTTILADAVILATGGFSNDKTADSLLREHAPHLVNFPTTNGPWATGDGVKLAQRLGAQLVDMDKVQLHPTGLINPKDPANPTKFLGPEALRGSGGVLLNKQGKRFVNELDLRSVVSKAIMEQGAEYPGSGGSMFAYCVLNAAAQKLFGVSSHEFYWKKMGLFVKADTMRDLAALIGCPVESVQQTLEEYERLSISQRSCPITRKSVYPCVLGTKGPYYVAFVTPSIHYTMGGCLISPSAEIQMKNTSSRAPLSHSNPILGLFGAGEVTGGVHGGNRLGGNSLLECVVFGRIAGDRASTILQRKSSALSFKVWTTVVLREVREGGVYGAGSRVLRFNLPGALQRSGLSLGQFIAIRGDWDGQQLIGYYSPITLPDDLGMIDILARSDKGTLREWISALEPGDAVEMKACGGLVIERRLSDKHFVFMGHIINKLCLIAGGTGVAPMLQIIKAAFMKPFIDTLESVHLIYAAEDVTELTYREVLEERRRESRGKFKKTFVLNRPPPLWTDGVGFIDRGILTNHVQPPSDNLLVAICGPPVMQRIVKATLKTLGYNMNLVRTVDETEPSGSSKI	Literature-reported	Purification and enzymatic activity of an NADH-fumarate reductase and other mitochondrial activities of Leishmania parasites. APMIS. 2001 Dec;109(12):801-8.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNJKC3	Leishmania DNA topoisomerase I (Leishm TOP1)	Q9NJG8	Q9NJG8_LEIDO	.	Leishm DNA topoisomerase I; DNA topoisomerase 1	Leishm TOP1	"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."	EC 5.6.2.2	.	MPLPGGGTEVLKGITLLTQHHGLKPVQPMSFCYLSFLNRHTHEHHLRLHCCRPHAYARAHPCTCLIDFPLTSYPISQQCAPRLLPLPRQPPLSSQPAEAPSQIGTKDGLLLFRVSNRPQWVFCVCVCVRACPSFPLPRSCDFNRRGAVSPLSSPPRRAPVCCWRFFFHSCSFFFLVLYLLSAPYFCSLWARCANEEDKQNKLRIKQHETKKETPFRVCGGDCPSCCVGLSSHLFFPRWRLLVPPLPYTLDSNNSIFCVFHLFIYFLVCLFVSLAPSTYPFVPLCQLRTLHLYEPRPHIGTPLRCFCCHRDSIRRIMKVENSKMGVKREQSHSNEDEEINEEDLNWWEQENLRIAMKGERRWETLAHNGVLFPPEYEPHGIPIFYDGREFKMTPEEEEVATMFAVMKEHDYYRMEVFRRNFFESWREILDKRQHPIRRLELCDFEPIYQWHLVQREKKLSRTKEEKKAIKEKQDAEAEPYRYCVWDGRREQVANFRVEPPGLFRGRGKHPLMGKLKVRVQPEDITINIGETAEVPVPPAGHKWAAVQHDHTVTWLAMWRDSVAGNMKYVMLAPSSSVKGQSDMVKFEKARKLKDKVDDIRASYMEDFKSNDLHVAQRAVAMYIDRLALRVGNEKGEDEADTVGCCSLRVEHIQLMPDNIVRFDFLGKDSIRYQNDVAVLPEVYALLQRFTRRKSPGMDIFDQLNPTQLNDHLKSFMDGLSAKVFRTYNASITLDRWFKEKPVDPKWSTADKLAYFNKANTEVAILCNHQKSVSKNFKLQMMQLTTKSEYTRKTIELLEKAEVTAKKKSVEEAAKEFLEEQDRMQREWLESYGTEEQKKEFEEIVAKRAAPRVRSEKKKSTSGAKKAESASGKKRAAKKKKSAKKGGKMLSKKAASKSSKKAPKKLKEEDEDDVPLVSVAAKTKKTAGVKRQRANKVVSDDDDVPLAALRV	Clinical trial	Inhibition of Leishmania donovani promastigote DNA topoisomerase I and human monocyte DNA topoisomerases I and II by antimonial drugs and classical antitopoisomerase agents. J Parasitol. 2004 Oct;90(5):1155-62.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTW3AMG	Leishmania Cdc2-related kinase 3 (Leishmania CRK3)	O15851	O15851_LEIME	Kinase	Cdc2-related kinase 3; CRK3 cyclin-dependent kinase; CRK3	Leishmania CRK3	Form an active protein kinase complex with Leishmania cyclins CYCA and CYC6.	.	.	MSSFGRVTARSGDAGTRDSLDRYNRLDVLGEGTYGVVYRAVDKITGQYVALKKVRLDRTEEGIPQTALREVSILQEFDHPNIVNLLDVICSDGKLYLVFEYVEADLKKAIEKQEGGYSGMDLKRLIYQLLDGLYFCHRHRIIHRDLKPANILLTSGNVLKLADFGLARAFQVPMHTYTHEVVTLWYRAPEILLGEKHYTPAVDMWSVGCIFAELARRKVLFRGDSEIGQLFEIFQVLGTPTDTEGSWPGVSRLPDYRDVFPKWTAKRLGQVLPELHPDAIDLLSKMLKYDPRERISAKEALQHPWFSDLRW	Literature-reported	Inhibitors of Leishmania mexicana CRK3 cyclin-dependent kinase: chemical library screen and antileishmanial activity. Antimicrob Agents Chemother. 2004 Aug;48(8):3033-42.	.	EC:2.7	.	protein kinase superfamily.	.	.	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	.	.
TTBJEZ5	Leptin (LEP)	P41159	LEP_HUMAN	.	Obesity factor; Obese protein; LEP	LEP	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.	.	1AX8	MHWGTLCGFLWLWPYLFYVQAVPIQKVQDDTKTLIKTIVTRINDISHTQSVSSKQKVTGLDFIPGLHPILTLSKMDQTLAVYQQILTSMPSRNVIQISNDLENLRDLLHVLAFSKSCHLPWASGLETLDSLGGVLEASGYSTEVVALSRLQGSLQDMLWQLDLSPGC	Literature-reported	Monitoring calcific aortic valve disease: the role of biomarkers. Curr Med Chem. 2012;19(16):2548-54.	.	.	.	.	.	.	.	.	.	.	.	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	"R-HSA-2586552: Signaling by Leptin; R-HSA-381340: Transcriptional regulation of white adipocyte differentiation; R-HSA-381771: Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1); R-HSA-422085: Synthesis, secretion, and deacylation of Ghrelin"	.	P41159
TTJWAQ7	Signal peptidase I (lepB)	P00803	LEP_ECOLI	Peptidase	SPase I; Leader peptidase I	lepB	.	EC 3.4.21.89	1B12;1KN9;1T7D;3IIQ;3S04;6B88	MANMFALILVIATLVTGILWCVDKFFFAPKRRERQAAAQAAAGDSLDKATLKKVAPKPGWLETGASVFPVLAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPIYQKTLIETGHPKRGDIVVFKYPEDPKLDYIKRAVGLPGDKVTYDPVSKELTIQPGCSSGQACENALPVTYSNVEPSDFVQTFSRRNGGEATSGFFEVPKNETKENGIRLSERKETLGDVTHRILTVPIAQDQVGMYYQQPGQQLATWIVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGRATAIWMSFDKQEGEWPTGLRLSRIGGIH	Clinical trial	"Clinical pipeline report, company report or official report of Roche"	.	.	.	.	.	.	.	.	.	.	.	ecj:JW2552;eco:b2568	.	EcoCyc:EG10530-MONOMER;MetaCyc:EG10530-MONOMER;	P00803;
TT0HD6V	Leptin receptor (LEPR)	P48357	LEPR_HUMAN	Cytokine receptor	OBR; OB-R; OB receptor; LEP-R; HuB219; DB; CD295	LEPR	"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."	.	6E2P; 3V6O	MICQKFCVVLLHWEFIYVITAFNLSYPITPWRFKLSCMPPNSTYDYFLLPAGLSKNTSNSNGHYETAVEPKFNSSGTHFSNLSKTTFHCCFRSEQDRNCSLCADNIEGKTFVSTVNSLVFQQIDANWNIQCWLKGDLKLFICYVESLFKNLFRNYNYKVHLLYVLPEVLEDSPLVPQKGSFQMVHCNCSVHECCECLVPVPTAKLNDTLLMCLKITSGGVIFQSPLMSVQPINMVKPDPPLGLHMEITDDGNLKISWSSPPLVPFPLQYQVKYSENSTTVIREADKIVSATSLLVDSILPGSSYEVQVRGKRLDGPGIWSDWSTPRVFTTQDVIYFPPKILTSVGSNVSFHCIYKKENKIVPSKEIVWWMNLAEKIPQSQYDVVSDHVSKVTFFNLNETKPRGKFTYDAVYCCNEHECHHRYAELYVIDVNINISCETDGYLTKMTCRWSTSTIQSLAESTLQLRYHRSSLYCSDIPSIHPISEPKDCYLQSDGFYECIFQPIFLLSGYTMWIRINHSLGSLDSPPTCVLPDSVVKPLPPSSVKAEITINIGLLKISWEKPVFPENNLQFQIRYGLSGKEVQWKMYEVYDAKSKSVSLPVPDLCAVYAVQVRCKRLDGLGYWSNWSNPAYTVVMDIKVPMRGPEFWRIINGDTMKKEKNVTLLWKPLMKNDSLCSVQRYVINHHTSCNGTWSEDVGNHTKFTFLWTEQAHTVTVLAINSIGASVANFNLTFSWPMSKVNIVQSLSAYPLNSSCVIVSWILSPSDYKLMYFIIEWKNLNEDGEIKWLRISSSVKKYYIHDHFIPIEKYQFSLYPIFMEGVGKPKIINSFTQDDIEKHQSDAGLYVIVPVIISSSILLLGTLLISHQRMKKLFWEDVPNPKNCSWAQGLNFQKPETFEHLFIKHTASVTCGPLLLEPETISEDISVDTSWKNKDEMMPTTVVSLLSTTDLEKGSVCISDQFNSVNFSEAEGTEVTYEDESQRQPFVKYATLISNSKPSETGEEQGLINSSVTKCFSSKNSPLKDSFSNSSWEIEAQAFFILSDQHPNIISPHLTFSEGLDELLKLEGNFPEENNDKKSIYYLGVTSIKKRESGVLLTDKSRVSCPFPAPCLFTDIRVLQDSCSHFVENNINLGTSSKKTFASYMPQFQTCSTQTHKIMENKMCDLTV	Successful	2014 FDA drug approvals. Nat Rev Drug Discov. 2015 Feb;14(2):77-81.	34	Cytokine receptor	Cytokine receptor	type I cytokine receptor family. Type 2 subfamily.	.	.	Ig-like C2-type domain; Obesity receptor immunoglobulin like domain	PF06328; PF18589	PF06328; Lep_receptor_Ig; PF18589; ObR_Ig	.	.	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)	R-HSA-2586552: Signaling by Leptin	.	P48357
TTO3NYT	Galectin-1 (LGALS1)	P09382	LEG1_HUMAN	.	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	LGALS1	"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."	.	6F83; 6B94; 5MWX; 5MWT; 4Y24	MACGLVASNLNLKPGECLRVRGEVAPDAKSFVLNLGKDSNNLCLHFNPRFNAHGDANTIVCNSKDGGAWGTEQREAVFPFQPGSVAEVCITFDQANLTVKLPDGYEFKFPNRLNLEAINYMAADGDFKIKCVAFD	Patented-recorded	Human Galectin-1 and its inhibitors: Privileged target for cancer and HIV. Mini Rev Med Chem. 2019 Mar 4.	.	.	.	.	.	.	Galactoside-binding lectin	PF00337	PF00337; Gal-bind_lectin	.	.	.	R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation	.	P09382
TTRHK90	Galectin-2 (LGALS2)	P05162	LEG2_HUMAN	.	SLac lectin 2; Lactosebinding lectin 2; LGALS2; HL14; Gal2; Betagalactosidebinding lectin L14II	LGALS2	This protein binds beta-galactoside. Its physiological function is not yet known.	.	5EWS; 5DG2; 5DG1; 1HLC	MTGELEVKNMDMKPGSTLKITGSIADGTDGFVINLGQGTDKLNLHFNPRFSESTIVCNSLDGSNWGQEQREDHLCFSPGSEVKFTVTFESDKFKVKLPDGHELTFPNRLGHSHLSYLSVRGGFNMSSFKLKE	Literature-reported	Immunohistochemical Studies on Galectin Expression in Colectomised Patients with Ulcerative Colitis. Biomed Res Int. 2016;2016:5989128.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P05162
TTFPQV7	Galectin-3 (LGALS3)	P17931	LEG3_HUMAN	.	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	LGALS3	"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."	.	6QGF; 6QGE; 6I78; 6I77; 6I76	MADNFSLHDALSGSGNPNPQGWPGAWGNQPAGAGGYPGASYPGAYPGQAPPGAYPGQAPPGAYPGAPGAYPGAPAPGVYPGPPSGPGAYPSSGQPSATGAYPATGPYGAPAGPLIVPYNLPLPGGVVPRMLITILGTVKPNANRIALDFQRGNDVAFHFNPRFNENNRRVIVCNTKLDNNWGREERQSVFPFESGKPFKIQVLVEPDHFKVAVNDAHLLQYNHRVKKLNEISKLGISGDIDLTSASYTMI	Clinical trial	Therapy of experimental NASH and fibrosis with galectin inhibitors. PLoS One. 2013 Dec 18;8(12):e83481.	21	.	.	.	.	.	Galactoside-binding lectin	PF00337	PF00337; Gal-bind_lectin	.	.	.	R-HSA-879415:Advanced glycosylation endproduct receptor signaling	.	P17931
TTPTWV5	Legumain (LGMN)	Q99538	LGMN_HUMAN	Peptidase	"Protease, cysteine 1; PRSC1; Asparaginyl endopeptidase"	LGMN	"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."	EC 3.4.22.34	5LUB; 5LUA; 5LU9; 5LU8; 4N6O	MVWKVAVFLSVALGIGAVPIDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIVVMMYDDIAYSEDNPTPGIVINRPNGTDVYQGVPKDYTGEDVTPQNFLAVLRGDAEAVKGIGSGKVLKSGPQDHVFIYFTDHGSTGILVFPNEDLHVKDLNETIHYMYKHKMYRKMVFYIEACESGSMMNHLPDNINVYATTAANPRESSYACYYDEKRSTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKTISTMKVMQFQGMKRKASSPVPLPPVTHLDLTPSPDVPLTIMKRKLMNTNDLEESRQLTEEIQRHLDARHLIEKSVRKIVSLLAASEAEVEQLLSERAPLTGHSCYPEALLHFRTHCFNWHSPTYEYALRHLYVLVNLCEKPYPLHRIKLSMDHVCLGHY	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2380).	24	EC:3.4	Peptidase	peptidase C13 family.	3.4.22.34	Acting on peptide bonds (peptidases)	Peptidase C13 family	PF01650	PF01650; Peptidase_C13	.	.	hsa04142:Lysosome; hsa04612:Antigen processing and presentation	R-HSA-1679131:Trafficking and processing of endosomal TLR; R-HSA-196791:Vitamin D (calciferol) metabolism; R-HSA-2132295:MHC class II antigen presentation	.	Q99538
TTY6C71	G-protein coupled receptor 48 (LGR4)	Q9BXB1	LGR4_HUMAN	.	G-protein coupled receptor 48	LGR4	"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)."	.	.	MPGPLGLLCFLALGLLGSAGPSGAAPPLCAAPCSCDGDRRVDCSGKGLTAVPEGLSAFTQALDISMNNITQLPEDAFKNFPFLEELQLAGNDLSFIHPKALSGLKELKVLTLQNNQLKTVPSEAIRGLSALQSLRLDANHITSVPEDSFEGLVQLRHLWLDDNSLTEVPVHPLSNLPTLQALTLALNKISSIPDFAFTNLSSLVVLHLHNNKIRSLSQHCFDGLDNLETLDLNYNNLGEFPQAIKALPSLKELGFHSNSISVIPDGAFDGNPLLRTIHLYDNPLSFVGNSAFHNLSDLHSLVIRGASMVQQFPNLTGTVHLESLTLTGTKISSIPNNLCQEQKMLRTLDLSYNNIRDLPSFNGCHALEEISLQRNQIYQIKEGTFQGLISLRILDLSRNLIHEIHSRAFATLGPITNLDVSFNELTSFPTEGLNGLNQLKLVGNFKLKEALAAKDFVNLRSLSVPYAYQCCAFWGCDSYANLNTEDNSLQDHSVAQEKGTADAANVTSTLENEEHSQIIIHCTPSTGAFKPCEYLLGSWMIRLTVWFIFLVALFFNLLVILTTFASCTSLPSSKLFIGLISVSNLFMGIYTGILTFLDAVSWGRFAEFGIWWETGSGCKVAGFLAVFSSESAIFLLMLATVERSLSAKDIMKNGKSNHLKQFRVAALLAFLGATVAGCFPLFHRGEYSASPLCLPFPTGETPSLGFTVTLVLLNSLAFLLMAVIYTKLYCNLEKEDLSENSQSSMIKHVAWLIFTNCIFFCPVAFFSFAPLITAISISPEIMKSVTLIFFPLPACLNPVLYVFFNPKFKEDWKLLKRRVTKKSGSVSVSISSQGGCLEQDFYYDCGMYSHLQGNLTVCDCCESFLLTKPVSCKHLIKSHSCPALAVASCQRPEGYWSDCGTQSAHSDYADEEDSFVSDSSDQVQACGRACFYQSRGFPLVRYAYNLPRVKD	Preclinical	Opportunities for therapeutic antibodies directed at G-protein-coupled receptors. Nat Rev Drug Discov. 2017 Sep 1;16(9):661.	.	.	.	.	.	.	.	.	.	.	.	hsa04310: Wnt signaling pathway	R-HSA-4641263: Regulation of FZD by ubiquitination	.	Q9BXB1
TTTSGRH	Leucine-rich repeat-containing GPCR 5 (LGR5)	O75473	LGR5_HUMAN	GPCR rhodopsin	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	LGR5	"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."	.	4UFS; 4UFR; 4KNG; 4BSU; 4BST	MDTSRLGVLLSLPVLLQLATGGSSPRSGVLLRGCPTHCHCEPDGRMLLRVDCSDLGLSELPSNLSVFTSYLDLSMNNISQLLPNPLPSLRFLEELRLAGNALTYIPKGAFTGLYSLKVLMLQNNQLRHVPTEALQNLRSLQSLRLDANHISYVPPSCFSGLHSLRHLWLDDNALTEIPVQAFRSLSALQAMTLALNKIHHIPDYAFGNLSSLVVLHLHNNRIHSLGKKCFDGLHSLETLDLNYNNLDEFPTAIRTLSNLKELGFHSNNIRSIPEKAFVGNPSLITIHFYDNPIQFVGRSAFQHLPELRTLTLNGASQITEFPDLTGTANLESLTLTGAQISSLPQTVCNQLPNLQVLDLSYNLLEDLPSFSVCQKLQKIDLRHNEIYEIKVDTFQQLLSLRSLNLAWNKIAIIHPNAFSTLPSLIKLDLSSNLLSSFPITGLHGLTHLKLTGNHALQSLISSENFPELKVIEMPYAYQCCAFGVCENAYKISNQWNKGDNSSMDDLHKKDAGMFQAQDERDLEDFLLDFEEDLKALHSVQCSPSPGPFKPCEHLLDGWLIRIGVWTIAVLALTCNALVTSTVFRSPLYISPIKLLIGVIAAVNMLTGVSSAVLAGVDAFTFGSFARHGAWWENGVGCHVIGFLSIFASESSVFLLTLAALERGFSVKYSAKFETKAPFSSLKVIILLCALLALTMAAVPLLGGSKYGASPLCLPLPFGEPSTMGYMVALILLNSLCFLMMTIAYTKLYCNLDKGDLENIWDCSMVKHIALLLFTNCILNCPVAFLSFSSLINLTFISPEVIKFILLVVVPLPACLNPLLYILFNPHFKEDLVSLRKQTYVWTRSKHPSLMSINSDDVEKQSCDSTQALVTFTSSSITYDLPPSSVPSPAYPVTESCHLSSVAFVPCL	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 148).	0	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	Leucine Rich Repeat; Leucine rich repeat; Leucine rich repeat N-terminal domain	PF00560; PF13855; PF01462	PF00560; LRR_1; PF13855; LRR_8; PF01462; LRRNT	.	.	hsa04310: Wnt signaling pathway	R-HSA-4641263:Regulation of FZD by ubiquitination	.	O75473
TT2O4W9	Luteinizing hormone receptor (LHCGR)	P22888	LSHR_HUMAN	GPCR rhodopsin	Luteinizing hormone-releasing hormone receptor; LSH-R; LHRH receptor; LHCGR; LH/CG-R	LHCGR	Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.	.	1XUL; 1LUT	MKQRFSALQLLKLLLLLQPPLPRALREALCPEPCNCVPDGALRCPGPTAGLTRLSLAYLPVKVIPSQAFRGLNEVIKIEISQIDSLERIEANAFDNLLNLSEILIQNTKNLRYIEPGAFINLPRLKYLSICNTGIRKFPDVTKVFSSESNFILEICDNLHITTIPGNAFQGMNNESVTLKLYGNGFEEVQSHAFNGTTLTSLELKENVHLEKMHNGAFRGATGPKTLDISSTKLQALPSYGLESIQRLIATSSYSLKKLPSRETFVNLLEATLTYPSHCCAFRNLPTKEQNFSHSISENFSKQCESTVRKVNNKTLYSSMLAESELSGWDYEYGFCLPKTPRCAPEPDAFNPCEDIMGYDFLRVLIWLINILAIMGNMTVLFVLLTSRYKLTVPRFLMCNLSFADFCMGLYLLLIASVDSQTKGQYYNHAIDWQTGSGCSTAGFFTVFASELSVYTLTVITLERWHTITYAIHLDQKLRLRHAILIMLGGWLFSSLIAMLPLVGVSNYMKVSICFPMDVETTLSQVYILTILILNVVAFFIICACYIKIYFAVRNPELMATNKDTKIAKKMAILIFTDFTCMAPISFFAISAAFKVPLITVTNSKVLLVLFYPINSCANPFLYAIFTKTFQRDFFLLLSKFGCCKRRAELYRRKDFSAYTSNCKNGFTGSNKPSQSTLKLSTLHCQGTALLDKTRYTEC	Successful	Lutropin alfa. Drugs. 2008;68(11):1529-40.	34	.	.	.	.	.	.	.	.	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04913:Ovarian steroidogenesis; hsa04917:Prolactin signaling pathway	R-HSA-375281:Hormone ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events	.	P22888
TTGZ5WN	Leukemia inhibitory factor (LIF)	P15018	LIF_HUMAN	.	Melanoma-derived LPL inhibitor; MLPLI; HILDA; Emfilermin; Differentiation-stimulating factor; D factor	LIF	"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."	.	2Q7N; 1PVH; 1EMR	MKVLAAGVVPLLLVLHWKHGAGSPLPITPVNATCAIRHPCHNNLMNQIRSQLAQLNGSANALFILYYTAQGEPFPNNLDKLCGPNVTDFPPFHANGTEKAKLVELYRIVVYLGTSLGNITRDQKILNPSALSLHSKLNATADILRGLLSNVLCRLCSKYHVGHVDVTYGPDTSGKDVFQKKKLGCQLLGKYKQIIAVLAQAF	Clinical trial	Biomarkers in psoriasis and psoriatic arthritis. Ann Rheum Dis. 2013 Apr;72 Suppl 2:ii104-10. 	.	.	.	LIF/OSM family.	.	.	LIF / OSM family	PF01291	PF01291; LIF_OSM	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04630: JAK-STAT signaling pathway; hsa04668: TNF signaling pathway	R-HSA-6783783: Interleukin-10 signaling; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6788467: IL-6-type cytokine receptor ligand interactions	.	P15018
TTID542	Leukemia inhibitory factor receptor (LIFR)	P42702	LIFR_HUMAN	Cytokine receptor	LIF-R; LIF receptor; CD118	LIFR	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.	.	3E0G	MMDIYVCLKRPSWMVDNKRMRTASNFQWLLSTFILLYLMNQVNSQKKGAPHDLKCVTNNLQVWNCSWKAPSGTGRGTDYEVCIENRSRSCYQLEKTSIKIPALSHGDYEITINSLHDFGSSTSKFTLNEQNVSLIPDTPEILNLSADFSTSTLYLKWNDRGSVFPHRSNVIWEIKVLRKESMELVKLVTHNTTLNGKDTLHHWSWASDMPLECAIHFVEIRCYIDNLHFSGLEEWSDWSPVKNISWIPDSQTKVFPQDKVILVGSDITFCCVSQEKVLSALIGHTNCPLIHLDGENVAIKIRNISVSASSGTNVVFTTEDNIFGTVIFAGYPPDTPQQLNCETHDLKEIICSWNPGRVTALVGPRATSYTLVESFSGKYVRLKRAEAPTNESYQLLFQMLPNQEIYNFTLNAHNPLGRSQSTILVNITEKVYPHTPTSFKVKDINSTAVKLSWHLPGNFAKINFLCEIEIKKSNSVQEQRNVTIKGVENSSYLVALDKLNPYTLYTFRIRCSTETFWKWSKWSNKKQHLTTEASPSKGPDTWREWSSDGKNLIIYWKPLPINEANGKILSYNVSCSSDEETQSLSEIPDPQHKAEIRLDKNDYIISVVAKNSVGSSPPSKIASMEIPNDDLKIEQVVGMGKGILLTWHYDPNMTCDYVIKWCNSSRSEPCLMDWRKVPSNSTETVIESDEFRPGIRYNFFLYGCRNQGYQLLRSMIGYIEELAPIVAPNFTVEDTSADSILVKWEDIPVEELRGFLRGYLFYFGKGERDTSKMRVLESGRSDIKVKNITDISQKTLRIADLQGKTSYHLVLRAYTDGGVGPEKSMYVVTKENSVGLIIAILIPVAVAVIVGVVTSILCYRKREWIKETFYPDIPNPENCKALQFQKSVCEGSSALKTLEMNPCTPNNVEVLETRSAFPKIEDTEIISPVAERPEDRSDAEPENHVVVSYCPPIIEEEIPNPAADEAGGTAQVIYIDVQSMYQPQAKPEEEQENDPVGGAGYKPQMHLPINSTVEDIAAEEDLDKTAGYRPQANVNTWNLVSPDSPRSIDSNSEIVSFGSPCSINSRQFLIPPKDEDSPKSNGGGWSFTNFFQNKPND	Clinical trial	"Population pharmacokinetic modelling of Emfilermin (recombinant human leukaemia inhibitory factor, r-hLIF) in healthy postmenopausal women and in infertile patients undergoing in vitro fertilization and embryo transfer. Br J Clin Pharmacol. 2004 May; 57(5): 576-585."	19	Cytokine receptor	Fibronectin	type I cytokine receptor family. Type 2 subfamily.	.	.	Fibronectin type III domain; Leukemia inhibitory factor receptor D2 domain; Leukemia inhibitory factor receptor N-terminal domain	PF00041; PF17971; PF18207	PF00041; fn3; PF17971; LIFR_D2; PF18207; LIFR_N	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04550:Signaling pathways regulating pluripotency of stem cells; hsa04630:Jak-STAT signaling pathway	R-HSA-6788467: IL-6-type cytokine receptor ligand interactions; R-HSA-8939247: RUNX1 regulates transcription of genes involved in interleukin signaling	.	P42702
TTGZN2L	Leukocyte Ig-like receptor-3 (LILR3)	Q8N6C8; O75022	LIRA3_HUMAN; LIRB3_HUMAN	.	Monocyte inhibitory receptor; Leukocyte immunoglobulin-like receptor; LIR; Immunoglobulin-like transcript; ILT; CD85 antigen-like family member; CD85	LILRA3	"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."	.	.	MTPILTVLICLGLSLDPRTHVQAGPLPKPTLWAEPGSVITQGSPVTLRCQGSLETQEYHLYREKKTALWITRIPQELVKKGQFPILSITWEHAGRYCCIYGSHTAGLSESSDPLELVVTGAYSKPTLSALPSPVVTSGGNVTIQCDSQVAFDGFILCKEGEDEHPQCLNSHSHARGSSRAIFSVGPVSPSRRWSYRCYGYDSRAPYVWSLPSDLLGLLVPGVSKKPSLSVQPGPVVAPGEKLTFQCGSDAGYDRFVLYKEWGRDFLQRPGRQPQAGLSQANFTLGPVSRSYGGQYTCSGAYNLSSEWSAPSDPLDILITGQIRARPFLSVRPGPTVASGENVTLLCQSQGGMHTFLLTKEGAADSPLRLKSKRQSHKYQAEFPMSPVTSAHAGTYRCYGSLSSNPYLLTHPSDPLELVVSGAAETLSPPQNKSDSKAGE	Literature-reported	Inhibitory leukocyte immunoglobulin-like receptors: Immune checkpoint proteins and tumor sustaining factors. Cell Cycle. 2016;15(1):25-40.	.	.	.	.	.	.	.	.	.	.	.	hsa04380: Osteoclast differentiation; hsa04662: B cell receptor signaling pathway	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-6798695: Neutrophil degranulation	.	Q8N6C8
TT7WTBR	Leukocyte immunoglobulin-like receptor subfamily A member 4 (LILRA4)	P59901	LIRA4_HUMAN	.	CD85 antigen-like family member G; Immunoglobulin-like transcript 7; ILT-7; CD85g	LILRA4	"Functions coreceptor to limit the innate immune responses to viral infections; signaling occurs via FCER1G (PubMed:16735691, PubMed:19564354). Down-regulates the production of IFNA1, IFNA2, IFNA4, IFNB1 and TNF by plasmacytoid dendritic cells that have been exposed to influenza virus or cytidine-phosphate-guanosine (CpG) dinucleotides, indicating it functions as negative regulator of TLR7 and TLR9 signaling cascades (PubMed:16735691, PubMed:19564354, PubMed:24586760). Down-regulates interferon production in response to interaction with BST2 on HIV-1 infected cells (PubMed:26172439). Activates a signaling cascade in complex with FCER1G that results in phosphorylation of Src family and Syk kinases and thereby triggers mobilization of intracellular Ca(2+) (PubMed:16735691, PubMed:19564354). Does not interfere with the differentiation of plasmacytoid dendritic cells into antigen-presenting cells (PubMed:24586760). {ECO:0000269|PubMed:16735691, ECO:0000269|PubMed:19564354, ECO:0000269|PubMed:24586760, ECO:0000269|PubMed:26172439}."	.	.	MTLILTSLLFFGLSLGPRTRVQAENLLKPILWAEPGPVITWHNPVTIWCQGTLEAQGYRLDKEGNSMSRHILKTLESENKVKLSIPSMMWEHAGRYHCYYQSPAGWSEPSDPLELVVTAYSRPTLSALPSPVVTSGVNVTLRCASRLGLGRFTLIEEGDHRLSWTLNSHQHNHGKFQALFPMGPLTFSNRGTFRCYGYENNTPYVWSEPSDPLQLLVSGVSRKPSLLTLQGPVVTPGENLTLQCGSDVGYIRYTLYKEGADGLPQRPGRQPQAGLSQANFTLSPVSRSYGGQYRCYGAHNVSSEWSAPSDPLDILIAGQISDRPSLSVQPGPTVTSGEKVTLLCQSWDPMFTFLLTKEGAAHPPLRLRSMYGAHKYQAEFPMSPVTSAHAGTYRCYGSRSSNPYLLSHPSEPLELVVSGATETLNPAQKKSDSKTAPHLQDYTVENLIRMGVAGLVLLFLGILLFEAQHSQRSPPRCSQEANSRKDNAPFRVVEPWEQI	Clinical trial	Emerging drugs for the treatment of alopecia areata. Expert Opin Emerg Drugs. 2022 Dec;27(4):379-387.	.	.	.	.	.	.	.	.	.	.	.	hsa:23547	R-HSA-198933;	.	P59901;
TTIVYCQ	Leukocyte Ig-like receptor-5 (LILR5)	A6NI73; O75023	LIRA5_HUMAN; LIRB5_HUMAN	.	ILT-11	LILRA5	May play a role in triggering innate immune responses. Does not seem to play a role for any class I MHC antigen recognition.	.	.	MAPWSHPSAQLQPVGGDAVSPALMVLLCLGLSLGPRTHVQAGNLSKATLWAEPGSVISRGNSVTIRCQGTLEAQEYRLVKEGSPEPWDTQNPLEPKNKARFSIPSMTEHHAGRYRCYYYSPAGWSEPSDPLELVVTGFYNKPTLSALPSPVVTSGENVTLQCGSRLRFDRFILTEEGDHKLSWTLDSQLTPSGQFQALFPVGPVTPSHRWMLRCYGSRRHILQVWSEPSDLLEIPVSGAADNLSPSQNKSDSGTASHLQDYAVENLIRMGMAGLILVVLGILIFQDWHSQRSPQAAAGR	Literature-reported	Inhibitory leukocyte immunoglobulin-like receptors: Immune checkpoint proteins and tumor sustaining factors. Cell Cycle. 2016;15(1):25-40.	.	.	.	.	.	.	.	.	.	.	.	hsa04380: Osteoclast differentiation; hsa04662: B cell receptor signaling pathway	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	A6NI73
TTC0QRJ	Leukocyte immunoglobulin-like receptor subfamily B member 1 (LILRB1)	Q8NHL6	LIRB1_HUMAN	.	LIR-1; Leukocyte immunoglobulin-like receptor 1; CD85 antigen-like family member J; Immunoglobulin-like transcript 2; ILT-2; Monocyte/macrophage immunoglobulin-like receptor 7; MIR-7; CD85j	LILRB1	"Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles (PubMed:16455647, PubMed:28636952). Receptor for H301/UL18, a human cytomegalovirus class I MHC homolog. Ligand binding results in inhibitory signals and down-regulation of the immune response. Engagement of LILRB1 present on natural killer cells or T-cells by class I MHC molecules protects the target cells from lysis. Interaction with HLA-B or HLA-E leads to inhibition of FCER1A signaling and serotonin release. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions (PubMed:11907092, PubMed:9285411, PubMed:9842885). Recognizes HLA-G in complex with B2M/beta-2 microglobulin and a nonamer self-peptide (PubMed:16455647). Upon interaction with peptide-bound HLA-G-B2M complex, triggers secretion of growth-promoting factors by decidual NK cells (PubMed:29262349, PubMed:19304799). Reprograms B cells toward an immune suppressive phenotype (PubMed:24453251). {ECO:0000269|PubMed:11907092, ECO:0000269|PubMed:16455647, ECO:0000269|PubMed:19304799, ECO:0000269|PubMed:24453251, ECO:0000269|PubMed:28636952, ECO:0000269|PubMed:29262349, ECO:0000269|PubMed:9285411, ECO:0000269|PubMed:9842885}."	.	1G0X;1P7Q;1UFU;1UGN;1VDG;3D2U;4LL9;4NO0;5KNM;6AEE;6EWA;6EWC;6EWO;6K60;6ZDX;7KFK	MTPILTVLICLGLSLGPRTHVQAGHLPKPTLWAEPGSVITQGSPVTLRCQGGQETQEYRLYREKKTALWITRIPQELVKKGQFPIPSITWEHAGRYRCYYGSDTAGRSESSDPLELVVTGAYIKPTLSAQPSPVVNSGGNVILQCDSQVAFDGFSLCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPSRRWWYRCYAYDSNSPYEWSLPSDLLELLVLGVSKKPSLSVQPGPIVAPEETLTLQCGSDAGYNRFVLYKDGERDFLQLAGAQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSEWSAPSDPLDILIAGQFYDRVSLSVQPGPTVASGENVTLLCQSQGWMQTFLLTKEGAADDPWRLRSTYQSQKYQAEFPMGPVTSAHAGTYRCYGSQSSKPYLLTHPSDPLELVVSGPSGGPSSPTTGPTSTSGPEDQPLTPTGSDPQSGLGRHLGVVIGILVAVILLLLLLLLLFLILRHRRQGKHWTSTQRKADFQHPAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKHTQPEDGVEMDTRSPHDEDPQAVTYAEVKHSRPRREMASPPSPLSGEFLDTKDRQAEEDRQMDTEAAASEAPQDVTYAQLHSLTLRREATEPPPSQEGPSPAVPSIYATLAIH	Clinical trial	"Clinical pipeline report, company report or official report of Sanofi "	.	.	.	.	.	.	.	.	.	.	.	hsa:10859	R-HSA-198933;	.	Q8NHL6;
TTHC6XU	Leukocyte immunoglobulin-like receptor B2 (LILRB2)	Q8N423	LIRB2_HUMAN	.	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	LILRB2	"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."	.	.	MTPIVTVLICLGLSLGPRTHVQTGTIPKPTLWAEPDSVITQGSPVTLSCQGSLEAQEYRLYREKKSASWITRIRPELVKNGQFHIPSITWEHTGRYGCQYYSRARWSELSDPLVLVMTGAYPKPTLSAQPSPVVTSGGRVTLQCESQVAFGGFILCKEGEEEHPQCLNSQPHARGSSRAIFSVGPVSPNRRWSHRCYGYDLNSPYVWSSPSDLLELLVPGVSKKPSLSVQPGPVVAPGESLTLQCVSDVGYDRFVLYKEGERDLRQLPGRQPQAGLSQANFTLGPVSRSYGGQYRCYGAHNLSSECSAPSDPLDILITGQIRGTPFISVQPGPTVASGENVTLLCQSWRQFHTFLLTKAGAADAPLRLRSIHEYPKYQAEFPMSPVTSAHAGTYRCYGSLNSDPYLLSHPSEPLELVVSGPSMGSSPPPTGPISTPAGPEDQPLTPTGSDPQSGLGRHLGVVIGILVAVVLLLLLLLLLFLILRHRRQGKHWTSTQRKADFQHPAGAVGPEPTDRGLQWRSSPAADAQEENLYAAVKDTQPEDGVEMDTRAAASEAPQDVTYAQLHSLTLRRKATEPPPSQEREPPAEPSIYATLAIH	Clinical trial	National Cancer Institute Drug Dictionary (drug name MK4830).	.	.	.	.	.	.	.	.	.	.	.	hsa04380: Osteoclast differentiation; hsa04662: B cell receptor signaling pathway	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-6798695: Neutrophil degranulation	.	Q8N423
TTREOKA	Leukocyte immunoglobulin-like receptor B4 (LILRB4)	Q8NHJ6	LIRB4_HUMAN	.	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	LILRB4	"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."	.	.	MIPTFTALLCLGLSLGPRTHMQAGPLPKPTLWAEPGSVISWGNSVTIWCQGTLEAREYRLDKEESPAPWDRQNPLEPKNKARFSIPSMTEDYAGRYRCYYRSPVGWSQPSDPLELVMTGAYSKPTLSALPSPLVTSGKSVTLLCQSRSPMDTFLLIKERAAHPLLHLRSEHGAQQHQAEFPMSPVTSVHGGTYRCFSSHGFSHYLLSHPSDPLELIVSGSLEDPRPSPTRSVSTAAGPEDQPLMPTGSVPHSGLRRHWEVLIGVLVVSILLLSLLLFLLLQHWRQGKHRTLAQRQADFQRPPGAAEPEPKDGGLQRRSSPAADVQGENFCAAVKNTQPEDGVEMDTRQSPHDEDPQAVTYAKVKHSRPRREMASPPSPLSGEFLDTKDRQAEEDRQMDTEAAASEAPQDVTYAQLHSFTLRQKATEPPPSQEGASPAEPSVYATLAIH	Clinical trial	"Clinical pipeline report, company report or official report of Immune-Onc Therapeutics."	.	.	.	.	.	.	.	.	.	.	.	hsa04380: Osteoclast differentiation; hsa04662: B cell receptor signaling pathway	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	Q8NHJ6
TTWL9TY	LIM domain kinase-1 (LIMK-1)	P53667	LIMK1_HUMAN	Kinase	LIMK-1; LIMK	LIMK1	"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."	EC 2.7.11.1	5NXC; 5L6W; 5HVK; 5HVJ; 3S95	MRLTLLCCTWREERMGEEGSELPVCASCGQRIYDGQYLQALNADWHADCFRCCDCSASLSHQYYEKDGQLFCKKDYWARYGESCHGCSEQITKGLVMVAGELKYHPECFICLTCGTFIGDGDTYTLVEHSKLYCGHCYYQTVVTPVIEQILPDSPGSHLPHTVTLVSIPASSHGKRGLSVSIDPPHGPPGCGTEHSHTVRVQGVDPGCMSPDVKNSIHVGDRILEINGTPIRNVPLDEIDLLIQETSRLLQLTLEHDPHDTLGHGLGPETSPLSSPAYTPSGEAGSSARQKPVLRSCSIDRSPGAGSLGSPASQRKDLGRSESLRVVCRPHRIFRPSDLIHGEVLGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIKSMDSQYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKNVVVADFGLARLMVDEKTQPEGLRSLKKPDRKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADPDYLPRTMDFGLNVRGFLDRYCPPNCPPSFFPITVRCCDLDPEKRPSFVKLEHWLETLRMHLAGHLPLGPQLEQLDRGFWETYRRGESGLPAHPEVPD	Literature-reported	Pyridylthiazole-based ureas as inhibitors of Rho associated protein kinases (ROCK1 and 2). Medchemcomm. 2012 Jun 1;3(6):699-709.	0	EC:2.7	.	protein kinase superfamily. TKL Ser/Thr protein kinase family.	2.7.11.1	Transferring phosphorus-containing groups	LIM domain; PDZ domain; Protein tyrosine kinase	PF00412; PF00595; PF07714	PF00412; LIM; PF00595; PDZ; PF07714; Pkinase_Tyr	.	.	hsa04360: Axon guidance; hsa04666: Fc gamma R-mediated phagocytosis; hsa04810: Regulation of actin cytoskeleton; hsa05135: Yersinia infection; hsa05170: Human immunodeficiency virus 1 infection	R-HSA-2029482: Regulation of actin dynamics for phagocytic cup formation; R-HSA-3928662: EPHB-mediated forward signaling; R-HSA-399954: Sema3A PAK dependent Axon repulsion; R-HSA-416572: Sema4D induced cell migration and growth-cone collapse; R-HSA-5627117: RHO GTPases Activate ROCKs; R-HSA-5627123: RHO GTPases activate PAKs	.	P53667
TTASMD8	LIM domain kinase-2 (LIMK-2)	P53671	LIMK2_HUMAN	Kinase	LIMK-2; LIM domain kinase 2	LIMK2	Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro.	EC 2.7.11.1	5NXD; 4TPT; 1X6A	MSALAGEDVWRCPGCGDHIAPSQIWYRTVNETWHGSCFRCSECQDSLTNWYYEKDGKLYCPKDYWGKFGEFCHGCSLLMTGPFMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCHNEVVLAPMFERLSTESVQEQLPYSVTLISMPATTEGRRGFSVSVESACSNYATTVQVKEVNRMHISPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAISQTSQTLQLLIEHDPVSQRLDQLRLEARLAPHMQNAGHPHALSTLDTKENLEGTLRRRSLRRSNSISKSPGPSSPKEPLLFSRDISRSESLRCSSSYSQQIFRPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATTKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEALSLYLGELGIPLPAELEELDHTVSMQYGLTRDSPP	Literature-reported	Novel class of LIM-kinase 2 inhibitors for the treatment of ocular hypertension and associated glaucoma. J Med Chem. 2009 Nov 12;52(21):6515-8.	0	.	.	.	.	.	.	.	.	.	.	hsa04360: Axon guidance; hsa04666: Fc gamma R-mediated phagocytosis; hsa04810: Regulation of actin cytoskeleton; hsa05170: Human immunodeficiency virus 1 infection	R-HSA-3928662: EPHB-mediated forward signaling; R-HSA-416572: Sema4D induced cell migration and growth-cone collapse; R-HSA-5627117: RHO GTPases Activate ROCKs	.	P53671
TTO50LN	Zinc finger CCHC domain-containing 1 (Lin-28A)	Q9H9Z2	LN28A_HUMAN	.	Zinc finger CCHC domain-containing protein 1; ZCCHC1; Protein lin-28 homolog A; Lin-28A; LIN28; CSDD1	LIN28A	"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)."	.	5UDZ; 2LI8; 2CQF	MGSVSNQQFAGGCAKAAEEAPEEAPEDAARAADEPQLLHGAGICKWFNVRMGFGFLSMTARAGVALDPPVDVFVHQSKLHMEGFRSLKEGEAVEFTFKKSAKGLESIRVTGPGGVFCIGSERRPKGKSMQKRRSKGDRCYNCGGLDHHAKECKLPPQPKKCHFCQSISHMVASCPLKAQQGPSAQGKPTYFREEEEEIHSPTLLPEAQN	Literature-reported	Perturbation of MicroRNA-370/Lin-28 homolog A/nuclear factor kappa B regulatory circuit contributes to the development of hepatocellular carcinoma. Hepatology. 2013 Dec;58(6):1977-91.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-452723: Transcriptional regulation of pluripotent stem cells	.	Q9H9Z2
TTZYQ80	Leucine-rich repeat neuronal protein 1 (LINGO1)	Q96FE5	LIGO1_HUMAN	Immunoglobulin	Leucinerich repeat neuronal protein 6A; Leucinerich repeat and immunoglobulinlike domaincontaining nogo receptorinteracting protein 1; Leucinerich repeat and immunoglobulin domaincontaining protein 1; LINGO1	LINGO1	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}.	.	4OQT; 2ID5	MQVSKRMLAGGVRSMPSPLLACWQPILLLVLGSVLSGSATGCPPRCECSAQDRAVLCHRKRFVAVPEGIPTETRLLDLGKNRIKTLNQDEFASFPHLEELELNENIVSAVEPGAFNNLFNLRTLGLRSNRLKLIPLGVFTGLSNLTKLDISENKIVILLDYMFQDLYNLKSLEVGDNDLVYISHRAFSGLNSLEQLTLEKCNLTSIPTEALSHLHGLIVLRLRHLNINAIRDYSFKRLYRLKVLEISHWPYLDTMTPNCLYGLNLTSLSITHCNLTAVPYLAVRHLVYLRFLNLSYNPISTIEGSMLHELLRLQEIQLVGGQLAVVEPYAFRGLNYLRVLNVSGNQLTTLEESVFHSVGNLETLILDSNPLACDCRLLWVFRRRWRLNFNRQQPTCATPEFVQGKEFKDFPDVLLPNYFTCRRARIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHVRSYSPDWPHQPNKTFAFISNQPGEGEANSTRATVPFPFDIKTLIIATTMGFISFLGVVLFCLVLLFLWSRGKGNTKHNIEIEYVPRKSDAGISSADAPRKFNMKMI	Clinical trial	Randomized phase I trials of the safety/tolerability of anti-LINGO-1 monoclonal antibody BIIB033. Neurol Neuroimmunol Neuroinflamm. 2014 Aug 21;1(2):e18.	21	.	.	.	.	.	.	.	.	.	.	.	R-HSA-193634:Axonal growth inhibition (RHOA activation)	.	Q96FE5
TTS8T1M	Lysosomal acid lipase (LIPA)	P38571	LICH_HUMAN	Carboxylic ester hydrolase	Sterol esterase; Lysosomal acid lipase/cholesteryl ester hydrolase; Lipase A; LIPA; LAL; Cholesteryl esterase; Acid cholesteryl ester hydrolase	LIPA	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.	EC 3.1.1.13	.	MKMRFLGLVVCLVLWTLHSEGSGGKLTAVDPETNMNVSEIISYWGFPSEEYLVETEDGYILCLNRIPHGRKNHSDKGPKPVVFLQHGLLADSSNWVTNLANSSLGFILADAGFDVWMGNSRGNTWSRKHKTLSVSQDEFWAFSYDEMAKYDLPASINFILNKTGQEQVYYVGHSQGTTIGFIAFSQIPELAKRIKMFFALGPVASVAFCTSPMAKLGRLPDHLIKDLFGDKEFLPQSAFLKWLGTHVCTHVILKELCGNLCFLLCGFNERNLNMSRVDVYTTHSPAGTSVQNMLHWSQAVKFQKFQAFDWGSSAKNYFHYNQSYPPTYNVKDMLVPTAVWSGGHDWLADVYDVNILLTQITNLVFHESIPEWEHLDFIWGLDAPWRLYNKIINLMRKYQ	Successful	A Phase 3 Trial of Sebelipase Alfa in Lysosomal Acid Lipase Deficiency. N Engl J Med. 2015 Sep 10;373(11):1010-20.	34	.	.	.	.	.	.	.	.	.	.	hsa00100:Steroid biosynthesis; hsa04142:Lysosome	R-HSA-8964038: LDL clearance	.	P38571
TTLUQ8E	Hormone sensitive lipase (LIPE)	Q05469	LIPS_HUMAN	Carboxylic ester hydrolase	Hormone-sensitive lipase; HSL	LIPE	"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."	EC 3.1.1.79	.	MEPGSKSVSRSDWQPEPHQRPITPLEPGPEKTPIAQPESKTLQGSNTQQKPASNQRPLTQQETPAQHDAESQKEPRAQQKSASQEEFLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLGKESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGAKREPSAPTESTSQETPEQSDKQTTPVQGAKSKQGSLTELGFLTKLQELSIQRSALEWKALSEWVTDSESESDVGSSSDTDSPATMGGMVAQGVKLGFKGKSGYKVMSGYSGTSPHEKTSARNHRHYQDTASRLIHNMDLRTMTQSLVTLAEDNIAFFSSQGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAHLFDLDPETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALTQLRALVYYAQRLLVTNRPGVLFFEGDEGLTADFLREYVTLHKGCFYGRCLGFQFTPAIRPFLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWKAFWNITEMEVLSSLANMASATVRVSRLLSLPPEAFEMPLTADPTLTVTISPPLAHTGPGPVLVRLISYDLREGQDSEELSSLIKSNGQRSLELWPRPQQAPRSRSLIVHFHGGGFVAQTSRSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGSTGERICLAGDSAGGNLCFTVALRAAAYGVRVPDGIMAAYPATMLQPAASPSRLLSLMDPLLPLSVLSKCVSAYAGAKTEDHSNSDQKALGMMGLVRRDTALLLRDFRLGASSWLNSFLELSGRKSQKMSEPIAEPMRRSVSEAALAQPQGPLGTDSLKNLTLRDLSLRGNSETSSDTPEMSLSAETLSPSTPSDVNFLLPPEDAGEEAEAKNELSPMDRGLGVRAAFPEGFHPRRSSQGATQMPLYSSPIVKNPFMSPLLAPDSMLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVEDLPHGFLTLAALCRETRQAAELCVERIRLVLTPPAGAGPSGETGAAGVDGGCGGRH	Successful	The ChEMBL database in 2017. Nucleic Acids Res. 2017 Jan 4;45(D1):D945-D954.	34	EC:3.1.1	Carboxylic ester hydrolase	'GDXG' lipolytic enzyme family.	3.1.1.79	Acting on ester bonds	alpha/beta hydrolase fold; Hormone-sensitive lipase (HSL) N-terminus	PF07859; PF06350	PF07859; Abhydrolase_3; PF06350; HSL_N	.	.	hsa04024:cAMP signaling pathway; hsa04152:AMPK signaling pathway; hsa04910:Insulin signaling pathway	R-HSA-163560:Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis	MetaCyc:HS01328-MON	Q05469
TTKYZA9	Gastric triacylglycerol lipase (LIPF)	P07098	LIPG_HUMAN	Carboxylic ester hydrolase	Gastric lipase; GL	LIPF	"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,"	EC 3.1.1.3	1HLG	MWLLLTMASLISVLGTTHGLFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFIAFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQFLATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSPVQNRMHYDQSQPPYYNVTAMNVPIAVWNGGKDLLADPQDVGLLLPKLPNLIYHKEIPFYNHLDFIWAMDAPQEVYNDIVSMISEDKK	Clinical trial	"Cetilistat (ATL-962), a novel lipase inhibitor: a 12-week randomized, placebo-controlled study of weight reduction in obese patients. Int J Obes (Lond). 2007 Mar;31(3):494-9."	25	.	.	.	.	.	.	.	.	.	.	hsa00561:Glycerolipid metabolism; hsa01100:Metabolic pathways; hsa04975:Fat digestion and absorption	R-HSA-192456: Digestion of dietary lipid	.	P07098
TTHSZXO	Endothelial lipase (LIPG)	Q9Y5X9	LIPE_HUMAN	.	Endothelial cell-derived lipase; EL; EDL	LIPG	Has phospholipase and triglyceride lipase activities. Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins. Binds heparin.	EC 3.1.1.3	.	MSNSVPLLCFWSLCYCFAAGSPVPFGPEGRLEDKLHKPKATQTEVKPSVRFNLRTSKDPEHEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVVVDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGNFVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTRSFGLSIGIQMPVGHIDIYPNGGDFQPGCGLNDVLGSIAYGTITEVVKCEHERAVHLFVDSLVNQDKPSFAFQCTDSNRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKNMGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGASQSWYNLWKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWFRKCRDGWRMKNETSPTVELP	Clinical trial	"Discovery of potent, selective sulfonylfuran urea endothelial lipase inhibitors. Bioorg Med Chem Lett. 2009 Jan 1;19(1):27-30."	16	.	.	.	.	.	.	.	.	.	.	hsa00561: Glycerolipid metabolism; hsa01100: Metabolic pathways; hsa04979: Cholesterol metabolism	R-HSA-8964058: HDL remodeling	.	Q9Y5X9
TTFX379	Rhombotin-2 (LMO2)	P25791	RBTN2_HUMAN	.	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	LMO2	Acts with LDB1 to maintain erythroid precursors in an immature state. Acts with TAL1/SCL to regulate red blood cell development.	.	4KFZ; 2YPA; 2XJZ; 2XJY	MSSAIERKSLDPSEEPVDEVLQIPPSLLTCGGCQQNIGDRYFLKAIDQYWHEDCLSCDLCGCRLGEVGRRLYYKLGRKLCRRDYLRLFGQDGLCASCDKRIRAYEMTMRVKDKVYHLECFKCAACQKHFCVGDRYLLINSDIVCEQDIYEWTKINGMI	Literature-reported	The LIM-domain protein Lmo2 is a key regulator of tumour angiogenesis: a new anti-angiogenesis drug target. Oncogene. 2002 Feb 21;21(9):1309-15.	.	.	.	.	.	.	LIM domain	PF00412	PF00412; LIM	.	.	hsa05202: Transcriptional misregulation in cancer	R-HSA-8939236: RUNX1 regulates transcription of genes involved in differentiation of HSCs	.	P25791
TTY2KP7	Leucyl-cysteinyl aminopeptidase (LNPEP)	Q9UIQ6	LCAP_HUMAN	Peptidase	Placental leucine aminopeptidase; P-LAP; Oxytocinase; OTase; Leucyl-cystinyl aminopeptidase; Insulin-responsive aminopeptidase; Insulin-regulated membrane aminopeptidase; IRAP; Cystinyl aminopeptidase	LNPEP	"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."	EC 3.4.11.3	5MJ6; 5JHQ; 5C97; 4Z7I; 4PJ6	MEPFTNDRLQLPRNMIENSMFEEEPDVVDLAKEPCLHPLEPDEVEYEPRGSRLLVRGLGEHEMEEDEEDYESSAKLLGMSFMNRSSGLRNSATGYRQSPDGACSVPSARTMVVCAFVIVVAVSVIMVIYLLPRCTFTKEGCHKKNQSIGLIQPFATNGKLFPWAQIRLPTAVVPLRYELSLHPNLTSMTFRGSVTISVQALQVTWNIILHSTGHNISRVTFMSAVSSQEKQAEILEYAYHGQIAIVAPEALLAGHNYTLKIEYSANISSSYYGFYGFSYTDESNEKKYFAATQFEPLAARSAFPCFDEPAFKATFIIKIIRDEQYTALSNMPKKSSVVLDDGLVQDEFSESVKMSTYLVAFIVGEMKNLSQDVNGTLVSIYAVPEKIGQVHYALETTVKLLEFFQNYFEIQYPLKKLDLVAIPDFEAGAMENWGLLTFREETLLYDSNTSSMADRKLVTKIIAHELAHQWFGNLVTMKWWNDLWLNEGFATFMEYFSLEKIFKELSSYEDFLDARFKTMKKDSLNSSHPISSSVQSSEQIEEMFDSLSYFKGSSLLLMLKTYLSEDVFQHAVVLYLHNHSYASIQSDDLWDSFNEVTNQTLDVKRMMKTWTLQKGFPLVTVQKKGKELFIQQERFFLNMKPEIQPSDTSYLWHIPLSYVTEGRNYSKYQSVSLLDKKSGVINLTEEVLWVKVNINMNGYYIVHYADDDWEALIHQLKINPYVLSDKDRANLINNIFELAGLGKVPLKRAFDLINYLGNENHTAPITEALFQTDLIYNLLEKLGYMDLASRLVTRVFKLLQNQIQQQTWTDEGTPSMRELRSALLEFACTHNLGNCSTTAMKLFDDWMASNGTQSLPTDVMTTVFKVGAKTDKGWSFLLGKYISIGSEAEKNKILEALASSEDVRKLYWLMKSSLNGDNFRTQKLSFIIRTVGRHFPGHLLAWDFVKENWNKLVQKFPLGSYTIQNIVAGSTYLFSTKTHLSEVQAFFENQSEATFRLRCVQEALEVIQLNIQWMEKNLKSLTWWL	Patented-recorded	Potent macrocyclic inhibitors of insulin-regulated aminopeptidase (IRAP) by olefin ring-closing metathesis. J Med Chem. 2011 Jun 9;54(11):3779-92.	0	EC:3.4	.	peptidase M1 family.	3.4.11.3	Acting on peptide bonds (peptidases)	ERAP1-like C-terminal domain; Peptidase family M1 domain	PF11838; PF01433	PF11838; ERAP1_C; PF01433; Peptidase_M1	.	.	hsa04614: Renin-angiotensin system	R-HSA-1236977: Endosomal/Vacuolar pathway; R-HSA-1445148: Translocation of SLC2A4 (GLUT4) to the plasma membrane; R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	Q9UIQ6
TTM1VPZ	ATP-dependent protease Lon (LONP1)	P36776	LONM_HUMAN	Peptidase	Serine protease 15; Mitochondrial ATP-dependent protease Lon; Lon protease-like protein; LONP1; LONP; LONHs	LONP1	"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."	EC 3.4.21.53	2X36	MAASTGYVRLWGAARCWVLRRPMLAAAGGRVPTAAGAWLLRGQRTCDASPPWALWGRGPAIGGQWRGFWEASSRGGGAFSGGEDASEGGAEEGAGGAGGSAGAGEGPVITALTPMTIPDVFPHLPLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDVVESLDEIYHTGTFAQIHEMQDLGDKLRMIVMGHRRVHISRQLEVEPEEPEAENKHKPRRKSKRGKKEAEDELSARHPAELAMEPTPELPAEVLMVEVENVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPQDKDAKGDKDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFPDEQAEALAVER	Literature-reported	Inhibition of LONP1 Suppresses Pancreatic Cancer Progression Via c-Jun N-Terminal Kinase Pathway-Meditated Epithelial-Mesenchymal Transition. Pancreas. 2019 May/Jun;48(5):629-635.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P36776
TTQHNAM	HUMAN lysyl oxidase (LOX)	P28300	LYOX_HUMAN	CH-NH(2) donor oxidoreductase	Protein-lysine 6-oxidase	LOX	"Human protein lysyl oxidase interacts with SARS-CoV-2 Orf8 protein with high significance, which indicates LOX as a potential therapeutic target."	EC 1.4.3.13	.	MRFAWTVLLLGPLQLCALVHCAPPAAGQQQPPREPPAAPGAWRQQIQWENNGQVFSLLSLGSQYQPQRRRDPGAAVPGAANASAQQPRTPILLIRDNRTAAARTRTAGSSGVTAGRPRPTARHWFQAGYSTSRAREAGASRAENQTAPGEVPALSNLRPPSRVDGMVGDDPYNPYKYSDDNPYYNYYDTYERPRPGGRYRPGYGTGYFQYGLPDLVADPYYIQASTYVQKMSMYNLRCAAEENCLASTAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDANTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYGADIDCQWIDITDVKPGNYILKVSVNPSYLVPESDYTNNVVRCDIRYTGHHAYASGCTISPY	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1566948: Elastic fibre formation; R-HSA-2243919: Crosslinking of collagen fibrils	.	P28300
TT4E26T	Lysyl oxidase (LOX)	P28300	LYOX_HUMAN	CH-NH(2) donor oxidoreductase	Protein-lysine 6-oxidase	LOX	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.	EC 1.4.3.13	.	MRFAWTVLLLGPLQLCALVHCAPPAAGQQQPPREPPAAPGAWRQQIQWENNGQVFSLLSLGSQYQPQRRRDPGAAVPGAANASAQQPRTPILLIRDNRTAAARTRTAGSSGVTAGRPRPTARHWFQAGYSTSRAREAGASRAENQTAPGEVPALSNLRPPSRVDGMVGDDPYNPYKYSDDNPYYNYYDTYERPRPGGRYRPGYGTGYFQYGLPDLVADPYYIQASTYVQKMSMYNLRCAAEENCLASTAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDANTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYGADIDCQWIDITDVKPGNYILKVSVNPSYLVPESDYTNNVVRCDIRYTGHHAYASGCTISPY	Literature-reported	Connective tissue growth factor: potential role in glomerulosclerosis and tubulointerstitial fibrosis. Kidney Int. 2000 Oct;58(4):1389-99.	.	EC:1.4	Oxidoreductases acting on CH-NH2 group of donors	lysyl oxidase family.	1.4.3.13 	Acting on the CH-NH2 group of donors	Lysyl oxidase 	PF01186	PF01186; Lysyl_oxidase	.	.	.	R-HSA-1566948: Elastic fibre formation; R-HSA-2243919: Crosslinking of collagen fibrils	.	P28300
TTFSUHX	Lysyl oxidase homolog 2 (LOXL2)	Q9Y4K0	LOXL2_HUMAN	.	Lysyl oxidaserelated protein WS914; Lysyl oxidaserelated protein 2; Lysyl oxidaselike protein 2; LOXL2	LOXL2	"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."	EC 1.4.3.13	5ZE3	MERPLCSHLCSCLAMLALLSPLSLAQYDSWPHYPEYFQQPAPEYHQPQAPANVAKIQLRLAGQKRKHSEGRVEVYYDGQWGTVCDDDFSIHAAHVVCRELGYVEAKSWTASSSYGKGEGPIWLDNLHCTGNEATLAACTSNGWGVTDCKHTEDVGVVCSDKRIPGFKFDNSLINQIENLNIQVEDIRIRAILSTYRKRTPVMEGYVEVKEGKTWKQICDKHWTAKNSRVVCGMFGFPGERTYNTKVYKMFASRRKQRYWPFSMDCTGTEAHISSCKLGPQVSLDPMKNVTCENGLPAVVSCVPGQVFSPDGPSRFRKAYKPEQPLVRLRGGAYIGEGRVEVLKNGEWGTVCDDKWDLVSASVVCRELGFGSAKEAVTGSRLGQGIGPIHLNEIQCTGNEKSIIDCKFNAESQGCNHEEDAGVRCNTPAMGLQKKLRLNGGRNPYEGRVEVLVERNGSLVWGMVCGQNWGIVEAMVVCRQLGLGFASNAFQETWYWHGDVNSNKVVMSGVKCSGTELSLAHCRHDGEDVACPQGGVQYGAGVACSETAPDLVLNAEMVQQTTYLEDRPMFMLQCAMEENCLSASAAQTDPTTGYRRLLRFSSQIHNNGQSDFRPKNGRHAWIWHDCHRHYHSMEVFTHYDLLNLNGTKVAEGHKASFCLEDTECEGDIQKNYECANFGDQGITMGCWDMYRHDIDCQWVDITDVPPGDYLFQVVINPNFEVAESDYSNNIMKCRSRYDGHRIWMYNCHIGGSFSEETEKKFEHFSGLLNNQLSPQ	Clinical trial	National Cancer Institute Drug Dictionary (drug id 681814).	21	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1566948: Elastic fibre formation; R-HSA-2243919: Crosslinking of collagen fibrils	.	Q9Y4K0
TTU9LGY	Apolipoprotein A messenger RNA (LPA mRNA)	P08519	APOA_HUMAN	mRNA target	Lp(a) (mRNA); Apolipoprotein(a) (mRNA); Apo(a) (mRNA)	LPA	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)).	EC 3.4.21.-	4KIV; 4BVW; 4BVV; 4BVD; 4BVC	MEHKEVVLLLLLFLKSAAPEQSHVVQDCYHGDGQSYRGTYSTTVTGRTCQAWSSMTPHQHNRTTENYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDPVAAPYCYTRDPSVRWEYCNLTQCSDAEGTAVAPPTITPIPSLEAPSEQAPTEQRPGVQECYHGNGQSYQGTYFITVTGRTCQAWSSMTPHSHSRTPAYYPNAGLIKNYCRNPDPVAAPWCYTTDPSVRWEYCNLTRCSDAEWTAFVPPNVILAPSLEAFFEQALTEETPGVQDCYYHYGQSYRGTYSTTVTGRTCQAWSSMTPHQHSRTPENYPNAGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTQCLVTESSVLATLTVVPDPSTEASSEEAPTEQSPGVQDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEISPWCYTMDPNVRWEYCNLTQCPVTESSVLATSTAVSEQAPTEQSPTVQDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTQCPVMESTLLTTPTVVPVPSTELPSEEAPTENSTGVQDCYRGDGQSYRGTLSTTITGRTCQSWSSMTPHWHRRIPLYYPNAGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTRCPVTESSVLTTPTVAPVPSTEAPSEQAPPEKSPVVQDCYHGDGRSYRGISSTTVTGRTCQSWSSMIPHWHQRTPENYPNAGLTENYCRNPDSGKQPWCYTTDPCVRWEYCNLTQCSETESGVLETPTVVPVPSMEAHSEAAPTEQTPVVRQCYHGNGQSYRGTFSTTVTGRTCQSWSSMTPHRHQRTPENYPNDGLTMNYCRNPDADTGPWCFTMDPSIRWEYCNLTRCSDTEGTVVAPPTVIQVPSLGPPSEQDCMFGNGKGYRGKKATTVTGTPCQEWAAQEPHRHSTFIPGTNKWAGLEKNYCRNPDGDINGPWCYTMNPRKLFDYCDIPLCASSSFDCGKPQVEPKKCPGSIVGGCVAHPHSWPWQVSLRTRFGKHFCGGTLISPEWVLTAAHCLKKSSRPSSYKVILGAHQEVNLESHVQEIEVSRLFLEPTQADIALLKLSRPAVITDKVMPACLPSPDYMVTARTECYITGWGETQGTFGTGLLKEAQLLVIENEVCNHYKYICAEHLARGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYARVSRFVTWIEGMMRNN	Clinical trial	"Clinical pipeline report, company report or official report of ISIS Pharmaceuticals."	21	mRNA	mRNA target	.	.	.	Kringle domain; Trypsin	PF00051; PF00089	PF00051; Kringle; PF00089; Trypsin	.	.	.	R-HSA-171052:LDL-mediated lipid transport	.	.
TTGUMYS	Apolipoprotein(a) (LPA)	P08519	APOA_HUMAN	Apolipoprotein	Lp(a); Lipoprotein(a); LPA; Apo(a)	LPA	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.	EC 3.4.21.-	4KIV; 4BVW; 4BVV; 4BVD; 4BVC	MEHKEVVLLLLLFLKSAAPEQSHVVQDCYHGDGQSYRGTYSTTVTGRTCQAWSSMTPHQHNRTTENYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQCSDAEGTAVAPPTVTPVPSLEAPSEQAPTEQRPGVQECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDPVAAPYCYTRDPSVRWEYCNLTQCSDAEGTAVAPPTITPIPSLEAPSEQAPTEQRPGVQECYHGNGQSYQGTYFITVTGRTCQAWSSMTPHSHSRTPAYYPNAGLIKNYCRNPDPVAAPWCYTTDPSVRWEYCNLTRCSDAEWTAFVPPNVILAPSLEAFFEQALTEETPGVQDCYYHYGQSYRGTYSTTVTGRTCQAWSSMTPHQHSRTPENYPNAGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTQCLVTESSVLATLTVVPDPSTEASSEEAPTEQSPGVQDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEISPWCYTMDPNVRWEYCNLTQCPVTESSVLATSTAVSEQAPTEQSPTVQDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTQCPVMESTLLTTPTVVPVPSTELPSEEAPTENSTGVQDCYRGDGQSYRGTLSTTITGRTCQSWSSMTPHWHRRIPLYYPNAGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTRCPVTESSVLTTPTVAPVPSTEAPSEQAPPEKSPVVQDCYHGDGRSYRGISSTTVTGRTCQSWSSMIPHWHQRTPENYPNAGLTENYCRNPDSGKQPWCYTTDPCVRWEYCNLTQCSETESGVLETPTVVPVPSMEAHSEAAPTEQTPVVRQCYHGNGQSYRGTFSTTVTGRTCQSWSSMTPHRHQRTPENYPNDGLTMNYCRNPDADTGPWCFTMDPSIRWEYCNLTRCSDTEGTVVAPPTVIQVPSLGPPSEQDCMFGNGKGYRGKKATTVTGTPCQEWAAQEPHRHSTFIPGTNKWAGLEKNYCRNPDGDINGPWCYTMNPRKLFDYCDIPLCASSSFDCGKPQVEPKKCPGSIVGGCVAHPHSWPWQVSLRTRFGKHFCGGTLISPEWVLTAAHCLKKSSRPSSYKVILGAHQEVNLESHVQEIEVSRLFLEPTQADIALLKLSRPAVITDKVMPACLPSPDYMVTARTECYITGWGETQGTFGTGLLKEAQLLVIENEVCNHYKYICAEHLARGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYARVSRFVTWIEGMMRNN	Clinical trial	"Targeted antivascular therapy with the apolipoprotein(a) kringle V, rhLK8, inhibits the growth and metastasis of human prostate cancer in an orthotopic nude mouse model. Neoplasia. 2012 Apr;14(4):335-43."	17	.	.	.	.	.	.	.	.	.	.	.	R-HSA-171052:LDL-mediated lipid transport	.	.
TTQ6S1K	Lysophosphatidic acid receptor 1 (LPAR1)	Q92633	LPAR1_HUMAN	GPCR rhodopsin	Lysophosphatidic acid receptor Edg-2; LPA1; LPA-1; LPA receptor 1; EDG2; EDG 2 receptor	LPAR1	"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)."	.	4Z36; 4Z35; 4Z34	MAAISTSIPVISQPQFTAMNEPQCFYNESIAFFYNRSGKHLATEWNTVSKLVMGLGITVCIFIMLANLLVMVAIYVNRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVSTWLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVVIWTMAIVMGAIPSVGWNCICDIENCSNMAPLYSDSYLVFWAIFNLVTFVVMVVLYAHIFGYVRQRTMRMSRHSSGPRRNRDTMMSLLKTVVIVLGAFIICWTPGLVLLLLDVCCPQCDVLAYEKFFLLLAEFNSAMNPIIYSYRDKEMSATFRQILCCQRSENPTGPTEGSDRSASSLNHTILAGVHSNDHSVV	Clinical trial	Promising Pharmacological Directions in the World of Lysophosphatidic Acid Signaling. Biomol Ther (Seoul) 2015 January; 23(1): 1-11.	21	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04015:Rap1 signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa04540:Gap junction; hsa05200:Pathways in cancer	R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events; R-HSA-419408:Lysosphingolipid and LPA receptors	.	Q92633
TTB7Y8I	Lysophosphatidic acid receptor 2 (LPAR2)	Q9HBW0	LPAR2_HUMAN	GPCR rhodopsin	Lysophosphatidic acid receptor Edg-4; LPA2; LPA-2; LPA receptor 2; EDG4	LPAR2	"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."	.	4P0C	MVIMGQCYYNETIGFFYNNSGKELSSHWRPKDVVVVALGLTVSVLVLLTNLLVIAAIASNRRFHQPIYYLLGNLAAADLFAGVAYLFLMFHTGPRTARLSLEGWFLRQGLLDTSLTASVATLLAIAVERHRSVMAVQLHSRLPRGRVVMLIVGVWVAALGLGLLPAHSWHCLCALDRCSRMAPLLSRSYLAVWALSSLLVFLLMVAVYTRIFFYVRRRVQRMAEHVSCHPRYRETTLSLVKTVVIILGAFVVCWTPGQVVLLLDGLGCESCNVLAVEKYFLLLAEANSLVNAAVYSCRDAEMRRTFRRLLCCACLRQSTRESVHYTSSAQGGASTRIMLPENGHPLMDSTL	Literature-reported	LPA and its analogs-attractive tools for elucidation of LPA biology and drug development. Curr Med Chem. 2008;15(21):2122-31.	0	PF00001	.	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.2.5	The G-protein-coupled receptor (GPCR) Family	.	R-HSA-416476: G alpha (q) signalling events; R-HSA-418594: G alpha (i) signalling events; R-HSA-419408: Lysosphingolipid and LPA receptors	.	Q9HBW0
TTE2YJR	Lysophosphatidate-3 receptor (LPAR3)	Q9UBY5	LPAR3_HUMAN	GPCR rhodopsin	Lysophosphatidic acid receptor Edg7; Lysophosphatidic acid receptor 3; LPAR3; LPA3; LPA receptor 3	LPAR3	"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."	.	.	MNECHYDKHMDFFYNRSNTDTVDDWTGTKLVIVLCVGTFFCLFIFFSNSLVIAAVIKNRKFHFPFYYLLANLAAADFFAGIAYVFLMFNTGPVSKTLTVNRWFLRQGLLDSSLTASLTNLLVIAVERHMSIMRMRVHSNLTKKRVTLLILLVWAIAIFMGAVPTLGWNCLCNISACSSLAPIYSRSYLVFWTVSNLMAFLIMVVVYLRIYVYVKRKTNVLSPHTSGSISRRRTPMKLMKTVMTVLGAFVVCWTPGLVVLLLDGLNCRQCGVQHVKRWFLLLALLNSVVNPIIYSYKDEDMYGTMKKMICCFSQENPERRPSRIPSTVLSRSDTGSQYIEDSISQGAVCNKSTS	Clinical trial	Promising Pharmacological Directions in the World of Lysophosphatidic Acid Signaling. Biomol Ther (Seoul) 2015 January; 23(1): 1-11.	21	.	.	.	.	.	.	.	.	.	.	hsa04015:Rap1 signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04151:PI3K-Akt signaling pathway; hsa05200:Pathways in cancer	R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events; R-HSA-419408:Lysosphingolipid and LPA receptors	.	Q9UBY5
TT7ZMY4	Lysophosphatidic acid receptor 4 (LPAR4)	Q99677	LPAR4_HUMAN	.	Purinergic receptor 9; P2Y9; P2Y5-like receptor; P2Y purinoceptor 9; P2RY9; LPA4; LPA-4; LPA receptor 4; GPR23; G-protein coupled receptor 23	LPAR4	"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."	.	.	MGDRRFIDFQFQDSNSSLRPRLGNATANNTCIVDDSFKYNLNGAVYSVVFILGLITNSVSLFVFCFRMKMRSETAIFITNLAVSDLLFVCTLPFKIFYNFNRHWPFGDTLCKISGTAFLTNIYGSMLFLTCISVDRFLAIVYPFRSRTIRTRRNSAIVCAGVWILVLSGGISASLFSTTNVNNATTTCFEGFSKRVWKTYLSKITIFIEVVGFIIPLILNVSCSSVVLRTLRKPATLSQIGTNKKKVLKMITVHMAVFVVCFVPYNSVLFLYALVRSQAITNCFLERFAKIMYPITLCLATLNCCFDPFIYYFTLESFQKSFYINAHIRMESLFKTETPLTTKPSLPAIQEEVSDQTTNNGGELMLESTF	Literature-reported	"Identification of p2y9/GPR23 as a novel G protein-coupled receptor for lysophosphatidic acid, structurally distant from the Edg family. J Biol Chem. 2003 Jul 11;278(28):25600-6."	0	.	.	.	.	.	.	.	.	.	.	hsa04015: Rap1 signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04080: Neuroactive ligand-receptor interaction; hsa04151: PI3K-Akt signaling pathway; hsa04810: Regulation of actin cytoskeleton; hsa05130: Pathogenic Escherichia coli infection; hsa05200: Pathways in cancer	R-HSA-416476: G alpha (q) signalling events; R-HSA-417957: P2Y receptors	.	Q99677
TTABCJ6	Lysophosphatidic acid receptor 5 (LPAR5)	Q9H1C0	LPAR5_HUMAN	.	LPA-5; LPA receptor 5; GPR93; GPR92; G-protein coupled receptor 93; G-protein coupled receptor 92	LPAR5	"Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities."	.	.	MLANSSSTNSSVLPCPDYRPTHRLHLVVYSLVLAAGLPLNALALWVFLRALRVHSVVSVYMCNLAASDLLFTLSLPVRLSYYALHHWPFPDLLCQTTGAIFQMNMYGSCIFLMLINVDRYAAIVHPLRLRHLRRPRVARLLCLGVWALILVFAVPAARVHRPSRCRYRDLEVRLCFESFSDELWKGRLLPLVLLAEALGFLLPLAAVVYSSGRVFWTLARPDATQSQRRRKTVRLLLANLVIFLLCFVPYNSTLAVYGLLRSKLVAASVPARDRVRGVLMVMVLLAGANCVLDPLVYYFSAEGFRNTLRGLGTPHRARTSATNGTRAALAQSERSAVTTDATRPDAASQGLLRPSDSHSLSSFTQCPQDSAL	Literature-reported	Identification of farnesyl pyrophosphate and N-arachidonylglycine as endogenous ligands for GPR92. J Biol Chem. 2008 Jul 25;283(30):21054-64.	0	.	.	.	.	.	.	.	.	.	.	hsa04015: Rap1 signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04810: Regulation of actin cytoskeleton; hsa05130: Pathogenic Escherichia coli infection; hsa05200: Pathways in cancer	R-HSA-416476: G alpha (q) signalling events; R-HSA-418594: G alpha (i) signalling events; R-HSA-419408: Lysosphingolipid and LPA receptors	.	Q9H1C0
TTZDAGB	Lysophosphatidic acid receptor 6 (LPAR6)	P43657	LPAR6_HUMAN	.	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	LPAR6	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.	.	.	MVSVNSSHCFYNDSFKYTLYGCMFSMVFVLGLISNCVAIYIFICVLKVRNETTTYMINLAMSDLLFVFTLPFRIFYFTTRNWPFGDLLCKISVMLFYTNMYGSILFLTCISVDRFLAIVYPFKSKTLRTKRNAKIVCTGVWLTVIGGSAPAVFVQSTHSQGNNASEACFENFPEATWKTYLSRIVIFIEIVGFFIPLILNVTCSSMVLKTLTKPVTLSRSKINKTKVLKMIFVHLIIFCFCFVPYNINLILYSLVRTQTFVNCSVVAAVRTMYPITLCIAVSNCCFDPIVYYFTSDTIQNSIKMKNWSVRRSDFRFSEVHGAENFIQHNLQTLKSKIFDNESAA	Literature-reported	G protein-coupled receptor P2Y5 and its ligand LPA are involved in maintenance of human hair growth. Nat Genet. 2008 Mar;40(3):329-34.	0	.	.	.	.	.	.	.	.	.	.	hsa04072: Phospholipase D signaling pathway; hsa04080: Neuroactive ligand-receptor interaction; hsa04151: PI3K-Akt signaling pathway; hsa05200: Pathways in cancer	R-HSA-416476: G alpha (q) signalling events; R-HSA-417957: P2Y receptors	.	P43657
TTPOI4B	Acetyl-CoA:lyso-PAF acetyltransferase (PCAT)	Q8NF37; Q7L5N7	PCAT1_HUMAN; PCAT2_HUMAN	.	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	LPCAT1	"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. "	.	.	MRLRGCGPRAAPASSAGASDARLLAPPGRNPFVHELRLSALQKAQVALMTLTLFPVRLLVAAAMMLLAWPLALVASLGSAEKEPEQPPALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPNKLDTITWTWQGPGALEILWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAEALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPEKLEKDLDRYSERARMKGGEKIGIAEFAASLEVPVSDLLEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELTVTDLFRAIDQEEKGKITFADFHRFAEMYPAFAEEYLYPDQTHFESCAETSPAPIPNGFCADFSPENSDAGRKPVRKKLD	Successful	Modulation by flavonoids of PAF and related phospholipids in endothelial cells during oxidative stress. J Lipid Res. 2003 Feb;44(2):380-7.	34	.	.	.	.	.	.	.	.	.	.	hsa00564: Glycerophospholipid metabolism; hsa00565: Ether lipid metabolism; hsa01100: Metabolic pathways	R-HSA-1482788: Acyl chain remodelling of PC; R-HSA-1482925: Acyl chain remodelling of PG; R-HSA-1483166: Synthesis of PA; R-HSA-1483191: Synthesis of PC; R-HSA-6798695: Neutrophil degranulation	.	Q8NF37
TTOF3WZ	Lipoprotein lipase (LPL)	P06858	LIPL_HUMAN	Carboxylic ester hydrolase	LIPD	LPL	"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."	EC 3.1.1.34	6OB0; 6OAZ; 6OAU; 6E7K	MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG	Successful	Effects of clofibrate treatment in laying hens. Poult Sci. 2007 Jun;86(6):1187-95.	34	EC:3.1.1	Carboxylic ester hydrolase	AB hydrolase superfamily. Lipase family.	3.1.1.34 	Acting on ester bonds	Lipase; PLAT/LH2 domain	PF00151; PF01477	PF00151; Lipase; PF01477; PLAT	.	.	hsa00561:Glycerolipid metabolism; hsa03320:PPAR signaling pathway; hsa05010:Alzheimer's disease	R-HSA-174800:Chylomicron-mediated lipid transport; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-975634:Retinoid metabolism and transport	.	P06858
TTF2V7I	Apolipoprotein E receptor (LRP1)	Q07954	LRP1_HUMAN	.	Prolow-density lipoprotein receptor-related protein 1; LRP-1; CD91; APR; APOER	LRP1	"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."	.	2KNY; 2KNX; 2FYL; 2FYJ; 1J8E	MLTPPLLLLLPLLSALVAAAIDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCQPNEHNCLGTELCVPMSRLCNGVQDCMDGSDEGPHCRELQGNCSRLGCQHHCVPTLDGPTCYCNSSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFICGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPGLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDIDDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAMGKVFFTDYGQIPKVERCDMDGQNRTKLVDSKIVFPHGITLDLVSRLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFENYLYATNSDNANAQQKTSVIRVNRFNSTEYQVVTRVDKGGALHIYHQRRQPRVRSHACENDQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCKKPEHELFLVYGKGRPGIIRGMDMGAKVPDEHMIPIENLMNPRALDFHAETGFIYFADTTSYLIGRQKIDGTERETILKDGIHNVEGVAVDWMGDNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLNGWMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPAGRLYWVDAFYDRIETILLNGTDRKIVYEGPELNHAFGLCHHGNYLFWTEYRSGSVYRLERGVGGAPPTVTLLRSERPPIFEIRMYDAQQQQVGTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDADGVTCLANPSYVPPPQCQPGEFACANSRCIQERWKCDGDNDCLDNSDEAPALCHQHTCPSDRFKCENNRCIPNRWLCDGDNDCGNSEDESNATCSARTCPPNQFSCASGRCIPISWTCDLDDDCGDRSDESASCAYPTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSHSCSSTQFKCNSGRCIPEHWTCDGDNDCGDYSDETHANCTNQATRPPGGCHTDEFQCRLDGLCIPLRWRCDGDTDCMDSSDEKSCEGVTHVCDPSVKFGCKDSARCISKAWVCDGDNDCEDNSDEENCESLACRPPSHPCANNTSVCLPPDKLCDGNDDCGDGSDEGELCDQCSLNNGGCSHNCSVAPGEGIVCSCPLGMELGPDNHTCQIQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGESCRSLDPFKPFIIFSNRHEIRRIDLHKGDYSVLVPGLRNTIALDFHLSQSALYWTDVVEDKIYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIAGNIYWVESNLDQIEVAKLDGTLRTTLLAGDIEHPRAIALDPRDGILFWTDWDASLPRIEAASMSGAGRRTVHRETGSGGWPNGLTVDYLEKRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGEVYWTDWRTNTLAKANKWTGHNVTVVQRTNTQPFDLQVYHPSRQPMAPNPCEANGGQGPCSHLCLINYNRTVSCACPHLMKLHKDNTTCYEFKKFLLYARQMEIRGVDLDAPYYNYIISFTVPDIDNVTVLDYDAREQRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVSRNLFWTSYDTNKKQINVARLDGSFKNAVVQGLEQPHGLVVHPLRGKLYWTDGDNISMANMDGSNRTLLFSGQKGPVGLAIDFPESKLYWISSGNHTINRCNLDGSGLEVIDAMRSQLGKATALAIMGDKLWWADQVSEKMGTCSKADGSGSVVLRNSTTLVMHMKVYDESIQLDHKGTNPCSVNNGDCSQLCLPTSETTRSCMCTAGYSLRSGQQACEGVGSFLLYSVHEGIRGIPLDPNDKSDALVPVSGTSLAVGIDFHAENDTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIAGNIYWTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEKGYLFWTEWGQYPRIERSRLDGTERVVLVNVSISWPNGISVDYQDGKLYWCDARTDKIERIDLETGENREVVLSSNNMDMFSVSVFEDFIYWSDRTHANGSIKRGSKDNATDSVPLRTGIGVQLKDIKVFNRDRQKGTNVCAVANGGCQQLCLYRGRGQRACACAHGMLAEDGASCREYAGYLLYSERTILKSIHLSDERNLNAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSRRITIVENVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQNLMFWTNWNEQHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKHVGSNMKLLRVDIPQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQDDLTCRAVNSSCRAQDEFECANGECINFSLTCDGVPHCKDKSDEKPSYCNSRRCKKTFRQCSNGRCVSNMLWCNGADDCGDGSDEIPCNKTACGVGEFRCRDGTCIGNSSRCNQFVDCEDASDEMNCSATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNYFACPSGRCIPMSWTCDKEDDCEHGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCADGADESIAAGCLYNSTCDDREFMCQNRQCIPKHFVCDHDRDCADGSDESPECEYPTCGPSEFRCANGRCLSSRQWECDGENDCHDQSDEAPKNPHCTSQEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDSSDERGCHINECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADVDECSTTFPCSQRCINTHGSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAVALDFDYREQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSSRSVIVDTKITWPNGLTLDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDYVYWTDWETKSINRAHKTTGTNKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGSDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECARFVCPPNRPFRCKNDRVCLWIGRQCDGTDNCGDGTDEEDCEPPTAHTTHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASICGDEARCVRTEKAAYCACRSGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQAFQGDESVRIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNISGLKMPRGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPIVAADSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLVNLTGGLSHASDVVLYHQHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTCNLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEHCRNGGTCAASPSGMPTCRCPTGFTGPKCTQQVCAGYCANNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGYCENFGTCQMAADGSRQCRCTAYFEGSRCEVNKCSRCLEGACVVNKQSGDVTCNCTDGRVAPSCLTCVGHCSNGGSCTMNSKMMPECQCPPHMTGPRCEEHVFSQQQPGHIASILIPLLLLLLLVLVAGVVFWYKRRVQGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA	Literature-reported	Human glioblastoma cell lines: levels of low-density lipoprotein receptor and low-density lipoprotein receptor-related protein. Cancer Res. 2000 Apr 15;60(8):2300-3.	.	.	.	.	.	.	.	.	.	.	.	hsa04979: Cholesterol metabolism; hsa05010: Alzheimer disease; hsa05144: Malaria	R-HSA-2168880: Scavenging of heme from plasma; R-HSA-975634: Retinoid metabolism and transport	.	.
TT9JAGO	LDL receptor related protein-1 (LRP-1)	Q07954	LRP1_HUMAN	Low density lipoprotein receptor	Alpha-2-macroglobulin receptor; A2MR	LRP1	"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."	.	2KNY; 2KNX; 2FYL; 2FYJ; 1J8E	MLTPPLLLLLPLLSALVAAAIDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCQPNEHNCLGTELCVPMSRLCNGVQDCMDGSDEGPHCRELQGNCSRLGCQHHCVPTLDGPTCYCNSSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFICGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPGLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDIDDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAMGKVFFTDYGQIPKVERCDMDGQNRTKLVDSKIVFPHGITLDLVSRLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFENYLYATNSDNANAQQKTSVIRVNRFNSTEYQVVTRVDKGGALHIYHQRRQPRVRSHACENDQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCKKPEHELFLVYGKGRPGIIRGMDMGAKVPDEHMIPIENLMNPRALDFHAETGFIYFADTTSYLIGRQKIDGTERETILKDGIHNVEGVAVDWMGDNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLNGWMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPAGRLYWVDAFYDRIETILLNGTDRKIVYEGPELNHAFGLCHHGNYLFWTEYRSGSVYRLERGVGGAPPTVTLLRSERPPIFEIRMYDAQQQQVGTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDADGVTCLANPSYVPPPQCQPGEFACANSRCIQERWKCDGDNDCLDNSDEAPALCHQHTCPSDRFKCENNRCIPNRWLCDGDNDCGNSEDESNATCSARTCPPNQFSCASGRCIPISWTCDLDDDCGDRSDESASCAYPTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSHSCSSTQFKCNSGRCIPEHWTCDGDNDCGDYSDETHANCTNQATRPPGGCHTDEFQCRLDGLCIPLRWRCDGDTDCMDSSDEKSCEGVTHVCDPSVKFGCKDSARCISKAWVCDGDNDCEDNSDEENCESLACRPPSHPCANNTSVCLPPDKLCDGNDDCGDGSDEGELCDQCSLNNGGCSHNCSVAPGEGIVCSCPLGMELGPDNHTCQIQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGESCRSLDPFKPFIIFSNRHEIRRIDLHKGDYSVLVPGLRNTIALDFHLSQSALYWTDVVEDKIYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIAGNIYWVESNLDQIEVAKLDGTLRTTLLAGDIEHPRAIALDPRDGILFWTDWDASLPRIEAASMSGAGRRTVHRETGSGGWPNGLTVDYLEKRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGEVYWTDWRTNTLAKANKWTGHNVTVVQRTNTQPFDLQVYHPSRQPMAPNPCEANGGQGPCSHLCLINYNRTVSCACPHLMKLHKDNTTCYEFKKFLLYARQMEIRGVDLDAPYYNYIISFTVPDIDNVTVLDYDAREQRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVSRNLFWTSYDTNKKQINVARLDGSFKNAVVQGLEQPHGLVVHPLRGKLYWTDGDNISMANMDGSNRTLLFSGQKGPVGLAIDFPESKLYWISSGNHTINRCNLDGSGLEVIDAMRSQLGKATALAIMGDKLWWADQVSEKMGTCSKADGSGSVVLRNSTTLVMHMKVYDESIQLDHKGTNPCSVNNGDCSQLCLPTSETTRSCMCTAGYSLRSGQQACEGVGSFLLYSVHEGIRGIPLDPNDKSDALVPVSGTSLAVGIDFHAENDTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIAGNIYWTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEKGYLFWTEWGQYPRIERSRLDGTERVVLVNVSISWPNGISVDYQDGKLYWCDARTDKIERIDLETGENREVVLSSNNMDMFSVSVFEDFIYWSDRTHANGSIKRGSKDNATDSVPLRTGIGVQLKDIKVFNRDRQKGTNVCAVANGGCQQLCLYRGRGQRACACAHGMLAEDGASCREYAGYLLYSERTILKSIHLSDERNLNAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSRRITIVENVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQNLMFWTNWNEQHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKHVGSNMKLLRVDIPQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQDDLTCRAVNSSCRAQDEFECANGECINFSLTCDGVPHCKDKSDEKPSYCNSRRCKKTFRQCSNGRCVSNMLWCNGADDCGDGSDEIPCNKTACGVGEFRCRDGTCIGNSSRCNQFVDCEDASDEMNCSATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNYFACPSGRCIPMSWTCDKEDDCEHGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCADGADESIAAGCLYNSTCDDREFMCQNRQCIPKHFVCDHDRDCADGSDESPECEYPTCGPSEFRCANGRCLSSRQWECDGENDCHDQSDEAPKNPHCTSQEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDSSDERGCHINECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADVDECSTTFPCSQRCINTHGSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAVALDFDYREQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSSRSVIVDTKITWPNGLTLDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDYVYWTDWETKSINRAHKTTGTNKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGSDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECARFVCPPNRPFRCKNDRVCLWIGRQCDGTDNCGDGTDEEDCEPPTAHTTHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASICGDEARCVRTEKAAYCACRSGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQAFQGDESVRIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNISGLKMPRGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPIVAADSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLVNLTGGLSHASDVVLYHQHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTCNLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEHCRNGGTCAASPSGMPTCRCPTGFTGPKCTQQVCAGYCANNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGYCENFGTCQMAADGSRQCRCTAYFEGSRCEVNKCSRCLEGACVVNKQSGDVTCNCTDGRVAPSCLTCVGHCSNGGSCTMNSKMMPECQCPPHMTGPRCEEHVFSQQQPGHIASILIPLLLLLLLVLVAGVVFWYKRRVQGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA	Literature-reported	Expression of LRP1 in retinal pigment epithelial cells and its regulation by growth factors. Invest Ophthalmol Vis Sci. 2004 Jun;45(6):2033-8.	.	Low density lipoprotein receptor	.	LDLR family.	.	.	Complement Clr-like EGF-like; Domain of unknown function (DUF5050); Calcium-binding EGF domain; Low-density lipoprotein receptor domain class A; Low-density lipoprotein receptor repeat class B	PF12662; PF16472; PF07645; PF00057; PF00058	PF12662; cEGF; PF16472; DUF5050; PF07645; EGF_CA; PF00057; Ldl_recept_a; PF00058; Ldl_recept_b	9.B.87.1.16	The Selenoprotein P Receptor (SelP-Receptor) Family	hsa04979: Cholesterol metabolism; hsa05010: Alzheimer disease; hsa05144: Malaria	R-HSA-2168880: Scavenging of heme from plasma; R-HSA-975634: Retinoid metabolism and transport	.	.
TTPH1AJ	LDL receptor related protein-2 (LRP-2)	P98164	LRP2_HUMAN	Low density lipoprotein receptor	Megalin; Lowdensity lipoprotein receptorrelated protein 2; Low-density lipoprotein receptor-related protein 2; Gp330; Glycoprotein 330	LRP2	"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."	.	2M0P	MDRGPAAVACTLLLALVACLAPASGQECDSAHFRCGSGHCIPADWRCDGTKDCSDDADEIGCAVVTCQQGYFKCQSEGQCIPNSWVCDQDQDCDDGSDERQDCSQSTCSSHQITCSNGQCIPSEYRCDHVRDCPDGADENDCQYPTCEQLTCDNGACYNTSQKCDWKVDCRDSSDEINCTEICLHNEFSCGNGECIPRAYVCDHDNDCQDGSDEHACNYPTCGGYQFTCPSGRCIYQNWVCDGEDDCKDNGDEDGCESGPHDVHKCSPREWSCPESGRCISIYKVCDGILDCPGREDENNTSTGKYCSMTLCSALNCQYQCHETPYGGACFCPPGYIINHNDSRTCVEFDDCQIWGICDQKCESRPGRHLCHCEEGYILERGQYCKANDSFGEASIIFSNGRDLLIGDIHGRSFRILVESQNRGVAVGVAFHYHLQRVFWTDTVQNKVFSVDINGLNIQEVLNVSVETPENLAVDWVNNKIYLVETKVNRIDMVNLDGSYRVTLITENLGHPRGIAVDPTVGYLFFSDWESLSGEPKLERAFMDGSNRKDLVKTKLGWPAGVTLDMISKRVYWVDSRFDYIETVTYDGIQRKTVVHGGSLIPHPFGVSLFEGQVFFTDWTKMAVLKANKFTETNPQVYYQASLRPYGVTVYHSLRQPYATNPCKDNNGGCEQVCVLSHRTDNDGLGFRCKCTFGFQLDTDERHCIAVQNFLIFSSQVAIRGIPFTLSTQEDVMVPVSGNPSFFVGIDFDAQDSTIFFSDMSKHMIFKQKIDGTGREILAANRVENVESLAFDWISKNLYWTDSHYKSISVMRLADKTRRTVVQYLNNPRSVVVHPFAGYLFFTDWFRPAKIMRAWSDGSHLLPVINTTLGWPNGLAIDWAASRLYWVDAYFDKIEHSTFDGLDRRRLGHIEQMTHPFGLAIFGEHLFFTDWRLGAIIRVRKADGGEMTVIRSGIAYILHLKSYDVNIQTGSNACNQPTHPNGDCSHFCFPVPNFQRVCGCPYGMRLASNHLTCEGDPTNEPPTEQCGLFSFPCKNGRCVPNYYLCDGVDDCHDNSDEQLCGTLNNTCSSSAFTCGHGECIPAHWRCDKRNDCVDGSDEHNCPTHAPASCLDTQYTCDNHQCISKNWVCDTDNDCGDGSDEKNCNSTETCQPSQFNCPNHRCIDLSFVCDGDKDCVDGSDEVGCVLNCTASQFKCASGDKCIGVTNRCDGVFDCSDNSDEAGCPTRPPGMCHSDEFQCQEDGICIPNFWECDGHPDCLYGSDEHNACVPKTCPSSYFHCDNGNCIHRAWLCDRDNDCGDMSDEKDCPTQPFRCPSWQWQCLGHNICVNLSVVCDGIFDCPNGTDESPLCNGNSCSDFNGGCTHECVQEPFGAKCLCPLGFLLANDSKTCEDIDECDILGSCSQHCYNMRGSFRCSCDTGYMLESDGRTCKVTASESLLLLVASQNKIIADSVTSQVHNIYSLVENGSYIVAVDFDSISGRIFWSDATQGKTWSAFQNGTDRRVVFDSSIILTETIAIDWVGRNLYWTDYALETIEVSKIDGSHRTVLISKNLTNPRGLALDPRMNEHLLFWSDWGHHPRIERASMDGSMRTVIVQDKIFWPCGLTIDYPNRLLYFMDSYLDYMDFCDYNGHHRRQVIASDLIIRHPYALTLFEDSVYWTDRATRRVMRANKWHGGNQSVVMYNIQWPLGIVAVHPSKQPNSVNPCAFSRCSHLCLLSSQGPHFYSCVCPSGWSLSPDLLNCLRDDQPFLITVRQHIIFGISLNPEVKSNDAMVPIAGIQNGLDVEFDDAEQYIYWVENPGEIHRVKTDGTNRTVFASISMVGPSMNLALDWISRNLYSTNPRTQSIEVLTLHGDIRYRKTLIANDGTALGVGFPIGITVDPARGKLYWSDQGTDSGVPAKIASANMDGTSVKTLFTGNLEHLECVTLDIEEQKLYWAVTGRGVIERGNVDGTDRMILVHQLSHPWGIAVHDSFLYYTDEQYEVIERVDKATGANKIVLRDNVPNLRGLQVYHRRNAAESSNGCSNNMNACQQICLPVPGGLFSCACATGFKLNPDNRSCSPYNSFIVVSMLSAIRGFSLELSDHSETMVPVAGQGRNALHVDVDVSSGFIYWCDFSSSVASDNAIRRIKPDGSSLMNIVTHGIGENGVRGIAVDWVAGNLYFTNAFVSETLIEVLRINTTYRRVLLKVTVDMPRHIVVDPKNRYLFWADYGQRPKIERSFLDCTNRTVLVSEGIVTPRGLAVDRSDGYVYWVDDSLDIIARIRINGENSEVIRYGSRYPTPYGITVFENSIIWVDRNLKKIFQASKEPENTEPPTVIRDNINWLRDVTIFDKQVQPRSPAEVNNNPCLENNGGCSHLCFALPGLHTPKCDCAFGTLQSDGKNCAISTENFLIFALSNSLRSLHLDPENHSPPFQTINVERTVMSLDYDSVSDRIYFTQNLASGVGQISYATLSSGIHTPTVIASGIGTADGIAFDWITRRIYYSDYLNQMINSMAEDGSNRTVIARVPKPRAIVLDPCQGYLYWADWDTHAKIERATLGGNFRVPIVNSSLVMPSGLTLDYEEDLLYWVDASLQRIERSTLTGVDREVIVNAAVHAFGLTLYGQYIYWTDLYTQRIYRANKYDGSGQIAMTTNLLSQPRGINTVVKNQKQQCNNPCEQFNGGCSHICAPGPNGAECQCPHEGNWYLANNRKHCIVDNGERCGASSFTCSNGRCISEEWKCDNDNDCGDGSDEMESVCALHTCSPTAFTCANGRCVQYSYRCDYYNDCGDGSDEAGCLFRDCNATTEFMCNNRRCIPREFICNGVDNCHDNNTSDEKNCPDRTCQSGYTKCHNSNICIPRVYLCDGDNDCGDNSDENPTYCTTHTCSSSEFQCASGRCIPQHWYCDQETDCFDASDEPASCGHSERTCLADEFKCDGGRCIPSEWICDGDNDCGDMSDEDKRHQCQNQNCSDSEFLCVNDRPPDRRCIPQSWVCDGDVDCTDGYDENQNCTRRTCSENEFTCGYGLCIPKIFRCDRHNDCGDYSDERGCLYQTCQQNQFTCQNGRCISKTFVCDEDNDCGDGSDELMHLCHTPEPTCPPHEFKCDNGRCIEMMKLCNHLDDCLDNSDEKGCGINECHDPSISGCDHNCTDTLTSFYCSCRPGYKLMSDKRTCVDIDECTEMPFVCSQKCENVIGSYICKCAPGYLREPDGKTCRQNSNIEPYLIFSNRYYLRNLTIDGYFYSLILEGLDNVVALDFDRVEKRLYWIDTQRQVIERMFLNKTNKETIINHRLPAAESLAVDWVSRKLYWLDARLDGLFVSDLNGGHRRMLAQHCVDANNTFCFDNPRGLALHPQYGYLYWADWGHRAYIGRVGMDGTNKSVIISTKLEWPNGITIDYTNDLLYWADAHLGYIEYSDLEGHHRHTVYDGALPHPFAITIFEDTIYWTDWNTRTVEKGNKYDGSNRQTLVNTTHRPFDIHVYHPYRQPIVSNPCGTNNGGCSHLCLIKPGGKGFTCECPDDFRTLQLSGSTYCMPMCSSTQFLCANNEKCIPIWWKCDGQKDCSDGSDELALCPQRFCRLGQFQCSDGNCTSPQTLCNAHQNCPDGSDEDRLLCENHHCDSNEWQCANKRCIPESWQCDTFNDCEDNSDEDSSHCASRTCRPGQFRCANGRCIPQAWKCDVDNDCGDHSDEPIEECMSSAHLCDNFTEFSCKTNYRCIPKWAVCNGVDDCRDNSDEQGCEERTCHPVGDFRCKNHHCIPLRWQCDGQNDCGDNSDEENCAPRECTESEFRCVNQQCIPSRWICDHYNDCGDNSDERDCEMRTCHPEYFQCTSGHCVHSELKCDGSADCLDASDEADCPTRFPDGAYCQATMFECKNHVCIPPYWKCDGDDDCGDGSDEELHLCLDVPCNSPNRFRCDNNRCIYSHEVCNGVDDCGDGTDETEEHCRKPTPKPCTEYEYKCGNGHCIPHDNVCDDADDCGDWSDELGCNKGKERTCAENICEQNCTQLNEGGFICSCTAGFETNVFDRTSCLDINECEQFGTCPQHCRNTKGSYECVCADGFTSMSDRPGKRCAAEGSSPLLLLPDNVRIRKYNLSSERFSEYLQDEEYIQAVDYDWDPKDIGLSVVYYTVRGEGSRFGAIKRAYIPNFESGRNNLVQEVDLKLKYVMQPDGIAVDWVGRHIYWSDVKNKRIEVAKLDGRYRKWLISTDLDQPAAIAVNPKLGLMFWTDWGKEPKIESAWMNGEDRNILVFEDLGWPTGLSIDYLNNDRIYWSDFKEDVIETIKYDGTDRRVIAKEAMNPYSLDIFEDQLYWISKEKGEVWKQNKFGQGKKEKTLVVNPWLTQVRIFHQLRYNKSVPNLCKQICSHLCLLRPGGYSCACPQGSSFIEGSTTECDAAIELPINLPPPCRCMHGGNCYFDETDLPKCKCPSGYTGKYCEMAFSKGISPGTTAVAVLLTILLIVVIGALAIAGFFHYRRTGSLLPALPKLPSLSSLVKPSENGNGVTFRSGADLNMDIGVSGFGPETAIDRSMAMSEDFVMEMGKQPIIFENPMYSARDSAVKVVQPIQVTVSENVDNKNYGSPINPSEIVPETNPTSPAADGTQVTKWNLFKRKSKQTTNFENPIYAQMENEQKESVAATPPPSPSLPAKPKPPSRRDPTPTYSATEDTFKDTANLVKEDSEV	Literature-reported	"The roles of cubilin and megalin, two multiligand receptors, in proximal tubule function: possible implication in the progression of renal disease. Curr Opin Nephrol Hypertens. 2001 Jan;10(1):33-8."	.	Low density lipoprotein receptor	.	LDLR family.	.	.	Complement Clr-like EGF-like; Calcium-binding EGF domain; Low-density lipoprotein receptor domain class A; Low-density lipoprotein receptor repeat class B	PF12662; PF07645; PF00057; PF00058	PF12662; cEGF; PF07645; EGF_CA; PF00057; Ldl_recept_a; PF00058; Ldl_recept_b	9.B.87.1.14	The Selenoprotein P Receptor (SelP-Receptor) Family	hsa04340: Hedgehog signaling pathway; hsa04918: Thyroid hormone synthesis; hsa04979: Cholesterol metabolism	R-HSA-196791: Vitamin D (calciferol) metabolism; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8856828: Clathrin-mediated endocytosis; R-HSA-975634: Retinoid metabolism and transport; R-HSA-9758890: Transport of RCbl within the body	.	.
TT7VMG4	Low-density lipoprotein receptor-related protein 5 (LRP5)	O75197	LRP5_HUMAN	.	LRP-5; Low-density lipoprotein receptor-related protein 7; LRP-7	LRP5	"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)."	.	.	MEAAPPGPPWPLLLLLLLLLALCGCPAPAAASPLLLFANRRDVRLVDAGGVKLESTIVVSGLEDAAAVDFQFSKGAVYWTDVSEEAIKQTYLNQTGAAVQNVVISGLVSPDGLACDWVGKKLYWTDSETNRIEVANLNGTSRKVLFWQDLDQPRAIALDPAHGYMYWTDWGETPRIERAGMDGSTRKIIVDSDIYWPNGLTIDLEEQKLYWADAKLSFIHRANLDGSFRQKVVEGSLTHPFALTLSGDTLYWTDWQTRSIHACNKRTGGKRKEILSALYSPMDIQVLSQERQPFFHTRCEEDNGGCSHLCLLSPSEPFYTCACPTGVQLQDNGRTCKAGAEEVLLLARRTDLRRISLDTPDFTDIVLQVDDIRHAIAIDYDPLEGYVYWTDDEVRAIRRAYLDGSGAQTLVNTEINDPDGIAVDWVARNLYWTDTGTDRIEVTRLNGTSRKILVSEDLDEPRAIALHPVMGLMYWTDWGENPKIECANLDGQERRVLVNASLGWPNGLALDLQEGKLYWGDAKTDKIEVINVDGTKRRTLLEDKLPHIFGFTLLGDFIYWTDWQRRSIERVHKVKASRDVIIDQLPDLMGLKAVNVAKVVGTNPCADRNGGCSHLCFFTPHATRCGCPIGLELLSDMKTCIVPEAFLVFTSRAAIHRISLETNNNDVAIPLTGVKEASALDFDVSNNHIYWTDVSLKTISRAFMNGSSVEHVVEFGLDYPEGMAVDWMGKNLYWADTGTNRIEVARLDGQFRQVLVWRDLDNPRSLALDPTKGYIYWTEWGGKPRIVRAFMDGTNCMTLVDKVGRANDLTIDYADQRLYWTDLDTNMIESSNMLGQERVVIADDLPHPFGLTQYSDYIYWTDWNLHSIERADKTSGRNRTLIQGHLDFVMDILVFHSSRQDGLNDCMHNNGQCGQLCLAIPGGHRCGCASHYTLDPSSRNCSPPTTFLLFSQKSAISRMIPDDQHSPDLILPLHGLRNVKAIDYDPLDKFIYWVDGRQNIKRAKDDGTQPFVLTSLSQGQNPDRQPHDLSIDIYSRTLFWTCEATNTINVHRLSGEAMGVVLRGDRDKPRAIVVNAERGYLYFTNMQDRAAKIERAALDGTEREVLFTTGLIRPVALVVDNTLGKLFWVDADLKRIESCDLSGANRLTLEDANIVQPLGLTILGKHLYWIDRQQQMIERVEKTTGDKRTRIQGRVAHLTGIHAVEEVSLEEFSAHPCARDNGGCSHICIAKGDGTPRCSCPVHLVLLQNLLTCGEPPTCSPDQFACATGEIDCIPGAWRCDGFPECDDQSDEEGCPVCSAAQFPCARGQCVDLRLRCDGEADCQDRSDEADCDAICLPNQFRCASGQCVLIKQQCDSFPDCIDGSDELMCEITKPPSDDSPAHSSAIGPVIGIILSLFVMGGVYFVCQRVVCQRYAGANGPFPHEYVSGTPHVPLNFIAPGGSQHGPFTGIACGKSMMSSVSLMGGRGGVPLYDRNHVTGASSSSSSSTKATLYPPILNPPPSPATDPSLYNMDMFYSSNIPATARPYRPYIIRGMAPPTTPCSTDVCDSDYSASRWKASKYYLDLNSDSDPYPPPPTPHSQYLSAEDSCPPSPATERSYFHLFPPPPSPCTDSS	Clinical trial	"Clinical pipeline report, company report or official report of Boehringer Ingelheim."	.	.	.	.	.	.	.	.	.	.	.	"hsa04150: mTOR signaling pathway; hsa04310: Wnt signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05200: Pathways in cancer; hsa05224: Breast cancer; hsa05225: Hepatocellular carcinoma; hsa05226: Gastric cancer"	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; R-HSA-5339717: Signaling by LRP5 mutants; R-HSA-5340588: Signaling by RNF43 mutants	.	O75197
TTSXOWE	LDL receptor related protein-6 (LRP-6)	O75581	LRP6_HUMAN	Low density lipoprotein receptor	Low-density lipoprotein receptor-related protein 6	LRP6	"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."	.	6H16; 6H15; 5GJE; 5FWW; 5AIR	MGAVLRSLLACSFCVLLRAAPLLLYANRRDLRLVDATNGKENATIVVGGLEDAAAVDFVFSHGLIYWSDVSEEAIKRTEFNKTESVQNVVVSGLLSPDGLACDWLGEKLYWTDSETNRIEVSNLDGSLRKVLFWQELDQPRAIALDPSSGFMYWTDWGEVPKIERAGMDGSSRFIIINSEIYWPNGLTLDYEEQKLYWADAKLNFIHKSNLDGTNRQAVVKGSLPHPFALTLFEDILYWTDWSTHSILACNKYTGEGLREIHSDIFSPMDIHAFSQQRQPNATNPCGIDNGGCSHLCLMSPVKPFYQCACPTGVKLLENGKTCKDGATELLLLARRTDLRRISLDTPDFTDIVLQLEDIRHAIAIDYDPVEGYIYWTDDEVRAIRRSFIDGSGSQFVVTAQIAHPDGIAVDWVARNLYWTDTGTDRIEVTRLNGTMRKILISEDLEEPRAIVLDPMVGYMYWTDWGEIPKIERAALDGSDRVVLVNTSLGWPNGLALDYDEGKIYWGDAKTDKIEVMNTDGTGRRVLVEDKIPHIFGFTLLGDYVYWTDWQRRSIERVHKRSAEREVIIDQLPDLMGLKATNVHRVIGSNPCAEENGGCSHLCLYRPQGLRCACPIGFELISDMKTCIVPEAFLLFSRRADIRRISLETNNNNVAIPLTGVKEASALDFDVTDNRIYWTDISLKTISRAFMNGSALEHVVEFGLDYPEGMAVDWLGKNLYWADTGTNRIEVSKLDGQHRQVLVWKDLDSPRALALDPAEGFMYWTEWGGKPKIDRAAMDGSERTTLVPNVGRANGLTIDYAKRRLYWTDLDTNLIESSNMLGLNREVIADDLPHPFGLTQYQDYIYWTDWSRRSIERANKTSGQNRTIIQGHLDYVMDILVFHSSRQSGWNECASSNGHCSHLCLAVPVGGFVCGCPAHYSLNADNRTCSAPTTFLLFSQKSAINRMVIDEQQSPDIILPIHSLRNVRAIDYDPLDKQLYWIDSRQNMIRKAQEDGSQGFTVVVSSVPSQNLEIQPYDLSIDIYSRYIYWTCEATNVINVTRLDGRSVGVVLKGEQDRPRAVVVNPEKGYMYFTNLQERSPKIERAALDGTEREVLFFSGLSKPIALALDSRLGKLFWADSDLRRIESSDLSGANRIVLEDSNILQPVGLTVFENWLYWIDKQQQMIEKIDMTGREGRTKVQARIAQLSDIHAVKELNLQEYRQHPCAQDNGGCSHICLVKGDGTTRCSCPMHLVLLQDELSCGEPPTCSPQQFTCFTGEIDCIPVAWRCDGFTECEDHSDELNCPVCSESQFQCASGQCIDGALRCNGDANCQDKSDEKNCEVLCLIDQFRCANGQCIGKHKKCDHNVDCSDKSDELDCYPTEEPAPQATNTVGSVIGVIVTIFVSGTVYFICQRMLCPRMKGDGETMTNDYVVHGPASVPLGYVPHPSSLSGSLPGMSRGKSMISSLSIMGGSSGPPYDRAHVTGASSSSSSSTKGTYFPAILNPPPSPATERSHYTMEFGYSSNSPSTHRSYSYRPYSYRHFAPPTTPCSTDVCDSDYAPSRRMTSVATAKGYTSDLNYDSEPVPPPPTPRSQYLSAEENYESCPPSPYTERSYSHHLYPPPPSPCTDSS	Clinical trial	NCBI GEO: archive for functional genomics data sets--update. Nucleic Acids Res. 2013 Jan;41(Database issue):D991-5.	.	Low density lipoprotein receptor	Low density lipoprotein receptor	LDLR family.	.	.	Low-density lipoprotein receptor domain class A; Low-density lipoprotein receptor repeat class B	PF00057; PF00058	PF00057; Ldl_recept_a; PF00058; Ldl_recept_b	.	.	hsa04310:Wnt signaling pathway	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	.	O75581
TT0FAYT	Transforming growth factor beta activator LRRC32 (LRRC32)	Q14392	LRC32_HUMAN	.	Garpin; Glycoprotein A repetitions predominant; GARP; Leucine-rich repeat-containing protein 32	LRRC32	"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)."	.	.	MRPQILLLLALLTLGLAAQHQDKVPCKMVDKKVSCQVLGLLQVPSVLPPDTETLDLSGNQLRSILASPLGFYTALRHLDLSTNEISFLQPGAFQALTHLEHLSLAHNRLAMATALSAGGLGPLPRVTSLDLSGNSLYSGLLERLLGEAPSLHTLSLAENSLTRLTRHTFRDMPALEQLDLHSNVLMDIEDGAFEGLPRLTHLNLSRNSLTCISDFSLQQLRVLDLSCNSIEAFQTASQPQAEFQLTWLDLRENKLLHFPDLAALPRLIYLNLSNNLIRLPTGPPQDSKGIHAPSEGWSALPLSAPSGNASGRPLSQLLNLDLSYNEIELIPDSFLEHLTSLCFLNLSRNCLRTFEARRLGSLPCLMLLDLSHNALETLELGARALGSLRTLLLQGNALRDLPPYTFANLASLQRLNLQGNRVSPCGGPDEPGPSGCVAFSGITSLRSLSLVDNEIELLRAGAFLHTPLTELDLSSNPGLEVATGALGGLEASLEVLALQGNGLMVLQVDLPCFICLKRLNLAENRLSHLPAWTQAVSLEVLDLRNNSFSLLPGSAMGGLETSLRRLYLQGNPLSCCGNGWLAAQLHQGRVDVDATQDLICRFSSQEEVSLSHVRPEDCEKGGLKNINLIIILTFILVSAILLTTLAACCCVRRQKFNQQYKA	Clinical trial	"Clinical pipeline report, company report or official report of Daiichi Sankyo."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q14392
TTK0FEA	Leucine-rich repeat kinase 2 (LRRK2)	Q5S007	LRRK2_HUMAN	Kinase	PARK8; Leucine-rich repeat serine/threonine-protein kinase 2; Dardarin	LRRK2	"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."	EC 2.7.11.1	6DLP; 6DLO; 5MYC; 5MY9; 3D6T	MASGSCQGCEEDEETLKKLIVRLNNVQEGKQIETLVQILEDLLVFTYSERASKLFQGKNIHVPLLIVLDSYMRVASVQQVGWSLLCKLIEVCPGTMQSLMGPQDVGNDWEVLGVHQLILKMLTVHNASVNLSVIGLKTLDLLLTSGKITLLILDEESDIFMLIFDAMHSFPANDEVQKLGCKALHVLFERVSEEQLTEFVENKDYMILLSALTNFKDEEEIVLHVLHCLHSLAIPCNNVEVLMSGNVRCYNIVVEAMKAFPMSERIQEVSCCLLHRLTLGNFFNILVLNEVHEFVVKAVQQYPENAALQISALSCLALLTETIFLNQDLEEKNENQENDDEGEEDKLFWLEACYKALTWHRKNKHVQEAACWALNNLLMYQNSLHEKIGDEDGHFPAHREVMLSMLMHSSSKEVFQASANALSTLLEQNVNFRKILLSKGIHLNVLELMQKHIHSPEVAESGCKMLNHLFEGSNTSLDIMAAVVPKILTVMKRHETSLPVQLEALRAILHFIVPGMPEESREDTEFHHKLNMVKKQCFKNDIHKLVLAALNRFIGNPGIQKCGLKVISSIVHFPDALEMLSLEGAMDSVLHTLQMYPDDQEIQCLGLSLIGYLITKKNVFIGTGHLLAKILVSSLYRFKDVAEIQTKGFQTILAILKLSASFSKLLVHHSFDLVIFHQMSSNIMEQKDQQFLNLCCKCFAKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADANQAKEGSSLICQVCEKESSPKLVELLLNSGSREQDVRKALTISIGKGDSQIISLLLRRLALDVANNSICLGGFCIGKVEPSWLGPLFPDKTSNLRKQTNIASTLARMVIRYQMKSAVEEGTASGSDGNFSEDVLSKFDEWTFIPDSSMDSVFAQSDDLDSEGSEGSFLVKKKSNSISVGEFYRDAVLQRCSPNLQRHSNSLGPIFDHEDLLKRKRKILSSDDSLRSSKLQSHMRHSDSISSLASEREYITSLDLSANELRDIDALSQKCCISVHLEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTVKCPTLKQFNLSYNQLSFVPENLTDVVEKLEQLILEGNKISGICSPLRLKELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLNFDFKHIGCKAKDIIRFLQQRLKKAVPYNRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATEESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRMYWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWALYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDILNSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKESWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILNIGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPVVEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFCNSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	EC:2.7	.	protein kinase superfamily. TKL Ser/Thr protein kinase family.	2.7.11.1	Transferring phosphorus-containing groups	"C-terminal of Roc, COR, domain; Leucine rich repeat; Protein kinase domain"	PF16095; PF13855; PF00069	PF16095; COR; PF13855; LRR_8; PF00069; Pkinase	.	.	hsa05012: Parkinson disease; hsa05022: Pathways of neurodegeneration - multiple diseases	R-HSA-8857538: PTK6 promotes HIF1A stabilization	.	Q5S007
TT6AXLY	Leucine-rich repeat kinase 2 G2019S mutant (LRRK2 G2019S)	Q5S007	LRRK2_HUMAN	Kinase	PARK8 G2019S mutant; LRRK2 G2019S mutant; Dardarin G2019S mutant	LRRK2	"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."	EC 2.7.11.1	6DLP; 6DLO; 5MYC; 5MY9; 3D6T	MASGSCQGCEEDEETLKKLIVRLNNVQEGKQIETLVQILEDLLVFTYSERASKLFQGKNIHVPLLIVLDSYMRVASVQQVGWSLLCKLIEVCPGTMQSLMGPQDVGNDWEVLGVHQLILKMLTVHNASVNLSVIGLKTLDLLLTSGKITLLILDEESDIFMLIFDAMHSFPANDEVQKLGCKALHVLFERVSEEQLTEFVENKDYMILLSALTNFKDEEEIVLHVLHCLHSLAIPCNNVEVLMSGNVRCYNIVVEAMKAFPMSERIQEVSCCLLHRLTLGNFFNILVLNEVHEFVVKAVQQYPENAALQISALSCLALLTETIFLNQDLEEKNENQENDDEGEEDKLFWLEACYKALTWHRKNKHVQEAACWALNNLLMYQNSLHEKIGDEDGHFPAHREVMLSMLMHSSSKEVFQASANALSTLLEQNVNFRKILLSKGIHLNVLELMQKHIHSPEVAESGCKMLNHLFEGSNTSLDIMAAVVPKILTVMKRHETSLPVQLEALRAILHFIVPGMPEESREDTEFHHKLNMVKKQCFKNDIHKLVLAALNRFIGNPGIQKCGLKVISSIVHFPDALEMLSLEGAMDSVLHTLQMYPDDQEIQCLGLSLIGYLITKKNVFIGTGHLLAKILVSSLYRFKDVAEIQTKGFQTILAILKLSASFSKLLVHHSFDLVIFHQMSSNIMEQKDQQFLNLCCKCFAKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADANQAKEGSSLICQVCEKESSPKLVELLLNSGSREQDVRKALTISIGKGDSQIISLLLRRLALDVANNSICLGGFCIGKVEPSWLGPLFPDKTSNLRKQTNIASTLARMVIRYQMKSAVEEGTASGSDGNFSEDVLSKFDEWTFIPDSSMDSVFAQSDDLDSEGSEGSFLVKKKSNSISVGEFYRDAVLQRCSPNLQRHSNSLGPIFDHEDLLKRKRKILSSDDSLRSSKLQSHMRHSDSISSLASEREYITSLDLSANELRDIDALSQKCCISVHLEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTVKCPTLKQFNLSYNQLSFVPENLTDVVEKLEQLILEGNKISGICSPLRLKELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLNFDFKHIGCKAKDIIRFLQQRLKKAVPYNRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATEESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRMYWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWALYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDILNSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKESWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILNIGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPVVEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFCNSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE	Patented-recorded	Leucine-rich repeat kinase 2 inhibitors: a patent review (2014-2016).Expert Opin Ther Pat. 2017 Jun;27(6):667-676.	15.5	EC:2.7	Protein kinase superfamily. TKL Ser/Thr protein kinase family	.	.	.	"C-terminal of Roc, COR, domain; Leucine rich repeat; Protein kinase domain"	PF16095; PF13855; PF00069	PF16095; COR; PF13855; LRR_8; PF00069; Pkinase	.	.	hsa05012: Parkinson disease; hsa05022: Pathways of neurodegeneration - multiple diseases	R-HSA-8857538: PTK6 promotes HIF1A stabilization	.	Q5S007
TTC7A6G	Leucine-rich repeat kinase 2 S935 phosphorylation (LRRK2 pS935)	Q5S007	LRRK2_HUMAN	Kinase	PARK8 S935 phosphorylation; LRRK2 S935 phosphorylation; Dardarin S935 phosphorylation	LRRK2	"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."	EC 2.7.11.1	6DLP; 6DLO; 5MYC; 5MY9; 3D6T	MASGSCQGCEEDEETLKKLIVRLNNVQEGKQIETLVQILEDLLVFTYSERASKLFQGKNIHVPLLIVLDSYMRVASVQQVGWSLLCKLIEVCPGTMQSLMGPQDVGNDWEVLGVHQLILKMLTVHNASVNLSVIGLKTLDLLLTSGKITLLILDEESDIFMLIFDAMHSFPANDEVQKLGCKALHVLFERVSEEQLTEFVENKDYMILLSALTNFKDEEEIVLHVLHCLHSLAIPCNNVEVLMSGNVRCYNIVVEAMKAFPMSERIQEVSCCLLHRLTLGNFFNILVLNEVHEFVVKAVQQYPENAALQISALSCLALLTETIFLNQDLEEKNENQENDDEGEEDKLFWLEACYKALTWHRKNKHVQEAACWALNNLLMYQNSLHEKIGDEDGHFPAHREVMLSMLMHSSSKEVFQASANALSTLLEQNVNFRKILLSKGIHLNVLELMQKHIHSPEVAESGCKMLNHLFEGSNTSLDIMAAVVPKILTVMKRHETSLPVQLEALRAILHFIVPGMPEESREDTEFHHKLNMVKKQCFKNDIHKLVLAALNRFIGNPGIQKCGLKVISSIVHFPDALEMLSLEGAMDSVLHTLQMYPDDQEIQCLGLSLIGYLITKKNVFIGTGHLLAKILVSSLYRFKDVAEIQTKGFQTILAILKLSASFSKLLVHHSFDLVIFHQMSSNIMEQKDQQFLNLCCKCFAKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADANQAKEGSSLICQVCEKESSPKLVELLLNSGSREQDVRKALTISIGKGDSQIISLLLRRLALDVANNSICLGGFCIGKVEPSWLGPLFPDKTSNLRKQTNIASTLARMVIRYQMKSAVEEGTASGSDGNFSEDVLSKFDEWTFIPDSSMDSVFAQSDDLDSEGSEGSFLVKKKSNSISVGEFYRDAVLQRCSPNLQRHSNSLGPIFDHEDLLKRKRKILSSDDSLRSSKLQSHMRHSDSISSLASEREYITSLDLSANELRDIDALSQKCCISVHLEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTVKCPTLKQFNLSYNQLSFVPENLTDVVEKLEQLILEGNKISGICSPLRLKELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLNFDFKHIGCKAKDIIRFLQQRLKKAVPYNRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATEESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRMYWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWALYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDILNSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKESWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILNIGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPVVEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFCNSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE	Patented-recorded	Leucine-rich repeat kinase 2 inhibitors: a patent review (2014-2016).Expert Opin Ther Pat. 2017 Jun;27(6):667-676.	15.5	EC:2.7	Protein kinase superfamily. TKL Ser/Thr protein kinase family	.	.	.	"C-terminal of Roc, COR, domain; Leucine rich repeat; Protein kinase domain"	PF16095; PF13855; PF00069	PF16095; COR; PF13855; LRR_8; PF00069; Pkinase	.	.	hsa05012: Parkinson disease; hsa05022: Pathways of neurodegeneration - multiple diseases	R-HSA-8857538: PTK6 promotes HIF1A stabilization	.	Q5S007
TT1HI8U	Leucine-rich repeat serine/threonine-protein kinase 2 messenger RNA (LRRK2 mRNA)	Q5S007	LRRK2_HUMAN	mRNA target	Dardarin (mRNA)	LRRK2	"Serine/threonine-protein kinase which phosphorylates a broad range of proteins involved in multiple processes such as neuronal plasticity, innate immunity, autophagy, and vesicle trafficking (PubMed:20949042, PubMed:22012985, PubMed:26824392, PubMed:27830463, PubMed:29125462, PubMed:28720718, PubMed:29127255, PubMed:30398148, PubMed:29212815, PubMed:30635421, PubMed:21850687, PubMed:23395371, PubMed:17114044, PubMed:24687852, PubMed:26014385, PubMed:25201882). Is a key regulator of RAB GTPases by regulating the GTP/GDP exchange and interaction partners of RABs through phosphorylation (PubMed:26824392, PubMed:28720718, PubMed:29127255, PubMed:30398148, PubMed:29212815, PubMed:29125462, PubMed:30635421). Phosphorylates RAB3A, RAB3B, RAB3C, RAB3D, RAB5A, RAB5B, RAB5C, RAB8A, RAB8B, RAB10, RAB12, RAB35, and RAB43 (PubMed:26824392, PubMed:28720718, PubMed:29127255, PubMed:30398148, PubMed:29212815, PubMed:29125462, PubMed:30635421, PubMed:23395371). Regulates the RAB3IP-catalyzed GDP/GTP exchange for RAB8A through the phosphorylation of 'Thr-72' on RAB8A (PubMed:26824392). Inhibits the interaction between RAB8A and GDI1 and/or GDI2 by phosphorylating 'Thr-72' on RAB8A (PubMed:26824392). Regulates primary ciliogenesis through phosphorylation of RAB8A and RAB10, which promotes SHH signaling in the brain (PubMed:29125462, PubMed:30398148). 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 (PubMed:23395371). Regulates neuronal process morphology in the intact central nervous system (CNS) (PubMed:17114044). Plays a role in synaptic vesicle trafficking (PubMed:24687852). Plays an important role in recruiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization (PubMed:25201882). Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway (PubMed:22012985). The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes (PubMed:22012985). Phosphorylates PRDX3 (PubMed:21850687). By phosphorylating APP on 'Thr-743', which promotes the production and the nuclear translocation of the APP intracellular domain (AICD), regulates dopaminergic neuron apoptosis (PubMed:28720718). Acts as a positive regulator of innate immunity by mediating phosphorylation of RIPK2 downstream of NOD1 and NOD2, thereby enhancing RIPK2 activation (PubMed:27830463). Independent of its kinase activity, inhibits the proteasomal degradation of MAPT, thus promoting MAPT oligomerization and secretion (PubMed:26014385). In addition, has GTPase activity via its Roc domain which regulates LRRK2 kinase activity (PubMed:18230735, PubMed:26824392, PubMed:29125462, PubMed:28720718, PubMed:29212815). {ECO:0000269|PubMed:17114044, ECO:0000269|PubMed:18230735, ECO:0000269|PubMed:20949042, ECO:0000269|PubMed:21850687, ECO:0000269|PubMed:22012985, ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:24687852, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:26014385, ECO:0000269|PubMed:26824392, ECO:0000269|PubMed:27830463, ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:29125462, ECO:0000269|PubMed:29127255, ECO:0000269|PubMed:29212815, ECO:0000269|PubMed:30398148, ECO:0000269|PubMed:30635421}."	EC 2.7.11.1; EC 3.6.5.-	2ZEJ;3D6T;5MY9;5MYC;6DLO;6DLP;6OJE;6OJF;6VNO;6VP6;6VP7;6XAF;6XR4;7LHT;7LHW;7LI3;7LI4;7THY;7THZ	MASGSCQGCEEDEETLKKLIVRLNNVQEGKQIETLVQILEDLLVFTYSERASKLFQGKNIHVPLLIVLDSYMRVASVQQVGWSLLCKLIEVCPGTMQSLMGPQDVGNDWEVLGVHQLILKMLTVHNASVNLSVIGLKTLDLLLTSGKITLLILDEESDIFMLIFDAMHSFPANDEVQKLGCKALHVLFERVSEEQLTEFVENKDYMILLSALTNFKDEEEIVLHVLHCLHSLAIPCNNVEVLMSGNVRCYNIVVEAMKAFPMSERIQEVSCCLLHRLTLGNFFNILVLNEVHEFVVKAVQQYPENAALQISALSCLALLTETIFLNQDLEEKNENQENDDEGEEDKLFWLEACYKALTWHRKNKHVQEAACWALNNLLMYQNSLHEKIGDEDGHFPAHREVMLSMLMHSSSKEVFQASANALSTLLEQNVNFRKILLSKGIHLNVLELMQKHIHSPEVAESGCKMLNHLFEGSNTSLDIMAAVVPKILTVMKRHETSLPVQLEALRAILHFIVPGMPEESREDTEFHHKLNMVKKQCFKNDIHKLVLAALNRFIGNPGIQKCGLKVISSIVHFPDALEMLSLEGAMDSVLHTLQMYPDDQEIQCLGLSLIGYLITKKNVFIGTGHLLAKILVSSLYRFKDVAEIQTKGFQTILAILKLSASFSKLLVHHSFDLVIFHQMSSNIMEQKDQQFLNLCCKCFAKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADANQAKEGSSLICQVCEKESSPKLVELLLNSGSREQDVRKALTISIGKGDSQIISLLLRRLALDVANNSICLGGFCIGKVEPSWLGPLFPDKTSNLRKQTNIASTLARMVIRYQMKSAVEEGTASGSDGNFSEDVLSKFDEWTFIPDSSMDSVFAQSDDLDSEGSEGSFLVKKKSNSISVGEFYRDAVLQRCSPNLQRHSNSLGPIFDHEDLLKRKRKILSSDDSLRSSKLQSHMRHSDSISSLASEREYITSLDLSANELRDIDALSQKCCISVHLEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTVKCPTLKQFNLSYNQLSFVPENLTDVVEKLEQLILEGNKISGICSPLRLKELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLNFDFKHIGCKAKDIIRFLQQRLKKAVPYNRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATEESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRMYWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWALYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDILNSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKESWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILNIGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPVVEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFCNSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE	Clinical trial	"Clinical pipeline report, company report or official report of Ionis"	.	.	.	.	.	.	.	.	.	.	.	hsa:120892	R-HSA-8857538;	.	Q5S007;
TT2KHSC	Small nuclear ribonuclear CaSm (LSM1)	O15116	LSM1_HUMAN	.	LSM1; Cancer-associated Sm-like (CaSm) oncogene; Cancer-associated Sm-like; CaSm	LSM1	Plays a role in replication-dependenthistone mRNA degradation. Binds specifically to the 3'-terminal U-tract of U6 snRNA.	.	.	MNYMPGTASLIEDIDKKHLVLLRDGRTLIGFLRSIDQFANLVLHQTVERIHVGKKYGDIPRGIFVVRGENVVLLGEIDLEKESDTPLQQVSIEEILEEQRVEQQTKLEAEKLKVQALKDRGLSIPRADTLDEY	Literature-reported	The cancer-associated Sm-like oncogene: a novel target for the gene therapy of pancreatic cancer. Surgery. 2000 Aug;128(2):353-60.	.	.	.	.	.	.	.	.	.	.	.	hsa03018: RNA degradation	R-HSA-430039: mRNA decay by 5' to 3' exoribonuclease	.	O15116
TT7O8ZA	Lanosterol synthase (LSS)	P48449	ERG7_HUMAN	Intramolecular transferases	"Oxidosqualene--lanosterol cyclase; Oxidosqualene cyclase; OSC; LSS; 2,3-epoxysqualene--lanosterol cyclase"	LSS	"Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus."	EC 5.4.99.7	1W6K; 1W6J	MTEGTCLRRRGGPYKTEPATDLGRWRLNCERGRQTWTYLQDERAGREQTGLEAYALGLDTKNYFKDLPKAHTAFEGALNGMTFYVGLQAEDGHWTGDYGGPLFLLPGLLITCHVARIPLPAGYREEIVRYLRSVQLPDGGWGLHIEDKSTVFGTALNYVSLRILGVGPDDPDLVRARNILHKKGGAVAIPSWGKFWLAVLNVYSWEGLNTLFPEMWLFPDWAPAHPSTLWCHCRQVYLPMSYCYAVRLSAAEDPLVQSLRQELYVEDFASIDWLAQRNNVAPDELYTPHSWLLRVVYALLNLYEHHHSAHLRQRAVQKLYEHIVADDRFTKSISIGPISKTINMLVRWYVDGPASTAFQEHVSRIPDYLWMGLDGMKMQGTNGSQIWDTAFAIQALLEAGGHHRPEFSSCLQKAHEFLRLSQVPDNPPDYQKYYRQMRKGGFSFSTLDCGWIVSDCTAEALKAVLLLQEKCPHVTEHIPRERLCDAVAVLLNMRNPDGGFATYETKRGGHLLELLNPSEVFGDIMIDYTYVECTSAVMQALKYFHKRFPEHRAAEIRETLTQGLEFCRRQQRADGSWEGSWGVCFTYGTWFGLEAFACMGQTYRDGTACAEVSRACDFLLSRQMADGGWGEDFESCEERRYLQSAQSQIHNTCWAMMGLMAVRHPDIEAQERGVRCLLEKQLPNGDWPQENIAGVFNKSCAISYTSYRNIFPIWALGRFSQLYPERALAGHP	Literature-reported	"Effects of a novel 2,3-oxidosqualene cyclase inhibitor on the regulation of cholesterol biosynthesis in HepG2 cells. J Lipid Res. 1996 Jan;37(1):148-58."	2	.	.	.	.	.	.	.	.	.	.	hsa00100:Steroid biosynthesis; hsa01100:Metabolic pathways; hsa01130:Biosynthesis of antibiotics	R-HSA-191273:Cholesterol biosynthesis; R-HSA-2426168:Activation of gene expression by SREBF (SREBP)	MetaCyc:HS08480-MON	.
TTM6Y9J	Lanosterol synthase	.	LSS_HUMAN	Single Protein	"Oxidosqualene--lanosterol cyclase; 2,3-epoxysqualene--lanosterol cyclase; OSC; hOSC"	LSS	"Key enzyme in the cholesterol biosynthesis pathway. Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus. Through the production of lanosterol may regulate lens protein aggregation and increase transparency."	.	.	MTEGTCLRRRGGPYKTEPATDLGRWRLNCERGRQTWTYLQDERAGREQTGLEAYALGLDTKNYFKDLPKAHTAFEGALNGMTFYVGLQAEDGHWTGDYGGPLFLLPGLLITCHVARIPLPAGYREEIVRYLRSVQLPDGGWGLHIEDKSTVFGTALNYVSLRILGVGPDDPDLVRARNILHKKGGAVAIPSWGKFWLAVLNVYSWEGLNTLFPEMWLFPDWAPAHPSTLWCHCRQVYLPMSYCYAVRLSAAEDPLVQSLRQELYVEDFASIDWLAQRNNVAPDELYTPHSWLLRVVYALLNLYEHHHSAHLRQRAVQKLYEHIVADDRFTKSISIGPISKTINMLVRWYVDGPASTAFQEHVSRIPDYLWMGLDGMKMQGTNGSQIWDTAFAIQALLEAGGHHRPEFSSCLQKAHEFLRLSQVPDNPPDYQKYYRQMRKGGFSFSTLDCGWIVSDCTAEALKAVLLLQEKCPHVTEHIPRERLCDAVAVLLNMRNPDGGFATYETKRGGHLLELLNPSEVFGDIMIDYTYVECTSAVMQALKYFHKRFPEHRAAEIRETLTQGLEFCRRQQRADGSWEGSWGVCFTYGTWFGLEAFACMGQTYRDGTACAEVSRACDFLLSRQMADGGWGEDFESCEERRYLQSAQSQIHNTCWAMMGLMAVRHPDIEAQERGVRCLLEKQLPNGDWPQENIAGVFNKSCAISYTSYRNIFPIWALGRFSQLYPERALAGHP	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P48449
TTP73TM	Lymphotoxin-alpha (LTA)	P01374	TNFB_HUMAN	Cytokine: tumor necrosis factor	Tumor necrosis factor ligand superfamily member 1; TNFSF1; TNFB; TNF-beta; LT-alpha	LTA	"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."	.	4MXW; 4MXV; 1TNR	MTPPERLFLPRVCGTTLHLLLLGLLLVLLPGAQGLPGVGLTPSAAQTARQHPKMHLAHSTLKPAAHLIGDPSKQNSLLWRANTDRAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHEVQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTHTDGIPHLVLSPSTVFFGAFAL	Clinical trial	"Clinical pipeline report, company report or official report of Genentech (2011)."	21	Cytokine	Cytokine: tumor necrosis factor	tumor necrosis factor family.	.	.	TNF(Tumour Necrosis Factor) family 	PF00229	PF00229; TNF	.	.	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	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	.	P01374
TTXZEAJ	Leukotriene A-4 hydrolase (LTA4H)	P09960	LKHA4_HUMAN	Ether bond hydrolase	Leukotriene A4 hydrolase; Leukotriene A(4)Leukotriene A-4 hydrolase hydrolase; Leukotriene A(4) hydrolase; LTA4; LTA-H; LTA-4hydrolase; LTA-4 hydrolase	LTA4H	Has also aminopeptidase activity. Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4.	EC 3.3.2.6	6END; 6ENC; 6ENB; 5NIE; 5NID	MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAMLVGKDLKVD	Successful	DrugBank 3.0: a comprehensive resource for 'omics' research on drugs. Nucleic Acids Res. 2011 Jan;39(Database issue):D1035-41.	34	EC:3.3	.	peptidase M1 family.	3.3.2.6	Acting on ether bonds	"Leukotriene A4 hydrolase, C-terminal; Peptidase family M1 domain"	PF09127; PF01433	PF09127; Leuk-A4-hydro_C; PF01433; Peptidase_M1	.	.	hsa00590:Arachidonic acid metabolism; hsa01100:Metabolic pathways	R-HSA-2142691: Synthesis of Leukotrienes (LT) and Eoxins (EX); R-HSA-6798695: Neutrophil degranulation; R-HSA-9018676: Biosynthesis of D-series resolvins; R-HSA-9018681: Biosynthesis of protectins; R-HSA-9018896: Biosynthesis of E-series 18(S)-resolvins; R-HSA-9020265: Biosynthesis of aspirin-triggered D-series resolvins; R-HSA-9023661: Biosynthesis of E-series 18(R)-resolvins	MetaCyc:HS03372-MON	P09960
TTHQ6US	Lymphotoxin-beta (LTB)	Q06643	TNFC_HUMAN	Cytokine: tumor necrosis factor	Tumor necrosis factor ligand superfamily member 3; Tumor necrosis factor C; TNF-C; LTB; LT-beta	LTB	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.	.	4MXW	MGALGLEGRGGRLQGRGSLLLAVAGATSLVTLLLAVPITVLAVLALVPQDQGGLVTETADPGAQAQQGLGFQKLPEEEPETDLSPGLPAAHLIGAPLKGQGLGWETTKEQAFLTSGTQFSDAEGLALPQDGLYYLYCLVGYRGRAPPGGGDPQGRSVTLRSSLYRAGGAYGPGTPELLLEGAETVTPVLDPARRQGYGPLWYTSVGFGGLVQLRRGERVYVNISHPDMVDFARGKTFFGAVMVG	Literature-reported	Expression of lymphotoxin-beta (LT-beta) in chronic inflammatory conditions. J Pathol. 2003 Jan;199(1):115-21.	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04064: NF-kappa B signaling pathway; hsa05323: Rheumatoid arthritis	R-HSA-5668541: TNFR2 non-canonical NF-kB pathway; R-HSA-5676594: TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway	.	Q06643
TTN53ZF	Leukotriene B4 receptor 1 (LTB4R)	Q15722	LT4R1_HUMAN	GPCR rhodopsin	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	LTB4R	"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."	.	.	MNTTSSAAPPSLGVEFISLLAIILLSVALAVGLPGNSFVVWSILKRMQKRSVTALMVLNLALADLAVLLTAPFFLHFLAQGTWSFGLAGCRLCHYVCGVSMYASVLLITAMSLDRSLAVARPFVSQKLRTKAMARRVLAGIWVLSFLLATPVLAYRTVVPWKTNMSLCFPRYPSEGHRAFHLIFEAVTGFLLPFLAVVASYSDIGRRLQARRFRRSRRTGRLVVLIILTFAAFWLPYHVVNLAEAGRALAGQAAGLGLVGKRLSLARNVLIALAFLSSSVNPVLYACAGGGLLRSAGVGFVAKLLEGTGSEASSTRRGGSLGQTARSGPAALEPGPSESLTASSPLKLNELN	Clinical trial	"LTB4 promotes insulin resistance in obese mice by acting on macrophages, hepatocytes and myocytes. Nat Med. 2015 Mar;21(3):239-47."	21	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.13.5	The G-protein-coupled receptor (GPCR) Family	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-391906:Leukotriene receptors; R-HSA-416476:G alpha (q) signalling events	.	Q15722
TTVJX54	Leukotriene B4 receptor 2 (LTB4R2)	Q9NPC1	LT4R2_HUMAN	GPCR rhodopsin	Seven transmembrane receptor BLTR2; Leukotriene B4 receptor BLT2; Leukotriene B(4) receptor BLT2; LTB4-R2; LTB4-R 2; LTB4 receptor JULF2; BLTR2; BLT2R	LTB4R2	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.	.	.	MSVCYRPPGNETLLSWKTSRATGTAFLLLAALLGLPGNGFVVWSLAGWRPARGRPLAATLVLHLALADGAVLLLTPLFVAFLTRQAWPLGQAGCKAVYYVCALSMYASVLLTGLLSLQRCLAVTRPFLAPRLRSPALARRLLLAVWLAALLLAVPAAVYRHLWRDRVCQLCHPSPVHAAAHLSLETLTAFVLPFGLMLGCYSVTLARLRGARWGSGRHGARVGRLVSAIVLAFGLLWAPYHAVNLLQAVAALAPPEGALAKLGGAGQAARAGTTALAFFSSSVNPVLYVFTAGDLLPRAGPRFLTRLFEGSGEARGGGRSREGTMELRTTPQLKVVGQGRGNGDPGGGMEKDGPEWDL	Clinical trial	"Diaryl ether/carboxylic acid derivatives of LY255283: Receptor antagonists of leukotriene B4, Bioorg. Med. Chem. Lett. 3(10):1985-1990 (1993)."	21	PF00001	.	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction	R-HSA-391906:Leukotriene receptors; R-HSA-416476:G alpha (q) signalling events	.	Q9NPC1
TTFO0PM	Lymphotoxin beta receptor (LTBR)	P36941	TNR3_HUMAN	Cytokine receptor	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	LTBR	"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."	.	4MXW; 1RF3	MLLPWATSAPGLAWGPLVLGLFGLLAASQPQAVPPYASENQTCRDQEKEYYEPQHRICCSRCPPGTYVSAKCSRIRDTVCATCAENSYNEHWNYLTICQLCRPCDPVMGLEEIAPCTSKRKTQCRCQPGMFCAAWALECTHCELLSDCPPGTEAELKDEVGKGNNHCVPCKAGHFQNTSSPSARCQPHTRCENQGLVEAAPGTAQSDTTCKNPLEPLPPEMSGTMLMLAVLLPLAFFLLLATVFSCIWKSHPSLCRKLGSLLKRRPQGEGPNPVAGSWEPPKAHPYFPDLVQPLLPISGDVSPVSTGLPAAPVLEAGVPQQQSPLDLTREPQLEPGEQSQVAHGTNGIHVTGGSMTITGNIYIYNGPVLGGPPGPGDLPATPEPPYPIPEEGDPGPPGLSTPHQEDGKAWHLAETEHCGATPSNRGPRNQFITHD	Clinical trial	ClinicalTrials.gov (NCT01552681) Baminercept in Sj ren's Syndrome. U.S. National Institutes of Health.	21	Cytokine receptor	Cytokine receptor	.	.	.	TNFR/NGFR cysteine-rich region	PF00020	PF00020; TNFR_c6	.	.	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	R-HSA-5668541:TNFR2 non-canonical NF-kB pathway; R-HSA-5676594:TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway	.	P36941
TTW7OTG	Leukotriene C4 synthase (LTC4S)	Q16873	LTC4S_HUMAN	Carbon-sulfur lyase	Leukotriene-C(4)Leukotriene C4 synthase synthase; Leukotriene-C(4) synthase; LTC4 synthase	LTC4S	Catalyzes the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4.	EC 4.4.1.20	5HV9; 4WAB; 4JRZ; 4JCZ; 4JC7	MKDEVALLAAVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERVYRAQVNCSEYFPLFLATLWVAGIFFHEGAAALCGLVYLFARLRYFQGYARSAQLRLAPLYASARALWLLVALAALGLLAHFLPAALRAALLGRLRTLLPWA	Patented-recorded	Leukotriene C4 synthase: a candidate gene for the aspirin-intolerant asthmatic phenotype. Allergy Asthma Proc. 1999 Nov-Dec;20(6):353-60.	.	EC:4.4	Carbon-sulfur lyases	MAPEG family.	4.4.1.20	Carbon-sulfur lyases	MAPEG family	PF01124	PF01124; MAPEG	.	.	hsa00590: Arachidonic acid metabolism; hsa01100: Metabolic pathways	R-HSA-2142688: Synthesis of 5-eicosatetraenoic acids; R-HSA-2142691: Synthesis of Leukotrienes (LT) and Eoxins (EX); R-HSA-2142700: Synthesis of Lipoxins (LX); R-HSA-9026762: Biosynthesis of maresin conjugates in tissue regeneration (MCTR); R-HSA-9026766: Biosynthesis of protectin and resolvin conjugates in tissue regeneration (PCTR and RCTR)	MetaCyc:HS08566-MON	Q16873
TTSZDQU	Lactotransferrin (LTF)	P02788	TRFL_HUMAN	Transferrin	Talalactoferrin; Lactoferrin; LF; Growth-inhibiting protein 12; GIG12	LTF	"Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate."	EC 3.4.21.-	2PMS; 2HD4; 2GMD; 2GMC; 2DP4	MKLVFLVLLFLGALGLCLAGRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAARRARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRKPVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNLLFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRK	Clinical trial	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	31	Transferrin	Peptidase	transferrin family.	3.4.21.-	Acting on peptide bonds (peptidases)	Transferrin	PF00405	PF00405; Transferrin	.	.	.	R-HSA-1222556:ROS production in response to bacteria; R-HSA-977225:Amyloid formation	.	P02788
TT1JZG6	Leukocyte receptor tyrosine kinase (LTK)	P29376	LTK_HUMAN	Kinase	TYK1; Protein tyrosine kinase 1; Leukocyte tyrosine kinase receptor	LTK	"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."	EC 2.7.10.1	.	MGCWGQLLVWFGAAGAILCSSPGSQETFLRSSPLPLASPSPRDPKVSAPPSILEPASPLNSPGTEGSWLFSTCGASGRHGPTQTQCDGAYAGTSVVVTVGAAGQLRGVQLWRVPGPGQYLISAYGAAGGKGAKNHLSRAHGVFVSAIFSLGLGESLYILVGQQGEDACPGGSPESQLVCLGESRAVEEHAAMDGSEGVPGSRRWAGGGGGGGGATYVFRVRAGELEPLLVAAGGGGRAYLRPRDRGRTQASPEKLENRSEAPGSGGRGGAAGGGGGWTSRAPSPQAGRSLQEGAEGGQGCSEAWATLGWAAAGGFGGGGGACTAGGGGGGYRGGDASETDNLWADGEDGVSFIHPSSELFLQPLAVTENHGEVEIRRHLNCSHCPLRDCQWQAELQLAECLCPEGMELAVDNVTCMDLHKPPGPLVLMVAVVATSTLSLLMVCGVLILVKQKKWQGLQEMRLPSPELELSKLRTSAIRTAPNPYYCQVGLGPAQSWPLPPGVTEVSPANVTLLRALGHGAFGEVYEGLVIGLPGDSSPLQVAIKTLPELCSPQDELDFLMEALIISKFRHQNIVRCVGLSLRATPRLILLELMSGGDMKSFLRHSRPHLGQPSPLVMRDLLQLAQDIAQGCHYLEENHFIHRDIAARNCLLSCAGPSRVAKIGDFGMARDIYRASYYRRGDRALLPVKWMPPEAFLEGIFTSKTDSWSFGVLLWEIFSLGYMPYPGRTNQEVLDFVVGGGRMDPPRGCPGPVYRIMTQCWQHEPELRPSFASILERLQYCTQDPDVLNSLLPMELGPTPEEEGTSGLGNRSLECLRPPQPQELSPEKLKSWGGSPLGPWLSSGLKPLKSRGLQPQNLWNPTYRS	Literature-reported	Design of potent and selective inhibitors to overcome clinical anaplastic lymphoma kinase mutations resistant to crizotinib. J Med Chem.> 2014 Feb 27;57(4):1170-87.	0	EC:2.7	.	protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Protein tyrosine kinase	PF07714	PF07714; Pkinase_Tyr	.	.	.	.	.	P29376
TTINE9B	Lymphocyte antigen 6D (LY6D)	Q14210	LY6D_HUMAN	.	LY6D; E48 antigen; Desmoglein III (dg4)	LY6D	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.	.	.	MRTALLLLAALAVATGPALTLRCHVCTSSSNCKHSVVCPASSRFCKTTNTVEPLRGNLVKKDCAESCTPSYTLQGQVSSGTSSTQCCQEDLCNEKLHNAAPTRTALAHSALSLGLALSLLAVILAPSL	Literature-reported	"The human E48 antigen, highly homologous to the murine Ly-6 antigen ThB, is a GPI-anchored molecule apparently involved in keratinocyte cell-cell a... J Cell Biol. 1995 Jun;129(6):1677-89."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-163125: Post-translational modification: synthesis of GPI-anchored proteins	.	Q14210
TT5GKHN	Lymphocyte antigen 6K (LY6K)	Q17RY6	LY6K_HUMAN	.	Ly-6K; CO16	LY6K	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.	.	.	MALLALLLVVALPRVWTDANLTARQRDPEDSQRTDEGDNRVWCHVCERENTFECQNPRRCKWTEPYCVIAAVKIFPRFFMVAKQCSAGCAAMERPKPEEKRFLLEEPMPFFYLKCCKIRYCNLEGPPINSSVFKEYAGSMGESCGGLWLAILLLLASIAAGLSLS	Literature-reported	"Characterization of the human Ly-6 antigens, the newly annotated member Ly-6K included, as molecular markers for head-and-neck squamous cell carcin... Int J Cancer. 2003 Mar 1;103(6):768-74."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-163125: Post-translational modification: synthesis of GPI-anchored proteins	.	Q17RY6
TTG180Q	Lymphocyte antigen 75 (LY75)	O60449	LY75_HUMAN	C-type lectin	gp200MR6; Ly75; DEC205; Ctype lectin domain family 13 member B; CD205	LY75	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.	.	.	MRTGWATPRRPAGLLMLLFWFFDLAEPSGRAANDPFTIVHGNTGKCIKPVYGWIVADDCDETEDKLWKWVSQHRLFHLHSQKCLGLDITKSVNELRMFSCDSSAMLWWKCEHHSLYGAARYRLALKDGHGTAISNASDVWKKGGSEESLCDQPYHEIYTRDGNSYGRPCEFPFLIDGTWHHDCILDEDHSGPWCATTLNYEYDRKWGICLKPENGCEDNWEKNEQFGSCYQFNTQTALSWKEAYVSCQNQGADLLSINSAAELTYLKEKEGIAKIFWIGLNQLYSARGWEWSDHKPLNFLNWDPDRPSAPTIGGSSCARMDAESGLWQSFSCEAQLPYVCRKPLNNTVELTDVWTYSDTRCDAGWLPNNGFCYLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEDIKEEVWIGLKNINIPTLFQWSDGTEVTLTYWDENEPNVPYNKTPNCVSYLGELGQWKVQSCEEKLKYVCKRKGEKLNDASSDKMCPPDEGWKRHGETCYKIYEDEVPFGTNCNLTITSRFEQEYLNDLMKKYDKSLRKYFWTGLRDVDSCGEYNWATVGGRRRAVTFSNWNFLEPASPGGCVAMSTGKSVGKWEVKDCRSFKALSICKKMSGPLGPEEASPKPDDPCPEGWQSFPASLSCYKVFHAERIVRKRNWEEAERFCQALGAHLSSFSHVDEIKEFLHFLTDQFSGQHWLWIGLNKRSPDLQGSWQWSDRTPVSTIIMPNEFQQDYDIRDCAAVKVFHRPWRRGWHFYDDREFIYLRPFACDTKLEWVCQIPKGRTPKTPDWYNPDRAGIHGPPLIIEGSEYWFVADLHLNYEEAVLYCASNHSFLATITSFVGLKAIKNKIANISGDGQKWWIRISEWPIDDHFTYSRYPWHRFPVTFGEECLYMSAKTWLIDLGKPTDCSTKLPFICEKYNVSSLEKYSPDSAAKVQCSEQWIPFQNKCFLKIKPVSLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPDMEATLWIGLRWTAYEKINKWTDNRELTYSNFHPLLVSGRLRIPENFFEEESRYHCALILNLQKSPFTGTWNFTSCSERHFVSLCQKYSEVKSRQTLQNASETVKYLNNLYKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLSVQALLHNSSLWIGLFSQDDELNFGWSDGKRLHFSRWAETNGQLEDCVVLDTDGFWKTVDCNDNQPGAICYYSGNETEKEVKPVDSVKCPSPVLNTPWIPFQNCCYNFIITKNRHMATTQDEVHTKCQKLNPKSHILSIRDEKENNFVLEQLLYFNYMASWVMLGITYRNKSLMWFDKTPLSYTHWRAGRPTIKNEKFLAGLSTDGFWDIQTFKVIEEAVYFHQHSILACKIEMVDYKEEYNTTLPQFMPYEDGIYSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGFPLWVGLSSHDGSESSFEWSDGSTFDYIPWKGQTSPGNCVLLDPKGTWKHEKCNSVKDGAICYKPTKSKKLSRLTYSSRCPAAKENGSRWIQYKGHCYKSDQALHSFSEAKKLCSKHDHSATIVSIKDEDENKFVSRLMRENNNITMRVWLGLSQHSVDQSWSWLDGSEVTFVKWENKSKSGVGRCSMLIASNETWKKVECEHGFGRVVCKVPLGPDYTAIAIIVATLSILVLMGGLIWFLFQRHRLHLAGFSSVRYAQGVNEDEIMLPSFHD	Clinical trial	"Altered expression and endocytic function of CD205 in human dendritic cells, and detection of a CD205-DCL-1 fusion protein upon dendritic cell matu... Immunology. 2007 Mar;120(3):362-71."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	O60449
TTZCL1U	T-lymphocyte surface antigen Ly-9 (LY9)	Q9HBG7	LY9_HUMAN	.	Signaling lymphocytic activation molecule 3; SLAMF3; SLAM family member 3; Lymphocyte antigen 9; LY9; Cell surface molecule Ly-9	LY9	May participate in adhesion reactions between T lymphocytes and accessory cells by homophilic interaction.	.	.	MVAPKSHTDDWAPGPFSSKPQRSQLQIFSSVLQTSLLFLLMGLRASGKDSAPTVVSGILGGSVTLPLNISVDTEIENVIWIGPKNALAFARPKENVTIMVKSYLGRLDITKWSYSLCISNLTLNDAGSYKAQINQRNFEVTTEEEFTLFVYEQLQEPQVTMKSVKVSENFSCNITLMCSVKGAEKSVLYSWTPREPHASESNGGSILTVSRTPCDPDLPYICTAQNPVSQRSSLPVHVGQFCTDPGASRGGTTGETVVGVLGEPVTLPLALPACRDTEKVVWLFNTSIISKEREEAATADPLIKSRDPYKNRVWVSSQDCSLKISQLKIEDAGPYHAYVCSEASSVTSMTHVTLLIYRRLRKPKITWSLRHSEDGICRISLTCSVEDGGNTVMYTWTPLQKEAVVSQGESHLNVSWRSSENHPNLTCTASNPVSRSSHQFLSENICSGPERNTKLWIGLFLMVCLLCVGIFSWCIWKRKGRCSVPAFCSSQAEAPADTPEPTAGHTLYSVLSQGYEKLDTPLRPARQQPTPTSDSSSDSNLTTEEDEDRPEVHKPISGRYEVFDQVTQEGAGHDPAPEGQADYDPVTPYVTEVESVVGENTMYAQVFNLQGKTPVSQKEESSATIYCSIRKPQVVPPPQQNDLEIPESPTYENFT	Literature-reported	Ly9 (CD229) Cell-Surface Receptor is Crucial for the Development of Spontaneous Autoantibody Production to Nuclear Antigens. Front Immunol. 2013 Jul 31;4:225.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9HBG7
TT8S9AV	Lymphocyte antigen 96 (LY96)	Q9Y6Y9	LY96_HUMAN	.	MD-2 protein; MD-2; LY96; ESOP-1	LY96	"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."	.	4G8A; 3ULA; 3FXI; 2Z65; 2.00E+59	MLPFLFFSTLFSSIFTEAQKQYWVCNSSDASISYTYCDKMQYPISINVNPCIELKRSKGLLHIFYIPRRDLKQLYFNLYITVNTMNLPKRKEVICRGSDDDYSFCRALKGETVNTTISFSFKGIKFSKGKYKCVVEAISGSPEEMLFCLEFVILHQPNSN	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	hsa04064:NF-kappa B signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa05130:Pathogenic Escherichia coli infection; hsa05133:Pertussis; hsa05145:Toxoplasmosis	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	.	Q9Y6Y9
TT1RWNJ	Tyrosine-protein kinase Lyn (JTK8)	P07948	LYN_HUMAN	Kinase	p56Lyn; p53Lyn; V-yes-1 Yamaguchi sarcoma viral related oncogene homolog; Lck/Yes-related novel protein tyrosine kinase	LYN	"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."	EC 2.7.10.2	6NMW; 5XY1; 3A4O; 1WA7; 1W1F	MGCIKSKGKDSLSDDGVDLKTQPVRNTERTIYVRDPTSNKQQRPVPESQLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDFDPVHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQADGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKRLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTREEPIYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMTALSQGYRMPRVENCPDELYDIMKMCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQQP	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	21	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. SRC subfamily.	2.7.10.2	Transferring phosphorus-containing groups	Protein tyrosine kinase; SH2 domain; SH3 domain	PF07714; PF00017; PF00018	PF07714; Pkinase_Tyr; PF00017; SH2; PF00018; SH3_1	.	.	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	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	.	P07948
TTG8DNU	Hyaluronic acid receptor (LYVE1)	Q9Y5Y7	LYVE1_HUMAN	.	Lymphatic vessel endothelial hyaluronic acid receptor 1; LYVE1; Extracellular link domaincontaining protein 1; Cell surface retention sequencebindingprotein 1; CRSBP1	LYVE1	"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."	.	.	MARCFSLVLLLTSIWTTRLLVQGSLRAEELSIQVSCRIMGITLVSKKANQQLNFTEAKEACRLLGLSLAGKDQVETALKASFETCSYGWVGDGFVVISRISPNPKCGKNGVGVLIWKVPVSRQFAAYCYNSSDTWTNSCIPEIITTKDPIFNTQTATQTTEFIVSDSTYSVASPYSTIPAPTTTPPAPASTSIPRRKKLICVTEVFMETSTMSTETEPFVENKAAFKNEAAGFGGVPTALLVLALLFFGAAAGLGFCYVKRYVKAFPFTNKNQQKEMIETKVVKEEKANDSNPNEESKKTDKNPEESKSPSKTTVRCLEAEV	Successful	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Ligand id: 4954).	34	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2160916:Hyaluronan uptake and degradation	.	Q9Y5Y7
TTAOZBW	Lysozyme (LYZ)	P61626	LYSC_HUMAN	Glycosylase	"Lysozyme C; LYZ; 1,4betaNacetylmuramidase C"	LYZ	Lysozymes have primarily a bacteriolytic function; those intissues and body fluids are associated with the monocyte- macrophage system and enhance the activity of immunoagents.	EC 3.2.1.17	5LVK; 5LSH; 4R0P; 4ML7; 4I0C	MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDVRQYVQGCGV	Literature-reported	Protective properties of lysozyme on -amyloid pathology: implications for Alzheimer disease. Neurobiol Dis. 2015 Nov;83:122-33.	.	.	.	.	.	.	.	.	.	.	.	hsa04970: Salivary secretion	R-HSA-6798695: Neutrophil degranulation; R-HSA-6803157: Antimicrobial peptides; R-HSA-977225: Amyloid fiber formation	.	P61626
TT95ICL	Mannose-6-phosphate receptor (M6PR)	P20645	MPRD_HUMAN	Mannose 6-phosphate receptor	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	M6PR	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.	.	1JUQ	MFPFYSCWRTGLLLLLLAVAVRESWQTEEKTCDLVGEKGKESEKELALVKRLKPLFNKSFESTVGQGSDTYIYIFRVCREAGNHTSGAGLVQINKSNGKETVVGRLNETHIFNGSNWIMLIYKGGDEYDNHCGKEQRRAVVMISCNRHTLADNFNPVSEERGKVQDCFYLFEMDSSLACSPEISHLSVGSILLVTFASLVAVYVVGGFLYQRLVVGAKGMEQFPHLAFWQDLGNLVADGCDFVCRSKPRNVPAAYRGVGDDQLGEESEERDDHLLPM	Successful	Early treatment with alglucosidase alpha prolongs long-term survival of infants with Pompe disease. Pediatr Res. 2009 Sep;66(3):329-35.	34	TC=9.B.247	.	.	.	.	Mannose-6-phosphate receptor	PF02157	PF02157; Man-6-P_recep	9.B.247.1.1	The Mannose 6-Phosphate Receptor (M6PR) Family	hsa04142:Lysosome; hsa04145:Phagosome	R-HSA-432720:Lysosome Vesicle Biogenesis	.	P20645
TTNE9U7	Mitotic checkpoint protein (MAD1L1)	Q9UNH0	MD1L1_HUMAN	.	"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"	MAD1L1	"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."	.	4DZO; 1GO4	MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLIQVEREKMQMELSHKRARVELERAASTSARNYEREVDRNQELLTRIRQLQEREAGAEEKMQEQLERNRQCQQNLDAASKRLREKEDSLAQAGETINALKGRISELQWSVMDQEMRVKRLESEKQELQEQLDLQHKKCQEANQKIQELQASQEARADHEQQIKDLEQKLSLQEQDAAIVKNMKSELVRLPRLERELKQLREESAHLREMRETNGLLQEELEGLQRKLGRQEKMQETLVGLELENERLLAKLQSWERLDQTMGLSIRTPEDLSRFVVELQQRELALKDKNSAVTSSARGLEKARQQLQEELRQVSGQLLEERKKRETHEALARRLQKRVLLLTKERDGMRAILGSYDSELTPAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEADTLRLKVEELEGERSRLEEEKRMLEAQLERRALQGDYDQSRTKVLHMSLNPTSVARQRLREDHSQLQAECERLRGLLRAMERGGTVPADLEAAAASLPSSKEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITTENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRRQDSIPAFLSSLTLELFSRQTVA	Literature-reported	"Search for in vivo somatic mutations in the mitotic checkpoint gene, hMAD1, in human lung cancers. Oncogene. 1999 Nov 25;18(50):7180-3."	.	.	.	MAD1 family.	.	.	Mitotic checkpoint protein	PF05557	PF05557; MAD	.	.	.	.	.	Q9Y6D9
TTBD6I7	Mucosal addressin cell adhesion molecule 1 (MADCAM1)	Q13477	MADCA_HUMAN	.	hMAdCAM-1; MAdCAM-1; MADCAM1	MADCAM1	"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."	.	4HD9; 4HCR; 4HC1; 4HBQ; 1GSM	MDFGLALLLAGLLGLLLGQSLQVKPLQVEPPEPVVAVALGASRQLTCRLACADRGASVQWRGLDTSLGAVQSDTGRSVLTVRNASLSAAGTRVCVGSCGGRTFQHTVQLLVYAFPDQLTVSPAALVPGDPEVACTAHKVTPVDPNALSFSLLVGGQELEGAQALGPEVQEEEEEPQGDEDVLFRVTERWRLPPLGTPVPPALYCQATMRLPGLELSHRQAIPVLHSPTSPEPPDTTSPESPDTTSPESPDTTSQEPPDTTSPEPPDKTSPEPAPQQGSTHTPRSPGSTRTRRPEISQAGPTQGEVIPTGSSKPAGDQLPAALWTSSAVLGLLLLALPTYHLWKRCRHLAEDDTHPPASLRLLPQVSAWAGLRGTGQVGISPS	Clinical trial	Emerging drugs to treat Crohn's disease. Expert Opin Emerg Drugs. 2007 Mar;12(1):49-59.	21	.	.	.	.	.	.	.	.	.	.	hsa04514:Cell adhesion molecules (CAMs); hsa04672:Intestinal immune network for IgA production	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell; R-HSA-216083: Integrin cell surface interactions	.	Q13477
TT9XFON	Myelin-associated glycoprotein (MAG)	P20916	MAG_HUMAN	Immunoglobulin	MAG	MAG	"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."	.	.	MIFLTALPLFWIMISASRGGHWGAWMPSSISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSNVSPELGGKYYFRGDLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPAVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQASFPNTTLQFEGYASMDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGTVLREAVAESLLLELEEVTPAEDGVYACLAENAYGQDNRTVGLSVMYAPWKPTVNGTMVAVEGETVSILCSTQSNPDPILTIFKEKQILSTVIYESELQLELPAVSPEDDGEYWCVAENQYGQRATAFNLSVEFAPVLLLESHCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNESEREFVYSERSGLVLTSILTLRGQAQAPPRVICTARNLYGAKSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKKNVTESPSFSAGDNPPVLFSSDFRISGAPEKYESERRLGSERRLLGLRGEPPELDLSYSHSDLGKRPTKDSYTLTEELAEYAEIRVK	Clinical trial	"First-time-in-human study with GSK249320, a myelin-associated glycoprotein inhibitor, in healthy volunteers. Clin Pharmacol Ther. 2013 Feb;93(2):163-9."	21	.	.	.	.	.	.	.	.	.	.	hsa04514: Cell adhesion molecules	R-HSA-193634: Axonal growth inhibition (RHOA activation); R-HSA-210991: Basigin interactions; R-HSA-9619665: EGR2 and SOX10-mediated initiation of Schwann cell myelination	.	P20916
TT63M7Q	Melanoma-associated antigen 1 (MAGEA1)	P43355	MAGA1_HUMAN	Melanoma associated antigen	Melanomaassociated antigen 1; MAGE1A; MAGE1 antigen; MAGE1; MAGE-1 antigen; Cancer/testis antigen 1.1; CT1.1; Antigen MZ2E; Antigen MZ2-E	MAGEA1	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.	.	3BO8; 1W72	MSLEQRSLHCKPEEALEAQQEALGLVCVQAATSSSSPLVLGTLEEVPTAGSTDPPQSPQGASAFPTTINFTRQRQPSEGSSSREEEGPSTSCILESLFRAVITKKVADLVGFLLLKYRAREPVTKAEMLESVIKNYKHCFPEIFGKASESLQLVFGIDVKEADPTGHSYVLVTCLGLSYDGLLGDNQIMPKTGFLIIVLVMIAMEGGHAPEEEIWEELSVMEVYDGREHSAYGEPRKLLTQDLVQEKYLEYRQVPDSDPARYEFLWGPRALAETSYVKVLEYVIKVSARVRFFFPSLREAALREEEEGV	Clinical trial	ClinicalTrials.gov (NCT03356808) Antigen-specific T Cells Against Lung Cancer	19	Melanoma associated antigen	Melanoma associated protein	.	.	.	MAGE family; Melanoma associated antigen family N terminal 	PF01454; PF12440	PF01454; MAGE; PF12440; MAGE_N	.	.	.	.	.	P43355
TT1VNVM	Melanoma-associated antigen 10 (MAGEA10)	P43363	MAGAA_HUMAN	.	Cancer/testis antigen 1.10; CT1.10; MAGE-10 antigen	MAGEA10	"Not known, though may play a role in embryonal development and tumor transformation or aspects of tumor progression."	.	7PBC;7PDW;7QPJ	MPRAPKRQRCMPEEDLQSQSETQGLEGAQAPLAVEEDASSSTSTSSSFPSSFPSSSSSSSSSCYPLIPSTPEEVSADDETPNPPQSAQIACSSPSVVASLPLDQSDEGSSSQKEESPSTLQVLPDSESLPRSEIDEKVTDLVQFLLFKYQMKEPITKAEILESVIRNYEDHFPLLFSEASECMLLVFGIDVKEVDPTGHSFVLVTSLGLTYDGMLSDVQSMPKTGILILILSIVFIEGYCTPEEVIWEALNMMGLYDGMEHLIYGEPRKLLTQDWVQENYLEYRQVPGSDPARYEFLWGPRAHAEIRKMSLLKFLAKVNGSDPRSFPLWYEEALKDEEERAQDRIATTDDTTAMASASSSATGSFSYPE	Clinical trial	Phase I clinical trial evaluating the safety and efficacy of ADP-A2M10 SPEAR T cells in patients with MAGE-A10(+) advanced non-small cell lung cancer. J Immunother Cancer. 2022 Jan;10(1):e003581.	.	.	.	.	.	.	.	.	.	.	.	hsa:4109	.	.	P43363;
TTOZT28	Melanoma-associated antigen 2 (MAGEA2)	P43356	MAGA2_HUMAN	.	MAGEA2B; MAGEA2A; MAGE2; MAGE-2 antigen; Cancer/testis antigen 1.2; CT1.2	MAGEA2	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.	.	.	MPLEQRSQHCKPEEGLEARGEALGLVGAQAPATEEQQTASSSSTLVEVTLGEVPAADSPSPPHSPQGASSFSTTINYTLWRQSDEGSSNQEEEGPRMFPDLESEFQAAISRKMVELVHFLLLKYRAREPVTKAEMLESVLRNCQDFFPVIFSKASEYLQLVFGIEVVEVVPISHLYILVTCLGLSYDGLLGDNQVMPKTGLLIIVLAIIAIEGDCAPEEKIWEELSMLEVFEGREDSVFAHPRKLLMQDLVQENYLEYRQVPGSDPACYEFLWGPRALIETSYVKVLHHTLKIGGEPHISYPPLHERALREGEE	Literature-reported	Overexpression of MAGEA2 has a prognostic significance and is a potential therapeutic target for patients with lung cancer. Int J Oncol. 2017 Jun;50(6):2154-2170.	.	.	.	.	.	.	MAGE family; Melanoma associated antigen family N terminal 	PF01454; PF12440	PF01454; MAGE; PF12440; MAGE_N	.	.	.	.	.	P43356
TTWSKHD	Melanoma-associated antigen 3 (MAGEA3)	P43357	MAGA3_HUMAN	Melanoma associated antigen	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	MAGEA3	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.	.	5BRZ; 4V0P; 1QEW	MPLEQRSQHCKPEEGLEARGEALGLVGAQAPATEEQEAASSSSTLVEVTLGEVPAAESPDPPQSPQGASSLPTTMNYPLWSQSYEDSSNQEEEGPSTFPDLESEFQAALSRKVAELVHFLLLKYRAREPVTKAEMLGSVVGNWQYFFPVIFSKASSSLQLVFGIELMEVDPIGHLYIFATCLGLSYDGLLGDNQIMPKAGLLIIVLAIIAREGDCAPEEKIWEELSVLEVFEGREDSILGDPKKLLTQHFVQENYLEYRQVPGSDPACYEFLWGPRALVETSYVKVLHHMVKISGGPHISYPPLHEWVLREGEE	Clinical trial	National Cancer Institute Drug Dictionary (drug id 600553).	25	Melanoma associated antigen	Melanoma associated antigen family	.	.	.	MAGE family; Melanoma associated antigen family N terminal 	PF01454; PF12440	PF01454; MAGE; PF12440; MAGE_N	.	.	.	.	.	P43357
TT9EQUY	Melanoma-associated antigen 4 (MAGEA4)	P43358	MAGA4_HUMAN	Melanoma associated antigen	MAGE4; MAGE-X2 antigen; MAGE-X2; MAGE-41 antigen; MAGE-41; MAGE-4 protein; MAGE-4 antigen; Cancer/testis antigen 1.4; CT1.4	MAGEA4	"Not known, though may play a role in embryonal development and tumor transformation or aspects of tumor progression."	.	2WA0; 1I4F	MSSEQKSQHCKPEEGVEAQEEALGLVGAQAPTTEEQEAAVSSSSPLVPGTLEEVPAAESAGPPQSPQGASALPTTISFTCWRQPNEGSSSQEEEGPSTSPDAESLFREALSNKVDELAHFLLRKYRAKELVTKAEMLERVIKNYKRCFPVIFGKASESLKMIFGIDVKEVDPASNTYTLVTCLGLSYDGLLGNNQIFPKTGLLIIVLGTIAMEGDSASEEEIWEELGVMGVYDGREHTVYGEPRKLLTQDWVQENYLEYRQVPGSNPARYEFLWGPRALAETSYVKVLEHVVRVNARVRIAYPSLREAALLEEEEGV	Clinical trial	ClinicalTrials.gov (NCT03356808) Antigen-specific T Cells Against Lung Cancer	19	Melanoma associated antigen	Melanoma associated antigen family	.	.	.	MAGE family; Melanoma associated antigen family N terminal 	PF01454; PF12440	PF01454; MAGE; PF12440; MAGE_N	.	.	.	.	.	P43358
TTJIWMO	Melanoma-associated antigen 6 (MAGEA6)	P43360	MAGA6_HUMAN	.	Cancer/testis antigen 1.6; CT1.6; MAGE-6 antigen; MAGE3B antigen	MAGEA6	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.	.	.	MPLEQRSQHCKPEEGLEARGEALGLVGAQAPATEEQEAASSSSTLVEVTLGEVPAAESPDPPQSPQGASSLPTTMNYPLWSQSYEDSSNQEEEGPSTFPDLESEFQAALSRKVAKLVHFLLLKYRAREPVTKAEMLGSVVGNWQYFFPVIFSKASDSLQLVFGIELMEVDPIGHVYIFATCLGLSYDGLLGDNQIMPKTGFLIIILAIIAKEGDCAPEEKIWEELSVLEVFEGREDSIFGDPKKLLTQYFVQENYLEYRQVPGSDPACYEFLWGPRALIETSYVKVLHHMVKISGGPRISYPLLHEWALREGEE	Clinical trial	ClinicalTrials.gov (NCT03139370) Safety and Efficacy of MAGE-A3/A6 T Cell Receptor Engineered T Cells (KITE-718) in HLA-DPB1*04:01 Positive Adults With Advanced Cancers. U.S. National Institutes of Health.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P43360
TT9M6NA	Cancer/testis antigen MAGE-C1/CT7 (MAGEC1)	O60732	MAGC1_HUMAN	Melanoma associated antigen family	Melanoma-associated antigen C1; MAGE-C1 antigen; Cancer/testis antigen 7.1; CT7.1	MAGEC1	Tumor antigen.	.	.	MGDKDMPTAGMPSLLQSSSESPQSCPEGEDSQSPLQIPQSSPESDDTLYPLQSPQSRSEGEDSSDPLQRPPEGKDSQSPLQIPQSSPEGDDTQSPLQNSQSSPEGKDSLSPLEISQSPPEGEDVQSPLQNPASSFFSSALLSIFQSSPESTQSPFEGFPQSVLQIPVSAASSSTLVSIFQSSPESTQSPFEGFPQSPLQIPVSRSFSSTLLSIFQSSPERTQSTFEGFAQSPLQIPVSPSSSSTLLSLFQSFSERTQSTFEGFAQSSLQIPVSPSFSSTLVSLFQSSPERTQSTFEGFPQSPLQIPVSSSSSSTLLSLFQSSPERTHSTFEGFPQSLLQIPMTSSFSSTLLSIFQSSPESAQSTFEGFPQSPLQIPGSPSFSSTLLSLFQSSPERTHSTFEGFPQSPLQIPMTSSFSSTLLSILQSSPESAQSAFEGFPQSPLQIPVSSSFSYTLLSLFQSSPERTHSTFEGFPQSPLQIPVSSSSSSSTLLSLFQSSPECTQSTFEGFPQSPLQIPQSPPEGENTHSPLQIVPSLPEWEDSLSPHYFPQSPPQGEDSLSPHYFPQSPPQGEDSLSPHYFPQSPQGEDSLSPHYFPQSPPQGEDSMSPLYFPQSPLQGEEFQSSLQSPVSICSSSTPSSLPQSFPESSQSPPEGPVQSPLHSPQSPPEGMHSQSPLQSPESAPEGEDSLSPLQIPQSPLEGEDSLSSLHFPQSPPEWEDSLSPLHFPQFPPQGEDFQSSLQSPVSICSSSTSLSLPQSFPESPQSPPEGPAQSPLQRPVSSFFSYTLASLLQSSHESPQSPPEGPAQSPLQSPVSSFPSSTSSSLSQSSPVSSFPSSTSSSLSKSSPESPLQSPVISFSSSTSLSPFSEESSSPVDEYTSSSDTLLESDSLTDSESLIESEPLFTYTLDEKVDELARFLLLKYQVKQPITKAEMLTNVISRYTGYFPVIFRKAREFIEILFGISLREVDPDDSYVFVNTLDLTSEGCLSDEQGMSQNRLLILILSIIFIKGTYASEEVIWDVLSGIGVRAGREHFAFGEPRELLTKVWVQEHYLEYREVPNSSPPRYEFLWGPRAHSEVIKRKVVEFLAMLKNTVPITFPSSYKDALKDVEERAQAIIDTTDDSTATESASSSVMSPSFSSE	Clinical trial	National Cancer Institute Drug Dictionary (drug id 648549).	19	.	.	.	.	.	.	.	.	.	.	.	.	.	O60732
TTKGUEB	Melanoma-associated antigen C2 (MAGEC2)	Q9UBF1	MAGC2_HUMAN	Melanoma associated antigen	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	MAGEC2	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.	.	.	MPPVPGVPFRNVDNDSPTSVELEDWVDAQHPTDEEEEEASSASSTLYLVFSPSSFSTSSSLILGGPEEEEVPSGVIPNLTESIPSSPPQGPPQGPSQSPLSSCCSSFSWSSFSEESSSQKGEDTGTCQGLPDSESSFTYTLDEKVAELVEFLLLKYEAEEPVTEAEMLMIVIKYKDYFPVILKRAREFMELLFGLALIEVGPDHFCVFANTVGLTDEGSDDEGMPENSLLIIILSVIFIKGNCASEEVIWEVLNAVGVYAGREHFVYGEPRELLTKVWVQGHYLEYREVPHSSPPYYEFLWGPRAHSESIKKKVLEFLAKLNNTVPSSFPSWYKDALKDVEERVQATIDTADDATVMASESLSVMSSNVSFSE	Clinical trial	National Cancer Institute Drug Dictionary (drug id 648549).	19	Melanoma associated antigen	Melanoma associated protein	.	.	.	.	.	.	.	.	.	.	.	Q9UBF1
TTYAWV0	Plasmodium Acetyl-CoA carboxylase 1 (Malaria ACC1)	Q9U752	Q9U752_PLAFA	Carbon-carbon ligase	Acetyl-CoA carboxylase; ACC1; ACC-alpha	Malaria ACC1	"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."	.	.	SQGGGGKGIRKVENEYEIKKAYEQVQNELPNSPIFLMKVCNNVRHIEIQVVGDMYGNVCSLSGRDCTTQRRFQKIFEEGPPSVVPYPIFREMEKSSIRLTKMIKYRGAGTIEYLYDQINKKYFFLELNPRL	Literature-reported	Reduced food intake and body weight in mice treated with fatty acid synthase inhibitors. Science. 2000 Jun 30;288(5475):2379-81.	0	.	.	.	.	.	.	.	.	.	.	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	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	.	.
TTYQ4AE	Plasmodium Adenylosuccinate synthetase (Malaria Adss)	Q9U8D3	PURA_PLAFA	Carbon-nitrogen ligase	IMP--aspartate ligase; Adenylosuccinate synthase; AdSS; AMPSase	Malaria Adss	Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.	EC 6.3.4.4	1P9B	MNIFDHQIKNVDKGNVVAILGAQWGDEGKGKIIDMLSEYSDITCRFNGGANAGHTISVNDKKYALHLLPCGVLYDNNISVLGNGMVIHVKSLMEEIESVGGKLLDRLYLSNKAHILFDIHQIIDSIQETKKLKEGKQIGTTKRGIGPCYSTKASRIGIRLGTLKNFENFKNMYSKLIDHLMDLYNITEYDKEKELNLFYNYHIKLRDRIVDVISFMNTNLENNKKVLIEGANAAMLDIDFGTYPYVTSSCTTVGGVFSGLGIHHKKLNLVVGVVKSYLTRVGCGPFLTELNNDVGQYLREKGHEYGTTTKRPRRCGWLDIPMLLYVKCINSIDMINLTKLDVLSGLEEILLCVNFKNKKTGELLEKGCYPVEEEISEEYEPVYEKFSGWKEDISTCNEFDELPENAKKYILAIEKYLKTPIVWIGVGPNRKNMIVKKNFNLN	Clinical trial	Lack of methylthioadenosine phosphorylase expression in mantle cell lymphoma is associated with shorter survival: implications for a potential targeted therapy. Clin Cancer Res. 2006 Jun 15;12(12):3754-61.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9U8D3
TTQZW34	Plasmodium Apical membrane protein (Malaria AMA-1)	P22621	AMA1_PLAFF	Apicomplexan parasites AMA1	Merozoite surface antigen; Apical membrane antigen 1; AMA1; AMA-1	Malaria AMA-1	Involved in parasite invasion of erythrocytes.	.	2Q8B; 2Q8A; 1YXE	MRKLYCVLLLSAFEFTYMINFGRGQNYWEHPYQKSDVYHPINEHREHPKEYQYPLHQEHTYQQEDSGEDENTLQHAYPIDHEGAEPAPQEQNLFSSIEIVERSNYMGNPWTEYMAKYDIEEVHGSGIRVDLGEDAEVAGTQYRLPSGKCPVFGKGIIIENSNTTFLTPVATGNQYLKDGGFAFPPTEPLMSPMTLDEMRHFYKDNKYVKNLDELTLCSRHAGNMIPDNDKNSNYKYPAVYDDKDKKCHILYIAAQENNGPRYCNKDESKRNSMFCFRPAKDISFQNYTYLSKNVVDNWEKVCPRKNLQNAKFGLWVDGNCEDIPHVNEFSAIDLFECNKLVFELSASDQPKQYEQHLTDYEKIKEGFKNKNASMIKSAFLPTGAFKADRYKSHGKGYNWGNYNTETQKCEIFNVKPTCLINNSSYIATTALSHPIEVEHNFPCSLYKNEIMKEIERESKRIKLNDNDDEGNKKIIAPRIFISDDKDSLKCPCDPEIVSNSTCNFFVCKCVERRAEVTSNNEVVVKEEYKDEYADIPEHKPTYDKMKIIIASSAAVAVLATILMVYLYKRKGNAEKYDKMDEPQHYGKSNSRNDEMLDPEASFWGEEKRASHTTPVLMEKPYY	Clinical trial	Sterile immunity to malaria after DNA prime/adenovirus boost immunization is associated with effector memory CD8+T cells targeting AMA1 class I epitopes. PLoS One. 2014 Sep 11;9(9):e106241.	19	.	.	.	.	.	.	.	.	.	.	.	.	.	P22621
TT7EASG	Plasmodium Cysteine protease falcipain-2 (Malaria CPF2)	Q9N6S8	Q9N6S8_PLAFA	Protease	Falcipain 2; Cysteine proteinase falcipain 2a	Malaria CPF2	A papain family cysteine protease and important hemoglobinase of erythrocytic Plasmodium falciparum parasites.	EC 3.4.22.-	3PNR; 3BPF; 2GHU; 1YVB	MDYNMDYAPHEVISQQGERFVDKYVDRKILKNKKSLLVIISLSVLSVVGFVLFYFTPNSRKSDLFKNSSVENNNDDYIINSLLKSPNGKKFIVSKIDEALSFYDSKKNDINKYNEGNNNNNADFKGLSLFKENTPSNNFIHNKDYFINFFDNKFLMNNAEHINQFYMFIKTNNKQYNSPNEMKERFQVFLQNAHKVNMHNNNKNSLYKKELNRFADLTYHEFKNKYLSLRSSKPLKNSKYLLDQMNYEEVIKKYRGEENFDHAAYDWRLHSGVTPVKDQKNCGSCWAFSSIGSVESQYAIRKNKLITLSEQELVDCSFKNYGCNGGLINNAFEDMIELGGICPDGDYPYVSDAPNLCNIDRCTEKYGIKNYLSVPDNKLKEALRFLGPISISVAVSDDFAFYKEGIFDGECGDQLNHAVMLVGFGMKEIVNPLTKKGEKHYYYIIKNSWGQQWGERGFINIETDESGLMRKCGLGTDAFIPLIE	Literature-reported	Novel molecular targets for antimalarial drug development. Chem Biol Drug Des. 2008 Apr;71(4):287-97.	2	.	.	.	.	.	.	.	.	.	.	.	.	MetaCyc:MON-15378	.
TTCS8WB	Plasmodium Choline transporter (Malaria CT)	Q8I5S7	Q8I5S7_PLAF7	.	Glycerol-3-phosphate 1-O-acyltransferase	Malaria CT	Mediates the delivery of these compounds to the intracellular parasite	EC 2.3.1.15	.	MPDFYFLIRWLCKVIVKSVFRDVNVINPENVPLYGSVIFVGNHNNQFIDACVLIANIPRQVKFIVAEKSMRRAVIGKLASVIGCISVKRPQDLKFKGIGHICWNEGDVKITGINTRFRLDVQIGDKLLIQNKMFPVVKIESETELLIQEVINIECEDKMNGVPFKIIPKINQTEVYNLVTNSLKNGDTIGIFPEGGSHDRTNLLPLKPGVAIMTLCALADGIEDVSIIPVGLSYSKLYQLQGCATLFYGNAIIISQDLCKEYNNNNREAISKLLSKIEEGMRSCMLTSKDHETSRCIELCVSLYTPERMTISKNKIYNNLQLFCKMFWKFGNSKVIENLSYELKCYEKLLQANKIKDDEVWMLKQSTSAATLKFIEHICTFIFCVIFGMTFSLLWLPLVLISIYLAERHRKAALRNSTIKIQGGDVVSSYKVLVLIVLLPTFNIVYGLLFSIYLYHSWLKRILFVFLSMCILPICYYINLNYAVQIPSLLRQMKILLKVICGKINVWRDNERELISTRHELQLKVRDLVSTLGPDVSDDFLEQLYRNIPKFVVDVDTKRLIRGKDEFLPILQRSQLEYKEEIL	Literature-reported	Novel molecular targets for antimalarial drug development. Chem Biol Drug Des. 2008 Apr;71(4):287-97.	0	.	.	.	.	.	.	.	.	.	.	pfa00561: Glycerolipid metabolism; pfa00564: Glycerophospholipid metabolism; pfa01100: Metabolic pathways; pfa01110: Biosynthesis of secondary metabolites	.	.	Q8I5S7
TTSDL7Z	Plasmodium Delta-aminolevulinic acid synthetase (Malaria DAAS)	Q27733	Q27733_PLAFA	Acyltransferase	Delta-aminolevulinic acid synthetase	Malaria DAAS	Vital for parasite haem synthesis and parasite survival.	EC 2.3.1.37	.	MRKKRTLKVSINEIKKYCPFVKNIQFLYNTNEKKNNLVLSVMSDLCPVGKAINEKHFIIIDNKSKINIIKILKQANMQSKVLVQCIKNKNIEKENMSNDDLLKSGKRNNNVLFYDILEKNKNDHSFQINDNTIQKNNIIYKYINSLDEYKLFKNNCNNNLKDLLNKLYTDKRYRIFTILNKYRINYPNVYIENNKLMLPSFYEFYQKYGYKPCIGNIRYQLSASFEDNNKNICSFSHKNKENYLFNFWNLHIDNVSNEKTVVWCSNDYLCLSNNEKIIEVGIETLKKIGNSSGGTRNISGSLLNHTHLEYIIAKWYNKESSLLFTSGYIANVGALETLGKLLNLIYISDEMNHASIINGIRESRCEKFIFKHNDMNDLERILYNLRINKQYENRKIMIVFESIYSMSGHISNIEYIVQLAKKYNALTYVDEVHAVGLYGNKGSGYLEELHLCNHIDIINGTLSKAIGSLGGFICANKYYIDVIRSYSSHFIFTTSLTPVNINTSAEAIHIIQNDMSLRKKLTQVVNKTKQKLQERGIQVLHNNSHIVVLMINSAEKCKQICDDLLKEYNIYIQPINYPTVPMGMERIRITPSPFHTDEQIFKLVNSLYTLFKKYQVNMFDKKNKHTLMKL	Literature-reported	Involvement of delta-aminolaevulinate synthase encoded by the parasite gene in de novo haem synthesis by Plasmodium falciparum. Biochem J. 2002 Oct 15;367(Pt 2):321-7.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTT4WBH	Plasmodium Folylpolyglutamate synthase (Malaria dhfs-fpgs)	Q9U738	Q9U738_PLAFA	Carbon-nitrogen ligase	dhfs-fpgs; Folylpolyglutamate synthetase; Folylpoly-gamma-glutamate synthetase; FPGS	Malaria dhfs-fpgs	"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."	.	.	MEKNQNDKSNKNDIIHMNDKSGNYDKNNINNFIDKNDEHDMSDILHKINNEEKKYEEIKSYSECLELLYKTHALKLGLDNPKKLNESFGHPCDKYKTIHIAGTNGKGSVCYKIYTCLKIKKFKVGLFSSPHIFSLRERIIVNDEPISEKELIHLVNEVLNKAKKLYINPSFFEIITLVAFLHFLNKKVDYAIIETGIGGRLDATNILTKPEVIVITSIGYDHLNILGDNLPIICNEKIGIFKKDANVVIGPSVAIYKNVFDKAKELNCTIHTVVPEPRGERYNEENSRIALRTLEILNISIDYFLKSIIPIKPPLRIQYLATEQIQHIKKKFSPDNLEHNVQYPLAVILDVGHNETAIDRLCTDINYFHKGQNIRICISITKPRNLSVFHPFIAQFGDTLKDIFYLPSLNERTYDFEEIVEMLNNEEEIKNEIKELILSSSKKVGKWLAHEKQGNINEEDALKLYKRGCIPLIIKNAFLECCKDNSILLVCGTFFVFDEVLNVFDIHSDMQDTIFMNEPSLV	Literature-reported	A bifunctional dihydrofolate synthetase--folylpolyglutamate synthetase in Plasmodium falciparum identified by functional complementation in yeast a... Mol Biochem Parasitol. 2001 Feb;112(2):239-52.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT09NOX	Plasmodium Dihydroorotase (Malaria dho)	A9CSR1	A9CSR1_PLAFA	Carbon-nitrogen hydrolase	Dihydroorotase	Malaria dho	A Zn2+ amidohydrolase superfamily that catalyzes reversible cyclization of N-carbamoyl-L-aspartate (L-CA) to form L-dihydroorotate (L-DHO).	EC 3.5.2.3	.	MKNYFYIPIADDMHCHLRQGDMLDFTVNSIRRGGCNRVLVMPNTHPIISTCSDAQKYLYQLKSRDDDIEYLMTLYLNKNTDENDILSNYYKCNLQGVKIYPSNVTTNSSDGITSLEPYYKVFHALEKLNKSIHIHCEEPNINPLYAEEKYLPHIHDLAIKFPGLNIVLEHISSSESINVIKEFRNVAGSITPHHLYLTIDDVVNMDIYDHAIDNTYIEKYIKNTYHYCKPLPKLLEDKIALQDVIKDDFPRVFLGSDSAPHYKVMKRKPYYKPGIYTQPFLINYVAHILNKFDALDKMENFTSKNASLFLNLAEKKKLAKYYICVEKHPFKLPREYNGVVPFLAGKTLDYDIHYVSKF	Literature-reported	Antimalarial activity of orotate analogs that inhibit dihydroorotase and dihydroorotate dehydrogenase. Biochem Pharmacol. 1992 Mar 17;43(6):1295-301.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3PQ2Y	Plasmodium Dihydroorotate dehydrogenase (Malaria DHOdehase)	Q08210	PYRD_PLAF7	CH-CH donor oxidoreductase	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	Malaria DHOdehase	Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.	EC 1.3.5.2	6GJG; 6E0B; 5TBO; 5FI8; 5DEL	MISKLKPQFMFLPKKHILSYCRKDVLNLFEQKFYYTSKRKESNNMKNESLLRLINYNRYYNKIDSNNYYNGGKILSNDRQYIYSPLCEYKKKINDISSYVSVPFKINIRNLGTSNFVNNKKDVLDNDYIYENIKKEKSKHKKIIFLLFVSLFGLYGFFESYNPEFFLYDIFLKFCLKYIDGEICHDLFLLLGKYNILPYDTSNDSIYACTNIKHLDFINPFGVAAGFDKNGVCIDSILKLGFSFIEIGTITPRGQTGNAKPRIFRDVESRSIINSCGFNNMGCDKVTENLILFRKRQEEDKLLSKHIVGVSIGKNKDTVNIVDDLKYCINKIGRYADYIAINVSSPNTPGLRDNQEAGKLKNIILSVKEEIDNLEKNNIMNDESTYNEDNKIVEKKNNFNKNNSHMMKDAKDNFLWFNTTKKKPLVFVKLAPDLNQEQKKEIADVLLETNIDGMIISNTTTQINDIKSFENKKGGVSGAKLKDISTKFICEMYNYTNKQIPIIASGGIFSGLDALEKIEAGASVCQLYSCLVFNGMKSAVQIKRELNHLLYQRGYYNLKEAIGRKHSKS	Successful	Inhibitor binding in a class 2 dihydroorotate dehydrogenase causes variations in the membrane-associated N-terminal domain. Protein Sci. 2004 Apr;13(4):1031-42.	34	.	.	.	.	.	.	.	.	.	.	hsa00240:Pyrimidine metabolism; hsa01100:Metabolic pathways	R-HSA-500753:Pyrimidine biosynthesis	.	Q08210
TTLH4J3	Plasmodium DOXP reductoisomerase (Malaria DXR)	O96693	DXR_PLAFX	Short-chain dehydrogenases reductase	IspC; DXR; DXP reductoisomerase; DOXP reductoisomerase; 2-C-Methyl-d-erythritol 4-phosphate synthase; 1-deoxyxylulose-5-phosphate reductoisomerase	Malaria DXR	Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).	EC 1.1.1.267	4KP7; 4GAE; 3WQS; 3WQR; 3WQQ	MKKYIYIYFFFITITINDLVINNTSKCVSIERRKNNAYINYGIGYNGPDNKITKSRRCKRIKLCKKDLIDIGAIKKPINVAIFGSTGSIGTNALNIIRECNKIENVFNVKALYVNKSVNELYEQAREFLPEYLCIHDKSVYEELKELVKNIKDYKPIILCGDEGMKEICSSNSIDKIVIGIDSFQGLYSTMYAIMNNKIVALANKESIVSAGFFLKKLLNIHKNAKIIPVDSEHSAIFQCLDNNKVLKTKCLQDNFSKINNINKIFLCSSGGPFQNLTMDELKNVTSENALKHPKWKMGKKITIDSATMMNKGLEVIETHFLFDVDYNDIEVIVHKECIIHSCVEFIDKSVISQMYYPDMQIPILYSLTWPDRIKTNLKPLDLAQVSTLTFHKPSLEHFPCIKLAYQAGIKGNFYPTVLNASNEIANNLFLNNKIKYFDISSIISQVLESFNSQKVSENSEDLMKQILQIHSWAKDKATDIYNKHNSS	Successful	Structural basis of fosmidomycin action revealed by the complex with 2-C-methyl-D-erythritol 4-phosphate synthase (IspC). Implications for the cata... J Biol Chem. 2003 May 16;278(20):18401-7.	34	.	.	.	.	.	.	.	.	.	.	.	.	MetaCyc:MON-18397	O96693
TTVL895	Plasmodium Enopyruvyl shikimate phosphate synthase (Malaria ESPS)	0A1C3KAW3	A0A1C3KAW3_PLAMA	Alkyl aryl transferase	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	Malaria ESPS	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.	EC 1.1.1.25	.	MCNKKCGPKCNEKYSEGGRNKGRTTNSSVEMIKHKNILSENKKRNRSDVEKYVQEEYTISDKFKGIIKQMINNHGTGSFEIGNVLIIVLNMKKYHDKSEKCKEFGKMLQEISISSKNELICFADTNIMDLLHFTYHLYFKGAHGTVALHSIEVYILTSLFKTSNAKEHKRGLSEALRLAILNDKNMFIRIKKNDLNYFVKNLKYFLNKCILNIRDIIKKGENNAKYIHVLSFGNTIGNAIKNVIKNSPGCTYINDRDYINYGIFYELKIMYELDAIDMLLLLNIEEIMIKYKLKYKLDSNFVNYYTNDIITYLHKTHSSTTNEIPLVHILNINKIQKNVLVHTPLSIIIKVFYPFICLSPFHNISTTSAQEGEFIGIVNEDRDGMIHTSTTIDMVQKKKEHTIRKINYVYLQGVGNKSEIIRVIYVSTMGRQNVRIENMNLCFDVIVFIKILKDLNFQIFLKKKKSNDIYTNVNRTVIRNCLFINGNVEQTVFLFKNFIFQKKIILNIYNSGTVCRFLLPLLCLYICKQNLKAKEEKKQLLKYIILKGDEQMESHRVINPLVNVVLKCFKYVKIKYLKKKNYLPICIYVKREIHESYTLFCSNDVAIDNYHSSQFVSSMLLISVYSETDTCIRLKFKKIHNCLNRSKKIKVKKEQKKKKITIFRKYIKRKEVSRFKCSYYTMLSICWSCNGKKCNSINKGSTLCCKCSSSPDFNFDENYRHPRKRYNWYNFGYPINEIRNRMNSSNFSTTSKAFIDLTVRVMKLWGVRVKMKRNNYTIKKNEKYLLYSNNNDSTSIRGIAGNRSSIKSRTSNRICRSGGNKNERFNNVHYKYASMINRKHHFNDSRHILFPGIHNKKEKMLVYSLHGRGEKSSKGSCDTCKQKGVDEVKKEVHNNPHEEYNFVMLKQKEKVDQINNKEKEEDKNISNDVTNDGGYTLVKNILRYEINNDLGLYFYFIIGSLIKRQNCVIFLKLNINRMKLKNVGKGYYKIETIDFQKNVLNYFLLNILLLLGINMYINMNDEIRKIYLLTSKRMNIKKKKIIRHLEKAIRNKWKRKNGYYKKRHRNIYTTACYGVNNSTCEHLSQGECTFKYYIFEKIYMKYKIMHFRNVLLKIVVDAEYFSDDFFSICVLFCYYLLTHERENNTELLFKIKNIHNQNIKESIRILNAVLILKICFHNILFIFCDNNSIYITKTHHQIQNCLFFKCKREHWALLCTSSDNNERKNNSSSIGSNSNNGNNNRRSRCKKKLFFNNSKYVINDDQELYLYIDAKKDHRIIFMATILSLIFKNIIIDNSYEVEKSYPHFYEQARKYLEININYVNSDNVKFHNFEEVNNYNILNEQDSKSCVEVISSSIESHESTYSCTDASRSDVDMLKNYKSPTMSTEGNYSINTRSKKLINKHTNCNSLNRPMENNTCTEKNFYKTNGAHIIHKKEANRTHRSTRGNLYFMNHEYWKTSNLNLKNVVMKKTKKCIHRKRAPKGIINLCNLTNPMLQLHTCGSTGSIASEENELTVMRCGERKGIISRKGIFTVSNSGGSDSYSDSYSDSYSDSFMKCNEDPSNERSNECNKDHSNERSNGSSKWFERRGGTEEGYQTKLRLNLRERLRSGKSSSFLNKVKNQLNGDKTNLFLPSDTNYMRTYKYEEVKVNNGNVFYLLKEINNLNVHIICGIRNVGKSYLGHRIENSLVIDIDEYILNGQISFDKLTIDDFRFYEYITFVSALYLSYCLLTLKNYLWANISGSISCNDRGDVWSNIQSSMHGNDDKKDVFLCRAENSKVCINRSCVAVHAYFDNIFFCMGNDIIFYNKKINDLYYNLKNKLLTCKNYDINSITIVLGGGIIEFYKSRQVLKKLKNVVLIKRNKRELCDICINDNVKPKLSGNIKEIINRRTVLFDELNSFHFSIPSEIKISNHIKNLKESRNKLIVSSFINFFNYKFFVKPTILDWGAIRTLSIHLKFFHSFDYELLRSSYDVVEIVYEHIGSTKDGQSEQKDGSGQRGCVEQRGCNERRCRGEELDMGGQHDQRGKNRKYAKNEEKLLALAIFIIRSYTTKPIAVKLHTSIFHAQFFKIKNRCTKLKKDGKKNVAHLFCNNLLNVLYKYKINIVEVDIKFLKVVKYFLAHKKKKANIFFIISKHRNKVNKLKIKSDLNKLNIFHADLIKLTYNYASKSDKEFLSKTINAYNSHRLINTKLSRIKNVYNNTNEEISLYSCYVNNSFVFLYNNVTHLEYQKTNLRNLETGKNSKNIENHNYDENKKNRDFYHNNFMYGFYYQKVKSIISYVPTEGDK	Literature-reported	The apicoplast as an antimalarial drug target. Drug Resist Updat. 2001 Jun;4(3):145-51.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTBE4IR	Plasmodium Oxoacyl-[acyl-carrier protein] reductase (Malaria fabG)	Q965D6	Q965D6_PLAFA	Short-chain dehydrogenases reductase	3-oxoacyl-acyl-carrier protein reductase	Malaria fabG	"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."	EC 1.1.1.100	.	MSVLHRFYLFFLFTKFFHCYKISYVLKNAKLAPNHAIKNINSLNLLSENKKENYYYCGENKVALVTGAGRGIGREIAKMLAKSVSHVICISRTQKSCDSVVDEIKSFGYESSGYAGDVSKKEEISEVINKILTEHKNVDILVSNAGITRDNLFLRMKNDEWEDVLRTNLNSLFYITQPISKRMINNRYGRIINISSIVGLTGNVGQANYSSSKAGVIGFTKSLAKELASRNITVNAIAPGFISSDMTDKISEQIKKNIISNIPAGRMGTPEEVANLACFLSSDKSGYINGRVFVIDGGLSP	Clinical trial	"Inhibition of Plasmodium falciparum fatty acid biosynthesis: evaluation of FabG, FabZ, and FabI as drug targets for flavonoids. J Med Chem. 2006 Jun 1;49(11):3345-53."	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNX2CS	Plasmodium Enoyl-ACP reductase (Malaria fabI)	Q965D5	Q965D5_PLAFA	CH-CH donor oxidoreductase	fabI; NADH-dependent enoyl-ACP reductase; Enoyl-acyl-carrier protein reductase; Enoyl-acyl carrier reductase; Enoyl-acyl carrier protein reductase; Enoyl-ACP reductase FabI	Malaria fabI	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.	EC 1.3.1.9	.	MNKISQRLLFLFLHFYTTVCFIQNNTQKTFHNVLQNEQIRGKEKAFYRKEKRENIFIGNKMKHVHNMNNTHNNNHYMEKEEQDASNINKIKEENKNEDICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNGKFDNDMIIDKDKKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYPIEDVANLIHQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSLISLCKYFVNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVLAYHLGRNYNIRINTISAGPLKSRAATAINKLNNTYENNTNQNKNRNSHDVHNIMNNSGEKEEKKNSASQNYTFIDYAIEYSEKYAPLRQKLLSTDIGSVASFLLSRESRAITGQTIYVDNGLNIMFLPDDIYRNENE	Successful	Novel molecular targets for antimalarial drug development. Chem Biol Drug Des. 2008 Apr;71(4):287-97.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHPFTS	Plasmodium Beta-hydroxyacyl-ACP dehydratase (Malaria FabZ)	Q965D7	Q965D7_PLAFA	.	fabZ; Fatty acid synthesis protein; Beta-hydroxyacyl-ACP dehydratase; 17 kDa actomyosin component; (3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; (3R)-hydroxymyristoyl-ACP dehydrase	Malaria FabZ	Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.	.	3AZB; 3AZA; 3AZ9; 3AZ8; 2OKI	MRFLIIHIAVIVLPFVLMIDVKRENSFFLRHSPKRLYKKADYNNMYDKIIKKQQNRIYDVSSQINQDNINGQNISFNLTFPNYDTSIDIEDIKKILPHRYPFLLVDKVIYMQPNKTIIGLKQVSTNEPFFNGHFPQKQIMPGVLQIEALAQLAGILCLKSDDSQKNNLFLFAGVDGVRWKKPVLPGDTLTMQANLISFKSSLGIAKLSGVGYVNGKVVINISEMTFALSK	Clinical trial	Antiplasmodial drug targets: a patent review (2000 - 2013).Expert Opin Ther Pat. 2016;26(1):107-30.	15.5	.	Thioester dehydratase family	.	.	.	FabA-like domain	PF07977	PF07977; FabA	.	.	pfa00061:Fatty acid biosynthesis; pfa00780:Biotin metabolism; pfa01100:Metabolic pathways; pfa01212:Fatty acid metabolism	.	.	.
TT1FL6V	Plasmodium Fructose-bisphosphate aldolase (Malaria FBA)	P14223	ALF_PLAFA	Carbon-carbon lyase	Fructose-bisphosphate aldolase; 41 kDa antigen	Malaria FBA	Catalyzes carboncarbon bond formation (or cleavage). Participate in the metabolically important pathways of gluconeogenesis and glycolysis.	.	2PC4; 2EPH; 1A5C	MAHCTEYMNAPKKLPADVAEELATTAQKLVQAGKGILAADESTQTIKKRFDNIKLENTIENRASYRDLLFGTKGLGKFISGAILFEETLFQKNEAGVPMVNLLHNENIIPGIKVDKGLVNIPCTDEEKSTQGLDGLAERCKEYYKAGARFAKWRTVLVIDTAKGKPTDLSIHETAWGLARYASICQQNRLVPIVEPEILADGPHSIEVCAVVTQKVLSCVFKALQENGVLLEGALLKPNMVTAGYECTAKTTTQDVGFLTVRTLRRTVPPALPGVVFLSGGQSEEEASVNLNSINALGPHPWALTFSYGRALQASVLNTWQGKKENVAKAREVLLQRAEANSLATYGKYKGGAGGENAGASLYEKKYVY	Literature-reported	"N-Sulfonyl hydroxamate derivatives as inhibitors of class II fructose-1,6-diphosphate aldolase. Bioorg Med Chem Lett. 2005 Dec 15;15(24):5375-7."	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P14223
TTAO7YK	Plasmodium Glutamate dehydrogenase (Malaria gdh)	Q9NGT0	Q9NGT0_PLAFA	CH-NH(2) donor oxidoreductase	Glutamate dehydrogenase	Malaria gdh	Catalyses the reversible oxidative deamination of L-glutamate to form -ketoglutarate and ammonia using NADP(H) or NAD(H) as co-factors	EC 1.4.1.2	.	MDIDRRSALSCSPNNMECGFGSGHFSNNSITWKEKYEQTKELLKSYNLFSDHLINYSIDFYFNKLGFNKFHFEETSPELISKVVVCIITAKINEQYSSDKYFPTFEETHDNVIFIITRVFADDNKTRLNYKMEKKIEEKYFNFSDMSKDCYRLKSFRSVHSVFDKEHTYQEPLRTYILELPTYNDDIIKENETDLKKLMDVNFYNYIKGTRSEQIYYELNKAVLYDLTGQFLQTHYYETSSSTFTLTIAVKRSNVISSIFSLIGDCLNMHRCFSYSKYVEPLKNGVLLIILNVKVIVNNEMEREKQKLDLKDKIYKVVKSLKTLCLFNDSKFIQLSVKRTFTAQESAYLFMIIKFITFFSTFTLSSYKNVEHALNLRNYNNNIMDTTTNSSSSPSSVLNDVYIIKEKLKSSKYTKEEILRCAQSNVRTIKMLFANFEKKLNHQRNKCNQMKYGENNMKNSGDLLKEYSTNNRNVDHPTLSSLASSSSSCSSSFSLHSYLSGSYESPYYHHNKDSKDIIDEIEDNHDKKILQYFYMFEKYALKTNFFLTHKISLAVAFDGALLKDSIYEAQPYSIIMILGLHFVGFHIRFSKISRGGVRIVISNNVNSYMHNSDNLFDEAYNLAYTQNFKNKDIPEGGSKGIILLDADVCNVANTKYIKNLSFYSYVNSILDLLINEDLNEERASSISVHSTKGANNTTITFDNVMSSVENMVDRGGVEGEHLNITLPYDANMACNNNTTNDNLSNMHDTYNLNNSGEATLDHHSVDNRIVSNSSGTNNMNAQKGEGEDEKAKDKEMSNNRKNEENERKRCDNVSNSNYNYVNGTTEDAVQKIMGSKCKGGRNNNGEEKDGDMNGHNNNNNDNNNIDDDEHIEECYKGAGCVINGENKTRKMILQEKMNEEEDLIFLGPDENTGSDQLMDWACIIAKREYIHIGKPFQQGKLRKNGGVPHDMYGMTTLGIETYISKLCEKLNIKEESISRSLVGGPDGDLGSNAILQSKTKIISIIDGSGILYDKQGLNKEELIRLAKRRNNKDKSKAITCCTLYDEKYFSKDGFKISIEDHNVDIFGNKIRNGLDFRNTFFLNPLNKCELFNPCGGRPHSINIFNVNNIIKNGECIYKYIVEGANVFISDDARNILESKNVILFKDAATNKGGVISSSLEVLAGLVLDDKQYIDYMCSPDSDILQVDENEINFVHQNQKMNHSLSFKRGSINNLEEDEKKDTSNNEKNKNIIKTVNKNDTQDNSHHHNNSNKCNEDQQDVSDFYKAYVKEIQKKITHYCELEFESLWKETRRTKTPISKAINILSNKISELKKDILSSDTLCRDYKLLKKVLERVIPPTLLKIVTFEQILERVPYVYIKSLLASARASKLLLFTTILE	Successful	Novel inhibitors complexed with glutamate dehydrogenase: allosteric regulation by control of protein dynamics. J Biol Chem. 2009 Aug 21;284(34):22988-3000.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZ82MR	Plasmodium DNA gyrase (Malaria gyrase)	Q8I0X3	Q8I0X3_PLAF7	.	Malaria DNA gyrase subunit A	Malaria gyrase	Essential for replication and transcription in prokaryotes. Catalyses ATP-dependent DNA supercoiling activity.	EC 5.99.1.3	.	MSFKFSIVFVLYLLFLLKFNKRFIFLKSEKITSYINTQIPNYSSSPPFFLKKEAKNNIKKCYFIKREGYRNIGTKNASNAFVLNFKSNRSTYTDNAFSCTSLCSEKKERKKVQDPYDLKAKKKEKTYELNDIKNNEKKKDDIVNASNDITNDKLDNINNNINESRKLIKGEYYDVEICEILSKSFLSYANFLILNRCLCDYRDGLKTVQRRIIWSMYEINKGIDKKGYKKCARIVGEVIGKYHPHGDKSVYDALVRLAQKHHNNNLLIKGYGNFGSVEYNAAAMRYTEAKISSFCYDILLDEINDENVEYIKNFDGNEREPKVLCSKIPLLLINGCSGIAVSILSSIPCHNLIDVANCCINFLINENIRDDELFHIIKGPDFSTGGIIISKYDILKNIYNSGKGNFEIRSNVFFEYIKNDKKVITKHINDLSSIENSDIDKLTKKIIIKNLPPNVKPNELIENIINLLNDKKNEHDNILLRIRDESEKEDMRIVLELKKHSQIEQIHNFLSYLFKYTNMQISYHCNFVCIGYENTYTQFSLKSFIKLWCNNRIKFIKTNYEIKNKNLQKQLNIIDLYLIIQNKILDIITFFQKNQNIEQIQLYLKNNFKLNPEQIKYILSIKLQKLINIKNIDFISQRNKIMHQIKLNDEIINNVQNIKNLIIQELIYIKNKYGIHNLNKQCIIPSTPKYKYSYINSEYHPNFSKNKQIIDTYNTVSTNDNNINHSNYTHDLPNTDNVTKDKNVVETNVHKNIHISSDISNNIKNSDKNSSLTKNQDSDNMMPYRNTYIDSLDNNMKDIYNNDEVLILITYGGYIKKIKINEKLKNHSNNIIKLSNVKYILKENEEKLNENNKRLKFNDLQKGNEQEKYKDNEQKLNNDIGHNINIQNNNNDNNNNNNDNNNVLLLNEEEYNSYKIKKSILVRNRDKILLTDNYNKAFLLNVYDLHLSSYDSKGTPINQIIHSSKNITGITKFQENKKYLIVCSENGKMKVINNDVFLKRKKKGIKLFKNKKNIYFSYCNFNDNCIVGTKNGYIIQFPLSSFKISKKNSLGNKCISLAKNDKVVDLLSYENNEKNLKNYKIIFVTKNGFGKMINLNELKIQKKKGKGHRIMKFKKSKTRKDNKKDIEKKQINAINNKDKDKDIPSNNDDNNILHNTKVDEFLGFKLYDMNKQNEKDILIMITDHAVLIRKNMSLLKEKNKKHSSQIYAKMNKINQLVYFDII	Successful	2017 FDA drug approvals.Nat Rev Drug Discov. 2018 Feb;17(2):81-85. 	34	.	.	.	.	.	.	.	.	.	.	.	.	.	Q8I0X3
TT3QW1X	Plasmodium Histidine-rich protein II (Malaria HRP II)	P90582	P90582_PLAFA	.	Histidine-rich protein II	Malaria HRP II	Functions as a diagnostic and prognostic marker for falciparum malaria.	.	.	MVSFSKNKVLSAAVFASVLLLDNNNSAFNNNLCSKNAKGLNLNKRLLHETQAHVDDAHHAHHVADAHHAHHAADAHHAHHAADAHHAHHAADAHHAHHAADAHHAHHAAYAHHAHHAADAHHAHHASDAHHAADAHHAAYAHHAHHAADAHHAHHASDAHHAADAHHAAYAHHAHHAADAHHAADAHHATDAHHAHHAADARHATDAHHAADAHHATDAHHAADAHHAADAHHATDAHHAADAHHATDAHHAADAHHAADAHHATDAHHAHHAADAHHAAAHHATDAHHATDAHHAAAHHEAATHCLRH	Literature-reported	Discovering antimalarials: a new strategy. Chem Biol. 2002 Aug;9(8):852-3.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYXA6Z	Plasmodium Hexose transporter 1 (Malaria ht1)	O97467	O97467_PLAFA	.	ht1; Putative sugar transporter; Hexose transporter	Malaria ht1	High-affinity glucose transporter.	.	.	MTKSSKDICSENEGKKNGKSGFFSTSFKYVLSACIASFIFGYQVSVLNTIKNFIVVEFEWCKGEKDRLNCSNNTIQSSFLLASVFIGAVLGCGFSGYLVQFGRRLSLLIIYNFFFLVSILTSITHHFHTILFARLLSGFGIGLVTVSVPMYISEMTHKDKKGAYGVMHQLFITFGIFVAVMLGLAMGEGPKADSTEPLTSFAKLWWRLMFLFPSVISLIGILALVVFFKEETPYFLFEKGRIEESKNILKKIYETDNVDEPLNAIKEAVEQNESAKKNSLSLLSALKIPSYRYVIILGCLLSGLQQFTGINVLVSNSNELYKEFLDSHLITILSVVMTAVNFLMTFPAIYIVEKLGRKTLLLWGCVGVLVAYLPTAIANEINRNSNFVKILSIVATFVMIISFAVSYGPVLWIYLHEMFPSEIKDSAASLASLVNWVCAIIVVFPSDIIIKKSPSILFIVFSVMSILTFFFIFFFIKETKGGEIGTSPYITMEERQKHMTKSVV	Literature-reported	Opportunities and challenges in antiparasitic drug discovery. Nat Rev Drug Discov. 2005 Sep;4(9):727-40.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNISW4	Plasmodium MECDP-synthase (Malaria ISPF)	P62368	ISPF_PLAF7	Phosphorus-oxygen lyase	MECPS; MECDP-synthase; ISPF	Malaria ISPF	"Converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2- phosphate into 2C-methyl-D-erythritol 2,4-cyclodiphosphate and CMP."	.	4C82; 4C81	MFLKGYTSNVVLIILTFFILLTKEEKNIKNNISGYCFLNFGLKKNAIIKKREKQNLKLFCYNGIRIGQGYDIHKIKVLDEEYNTYANNDFNKNEQSFKTLTLGGVKINNVLVLSHSDGDIIYHSIVDSILGALGSLDIGTLFPDKDEKNKNKNSAIFLRYARLLIYKKNYDIGNVDINVIAQVPKISNIRKNIIKNISTVLNIDESQISVKGKTHEKLGVIGEKKAIECFANILLIPKNS	Literature-reported	"Biosynthesis of terpenoids. 2C-Methyl-D-erythritol 2,4-cyclodiphosphate synthase (IspF) from Plasmodium falciparum. Eur J Biochem. 2001 Jun;268(11):3190-7."	.	.	.	.	.	.	.	.	.	.	.	pfa00900: Terpenoid backbone biosynthesis; pfa01100: Metabolic pathways; pfa01110: Biosynthesis of secondary metabolites	.	.	P62368
TTBL49X	Plasmodium Hypoxanthine-guanine phosphoribosyltransferase (Malaria LACZ)	P20035	HGXR_PLAFG	Pentosyltransferase	LACZ of Plasmodium falciparum (isolate FCR-3 / Gambia); Hypoxanthine phosphoribosyltransferase; HPRT; HGPRTase; HGPRT of Plasmodium falciparum (isolate FCR-3 / Gambia); Guanine phosphoribosyltransferase; GPRT	Malaria LACZ	"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."	.	3OZG; 3OZF; 2VFA; 1CJB	MPIPNNPGAGENAFDPVFVNDDDGYDLDSFMIPAHYKKYLTKVLVPNGVIKNRIEKLAYDIKKVYNNEEFHILCLLKGSRGFFTALLKHLSRIHNYSAVETSKPLFGEHYVRVKSYCNDQSTGTLEIVSEDLSCLKGKHVLIVEDIIDTGKTLVKFCEYLKKFEIKTVAIACLFIKRTPLWNGFKADFVGFSIPDHFVVGYSLDYNEIFRDLDHCCLVNDEGKKKYKATSL	Patented-recorded	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	hsa00230:Purine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways	R-HSA-74217:Purine salvage	.	P20035
TTOY91U	Plasmodium Hypoxanthine-guanine-xanthine phosphoribosyltransferase (Malaria LACZ)	P07833	HGXR_PLAFK	Pentosyltransferase	LACZ of Plasmodium falciparum (isolate K1 / Thailand); HGXPRTase; HGXPRT; HGPRT of Plasmodium falciparum (isolate K1 / Thailand)	Malaria LACZ	"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."	.	.	MPIPNNPGAGENAFDPVFVKDDDGYDLDSFMIPAHYKKYLTKVLVPNGVIKNRIEKLAYDIKKVYNNEEFHILCLLKGSRGFFTALLKHLSRIHNYSAVEMSKPLFGEHYVRVKSYCNDQSTGTLEIVSEDLSCLKGKHVLIVEDIIDTGKTLVKFCEYLKKFEIKTVAIACLFIKRTPLWNGFKADFVGFSIPDHFVVGYSLDYNEIFRDLDHCCLVNDEGKKKYKATSL	Literature-reported	The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P07833
TTG45NU	Plasmodium Elongation factor 1-alpha 1 (Malaria MEF-1)	Q00080	EF1A_PLAFK	Acid anhydrides hydrolase	MEF-1; Elongation factor Tu of Plasmodium falciparum; Elongation factor 1 A-1; EF-Tu; EF-1-alpha-1 of Plasmodium falciparum; EEF1A-1	Malaria MEF-1	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.	.	.	MGKEKTHINLVVIGHVDSGKSTTTGHIIYKLGGIDRRTIEKFEKESAEMGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYFFTVIDAPGHKDFIKNMITGTSQADVALLVVPADVGGFDGAFSKEGQTKEHVLLAFTLGVKQIVVGVNKMDTVKYSEDRYEEIKKEVKDYLKKVGYQADKVDFIPISGFEGDNLIEKSDKTPWYKGRTLIEALDTMQPPKRPYDKPLRIPLQGVYKIGGIGTVPVGRVETGILKAGMVLNFAPSAVVSECKSVEMHKEVLEEARPGDNIGFNVKNVSVKEIKRGYVASDTKNEPAKGCSKFTAQVIILNHPGEIKNGYTPLLDCHTSHISCKFLNIDSKIDKRSGKVVEENPKAIKSGDSALVSLEPKKPMVVETFTEYPPLGRFAIRDMRQTIAVGIINQLKRKNLGAVTAKAPAKK	Clinical trial	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	Q00080
TT86VZE	Plasmodium M1-family aminopeptidase (Malaria MFA)	O96935	AMP1_PLAFQ	Peptidase	Pfa-M1	Malaria MFA	"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."	EC 3.4.11.-	6EED; 6EE6; 6EE4; 6EE3; 6EAB	MKLTKGCAYKYIIFTVLILANILYDNKKRCMIKKNLRISSCGIISRLLKSNSNYNSFNKNYNFTSAISELQFSNFWNLDILQKDIFSNIHNNKNKPQSYIIHKRLMSEKGDNNNNNHQNNNGNDNKKRLGSVVNNEENTCSDKRMKPFEEGHGITQVDKMNNNSDHLQQNGVMNLNSNNVENNNNNNSVVVKKNEPKIHYRKDYKPSGFIINNVTLNINIHDNETIVRSVLDMDISKHNVGEDLVFDGVGLKINEISINNKKLVEGEEYTYDNEFLTIFSKFVPKSKFAFSSEVIIHPETNYALTGLYKSKNIIVSQCEATGFRRITFFIDRPDMMAKYDVTVTADKEKYPVLLSNGDKVNEFEIPGGRHGARFNDPHLKPCYLFAVVAGDLKHLSATYITKYTKKKVELYVFSEEKYVSKLQWALECLKKSMAFDEDYFGLEYDLSRLNLVAVSDFNVGAMENKGLNIFNANSLLASKKNSIDFSYARILTVVGHEYFHNYTGNRVTLRDWFQLTLKEGLTVHRENLFSEEMTKTVTTRLSHVDLLRSVQFLEDSSPLSHPIRPESYVSMENFYTTTVYDKGSEVMRMYLTILGEEYYKKGFDIYIKKNDGNTATCEDFNYAMEQAYKMKKADNSANLNQYLLWFSQSGTPHVSFKYNYDAEKKQYSIHVNQYTKPDENQKEKKPLFIPISVGLINPENGKEMISQTTLELTKESDTFVFNNIAVKPIPSLFRGFSAPVYIEDNLTDEERILLLKYDSDAFVRYNSCTNIYMKQILMNYNEFLKAKNEKLESFNLTPVNAQFIDAIKYLLEDPHADAGFKSYIVSLPQDRYIINFVSNLDTDVLADTKEYIYKQIGDKLNDVYYKMFKSLEAKADDLTYFNDESHVDFDQMNMRTLRNTLLSLLSKAQYPNILNEIIEHSKSPYPSNWLTSLSVSAYFDKYFELYDKTYKLSKDDELLLQEWLKTVSRSDRKDIYEILKKLENEVLKDSKNPNDIRAVYLPFTNNLRRFHDISGKGYKLIAEVITKTDKFNPMVATQLCEPFKLWNKLDTKRQELMLNEMNTMLQEPNISNNLKEYLLRLTNKL	Literature-reported	In silico identification and biochemical evaluation of novel inhibitors of NRH:quinone oxidoreductase 2 (NQO2). Bioorg Med Chem Lett. 2010 Dec 15;20(24):7331-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	O96935
TT68ZYJ	Plasmodium Merozoite surface protein 1 (Malaria MSP-1)	P04933	MSP1_PLAFW	Merozoite surface protein	p195; PMMSA; Merozoite surface protein 1; Merozoite surface antigens	Malaria MSP-1	"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."	.	2MUE; 2MU7; 2FLG; 1CEJ	MKIIFFLCSFLFFIINTQCVTHESYQELVKKLEALEDAVLTGYSLFQKEKMVLNEGTSGTAVTTSTPGSKGSVASGGSGGSVASGGSVASGGSVASGGSVASGGSGNSRRTNPSDNSSDSDAKSYADLKHRVRNYLLTIKELKYPQLFDLTNHMLTLCDNIHGFKYLIDGYEEINELLYKLNFYFDLLRAKLNDVCANDYCQIPFNLKIRANELDVLKKLVFGYRKPLDNIKDNVGKMEDYIKKNKKTIENINELIEESKKTIDKNKNATKEEEKKKLYQAQYDLSIYNKQLEEAHNLISVLEKRIDTLKKNENIKELLDKINEIKNPPPANSGNTPNTLLDKNKKIEEHEKEIKEIAKTIKFNIDSLFTDPLELEYYLREKNKNIDISAKVETKESTEPNEYPNGVTYPLSYNDINNALNELNSFGDLINPFDYTKEPSKNIYTDNERKKFINEIKEKIKIEKKKIESDKKSYEDRSKSLNDITKEYEKLLNEIYDSKFNNNIDLTNFEKMMGKRYSYKVEKLTHHNTFASYENSKHNLEKLTKALKYMEDYSLRNIVVEKELKYYKNLISKIENEIETLVENIKKDEEQLFEKKITKDENKPDEKILEVSDIVKVQVQKVLLMNKIDELKKTQLILKNVELKHNIHVPNSYKQENKQEPYYLIVLKKEIDKLKVFMPKVESLINEEKKNIKTEGQSDNSEPSTEGEITGQATTKPGQQAGSALEGDSVQAQAQEQKQAQPPVPVPVPEAKAQVPTPPAPVNNKTENVSKLDYLEKLYEFLNTSYICHKYILVSHSTMNEKILKQYKITKEEESKLSSCDPLDLLFNIQNNIPVMYSMFDSLNNSLSQLFMEIYEKEMVCNLYKLKDNDKIKNLLEEAKKVSTSVKTLSSSSMQPLSLTPQDKPEVSANDDTSHSTNLNNSLKLFENILSLGKNKNIYQELIGQKSSENFYEKILKDSDTFYNESFTNFVKSKADDINSLNDESKRKKLEEDINKLKKTLQLSFDLYNKYKLKLERLFDKKKTVGKYKMQIKKLTLLKEQLESKLNSLNNPKHVLQNFSVFFNKKKEAEIAETENTLENTKILLKHYKGLVKYYNGESSPLKTLSEESIQTEDNYASLENFKVLSKLEGKLKDNLNLEKKKLSYLSSGLHHLIAELKEVIKNKNYTGNSPSENNTDVNNALESYKKFLPEGTDVATVVSESGSDTLEQSQPKKPASTHVGAESNTITTSQNVDDEVDDVIIVPIFGESEEDYDDLGQVVTGEAVTPSVIDNILSKIENEYEVLYLKPLAGVYRSLKKQLENNVMTFNVNVKDILNSRFNKRENFKNVLESDLIPYKDLTSSNYVVKDPYKFLNKEKRDKFLSSYNYIKDSIDTDINFANDVLGYYKILSEKYKSDLDSIKKYINDKQGENEKYLPFLNNIETLYKTVNDKIDLFVIHLEAKVLNYTYEKSNVEVKIKELNYLKTIQDKLADFKKNNNFVGIADLSTDYNHNNLLTKFLSTGMVFENLAKTVLSNLLDGNLQGMLNISQHQCVKKQCPQNSGCFRHLDEREECKCLLNYKQEGDKCVENPNPTCNENNGGCDADAKCTEEDSGSNGKKITCECTKPDSYPLFDGIFCSSSNFLGISFLLILMLILYSFI	Clinical trial	Analysis of human B-cell responses following ChAd63-MVA MSP1 and AMA1 immunization and controlled malaria infection. Immunology. 2014 Apr;141(4):628-44.	19	.	.	.	.	.	.	.	.	.	.	.	.	.	P04933
TTX6NHY	Plasmodium Cytochrome C oxidoreductase (Malaria MT-CO1)	Q02766	COX1_PLAFA	Heme-copper respiratory oxidase family	MT-CO1; Cytochrome c oxidase subunit 1; Cytochrome c oxidase polypeptide I	Malaria MT-CO1	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.	EC 1.9.3.1	.	MVLNRYSLITNCNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQENVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILCGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSLSPVAVDVIIFGLLVSGVASIMSSLNFITTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWICTYMSSNFGMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKNLRENSIVILWSMLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIFK	Literature-reported	Novel molecular targets for antimalarial drug development. Chem Biol Drug Des. 2008 Apr;71(4):287-97.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q02766
TTRAMF0	Plasmodium Cytochrome B (Malaria MT-CYB)	Q02768	CYB_PLAFA	Cytochrome b family	MT-CYB; Cyb	Malaria MT-CYB	"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."	.	.	MNFYSINLVKAHLINYPCPLNINFLWNYGFLLGIIFFIQIITGVFLASRYTPDVSYAYYSIQHILRELWSGWCFRYMHATGASLVFLLTYLHILRGLNYSYMYLPLSWISGLILFMIFIVTAFVGYVLPWGQMSYWGATVITNLLSSIPVAVIWICGGYTVSDPTIKRFFVLHFILPFIGLCIVFIHIFFLHLHGSTNPLGYDTALKIPFYPNLLSLDVKGFNNVIILFLIQSLFGIIPLSHPDNAIVVNTYVTPSQIVPEWYFLPFYAMLKTVPSKPAGLVIVLLSLQLLFLLAEQRSLTTIIQFKMIFGARDYSVPIIWFMCAFYALLWIGCQLPQDIFILYGRLFIVLFFCSGLFVLVHYRRTHYDYSSQANI	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	pfa00190:Oxidative phosphorylation; pfa01100:Metabolic pathways	.	.	Q02768
TTSFWA7	Plasmodium CDK Pfmrk (Malaria Pfmrk)	P90584	P90584_PLAFA	Kinase	Pfmrk; MO15-related protein kinase Pfmrk	Malaria Pfmrk	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.	EC 2.7.1.37	.	MENNSTERYIFKPNFLGEGSYGKVYKAYDTILKKEVAIKKMKLNEISNYIDDCGINFVLLREIKIMKEIKHKNIMSALDLYCEKDYINLVMEIMDYDLSKIINRKIFLTDSQKKCILLQILNGLNVLHKYYFMHRDLSPANIFINKKGEVKLADFGLCTKYGYDMYSDKLFRDKYKKNLNLTSKVVTLWYRAPELLLGSNKYNSSIDMWSFGCIFAELLLQKALFPGENEIDQLGKIFFLLGTPNENNWPEALCLPLYTEFTKATKKDFKTYFKIDDDDCIDLLTSFLKLNAHERISAEDAMKHRYFFNDPLPCDISQLPFNDL	Patented-recorded	A three-dimensional in silico pharmacophore model for inhibition of Plasmodium falciparum cyclin-dependent kinases and discovery of different class... J Med Chem. 2004 Oct 21;47(22):5418-26.	15.5	EC:2.7	.	.	2.7.1.37 	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	.	.
TT9PCE0	Plasmodium CDK PfPK5 (Malaria PfPK5)	Q07785	CDC2H_PLAFK	Kinase	PfPK5; PK5; Cell division control protein 2 homolog; CRK2	Malaria PfPK5	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.	.	1V0P; 1V0O; 1V0B; 1OB3; 1LCH	MEKYHGLEKIGEGTYGVVYKAQNNYGETFALKKIRLEKEDEGIPSTTIREISILKELKHSNIVKLYDVIHTKKRLVLVFEHLDQDLKKLLDVCEGGLESVTAKSFLLQLLNGIAYCHDRRVLHRDLKPQNLLINREGELKIADFGLARAFGIPVRKYTHEVVTLWYRAPDVLMGSKKYSTTIDIWSVGCIFAEMVNGTPLFPGVSEADQLMRIFRILGTPNSKNWPNVTELPKYDPNFTVYEPLPWESFLKGLDESGIDLLSKMLKLDPNQRITAKQALEHAYFKENN	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	EC:2.7	.	.	2.7.11.22	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	.	.
TTQ4N7K	Plasmodium CDK PfPK6 (Malaria PfPK6)	Q8IDW1	Q8IDW1_PLAF7	Kinase	Protein kinase 6; PF3D7_1337100; CDK-related protein kinase 6	Malaria PfPK6	"Cyclin-dependent protein serine/threonine kinase activity, protein phosphorylation."	EC 2.7.11.22	.	MNRIDISNFDFLYVIGKGTYGIVYKALDKKENNFVAIKKIINLCDENYGISKCILRELTILQKIKHKNIINLKYVFYGKDIEDKLKGENLENSCLYLAFEYCDIDLFNLIKKHNLNIKEIKYIIFELLLALSYFHSNNYIHRDIKPENIFITSEGEIKLGDLGMSVEKSDHMTPTVVTLWYRAPEILLKSTNYDQKVDIWSLGCLFMELIQGRPLFPGKNDCTQLELIYLLLGDKDKLTTVDKERKDMFPYFEINMLKDAIDDEHTLDLISKMLIYDPNYRISSKEALKHPCFQDIEQVKFSYNF	Literature-reported	Cyclin-dependent protein kinases as therapeutic drug targets for antimalarial drug development. Expert Opin Ther Targets. 2003 Feb;7(1):7-17.	.	EC:2.7	.	protein kinase superfamily.	2.7.11.22 	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	.	Q8IDW1
TTH9VL3	Plasmodium Plasmepsin 1 (Malaria PLA1)	P39898	PLM1_PLAFA	Peptidase	Plasmepsin I; PFAPG; Aspartic hemoglobinase I	Malaria PLA1	"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."	.	3QS1; 3QRV; 1LDU; 1LCR	MALSIKEDFSSAFAKNESAVNSSTFNNNMKTWKIQKRFQILYVFFFLLITGALFYYLIDNVLFPKNKKINEIMNTSKHVIIGFSIENSHDRIMKTVKQHRLKNYIKESLKFFKTGLTQKPHLGNAGDSVTLNDVANVMYYGEAQIGDNKQKFAFIFDTGSANLWVPSAQCNTIGCKTKNLYDSNKSKTYEKDGTKVEMNYVSGTVSGFFSKDIVTIANLSFPYKFIEVTDTNGFEPAYTLGQFDGIVGLGWKDLSIGSVDPVVVELKNQNKIEQAVFTFYLPFDDKHKGYLTIGGIEDRFYEGQLTYEKLNHDLYWQVDLDLHFGNLTVEKATAIVDSGTSSITAPTEFLNKFFEGLDVVKIPFLPLYITTCNNPKLPTLEFRSATNVYTLEPEYYLQQIFDFGISLCMVSIIPVDLNKNTFILGDPFMRKYFTVFDYDNHTVGFALAKKKL	Literature-reported	Novel molecular targets for antimalarial chemotherapy. Int J Antimicrob Agents. 2007 Jul;30(1):4-10.	2	.	.	.	.	.	.	.	.	.	.	.	.	MetaCyc:MON-15375	.
TTXMNHO	Plasmodium Plasmepsin 2 (Malaria PLA2)	P46925	PLM2_PLAFA	Peptidase	Plasmepsin-2; PFAPD; Aspartic hemoglobinase II	Malaria PLA2	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.	EC 3.4.23.39	5BWY; 4Z22; 4YA8; 4Y6M; 4CKU	MDITVREHDFKHGFIKSNSTFDGLNIDNSKNKKKIQKGFQILYVLLFCSVMCGLFYYVYENVWLQRDNEMNEILKNSEHLTIGFKVENAHDRILKTIKTHKLKNYIKESVNFLNSGLTKTNYLGSSNDNIELVDFQNIMFYGDAEVGDNQQPFTFILDTGSANLWVPSVKCTTAGCLTKHLYDSSKSRTYEKDGTKVEMNYVSGTVSGFFSKDLVTVGNLSLPYKFIEVIDTNGFEPTYTASTFDGILGLGWKDLSIGSVDPIVVELKNQNKIENALFTFYLPVHDKHTGFLTIGGIEERFYEGPLTYEKLNHDLYWQITLDAHVGNIMLEKANCIVDSGTSAITVPTDFLNKMLQNLDVIKVPFLPFYVTLCNNSKLPTFEFTSENGKYTLEPEYYLQHIEDVGPGLCMLNIIGLDFPVPTFILGDPFMRKYFTVFDYDNHSVGIALAKKNL	Patented-recorded	Novel molecular targets for antimalarial chemotherapy. Int J Antimicrob Agents. 2007 Jul;30(1):4-10.	2	.	.	.	.	.	.	.	.	.	.	.	.	MetaCyc:MON-15374	.
TT5A6VQ	Plasmodium Plasmepsin 4 (Malaria PLA4)	Q8IM16	Q8IM16_PLAF7	.	Plasmepsin IV	Malaria PLA4	Plays a crucial role in this critical process which yields nutrients for parasite growth.	EC 3.4.23.-	1LS5	MALTVKEEEFSNTLIKNASAFDRLKLGNLKNLKIQKKLQFLYLILFVLITGVFFFFLIGNFYSHRKLYQVIKNTKHTTIGFKIDRPHDKVLSSVLKNKLSTYVKESFKFFKSGYAQKGYLGSENDSIELDDVANLMFYGEGQIGTNKQPFMFIFDTGSANLWVPSVNCDSIGCSTKHLYDASASKSYEKDGTKVEISYGSGTVRGYFSKDVISLGDLSLPYKFIEVTDADDLEPIYSGSEFDGILGLGWKDLSIGSIDPVVVELKKQNKIDNALFTFYLPVHDKHVGYLTIGGIESDFYEGPLTYEKLNHDLYWQIDLDIHFGKYVMQKANAVVDSGTSTITAPTSFLNKFFRDMNVIKVPFLPLYVTTCDNDDLPTLEFHSRNNKYTLEPEFYMDPLSDIDPALCMLYILPVDIDDNTFILGDPFMRKYFTVFDYEKESVGFAVAKNL	Literature-reported	"Activity and inhibition of plasmepsin IV, a new aspartic proteinase from the malaria parasite, Plasmodium falciparum. FEBS Lett. 2002 Feb 27;513(2-3):159-62."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT7PLWT	Plasmodium Plasmepsin 5 (Malaria PLA5)	Q8I6Z5	Q8I6Z5_PLAF7	.	Plasmepsin V	Malaria PLA5	"endoplasmic reticulum, integral component of membrane, aspartic-type endopeptidase activity, protein catabolic process, proteolysis"	EC 3.4.23.-	.	MNNYFLRKENFFILFCFVFVSIFFVSNVTIIKCNNVENKIDNVGKKIENVGKKIGDMENKNDNVENKNDNVGNKNDNVKNASSDLYKYKLYGDIDEYAYYFLDIDIGKPSQRISLILDTGSSSLSFPCNGCKDCGIHMEKPYNLNYSKTSSILYCNKSNCPYGLKCVGNKCEYLQSYCEGSQIYGFYFSDIVTLPSYNNKNKISFEKLMGCHMHEESLFLHQQATGVLGFSLTKPNGVPTFVDLLFKHTPSLKPIYSICVSEHGGELIIGGYEPDYFLSNQKEKQKMDKSDNNSSNKGNVSIKLKNNDKNDDEENNSKDVIVSNNVEDIVWQAITRKYYYYIKIYGLDLYGTNIMDKKELDMLVDSGSTFTHIPENIYNQINYYLDILCIHDMTNIYEINKRLKLTNESLNKPLVYFEDFKTALKNIIQNENLCIKIVDGVQCWKSLENLPNLYITLSNNYKMIWKPSSYLYKKESFWCKGLEKQVNNKPILGLTFFKNKQVIFDLQQNQIAFIESKCPSNLTSSRPRTFNEYREKENIFLKVSYINLYCLWLLLALTILLSLILYVRKMFYMDYFPLSDQNKSPIQEST	Literature-reported	Yield improvement and enzymatic dissection of Plasmodium falciparum plasmepsin V. Mol Biochem Parasitol. 2019 May 17;231:111188.	.	.	.	.	.	.	.	.	.	.	.	.	R-PFA-2132295: MHC class II antigen presentation; R-PFA-6798695: Neutrophil degranulation	.	.
TTMDS9W	Plasmodium Phosphoethanolamine N-methyltransferase (Malaria PNM)	Q8IDQ9	Q8IDQ9_PLAF7	Transferases of one-carbon groups	Phosphoethanolamine N-methyltransferase	Malaria PNM	"Golgi apparatus, phosphoethanolamine N-methyltransferase activity, phosphatidylcholine biosynthetic process"	EC 2.1.1.103	.	MTLIENLNSDKTFLENNQYTDEGVKVYEFIFGENYISSGGLEATKKILSDIELNENSKVLDIGSGLGGGCMYINEKYGAHTHGIDICSNIVNMANERVSGNNKIIFEANDILTKEFPENNFDLIYSRDAILHLSLENKNKLFQKCYKWLKPTGTLLITDYCATEKENWDDEFKEYVKQRKYTLITVEEYADILTACNFKNVVSKDLSDYWNQLLEVEHKYLHENKEEFLKLFSEKKFISLDDGWSRKIKDSKRKMQRWGYFKATKN	Literature-reported	A pathway for phosphatidylcholine biosynthesis in Plasmodium falciparum involving phosphoethanolamine methylation. Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):6206-11.	.	.	.	.	.	.	.	.	.	.	.	pfa00564: Glycerophospholipid metabolism	.	.	Q8IDQ9
TTVF721	Plasmodium Serine repeat antigen 4 (Malaria PvSERA4)	Q0PCM2	Q0PCM2_PLAVI	.	Serine repeat antigen 4	Malaria PvSERA4	"Constitutes major substrates of SUB1, may lead to the identification of parasite and/or host cell substrates and the underlying molecular mechanisms of proteolysis."	.	.	FNLDMPLATHSINKDPEISDYYLKNSSDYYENLYYKKFQGSGATGGAGKQWVQGASTVYGQEGDPKVADEAGGEAAQSITTHSRAEPAGDAPPSGPLHAGTDSEQGEGTGPTDGEGPTRVVDEKAQAGGPLTSPGTLQDAVAPGGPQGPPEQGSPGPQLPPVQPTAPVPPVLPVPPAAPLPDAPTNSTVPTTESDVKEVLH	Literature-reported	Genetic and structural characterization of PvSERA4: potential implication as therapeutic target for Plasmodium vivax malaria. J Biomol Struct Dyn. 2014 Apr;32(4):580-90.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTF1Z4J	Plasmodium Apicoplast ribosome (Malaria RPL18)	Q6LFD5	RK18_PLAF7	Ribosomal protein	"Putative 50S ribosomal protein L18, apicoplastic"	Malaria RPL18	"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."	.	.	MYISFILFSIIFIFLGVIENFIINKRVLYKPNFLLYSEKKNKKKSTPEQVTTRVNKDLKEKKRKRPRSKILECLLKEKVEKVEKVEKNSDENQCSNVDKEIREGKRVPRLRVRNTNNHIYASIIDDYKKYVLCSTCSRDATLSKILGTYRRKATNRVINNGRTIKSAWEIGKIIGKKALSKGIFKVRFDRARHPYAGKVEALAEGARAVGLLL	Literature-reported	An rRNA mutation identifies the apicoplast as the target for clindamycin in Toxoplasma gondii. Mol Microbiol. 2002 Mar;43(5):1309-18.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q6LFD5
TTO8YH2	Plasmodium Serine hydroxymethyltransferase (Malaria SHMT)	Q8I566	Q8I566_PLAF7	Methyltransferase	Serine methylase; SHMT; Glycine hydroxymethyltransferase	Malaria SHMT	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.	EC 2.1.2.1	4O6Z	MFNNDPLQKYDKELFDLLEKEKNRQIETINLIASENLTNTAVRECLGDRISNKYSEGYPHKRYYGGNDYVDKIEELCYKRALEAFNVSEEEWGVNVQPLSGSAANVQALYALVGVKGKIMGMHLCSGGHLTHGFFDEKKKVSITSDLFESKLYKCNSEGYVDMESVRNLALSFQPKVIICGYTSYPRDIDYKGFREICDEVNAYLFADISHISSFVACNLLNNPFTYADVVTTTTHKILRGPRSALIFFNKKRNPGIDQKINSSVFPSFQGGPHNNKIAAVACQLKEVNTPFFKEYTKQVLLNSKALAECLLKRNLDLVTNGTDNHLIVVDLRKYNITGSKLQETCNAINIALNKNTIPSDVDCVSPSGIRIGTPALTTRGCKEKDMEFIADMLLKAILLTDELQQKYGKKLVDFKKGLVNNPKIDELKKEVVQWAKNLPFA	Literature-reported	Mimosine targets serine hydroxymethyltransferase. J Biol Chem. 1996 Feb 2;271(5):2548-56.	2	.	.	.	.	.	.	.	.	.	.	"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"	R-HSA-196757:Metabolism of folate and pterines	.	.
TT7UPN3	Plasmodium Subtilisin-like protease (Malaria sub-1)	O61142	O61142_PLAFA	Protease	Subtilisin-like protease	Malaria sub-1	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. 	.	.	MMLNKKVVALCTLTLHLFCIFLCLGKEVRSEENGKIQDDAKKIVSELRFLEKVEDVIEKSNIGGNEVDADENSFNPDTEVPIEEIEEIKMRELKDVKEEKNKNDNHNNNNNNNNISSSSSSSSNTFGEEKEEVSKKKKKLRLIVSENHATTPSFFQESLLEPDVLSFLESKGNLSNLKNINSMIIELKEDTTDDELISYIKILEEKGALIESDKLVSADNIDISGIKDAIRRGEENIDVNDYKSMLEVENDAEDYDKMFGMFNESHAATSKRKRHSTNERGYDTFSSPSYKTYSKSDYLYDDDNNNNNYYYSHSSNGHNSSSRNSSSSRSRPGKYHFNDEFRNLQWGLDLSRLDETQELINEHQVMSTRICVIDSGIDYNHPDLKDNIELNLKELHGRKGFDDDNNGIVDDIYGANFVNNSGNPMDDNYHGTHVSGIISAIGNNNIGVVGVDVNSKLIICKALDEHKLGRLGDMFKCLDYCISRNAHMINGSFSFDEYSGIFNSSVEYLQRKGILFFVSASNCSHPKSSTPDIRKCDLSINAKYPPILSTVYDNVISVANLKKNDNNNHYSLSINSFYSNKYCQLAAPGTNIYSTAPHNSYRKLNGTSMAAPHVAAIASLIFSINPDLSYKKVIQILKDSIVYLPSLKNMVAWAGYADINKAVNLAIKSKKTYINSNISNKWKKKSRYLH	Literature-reported	A subtilisin-like protein in secretory organelles of Plasmodium falciparum merozoites. J Biol Chem. 1998 Sep 4;273(36):23398-409.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3B9JV	Plasmodium Subtilisin-like protease 2 (Malaria sub2)	Q9NG20	Q9NG20_PLABE	Protease	Subtilisin-like protease 2	Malaria sub2	Essential for red cell invasion.	.	.	MLRTFYVLSLMLIEFILHNGQYNKHICSKNSKKYNFVGKKHRILVSDIEDRENHIEGIADIYKPIFNIYEISAEFHKKKNIADKKKKRKYGINQSIEKRRIAEENERRQLNKTEGTQFLELSNRYPNIGKQNSQQNKVNEINNQNAASNSNDNIGNDNIGNDNIGNDEDDDEDDDEDLIEGRKDNLEEDDLIEKNDSNLPRGKMHEKEEKNKNINTTPGNESSNKNVNDKKKNGISLKDKIDNKQNNGGLKEKGNNLDDNIKTYTFDHYKIITNSDNILNDIKVDASDISKLSINSINIEYNEKNKAEYTHQRHIVLSNNGNRRYKIFLMTKNPKFTKTEDIEEPGMSFIQTETGENEDEKEDEENYLNENLYSGFGTIDYENDYSKKKKKIESEHASGLNDKISNSQNIEKSGSHENEKYNHGYIEKIRSFFSFLSMPSSKKDDSIGSEKKTEERSNTDSKAKLNKKTNDMAKKNNSNAFLSVDKIIDQYLLNLKNKNMKEQELIFIFHGNLDLHSKEMKTVINEANAKFTKYINMHFKDVKNIRYDISSPINFVCFFIPIIFDMSNLKILKEALIILNNELKDYIDNWNFSNTYVAFDNNYENEDIDNVMNKLNENMEKYIKKPKKLYNIKYSFLRKIWGLKSIISLSKNQDKKDAEIEEKILSALPKELKEYSTWNLSFIRVFNAWLLSGYGNKNVKICVIDSGIDKNHIDLANNIYTPKYSDRYEMTDELFDFMVKNPIDTSGHGTHVSGIAAASANSLGMVGVAPNINLISLRFIDGDNYGGSFHVIKAINICILNKSPIINASWGSRNYDTNMFLAIERLKYTFKGKGTVFIAAAGNENKNNDLYPIYPASYKLQNVYSVGSINKFLQISPFSNYGANSVHILAPGHHIYSTTPMNTYKMNTGTSMAAPHVSGVAGLIYSVCYKQGFIPDADEVLEIITRTSIKIVSKDKKTIHNSLINAEAAVLTTLLGGLWIQMDCHFAKFYLNENKQKSVPIVFSAYKDGVYESDIIIGIQPEDANSKEYGEIVIPIKILTNPKLKDFSLSPRVGKKIRIDENESNDDILSYICENALYNLYEHDNSFLISSLILFFIGIILIVLASIVFFLKHHQSKQRDGEKYMHQKMVDRTYNVKYNFKDSGTDGIKRINTLDDNINNHRNTQRFTIVQNEDNMYVLKKKSSIQAKYEPRNELVKRSLVKRPIVKHADINVNFSNVDVLYEPKNNSSE	Literature-reported	Gene targeting demonstrates that the Plasmodium berghei subtilisin PbSUB2 is essential for red cell invasion and reveals spontaneous genetic recomb... Cell Microbiol. 2004 Jan;6(1):65-78.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTN8WFB	Plasmodium Trophozoite cysteine proteinase (Malaria TCP)	P25805	CYSP_PLAFA	.	Trophozoite cysteine proteinase; TCP	Malaria TCP	Probably degrades erythrocyte hemoglobin.	EC 3.4.22.-	.	MVAIKEMKELAFARPSLVETLNKKKKFLKKKEKRTFVLSIYAFITFIIFCIGILYFTNKSSAHNNNNNKNEHSLKKEEIELLRVLLEKYKKQKDGILNESSNEEDEEKYTLNSETYNNKNNVSNIKNDSIKSKKEEYINLERILLEKYKKFINENNEENRKELSNILHKLLEINKLILREEKDDKKVYLINDNYDEKGALEIGMNEEMKYKKEDPINNIKYASKFFKFMKEHNKVYKNIDEQMRKFEIFKINYISIKNHNKLNKNAMYKKKVNQFSDYSEEELKEYFKTLLHVPNHMIEKYSKPFENHLKDNILISEFYTNGKRNEKDIFSKVPEILDYREKGIVHEPKDQGLCGSCWAFASVGNIESVFAKKNKNILSFSEQEVVDCSKDNFGCDGGHPFYSFLYVLQNELCLGDEYKYKAKDDMFCLNYRCKRKVSLSSIGAVKENQLILALNEVGPLSVNVGVNNDFVAYSEGVYNGTCSEELNHSVLLVGYGQVEKTKLNYNNKIQTYNTKENSNQPDDNIIYYWIIKNSWSKKWGENGFMRLSRNKNGDNVFCGIGEEVFYPIL	Literature-reported	Isolation and characterization of a cysteine proteinase gene of Plasmodium falciparum. Mol Biochem Parasitol. 1992 Mar;51(1):143-52.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P25805
TTCI81G	MALT lymphoma-associated translocation (MALT1)	Q9UDY8	MALT1_HUMAN	.	MALT lymphoma-associated translocation; Paracaspase	MALT1	"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."	EC 3.4.22.-	.	MSLLGDPLQALPPSAAPTGPLLAPPAGATLNRLREPLLRRLSELLDQAPEGRGWRRLAELAGSRGRLRLSCLDLEQCSLKVLEPEGSPSLCLLKLMGEKGCTVTELSDFLQAMEHTEVLQLLSPPGIKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPNGNTSELIFNAVHVKDAGFYVCRVNNNFTFEFSQWSQLDVCDIPESFQRSVDGVSESKLQICVEPTSQKLMPGSTLVLQCVAVGSPIPHYQWFKNELPLTHETKKLYMVPYVDLEHQGTYWCHVYNDRDSQDSKKVEIIIGRTDEAVECTEDELNNLGHPDNKEQTTDQPLAKDKVALLIGNMNYREHPKLKAPLVDVYELTNLLRQLDFKVVSLLDLTEYEMRNAVDEFLLLLDKGVYGLLYYAGHGYENFGNSFMVPVDAPNPYRSENCLCVQNILKLMQEKETGLNVFLLDMCRKRNDYDDTIPILDALKVTANIVFGYATCQGAEAFEIQHSGLANGIFMKFLKDRLLEDKKITVLLDEVAEDMGKCHLTKGKQALEIRSSLSEKRALTDPIQGTEYSAESLVRNLQWAKAHELPESMCLKFDCGVQIQLGFAAEFSNVMIIYTSIVYKPPEIIMCDAYVTDFPLDLDIDPKDANKGTPEETGSYLVSKDLPKHCLYTRLSSLQKLKEHLVFTVCLSYQYSGLEDTVEDKQEVNVGKPLIAKLDMHRGLGRKTCFQTCLMSNGPYQSSAATSGGAGHYHSLQDPFHGVYHSHPGNPSNVTPADSCHCSRTPDAFISSFAHHASCHFSRSNVPVETTDEIPFSFSDRLRISEK	Clinical trial	National Cancer Institute Drug Dictionary (drug name JNJ67856633).	.	.	.	.	.	.	.	.	.	.	.	hsa04064: NF-kappa B signaling pathway; hsa04625: C-type lectin receptor signaling pathway; hsa04660: T cell receptor signaling pathway; hsa04662: B cell receptor signaling pathway; hsa05131: Shigellosis; hsa05152: Tuberculosis	R-HSA-1169091: Activation of NF-kappaB in B cells; R-HSA-202424: Downstream TCR signaling; R-HSA-2871837: FCERI mediated NF-kB activation; R-HSA-5607764: CLEC7A (Dectin-1) signaling; R-HSA-5660668: CLEC7A/inflammasome pathway	.	Q9UDY8
TT34DCN	Golgi alpha-mannosidase II (MAN2A1)	Q16706	MA2A1_HUMAN	Glycosylase	"Mannosyloligosaccharide 1,31,6alphamannosidase; Mannosidase alpha class 2A member 1; Man II; MAN2A1; Alphamannosidase 2; AMan II"	MAN2A1	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.	EC 3.2.1.114	.	MKLSRQFTVFGSAIFCVVIFSLYLMLDRGHLDYPRNPRREGSFPQGQLSMLQEKIDHLERLLAENNEIISNIRDSVINLSESVEDGPKSSQSNFSQGAGSHLLPSQLSLSVDTADCLFASQSGSHNSDVQMLDVYSLISFDNPDGGVWKQGFDITYESNEWDTEPLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIENGQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYLLNRAGLSHMLIQRVHYAVKKHFALHKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRFGCPWGVPPETIHPGNVQSRARMLLDQYRKKSKLFRTKVLLAPLGDDFRYCEYTEWDLQFKNYQQLFDYMNSQSKFKVKIQFGTLSDFFDALDKADETQRDKGQSMFPVLSGDFFTYADRDDHYWSGYFTSRPFYKRMDRIMESHLRAAEILYYFALRQAHKYKINKFLSSSLYTALTEARRNLGLFQHHDAITGTAKDWVVVDYGTRLFHSLMVLEKIIGNSAFLLILKDKLTYDSYSPDTFLEMDLKQKSQDSLPQKNIIRLSAEPRYLVVYNPLEQDRISLVSVYVSSPTVQVFSASGKPVEVQVSAVWDTANTISETAYEISFRAHIPPLGLKVYKILESASSNSHLADYVLYKNKVEDSGIFTIKNMINTEEGITLENSFVLLRFDQTGLMKQMMTKEDGKHHEVNVQFSWYGTTIKRDKSGAYLFLPDGNAKPYVYTTPPFVRVTHGRIYSEVTCFFDHVTHRVRLYHIQGIEGQSVEVSNIVDIRKVYNREIAMKISSDIKSQNRFYTDLNGYQIQPRMTLSKLPLQANVYPMTTMAYIQDAKHRLTLLSAQSLGVSSLNSGQIEVIMDRRLMQDDNRGLEQGIQDNKITANLFRILLEKRSAVNTEEEKKSVSYPSLLSHITSSLMNHPVIPMANKFSSPTLELQGEFSPLQSSLPCDIHLVNLRTIQSKVGNGHSNEAALILHRKGFDCRFSSKGTGLFCSTTQGKILVQKLLNKFIVESLTPSSLSLMHSPPGTQNISEINLSPMEISTFRIQLR	Discontinued	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800010383)"	5	.	.	.	.	.	.	.	.	.	.	hsa00510:N-Glycan biosynthesis; hsa01100:Metabolic pathways	R-HSA-6811438: Intra-Golgi traffic; R-HSA-9694548: Maturation of spike protein; R-HSA-975578: Reactions specific to the complex N-glycan synthesis pathway	MetaCyc:HS03629-MON	Q16706
TTC12RO	Lysosomal alpha-mannosidase (MAN2B1)	O00754	MA2B1_HUMAN	Glycosyl hydrolase	Laman; Lysosomal acid alpha-mannosidase; Mannosidase alpha class 2B member 1; Mannosidase alpha-B	MAN2B1	Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. Cleaves all known types of alpha-mannosidic linkages.	EC 3.2.1.24	.	MGAYARASGVCARGCLDSAGPWTMSRALRPPLPPLCFFLLLLAAAGARAGGYETCPTVQPNMLNVHLLPHTHDDVGWLKTVDQYFYGIKNDIQHAGVQYILDSVISALLADPTRRFIYVEIAFFSRWWHQQTNATQEVVRDLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGNDGRPRVAWHIDPFGHSREQASLFAQMGFDGFFFGRLDYQDKWVRMQKLEMEQVWRASTSLKPPTADLFTGVLPNGYNPPRNLCWDVLCVDQPLVEDPRSPEYNAKELVDYFLNVATAQGRYYRTNHTVMTMGSDFQYENANMWFKNLDKLIRLVNAQQAKGSSVHVLYSTPACYLWELNKANLTWSVKHDDFFPYADGPHQFWTGYFSSRPALKRYERLSYNFLQVCNQLEALVGLAANVGPYGSGDSAPLNEAMAVLQHHDAVSGTSRQHVANDYARQLAAGWGPCEVLLSNALARLRGFKDHFTFCQQLNISICPLSQTAARFQVIVYNPLGRKVNWMVRLPVSEGVFVVKDPNGRTVPSDVVIFPSSDSQAHPPELLFSASLPALGFSTYSVAQVPRWKPQARAPQPIPRRSWSPALTIENEHIRATFDPDTGLLMEIMNMNQQLLLPVRQTFFWYNASIGDNESDQASGAYIFRPNQQKPLPVSRWAQIHLVKTPLVQEVHQNFSAWCSQVVRLYPGQRHLELEWSVGPIPVGDTWGKEVISRFDTPLETKGRFYTDSNGREILERRRDYRPTWKLNQTEPVAGNYYPVNTRIYITDGNMQLTVLTDRSQGGSSLRDGSLELMVHRRLLKDDGRGVSEPLMENGSGAWVRGRHLVLLDTAQAAAAGHRLLAEQEVLAPQVVLAPGGGAAYNLGAPPRTQFSGLRRDLPPSVHLLTLASWGPEMVLLRLEHQFAVGEDSGRNLSAPVTLNLRDLFSTFTITRLQETTLVANQLREAASRLKWTTNTGPTPHQTPYQLDPANITLEPMEIRTFLASVQWKEVDG	Successful	FDA Approved Drug Products from FDA Official Website. 2022. Application Number: 761261	.	.	.	.	.	.	.	.	.	.	.	hsa:4125	R-HSA-6798695;R-HSA-8853383;	.	O00754;
TTT2KE3	Alpha-mannosidase (MANA)	O00754; Q9Y2E5; Q9NTJ4	MA2B1_HUMAN; MA2B2_HUMAN; MA2C1_HUMAN	Glycosylase	Mannosidase alpha class 2	MAN2B1	Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. Cleaves all known types of alpha-mannosidic linkages.	.	.	MGAYARASGVCARGCLDSAGPWTMSRALRPPLPPLCFFLLLLAAAGARAGGYETCPTVQPNMLNVHLLPHTHDDVGWLKTVDQYFYGIKNDIQHAGVQYILDSVISALLADPTRRFIYVEIAFFSRWWHQQTNATQEVVRDLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGNDGRPRVAWHIDPFGHSREQASLFAQMGFDGFFFGRLDYQDKWVRMQKLEMEQVWRASTSLKPPTADLFTGVLPNGYNPPRNLCWDVLCVDQPLVEDPRSPEYNAKELVDYFLNVATAQGRYYRTNHTVMTMGSDFQYENANMWFKNLDKLIRLVNAQQAKGSSVHVLYSTPACYLWELNKANLTWSVKHDDFFPYADGPHQFWTGYFSSRPALKRYERLSYNFLQVCNQLEALVGLAANVGPYGSGDSAPLNEAMAVLQHHDAVSGTSRQHVANDYARQLAAGWGPCEVLLSNALARLRGFKDHFTFCQQLNISICPLSQTAARFQVIVYNPLGRKVNWMVRLPVSEGVFVVKDPNGRTVPSDVVIFPSSDSQAHPPELLFSASLPALGFSTYSVAQVPRWKPQARAPQPIPRRSWSPALTIENEHIRATFDPDTGLLMEIMNMNQQLLLPVRQTFFWYNASIGDNESDQASGAYIFRPNQQKPLPVSRWAQIHLVKTPLVQEVHQNFSAWCSQVVRLYPGQRHLELEWSVGPIPVGDTWGKEVISRFDTPLETKGRFYTDSNGREILERRRDYRPTWKLNQTEPVAGNYYPVNTRIYITDGNMQLTVLTDRSQGGSSLRDGSLELMVHRRLLKDDGRGVSEPLMENGSGAWVRGRHLVLLDTAQAAAAGHRLLAEQEVLAPQVVLAPGGGAAYNLGAPPRTQFSGLRRDLPPSVHLLTLASWGPEMVLLRLEHQFAVGEDSGRNLSAPVTLNLRDLFSTFTITRLQETTLVANQLREAASRLKWTTNTGPTPHQTPYQLDPANITLEPMEIRTFLASVQWKEVDG	Clinical trial	ClinicalTrials.gov (NCT01681953) A Placebo-Controlled Phase 3 Trial of Repeated Lamazym Treatment of Subjects With Alpha-Mannosidosis. U.S. National Institutes of Health.	25	.	.	.	.	.	.	.	.	.	.	hsa00511: Other glycan degradation; hsa04142: Lysosome	R-HSA-6798695: Neutrophil degranulation; R-HSA-8853383: Lysosomal oligosaccharide catabolism	.	O00754
TT56RYE	Mesencephalic astrocyte-derived neurotrophic factor (ARMET)	P55145	MANF_HUMAN	.	Mesencephalic astrocytederived neurotrophic factor; MANF; Argininerich protein	MANF	"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."	.	2W51; 2KVE; 2KVD	MRRMWATQGLAVALALSVLPGSRALRPGDCEVCISYLGRFYQDLKDRDVTFSPATIENELIKFCREARGKENRLCYYIGATDDAATKIINEVSKPLAHHIPVEKICEKLKKKDSQICELKYDKQIDLSTVDLKKLRVKELKKILDDWGETCKGCAEKSDYIRKINELMPKYAPKAASARTDL	Literature-reported	Armet/Manf and Creld2 are components of a specialized ER stress response provoked by inappropriate formation of disulphide bonds: implications for ... Hum Mol Genet. 2013 Dec 20;22(25):5262-75.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-114608: Platelet degranulation	.	P55145
TT3WG5C	Monoamine oxidase type A (MAO-A)	P21397	AOFA_HUMAN	CH-NH(2) donor oxidoreductase	Monoamine oxidase A; Amine oxidase [flavin-containing] A	MAOA	"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."	EC 1.4.3.4	2Z5Y; 2Z5X; 2BXS; 2BXR; 1H8Q	MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIAYLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNINVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKDVPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS	Successful	"Tramadol and another atypical opioid meperidine have exaggerated serotonin syndrome behavioural effects, but decreased analgesic effects, in genetically deficient serotonin transporter (SERT) mice. Int J Neuropsychopharmacol. 2009 Mar 11:1-11."	34	EC:1.4	CH NH2 donor oxidoreductase	flavin monoamine oxidase family.	1.4.3.4	Acting on the CH-NH2 group of donors	Flavin containing amine oxidoreductase	PF01593	PF01593; Amino_oxidase	.	.	"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"	R-HSA-181430:Norepinephrine Neurotransmitter Release Cycle	MetaCyc:HS01798-MON	P21397
TTGP7BY	Monoamine oxidase type B (MAO-B)	P27338	AOFB_HUMAN	CH-NH(2) donor oxidoreductase	MAO-B; Amine oxidase [flavin-containing] B	MAOB	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.	EC 1.4.3.4	6FWC; 6FW0; 6FVZ; 5MRL; 4CRT	MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWRTMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQTRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYYKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEERLKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDRIYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTTFLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV	Successful	"Tranylcypromine: new perspectives on an ""old"" drug. Eur Arch Psychiatry Clin Neurosci. 2006 Aug;256(5):268-73."	34	EC:1.4	CH NH2 donor oxidoreductase	flavin monoamine oxidase family.	1.4.3.4	Acting on the CH-NH2 group of donors	Flavin containing amine oxidoreductase	PF01593	PF01593; Amino_oxidase	.	.	"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"	R-HSA-141333: Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB	MetaCyc:HS00966-MON	P27338
TT1EDJZ	Microtubule-associated protein (MAP)	P78559; P46821	MAP1A_HUMAN; MAP1B_HUMAN	.	Microtubule-associated protein 1; MAP-1	MAP1A	"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."	.	.	MDGVAEFSEYVSETVDVPSPFDLLEPPTSGGFLKLSKPCCYIFPGGRGDSALFAVNGFNILVDGGSDRKSCFWKLVRHLDRIDSVLLTHIGADNLPGINGLLQRKVAELEEEQSQGSSSYSDWVKNLISPELGVVFFNVPEKLRLPDASRKAKRSIEEACLTLQHLNRLGIQAEPLYRVVSNTIEPLTLFHKMGVGRLDMYVLNPVKDSKEMQFLMQKWAGNSKAKTGIVLPNGKEAEISVPYLTSITALVVWLPANPTEKIVRVLFPGNAPQNKILEGLEKLRHLDFLRYPVATQKDLASGAVPTNLKPSKIKQRADSKESLKATTKTAVSKLAKREEVVEEGAKEARSELAKELAKTEKKAKESSEKPPEKPAKPERVKTESSEALKAEKRKLIKDKVGKKHLKEKISKLEEKKDKEKKEIKKERKELKKDEGRKEEKKDAKKEEKRKDTKPELKKISKPDLKPFTPEVRKTLYKAKVPGRVKIDRSRAIRGEKELSSEPQTPPAQKGTVPLPTISGHRELVLSSPEDLTQDFEEMKREERALLAEQRDTGLGDKPFPLDTAEEGPPSTAIQGTPPSVPGLGQEEHVMKEKELVPEVPEEQGSKDRGLDSGAETEEEKDTWEEKKQREAERLPDRTEAREESEPEVKEDVIEKAELEEMEEVHPSDEEEEDATKAEGFYQKHMQEPLKVTPRSREAFGGRELGLQGKAPEKETSLFLSSLTTPAGATEHVSYIQDETIPGYSETEQTISDEEIHDEPEERPAPPRFHTSTYDLPGPEGAGPFEASQPADSAVPATSGKVYGTPETELTYPTNIVAAPLAEEEHVSSATSITECDKLSSFATSVAEDQSVASLTAPQTEETGKSSLLLDTVTSIPSSRTEATQGLDYVPSAGTISPTSSLEEDKGFKSPPCEDFSVTGESEKRGEIIGKGLSGERAVEEEEEETANVEMSEKLCSQYGTPVFSAPGHALHPGEPALGEAEERCLSPDDSTVKMASPPPSGPPSATHTPFHQSPVEEKSEPQDFQEADSWGDTKRTPGVGKEDAAEETVKPGPEEGTLEKEEKVPPPRSPQAQEAPVNIDEGLTGCTIQLLPAQDKAIVFEIMEAGEPTGPILGAEALPGGLRTLPQEPGKPQKDEVLRYPDRSLSPEDAESLSVLSVPSPDTANQEPTPKSPCGLTEQYLHKDRWPEVSPEDTQSLSLSEESPSKETSLDVSSKQLSPESLGTLQFGELNLGKEEMGHLMQAEDTSHHTAPMSVPEPHAATASPPTDGTTRYSAQTDITDDSLDRKSPASSFSHSTPSGNGKYLPGAITSPDEHILTPDSSFSKSPESLPGPALEDIAIKWEDKVPGLKDRTSEQKKEPEPKDEVLQQKDKTLEHKEVVEPKDTAIYQKDEALHVKNEAVKQQDKALEQKGRDLEQKDTALEQKDKALEPKDKDLEEKDKALEQKDKIPEEKDKALEQKDTALEQKDKALEPKDKDLEQKDRVLEQKEKIPEEKDKALDQKVRSVEHKAPEDTVAEMKDRDLEQTDKAPEQKHQAQEQKDKVSEKKDQALEQKYWALGQKDEALEQNIQALEENHQTQEQESLVQEDKTRKPKMLEEKSPEKVKAMEEKLEALLEKTKALGLEESLVQEGRAREQEEKYWRGQDVVQEWQETSPTREEPAGEQKELAPAWEDTSPEQDNRYWRGREDVALEQDTYWRELSCERKVWFPHELDGQGARPHYTEERESTFLDEGPDDEQEVPLREHATRSPWASDFKDFQESSPQKGLEVERWLAESPVGLPPEEEDKLTRSPFEIISPPASPPEMVGQRVPSAPGQESPIPDPKLMPHMKNEPTTPSWLADIPPWVPKDRPLPPAPLSPAPGPPTPAPESHTPAPFSWGTAEYDSVVAAVQEGAAELEGGPYSPLGKDYRKAEGEREEEGRAEAPDKSSHSSKVPEASKSHATTEPEQTEPEQREPTPYPDERSFQYADIYEQMMLTGLGPACPTREPPLGAAGDWPPCLSTKEAAAGRNTSAEKELSSPISPKSLQSDTPTFSYAALAGPTVPPRPEPGPSMEPSLTPPAVPPRAPILSKGPSPPLNGNILSCSPDRRSPSPKESGRSHWDDSTSDSELEKGAREQPEKEAQSPSPPHPIPMGSPTLWPETEAHVSPPLDSHLGPARPSLDFPASAFGFSSLQPAPPQLPSPAEPRSAPCGSLAFSGDRALALAPGPPTRTRHDEYLEVTKAPSLDSSLPQLPSPSSPGAPLLSNLPRPASPALSEGSSSEATTPVISSVAERFSPSLEAAEQESGELDPGMEPAAHSLWDLTPLSPAPPASLDLALAPAPSLPGDMGDGILPCHLECSEAATEKPSPFQVPSEDCAANGPTETSPNPPGPAPAKAENEEAAACPAWERGAWPEGAERSSRPDTLLSPEQPVCPAGGSGGPPSSASPEVEAGPQGCATEPRPHRGELSPSFLNPPLPPSIDDRDLSTEEVRLVGRGGRRRVGGPGTTGGPCPVTDETPPTSASDSGSSQSDSDVPPETEECPSITAEAALDSDEDGDFLPVDKAGGVSGTHHPRPGHDPPPLPQPDPRPSPPRPDVCMADPEGLSSESGRVERLREKEKVQGRVGRRAPGKAKPASPARRLDLRGKRSPTPGKGPADRASRAPPRPRSTTSQVTPAEEKDGHSPMSKGLVNGLKAGPMALSSKGSSGAPVYVDLAYIPNHCSGKTADLDFFRRVRASYYVVSGNDPANGEPSRAVLDALLEGKAQWGENLQVTLIPTHDTEVTREWYQQTHEQQQQLNVLVLASSSTVVMQDESFPACKIEF	Successful	Medicinal plants in therapy. Bull World Health Organ. 1985;63(6):965-81.	34	.	.	.	.	.	.	.	.	.	.	hsa03250: Viral life cycle - HIV-1	.	.	.
TTIDAPM	ERK activator kinase 1 (MEK1)	Q02750	MP2K1_HUMAN	Kinase	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	MAP2K1	"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."	EC 2.7.12.2	5YT3; 5HZE; 5EYM; 5BX0; 4U81	MPKKKPTPIQLNPAPDGSAVNGTSSAETNLEALQKKLEELELDEQQRKRLEAFLTQKQKVGELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYGMDSRPPMAIFELLDYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAEEVDFAGWLCSTIGLNQPSTPTHAAGV	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.	2.7.12.2	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	Q02750
TTAW3TO	HUMAN ERK activator kinase 1 (MEK1)	Q02750	MP2K1_HUMAN	Kinase	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	MAP2K1	"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."	EC 2.7.12.2	5YT3; 5HZE; 5EYM; 5BX0; 4U81	MPKKKPTPIQLNPAPDGSAVNGTSSAETNLEALQKKLEELELDEQQRKRLEAFLTQKQKVGELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYGMDSRPPMAIFELLDYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAEEVDFAGWLCSTIGLNQPSTPTHAAGV	.	Coronaviruses - drug discovery and therapeutic options. Nat Rev Drug Discov. 2016 May;15(5):327-47.	25	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.	2.7.12.2	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	"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; 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; hsa04072: Phospholipase D signaling pathway; hsa04114: Oocyte meiosis; hsa04140: Autophagy - animal; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04210: Apoptosis; hsa04218: Cellular senescence; hsa04270: Vascular smooth muscle contraction; hsa04370: VEGF signaling pathway; hsa04371: Apelin signaling pathway; hsa04380: Osteoclast differentiation; hsa04510: Focal adhesion; hsa04540: Gap junction; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04613: Neutrophil extracellular trap formation; 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; hsa04926: Relaxin signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action; hsa04929: GnRH secretion; hsa04934: Cushing syndrome; hsa04935: Growth hormone synthesis, secretion and action; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05034: Alcoholism; hsa05132: Salmonella infection; hsa05135: Yersinia infection; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; 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; hsa05205: Proteoglycans in cancer; hsa05206: MicroRNAs in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; 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"	R-HSA-110056: MAPK3 (ERK1) activation; R-HSA-170968: Frs2-mediated activation; R-HSA-445144: Signal transduction by L1; 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; R-HSA-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9652169: Signaling by MAP2K mutants; R-HSA-9656223: Signaling by RAF1 mutants	.	Q02750
TT8H9GB	MEK2 messenger RNA (MEK2 mRNA)	P36507	MP2K2_HUMAN	mRNA target	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)	MAP2K2	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.	EC 2.7.12.2	4H3Q; 1S9I	MLARRKPVLPALTINPTIAEGPSPTSEGASEANLVDLQKKLEELELDEQQKKRLEAFLTQKAKVGELKDDDFERISELGAGNGGVVTKVQHRPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMAPERLQGTHYSVQSDIWSMGLSLVELAVGRYPIPPPDAKELEAIFGRPVVDGEEGEPHSISPRPRPPGRPVSGHGMDSRPAMAIFELLDYIVNEPPPKLPNGVFTPDFQEFVNKCLIKNPAERADLKMLTNHTFIKRSEVEEVDFAGWLCKTLRLNQPGTPTRTAV	Literature-reported	"US patent application no. 5,959,097, Antisense modulation of MEK2 expression."	0	mRNA	mRNA target	.	.	.	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	P36507
TTTW2NY	ERK activator kinase 2 (MEK2)	P36507	MP2K2_HUMAN	Kinase	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	MAP2K2	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.	EC 2.7.12.2	4H3Q; 1S9I	MLARRKPVLPALTINPTIAEGPSPTSEGASEANLVDLQKKLEELELDEQQKKRLEAFLTQKAKVGELKDDDFERISELGAGNGGVVTKVQHRPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMAPERLQGTHYSVQSDIWSMGLSLVELAVGRYPIPPPDAKELEAIFGRPVVDGEEGEPHSISPRPRPPGRPVSGHGMDSRPAMAIFELLDYIVNEPPPKLPNGVFTPDFQEFVNKCLIKNPAERADLKMLTNHTFIKRSEVEEVDFAGWLCKTLRLNQPGTPTRTAV	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.	2.7.12.2 	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	P36507
TTWX403	HUMAN ERK activator kinase 2 (MEK2)	P36507	MP2K2_HUMAN	Kinase	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	MAP2K2	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.	EC 2.7.12.2	4H3Q; 1S9I	MLARRKPVLPALTINPTIAEGPSPTSEGASEANLVDLQKKLEELELDEQQKKRLEAFLTQKAKVGELKDDDFERISELGAGNGGVVTKVQHRPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMAPERLQGTHYSVQSDIWSMGLSLVELAVGRYPIPPPDAKELEAIFGRPVVDGEEGEPHSISPRPRPPGRPVSGHGMDSRPAMAIFELLDYIVNEPPPKLPNGVFTPDFQEFVNKCLIKNPAERADLKMLTNHTFIKRSEVEEVDFAGWLCKTLRLNQPGTPTRTAV	.	Coronaviruses - drug discovery and therapeutic options. Nat Rev Drug Discov. 2016 May;15(5):327-47.	25	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.	2.7.12.2 	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	"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; hsa04022: cGMP-PKG signaling pathway; hsa04024: cAMP signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04068: FoxO signaling pathway; hsa04071: Sphingolipid signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04140: Autophagy - animal; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04210: Apoptosis; hsa04218: Cellular senescence; hsa04270: Vascular smooth muscle contraction; hsa04370: VEGF signaling pathway; hsa04371: Apelin signaling pathway; hsa04540: Gap junction; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04613: Neutrophil extracellular trap formation; 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; hsa04926: Relaxin signaling pathway; hsa04929: GnRH secretion; hsa04934: Cushing syndrome; hsa04935: Growth hormone synthesis, secretion and action; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05132: Salmonella infection; hsa05135: Yersinia infection; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; 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; hsa05205: Proteoglycans in cancer; hsa05206: MicroRNAs in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05210: Colorectal 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; 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"	R-HSA-112411: MAPK1 (ERK2) activation; R-HSA-170968: Frs2-mediated activation; R-HSA-445144: Signal transduction by L1; 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-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9652169: Signaling by MAP2K mutants; R-HSA-9656223: Signaling by RAF1 mutants	.	P36507
TTV3O87	ERK activator kinase 5 (MAP2K5)	Q13163	MP2K5_HUMAN	Kinase	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	MAP2K5	"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."	EC 2.7.12.2	4IC7; 2O2V; 2NPT	MLWLALGPFPAMENQVLVIRIKIPNSGAVDWTVHSGPQLLFRDVLDVIGQVLPEATTTAFEYEDEDGDRITVRSDEEMKAMLSYYYSTVMEQQVNGQLIEPLQIFPRACKPPGERNIHGLKVNTRAGPSQHSSPAVSDSLPSNSLKKSSAELKKILANGQMNEQDIRYRDTLGHGNGGTVYKAYHVPSGKILAVKVILLDITLELQKQIMSELEILYKCDSSYIIGFYGAFFVENRISICTEFMDGGSLDVYRKMPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNQGSLMPLQLLQCIVDEDSPVLPVGEFSEPFVHFITQCMRKQPKERPAPEELMGHPFIVQFNDGNAAVVSMWVCRALEERRSQQGPP	Literature-reported	Identification of pharmacological inhibitors of the MEK5/ERK5 pathway. Biochem Biophys Res Commun. 2008 Dec 5;377(1):120-5.	0	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.	2.7.12.2	Transferring phosphorus-containing groups	PB1 domain; Protein kinase domain	PF00564; PF00069	PF00564; PB1; PF00069; Pkinase	.	.	hsa04010: MAPK signaling pathway; hsa04540: Gap junction; hsa04722: Neurotrophin signaling pathway; hsa04921: Oxytocin signaling pathway; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-198765: Signalling to ERK5	.	Q13163
TT6QY3J	ERK activator kinase 7 (MAP2K7)	O14733	MP2K7_HUMAN	Kinase	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	MAP2K7	"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."	EC 2.7.12.2	6QHR; 6QHO; 6QG7; 6QG4; 6QFT	MAASSLEQKLSRLEAKLKQENREARRRIDLNLDISPQRPRPTLQLPLANDGGSRSPSSESSPQHPTPPARPRHMLGLPSTLFTPRSMESIEIDQKLQEIMKQTGYLTIGGQRYQAEINDLENLGEMGSGTCGQVWKMRFRKTGHVIAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVQCFGTFITNTDVFIAMELMGTCAEKLKKRMQGPIPERILGKMTVAIVKALYYLKEKHGVIHRDVKPSNILLDERGQIKLCDFGISGRLVDSKAKTRSAGCAAYMAPERIDPPDPTKPDYDIRADVWSLGISLVELATGQFPYKNCKTDFEVLTKVLQEEPPLLPGHMGFSGDFQSFVKDCLTKDHRKRPKYNKLLEHSFIKRYETLEVDVASWFKDVMAKTESPRTSGVLSQPHLPFFR	Literature-reported	miR-125b inhibited epithelial-mesenchymal transition of triple-negative breast cancer by targeting MAP2K7. Onco Targets Ther. 2016 May 4;9:2639-48.	.	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.	2.7.12.2	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04010: MAPK signaling pathway; hsa04012: ErbB signaling pathway; hsa04141: Protein processing in endoplasmic reticulum; hsa04380: Osteoclast differentiation; hsa04530: Tight junction; hsa04620: Toll-like receptor signaling pathway; hsa04660: T cell receptor signaling pathway; hsa04664: Fc epsilon RI signaling pathway; hsa04668: TNF signaling pathway; hsa04722: Neurotrophin signaling pathway; hsa04912: GnRH signaling pathway; hsa04926: Relaxin signaling pathway; hsa04936: Alcoholic liver disease; hsa05010: Alzheimer disease; hsa05016: Huntington disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05132: Salmonella infection; hsa05135: Yersinia infection; hsa05161: Hepatitis B; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05417: Lipid and atherosclerosis; hsa05418: Fluid shear stress and atherosclerosis	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-5210891: Uptake and function of anthrax toxins	.	O14733
TTW8TJI	MEKK1 messenger RNA (MAP3K1 mRNA)	Q13233	M3K1_HUMAN	mRNA target	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)	MAP3K1	"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."	EC 2.7.11.25	.	MAAAAGNRASSSGFPGARATSPEAGGGGGALKASSAPAAAAGLLREAGSGGRERADWRRRQLRKVRSVELDQLPEQPLFLAASPPASSTSPSPEPADAAGSGTGFQPVAVPPPHGAASRGGAHLTESVAAPDSGASSPAAAEPGEKRAPAAEPSPAAAPAGREMENKETLKGLHKMDDRPEERMIREKLKATCMPAWKHEWLERRNRRGPVVVKPIPVKGDGSEMNHLAAESPGEVQASAASPASKGRRSPSPGNSPSGRTVKSESPGVRRKRVSPVPFQSGRITPPRRAPSPDGFSPYSPEETNRRVNKVMRARLYLLQQIGPNSFLIGGDSPDNKYRVFIGPQNCSCARGTFCIHLLFVMLRVFQLEPSDPMLWRKTLKNFEVESLFQKYHSRRSSRIKAPSRNTIQKFVSRMSNSHTLSSSSTSTSSSENSIKDEEEQMCPICLLGMLDEESLTVCEDGCRNKLHHHCMSIWAEECRRNREPLICPLCRSKWRSHDFYSHELSSPVDSPSSLRAAQQQTVQQQPLAGSRRNQESNFNLTHYGTQQIPPAYKDLAEPWIQVFGMELVGCLFSRNWNVREMALRRLSHDVSGALLLANGESTGNSGGSSGSSPSGGATSGSSQTSISGDVVEACCSVLSMVCADPVYKVYVAALKTLRAMLVYTPCHSLAERIKLQRLLQPVVDTILVKCADANSRTSQLSISTLLELCKGQAGELAVGREILKAGSIGIGGVDYVLNCILGNQTESNNWQELLGRLCLIDRLLLEFPAEFYPHIVSTDVSQAEPVEIRYKKLLSLLTFALQSIDNSHSMVGKLSRRIYLSSARMVTTVPHVFSKLLEMLSVSSSTHFTRMRRRLMAIADEVEIAEAIQLGVEDTLDGQQDSFLQASVPNNYLETTENSSPECTVHLEKTGKGLCATKLSASSEDISERLASISVGPSSSTTTTTTTTEQPKPMVQTKGRPHSQCLNSSPLSHHSQLMFPALSTPSSSTPSVPAGTATDVSKHRLQGFIPCRIPSASPQTQRKFSLQFHRNCPENKDSDKLSPVFTQSRPLPSSNIHRPKPSRPTPGNTSKQGDPSKNSMTLDLNSSSKCDDSFGCSSNSSNAVIPSDETVFTPVEEKCRLDVNTELNSSIEDLLEASMPSSDTTVTFKSEVAVLSPEKAENDDTYKDDVNHNQKCKEKMEAEEEEALAIAMAMSASQDALPIVPQLQVENGEDIIIIQQDTPETLPGHTKAKQPYREDTEWLKGQQIGLGAFSSCYQAQDVGTGTLMAVKQVTYVRNTSSEQEEVVEALREEIRMMSHLNHPNIIRMLGATCEKSNYNLFIEWMAGGSVAHLLSKYGAFKESVVINYTEQLLRGLSYLHENQIIHRDVKGANLLIDSTGQRLRIADFGAAARLASKGTGAGEFQGQLLGTIAFMAPEVLRGQQYGRSCDVWSVGCAIIEMACAKPPWNAEKHSNHLALIFKIASATTAPSIPSHLSPGLRDVALRCLELQPQDRPPSRELLKHPVFRTTW	Literature-reported	"US patent application no. 6,168,950, Antisense modulation of MEKK1 expression."	0	mRNA	mRNA target	.	.	.	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	Q13233
TTQBCEJ	MAPK/ERK kinase kinase 1 (MAP3K1)	Q13233	M3K1_HUMAN	Kinase	Mitogenactivated protein kinase kinase kinase 1; Mitogen-activated protein kinase kinase kinase 1; MEKK1; MEKK 1; MEKK; MEK kinase 1; MAPKKK1	MAP3K1	"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."	EC 2.7.11.25	.	MAAAAGNRASSSGFPGARATSPEAGGGGGALKASSAPAAAAGLLREAGSGGRERADWRRRQLRKVRSVELDQLPEQPLFLAASPPASSTSPSPEPADAAGSGTGFQPVAVPPPHGAASRGGAHLTESVAAPDSGASSPAAAEPGEKRAPAAEPSPAAAPAGREMENKETLKGLHKMDDRPEERMIREKLKATCMPAWKHEWLERRNRRGPVVVKPIPVKGDGSEMNHLAAESPGEVQASAASPASKGRRSPSPGNSPSGRTVKSESPGVRRKRVSPVPFQSGRITPPRRAPSPDGFSPYSPEETNRRVNKVMRARLYLLQQIGPNSFLIGGDSPDNKYRVFIGPQNCSCARGTFCIHLLFVMLRVFQLEPSDPMLWRKTLKNFEVESLFQKYHSRRSSRIKAPSRNTIQKFVSRMSNSHTLSSSSTSTSSSENSIKDEEEQMCPICLLGMLDEESLTVCEDGCRNKLHHHCMSIWAEECRRNREPLICPLCRSKWRSHDFYSHELSSPVDSPSSLRAAQQQTVQQQPLAGSRRNQESNFNLTHYGTQQIPPAYKDLAEPWIQVFGMELVGCLFSRNWNVREMALRRLSHDVSGALLLANGESTGNSGGSSGSSPSGGATSGSSQTSISGDVVEACCSVLSMVCADPVYKVYVAALKTLRAMLVYTPCHSLAERIKLQRLLQPVVDTILVKCADANSRTSQLSISTLLELCKGQAGELAVGREILKAGSIGIGGVDYVLNCILGNQTESNNWQELLGRLCLIDRLLLEFPAEFYPHIVSTDVSQAEPVEIRYKKLLSLLTFALQSIDNSHSMVGKLSRRIYLSSARMVTTVPHVFSKLLEMLSVSSSTHFTRMRRRLMAIADEVEIAEAIQLGVEDTLDGQQDSFLQASVPNNYLETTENSSPECTVHLEKTGKGLCATKLSASSEDISERLASISVGPSSSTTTTTTTTEQPKPMVQTKGRPHSQCLNSSPLSHHSQLMFPALSTPSSSTPSVPAGTATDVSKHRLQGFIPCRIPSASPQTQRKFSLQFHRNCPENKDSDKLSPVFTQSRPLPSSNIHRPKPSRPTPGNTSKQGDPSKNSMTLDLNSSSKCDDSFGCSSNSSNAVIPSDETVFTPVEEKCRLDVNTELNSSIEDLLEASMPSSDTTVTFKSEVAVLSPEKAENDDTYKDDVNHNQKCKEKMEAEEEEALAIAMAMSASQDALPIVPQLQVENGEDIIIIQQDTPETLPGHTKAKQPYREDTEWLKGQQIGLGAFSSCYQAQDVGTGTLMAVKQVTYVRNTSSEQEEVVEALREEIRMMSHLNHPNIIRMLGATCEKSNYNLFIEWMAGGSVAHLLSKYGAFKESVVINYTEQLLRGLSYLHENQIIHRDVKGANLLIDSTGQRLRIADFGAAARLASKGTGAGEFQGQLLGTIAFMAPEVLRGQQYGRSCDVWSVGCAIIEMACAKPPWNAEKHSNHLALIFKIASATTAPSIPSHLSPGLRDVALRCLELQPQDRPPSRELLKHPVFRTTW	Clinical trial	Pharmacological inhibitors of MAPK pathways. Trends Pharmacol Sci. 2002 Jan;23(1):40-5.	21	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.	2.7.11.25	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	Q13233
TT9FN4J	Mixed lineage kinase 2 (MAP3K10)	Q02779	M3K10_HUMAN	Kinase	Protein kinase MST; Mitogen-activated protein kinase kinase kinase 10; MST; MLK2	MAP3K10	Activates the JUN N-terminal pathway.	EC 2.7.11.25	2RF0	MEEEEGAVAKEWGTTPAGPVWTAVFDYEAAGDEELTLRRGDRVQVLSQDCAVSGDEGWWTGQLPSGRVGVFPSNYVAPGAPAAPAGLQLPQEIPFHELQLEEIIGVGGFGKVYRALWRGEEVAVKAARLDPEKDPAVTAEQVCQEARLFGALQHPNIIALRGACLNPPHLCLVMEYARGGALSRVLAGRRVPPHVLVNWAVQVARGMNYLHNDAPVPIIHRDLKSINILILEAIENHNLADTVLKITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTKEKELRSREEELLRAAQEQRFQEEQLRRREQELAEREMDIVERELHLLMCQLSQEKPRVRKRKGNFKRSRLLKLREGGSHISLPSGFEHKITVQASPTLDKRKGSDGASPPASPSIIPRLRAIRLTPVDCGGSSSGSSSGGSGTWSRGGPPKKEELVGGKKKGRTWGPSSTLQKERVGGEERLKGLGEGSKQWSSSAPNLGKSPKHTPIAPGFASLNEMEEFAEAEDGGSSVPPSPYSTPSYLSVPLPAEPSPGARAPWEPTPSAPPARWGHGARRRCDLALLGCATLLGAVGLGADVAEARAADGEEQRRWLDGLFFPRAGRFPRGLSPPARPHGRREDVGPGLGLAPSATLVSLSSVSDCNSTRSLLRSDSDEAAPAAPSPPPSPPAPTPTPSPSTNPLVDLELESFKKDPRQSLTPTHVTAACAVSRGHRRTPSDGALGQRGPPEPAGHGPGPRDLLDFPRLPDPQALFPARRRPPEFPGRPTTLTFAPRPRPAASRPRLDPWKLVSFGRTLTISPPSRPDTPESPGPPSVQPTLLDMDMEGQNQDSTVPLCGAHGSH	Literature-reported	"Discovery, synthesis, and characterization of an orally bioavailable, brain penetrant inhibitor of mixed lineage kinase 3. J Med Chem. 2013 Oct 24;56(20):8032-48."	0	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.	2.7.11.25	Transferring phosphorus-containing groups	Protein tyrosine kinase; Variant SH3 domain	PF07714; PF14604	PF07714; Pkinase_Tyr; PF14604; SH3_9	.	.	hsa05016: Huntington disease; hsa05022: Pathways of neurodegeneration - multiple diseases	.	.	Q02779
TTETX6Q	Mixed lineage kinase 3 (MAP3K11)	Q16584	M3K11_HUMAN	Kinase	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	MAP3K11	"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."	EC 2.7.11.25	6CQ7; 6AQB; 5K28; 5K26	MEPLKSLFLKSPLGSWNGSGSGGGGGGGGGRPEGSPKAAGYANPVWTALFDYEPSGQDELALRKGDRVEVLSRDAAISGDEGWWAGQVGGQVGIFPSNYVSRGGGPPPCEVASFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLLQPIESDDMEHKTLKITDFGLAREWHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEALEAQVLREMPRDSFHSMQEGWKREIQGLFDELRAKEKELLSREEELTRAAREQRSQAEQLRRREHLLAQWELEVFERELTLLLQQVDRERPHVRRRRGTFKRSKLRARDGGERISMPLDFKHRITVQASPGLDRRRNVFEVGPGDSPTFPRFRAIQLEPAEPGQAWGRQSPRRLEDSSNGERRACWAWGPSSPKPGEAQNGRRRSRMDEATWYLDSDDSSPLGSPSTPPALNGNPPRPSLEPEEPKRPVPAERGSSSGTPKLIQRALLRGTALLASLGLGRDLQPPGGPGRERGESPTTPPTPTPAPCPTEPPPSPLICFSLKTPDSPPTPAPLLLDLGIPVGQRSAKSPRREEEPRGGTVSPPPGTSRSAPGTPGTPRSPPLGLISRPRPSPLRSRIDPWSFVSAGPRPSPLPSPQPAPRRAPWTLFPDSDPFWDSPPANPFQGGPQDCRAQTKDMGAQAPWVPEAGP	Literature-reported	"Discovery, synthesis, and characterization of an orally bioavailable, brain penetrant inhibitor of mixed lineage kinase 3. J Med Chem. 2013 Oct 24;56(20):8032-48."	0	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.	2.7.11.25	Transferring phosphorus-containing groups	Protein tyrosine kinase; Variant SH3 domain	PF07714; PF14604	PF07714; Pkinase_Tyr; PF14604; SH3_9	.	.	mmu04010:MAPK signaling pathway; mmu04932:Non-alcoholic fatty liver disease (NAFLD)	R-HSA-5673000: RAF activation; R-HSA-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-9013148: CDC42 GTPase cycle; R-HSA-9013408: RHOG GTPase cycle; R-HSA-9013424: RHOV GTPase cycle; R-HSA-9649948: Signaling downstream of RAS mutants	.	Q16584
TT4LIAC	Serine/threonine-protein kinase NIK (MAP3K14)	Q99558	M3K14_HUMAN	Kinase	NIK; NF-kappa-beta-inducing kinase; Mitogen-activated protein kinase kinase kinase 14; HsNIK	MAP3K14	"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."	EC 2.7.11.25	4IDV; 4IDT; 4G3D; 4DN5	MAVMEMACPGAPGSAVGQQKELPKAKEKTPPLGKKQSSVYKLEAVEKSPVFCGKWEILNDVITKGTAKEGSEAGPAAISIIAQAECENSQEFSPTFSERIFIAGSKQYSQSESLDQIPNNVAHATEGKMARVCWKGKRRSKARKKRKKKSSKSLAHAGVALAKPLPRTPEQESCTIPVQEDESPLGAPYVRNTPQFTKPLKEPGLGQLCFKQLGEGLRPALPRSELHKLISPLQCLNHVWKLHHPQDGGPLPLPTHPFPYSRLPHPFPFHPLQPWKPHPLESFLGKLACVDSQKPLPDPHLSKLACVDSPKPLPGPHLEPSCLSRGAHEKFSVEEYLVHALQGSVSSGQAHSLTSLAKTWAARGSRSREPSPKTEDNEGVLLTEKLKPVDYEYREEVHWATHQLRLGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAEELMACAGLTSPRIVPLYGAVREGPWVNIFMELLEGGSLGQLVKEQGCLPEDRALYYLGQALEGLEYLHSRRILHGDVKADNVLLSSDGSHAALCDFGHAVCLQPDGLGKSLLTGDYIPGTETHMAPEVVLGRSCDAKVDVWSSCCMMLHMLNGCHPWTQFFRGPLCLKIASEPPPVREIPPSCAPLTAQAIQEGLRKEPIHRVSAAELGGKVNRALQQVGGLKSPWRGEYKEPRHPPPNQANYHQTLHAQPRELSPRAPGPRPAEETTGRAPKLQPPLPPEPPEPNKSPPLTLSKEESGMWEPLPLSSLEPAPARNPSSPERKATVPEQELQQLEIELFLNSLSQPFSLEEQEQILSCLSIDSLSLSDDSEKNPSKASQSSRDTLSSGVHSWSSQAEARSSSWNMVLARGRPTDTPSYFNGVKVQIQSLNGEHLHIREFHRVKVGDIATGISSQIPAAAFSLVTKDGQPVRYDMEVPDSGIDLQCTLAPDGSFAWSWRVKHGQLENRP	Literature-reported	"Inhibiting NF- B-inducing kinase (NIK): discovery, structure-based design, synthesis, structure-activity relationship, and co-crystal structures. Bioorg Med Chem Lett. 2013 Mar 1;23(5):1238-44."	0	EC:2.7	.	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.	2.7.11.25	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04010: MAPK signaling pathway; hsa04064: NF-kappa B signaling pathway; hsa04210: Apoptosis; hsa04380: Osteoclast differentiation; hsa04625: C-type lectin receptor signaling pathway; hsa04660: T cell receptor signaling pathway; hsa04668: TNF signaling pathway; hsa04672: Intestinal immune network for IgA production; hsa04936: Alcoholic liver disease; hsa05120: Epithelial cell signaling in Helicobacter pylori infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05208: Chemical carcinogenesis - reactive oxygen species	R-HSA-389357: CD28 dependent PI3K/Akt signaling; R-HSA-5607761: Dectin-1 mediated noncanonical NF-kB signaling; R-HSA-5668541: TNFR2 non-canonical NF-kB pathway; R-HSA-5676590: NIK-->noncanonical NF-kB signaling; R-HSA-5676594: TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway	.	Q99558
TTRHJA3	SPS1/STE20-related protein kinase YSK4 (YSK4)	Q56UN5	M3K19_HUMAN	Kinase	"Regulated in COPD, protein kinase; RCK; Mitogen-activated protein kinase kinase kinase 19"	MAP3K19	"Protein serine/threonine kinase activity, activation of protein kinase activity, signal transduction by protein phosphorylation, stress-activated protein kinase signaling cascade."	EC 2.7.11.1	.	MSSMPKPERHAESLLDICHDTNSSPTDLMTVTKNQNIILQSISRSEEFDQDGDCSHSTLVNEEEDPSGGRQDWQPRTEGVEITVTFPRDVSPPQEMSQEDLKEKNLINSSLQEWAQAHAVSHPNEIETVELRKKKLTMRPLVLQKEESSRELCNVNLGFLLPRSCLELNISKSVTREDAPHFLKEQQRKSEEFSTSHMKYSGRSIKFLLPPLSLLPTRSGVLTIPQNHKFPKEKERNIPSLTSFVPKLSVSVRQSDELSPSNEPPGALVKSLMDPTLRSSDGFIWSRNMCSFPKTNHHRQCLEKEENWKSKEIEECNKIEITHFEKGQSLVSFENLKEGNIPAVREEDIDCHGSKTRKPEEENSQYLSSRKNESSVAKNYEQDPEIVCTIPSKFQETQHSEITPSQDEEMRNNKAASKRVSLHKNEAMEPNNILEECTVLKSLSSVVFDDPIDKLPEGCSSMETNIKISIAERAKPEMSRMVPLIHITFPVDGSPKEPVIAKPSLQTRKGTIHNNHSVNIPVHQENDKHKMNSHRSKLDSKTKTSKKTPQNFVISTEGPIKPTMHKTSIKTQIFPALGLVDPRPWQLPRFQKKMPQIAKKQSTHRTQKPKKQSFPCICKNPGTQKSCVPLSVQPTEPRLNYLDLKYSDMFKEINSTANGPGIYEMFGTPVYCHVRETERDENTYYREICSAPSGRRITNKCRSSHSERKSNIRTRLSQKKTHMKCPKTSFGIKQEHKVLISKEKSSKAVHSNLHDIENGDGISEPDWQIKSSGNEFLSSKDEIHPMNLAQTPEQSMKQNEFPPVSDLSIVEEVSMEESTGDRDISNNQILTTSLRDLQELEELHHQIPFIPSEDSWAVPSEKNSNKYVQQEKQNTASLSKVNASRILTNDLEFDSVSDHSKTLTNFSFQAKQESASSQTYQYWVHYLDHDSLANKSITYQMFGKTLSGTNSISQEIMDSVNNEELTDELLGCLAAELLALDEKDNNSCQKMANETDPENLNLVLRWRGSTPKEMGRETTKVKIQRHSSGLRIYDREEKFLISNEKKIFSENSLKSEEPILWTKGEILGKGAYGTVYCGLTSQGQLIAVKQVALDTSNKLAAEKEYRKLQEEVDLLKALKHVNIVAYLGTCLQENTVSIFMEFVPGGSISSIINRFGPLPEMVFCKYTKQILQGVAYLHENCVVHRDIKGNNVMLMPTGIIKLIDFGCARRLAWAGLNGTHSDMLKSMHGTPYWMAPEVINESGYGRKSDIWSIGCTVFEMATGKPPLASMDRMAAMFYIGAHRGLMPPLPDHFSENAADFVRMCLTRDQHERPSALQLLKHSFLERSH	Patented-recorded	Cyclin-dependent kinase inhibitors for cancer therapy: a patent review (2009 - 2014).Expert Opin Ther Pat. 2015;25(9):953-70.	15.5	EC:2.7	.	protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	.	.	Q56UN5
TTIX0ZU	MEKK2 messenger RNA (MAP3K2 mRNA)	Q9Y2U5	M3K2_HUMAN	mRNA target	Mitogen-activated protein kinase kinase kinase 2 (mRNA); MEKK2 (mRNA); MEKK 2 (mRNA); MEK kinase 2 (mRNA); MAPKKK2 (mRNA)	MAP3K2	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.	EC 2.7.11.25	5HQ8; 5EX0; 2NPT; 2CU1	MDDQQALNSIMQDLAVLHKASRPALSLQETRKAKSSSPKKQNDVRVKFEHRGEKRILQFPRPVKLEDLRSKAKIAFGQSMDLHYTNNELVIPLTTQDDLDKAVELLDRSIHMKSLKILLVINGSTQATNLEPLPSLEDLDNTVFGAERKKRLSIIGPTSRDRSSPPPGYIPDELHQVARNGSFTSINSEGEFIPESMDQMLDPLSLSSPENSGSGSCPSLDSPLDGESYPKSRMPRAQSYPDNHQEFSDYDNPIFEKFGKGGTYPRRYHVSYHHQEYNDGRKTFPRARRTQGTSLRSPVSFSPTDHSLSTSSGSSIFTPEYDDSRIRRRGSDIDNPTLTVMDISPPSRSPRAPTNWRLGKLLGQGAFGRVYLCYDVDTGRELAVKQVQFDPDSPETSKEVNALECEIQLLKNLLHERIVQYYGCLRDPQEKTLSIFMEYMPGGSIKDQLKAYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSTGNVKLGDFGASKRLQTICLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVACTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPKLPPHVSDYTRDFLKRIFVEAKLRPSADELLRHMFVHYH	Literature-reported	"US patent application no. 6,287,860, Antisense inhibition of MEKK2 expression."	0	mRNA	mRNA target	.	.	.	PB1 domain; Protein kinase domain	PF00564; PF00069	PF00564; PB1; PF00069; Pkinase	.	.	hsa04010:MAPK signaling pathway; hsa04540:Gap junction; hsa04912:GnRH signaling pathway	.	.	Q9Y2U5
TTK1N5G	MAPK/ERK kinase kinase 2 (MAP3K2)	Q9Y2U5	M3K2_HUMAN	Kinase	Mitogen-activated protein kinase kinase kinase 2; MEKK2; MEKK 2; MEK kinase 2; MAPKKK2	MAP3K2	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.	EC 2.7.11.25	5HQ8; 5EX0; 2NPT; 2CU1	MDDQQALNSIMQDLAVLHKASRPALSLQETRKAKSSSPKKQNDVRVKFEHRGEKRILQFPRPVKLEDLRSKAKIAFGQSMDLHYTNNELVIPLTTQDDLDKAVELLDRSIHMKSLKILLVINGSTQATNLEPLPSLEDLDNTVFGAERKKRLSIIGPTSRDRSSPPPGYIPDELHQVARNGSFTSINSEGEFIPESMDQMLDPLSLSSPENSGSGSCPSLDSPLDGESYPKSRMPRAQSYPDNHQEFSDYDNPIFEKFGKGGTYPRRYHVSYHHQEYNDGRKTFPRARRTQGTSLRSPVSFSPTDHSLSTSSGSSIFTPEYDDSRIRRRGSDIDNPTLTVMDISPPSRSPRAPTNWRLGKLLGQGAFGRVYLCYDVDTGRELAVKQVQFDPDSPETSKEVNALECEIQLLKNLLHERIVQYYGCLRDPQEKTLSIFMEYMPGGSIKDQLKAYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSTGNVKLGDFGASKRLQTICLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVACTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPKLPPHVSDYTRDFLKRIFVEAKLRPSADELLRHMFVHYH	Clinical trial	Pharmacological inhibitors of MAPK pathways. Trends Pharmacol Sci. 2002 Jan;23(1):40-5.	21	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.	2.7.11.25	Transferring phosphorus-containing groups	PB1 domain; Protein kinase domain	PF00564; PF00069	PF00564; PB1; PF00069; Pkinase	.	.	hsa04010:MAPK signaling pathway; hsa04540:Gap junction; hsa04912:GnRH signaling pathway	.	.	Q9Y2U5
TTTUZ3O	MLK-related kinase (MLTK)	Q9NYL2	M3K20_HUMAN	.	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	MAP3K20	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.	EC 2.7.11.25	5X5O; 5HES	MSSLGASFVQIKFDDLQFFENCGGGSFGSVYRAKWISQDKEVAVKKLLKIEKEAEILSVLSHRNIIQFYGVILEPPNYGIVTEYASLGSLYDYINSNRSEEMDMDHIMTWATDVAKGMHYLHMEAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFHNHTTHMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERLTIPSSCPRSFAELLHQCWEADAKKRPSFKQIISILESMSNDTSLPDKCNSFLHNKAEWRCEIEATLERLKKLERDLSFKEQELKERERRLKMWEQKLTEQSNTPLLPSFEIGAWTEDDVYCWVQQLVRKGDSSAEMSVYASLFKENNITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEKLTHDYINLFHFPPLIKDSGGEPEENEEKIVNLELVFGFHLKPGTGPQDCKWKMYMEMDGDEIAITYIKDVTFNTNLPDAEILKMTKPPFVMEKWIVGIAKSQTVECTVTYESDVRTPKSTKHVHSIQWSRTKPQDEVKAVQLAIQTLFTNSDGNPGSRSDSSADCQWLDTLRMRQIASNTSLQRSQSNPILGSPFFSHFDGQDSYAAAVRRPQVPIKYQQITPVNQSRSSSPTQYGLTKNFSSLHLNSRDSGFSSGNTDTSSERGRYSDRSRNKYGRGSISLNSSPRGRYSGKSQHSTPSRGRYPGKFYRVSQSALNPHQSPDFKRSPRDLHQPNTIPGMPLHPETDSRASEEDSKVSEGGWTKVEYRKKPHRPSPAKTNKERARGDHRGWRNF	Literature-reported	Dihydropyrrolopyrazole transforming growth factor-beta type I receptor kinase domain inhibitors: a novel benzimidazole series with selectivity vers... J Med Chem. 2006 Mar 23;49(6):2138-42.	0	.	.	.	.	.	.	.	.	.	.	hsa04010: MAPK signaling pathway	.	.	Q9NYL2
TTSW9YL	Mixed lineage kinase 4 (MAP3K21)	Q5TCX8	M3K21_HUMAN	Protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily	Mitogen-activated protein kinase kinase kinase MLK4; MLK4beta	MAP3K21	"Negative regulator of TLR4 signaling. Does not activate JNK1/MAPK8 pathway, p38/MAPK14, nor ERK2/MAPK1 pathways."	EC 2.7.11.25	4UYA	MALRGAAGATDTPVSSAGGAPGGSASSSSTSSGGSASAGAGLWAALYDYEARGEDELSLRRGQLVEVLSQDAAVSGDEGWWAGQVQRRLGIFPANYVAPCRPAASPAPPPSRPSSPVHVAFERLELKELIGAGGFGQVYRATWQGQEVAVKAARQDPEQDAAAAAESVRREARLFAMLRHPNIIELRGVCLQQPHLCLVLEFARGGALNRALAAANAAPDPRAPGPRRARRIPPHVLVNWAVQIARGMLYLHEEAFVPILHRDLKSSNILLLEKIEHDDICNKTLKITDFGLAREWHRTTKMSTAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTLPIPSTCPEPFAKLMKECWQQDPHIRPSFALILEQLTAIEGAVMTEMPQESFHSMQDDWKLEIQQMFDELRTKEKELRSREEELTRAALQQKSQEELLKRREQQLAEREIDVLERELNILIFQLNQEKPKVKKRKGKFKRSRLKLKDGHRISLPSDFQHKITVQASPNLDKRRSLNSSSSSPPSSPTMMPRLRAIQLTSDESNKTWGRNTVFRQEEFEDVKRNFKKKGCTWGPNSIQMKDRTDCKERIRPLSDGNSPWSTILIKNQKTMPLASLFVDQPGSCEEPKLSPDGLEHRKPKQIKLPSQAYIDLPLGKDAQRENPAEAESWEEAASANAATVSIEMTPTNSLSRSPQRKKTESALYGCTVLLASVALGLDLRELHKAQAAEEPLPKEEKKKREGIFQRASKSRRSASPPTSLPSTCGEASSPPSLPLSSALGILSTPSFSTKCLLQMDSEDPLVDSAPVTCDSEMLTPDFCPTAPGSGREPALMPRLDTDCSVSRNLPSSFLQQTCGNVPYCASSKHRPSHHRRTMSDGNPTPTGATIISATGASALPLCPSPAPHSHLPREVSPKKHSTVHIVPQRRPASLRSRSDLPQAYPQTAVSQLAQTACVVGRPGPHPTQFLAAKERTKSHVPSLLDADVEGQSRDYTVPLCRMRSKTSRPSIYELEKEFLS	Literature-reported	Mitogen-activated protein kinase signaling pathway and invasion and metastasis of gastric cancer. World J Gastroenterol. 2015 Nov 7;21(41):11673-9.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q5TCX8
TTJZNIG	MEKK3 messenger RNA (MAP3K3 mRNA)	Q99759	M3K3_HUMAN	mRNA target	Mitogen-activated protein kinase kinase kinase 3 (mRNA); MEKK3 (mRNA); MEKK 3 (mRNA); MEK kinase 3 (mRNA); MAPKKK3 (mRNA)	MAP3K3	"Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators. Component of a protein kinase signal transduction cascade."	EC 2.7.11.25	4YL6; 4Y5O; 2PPH; 2O2V; 2JRH	MDEQEALNSIMNDLVALQMNRRHRMPGYETMKNKDTGHSNRQSDVRIKFEHNGERRIIAFSRPVKYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDLDKAIDILDRSSSMKSLRILLLSQDRNHNSSSPHSGVSRQVRIKASQSAGDINTIYQPPEPRSRHLSVSSQNPGRSSPPPGYVPERQQHIARQGSYTSINSEGEFIPETSEQCMLDPLSSAENSLSGSCQSLDRSADSPSFRKSRMSRAQSFPDNRQEYSDRETQLYDKGVKGGTYPRRYHVSVHHKDYSDGRRTFPRIRRHQGNLFTLVPSSRSLSTNGENMGLAVQYLDPRGRLRSADSENALSVQERNVPTKSPSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFLRRIFVEARQRPSAEELLTHHFAQLMY	Literature-reported	"US patent application no. 6,498,035, Antisense modulation of MEKK3 expression."	0	mRNA	mRNA target	.	.	.	PB1 domain; Protein kinase domain	PF00564; PF00069	PF00564; PB1; PF00069; Pkinase	.	.	hsa04010:MAPK signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa04912:GnRH signaling pathway; hsa05166:HTLV-I infection	R-HSA-446652:Interleukin-1 signaling	.	Q99759
TTE7RCU	MAPK/ERK kinase kinase 3 (MAP3K3)	Q99759	M3K3_HUMAN	Kinase	Mitogen-activated protein kinase kinase kinase 3; MEKK3; MEKK 3; MEK kinase 3; MAPKKK3	MAP3K3	"Mediates activation of the NF-kappa-B, AP1 and DDIT3 transcriptional regulators. Component of a protein kinase signal transduction cascade."	EC 2.7.11.25	4YL6; 4Y5O; 2PPH; 2O2V; 2JRH	MDEQEALNSIMNDLVALQMNRRHRMPGYETMKNKDTGHSNRQSDVRIKFEHNGERRIIAFSRPVKYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDLDKAIDILDRSSSMKSLRILLLSQDRNHNSSSPHSGVSRQVRIKASQSAGDINTIYQPPEPRSRHLSVSSQNPGRSSPPPGYVPERQQHIARQGSYTSINSEGEFIPETSEQCMLDPLSSAENSLSGSCQSLDRSADSPSFRKSRMSRAQSFPDNRQEYSDRETQLYDKGVKGGTYPRRYHVSVHHKDYSDGRRTFPRIRRHQGNLFTLVPSSRSLSTNGENMGLAVQYLDPRGRLRSADSENALSVQERNVPTKSPSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELASKQVQFDPDSPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTGMRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHGRDFLRRIFVEARQRPSAEELLTHHFAQLMY	Literature-reported	"Synthesis and structure-activity relationships of 1,2,3,4-tetrahydropyrido[2,3-b]pyrazines as potent and selective inhibitors of the anaplastic lymphoma kinase. Bioorg Med Chem. 2010 Jun 15;18(12):4351-62."	0	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.	2.7.11.25	Transferring phosphorus-containing groups	PB1 domain; Protein kinase domain	PF00564; PF00069	PF00564; PB1; PF00069; Pkinase	.	.	hsa04010: MAPK signaling pathway; hsa04722: Neurotrophin signaling pathway; hsa04912: GnRH signaling pathway; hsa05166: Human T-cell leukemia virus 1 infection; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer	R-HSA-446652:Interleukin-1 signaling	.	Q99759
TT1RSX7	MAPK/ERK kinase kinase 4 (MAP3K4)	Q9Y6R4	M3K4_HUMAN	Kinase	Mitogen-activated protein kinase kinase kinase 4; MTK1; MEKK4; MEKK 4; MEK kinase 4; MAPKKK4; MAP three kinase 1; KIAA0213	MAP3K4	"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."	EC 2.7.11.25	.	MREAAAALVPPPAFAVTPAAAMEEPPPPPPPPPPPPEPETESEPECCLAARQEGTLGDSACKSPESDLEDFSDETNTENLYGTSPPSTPRQMKRMSTKHQRNNVGRPASRSNLKEKMNAPNQPPHKDTGKTVENVEEYSYKQEKKIRAALRTTERDRKKNVQCSFMLDSVGGSLPKKSIPDVDLNKPYLSLGCSNAKLPVSVPMPIARPARQTSRTDCPADRLKFFETLRLLLKLTSVSKKKDREQRGQENTSGFWLNRSNELIWLELQAWHAGRTINDQDFFLYTARQAIPDIINEILTFKVDYGSFAFVRDRAGFNGTSVEGQCKATPGTKIVGYSTHHEHLQRQRVSFEQVKRIMELLEYIEALYPSLQALQKDYEKYAAKDFQDRVQALCLWLNITKDLNQKLRIMGTVLGIKNLSDIGWPVFEIPSPRPSKGNEPEYEGDDTEGELKELESSTDESEEEQISDPRVPEIRQPIDNSFDIQSRDCISKKLERLESEDDSLGWGAPDWSTEAGFSRHCLTSIYRPFVDKALKQMGLRKLILRLHKLMDGSLQRARIALVKNDRPVEFSEFPDPMWGSDYVQLSRTPPSSEEKCSAVSWEELKAMDLPSFEPAFLVLCRVLLNVIHECLKLRLEQRPAGEPSLLSIKQLVRECKEVLKGGLLMKQYYQFMLQEVLEDLEKPDCNIDAFEEDLHKMLMVYFDYMRSWIQMLQQLPQASHSLKNLLEEEWNFTKEITHYIRGGEAQAGKLFCDIAGMLLKSTGSFLEFGLQESCAEFWTSADDSSASDEIRRSVIEISRALKELFHEARERASKALGFAKMLRKDLEIAAEFRLSAPVRDLLDVLKSKQYVKVQIPGLENLQMFVPDTLAEEKSIILQLLNAAAGKDCSKDSDDVLIDAYLLLTKHGDRARDSEDSWGTWEAQPVKVVPQVETVDTLRSMQVDNLLLVVMQSAHLTIQRKAFQQSIEGLMTLCQEQTSSQPVIAKALQQLKNDALELCNRISNAIDRVDHMFTSEFDAEVDESESVTLQQYYREAMIQGYNFGFEYHKEVVRLMSGEFRQKIGDKYISFARKWMNYVLTKCESGRGTRPRWATQGFDFLQAIEPAFISALPEDDFLSLQALMNECIGHVIGKPHSPVTGLYLAIHRNSPRPMKVPRCHSDPPNPHLIIPTPEGFSTRSMPSDARSHGSPAAAAAAAAAAVAASRPSPSGGDSVLPKSISSAHDTRGSSVPENDRLASIAAELQFRSLSRHSSPTEERDEPAYPRGDSSGSTRRSWELRTLISQSKDTASKLGPIEAIQKSVRLFEEKRYREMRRKNIIGQVCDTPKSYDNVMHVGLRKVTFKWQRGNKIGEGQYGKVYTCISVDTGELMAMKEIRFQPNDHKTIKETADELKIFEGIKHPNLVRYFGVELHREEMYIFMEYCDEGTLEEVSRLGLQEHVIRLYSKQITIAINVLHEHGIVHRDIKGANIFLTSSGLIKLGDFGCSVKLKNNAQTMPGEVNSTLGTAAYMAPEVITRAKGEGHGRAADIWSLGCVVIEMVTGKRPWHEYEHNFQIMYKVGMGHKPPIPERLSPEGKDFLSHCLESDPKMRWTASQLLDHSFVKVCTDEE	Literature-reported	Specific amino acid deficiency alters the expression of genes in human melanoma and other tumor cell lines. J Nutr. 2001 Nov;131(11 Suppl):3047S-50S.	.	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.	2.7.11.25	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04010: MAPK signaling pathway; hsa04912: GnRH signaling pathway	.	.	Q9Y6R4
TTOQCD8	Apoptosis signal-regulating kinase 1 (MAP3K5)	Q99683	M3K5_HUMAN	Kinase	Mitogen-activated protein kinase kinase kinase 5; MEKK5; MEKK 5; MEK kinase 5; MAPKKK5; MAPK/ERK kinase kinase 5; ASK1; ASK-1	MAP3K5	"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."	EC 2.7.11.25	6EJL; 6E2O; 6E2N; 6E2M; 5VIO	MSTEADEGITFSVPPFAPSGFCTIPEGGICRRGGAAAVGEGEEHQLPPPPPGSFWNVESAAAPGIGCPAATSSSSATRGRGSSVGGGSRRTTVAYVINEASQGQLVVAESEALQSLREACETVGATLETLHFGKLDFGETTVLDRFYNADIAVVEMSDAFRQPSLFYHLGVRESFSMANNIILYCDTNSDSLQSLKEIICQKNTMCTGNYTFVPYMITPHNKVYCCDSSFMKGLTELMQPNFELLLGPICLPLVDRFIQLLKVAQASSSQYFRESILNDIRKARNLYTGKELAAELARIRQRVDNIEVLTADIVINLLLSYRDIQDYDSIVKLVETLEKLPTFDLASHHHVKFHYAFALNRRNLPGDRAKALDIMIPMVQSEGQVASDMYCLVGRIYKDMFLDSNFTDTESRDHGASWFKKAFESEPTLQSGINYAVLLLAAGHQFESSFELRKVGVKLSSLLGKKGNLEKLQSYWEVGFFLGASVLANDHMRVIQASEKLFKLKTPAWYLKSIVETILIYKHFVKLTTEQPVAKQELVDFWMDFLVEATKTDVTVVRFPVLILEPTKIYQPSYLSINNEVEEKTISIWHVLPDDKKGIHEWNFSASSVRGVSISKFEERCCFLYVLHNSDDFQIYFCTELHCKKFFEMVNTITEEKGRSTEEGDCESDLLEYDYEYDENGDRVVLGKGTYGIVYAGRDLSNQVRIAIKEIPERDSRYSQPLHEEIALHKHLKHKNIVQYLGSFSENGFIKIFMEQVPGGSLSALLRSKWGPLKDNEQTIGFYTKQILEGLKYLHDNQIVHRDIKGDNVLINTYSGVLKISDFGTSKRLAGINPCTETFTGTLQYMAPEIIDKGPRGYGKAADIWSLGCTIIEMATGKPPFYELGEPQAAMFKVGMFKVHPEIPESMSAEAKAFILKCFEPDPDKRACANDLLVDEFLKVSSKKKKTQPKLSALSAGSNEYLRSISLPVPVLVEDTSSSSEYGSVSPDTELKVDPFSFKTRAKSCGERDVKGIRTLFLGIPDENFEDHSAPPSPEEKDSGFFMLRKDSERRATLHRILTEDQDKIVRNLMESLAQGAEEPKLKWEHITTLIASLREFVRSTDRKIIATTLSKLKLELDFDSHGISQVQVVLFGFQDAVNKVLRNHNIKPHWMFALDSIIRKAVQTAITILVPELRPHFSLASESDTADQEDLDVEDDHEEQPSNQTVRRPQAVIEDAVATSGVSTLSSTVSHDSQSAHRSLNVQLGRMKIETNRLLEELVRKEKELQALLHRAIEEKDQEIKHLKLKSQPIEIPELPVFHLNSSGTNTEDSELTDWLRVNGADEDTISRFLAEDYTLLDVLYYVTRDDLKCLRLRGGMLCTLWKAIIDFRNKQT	Clinical trial	"Design of a phase 2 clinical trial of an ASK1 inhibitor, GS-4997, in patients with diabetic kidney disease. Nephron. 2015;129(1):29-33."	21	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.	2.7.11.25	Transferring phosphorus-containing groups	Domain of unknown function (DUF4071); Protein kinase domain	PF13281; PF00069	PF13281; DUF4071; PF00069; Pkinase	.	.	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)	R-HSA-2559580:Oxidative Stress Induced Senescence	.	Q99683
TT64GC2	Apoptosis signal-regulating kinase 2 (MAP3K6)	O95382	M3K6_HUMAN	.	MAP3K6	MAP3K6	"Component of a protein kinase signal transduction cascade. Activates the JNK, but not ERK or p38 kinase pathways."	EC 2.7.11.25	.	MAGPCPRSGAERAGSCWQDPLAVALSRGRQLAAPPGRGCARSRPLSVVYVLTREPQPGLEPREGTEAEPLPLRCLREACAQVPRPRPPPQLRSLPFGTLELGDTAALDAFYNADVVVLEVSSSLVQPSLFYHLGVRESFSMTNNVLLCSQADLPDLQALREDVFQKNSDCVGSYTLIPYVVTATGRVLCGDAGLLRGLADGLVQAGVGTEALLTPLVGRLARLLEATPTDSCGYFRETIRRDIRQARERFSGPQLRQELARLQRRLDSVELLSPDIIMNLLLSYRDVQDYSAIIELVETLQALPTCDVAEQHNVCFHYTFALNRRNRPGDRAKALSVLLPLVQLEGSVAPDLYCMCGRIYKDMFFSSGFQDAGHREQAYHWYRKAFDVEPSLHSGINAAVLLIAAGQHFEDSKELRLIGMKLGCLLARKGCVEKMQYYWDVGFYLGAQILANDPTQVVLAAEQLYKLNAPIWYLVSVMETFLLYQHFRPTPEPPGGPPRRAHFWLHFLLQSCQPFKTACAQGDQCLVLVLEMNKVLLPAKLEVRGTDPVSTVTLSLLEPETQDIPSSWTFPVASICGVSASKRDERCCFLYALPPAQDVQLCFPSVGHCQWFCGLIQAWVTNPDSTAPAEEAEGAGEMLEFDYEYTETGERLVLGKGTYGVVYAGRDRHTRVRIAIKEIPERDSRFSQPLHEEIALHRRLRHKNIVRYLGSASQGGYLKIFMEEVPGGSLSSLLRSVWGPLKDNESTISFYTRQILQGLGYLHDNHIVHRDIKGDNVLINTFSGLLKISDFGTSKRLAGITPCTETFTGTLQYMAPEIIDQGPRGYGKAADIWSLGCTVIEMATGRPPFHELGSPQAAMFQVGMYKVHPPMPSSLSAEAQAFLLRTFEPDPRLRASAQTLLGDPFLQPGKRSRSPSSPRHAPRPSDAPSASPTPSANSTTQSQTFPCPQAPSQHPPSPPKRCLSYGGTSQLRVPEEPAAEEPASPEESSGLSLLHQESKRRAMLAAVLEQELPALAENLHQEQKQEQGARLGRNHVEELLRCLGAHIHTPNRRQLAQELRALQGRLRAQGLGPALLHRPLFAFPDAVKQILRKRQIRPHWMFVLDSLLSRAVRAALGVLGPEVEKEAVSPRSEELSNEGDSQQSPGQQSPLPVEPEQGPAPLMVQLSLLRAETDRLREILAGKEREYQALVQRALQRLNEEARTYVLAPEPPTALSTDQGLVQWLQELNVDSGTIQMLLNHSFTLHTLLTYATRDDLIYTRIRGGMVCRIWRAILAQRAGSTPVTSGP	Literature-reported	"Design and biological evaluation of imidazo[1,2-a]pyridines as novel and potent ASK1 inhibitors. Bioorg Med Chem Lett. 2012 Dec 15;22(24):7326-9."	0	.	.	.	.	.	.	.	.	.	.	hsa04010: MAPK signaling pathway	.	.	O95382
TTJQT60	TGF-beta-activated kinase 1 (MAP3K7)	O43318	M3K7_HUMAN	Kinase	Transforming growth factor-beta-activated kinase 1; TAK1; Mitogen-activated protein kinase kinase kinase 7	MAP3K7	"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."	EC 2.7.11.25	5V5N; 5JK3; 5JH6; 5JGD; 5JGB	MSTASAASSSSSSSAGEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFMDIASTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSESGRLSLGASRGSSVESLPPTSEGKRMSADMSEIEARIAATTAYSKPKRGHRKTASFGNILDVPEIVISGNGQPRRRSIQDLTVTGTEPGQVSSRSSSPSVRMITTSGPTSEKPTRSHPWTPDDSTDTNGSDNSIPMAYLTLDHQLQPLAPCPNSKESMAVFEQHCKMAQEYMKVQTEIALLLQRKQELVAELDQDEKDQQNTSRLVQEHKKLLDENKSLSTYYQQCKKQLEVIRSQQQKRQGTS	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2082).	0	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.	2.7.11.25 	Transferring phosphorus-containing groups	Protein tyrosine kinase	PF07714	PF07714; Pkinase_Tyr	.	.	hsa04010: MAPK signaling pathway; hsa04064: NF-kappa B signaling pathway; hsa04140: Autophagy - animal; hsa04152: AMPK signaling pathway; hsa04310: Wnt signaling pathway; hsa04380: Osteoclast differentiation; hsa04520: Adherens junction; hsa04613: Neutrophil extracellular trap formation; hsa04620: Toll-like receptor signaling pathway; hsa04621: NOD-like receptor signaling pathway; hsa04622: RIG-I-like receptor signaling pathway; hsa04657: IL-17 signaling pathway; hsa04660: T cell receptor signaling pathway; hsa04668: TNF signaling pathway; hsa04936: Alcoholic liver disease; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05135: Yersinia infection; hsa05140: Leishmaniasis; hsa05145: Toxoplasmosis; hsa05161: Hepatitis B; hsa05162: Measles; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05171: Coronavirus disease - COVID-19; hsa05417: Lipid and atherosclerosis; hsa05418: Fluid shear stress and atherosclerosis	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	.	O43318
TTGECUM	Cot oncogene messenger RNA (MAP3K8 mRNA)	P41279	M3K8_HUMAN	mRNA target	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)	MAP3K8	"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."	EC 2.7.11.25	5IU2; 4Y85; 4Y83	MEYMSTGSDNKEEIDLLIKHLNVSDVIDIMENLYASEEPAVYEPSLMTMCQDSNQNDERSKSLLLSGQEVPWLSSVRYGTVEDLLAFANHISNTAKHFYGQRPQESGILLNMVITPQNGRYQIDSDVLLIPWKLTYRNIGSDFIPRGAFGKVYLAQDIKTKKRMACKLIPVDQFKPSDVEIQACFRHENIAELYGAVLWGETVHLFMEAGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKKVIHHDIKPSNIVFMSTKAVLVDFGLSVQMTEDVYFPKDLRGTEIYMSPEVILCRGHSTKADIYSLGATLIHMQTGTPPWVKRYPRSAYPSYLYIIHKQAPPLEDIADDCSPGMRELIEASLERNPNHRPRAADLLKHEALNPPREDQPRCQSLDSALLERKRLLSRKELELPENIADSSCTGSTEESEMLKRQRSLYIDLGALAGYFNLVRGPPTLEYG	Literature-reported	"Inhibition of Tpl2 kinase and TNF-alpha production with 1,7-naphthyridine-3-carbonitriles: synthesis and structure-activity relationships. Bioorg Med Chem Lett. 2005 Dec 1;15(23):5288-92."	0	mRNA	mRNA target	.	.	.	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04010:MAPK signaling pathway; hsa04620:Toll-like receptor signaling pathway; hsa04660:T cell receptor signaling pathway; hsa04668:TNF signaling pathway	R-HSA-389357:CD28 dependent PI3K/Akt signaling; R-HSA-5684264:MAP3K8 (TPL2)-dependent MAPK1/3 activation	.	P41279
TTNM0P7	Serine/threonine-protein kinase cot (COT)	P41279	M3K8_HUMAN	.	Tumor progression locus 2; TPL-2; Proto-oncogene c-Cot; Mitogen-activated protein kinase kinase kinase 8; ESTF; Cancer Osaka thyroid oncogene; COT	MAP3K8	"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."	EC 2.7.11.25	5IU2; 4Y85; 4Y83	MEYMSTGSDNKEEIDLLIKHLNVSDVIDIMENLYASEEPAVYEPSLMTMCQDSNQNDERSKSLLLSGQEVPWLSSVRYGTVEDLLAFANHISNTAKHFYGQRPQESGILLNMVITPQNGRYQIDSDVLLIPWKLTYRNIGSDFIPRGAFGKVYLAQDIKTKKRMACKLIPVDQFKPSDVEIQACFRHENIAELYGAVLWGETVHLFMEAGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKKVIHHDIKPSNIVFMSTKAVLVDFGLSVQMTEDVYFPKDLRGTEIYMSPEVILCRGHSTKADIYSLGATLIHMQTGTPPWVKRYPRSAYPSYLYIIHKQAPPLEDIADDCSPGMRELIEASLERNPNHRPRAADLLKHEALNPPREDQPRCQSLDSALLERKRLLSRKELELPENIADSSCTGSTEESEMLKRQRSLYIDLGALAGYFNLVRGPPTLEYG	Literature-reported	Cot/Tpl-2 protein kinase as a target for the treatment of inflammatory disease. Curr Top Med Chem. 2009;9(7):611-22.	.	.	.	.	.	.	.	.	.	.	.	hsa04010: MAPK signaling pathway; hsa04620: Toll-like receptor signaling pathway; hsa04660: T cell receptor signaling pathway; hsa04668: TNF signaling pathway	R-HSA-389357: CD28 dependent PI3K/Akt signaling; R-HSA-5684264: MAP3K8 (TPL2)-dependent MAPK1/3 activation	.	P41279
TTUNSIX	Mixed lineage kinase 1 (MAP3K9)	P80192	M3K9_HUMAN	Kinase	PRKE1; Mitogen-activated protein kinase kinase kinase 9; MLK1	MAP3K9	"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."	EC 2.7.11.25	4UY9; 3DTC	MEPSRALLGCLASAAAAAPPGEDGAGAGAEEEEEEEEEAAAAVGPGELGCDAPLPYWTAVFEYEAAGEDELTLRLGDVVEVLSKDSQVSGDEGWWTGQLNQRVGIFPSNYVTPRSAFSSRCQPGGEDPSCYPPIQLLEIDFAELTLEEIIGIGGFGKVYRAFWIGDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHDEAIVPIIHRDLKSSNILILQKVENGDLSNKILKITDFGLAREWHRTTKMSAAGTYAWMAPEVIRASMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLALPIPSTCPEPFAKLMEDCWNPDPHSRPSFTNILDQLTTIEESGFFEMPKDSFHCLQDNWKHEIQEMFDQLRAKEKELRTWEEELTRAALQQKNQEELLRRREQELAEREIDILERELNIIIHQLCQEKPRVKKRKGKFRKSRLKLKDGNRISLPSDFQHKFTVQASPTMDKRKSLINSRSSPPASPTIIPRLRAIQLTPGESSKTWGRSSVVPKEEGEEEEKRAPKKKGRTWGPGTLGQKELASGDEGSPQRREKANGLSTPSESPHFHLGLKSLVDGYKQWSSSAPNLVKGPRSSPALPGFTSLMEMEDEDSEGPGSGESRLQHSPSQSYLCIPFPRGEDGDGPSSDGIHEEPTPVNSATSTPQLTPTNSLKRGGAHHRRCEVALLGCGAVLAATGLGFDLLEAGKCQLLPLEEPEPPAREEKKRREGLFQRSSRPRRSTSPPSRKLFKKEEPMLLLGDPSASLTLLSLSSISECNSTRSLLRSDSDEIVVYEMPVSPVEAPPLSPCTHNPLVNVRVERFKRDPNQSLTPTHVTLTTPSQPSSHRRTPSDGALKPETLLASRSPSSNGLSPSPGAGMLKTPSPSRDPGEFPRLPDPNVVFPPTPRRWNTQQDSTLERPKTLEFLPRPRPSANRQRLDPWWFVSPSHARSTSPANSSSTETPSNLDSCFASSSSTVEERPGLPALLPFQAGPLPPTERTLLDLDAEGQSQDSTVPLCRAELNTHRPAPYEIQQEFWS	Clinical trial	Pharmacological inhibitors of MAPK pathways. Trends Pharmacol Sci. 2002 Jan;23(1):40-5.	24	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.	2.7.11.25	Transferring phosphorus-containing groups	Protein kinase domain; Variant SH3 domain	PF00069; PF14604	PF00069; Pkinase; PF14604; SH3_9	.	.	.	.	.	P80192
TT0VFPN	Microtubule-associated protein 4 (MAP4)	P27816	MAP4_HUMAN	.	Microtubuleassociated protein 4; MAP4	MAP4	Non-neuronal microtubule-associated protein. Promotes microtubule assembly.	.	.	MADLSLADALTEPSPDIEGEIKRDFIATLEAEAFDDVVGETVGKTDYIPLLDVDEKTGNSESKKKPCSETSQIEDTPSSKPTLLANGGHGVEGSDTTGSPTEFLEEKMAYQEYPNSQNWPEDTNFCFQPEQVVDPIQTDPFKMYHDDDLADLVFPSSATADTSIFAGQNDPLKDSYGMSPCNTAVVPQGWSVEALNSPHSESFVSPEAVAEPPQPTAVPLELAKEIEMASEERPPAQALEIMMGLKTTDMAPSKETEMALAKDMALATKTEVALAKDMESPTKLDVTLAKDMQPSMESDMALVKDMELPTEKEVALVKDVRWPTETDVSSAKNVVLPTETEVAPAKDVTLLKETERASPIKMDLAPSKDMGPPKENKKETERASPIKMDLAPSKDMGPPKENKIVPAKDLVLLSEIEVAQANDIISSTEISSAEKVALSSETEVALARDMTLPPETNVILTKDKALPLEAEVAPVKDMAQLPETEIAPAKDVAPSTVKEVGLLKDMSPLSETEMALGKDVTPPPETEVVLIKNVCLPPEMEVALTEDQVPALKTEAPLAKDGVLTLANNVTPAKDVPPLSETEATPVPIKDMEIAQTQKGISEDSHLESLQDVGQSAAPTFMISPETVTGTGKKCSLPAEEDSVLEKLGERKPCNSQPSELSSETSGIARPEEGRPVVSGTGNDITTPPNKELPPSPEKKTKPLATTQPAKTSTSKAKTQPTSLPKQPAPTTIGGLNKKPMSLASGLVPAAPPKRPAVASARPSILPSKDVKPKPIADAKAPEKRASPSKPASAPASRSGSKSTQTVAKTTTAAAVASTGPSSRSPSTLLPKKPTAIKTEGKPAEVKKMTAKSVPADLSRPKSTSTSSMKKTTTLSGTAPAAGVVPSRVKATPMPSRPSTTPFIDKKPTSAKPSSTTPRLSRLATNTSAPDLKNVRSKVGSTENIKHQPGGGRAKVEKKTEAAATTRKPESNAVTKTAGPIASAQKQPAGKVQIVSKKVSYSHIQSKCGSKDNIKHVPGGGNVQIQNKKVDISKVSSKCGSKANIKHKPGGGDVKIESQKLNFKEKAQAKVGSLDNVGHLPAGGAVKTEGGGSEAPLCPGPPAGEEPAISEAAPEAGAPTSASGLNGHPTLSGGGDQREAQTLDSQIQETSI	Literature-reported	Microtubule-associated proteins as targets in cancer chemotherapy. Clin Cancer Res. 2007 May 15;13(10):2849-54.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P27816
TTSHWUP	MEK kinase kinase 1 (MAP4K1)	Q92918	M4K1_HUMAN	Kinase	Mitogen-activated protein kinase kinase kinase kinase 1; MEKKK 1; MAPK/ERK kinase kinase kinase 1; Hematopoietic progenitor kinase; HPK1	MAP4K1	"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."	EC 2.7.11.1	6NG0; 6NFZ; 6NFY; 6CQF; 6CQE	MDVVDPDIFNRDPRDHYDLLQRLGGGTYGEVFKARDKVSGDLVALKMVKMEPDDDVSTLQKEILILKTCRHANIVAYHGSYLWLQKLWICMEFCGAGSLQDIYQVTGSLSELQISYVCREVLQGLAYLHSQKKIHRDIKGANILINDAGEVRLADFGISAQIGATLARRLSFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIELAELQPPLFDVHPLRVLFLMTKSGYQPPRLKEKGKWSAAFHNFIKVTLTKSPKKRPSATKMLSHQLVSQPGLNRGLILDLLDKLKNPGKGPSIGDIEDEEPELPPAIPRRIRSTHRSSSLGIPDADCCRRHMEFRKLRGMETRPPANTARLQPPRDLRSSSPRKQLSESSDDDYDDVDIPTPAEDTPPPLPPKPKFRSPSDEGPGSMGDDGQLSPGVLVRCASGPPPNSPRPGPPPSTSSPHLTAHSEPSLWNPPSRELDKPPLLPPKKEKMKRKGCALLVKLFNGCPLRIHSTAAWTHPSTKDQHLLLGAEEGIFILNRNDQEATLEMLFPSRTTWVYSINNVLMSLSGKTPHLYSHSILGLLERKETRAGNPIAHISPHRLLARKNMVSTKIQDTKGCRACCVAEGASSGGPFLCGALETSVVLLQWYQPMNKFLLVRQVLFPLPTPLSVFALLTGPGSELPAVCIGVSPGRPGKSVLFHTVRFGALSCWLGEMSTEHRGPVQVTQVEEDMVMVLMDGSVKLVTPEGSPVRGLRTPEIPMTEAVEAVAMVGGQLQAFWKHGVQVWALGSDQLLQELRDPTLTFRLLGSPRLECSGTISPHCNLLLPGSSNSPASASRVAGITGL	Clinical trial	MAP4K Family Kinases in Immunity and Inflammation. Adv Immunol. 2016;129:277-314.	.	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	CNH domain; Protein kinase domain	PF00780; PF00069	PF00780; CNH; PF00069; Pkinase	.	.	hsa04010: MAPK signaling pathway	.	.	Q92918
TTQFRP0	MEK kinase kinase 2 (MAP4K2)	Q12851	M4K2_HUMAN	Kinase	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	MAP4K2	"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."	EC 2.7.11.1	.	MALLRDVSLQDPRDRFELLQRVGAGTYGDVYKARDTVTSELAAVKIVKLDPGDDISSLQQEITILRECRHPNVVAYIGSYLRNDRLWICMEFCGGGSLQEIYHATGPLEERQIAYVCREALKGLHHLHSQGKIHRDIKGANLLLTLQGDVKLADFGVSGELTASVAKRRSFIGTPYWMAPEVAAVERKGGYNELCDVWALGITAIELGELQPPLFHLHPMRALMLMSKSSFQPPKLRDKTRWTQNFHHFLKLALTKNPKKRPTAEKLLQHPFTTQQLPRALLTQLLDKASDPHLGTPSPEDCELETYDMFPDTIHSRGQHGPAERTPSEIQFHQVKFGAPRRKETDPLNEPWEEEWTLLGKEELSGSLLQSVQEALEERSLTIRSASEFQELDSPDDTMGTIKRAPFLGPLPTDPPAEEPLSSPPGTLPPPPSGPNSSPLLPTAWATMKQREDPERSSCHGLPPTPKVHMGACFSKVFNGCPLRIHAAVTWIHPVTRDQFLVVGAEEGIYTLNLHELHEDTLEKLISHRCSWLYCVNNVLLSLSGKSTHIWAHDLPGLFEQRRLQQQVPLSIPTNRLTQRIIPRRFALSTKIPDTKGCLQCRVVRNPYTGATFLLAALPTSLLLLQWYEPLQKFLLLKNFSSPLPSPAGMLEPLVLDGKELPQVCVGAEGPEGPGCRVLFHVLPLEAGLTPDILIPPEGIPGSAQQVIQVDRDTILVSFERCVRIVNMQGEPTATLAPELTFDFPIETVVCLQDSVLAFWSHGMQGRSLDTNEVTQEITDETRIFRVLGAHRDIILESIPTDNPEAHSNLYILTGHQSTY	Patented-recorded	Cyclin-dependent kinase inhibitors for cancer therapy: a patent review (2009 - 2014).Expert Opin Ther Pat. 2015;25(9):953-70.	15.5	EC:2.7	.	protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	CNH domain; Protein kinase domain	PF00780; PF00069	PF00780; CNH; PF00069; Pkinase	.	.	hsa04010: MAPK signaling pathway	.	.	Q12851
TTI0AHJ	MEK kinase kinase 3 (MAP4K3)	Q8IVH8	M4K3_HUMAN	Kinase	RAB8IPL1; Mitogen-activated protein kinase kinase kinase kinase 3; MEKKK 3; MAPK/ERK kinase kinase kinase 3; Germinal center kinase-related protein kinase; GLK	MAP4K3	Appears to act upstream of the JUN N-terminal pathway. May play a role in the response to environmental stress.	EC 2.7.11.1	5J5T	MNPGFDLSRRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHPNIVAYFGSYLRRDKLWICMEFCGGGSLQDIYHVTGPLSELQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKSFIGTPYWMAPEVAAVERKGGYNQLCDLWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPKLKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFVTQHLTRSLAIELLDKVNNPDHSTYHDFDDDDPEPLVAVPHRIHSTSRNVREEKTRSEITFGQVKFDPPLRKETEPHHELPDSDGFLDSSEEIYYTARSNLDLQLEYGQGHQGGYFLGANKSLLKSVEEELHQRGHVAHLEDDEGDDDESKHSTLKAKIPPPLPPKPKSIFIPQEMHSTEDENQGTIKRCPMSGSPAKPSQVPPRPPPPRLPPHKPVALGNGMSSFQLNGERDGSLCQQQNEHRGTNLSRKEKKDVPKPISNGLPPTPKVHMGACFSKVFNGCPLKIHCASSWINPDTRDQYLIFGAEEGIYTLNLNELHETSMEQLFPRRCTWLYVMNNCLLSISGKASQLYSHNLPGLFDYARQMQKLPVAIPAHKLPDRILPRKFSVSAKIPETKWCQKCCVVRNPYTGHKYLCGALQTSIVLLEWVEPMQKFMLIKHIDFPIPCPLRMFEMLVVPEQEYPLVCVGVSRGRDFNQVVRFETVNPNSTSSWFTESDTPQTNVTHVTQLERDTILVCLDCCIKIVNLQGRLKSSRKLSSELTFDFQIESIVCLQDSVLAFWKHGMQGRSFRSNEVTQEISDSTRIFRLLGSDRVVVLESRPTDNPTANSNLYILAGHENSY	Literature-reported	"The design, synthesis, and biological evaluation of potent receptor tyrosine kinase inhibitors. Bioorg Med Chem Lett. 2012 Aug 1;22(15):4979-85."	0	EC:2.7	.	protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	CNH domain; Protein kinase domain	PF00780; PF00069	PF00780; CNH; PF00069; Pkinase	.	.	hsa04010: MAPK signaling pathway	.	.	Q8IVH8
TT6NI13	MEK kinase kinase 4 (MAP4K4)	O95819	M4K4_HUMAN	Kinase	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	MAP4K4	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.	EC 2.7.11.1	5W5Q; 5J95; 5DI1; 4ZP5; 4ZK5	MANDSPAKSLVDIDLSSLRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPGHDDQLWLVMEFCGAGSITDLVKNTKGNTLKEDWIAYISREILRGLAHLHIHHVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDLWSCGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKFFSFIEGCLVKNYMQRPSTEQLLKHPFIRDQPNERQVRIQLKDHIDRTRKKRGEKDETEYEYSGSEEEEEEVPEQEGEPSSIVNVPGESTLRRDFLRLQQENKERSEALRRQQLLQEQQLREQEEYKRQLLAERQKRIEQQKEQRRRLEEQQRREREARRQQEREQRRREQEEKRRLEELERRRKEEEERRRAEEEKRRVEREQEYIRRQLEEEQRHLEVLQQQLLQEQAMLLECRWREMEEHRQAERLQRQLQQEQAYLLSLQHDHRRPHPQHSQQPPPPQQERSKPSFHAPEPKAHYEPADRAREVEDRFRKTNHSSPEAQSKQTGRVLEPPVPSRSESFSNGNSESVHPALQRPAEPQVPVRTTSRSPVLSRRDSPLQGSGQQNSQAGQRNSTSIEPRLLWERVEKLVPRPGSGSSSGSSNSGSQPGSHPGSQSGSGERFRVRSSSKSEGSPSQRLENAVKKPEDKKEVFRPLKPADLTALAKELRAVEDVRPPHKVTDYSSSSEESGTTDEEDDDVEQEGADESTSGPEDTRAASSLNLSNGETESVKTMIVHDDVESEPAMTPSKEGTLIVRQTQSASSTLQKHKSSSSFTPFIDPRLLQISPSSGTTVTSVVGFSCDGMRPEAIRQDPTRKGSVVNVNPTNTRPQSDTPEIRKYKKRFNSEILCAALWGVNLLVGTESGLMLLDRSGQGKVYPLINRRRFQQMDVLEGLNVLVTISGKKDKLRVYYLSWLRNKILHNDPEVEKKQGWTTVGDLEGCVHYKVVKYERIKFLVIALKSSVEVYAWAPKPYHKFMAFKSFGELVHKPLLVDLTVEEGQRLKVIYGSCAGFHAVDVDSGSVYDIYLPTHIQCSIKPHAIIILPNTDGMELLVCYEDEGVYVNTYGRITKDVVLQWGEMPTSVAYIRSNQTMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVYFMTLGRTSLLSW	Patented-recorded	"Optimization of highly selective 2,4-diaminopyrimidine-5-carboxamide inhibitors of Sky kinase. Bioorg Med Chem Lett. 2013 Feb 15;23(4):1051-5."	0	EC:2.7	Kinase	protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	CNH domain; Protein kinase domain	PF00780; PF00069	PF00780; CNH; PF00069; Pkinase	.	.	hsa04010: MAPK signaling pathway	R-HSA-2559580:Oxidative Stress Induced Senescence	.	O95819
TT4TQBX	Extracellular signal-regulated kinase 2 (ERK2)	P28482	MK01_HUMAN	Kinase	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	MAPK1	"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."	EC 2.7.11.24	6QAW; 6QAQ; 6QAL; 6QAG; 6Q7K	MAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS	Clinical trial	Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J. 2000 Oct 1;351(Pt 1):95-105.	21	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.	2.7.11.24	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	P28482
TT056SO	Stress-activated protein kinase JNK3 (JNK3)	P53779	MK10_HUMAN	Kinase	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	MAPK10	"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."	EC 2.7.11.24	6EQ9; 6EMH; 6EKD; 4Z9L; 4Y5H	MSLHFLYYCSEPTLDVKIAFCQGFDKQVDVSYIAKHYNMSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMNSEEKTKNGVVKGQPSPSGAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR	Patented-recorded	c-Jun N-terminal kinase inhibitors: a patent review (2010 - 2014).Expert Opin Ther Pat. 2015;25(8):849-72.	15.5	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.	2.7.11.24	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	P53779
TT73U6C	Stress-activated protein kinase 2b (p38 beta)	Q15759	MK11_HUMAN	Kinase	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	MAPK11	"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."	EC 2.7.11.24	3GP0; 3GC9; 3GC8	MSGPRAGFYRQELNKTVWEVPQRLQGLRPVGSGAYGSVCSAYDARLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHLKHENVIGLLDVFTPATSIEDFSEVYLVTTLMGADLNNIVKCQALSDEHVQFLVYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADEEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLQGKALFPGSDYIDQLKRIMEVVGTPSPEVLAKISSEHARTYIQSLPPMPQKDLSSIFRGANPLAIDLLGRMLVLDSDQRVSAAEALAHAYFSQYHDPEDEPEAEPYDESVEAKERTLEEWKELTYQEVLSFKPPEPPKPPGSLEIEQ	Clinical trial	Pharmacological inhibitors of MAPK pathways. Trends Pharmacol Sci. 2002 Jan;23(1):40-5.	21	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.	2.7.11.24	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	Q15759
TTYT93M	MAP kinase p38 (MAPK12)	P53778	MK12_HUMAN	Kinase	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	MAPK12	"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."	EC 2.7.11.24	4QUM; 1CM8	MSSPPPARSGFYRQEVTKTAWEVRAVYRDLQPVGSGAYGAVCSAVDGRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDETLDDFTDFYLVMPFMGTDLGKLMKHEKLGEDRIQFLVYQMLKGLRYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQADSEMTGYVVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKTLFKGSDHLDQLKEIMKVTGTPPAEFVQRLQSDEAKNYMKGLPELEKKDFASILTNASPLAVNLLEKMLVLDAEQRVTAGEALAHPYFESLHDTEDEPQVQKYDDSFDDVDRTLDEWKRVTYKEVLSFKPPRQLGARVSKETPL	Successful	Agents in development for the treatment of diabetic nephropathy. Expert Opin Emerg Drugs. 2008 Sep;13(3):447-63.	34	.	.	.	.	.	.	.	.	.	.	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	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	.	P53778
TTQBR95	Stress-activated protein kinase 2a (p38 alpha)	Q16539	MK14_HUMAN	Kinase	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	MAPK14	"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."	EC 2.7.11.24	6M9L; 6M95; 6HWV; 6HWU; 6HWT	MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES	Clinical trial	"Clinical pipeline report, company report or official report of GlaxoSmithKline (2009)."	25	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.	2.7.11.24 	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	MetaCyc:HS03507-MON	Q16539
TT1MG9E	Extracellular signal-regulated kinase 1 (ERK1)	P27361	MK03_HUMAN	Kinase	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	MAPK3	"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."	EC 2.7.11.24	6GES; 4QTB; 2ZOQ	MAAAAAQGGGGGEPRRTEGVGPGVPGEVEMVKGQPFDVGPRYTQLQYIGEGAYGMVSSAYDHVRKTRVAIKKISPFEHQTYCQRTLREIQILLRFRHENVIGIRDILRASTLEAMRDVYIVQDLMETDLYKLLKSQQLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLINTTCDLKICDFGLARIADPEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINMKARNYLQSLPSKTKVAWAKLFPKSDSKALDLLDRMLTFNPNKRITVEEALAHPYLEQYYDPTDEPVAEEPFTFAMELDDLPKERLKELIFQETARFQPGVLEAP	Clinical trial	DOI: 10.1158/1538-7445.AM2015-4693	19	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.	2.7.11.24	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	P27361
TTU6FSC	Extracellular signal-regulated kinase 5 (ERK5)	Q13164	MK07_HUMAN	Kinase	PRKM7; Mitogen-activated protein kinase 7; MAPK 7; MAP kinase 7; ERK-5; Big MAP kinase 1; BMK1; BMK-1	MAPK7	"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."	EC 2.7.11.24	6HKN; 6HKM; 5O7I; 5BYZ; 5BYY	MAEPLKEEDGEDGSAEPPGPVKAEPAHTAASVAAKNLALLKARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFAFDREALTRERIKEAIVAEIEDFHARREGIRQQIRFQPSLQPVASEPGCPDVEMPSPWAPSGDCAMESPPPAPPPCPGPAPDTIDLTLQPPPPVSEPAPPKKDGAISDNTKAALKAALLKSLRSRLRDGPSAPLEAPEPRKPVTAQERQREREEKRRRRQERAKEREKRRQERERKERGAGASGGPSTDPLAGLVLSDNDRSLLERWTRMARPAAPALTSVPAPAPAPTPTPTPVQPTSPPPGPVAQPTGPQPQSAGSTSGPVPQPACPPPGPAPHPTGPPGPIPVPAPPQIATSTSLLAAQSLVPPPGLPGSSTPGVLPYFPPGLPPPDAGGAPQSSMSESPDVNLVTQQLSKSQVEDPLPPVFSGTPKGSGAGYGVGFDLEEFLNQSFDMGVADGPQDGQADSASLSASLLADWLEGHGMNPADIESLQREIQMDSPMLLADLPDLQDP	Patented-recorded	BET inhibitors in cancer therapeutics: a patent review.Expert Opin Ther Pat. 2016;26(4):505-22.	15.5	EC:2.7	.	protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.	2.7.11.24	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04010: MAPK signaling pathway; hsa04540: Gap junction; hsa04657: IL-17 signaling pathway; hsa04722: Neurotrophin signaling pathway; hsa04912: GnRH signaling pathway; hsa04921: Oxytocin signaling pathway; hsa05206: MicroRNAs in cancer; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-198753: ERK/MAPK targets; R-HSA-198765: Signalling to ERK5; R-HSA-202670: ERKs are inactivated; R-HSA-2559582: Senescence-Associated Secretory Phenotype (SASP); R-HSA-881907: Gastrin-CREB signalling pathway via PKC and MAPK; R-HSA-8853659: RET signaling	.	Q13164
TT0K6EO	Stress-activated protein kinase JNK1 (JNK1)	P45983	MK08_HUMAN	Kinase	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	MAPK8	"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."	EC 2.7.11.24	6F5E; 5LW1; 4YR8; 4UX9; 4QTD	MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLEERTKNGVIRGQPSPLGAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR	Clinical trial	Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J. 2000 Oct 1;351(Pt 1):95-105.	21	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.	2.7.11.24 	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	P45983
TTR2TXZ	Jun N terminal kinase (JNK)	P45983; P45984; P53779	MK08_HUMAN; MK09_HUMAN; MK10_HUMAN	Kinase	c-Jun N-terminal kinase; Stress-activated protein kinase JNK; SAPK1; PRKM; MAP kinase; JNK	MAPK8	"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."	.	.	MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLEERTKNGVIRGQPSPLGAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	"hsa01522: Endocrine resistance; hsa04010: MAPK signaling pathway; hsa04012: ErbB signaling pathway; hsa04014: Ras signaling pathway; hsa04024: cAMP signaling pathway; hsa04068: FoxO signaling pathway; hsa04071: Sphingolipid signaling pathway; hsa04137: Mitophagy - animal; hsa04140: Autophagy - animal; hsa04141: Protein processing in endoplasmic reticulum; hsa04210: Apoptosis; hsa04215: Apoptosis - multiple species; hsa04217: Necroptosis; hsa04310: Wnt signaling pathway; hsa04380: Osteoclast differentiation; hsa04510: Focal adhesion; hsa04530: Tight junction; hsa04620: Toll-like receptor signaling pathway; hsa04621: NOD-like receptor signaling pathway; hsa04622: RIG-I-like receptor signaling pathway; hsa04625: C-type lectin receptor signaling pathway; hsa04657: IL-17 signaling pathway; hsa04658: Th1 and Th2 cell differentiation; hsa04659: Th17 cell differentiation; 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; hsa04926: Relaxin signaling pathway; hsa04930: Type II diabetes mellitus; hsa04931: Insulin resistance; hsa04932: Non-alcoholic fatty liver disease; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04935: Growth hormone synthesis, secretion and action; hsa04936: Alcoholic liver disease; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05016: Huntington disease; hsa05017: Spinocerebellar ataxia; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05120: Epithelial cell signaling in Helicobacter pylori infection; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05133: Pertussis; hsa05135: Yersinia infection; hsa05142: Chagas disease; hsa05145: Toxoplasmosis; hsa05152: Tuberculosis; hsa05161: Hepatitis B; hsa05162: Measles; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05210: Colorectal cancer; hsa05212: Pancreatic cancer; hsa05231: Choline metabolism in cancer; hsa05415: Diabetic cardiomyopathy; hsa05417: Lipid and atherosclerosis; hsa05418: Fluid shear stress and atherosclerosis"	R-HSA-111446: Activation of BIM and translocation to mitochondria; R-HSA-139910: Activation of BMF and translocation to mitochondria; 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; R-HSA-9007892: Interleukin-38 signaling; R-HSA-9673324: WNT5:FZD7-mediated leishmania damping	.	P45983
TTXKZ8Q	JNK-interacting protein 1 peptide (pepJIP1)	Q9UQF2	JIP1_HUMAN	.	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	MAPK8IP1	"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."	.	6FUZ; 5LW1; 4IZY; 4HYU; 4HYS	MAERESGGLGGGAASPPAASPFLGLHIASPPNFRLTHDISLEEFEDEDLSEITDECGISLQCKDTLSLRPPRAGLLSAGGGGAGSRLQAEMLQMDLIDATGDTPGAEDDEEDDDEERAARRPGAGPPKAESGQEPASRGQGQSQGQSQGPGSGDTYRPKRPTTLNLFPQVPRSQDTLNNNSLGKKHSWQDRVSRSSSPLKTGEQTPPHEHICLSDELPPQSGPAPTTDRGTSTDSPCRRSTATQMAPPGGPPAAPPGGRGHSHRDRIHYQADVRLEATEEIYLTPVQRPPDAAEPTSAFLPPTESRMSVSSDPDPAAYPSTAGRPHPSISEEEEGFDCLSSPERAEPPGGGWRGSLGEPPPPPRASLSSDTSALSYDSVKYTLVVDEHAQLELVSLRPCFGDYSDESDSATVYDNCASVSSPYESAIGEEYEEAPRPQPPACLSEDSTPDEPDVHFSKKFLNVFMSGRSRSSSAESFGLFSCIINGEEQEQTHRAIFRFVPRHEDELELEVDDPLLVELQAEDYWYEAYNMRTGARGVFPAYYAIEVTKEPEHMAALAKNSDWVDQFRVKFLGSVQVPYHKGNDVLCAAMQKIATTRRLTVHFNPPSSCVLEISVRGVKIGVKADDSQEAKGNKCSHFFQLKNISFCGYHPKNNKYFGFITKHPADHRFACHVFVSEDSTKALAESVGRAFQQFYKQFVEYTCPTEDIYLE	Patented-recorded	c-Jun N-terminal kinase inhibitors: a patent review (2010 - 2014).Expert Opin Ther Pat. 2015;25(8):849-72.	15.5	.	JIP scaffold family	JIP scaffold family.	.	.	Phosphotyrosine interaction domain (PTB/PID); Variant SH3 domain	PF00640; PF14604	PF00640; PID; PF14604; SH3_9	.	.	hsa04010:MAPK signaling pathway	.	.	Q9UQF2
TT3IVG2	JNK2 messenger RNA (JNK2 mRNA)	P45984	MK09_HUMAN	mRNA target	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)	MAPK9	"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."	EC 2.7.11.24	3NPC; 3E7O	MSDSKCDSQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGCVIFQGTDHIDQWNKVIEQLGTPSAEFMKKLQPTVRNYVENRPKYPGIKFEELFPDWIFPSESERDKIKTSQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEAEAPPPQIYDAQLEEREHAIEEWKELIYKEVMDWEERSKNGVVKDQPSDAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR	Literature-reported	"N-(3-Cyano-4,5,6,7-tetrahydro-1-benzothien-2-yl)amides as potent, selective, inhibitors of JNK2 and JNK3. Bioorg Med Chem Lett. 2007 Mar 1;17(5):1296-301."	0	mRNA	mRNA target	.	.	.	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	P45984
TTHS0U8	Stress-activated protein kinase JNK2 (JNK2)	P45984	MK09_HUMAN	Kinase	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	MAPK9	"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."	EC 2.7.11.24	3NPC; 3E7O	MSDSKCDSQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGCVIFQGTDHIDQWNKVIEQLGTPSAEFMKKLQPTVRNYVENRPKYPGIKFEELFPDWIFPSESERDKIKTSQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEAEAPPPQIYDAQLEEREHAIEEWKELIYKEVMDWEERSKNGVVKDQPSDAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR	Preclinical	c-Jun N-terminal kinase inhibitors: a patent review (2010 - 2014).Expert Opin Ther Pat. 2015;25(8):849-72.	15.5	EC:2.7	Kinase	protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.	2.7.11.24 	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	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	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	.	P45984
TTWDKCL	Target of rapamycin complex 2 MAPKAP1 (MTORC2)	Q9BPZ7	SIN1_HUMAN	.	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	MAPKAP1	"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."	.	5ZCS; 3VOQ	MAFLDNPTIILAHIRQSHVTSDDTGMCEMVLIDHDVDLEKIHPPSMPGDSGSEIQGSNGETQGYVYAQSVDITSSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQELKSLFEKKSLKEKPPISGKQSILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTATKKIDVYLPLHSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGREPKLNDNVSAYCLHIAEDDGEVDTDFPPLDSNEPIHKFGFSTLALVEKYSSPGLTSKESLFVRINAAHGFSLIQVDNTKVTMKEILLKAVKRRKGSQKVSGPQYRLEKQSEPNVAVDLDSTLESQSAWEFCLVRENSSRADGVFEEDSQIDIATVQDMLSSHHYKSFKVSMIHRLRFTTDVQLGISGDKVEIDPVTNQKASTKFWIKQKPISIDSDLLCACDLAEEKSPSHAIFKLTYLSNHDYKHLYFESDAATVNEIVLKVNYILESRASTARADYFAQKQRKLNRRTSFSFQKEKKSGQQ	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	SIN1 family.	.	.	"SAPK-interacting protein 1 (Sin1), middle CRIM domain; Stress-activated map kinase interacting protein 1 (SIN1); SAPK-interacting protein 1 (Sin1), Pleckstrin-homology"	PF16978; PF05422; PF16979	PF16978; CRIM; PF05422; SIN1; PF16979; SIN1_PH	.	.	hsa04150: mTOR signaling pathway	R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-389357: CD28 dependent PI3K/Akt signaling; R-HSA-5218920: VEGFR2 mediated vascular permeability; R-HSA-5674400: Constitutive Signaling by AKT1 E17K in Cancer; R-HSA-6804757: Regulation of TP53 Degradation	.	Q9BPZ7
TTMUG9D	MAPK-activated protein kinase 2 (MAPKAPK2)	P49137	MAPK2_HUMAN	Kinase	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	MAPKAPK2	"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."	EC 2.7.11.1	4TYH; 3WI6; 3R30; 3R2Y; 3R2B	MLSNSQGQSPPVPFPAPAPPPQPPTPALPHPPAQPPPPPPQQFPQFHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYENLYAGRKCLLIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSALATMRVDYEQIKIKKIEDASNPLLLKRRKKARALEAAALAH	Clinical trial	National Cancer Institute Drug Dictionary (drug id 577812).	19	EC:2.7	Kinase	protein kinase superfamily. CAMK Ser/Thr protein kinase family.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04010:MAPK signaling pathway; hsa04370:VEGF signaling pathway; hsa04722:Neurotrophin signaling pathway; hsa05203:Viral carcinogenesis	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	MetaCyc:HS08751-MON	P49137
TTFS4VU	MAPK-activated protein kinase 3 (MAPKAPK3)	Q16644	MAPK3_HUMAN	.	MAPKAPK3	MAPKAPK3	"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."	EC 2.7.11.1	3SHE; 3R1N; 3FXW; 3FHR	MDGETAEEQGGPVPPPVAPGGPGLGGAPGGRREPKKYAVTDDYQLSKQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARQEVDHHWQASGGPHIVCILDVYENMHHGKRCLLIIMECMEGGELFSRIQERGDQAFTEREAAEIMRDIGTAIQFLHSHNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRIRLGQYGFPNPEWSEVSEDAKQLIRLLLKTDPTERLTITQFMNHPWINQSMVVPQTPLHTARVLQEDKDHWDEVKEEMTSALATMRVDYDQVKIKDLKTSNNRLLNKRRKKQAGSSSASQGCNNQ	Literature-reported	Pyrrolopyridine inhibitors of mitogen-activated protein kinase-activated protein kinase 2 (MK-2). J Med Chem. 2007 May 31;50(11):2647-54.	0	.	.	.	.	.	.	.	.	.	.	hsa04010: MAPK signaling pathway; hsa04370: VEGF signaling pathway	R-HSA-171007: p38MAPK events; R-HSA-2559580: Oxidative Stress Induced Senescence; R-HSA-4420097: VEGFA-VEGFR2 Pathway; R-HSA-450302: activated TAK1 mediates p38 MAPK activation	.	Q16644
TT3UJ7Z	MAPK-activated protein kinase 5 (MAPKAPK5)	Q8IW41	MAPK5_HUMAN	Kinase	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	MAPKAPK5	"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."	EC 2.7.11.1	.	MSEESDMDKAIKETSILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQIALALRHCHLLNIAHRDLKPENLLFKDNSLDAPVKLCDFGFAKIDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQLMMDKAVVAGIQQAHAEQLANMRIQDLKVSLKPLHSVNNPILRKRKLLGTKPKDSVYIHDHENGAEDSNVALEKLRDVIAQCILPQAGKGENEDEKLNEVMQEAWKYNRECKLLRDTLQSFSWNGRGFTDKVDRLKLAEIVKQVIEEQTTSHESQ	Discontinued	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 2096).	5	EC:2.7	Kinase	protein kinase superfamily. CAMK Ser/Thr protein kinase family.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	hsa04010: MAPK signaling pathway	R-HSA-2559580:Oxidative Stress Induced Senescence; R-HSA-5687128:MAPK6/MAPK4 signaling	.	Q8IW41
TTS87KH	Microtubule-associated protein tau (MAPT)	P10636	TAU_HUMAN	.	tau; Paired helical filamenttau; Paired helical filament-tau; Neurofibrillary tangle protein; MTBT1; MAPTL	MAPT	"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."	.	6QJQ; 6QJP; 6QJM; 6QJH; 6NWQ	MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQEPESGKVVQEGFLREPGPPGLSHQLMSGMPGAPLLPEGPREATRQPSGTGPEDTEGGRHAPELLKHQLLGDLHQEGPPLKGAGGKERPGSKEEVDEDRDVDESSPQDSPPSKASPAQDGRPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVSKSKDGTGSDDKKAKTSTRSSAKTLKNRPCLSPKHPTPGSSDPLIQPSSPAVCPEPPSSPKYVSSVTSRTGSSGAKEMKLKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL	Clinical trial	Microtubules (tau) as an emerging therapeutic target: NAP (davunetide). Curr Pharm Des. 2011;17(31):3413-7.	25	.	.	.	.	.	"Tau and MAP protein, tubulin-binding repeat"	PF00418	PF00418; Tubulin-binding	.	.	hsa04010:MAPK signaling pathway; hsa05010:Alzheimer's disease	R-HSA-264870:Caspase-mediated cleavage of cytoskeletal proteins	.	P10636
TTHPOGR	Tau messenger RNA (TAU mRNA)	P10636	TAU_HUMAN	mRNA target	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)	MAPT	"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."	.	6QJQ; 6QJP; 6QJM; 6QJH; 6NWQ	MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQEPESGKVVQEGFLREPGPPGLSHQLMSGMPGAPLLPEGPREATRQPSGTGPEDTEGGRHAPELLKHQLLGDLHQEGPPLKGAGGKERPGSKEEVDEDRDVDESSPQDSPPSKASPAQDGRPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVSKSKDGTGSDDKKAKTSTRSSAKTLKNRPCLSPKHPTPGSSDPLIQPSSPAVCPEPPSSPKYVSSVTSRTGSSGAKEMKLKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL	Literature-reported	The Tau-Induced Reduction of mRNA Levels of Kv Channels in Human Neuroblastoma SK-N-SH Cells. J Mol Neurosci. 2016 Feb;58(2):306-11.	.	mRNA	mRNA target	.	.	.	"Tau and MAP protein, tubulin-binding repeat"	PF00418	PF00418; Tubulin-binding	.	.	hsa04010: MAPK signaling pathway; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05022: Pathways of neurodegeneration - multiple diseases	R-HSA-264870: Caspase-mediated cleavage of cytoskeletal proteins; R-HSA-9619483: Activation of AMPK downstream of NMDARs	.	P10636
TTXZCO0	Microtubule-associated protein tau phosphorylation (MAPT p)	P10636	TAU_HUMAN	.	tau phosphorylation; Paired helical filamenttau phosphorylation; Paired helical filament-tau phosphorylation; PHFtau; PHF-tau; Neurofibrillary tangle protein phosphorylation; MTBT1 phosphorylation; MAPTL phosphorylation	MAPT	"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."	.	6QJQ; 6QJP; 6QJM; 6QJH; 6NWQ	MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQEPESGKVVQEGFLREPGPPGLSHQLMSGMPGAPLLPEGPREATRQPSGTGPEDTEGGRHAPELLKHQLLGDLHQEGPPLKGAGGKERPGSKEEVDEDRDVDESSPQDSPPSKASPAQDGRPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVSKSKDGTGSDDKKAKTSTRSSAKTLKNRPCLSPKHPTPGSSDPLIQPSSPAVCPEPPSSPKYVSSVTSRTGSSGAKEMKLKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL	Patented-recorded	Dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) inhibitors: a survey of recent patent literature.Expert Opin Ther Pat. 2017 Nov;27(11):1183-1199.	15.5	.	.	.	.	.	"Tau and MAP protein, tubulin-binding repeat"	PF00418	PF00418; Tubulin-binding	.	.	hsa04010: MAPK signaling pathway; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05022: Pathways of neurodegeneration - multiple diseases	R-HSA-264870: Caspase-mediated cleavage of cytoskeletal proteins; R-HSA-9619483: Activation of AMPK downstream of NMDARs	.	P10636
TTHRM39	Myristoylated alanine-rich C-kinase substrate (MARCKS)	P29966	MARCS_HUMAN	.	"Protein kinase C substrate, 80 kDa protein, light chain; PRKCSL; PKCSL; Myristoylated alaninerich Ckinase substrate; MACS; 80KL protein; 80K-L protein"	MARCKS	"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."	.	.	MGAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAESGAKEELQANGSAPAADKEEPAAAGSGAASPSAAEKGEPAAAAAPEAGASPVEKEAPAEGEAAEPGSPTAAEGEAASAASSTSSPKAEDGATPSPSNETPKKKKKRFSFKKSFKLSGFSFKKNKKEAGEGGEAEAPAAEGGKDEAAGGAAAAAAEAGAASGEQAAAPGEEAAAGEEGAAGGDPQEAKPQEAAVAPEKPPASDETKAAEEPSKVEEKKAEEAGASAAACEAPSAAGPGAPPEQEAAPAEEPAAAAASSACAAPSQEAQPECSPEAPPAEAAE	Clinical trial	Inhibition of myristoylated alanine-rich C kinase substrate (MARCKS) protein inhibits ozone-induced airway neutrophilia and inflammation. Exp Lung Res. 2010 Mar;36(2):75-84.	21	.	.	MARCKS family.	.	.	MARCKS family	PF02063	PF02063; MARCKS	.	.	hsa04666: Fc gamma R-mediated phagocytosis; hsa05206: MicroRNAs in cancer	R-HSA-399997: Acetylcholine regulates insulin secretion	.	P29966
TTAJ45Y	HUMAN microtubule affinity regulating kinase 2 (MARK2)	Q7KZI7	MARK2_HUMAN	Kinase	Par-1b; Par1b; PAR1 homolog b; PAR1 homolog; MAP/microtubule affinity-regulating kinase 2; EMK-1; ELKL motif kinase 1	MARK2	"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."	EC 2.7.11.1	3IEC; 5EAK; 5KZ7; 5KZ8	MSSARTPLPTLNERDTEQPTLGHLDSKPSSKSNMIRGRNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYKSSELEGDTITLKPRPSADLTNSSAPSPSHKVQRSVSANPKQRRFSDQAAGPAIPTSNSYSKKTQSNNAENKRPEEDRESGRKASSTAKVPASPLPGLERKKTTPTPSTNSVLSTSTNRSRNSPLLERASLGQASIQNGKDSLTMPGSRASTASASAAVSAARPRQHQKSMSASVHPNKASGLPPTESNCEVPRPSTAPQRVPVASPSAHNISSSGGAPDRTNFPRGVSSRSTFHAGQLRQVRDQQNLPYGVTPASPSGHSQGRRGASGSIFSKFTSKFVRRNLSFRFARRNLNEPESKDRVETLRPHVVGSGGNDKEKEEFREAKPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHEKYMLLCMHGTPGHEDFVQWEMEVCKLPRLSLNGVRFKRISGTSMAFKNIASKIANELKL	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q7KZI7
TT3DCYJ	Microtubule affinity regulating kinase 3 (MARK3)	P27448	MARK3_HUMAN	Kinase	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	MARK3	"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."	EC 2.7.11.1	3FE3; 2QNJ	MSTRTPLPTVNERDTENHTSHGDGRQEVTSRTSRSGARCRNSIASCADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGREVAIKIIDKTQLNPTSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLIMEYASGGEVFDYLVAHGRMKEKEARSKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTVGGKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKRFLVLNPIKRGTLEQIMKDRWINAGHEEDELKPFVEPELDISDQKRIDIMVGMGYSQEEIQESLSKMKYDEITATYLLLGRKSSELDASDSSSSSNLSLAKVRPSSDLNNSTGQSPHHKVQRSVSSSQKQRRYSDHAGPAIPSVVAYPKRSQTSTADSDLKEDGISSRKSSGSAVGGKGIAPASPMLGNASNPNKADIPERKKSSTVPSSNTASGGMTRRNTYVCSERTTADRHSVIQNGKENSTIPDQRTPVASTHSISSAATPDRIRFPRGTASRSTFHGQPRERRTATYNGPPASPSLSHEATPLSQTRSRGSTNLFSKLTSKLTRRNMSFRFIKRLPTEYERNGRYEGSSRNVSAEQKDENKEAKPRSLRFTWSMKTTSSMDPGDMMREIRKVLDANNCDYEQRERFLLFCVHGDGHAENLVQWEMEVCKLPRLSLNGVRFKRISGTSIAFKNIASKIANELKL	Clinical trial	National Cancer Institute Drug Dictionary (drug id 577812).	19	EC:2.7	Kinase	protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Kinase associated domain 1; Protein kinase domain; UBA/TS-N domain	PF02149; PF00069; PF00627	PF02149; KA1; PF00069; Pkinase; PF00627; UBA	.	.	.	R-HSA-5673000:RAF activation; R-HSA-5674135:MAP2K and MAPK activation; R-HSA-5675221:Negative regulation of MAPK pathway	.	P27448
TT0MFOL	HUMAN microtubule affinity regulating kinase 3 (MARK3)	P27448	MARK3_HUMAN	Kinase	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	MARK3	"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."	EC 2.7.11.1	3FE3; 2QNJ	MSTRTPLPTVNERDTENHTSHGDGRQEVTSRTSRSGARCRNSIASCADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGREVAIKIIDKTQLNPTSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLIMEYASGGEVFDYLVAHGRMKEKEARSKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTVGGKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKRFLVLNPIKRGTLEQIMKDRWINAGHEEDELKPFVEPELDISDQKRIDIMVGMGYSQEEIQESLSKMKYDEITATYLLLGRKSSELDASDSSSSSNLSLAKVRPSSDLNNSTGQSPHHKVQRSVSSSQKQRRYSDHAGPAIPSVVAYPKRSQTSTADSDLKEDGISSRKSSGSAVGGKGIAPASPMLGNASNPNKADIPERKKSSTVPSSNTASGGMTRRNTYVCSERTTADRHSVIQNGKENSTIPDQRTPVASTHSISSAATPDRIRFPRGTASRSTFHGQPRERRTATYNGPPASPSLSHEATPLSQTRSRGSTNLFSKLTSKLTRRNMSFRFIKRLPTEYERNGRYEGSSRNVSAEQKDENKEAKPRSLRFTWSMKTTSSMDPGDMMREIRKVLDANNCDYEQRERFLLFCVHGDGHAENLVQWEMEVCKLPRLSLNGVRFKRISGTSIAFKNIASKIANELKL	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-5673000: RAF activation; R-HSA-5674135: MAP2K and MAPK activation; R-HSA-5675221: Negative regulation of MAPK pathway; R-HSA-6802946: Signaling by moderate kinase activity BRAF mutants; R-HSA-6802948: Signaling by high-kinase activity BRAF mutants; R-HSA-6802952: Signaling by BRAF and RAF1 fusions; R-HSA-6802955: Paradoxical activation of RAF signaling by kinase inactive BRAF; R-HSA-9649948: Signaling downstream of RAS mutants; R-HSA-9656223: Signaling by RAF1 mutants	.	P27448
TTOISYB	Proto-oncogene Mas (MAS)	P04201	MAS_HUMAN	GPCR rhodopsin	"MGRA; MAS1 proto-oncogene, G protein-coupled receptor"	MAS1	"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."	.	.	MDGSNVTSFVVEEPTNISTGRNASVGNAHRQIPIVHWVIMSISPVGFVENGILLWFLCFRMRRNPFTVYITHLSIADISLLFCIFILSIDYALDYELSSGHYYTIVTLSVTFLFGYNTGLYLLTAISVERCLSVLYPIWYRCHRPKYQSALVCALLWALSCLVTTMEYVMCIDREEESHSRNDCRAVIIFIAILSFLVFTPLMLVSSTILVVKIRKNTWASHSSKLYIVIMVTIIIFLIFAMPMRLLYLLYYEYWSTFGNLHHISLLFSTINSSANPFIYFFVGSSKKKRFKESLKVVLTRAFKDEMQPRRQKDNCNTVTVETVV	Clinical trial	New therapeutic pathways in the RAS. J Renin Angiotensin Aldosterone Syst. 2012 Dec;13(4):505-8.	25	PF00001	.	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04614:Renin-angiotensin system	.	.	P04201
TTTQH13	Angiotensin-(1-7) receptor (MAS1)	P04201	MAS_HUMAN	.	MAS	MAS1	"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."	.	.	MDGSNVTSFVVEEPTNISTGRNASVGNAHRQIPIVHWVIMSISPVGFVENGILLWFLCFRMRRNPFTVYITHLSIADISLLFCIFILSIDYALDYELSSGHYYTIVTLSVTFLFGYNTGLYLLTAISVERCLSVLYPIWYRCHRPKYQSALVCALLWALSCLVTTMEYVMCIDREEESHSRNDCRAVIIFIAILSFLVFTPLMLVSSTILVVKIRKNTWASHSSKLYIVIMVTIIIFLIFAMPMRLLYLLYYEYWSTFGNLHHISLLFSTINSSANPFIYFFVGSSKKKRFKESLKVVLTRAFKDEMQPRRQKDNCNTVTVETVV	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction; hsa04614: Renin-angiotensin system; hsa05171: Coronavirus disease - COVID-19	.	.	P04201
TTR01E9	Mannan-binding lectin serine protease-2 (MASP2)	O00187	MASP2_HUMAN	Peptidase	Mannosebinding proteinassociated serine protease 2; Mannanbinding lectin serine protease 2 B chain; Mannanbinding lectin serine protease 2; MBLassociated serine protease 2; MASP2	MASP2	"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}."	EC 3.4.21.104	5JPM; 4FXG; 3TVJ; 1ZJK; 1SZB	MRLLTLLGLLCGSVATPLGPKWPEPVFGRLASPGFPGEYANDQERRWTLTAPPGYRLRLYFTHFDLELSHLCEYDFVKLSSGAKVLATLCGQESTDTERAPGKDTFYSLGSSLDITFRSDYSNEKPFTGFEAFYAAEDIDECQVAPGEAPTCDHHCHNHLGGFYCSCRAGYVLHRNKRTCSALCSGQVFTQRSGELSSPEYPRPYPKLSSCTYSISLEEGFSVILDFVESFDVETHPETLCPYDFLKIQTDREEHGPFCGKTLPHRIETKSNTVTITFVTDESGDHTGWKIHYTSTAQPCPYPMAPPNGHVSPVQAKYILKDSFSIFCETGYELLQGHLPLKSFTAVCQKDGSWDRPMPACSIVDCGPPDDLPSGRVEYITGPGVTTYKAVIQYSCEETFYTMKVNDGKYVCEADGFWTSSKGEKSLPVCEPVCGLSARTTGGRIYGGQKAKPGDFPWQVLILGGTTAAGALLYDNWVLTAAHAVYEQKHDASALDIRMGTLKRLSPHYTQAWSEAVFIHEGYTHDAGFDNDIALIKLNNKVVINSNITPICLPRKEAESFMRTDDIGTASGWGLTQRGFLARNLMYVDIPIVDHQKCTAAYEKPPYPRGSVTANMLCAGLESGGKDSCRGDSGGALVFLDSETERWFVGGIVSWGSMNCGEAGQYGVYTKVINYIPWIENIISDF	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	hsa04610: Complement and coagulation cascades; hsa05150: Staphylococcus aureus infection; hsa05171: Coronavirus disease - COVID-19	R-HSA-166662: Lectin pathway of complement activation; R-HSA-166663: Initial triggering of complement; R-HSA-2855086: Ficolins bind to repetitive carbohydrate structures on the target cell surface; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses	.	O00187
TTSMPXQ	S-adenosylmethionine synthase type-2 (MAT2A)	P31153	METK2_HUMAN	AdoMet synthase family	Methionine adenosyltransferase II; Methionine adenosyltransferase 2; MAT-II; MAT 2; AdoMet synthase 2	MAT2A	"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."	EC 2.5.1.6	6G6R; 6FWB; 6FCD; 6FCB; 6FBP	MNGQLNGFHEAFIEEGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways; hsa01230:Biosynthesis of amino acids	R-HSA-156581: Methylation	MetaCyc:HS09847-MON	P31153
TT059DA	Serum amyloid A-activating factor-1 (MAZ)	P56270	MAZ_HUMAN	.	Zinc finger protein 801; ZNF801; ZF87; Transcription factor Zif87; SAF-1; Purine-binding transcription factor; Pur-1; Myc-associated zinc finger protein; MAZI	MAZ	"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."	.	.	MFPVFPCTLLAPPFPVLGLDSRGVGGLMNSFPPPQGHAQNPLQVGAELQSRFFASQGCAQSPFQAAPAPPPTPQAPAAEPLQVDLLPVLAAAQESAAAAAAAAAAAAAVAAAPPAPAAASTVDTAALKQPPAPPPPPPPVSAPAAEAAPPASAATIAAAAATAVVAPTSTVAVAPVASALEKKTKSKGPYICALCAKEFKNGYNLRRHEAIHTGAKAGRVPSGAMKMPTMVPLSLLSVPQLSGAGGGGGEAGAGGGAAAVAAGGVVTTTASGKRIRKNHACEMCGKAFRDVYHLNRHKLSHSDEKPYQCPVCQQRFKRKDRMSYHVRSHDGAVHKPYNCSHCGKSFSRPDHLNSHVRQVHSTERPFKCEKCEAAFATKDRLRAHTVRHEEKVPCHVCGKMLSSAYISDHMKVHSQGPHHVCELCNKGTGEVCPMAAAAAAAAAAAAAAVAAPPTAVGSLSGAEGVPVSSQPLPSQPW	Literature-reported	Induction of matrix metalloproteinase 1 gene expression is regulated by inflammation-responsive transcription factor SAF-1 in osteoarthritis. Arthritis Rheum. 2003 Jan;48(1):134-45.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P56270
TTMQDZ5	Mannose binding protein (MBL2)	P11226	MBL2_HUMAN	.	Mannosebinding protein C; Mannosebinding lectin; Mannanbinding protein; MBPC; MBP1; MBL2; Collectin1	MBL2	"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}."	.	1HUP	MSLFPSLPLLLLSMVAASYSETVTCEDAQKTCPAVIACSSPGINGFPGKDGRDGTKGEKGEPGQGLRGLQGPPGKLGPPGNPGPSGSPGPKGQKGDPGKSPDGDSSLAASERKALQTEMARIKKWLTFSLGKQVGNKFFLTNGEIMTFEKVKALCVKFQASVATPRNAAENGAIQNLIKEEAFLGITDEKTEGQFVDLTGNRLTYTNWNEGEPNNAGSDEDCVLLLKNGQWNDVPCSTSHLAVCEFPI	Literature-reported	Pharmacological inhibition of mannose-binding lectin ameliorates neurobehavioral dysfunction following experimental traumatic brain injury. J Cereb Blood Flow Metab. 2017 Mar;37(3):938-950.	.	.	.	.	.	.	.	.	.	.	.	hsa04145: Phagosome; hsa04610: Complement and coagulation cascades; hsa05150: Staphylococcus aureus infection; hsa05171: Coronavirus disease - COVID-19	R-HSA-166662: Lectin pathway of complement activation; R-HSA-166663: Initial triggering of complement; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses	.	P11226
TTH9OLG	Muscleblind-like protein 1 (MBNL2)	Q5VZF2	MBNL2_HUMAN	.	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	MBNL2	"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."	.	2RPP; 2E5S	MALNVAPVRDTKWLTLEVCRQFQRGTCSRSDEECKFAHPPKSCQVENGRVIACFDSLKGRCSRENCKYLHPPTHLKTQLEINGRNNLIQQKTAAAMLAQQMQFMFPGTPLHPVPTFPVGPAIGTNTAISFAPYLAPVTPGVGLVPTEILPTTPVIVPGSPPVTVPGSTATQKLLRTDKLEVCREFQRGNCARGETDCRFAHPADSTMIDTSDNTVTVCMDYIKGRCMREKCKYFHPPAHLQAKIKAAQHQANQAAVAAQAAAAAATVMAFPPGALHPLPKRQALEKSNGTSAVFNPSVLHYQQALTSAQLQQHAAFIPTGSVLCMTPATSIDNSEIISRNGMECQESALRITKHCYCTYYPVSSSIELPQTAC	Literature-reported	Muscleblind-like 1 (Mbnl1) regulates pre-mRNA alternative splicing during terminal erythropoiesis. Blood. 2014 Jul 24;124(4):598-610.	.	.	Muscleblind family	muscleblind family.	.	.	Zinc finger C-x8-C-x5-C-x3-H type (and similar)	PF00642	PF00642; zf-CCCH	.	.	.	.	.	Q5VZF2
TTSYOWR	Ghrelin O acyltransferase (GOAT)	Q96T53	MBOA4_HUMAN	Acyltransferase	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	MBOAT4	"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'."	EC 2.3.1.-	.	MEWLWLFFLHPISFYQGAAFPFALLFNYLCIMDSFSTRARYLFLLTGGGALAVAAMGSYAVLVFTPAVCAVALLCSLAPQQVHRWTFCFQMSWQTLCHLGLHYTEYYLHEPPSVRFCITLSSLMLLTQRVTSLSLDICEGKVKAASGGFRSRSSLSEHVCKALPYFSYLLFFPALLGGSLCSFQRFQARVQGSSALHPRHSFWALSWRGLQILGLECLNVAVSRVVDAGAGLTDCQQFECIYVVWTTAGLFKLTYYSHWILDDSLLHAAGFGPELGQSPGEEGYVPDADIWTLERTHRISVFSRKWNQSTARWLRRLVFQHSRAWPLLQTFAFSAWWHGLHPGQVFGFVCWAVMVEADYLIHSFANEFIRSWPMRLFYRTLTWAHTQLIIAYIMLAVEVRSLSSLWLLCNSYNSVFPMVYCILLLLLAKRKHKCN	Patented-recorded	Acyltransferase inhibitors: a patent review (2010-present).Expert Opin Ther Pat. 2015 Feb;25(2):145-58.	15.5	EC:2.3	Acyltransferase	membrane-bound acyltransferase family.	2.3.1.-	Acyltransferases	"MBOAT, membrane-bound O-acyltransferase family"	PF03062	PF03062; MBOAT	.	.	.	"R-HSA-422085: Synthesis, secretion, and deacylation of Ghrelin"	.	Q96T53
TT2RY5P	Myelin basic protein (MBP)	P02686	MBP_HUMAN	.	Myelin membrane encephalitogenic protein; Myelin A1 protein	MBP	"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."	.	1ZGL; 1YMM; 1QCL; 1K2D; 1HQR	MGNHAGKRELNAEKASTNSETNRGESEKKRNLGELSRTTSEDNEVFGEADANQNNGTSSQDTAVTDSKRTADPKNAWQDAHPADPGSRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDSAATSESLDVMASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR	Clinical trial	"NBI-5788, an altered MBP83-99 peptide, induces a T-helper 2-like immune response in multiple sclerosis patients. Ann Neurol. 2000 Nov;48(5):758-65."	21	.	Myelin basic protein	myelin basic protein family.	.	.	Myelin basic protein	PF01669	PF01669; Myelin_MBP	.	.	.	R-HSA-9619665: EGR2 and SOX10-mediated initiation of Schwann cell myelination	.	P02686
TTNSM2I	Endopeptidase S1P (MBTPS1)	Q14703	MBTP1_HUMAN	Peptidase	Subtilisin/kexin-isozyme-1; Subtilisin/kexin-isozyme 1; Site-1 protease; SKI1; SKI-1; S1P; Membrane-bound transcription factor site-1 protease; KIAA0091	MBTPS1	"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)."	EC 3.4.21.112	.	MKLVNIWLLLLVVLLCGKKHLGDRLEKKSFEKAPCPGCSHLTLKVEFSSTVVEYEYIVAFNGYFTAKARNSFISSALKSSEVDNWRIIPRNNPSSDYPSDFEVIQIKEKQKAGLLTLEDHPNIKRVTPQRKVFRSLKYAESDPTVPCNETRWSQKWQSSRPLRRASLSLGSGFWHATGRHSSRRLLRAIPRQVAQTLQADVLWQMGYTGANVRVAVFDTGLSEKHPHFKNVKERTNWTNERTLDDGLGHGTFVAGVIASMRECQGFAPDAELHIFRVFTNNQVSYTSWFLDAFNYAILKKIDVLNLSIGGPDFMDHPFVDKVWELTANNVIMVSAIGNDGPLYGTLNNPADQMDVIGVGGIDFEDNIARFSSRGMTTWELPGGYGRMKPDIVTYGAGVRGSGVKGGCRALSGTSVASPVVAGAVTLLVSTVQKRELVNPASMKQALIASARRLPGVNMFEQGHGKLDLLRAYQILNSYKPQASLSPSYIDLTECPYMWPYCSQPIYYGGMPTVVNVTILNGMGVTGRIVDKPDWQPYLPQNGDNIEVAFSYSSVLWPWSGYLAISISVTKKAASWEGIAQGHVMITVASPAETESKNGAEQTSTVKLPIKVKIIPTPPRSKRVLWDQYHNLRYPPGYFPRDNLRMKNDPLDWNGDHIHTNFRDMYQHLRSMGYFVEVLGAPFTCFDASQYGTLLMVDSEEEYFPEEIAKLRRDVDNGLSLVIFSDWYNTSVMRKVKFYDENTRQWWMPDTGGANIPALNELLSVWNMGFSDGLYEGEFTLANHDMYYASGCSIAKFPEDGVVITQTFKDQGLEVLKQETAVVENVPILGLYQIPAEGGGRIVLYGDSNCLDDSHRQKDCFWLLDALLQYTSYGVTPPSLSHSGNRQRPPSGAGSVTPERMEGNHLHRYSKVLEAHLGDPKPRPLPACPRLSWAKPQPLNETAPSNLWKHQKLLSIDLDKVVLPNFRSNRPQVRPLSPGESGAWDIPGGIMPGRYNQEVGQTIPVFAFLGAMVVLAFFVVQINKAKSRPKRRKPRVKRPQLMQQVHPPKTPSV	Literature-reported	Aminopyrrolidineamide inhibitors of site-1 protease. Bioorg Med Chem Lett. 2007 Aug 15;17(16):4411-4.	0	EC:3.4	.	peptidase S8 family.	3.4.21.112	Acting on peptide bonds (peptidases)	Subtilase family	PF00082	PF00082; Peptidase_S8	.	.	hsa04141:Protein processing in endoplasmic reticulum	R-HSA-1655829: Regulation of cholesterol biosynthesis by SREBP (SREBF); R-HSA-381033: ATF6 (ATF6-alpha) activates chaperones; R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8874211: CREB3 factors activate genes; R-HSA-8957275: Post-translational protein phosphorylation; R-HSA-8963889: Assembly of active LPL and LIPC lipase complexes	.	Q14703
TT0MV2T	Melanocortin receptor 1 (MC1R)	Q01726	MSHR_HUMAN	GPCR rhodopsin	Melanotropin receptor; Melanocyte-stimulating hormone receptor; Melanocortin-1 receptor; MSHR; MSH-R; MC1-R	MC1R	"The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Receptor for MSH (alpha, beta and gamma) and ACTH."	.	.	MAVQGSQRRLLGSLNSTPTAIPQLGLAANQTGARCLEVSISDGLFLSLGLVSLVENALVVATIAKNRNLHSPMYCFICCLALSDLLVSGSNVLETAVILLLEAGALVARAAVLQQLDNVIDVITCSSMLSSLCFLGAIAVDRYISIFYALRYHSIVTLPRARRAVAAIWVASVVFSTLFIAYYDHVAVLLCLVVFFLAMLVLMAVLYVHMLARACQHAQGIARLHKRQRPVHQGFGLKGAVTLTILLGIFFLCWGPFFLHLTLIVLCPEHPTCGCIFKNFNLFLALIICNAIIDPLIYAFHSQELRRTLKEVLTCSW	Successful	The ChEMBL database in 2017. Nucleic Acids Res. 2017 Jan 4;45(D1):D945-D954.	21	PF00001	.	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04916:Melanogenesis	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events	.	Q01726
TTPWFDX	Melanocortin receptor 2 (MC2R)	Q01718	ACTHR_HUMAN	GPCR rhodopsin	Melanocortin-2 receptor; MC2-R; Adrenocorticotropin receptor; Adrenocorticotropic hormone receptor; ACTHR; ACTH-R; ACTH receptor	MC2R	Receptor for corticotropin (ACTH). This receptor is mediated by G proteins (G(s)) which activate adenylate cyclase (cAMP).	.	.	MKHIINSYENINNTARNNSDCPRVVLPEEIFFTISIVGVLENLIVLLAVFKNKNLQAPMYFFICSLAISDMLGSLYKILENILIILRNMGYLKPRGSFETTADDIIDSLFVLSLLGSIFSLSVIAADRYITIFHALRYHSIVTMRRTVVVLTVIWTFCTGTGITMVIFSHHVPTVITFTSLFPLMLVFILCLYVHMFLLARSHTRKISTLPRANMKGAITLTILLGVFIFCWAPFVLHVLLMTFCPSNPYCACYMSLFQVNGMLIMCNAVIDPFIYAFRSPELRDAFKKMIFCSRYW	Successful	Hypothalamic-pituitary-adrenal axis dysfunction in hospitalized neonatal foals. J Vet Intern Med. 2009 Jul-Aug;23(4):901-12.	34	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.2.4	The G-protein-coupled receptor (GPCR) Family	hsa04024:cAMP signaling pathway; hsa04080:Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events	.	Q01718
TTNI91K	Melanocortin receptor 3 (MC3R)	P41968	MC3R_HUMAN	GPCR rhodopsin	MC3-R	MC3R	"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."	.	.	MNASCCLPSVQPTLPNGSEHLQAPFFSNQSSSAFCEQVFIKPEVFLSLGIVSLLENILVILAVVRNGNLHSPMYFFLCSLAVADMLVSVSNALETIMIAIVHSDYLTFEDQFIQHMDNIFDSMICISLVASICNLLAIAVDRYVTIFYALRYHSIMTVRKALTLIVAIWVCCGVCGVVFIVYSESKMVIVCLITMFFAMMLLMGTLYVHMFLFARLHVKRIAALPPADGVAPQQHSCMKGAVTITILLGVFIFCWAPFFLHLVLIITCPTNPYCICYTAHFNTYLVLIMCNSVIDPLIYAFRSLELRNTFREILCGCNGMNLG	Literature-reported	Emerging drugs for obesity: linking novel biological mechanisms to pharmaceutical pipelines. Expert Opin Emerg Drugs. 2005 Aug;10(3):643-60.	2.1	PF00001	.	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events	.	P41968
TTD0CIQ	Melanocortin receptor 4 (MC4R)	P32245	MC4R_HUMAN	GPCR rhodopsin	MC4-R	MC4R	"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."	.	2IQW; 2IQV; 2IQU; 2IQS; 2IQR	MVNSTHRGMHTSLHLWNRSSYRLHSNASESLGKGYSDGGCYEQLFVSPEVFVTLGVISLLENILVIVAIAKNKNLHSPMYFFICSLAVADMLVSVSNGSETIVITLLNSTDTDAQSFTVNIDNVIDSVICSSLLASICSLLSIAVDRYFTIFYALQYHNIMTVKRVGIIISCIWAACTVSGILFIIYSDSSAVIICLITMFFTMLALMASLYVHMFLMARLHIKRIAVLPGTGAIRQGANMKGAITLTILIGVFVVCWAPFFLHLIFYISCPQNPYCVCFMSHFNLYLILIMCNSIIDPLIYALRSQELRKTFKEIICCYPLGGLCDLSSRY	Successful	Emerging drugs for obesity: linking novel biological mechanisms to pharmaceutical pipelines. Expert Opin Emerg Drugs. 2005 Aug;10(3):643-60.	34	PF00001	.	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.2.3	The G-protein-coupled receptor (GPCR) Family	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events	.	P32245
TT6QAJ3	Melanocortin receptor 5 (MC5R)	P33032	MC5R_HUMAN	GPCR rhodopsin	MC5-R; MC2; MC-2	MC5R	"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."	.	.	MNSSFHLHFLDLNLNATEGNLSGPNVKNKSSPCEDMGIAVEVFLTLGVISLLENILVIGAIVKNKNLHSPMYFFVCSLAVADMLVSMSSAWETITIYLLNNKHLVIADAFVRHIDNVFDSMICISVVASMCSLLAIAVDRYVTIFYALRYHHIMTARRSGAIIAGIWAFCTGCGIVFILYSESTYVILCLISMFFAMLFLLVSLYIHMFLLARTHVKRIAALPGASSARQRTSMQGAVTVTMLLGVFTVCWAPFFLHLTLMLSCPQNLYCSRFMSHFNMYLILIMCNSVMDPLIYAFRSQEMRKTFKEIICCRGFRIACSFPRRD	Clinical trial	"Clinical pipeline report, company report or official report of Avarx."	21	PF00001	.	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-418555:G alpha (s) signalling events	.	P33032
TTHRE05	Cell surface glycoprotein MUC18 (MCAM)	P43121	MUC18_HUMAN	.	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	MCAM	"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."	.	.	MGLPRLVCAFLLAACCCCPRVAGVPGEAEQPAPELVEVEVGSTALLKCGLSQSQGNLSHVDWFSVHKEKRTLIFRVRQGQGQSEPGEYEQRLSLQDRGATLALTQVTPQDERIFLCQGKRPRSQEYRIQLRVYKAPEEPNIQVNPLGIPVNSKEPEEVATCVGRNGYPIPQVIWYKNGRPLKEEKNRVHIQSSQTVESSGLYTLQSILKAQLVKEDKDAQFYCELNYRLPSGNHMKESREVTVPVFYPTEKVWLEVEPVGMLKEGDRVEIRCLADGNPPPHFSISKQNPSTREAEEETTNDNGVLVLEPARKEHSGRYECQGLDLDTMISLLSEPQELLVNYVSDVRVSPAAPERQEGSSLTLTCEAESSQDLEFQWLREETGQVLERGPVLQLHDLKREAGGGYRCVASVPSIPGLNRTQLVNVAIFGPPWMAFKERKVWVKENMVLNLSCEASGHPRPTISWNVNGTASEQDQDPQRVLSTLNVLVTPELLETGVECTASNDLGKNTSILFLELVNLTTLTPDSNTTTGLSTSTASPHTRANSTSTERKLPEPESRGVVIVAVIVCILVLAVLGAVLYFLYKKGKLPCRRSGKQEITLPPSRKSELVVEVKSDKLPEEMGLLQGSSGDKRAPGDQGEKYIDLRH	Literature-reported	"A novel anti-CD146 monoclonal antibody, AA98, inhibits angiogenesis and tumor growth. Blood. 2003 Jul 1;102(1):184-91."	.	.	Transmembrane protein	.	.	.	CD80-like C2-set immunoglobulin domain ; Immunoglobulin domain; Immunoglobulin V-set domain	PF08205; PF00047; PF07686	PF08205; C2-set_2; PF00047; ig; PF07686; V-set	.	.	.	R-HSA-8980692: RHOA GTPase cycle; R-HSA-9013026: RHOB GTPase cycle; R-HSA-9013106: RHOC GTPase cycle; R-HSA-9013149: RAC1 GTPase cycle; R-HSA-9013404: RAC2 GTPase cycle; R-HSA-9013405: RHOD GTPase cycle; R-HSA-9013408: RHOG GTPase cycle; R-HSA-9013423: RAC3 GTPase cycle; R-HSA-9035034: RHOF GTPase cycle	.	P43121
TTX4RTB	Melanin-concentrating hormone receptor 1 (MCHR1)	Q99705	MCHR1_HUMAN	GPCR rhodopsin	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	MCHR1	"Receptor for melanin-concentrating hormone, coupled to both G proteins that inhibit adenylyl cyclase and G proteins that activate phosphoinositide hydrolysis."	.	.	MSVGAMKKGVGRAVGLGGGSGCQATEEDPLPNCGACAPGQGGRRWRLPQPAWVEGSSARLWEQATGTGWMDLEASLLPTGPNASNTSDGPDNLTSAGSPPRTGSISYINIIMPSVFGTICLLGIIGNSTVIFAVVKKSKLHWCNNVPDIFIINLSVVDLLFLLGMPFMIHQLMGNGVWHFGETMCTLITAMDANSQFTSTYILTAMAIDRYLATVHPISSTKFRKPSVATLVICLLWALSFISITPVWLYARLIPFPGGAVGCGIRLPNPDTDLYWFTLYQFFLAFALPFVVITAAYVRILQRMTSSVAPASQRSIRLRTKRVTRTAIAICLVFFVCWAPYYVLQLTQLSISRPTLTFVYLYNAAISLGYANSCLNPFVYIVLCETFRKRLVLSVKPAAQGQLRAVSNAQTADEERTESKGT	Clinical trial	Phase I clinical trial of AZD1979 for treating obesity. AstraZeneca plc	17	PF00001	GPCR rhodopsin	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.13.6	The G-protein-coupled receptor (GPCR) Family	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events	.	Q99705
TTS17MG	Melanin-concentrating hormone receptor 2 (MCHR2)	Q969V1	MCHR2_HUMAN	GPCR rhodopsin	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	MCHR2	"Receptor for melanin-concentrating hormone, coupled to G proteins that activate phosphoinositide hydrolysis."	.	.	MNPFHASCWNTSAELLNKSWNKEFAYQTASVVDTVILPSMIGIICSTGLVGNILIVFTIIRSRKKTVPDIYICNLAVADLVHIVGMPFLIHQWARGGEWVFGGPLCTIITSLDTCNQFACSAIMTVMSVDRYFALVQPFRLTRWRTRYKTIRINLGLWAASFILALPVWVYSKVIKFKDGVESCAFDLTSPDDVLWYTLYLTITTFFFPLPLILVCYILILCYTWEMYQQNKDARCCNPSVPKQRVMKLTKMVLVLVVVFILSAAPYHVIQLVNLQMEQPTLAFYVGYYLSICLSYASSSINPFLYILLSGNFQKRLPQIQRRATEKEINNMGNTLKSHF	Literature-reported	"Identification and characterization of a second melanin-concentrating hormone receptor, MCH-2R. Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7564-9."	0	PF00001	.	.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04080: Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events; R-HSA-418594:G alpha (i) signalling events	.	Q969V1
TTL53M6	Induced myeloid leukemia cell differentiation protein Mcl-1 (MCL1)	Q07820	MCL1_HUMAN	B-cell lymphoma Bcl-2	mcl1/EAT; Bcl2-L-3; Bcl-2-related protein EAT/mcl1; Bcl-2-like protein 3; BCL2L3	MCL1	"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."	.	6OVC; 6OQN; 6OQD; 6OQC; 6OQB	MFGLKRNAVIGLNLYCGGAGLGAGSGGATRPGGRLLATEKEASARREIGGGEAGAVIGGSAGASPPSTLTPDSRRVARPPPIGAEVPDVTATPARLLFFAPTRRAAPLEEMEAPAADAIMSPEEELDGYEPEPLGKRPAVLPLLELVGESGNNTSTDGSLPSTPPPAEEEEDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGGIRNVLLAFAGVAGVGAGLAYLIR	Clinical trial	"Phase II study of obatoclax mesylate (GX15-070), a small-molecule BCL-2 family antagonist, for patients with myelofibrosis. Clin Lymphoma Myeloma Leuk. 2010 Aug;10(4):285-9."	21	TC=1.A.21	BCL2 family	Bcl-2 family.	.	.	"Apoptosis regulator proteins, Bcl-2 family"	PF00452	PF00452; Bcl-2	.	.	hsa04151:PI3K-Akt signaling pathway; hsa05206:MicroRNAs in cancer	R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling	.	Q07820
TTN6ORK	Mcl-1 messenger RNA (MCL-1 mRNA)	Q07820	MCL1_HUMAN	mRNA target	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)	MCL1	"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."	.	6OVC; 6OQN; 6OQD; 6OQC; 6OQB	MFGLKRNAVIGLNLYCGGAGLGAGSGGATRPGGRLLATEKEASARREIGGGEAGAVIGGSAGASPPSTLTPDSRRVARPPPIGAEVPDVTATPARLLFFAPTRRAAPLEEMEAPAADAIMSPEEELDGYEPEPLGKRPAVLPLLELVGESGNNTSTDGSLPSTPPPAEEEEDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGGIRNVLLAFAGVAGVGAGLAYLIR	Successful	Design and development of antisense drugs. Expert Opin. Drug Discov. 2008 3(10):1189-1207.	34	mRNA	mRNA target	.	.	.	"Apoptosis regulator proteins, Bcl-2 family"	PF00452	PF00452; Bcl-2	.	.	hsa04151: PI3K-Akt signaling pathway; hsa04210: Apoptosis; hsa04630: JAK-STAT signaling pathway; hsa05206: MicroRNAs in cancer	R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling	.	Q07820
TTQGKSD	DNA replication licensing factor MCM6 (MCM6)	Q14566	MCM6_HUMAN	Acid anhydride hydrolase	p105MCM; Minichromosome maintenanceprotein 6	MCM6	"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."	EC 3.6.4.12	2LE8; 2KLQ	MDLAAAAEPGAGSQHLEVRDEVAEKCQKLFLDFLEEFQSSDGEIKYLQLAEELIRPERNTLVVSFVDLEQFNQQLSTTIQEEFYRVYPYLCRALKTFVKDRKEIPLAKDFYVAFQDLPTRHKIRELTSSRIGLLTRISGQVVRTHPVHPELVSGTFLCLDCQTVIRDVEQQFKYTQPNICRNPVCANRRRFLLDTNKSRFVDFQKVRIQETQAELPRGSIPRSLEVILRAEAVESAQAGDKCDFTGTLIVVPDVSKLSTPGARAETNSRVSGVDGYETEGIRGLRALGVRDLSYRLVFLACCVAPTNPRFGGKELRDEEQTAESIKNQMTVKEWEKVFEMSQDKNLYHNLCTSLFPTIHGNDEVKRGVLLMLFGGVPKTTGEGTSLRGDINVCIVGDPSTAKSQFLKHVEEFSPRAVYTSGKASSAAGLTAAVVRDEESHEFVIEAGALMLADNGVCCIDEFDKMDVRDQVAIHEAMEQQTISITKAGVKATLNARTSILAAANPISGHYDRSKSLKQNINLSAPIMSRFDLFFILVDECNEVTDYAIARRIVDLHSRIEESIDRVYSLDDIRRYLLFARQFKPKISKESEDFIVEQYKHLRQRDGSGVTKSSWRITVRQLESMIRLSEAMARMHCCDEVQPKHVKEAFRLLNKSIIRVETPDVNLDQEEEIQMEVDEGAGGINGHADSPAPVNGINGYNEDINQESAPKASLRLGFSEYCRISNLIVLHLRKVEEEEDESALKRSELVNWYLKEIESEIDSEEELINKKRIIEKVIHRLTHYDHVLIELTQAGLKGSTEGSESYEEDPYLVVNPNYLLED	Literature-reported	Atorvastatin inhibits expression of minichromosome maintenance proteins in vascular smooth muscle cells. Eur J Pharmacol. 2003 Feb 21;462(1-3):15-23.	.	EC:3.6	Acid anhydrides hydrolase	MCM family.	3.6.4.12	Acting on acid anhydrides	MCM P-loop domain; MCM6 C-terminal winged-helix domain; MCM AAA-lid domain; MCM N-terminal domain; MCM OB domain	PF00493; PF18263; PF17855; PF14551; PF17207	PF00493; MCM; PF18263; MCM6_C; PF17855; MCM_lid; PF14551; MCM_N; PF17207; MCM_OB	.	.	hsa03030: DNA replication; hsa04110: Cell cycle	R-HSA-176187: Activation of ATR in response to replication stress; R-HSA-176974: Unwinding of DNA; R-HSA-68867: Assembly of the pre-replicative complex; R-HSA-68949: Orc1 removal from chromatin; R-HSA-68962: Activation of the pre-replicative complex; R-HSA-69052: Switching of origins to a post-replicative state	.	Q14566
TT1RM3F	DNA replication licensing factor MCM7 (MCM7)	P33993	MCM7_HUMAN	Acid anhydride hydrolase	P1.1-MCM3; Minichromosome maintenanceprotein 7; MCM2; CDC47 homolog; CDC47	MCM7	"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."	EC 3.6.4.12	.	MALKDYALEKEKVKKFLQEFYQDDELGKKQFKYGNQLVRLAHREQVALYVDLDDVAEDDPELVDSICENARRYAKLFADAVQELLPQYKEREVVNKDVLDVYIEHRLMMEQRSRDPGMVRSPQNQYPAELMRRFELYFQGPSSNKPRVIREVRADSVGKLVTVRGIVTRVSEVKPKMVVATYTCDQCGAETYQPIQSPTFMPLIMCPSQECQTNRSGGRLYLQTRGSRFIKFQEMKMQEHSDQVPVGNIPRSITVLVEGENTRIAQPGDHVSVTGIFLPILRTGFRQVVQGLLSETYLEAHRIVKMNKSEDDESGAGELTREELRQIAEEDFYEKLAASIAPEIYGHEDVKKALLLLLVGGVDQSPRGMKIRGNINICLMGDPGVAKSQLLSYIDRLAPRSQYTTGRGSSGVGLTAAVLRDSVSGELTLEGGALVLADQGVCCIDEFDKMAEADRTAIHEVMEQQTISIAKAGILTTLNARCSILAAANPAYGRYNPRRSLEQNIQLPAALLSRFDLLWLIQDRPDRDNDLRLAQHITYVHQHSRQPPSQFEPLDMKLMRRYIAMCREKQPMVPESLADYITAAYVEMRREAWASKDATYTSARTLLAILRLSTALARLRMVDVVEKEDVNEAIRLMEMSKDSLLGDKGQTARTQRPADVIFATVRELVSGGRSVRFSEAEQRCVSRGFTPAQFQAALDEYEELNVWQVNASRTRITFV	Literature-reported	Atorvastatin inhibits expression of minichromosome maintenance proteins in vascular smooth muscle cells. Eur J Pharmacol. 2003 Feb 21;462(1-3):15-23.	.	EC:3.6	Acid anhydrides hydrolase	MCM family.	3.6.4.12	Acting on acid anhydrides	MCM P-loop domain; MCM AAA-lid domain; MCM N-terminal domain; MCM OB domain	PF00493; PF17855; PF14551; PF17207	PF00493; MCM; PF17855; MCM_lid; PF14551; MCM_N; PF17207; MCM_OB	.	.	hsa03030: DNA replication; hsa04110: Cell cycle	R-HSA-176187: Activation of ATR in response to replication stress; R-HSA-176974: Unwinding of DNA; R-HSA-68867: Assembly of the pre-replicative complex; R-HSA-68949: Orc1 removal from chromatin; R-HSA-68962: Activation of the pre-replicative complex; R-HSA-69052: Switching of origins to a post-replicative state	.	P33993
TT9XBVO	Mucolipin-1 (TRPML1)	Q9GZU1	MCLN1_HUMAN	.	Transient receptor potential channel mucolipin 1; TRPML1; Mucolipidin; MSTP080; ML4; ML1; MG-2	MCOLN1	"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)."	.	6E7Z; 6E7Y; 6E7P; 5WJ9; 5WJ5	MTAPAGPRGSETERLLTPNPGYGTQAGPSPAPPTPPEEEDLRRRLKYFFMSPCDKFRAKGRKPCKLMLQVVKILVVTVQLILFGLSNQLAVTFREENTIAFRHLFLLGYSDGADDTFAAYTREQLYQAIFHAVDQYLALPDVSLGRYAYVRGGGDPWTNGSGLALCQRYYHRGHVDPANDTFDIDPMVVTDCIQVDPPERPPPPPSDDLTLLESSSSYKNLTLKFHKLVNVTIHFRLKTINLQSLINNEIPDCYTFSVLITFDNKAHSGRIPISLETQAHIQECKHPSVFQHGDNSFRLLFDVVVILTCSLSFLLCARSLLRGFLLQNEFVGFMWRQRGRVISLWERLEFVNGWYILLVTSDVLTISGTIMKIGIEAKNLASYDVCSILLGTSTLLVWVGVIRYLTFFHNYNILIATLRVALPSVMRFCCCVAVIYLGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVTFAAMQAQQGRSSLVWLFSQLYLYSFISLFIYMVLSLFIALITGAYDTIKHPGGAGAEESELQAYIAQCQDSPTSGKFRRGSGSACSLLCCCGRDPSEEHSLLVN	Preclinical	"PI(3,5)P(2) controls membrane trafficking by direct activation of mucolipin Ca(2+) release channels in the endolysosome. Nat Commun. 2010 Jul 13;1:38."	0	.	.	.	.	.	.	.	.	.	.	hsa04020: Calcium signaling pathway; hsa04142: Lysosome	R-HSA-3295583: TRP channels; R-HSA-917977: Transferrin endocytosis and recycling	.	Q9GZU1
TT0NLAQ	Mucolipin-3 (TRPML3)	Q8TDD5	MCLN3_HUMAN	.	Transient receptor potential channel mucolipin 3; TRPML3	MCOLN3	"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."	.	6AYG; 6AYF; 6AYE	MADPEVVVSSCSSHEEENRCNFNQQTSPSEELLLEDQMRRKLKFFFMNPCEKFWARGRKPWKLAIQILKIAMVTIQLVLFGLSNQMVVAFKEENTIAFKHLFLKGYMDRMDDTYAVYTQSDVYDQLIFAVNQYLQLYNVSVGNHAYENKGTKQSAMAICQHFYKRGNIYPGNDTFDIDPEIETECFFVEPDEPFHIGTPAENKLNLTLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIRECKDWHVSGSIQKNTHYMMIFDAFVILTCLVSLILCIRSVIRGLQLQQEFVNFFLLHYKKEVSVSDQMEFVNGWYIMIIISDILTIIGSILKMEIQAKSLTSYDVCSILLGTSTMLVWLGVIRYLGFFAKYNLLILTLQAALPNVIRFCCCAAMIYLGYCFCGWIVLGPYHDKFRSLNMVSECLFSLINGDDMFATFAKMQQKSYLVWLFSRIYLYSFISLFIYMILSLFIALITDTYETIKQYQQDGFPETELRTFISECKDLPNSGKYRLEDDPPVSLFCCCKK	Literature-reported	Small molecule activators of TRPML3. Chem Biol. 2010 Feb 26;17(2):135-48.	0	.	.	.	.	.	.	.	.	.	.	hsa04020: Calcium signaling pathway	R-HSA-3295583: TRP channels	.	Q8TDD5
TTLOHU4	Mycobacterium Decaprenylphosphoryl-beta-D-ribose oxidase (McyB dprE1)	P9WJF1	DPRE1_MYCTU	.	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	McyB dprE1	"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."	EC 1.1.98.3	6HFW; 6HFV; 6HF3; 6HF0; 6HEZ	MLSVGATTTATRLTGWGRTAPSVANVLRTPDAEMIVKAVARVAESGGGRGAIARGLGRSYGDNAQNGGGLVIDMTPLNTIHSIDADTKLVDIDAGVNLDQLMKAALPFGLWVPVLPGTRQVTVGGAIACDIHGKNHHSAGSFGNHVRSMDLLTADGEIRHLTPTGEDAELFWATVGGNGLTGIIMRATIEMTPTSTAYFIADGDVTASLDETIALHSDGSEARYTYSSAWFDAISAPPKLGRAAVSRGRLATVEQLPAKLRSEPLKFDAPQLLTLPDVFPNGLANKYTFGPIGELWYRKSGTYRGKVQNLTQFYHPLDMFGEWNRAYGPAGFLQYQFVIPTEAVDEFKKIIGVIQASGHYSFLNVFKLFGPRNQAPLSFPIPGWNICVDFPIKDGLGKFVSELDRRVLEFGGRLYTAKDSRTTAETFHAMYPRVDEWISVRRKVDPLRVFASDMARRLELL	Clinical trial	Decaprenyl-phosphoryl-ribose 2'-epimerase (DprE1): challenging target for antitubercular drug discovery. Chem Cent J. 2018 Jun 23;12(1):72.	.	.	.	.	.	.	.	.	.	.	.	.	.	MetaCyc:G185E-8086-MON	P9WJF1
TTV8UE7	Midgestation and kidney protein (Midkine)	P21741	MK_HUMAN	.	Neurite outgrowth-promoting protein; Neurite outgrowth-promoting factor 2; NEGF2; MK1; MK; Amphiregulin-associated protein; ARAP	MDK	"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."	.	1MKN; 1MKC	MQHRGFLLLTLLALLALTSAVAKKKDKVKKGGPGSECAEWAWGPCTPSSKDCGVGFREGTCGAQTQRIRCRVPCNWKKEFGADCKYKFENWGACDGGTGTKVRQGTLKKARYNAQCQETIRVTKPCTPKTKAKAKAKKGKGKD	Literature-reported	Recent progress of midkine research on cancer. Nihon Rinsho. 2000 Jun;58(6):1337-47.	.	.	.	pleiotrophin family.	.	.	"PTN/MK heparin-binding protein family, C-terminal domain; PTN/MK heparin-binding protein family, N-terminal domain"	PF01091; PF05196	PF01091; PTN_MK_C; PF05196; PTN_MK_N	.	.	.	R-HSA-201556: Signaling by ALK; R-HSA-2979096: NOTCH2 Activation and Transmission of Signal to the Nucleus	.	P21741
TT9TE0O	Mdm2 messenger RNA (MDM2 mRNA)	Q00987	MDM2_HUMAN	mRNA target	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)	MDM2	"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."	EC 2.3.2.27	6Q9O; 6Q9L; 6Q9H; 6Q96; 6IM9	MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP	Literature-reported	"US patent application no. 6,238,921, Antisense oligonucleotide modulation of human mdm2 expression."	0	mRNA	mRNA target	.	.	.	SWIB/MDM2 domain; Zn-finger in Ran binding protein and others	PF02201; PF00641	PF02201; SWIB; PF00641; zf-RanBP	.	.	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	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	.	Q00987
TT08GJW	Ubiquitin-protein ligase E3 Mdm2 (MDM2)	Q00987	MDM2_HUMAN	Acyltransferase	RING-type E3 ubiquitin transferase Mdm2; P53-binding protein Mdm2; Oncoprotein Mdm2; MDM2 protein; Hdm2; E3 ubiquitin-protein ligase Mdm2; Double minute 2 protein	MDM2	"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."	EC 2.3.2.27	6Q9O; 6Q9L; 6Q9H; 6Q96; 6IM9	MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP	Clinical trial	Pre-clinical evaluation of the MDM2-p53 antagonist RG7388 alone and in combination with chemotherapy in neuroblastoma. Oncotarget. 2015 Apr 30;6(12):10207-21.	21	EC:2.3	Peptide synthase	MDM2/MDM4 family.	2.3.2.27 	Acyltransferases	SWIB/MDM2 domain; Zn-finger in Ran binding protein and others	PF02201; PF00641	PF02201; SWIB; PF00641; zf-RanBP	.	.	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	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	.	Q00987
TT9OUDQ	p53-binding protein Mdm4 (MDM4)	O15151	MDM4_HUMAN	MDM2/MDM4 family	Protein Mdmx; Mdm2-like p53-binding protein; Double minute 4 protein	MDM4	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.	.	6Q9Y; 6Q9W; 6Q9U; 6Q9S; 6Q9Q	MTSFSTSAQCSTSDSACRISPGQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGELLGRQSFSVKDPSPLYDMLRKNLVTLATATTDAAQTLALAQDHSMDIPSQDQLKQSAEESSTSRKRTTEDDIPTLPTSEHKCIHSREDEDLIENLAQDETSRLDLGFEEWDVAGLPWWFLGNLRSNYTPRSNGSTDLQTNQDVGTAIVSDTTDDLWFLNESVSEQLGVGIKVEAADTEQTSEEVGKVSDKKVIEVGKNDDLEDSKSLSDDTDVEVTSEDEWQCTECKKFNSPSKRYCFRCWALRKDWYSDCSKLTHSLSTSDITAIPEKENEGNDVPDCRRTISAPVVRPKDAYIKKENSKLFDPCNSVEFLDLAHSSESQETISSMGEQLDNLSEQRTDTENMEDCQNLLKPCSLCEKRPRDGNIIHGRTGHLVTCFHCARRLKKAGASCPICKKEIQLVIKVFIA	Clinical trial	Anti-ageing pipeline starts to mature.Nat Rev Drug Discov. 2018 Sep;17(9):609-612.	17	.	.	.	.	.	.	.	.	.	.	hsa04115:p53 signaling pathway; hsa05206:MicroRNAs in cancer	R-HSA-2559580: Oxidative Stress Induced Senescence; R-HSA-2559585: Oncogene Induced Senescence; R-HSA-5689880: Ub-specific processing proteases; R-HSA-6804756: Regulation of TP53 Activity through Phosphorylation; R-HSA-6804757: Regulation of TP53 Degradation; R-HSA-6804760: Regulation of TP53 Activity through Methylation; R-HSA-69541: Stabilization of p53	.	O15151
TTTAU9R	Methyl cpg binding protein 2 (MECP2)	P51608	MECP2_HUMAN	.	MethylCpGbinding protein 2; Methyl-CpG-binding protein 2; MeCp2 protein; MeCp2; MeCp-2 protein	MECP2	"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."	.	6OGK; 6OGJ; 6C1Y; 5BT2; 3C2I	MVAGMLGLREEKSEDQDLQGLKDKPLKFKKVKKDKKEEKEGKHEPVQPSAHHSAEPAEAGKAETSEGSGSAPAVPEASASPKQRRSIIRDRGPMYDDPTLPEGWTRKLKQRKSGRSAGKYDVYLINPQGKAFRSKVELIAYFEKVGDTSLDPNDFDFTVTGRGSPSRREQKPPKKPKSPKAPGTGRGRGRPKGSGTTRPKAATSEGVQVKRVLEKSPGKLLVKMPFQTSPGGKAEGGGATTSTQVMVIKRPGRKRKAEADPQAIPKKRGRKPGSVVAAAAAEAKKKAVKESSIRSVQETVLPIKKRKTRETVSIEVKEVVKPLLVSTLGEKSGKGLKTCKSPGRKSKESSPKGRSSSASSPPKKEHHHHHHHSESPKAPVPLLPPLPPPPPEPESSEDPTSPPEPQDLSSSVCKEEKMPRGGSLESDGCPKEPAKTQPAVATAATAAEKYKHRGEGERKDIVSSSMPRPNREEPVDSRTPVTERVS	Literature-reported	"MECP2, a multi-talented modulator of chromatin architecture. Brief Funct Genomics. 2016 Nov;15(6):420-431."	.	.	.	.	.	.	Methyl-CpG binding domain	PF01429	PF01429; MBD	.	.	.	R-HSA-8986944: Transcriptional Regulation by MECP2; R-HSA-9022534: Loss of MECP2 binding ability to 5hmC-DNA; R-HSA-9022535: Loss of phosphorylation of MECP2 at T308; R-HSA-9022537: Loss of MECP2 binding ability to the NCoR/SMRT complex; R-HSA-9022538: Loss of MECP2 binding ability to 5mC-DNA; R-HSA-9022692: Regulation of MECP2 expression and activity; R-HSA-9022699: MECP2 regulates neuronal receptors and channels; R-HSA-9022702: MECP2 regulates transcription of neuronal ligands; R-HSA-9022707: MECP2 regulates transcription factors; R-HSA-9022927: MECP2 regulates transcription of genes involved in GABA signaling; R-HSA-9725371: Nuclear events stimulated by ALK signaling in cancer	.	P51608
TTBZOTY	Tyrosine-protein kinase MELK (MELK)	Q14680	MELK_HUMAN	.	pEg3 kinase; hPK38; hMELK; MELK	MELK	"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}."	EC 2.7.11.1	5TX3; 5TWZ; 5TWY; 5TWU; 5TWL	MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCGQASATPFTDIKSNNWSLEDVTASDKNYVAGLIDYDWCEDDLSTGAATPRTSQFTKYWTESNGVESKSLTPALCRTPANKLKNKENVYTPKSAVKNEEYFMFPEPKTPVNKNQHKREILTTPNRYTTPSKARNQCLKETPIKIPVNSTGTDKLMTGVISPERRCRSVELDLNQAHMEETPKRKGAKVFGSLERGLDKVITVLTRSKRKGSARDGPRRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV	Clinical trial	Development of an orally-administrative MELK-targeting inhibitor that suppresses the growth of various types of human cancer. Oncotarget. 2012 Dec;3(12):1629-40.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	Q14680
TT5MN2U	Maternal embryonic leucine zipper kinase (MELK)	Q14680	MELK_HUMAN	Protein kinase superfamily. CAMK Ser/Thr protein kinase family	Protein kinase PK38; Protein kinase Eg3	MELK	"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."	EC 2.7.11.1	5TX3; 5TWZ; 5TWY; 5TWU; 5TWL	MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKPKGNKDYHLQTCCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARGKPVRLRLSSFSCGQASATPFTDIKSNNWSLEDVTASDKNYVAGLIDYDWCEDDLSTGAATPRTSQFTKYWTESNGVESKSLTPALCRTPANKLKNKENVYTPKSAVKNEEYFMFPEPKTPVNKNQHKREILTTPNRYTTPSKARNQCLKETPIKIPVNSTGTDKLMTGVISPERRCRSVELDLNQAHMEETPKRKGAKVFGSLERGLDKVITVLTRSKRKGSARDGPRRLKLHYNVTTTRLVNPDQLLNEIMSILPKKHVDFVQKGYTLKCQTQSDFGKVTMQFELEVCQLQKPDVVGIRRQRLKGDAWVYKRLVEDILSSCKV	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	.	.	.	Q14680
TT8OBT3	Melanotransferrin (MELTF)	P08582	TRFM_HUMAN	.	Melanoma-associated antigen p97; DE   AltName: CD_antigen=CD228	MELTF	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.	.	.	MRGPSGALWLLLALRTVLGGMEVRWCATSDPEQHKCGNMSEAFREAGIQPSLLCVRGTSADHCVQLIAAQEADAITLDGGAIYEAGKEHGLKPVVGEVYDQEVGTSYYAVAVVRRSSHVTIDTLKGVKSCHTGINRTVGWNVPVGYLVESGRLSVMGCDVLKAVSDYFGGSCVPGAGETSYSESLCRLCRGDSSGEGVCDKSPLERYYDYSGAFRCLAEGAGDVAFVKHSTVLENTDGKTLPSWGQALLSQDFELLCRDGSRADVTEWRQCHLARVPAHAVVVRADTDGGLIFRLLNEGQRLFSHEGSSFQMFSSEAYGQKDLLFKDSTSELVPIATQTYEAWLGHEYLHAMKGLLCDPNRLPPYLRWCVLSTPEIQKCGDMAVAFRRQRLKPEIQCVSAKSPQHCMERIQAEQVDAVTLSGEDIYTAGKTYGLVPAAGEHYAPEDSSNSYYVVAVVRRDSSHAFTLDELRGKRSCHAGFGSPAGWDVPVGALIQRGFIRPKDCDVLTAVSEFFNASCVPVNNPKNYPSSLCALCVGDEQGRNKCVGNSQERYYGYRGAFRCLVENAGDVAFVRHTTVFDNTNGHNSEPWAAELRSEDYELLCPNGARAEVSQFAACNLAQIPPHAVMVRPDTNIFTVYGLLDKAQDLFGDDHNKNGFKMFDSSNYHGQDLLFKDATVRAVPVGEKTTYRGWLGLDYVAALEGMSSQQCSGAAAPAPGAPLLPLLLPALAARLLPPAL	Clinical trial	"Clinical pipeline report, company report or official report of Seagen."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-163125: Post-translational modification: synthesis of GPI-anchored proteins; R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation	.	P08582
TT0CZBQ	Menin-MLL1 interaction (MEN1-KMT2A PPI)	MEN1-KMT2A	MEN1_HUMAN-KMT2A_HUMAN	.	.	MEN1-KMT2A	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of Kura Oncology."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	O00255
TTYJOLE	MERS-CoV papain-like proteinase (PL-PRO)	K9N7C7 (854-2740)	R1AB_CVEMC (854-2740)	Coronaviruses polyprotein 1ab family	MERS-CoV PLpro; MERS-CoV Non-structural protein 3; MERS-CoV nsp3	MERS-CoV rep	"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."	EC 3.4.19.12	.	APVKKVAFGGDQVHEVAAVRSVTVEYNIHAVLDTLLASSSLRTFVVDKSLSIEEFADVVKEQVSDLLVKLLRGMPIPDFDLDDFIDAPCYCFNAEGDASWSSTMIFSLHPVECDEECSEVEASDLEEGESECISETSTEQVDVSHEISDDEWAAAVDEAFPLDEAEDVTESVQEEAQPVEVPVEDIAQVVIADTLQETPVVSDTVEVPPQVVKLPSEPQTIQPEVKEVAPVYEADTEQTQSVTVKPKRLRKKRNVDPLSNFEHKVITECVTIVLGDAIQVAKCYGESVLVNAANTHLKHGGGIAGAINAASKGAVQKESDEYILAKGPLQVGDSVLLQGHSLAKNILHVVGPDARAKQDVSLLSKCYKAMNAYPLVVTPLVSAGIFGVKPAVSFDYLIREAKTRVLVVVNSQDVYKSLTIVDIPQSLTFSYDGLRGAIRKAKDYGFTVFVCTDNSANTKVLRNKGVDYTKKFLTVDGVQYYCYTSKDTLDDILQQANKSVGIISMPLGYVSHGLDLIQAGSVVRRVNVPYVCLLANKEQEAILMSEDVKLNPSEDFIKHVRTNGGYNSWHLVEGELLVQDLRLNKLLHWSDQTICYKDSVFYVVKNSTAFPFETLSACRAYLDSRTTQQLTIEVLVTVDGVNFRTVVLNNKNTYRSQLGCVFFNGADISDTIPDEKQNGHSLYLADNLTADETKALKELYGPVDPTFLHRFYSLKAAVHKWKMVVCDKVRSLKLSDNNCYLNAVIMTLDLLKDIKFVIPALQHAFMKHKGGDSTDFIALIMAYGNCTFGAPDDASRLLHTVLAKAELCCSARMVWREWCNVCGIKDVVLQGLKACCYVGVQTVEDLRARMTYVCQCGGERHRQIVEHTTPWLLLSGTPNEKLVTTSTAPDFVAFNVFQGIETAVGHYVHARLKGGLILKFDSGTVSKTSDWKCKVTDVLFPGQKYSSDCNVVRYSLDGNFRTEVDPDLSAFYVKDGKYFTSEPPVTYSPATILAGSVYTNSCLVSSDGQPGGDAISLSFNNLLGFDSSKPVTKKYTYSFLPKEDGDVLLAEFDTYDPIYKNGAMYKGKPILWVNKASYDTNLNKFNRASLRQIFDVAPIELENKFTPLSVESTPVEPPTVDVVALQQEMTIVKCKGLNKPFVKDNVSFVADDSGTPVVEYLSKEDLHTLYVDPKYQVIVLKDNVLSSMLRLHTVESGDINVVAASGSLTRKVKLLFRASFYFKEFATRTFTATTAVGSCIKSVVRHLGVTKGILTGCFSFVKMLFMLPLAYFSDSKLGTTEVKVSALKTAGVVTGNVVKQCCTAAVDLSMDKLRRVDWKSTLRLLLMLCTTMVLLSSVYHLYVFNQVLSSDVMFEDAQGLKKFYKEVRAYLGISSACDGLASAYRANSFDVPTFCANRSAMCNWCLISQDSITHYPALKMVQTHLSHYVLNIDWLWFAFETGLAYMLYTSAFNWLLLAGTLHYFFAQTSIFVDWRSYNYAVSSAFWLFTHIPMAGLVRMYNLLACLWLLRKFYQHVINGCKDTACLLCYKRNRLTRVEASTVVCGGKRTFYITANGGISFCRRHNWNCVDCDTAGVGNTFICEEVANDLTTALRRPINATDRSHYYVDSVTVKETVVQFNYRRDGQPFYERFPLCAFTNLDKLKFKEVCKTTTGIPEYNFIIYDSSDRGQESLARSACVYYSQVLCKSILLVDSSLVTSVGDSSEIATKMFDSFVNSFVSLYNVTRDKLEKLISTARDGVRRGDNFHSVLTTFIDAARGPAGVESDVETNEIVDSVQYAHKHDIQITNESYNNYVPSYVKPDSVSTSDLGSLIDCNAASVNQIVLRNSNGACIWNAAAYMKLSDALKRQIRIACRKCNLAFRLTTSKLRANDNILSVRFTANKIVGG	.	Thiopurine analogs and mycophenolic acid synergistically inhibit the papain-like protease of Middle East respiratory syndrome coronavirus. Antiviral Res. 2015 Mar;115:9-16.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTY732E	MERS-CoV helicase (Hel)	K9N7C7 (5311-5908)	R1AB_CVEMC (5311-5908)	Coronaviruses polyprotein 1ab family	MERS-CoV Helicase; MERS-CoV Hel	MERS-CoV rep	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.	EC 3.6.4.12	.	AVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPHKMVLSVSPYVCNAPGCGVSDVTKLYLGGMSYFCVDHRPVCSFPLCANGLVFGLYKNMCTGSPSIVEFNRLATCDWTESGDYTLANTTTEPLKLFAAETLRATEEASKQSYAIATIKEIVGERQLLLVWEAGKSKPPLNRNYVFTGYHITKNSKVQLGEYIFERIDYSDAVSYKSSTTYKLTVGDIFVLTSHSVATLTAPTIVNQERYVKITGLYPTITVPEEFASHVANFQKSGYSKYVTVQGPPGTGKSHFAIGLAIYYPTARVVYTACSHAAVDALCEKAFKYLNIAKCSRIIPAKARVECYDRFKVNETNSQYLFSTINALPETSADILVVDEVSMCTNYDLSIINARIKAKHIVYVGDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLSMCYRCPKEIVSTVSALVYNNKLLAKKELSGQCFKILYKGNVTHDASSAINRPQLTFVKNFITANPAWSKAVFISPYNSQNAVARSMLGLTTQTVDSSQGSEYQYVIFCQTADTAHANNINRFNVAITRAQKGILCVMTSQALFESLEFTELSFTNYKLQ	.	"Design, synthesis and molecular docking of novel triazole derivatives as potential CoV helicase inhibitors. Acta Pharm. 2020 Jun 1;70(2):145-159."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOA6YT	MERS-CoV RNA-directed RNA polymerase (RdRp)	K9N7C7 (4378-5310)	R1AB_CVEMC (4378-5310)	Coronaviruses polyprotein 1ab family	MERS-CoV RNA-directed RNA polymerase; MERS-CoV Pol; MERS-CoV RdRp	MERS-CoV rep	Responsible for replication and transcription of the viral RNA genome.	EC 2.7.7.48	.	SKDSNFLKRVRGSIVNARIEPCSSGLSTDVVFRAFDICNYKAKVAGIGKYYKTNTCRFVELDDQGHHLDSYFVVKRHTMENYELEKHCYDLLRDCDAVAPHDFFIFDVDKVKTPHIVRQRLTEYTMMDLVYALRHFDQNSEVLKAILVKYGCCDVTYFENKLWFDFVENPSVIGVYHKLGERVRQAILNTVKFCDHMVKAGLVGVLTLDNQDLNGKWYDFGDFVITQPGSGVAIVDSYYSYLMPVLSMTDCLAAETHRDCDFNKPLIEWPLTEYDFTDYKVQLFEKYFKYWDQTYHANCVNCTDDRCVLHCANFNVLFAMTMPKTCFGPIVRKIFVDGVPFVVSCGYHYKELGLVMNMDVSLHRHRLSLKELMMYAADPAMHIASSNAFLDLRTSCFSVAALTTGLTFQTVRPGNFNQDFYDFVVSKGFFKEGSSVTLKHFFFAQDGNAAITDYNYYSYNLPTMCDIKQMLFCMEVVNKYFEIYDGGCLNASEVVVNNLDKSAGHPFNKFGKARVYYESMSYQEQDELFAMTKRNVIPTMTQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAATRGATCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYPKCDRAMPNMCRIFASLILARKHGTCCTTRDRFYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNKIVDKEVKDMQFDLYVNVYRSTSPDPKFVDKYYAFLNKHFSMMILSDDGVVCYNSDYAAKGYIAGIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHEFCSQHTLYIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHEDIEYQNVFWVYLQYIEKLYKDLTGHMLDSYSVMLCGDNSAKFWEEAFYRDLYSSPTTLQ	.	Coronaviruses - drug discovery and therapeutic options. Nat Rev Drug Discov. 2016 May;15(5):327-47.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTWOH4Q	MERS-CoV 3C-like proteinase (3CLpro)	K9N7C7 (3248-3553)	R1AB_CVEMC (3248-3553)	Coronaviruses polyprotein 1ab family	MERS-CoV 3C-like proteinase; MERS-CoV 3CLp; MERS-CoV 3CL-PRO; MERS-CoV 3CLpro	MERS-CoV rep	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).	EC 3.4.22.-	.	SGLVKMSHPSGDVEACMVQVTCGSMTLNGLWLDNTVWCPRHVMCPADQLSDPNYDALLISMTNHSFSVQKHIGAPANLRVVGHAMQGTLLKLTVDVANPSTPAYTFTTVKPGAAFSVLACYNGRPTGTFTVVMRPNYTIKGSFLCGSCGSVGYTKEGSVINFCYMHQMELANGTHTGSAFDGTMYGAFMDKQVHQVQLTDKYCSVNVVAWLYAAILNGCAWFVKPNRTSVVSFNEWALANQFTEFVGTQSVDMLAVKTGVAIEQLLYAIQQLYTGFQGKQILGSTMLEDEFTPEDVNMQIMGVVMQ	.	Structure-guided Design of Potent and Permeable Inhibitors of MERS Coronavirus 3CL Protease That Utilize a Piperidine Moiety as a Novel Design Element Eur J Med Chem. 2018 Apr 25;150:334-346.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT854FJ	MERS-CoV spike glycoprotein S2' HR1 region (S S2'HR1)	A0A140AYZ5 (888-1353)	A0A140AYZ5_9BETC (888-1353)	Betacoronaviruses spike protein family.	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	MERS-CoV S	Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.	.	.	SAIEDLLFDKVTIADPGYMQGYDDCMQQGPASARDLICAQYVAGYKVLPPLMDVNMEAAYTSSLLGSIAGVGWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTTNEAFRKVQDAVNNNAQALSKLASELSNTFGAISASIGDIIQRLDVLEQDAQIDRLINGRLTTLNAFVAQQLVRSESAALSAQLAKDKVNECVKAQSKRSGFCGQGTHIVSFVVNAPNGLYFMHVGYYPSNHIEVVSAYGLCDAANPTNCIAPVNGYFIKTNNTRIVDEWSYTGSSFYAPEPITSLNTKYVAPQVTYQNISTNLPPPLLGNSTGIDFQDELDEFFKNVSTSIPNFGSLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKELGNYTYYNKWPWYIWLGFIAGLVALALCVFFILCCTGCGTNCMGKLKCNRCCDRYEEYDLEPHKVHVH	.	A pan-coronavirus fusion inhibitor targeting the HR1 domain of human coronavirus spike. Sci Adv. 2019 Apr 10;5(4):eaav4580.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJ4EIV	MERS-CoV spike glycoprotein S2 subunit (S S2)	A0A140AYZ5 (748-1353)	A0A140AYZ5_9BETC (748-1353)	Betacoronaviruses spike protein family	MERS-CoV S glycoprotein S2 subunit; MERS-CoV E2 S2 subunit; MERS-CoV Peplomer protein S2 subunit	MERS-CoV S	"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."	.	.	TPSTLTPRSVRSVPGEMRLASIAFNHPIQVDQLNSSYFKLSIPTNFSFGVTQEYIQTTIQKVTVDCKQYVCNGFQKCEQLLREYGQFCSKINQALHGANLRQDDSVRNLFASVKSSQSSPIIPGFGGDFNLTLLEPVSISTGSRSARSAIEDLLFDKVTIADPGYMQGYDDCMQQGPASARDLICAQYVAGYKVLPPLMDVNMEAAYTSSLLGSIAGVGWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTTNEAFRKVQDAVNNNAQALSKLASELSNTFGAISASIGDIIQRLDVLEQDAQIDRLINGRLTTLNAFVAQQLVRSESAALSAQLAKDKVNECVKAQSKRSGFCGQGTHIVSFVVNAPNGLYFMHVGYYPSNHIEVVSAYGLCDAANPTNCIAPVNGYFIKTNNTRIVDEWSYTGSSFYAPEPITSLNTKYVAPQVTYQNISTNLPPPLLGNSTGIDFQDELDEFFKNVSTSIPNFGSLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKELGNYTYYNKWPWYIWLGFIAGLVALALCVFFILCCTGCGTNCMGKLKCNRCCDRYEEYDLEPHKVHVH	.	Structure-based discovery of Middle East respiratory syndrome coronavirus fusion inhibitor. Nat Commun. 2014;5:3067.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT85VHW	MERS-CoV spike glycoprotein (S)	A0A140AYZ5	A0A140AYZ5_9BETC	Betacoronaviruses spike protein family	MERS-CoV S glycoprotein; MERS-CoV E2; MERS-CoV Peplomer protein	MERS-CoV S	"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."	.	.	MIHSVFLLMFLLTPTESYVDVGPDSVKSACIEVDIQQTFFDKTWPRPIDVSKADGIIYPQGRTYSNITITYQGLFPYQGDHGDMYVYSAGHATGTTPQKLFVANYSQDVKQFANGFVVRIGAAANSTGTVIISPSTSATIRKIYPAFMLGSSVGNFSDGKMGRFFNHTLVLLPDGCGTLLRAFYCILEPRSGNHCPAGNSYTSFATYHTPATDCSDGNYNRNASLNSFKEYFNLRNCTFMYTYNITEDEILEWFGITQTAQGVHLFSSRYVDLYGGNMFQFATLPVYDTIKYYSIIPHSIRSIQSDRKAWAAFYVYKLQPLTFLLDFSVDGYIRRAIDCGFNDLSQLHCSYESFDVESGVYSVSSFEAKPSGSVVEQAEGVECDFSPLLSGTPPQVYNFKRLVFTNCNYNLTKLLSLFSVNDFTCSQISPAAIASNCYSSLILDYFSYPLSMKSDLSVSSAGPISQFNYKQSFSNPTCLILATVPHNLTTITKPLKYSYINKCSRLLSDDRTEVPQLVNANQYSPCVSTVPSTVWEDGDYYRKQLSPLEGGGWLVASGSTVAMTEQLQMGFGITVQYGTDTNSVCPKLEFANDTKIASQLGNCVEYSLYGVSGRGVFQNCTAVGVRQQRFVYDAYQNLVGYYSDDGNYYCLRACVSVPVSVIYDKETKTHATLFGSVACEHISSTMSQYSRSTRSMLKRRDSTYGPLQTPVGCVLGLVNSSLFVEDCKLPLGQSLCALPDTPSTLTPRSVRSVPGEMRLASIAFNHPIQVDQLNSSYFKLSIPTNFSFGVTQEYIQTTIQKVTVDCKQYVCNGFQKCEQLLREYGQFCSKINQALHGANLRQDDSVRNLFASVKSSQSSPIIPGFGGDFNLTLLEPVSISTGSRSARSAIEDLLFDKVTIADPGYMQGYDDCMQQGPASARDLICAQYVAGYKVLPPLMDVNMEAAYTSSLLGSIAGVGWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTTNEAFRKVQDAVNNNAQALSKLASELSNTFGAISASIGDIIQRLDVLEQDAQIDRLINGRLTTLNAFVAQQLVRSESAALSAQLAKDKVNECVKAQSKRSGFCGQGTHIVSFVVNAPNGLYFMHVGYYPSNHIEVVSAYGLCDAANPTNCIAPVNGYFIKTNNTRIVDEWSYTGSSFYAPEPITSLNTKYVAPQVTYQNISTNLPPPLLGNSTGIDFQDELDEFFKNVSTSIPNFGSLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKELGNYTYYNKWPWYIWLGFIAGLVALALCVFFILCCTGCGTNCMGKLKCNRCCDRYEEYDLEPHKVHVH	.	Identification of Nafamostat as a Potent Inhibitor of Middle East Respiratory Syndrome Coronavirus S Protein-Mediated Membrane Fusion Using the Split-Protein-Based Cell-Cell Fusion Assay Antimicrob Agents Chemother. 2016 Oct 21;60(11):6532-6539.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXMITO	SARS-CoV spike glycoprotein S2' HR1 region (S S2'HR1)	P59594 (798-1255)	SPIKE_CVHSA (798-1255)	Betacoronaviruses spike protein family.	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	MERS-CoV S	Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.	.	.	SFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSC	.	A pan-coronavirus fusion inhibitor targeting the HR1 domain of human coronavirus spike. Sci Adv. 2019 Apr 10;5(4):eaav4580.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTO7LKR	Tyrosine-protein kinase Mer (MERTK)	Q12866	MERTK_HUMAN	Kinase	Receptor tyrosine kinase MerTK; Proto-oncogene c-Mer	MERTK	"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."	EC 2.7.10.1	5U6C; 5TD2; 5TC0; 5K0X; 5K0K	MGPAPLPLLLGLFLPALWRRAITEAREEAKPYPLFPGPFPGSLQTDHTPLLSLPHASGYQPALMFSPTQPGRPHTGNVAIPQVTSVESKPLPPLAFKHTVGHIILSEHKGVKFNCSISVPNIYQDTTISWWKDGKELLGAHHAITQFYPDDEVTAIIASFSITSVQRSDNGSYICKMKINNEEIVSDPIYIEVQGLPHFTKQPESMNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNEQPEKSPSVLTVPGLTEMAVFSCEAHNDKGLTVSKGVQINIKAIPSPPTEVSIRNSTAHSILISWVPGFDGYSPFRNCSIQVKEADPLSNGSVMIFNTSALPHLYQIKQLQALANYSIGVSCMNEIGWSAVSPWILASTTEGAPSVAPLNVTVFLNESSDNVDIRWMKPPTKQQDGELVGYRISHVWQSAGISKELLEEVGQNGSRARISVQVHNATCTVRIAAVTRGGVGPFSDPVKIFIPAHGWVDYAPSSTPAPGNADPVLIIFGCFCGFILIGLILYISLAIRKRVQETKFGNAFTEEDSELVVNYIAKKSFCRRAIELTLHSLGVSEELQNKLEDVVIDRNLLILGKILGEGEFGSVMEGNLKQEDGTSLKVAVKTMKLDNSSQREIEEFLSEAACMKDFSHPNVIRLLGVCIEMSSQGIPKPMVILPFMKYGDLHTYLLYSRLETGPKHIPLQTLLKFMVDIALGMEYLSNRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWAFGVTMWEIATRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDELYEIMYSCWRTDPLDRPTFSVLRLQLEKLLESLPDVRNQADVIYVNTQLLESSEGLAQGSTLAPLDLNIDPDSIIASCTPRAAISVVTAEVHDSKPHEGRYILNGGSEEWEDLTSAPSAAVTAEKNSVLPGERLVRNGVSWSHSSMLPLGSSLPDELLFADDSSEGSEVLM	Clinical trial	"MK-2461, a novel multitargeted kinase inhibitor, preferentially inhibits the activated c-Met receptor. Cancer Res. 2010 Feb 15;70(4):1524-33."	19	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family. AXL/UFO subfamily.	2.7.10.1	Transferring phosphorus-containing groups	Fibronectin type III domain; Immunoglobulin domain; Immunoglobulin domain; Protein tyrosine kinase	PF00041; PF00047; PF13895; PF07714	PF00041; fn3; PF00047; ig; PF13895; Ig_2; PF07714; Pkinase_Tyr	.	.	.	R-HSA-202733:Cell surface interactions at the vascular wall	.	Q12866
TTNDSF4	Proto-oncogene c-Met (MET)	P08581	MET_HUMAN	Kinase	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	MET	"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."	EC 2.7.10.1	6I04; 6GCU; 5YA5; 5UAF; 5UAD	MKAPAVLAPGILVLLFTLVQRSNGECKEALAKSEMNVNMKYQLPNFTAETPIQNVILHEHHIFLGATNYIYVLNEEDLQKVAEYKTGPVLEHPDCFPCQDCSSKANLSGGVWKDNINMALVVDTYYDDQLISCGSVNRGTCQRHVFPHNHTADIQSEVHCIFSPQIEEPSQCPDCVVSALGAKVLSSVKDRFINFFVGNTINSSYFPDHPLHSISVRRLKETKDGFMFLTDQSYIDVLPEFRDSYPIKYVHAFESNNFIYFLTVQRETLDAQTFHTRIIRFCSINSGLHSYMEMPLECILTEKRKKRSTKKEVFNILQAAYVSKPGAQLARQIGASLNDDILFGVFAQSKPDSAEPMDRSAMCAFPIKYVNDFFNKIVNKNNVRCLQHFYGPNHEHCFNRTLLRNSSGCEARRDEYRTEFTTALQRVDLFMGQFSEVLLTSISTFIKGDLTIANLGTSEGRFMQVVVSRSGPSTPHVNFLLDSHPVSPEVIVEHTLNQNGYTLVITGKKITKIPLNGLGCRHFQSCSQCLSAPPFVQCGWCHDKCVRSEECLSGTWTQQICLPAIYKVFPNSAPLEGGTRLTICGWDFGFRRNNKFDLKKTRVLLGNESCTLTLSESTMNTLKCTVGPAMNKHFNMSIIISNGHGTTQYSTFSYVDPVITSISPKYGPMAGGTLLTLTGNYLNSGNSRHISIGGKTCTLKSVSNSILECYTPAQTISTEFAVKLKIDLANRETSIFSYREDPIVYEIHPTKSFISGGSTITGVGKNLNSVSVPRMVINVHEAGRNFTVACQHRSNSEIICCTTPSLQQLNLQLPLKTKAFFMLDGILSKYFDLIYVHNPVFKPFEKPVMISMGNENVLEIKGNDIDPEAVKGEVLKVGNKSCENIHLHSEAVLCTVPNDLLKLNSELNIEWKQAISSTVLGKVIVQPDQNFTGLIAGVVSISTALLLLLGFFLWLKKRKQIKDLGSELVRYDARVHTPHLDRLVSARSVSPTTEMVSNESVDYRATFPEDQFPNSSQNGSCRQVQYPLTDMSPILTSGDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIGEHYVHVNATYVNVKCVAPYPSLLSSEDNADDEVDTRPASFWETS	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. 2015	34	EC:2.7	Kinase	protein kinase superfamily. Tyr protein kinase family.	2.7.10.1	Transferring phosphorus-containing groups	Protein tyrosine kinase; Plexin repeat; Sema domain; IPT/TIG domain	PF07714; PF01437; PF01403; PF01833	PF07714; Pkinase_Tyr; PF01437; PSI; PF01403; Sema; PF01833; TIG	.	.	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	R-HSA-416550:Sema4D mediated inhibition of cell attachment and migration	.	P08581
TT1L79K	Methionyl aminopeptidase 1 (METAP1)	P53582	MAP11_HUMAN	.	Peptidase M 1; Methionine aminopeptidase 1; MetAP 1; MAP 1; KIAA0094	METAP1	"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."	EC 3.4.11.18	5YR7; 5YR6; 5YR5; 5YR4; 5YKP	MAAVETRVCETDGCSSEAKLQCPTCIKLGIQGSYFCSQECFKGSWATHKLLHKKAKDEKAKREVSSWTVEGDINTDPWAGYRYTGKLRPHYPLMPTRPVPSYIQRPDYADHPLGMSESEQALKGTSQIKLLSSEDIEGMRLVCRLAREVLDVAAGMIKPGVTTEEIDHAVHLACIARNCYPSPLNYYNFPKSCCTSVNEVICHGIPDRRPLQEGDIVNVDITLYRNGYHGDLNETFFVGEVDDGARKLVQTTYECLMQAIDAVKPGVRYRELGNIIQKHAQANGFSVVRSYCGHGIHKLFHTAPNVPHYAKNKAVGVMKSGHVFTIEPMICEGGWQDETWPDGWTAVTRDGKRSAQFEHTLLVTDTGCEILTRRLDSARPHFMSQF	Literature-reported	Pyridinylquinazolines selectively inhibit human methionine aminopeptidase-1 in cells. J Med Chem. 2013 May 23;56(10):3996-4016.	0	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-2514859: Inactivation, recovery and regulation of the phototransduction cascade"	MetaCyc:HS08982-MON	P53582
TTZL0OI	Methionine aminopeptidase 2 (METAP2)	P50579	MAP2_HUMAN	Peptidase	Peptidase M 2; P67eIF2; P67; MetAP 2; METAP2; Initiation factor 2 associated 67 kDa glycoprotein; (MetAP)-2	METAP2	"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)."	EC 3.4.11.18	6QEJ; 6QEI; 6QEH; 6QEG; 6QEF	MAGVEEVAASGSHLNGDLDPDDREEGAASTAEEAAKKKRRKKKKSKGPSAAGEQEPDKESGASVDEVARQLERSALEDKERDEDDEDGDGDGDGATGKKKKKKKKKRGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY	Clinical trial	2011 Pipeline of Zafgen.	25	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-2514859:Inactivation, recovery and regulation of the phototransduction cascade"	MetaCyc:HS03371-MON	P50579
TTUPB12	Measles virus Fusion glycoprotein (MeV F)	Q786F3	FUS_MEASC	Paramyxoviruses fusion glycoprotein	Measles virus fusion protein; MV fusion protein; Fusion protein	MeV F	"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."	.	5YZD; 5YZC; 5YXW	MGLKVNVSAIFMAVLLTLQTPTGQIHWGNLSKIGVVGIGSASYKVMTRSSHQSLVIKLMPNITLLNNCTRVEIAEYRRLLRTVLEPIRDALNAMTQNIRPVQSVASSRRHKRFAGVVLAGAALGVATAAQITAGIALHQSMLNSQAIDNLRASLETTNQAIEAIRQAGQEMILAVQGVQDYINNELIPSMNQLSCDLIGQKLGLKLLRYYTEILSLFGPSLRDPISAEISIQALSYALGGDINKVLEKLGYSGGDLLGILESRGIKARITHVDTESYFIVLSIAYPTLSEIKGVIVHRLEGVSYNIGSQEWYTTVPKYVATQGYLISNFDESSCTFMPEGTVCSQNALYPMSPLLQECLRGSTKSCARTLVSGSFGNRFILSQGNLIANCASILCKCYTTGTIINQDPDKILTYIAADHCPVVEVNGVTIQVGSRRYPDAVYLHRIDLGPPISLERLDVGTNLGNAIAKLEDAKELLESSDQILRSMKGLSSTSIVYILIAVCLGGLIGIPALICCCRGRCNKKGEQVGMSRPGLKPDLTGTSKSYVRSL	Clinical trial	Emerging drugs for respiratory syncytial virus infection. Expert Opin Emerg Drugs. 2009 Jun;14(2):207-17.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT1GLAJ	Lactadherin (MFGE8)	Q08431	MFGM_HUMAN	Growth factor	Milk fat globule-EGF factor 8; MFGM; MFGE8; MFG-E8; Human milk fat globule membrane protein BA46; HMFG; Breast epithelial antigen BA46	MFGE8	Medin is the main constituent of aortic medial amyloid.	.	.	MPRPRLLAALCGALLCAPSLLVALDICSKNPCHNGGLCEEISQEVRGDVFPSYTCTCLKGYAGNHCETKCVEPLGLENGNIANSQIAASSVRVTFLGLQHWVPELARLNRAGMVNAWTPSSNDDNPWIQVNLLRRMWVTGVVTQGASRLASHEYLKAFKVAYSLNGHEFDFIHDVNKKHKEFVGNWNKNAVHVNLFETPVEAQYVRLYPTSCHTACTLRFELLGCELNGCANPLGLKNNSIPDKQITASSSYKTWGLHLFSWNPSYARLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQFVASYKVAYSNDSANWTEYQDPRTGSSKIFPGNWDNHSHKKNLFETPILARYVRILPVAWHNRIALRLELLGC	Literature-reported	Characterization of novel breast carcinoma-associated BA46-derived peptides in HLA-A2.1/D(b)-beta2m transgenic mice. J Clin Invest. 2002 Aug;110(4):453-62.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation; R-HSA-977225: Amyloid fiber formation	.	Q08431
TTXWASR	Intestinal maltase-glucoamylase (MGAM)	O43451	MGA_HUMAN	Glycosylase	MGAM	MGAM	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.	.	3TOP; 3TON; 3L4Z; 3L4Y; 3L4X	MARKKLKKFTTLEIVLSVLLLVLFIISIVLIVLLAKESLKSTAPDPGTTGTPDPGTTGTPDPGTTGTTHARTTGPPDPGTTGTTPVSAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGSNVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLLFADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNAMEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLPYDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTPLIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCKTLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEFNLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTLFFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMELPGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDNGETKDTVANKVYLLCEFSVTQNRLEVNISQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWSIKIRDEEKIDCYPDENGASAENCTARGCIWEASNSSGVPFCYFVNDLYSVSDVQYNSHGATADISLKSSVYANAFPSTPVNPLRLDVTYHKNEMLQFKIYDPNKNRYEVPVPLNIPSMPSSTPEGQLYDVLIKKNPFGIEIRRKSTGTIIWDSQLLGFTFSDMFIRISTRLPSKYLYGFGETEHRSYRRDLEWHTWGMFSRDQPPGYKKNSYGVHPYYMGLEEDGSAHGVLLLNSNAMDVTFQPLPALTYRTTGGVLDFYVFLGPTPELVTQQYTELIGRPVMVPYWSLGFQLCRYGYQNDSEIASLYDEMVAAQIPYDVQYSDIDYMERQLDFTLSPKFAGFPALINRMKADGMRVILILDPAISGNETQPYPAFTRGVEDDVFIKYPNDGDIVWGKVWPDFPDVVVNGSLDWDSQVELYRAYVAFPDFFRNSTAKWWKREIEELYNNPQNPERSLKFDGMWIDMNEPSSFVNGAVSPGCRDASLNHPPYMPHLESRDRGLSSKTLCMESQQILPDGSLVQHYNVHNLYGWSQTRPTYEAVQEVTGQRGVVITRSTFPSSGRWAGHWLGDNTAAWDQLKKSIIGMMEFSLFGISYTGADICGFFQDAEYEMCVRWMQLGAFYPFSRNHNTIGTRRQDPVSWDVAFVNISRTVLQTRYTLLPYLYTLMHKAHTEGVTVVRPLLHEFVSDQVTWDIDSQFLLGPAFLVSPVLERNARNVTAYFPRARWYDYYTGVDINARGEWKTLPAPLDHINLHVRGGYILPWQEPALNTHLSRQKFMGFKIALDDEGTAGGWLFWDDGQSIDTYGKGLYYLASFSASQNTMQSHIIFNNYITGTNPLKLGYIEIWGVGSVPVTSVSISVSGMVITPSFNNDPTTQVLSIDVTDRNISLHNFTSLTWISTL	Successful	Effects of changeover from voglibose to acarbose on postprandial triglycerides in type 2 diabetes mellitus patients. Adv Ther. 2009 Jun;26(6):660-6.	34	.	.	.	.	.	.	.	.	.	.	hsa00052:Galactose metabolism; hsa00500:Starch and sucrose metabolism; hsa01100:Metabolic pathways; hsa04973:Carbohydrate digestion and absorption	R-HSA-189085: Digestion of dietary carbohydrate; R-HSA-6798695: Neutrophil degranulation	.	O43451
TTYJRN5	N-acetylglucosaminyltransferase I (NAGAT1)	P26572	MGAT1_HUMAN	.	"N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I; MGAT; GlcNAc-T I; GNT-I; GLCT1; GGNT1; Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase"	MGAT1	Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.	EC 2.4.1.101	.	MLKKQSAGLVLWGAILFVAWNALLLLFFWTRPAPGRPPSVSALDGDPASLTREVIRLAQDAEVELERQRGLLQQIGDALSSQRGRVPTAAPPAQPRVPVTPAPAVIPILVIACDRSTVRRCLDKLLHYRPSAELFPIIVSQDCGHEETAQAIASYGSAVTHIRQPDLSSIAVPPDHRKFQGYYKIARHYRWALGQVFRQFRFPAAVVVEDDLEVAPDFFEYFRATYPLLKADPSLWCVSAWNDNGKEQMVDASRPELLYRTDFFPGLGWLLLAELWAELEPKWPKAFWDDWMRRPEQRQGRACIRPEISRTMTFGRKGVSHGQFFDQHLKFIKLNQQFVHFTQLDLSYLQREAYDRDFLARVYGAPQLQVEKVRTNDRKELGEVRVQYTGRDSFKAFAKALGVMDDLKSGVPRAGYRGIVTFQFRGRRVHLAPPLTWEGYDPSWN	Patented-recorded	N-acetylglucosaminyltransferase-I as a novel regulator of epithelial-mesenchymal transition. FASEB J. 2019 Feb;33(2):2823-2835.	.	.	.	.	.	.	.	.	.	.	.	hsa00510: N-Glycan biosynthesis; hsa00513: Various types of N-glycan biosynthesis; hsa01100: Metabolic pathways	R-HSA-964739: N-glycan trimming and elongation in the cis-Golgi; R-HSA-9683686: Maturation of spike protein; R-HSA-9694548: Maturation of spike protein	MetaCyc:HS05528-MON	P26572
TTJOW1I	Mannoside acetylglucosaminyltransferase 2 (MGAT2)	Q10469	MGAT2_HUMAN	Glycosyltransferases	"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"	MGAT2	"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."	EC 2.4.1.143	5VCS; 5VCR; 5VCM	MRFRIYKRKVLILTLVVAACGFVLWSSNGRQRKNEALAPPLLDAEPARGAGGRGGDHPSVAVGIRRVSNVSAASLVPAVPQPEADNLTLRYRSLVYQLNFDQTLRNVDKAGTWAPRELVLVVQVHNRPEYLRLLLDSLRKAQGIDNVLVIFSHDFWSTEINQLIAGVNFCPVLQVFFPFSIQLYPNEFPGSDPRDCPRDLPKNAALKLGCINAEYPDSFGHYREAKFSQTKHHWWWKLHFVWERVKILRDYAGLILFLEEDHYLAPDFYHVFKKMWKLKQQECPECDVLSLGTYSASRSFYGMADKVDVKTWKSTEHNMGLALTRNAYQKLIECTDTFCTYDDYNWDWTLQYLTVSCLPKFWKVLVPQIPRIFHAGDCGMHHKKTCRPSTQSAQIESLLNNNKQYMFPETLTISEKFTVVAISPPRKNGGWGDIRDHELCKSYRRLQ	Patented-recorded	Acyltransferase inhibitors: a patent review (2010-present).Expert Opin Ther Pat. 2015 Feb;25(2):145-58.	15.5	EC:2.4	Glycosyltransferase 16 (GT16) protein family	glycosyltransferase 16 (GT16) protein family.	2.4.1.143 	Glycosyltransferases	N-acetylglucosaminyltransferase II (MGAT2)	PF05060	PF05060; MGAT2	.	.	hsa00510:N-Glycan biosynthesis; hsa01100:Metabolic pathways	R-HSA-4793952: Defective MGAT2 causes CDG-2a; R-HSA-9694548: Maturation of spike protein; R-HSA-975578: Reactions specific to the complex N-glycan synthesis pathway	MetaCyc:HS09725-MON	Q10469
TT2I6UX	Beta-N-acetylhexosaminidase (OGA)	O60502	OGA_HUMAN	Glycosylase	OGA; Nuclear cytoplasmic OGlcNAcase and acetyltransferase; Meningiomaexpressed antigen 5; MGEA5; Histone acetyltransferase; Bifunctional protein NCOAT	MGEA5	"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}."	EC 3.2.1.169	6HKI; 5VVX; 5VVV; 5VVU; 5VVT	MVQKESQATLEERESELSSNPAASAGASLEPPAAPAPGEDNPAGAGGAAVAGAAGGARRFLCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEKLLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGVLTNPNCEFEANYVAIHTLATWYKSNMNGVRKDVVMTDSEDSTVSIQIKLENEGSDEDIETDVLYSPQMALKLALTEWLQEFGVPHQYSSRQVAHSGAKASVVDGTPLVAAPSLNATTVVTTVYQEPIMSQGAALSGEPTTLTKEEEKKQPDEEPMDMVVEKQEETDHKNDNQILSEIVEAKMAEELKPMDTDKESIAESKSPEMSMQEDCISDIAPMQTDEQTNKEQFVPGPNEKPLYTAEPVTLEDLQLLADLFYLPYEHGPKGAQMLREFQWLRANSSVVSVNCKGKDSEKIEEWRSRAAKFEEMCGLVMGMFTRLSNCANRTILYDMYSYVWDIKSIMSMVKSFVQWLGCRSHSSAQFLIGDQEPWAFRGGLAGEFQRLLPIDGANDLFFQPPPLTPTSKVYTIRPYFPKDEASVYKICREMYDDGVGLPFQSQPDLIGDKLVGGLLSLSLDYCFVLEDEDGICGYALGTVDVTPFIKKCKISWIPFMQEKYTKPNGDKELSEAEKIMLSFHEEQEVLPETFLANFPSLIKMDIHKKVTDPSVAKSMMACLLSSLKANGSRGAFCEVRPDDKRILEFYSKLGCFEIAKMEGFPKDVVILGRSL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	hsa04931: Insulin resistance	.	MetaCyc:HS03036-MON	O60502
TTZ963I	Monoglyceride lipase (MAGL)	Q99685	MGLL_HUMAN	Carboxylic ester hydrolase	Monoacylglycerol lipase; MGL; Lysophospholipaselike; Lysophospholipase-like; Lysophospholipase homolog; HUK5; HU-K5	MGLL	"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."	EC 3.1.1.23	6BQ0; 6AX1; 5ZUN; 4UUQ; 3PE6	MPEESSPRRTPQSIPYQDLPHLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTASPP	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	EC:3.1.1	Carboxylic ester hydrolase	AB hydrolase superfamily. Monoacylglycerol lipase family.	3.1.1.23 	Acting on ester bonds	"Serine aminopeptidase, S33"	PF12146	PF12146; Hydrolase_4	.	.	hsa00561:Glycerolipid metabolism; hsa01100:Metabolic pathways; hsa04723:Retrograde endocannabinoid signaling	R-HSA-1482883:Acyl chain remodeling of DAG and TAG; R-HSA-163560:Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis	MetaCyc:HS01140-MON	Q99685
TTJ8DV7	O-6-methylguanine-DNA-alkyltransferase (MGMT)	P16455	MGMT_HUMAN	Methyltransferase	Methylated-DNA--protein-cysteine methyltransferase; Human O(6)-alkylguanine-DNA alkyltransferase; 6-O-methylguanine-DNA methyltransferase	MGMT	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.	EC 2.1.1.63	1YFH; 1T39; 1T38; 1QNT; 1EH8	MDKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLLGKGTSAADAVEVPAPAAVLGGPEPLMQCTAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTRQVLWKLLKVVKFGEVISYQQLAALAGNPKAARAVGGAMRGNPVPILIPCHRVVCSSGAVGNYSGGLAVKEWLLAHEGHRLGKPGLGGSSGLAGAWLKGAGATSGSPPAGRN	Clinical trial	"Phase II trial of temozolomide plus o6-benzylguanine in adults with recurrent, temozolomide-resistant malignant glioma. J Clin Oncol. 2009 Mar 10;27(8):1262-7."	25	EC:2.1	Methyltransferase	MGMT family.	2.1.1.63	Transferring one-carbon groups	"6-O-methylguanine DNA methyltransferase, DNA binding domain; 6-O-methylguanine DNA methyltransferase, ribonuclease-like domain"	PF01035; PF02870	PF01035; DNA_binding_1; PF02870; Methyltransf_1N	.	.	.	R-HSA-5657655: MGMT-mediated DNA damage reversal	.	P16455
TT5HNVS	Melanoma derived growth regulator (MIA)	Q16674	MIA_HUMAN	.	Melanoma-derived growth regulatory protein; Melanoma inhibitory activity protein	MIA	"Elicits growth inhibition on melanoma cells in vitro as well as some other neuroectodermal tumors, including gliomas."	.	5IXB; 1K0X; 1I1J; 1HJD	MARSLVCLGVIILLSAFSGPGVRGGPMPKLADRKLCADQECSHPISMAVALQDYMAPDCRFLTIHRGQVVYVFSKLKGRGRLFWGGSVQGDYYGDLAARLGYFPSSIVREDQTLKPGKVDVKTDKWDFYCQ	Literature-reported	Melanoma-derived factors alter the maturation and activation of differentiated tissue-resident dendritic cells. Immunol Cell Biol. 2016 Jan;94(1):24-38.	.	.	.	MIA/OTOR family.	.	.	Variant SH3 domain	PF07653	PF07653; SH3_2	.	.	.	.	.	Q16674
TT6804T	MIF messenger RNA (MIF mRNA)	P14174	MIF_HUMAN	mRNA target	Phenylpyruvate tautomerase (mRNA); MMIF (mRNA); L-dopachrome tautomerase (mRNA); L-dopachrome isomerase (mRNA); Glycosylation-inhibiting factor (mRNA); GLIF (mRNA); GIF (mRNA)	MIF	"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."	EC 5.3.2.1	6FVH; 6FVE; 6CBH; 6CBG; 6CBF	MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTFA	Literature-reported	"US patent application no. 6,268,151, Antisense modulation of macrophage migration inhibitory factor expression."	0	mRNA	mRNA target	.	.	.	Macrophage migration inhibitory factor (MIF)	PF01187	PF01187; MIF	.	.	hsa00350:Tyrosine metabolism; hsa00360:Phenylalanine metabolism	R-HSA-202733: Cell surface interactions at the vascular wall; R-HSA-6798695: Neutrophil degranulation; R-HSA-8950505: Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation	.	P14174
TT2AST1	Macrophage migration inhibitory factor (MIF)	P14174	MIF_HUMAN	Intramolecular oxidoreductase	Phenylpyruvate tautomerase; MMIF; L-dopachrome tautomerase; L-dopachrome isomerase; Glycosylation-inhibiting factor; GLIF; GIF	MIF	"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."	EC 5.3.2.1	6FVH; 6FVE; 6CBH; 6CBG; 6CBF	MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTFA	Clinical trial	Neutralization of Macrophage Migration Inhibitory Factor (MIF) by Fully Human Antibodies Correlates with Their Specificity for the beta-Sheet Structure of MIF. J Biol Chem. 2012 March 2; 287(10): 7446-7455.	31	EC:5.3	Intramolecular oxidoreductases	MIF family.	5.3.2.1	Intramolecular oxidoreductases	Macrophage migration inhibitory factor (MIF)	PF01187	PF01187; MIF	.	.	hsa00350:Tyrosine metabolism; hsa00360:Phenylalanine metabolism	R-HSA-202733: Cell surface interactions at the vascular wall; R-HSA-6798695: Neutrophil degranulation; R-HSA-8950505: Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation	.	P14174
TTB4UNG	Antigen KI-67 messenger RNA (MKI67 mRNA)	P46013	KI67_HUMAN	mRNA target	Proliferation marker protein Ki-67 (mRNA); Antigen identified by monoclonal antibody Ki-67 (mRNA); Antigen Ki67 (mRNA); Antigen KI-67 (mRNA)	MKI67	"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."	.	5J28; 2AFF; 1R21	MWPTRRLVTIKRSGVDGPHFPLSLSTCLFGRGIECDIRIQLPVVSKQHCKIEIHEQEAILHNFSSTNPTQVNGSVIDEPVRLKHGDVITIIDRSFRYENESLQNGRKSTEFPRKIREQEPARRVSRSSFSSDPDEKAQDSKAYSKITEGKVSGNPQVHIKNVKEDSTADDSKDSVAQGTTNVHSSEHAGRNGRNAADPISGDFKEISSVKLVSRYGELKSVPTTQCLDNSKKNESPFWKLYESVKKELDVKSQKENVLQYCRKSGLQTDYATEKESADGLQGETQLLVSRKSRPKSGGSGHAVAEPASPEQELDQNKGKGRDVESVQTPSKAVGASFPLYEPAKMKTPVQYSQQQNSPQKHKNKDLYTTGRRESVNLGKSEGFKAGDKTLTPRKLSTRNRTPAKVEDAADSATKPENLSSKTRGSIPTDVEVLPTETEIHNEPFLTLWLTQVERKIQKDSLSKPEKLGTTAGQMCSGLPGLSSVDINNFGDSINESEGIPLKRRRVSFGGHLRPELFDENLPPNTPLKRGEAPTKRKSLVMHTPPVLKKIIKEQPQPSGKQESGSEIHVEVKAQSLVISPPAPSPRKTPVASDQRRRSCKTAPASSSKSQTEVPKRGGRKSGNLPSKRVSISRSQHDILQMICSKRRSGASEANLIVAKSWADVVKLGAKQTQTKVIKHGPQRSMNKRQRRPATPKKPVGEVHSQFSTGHANSPCTIIIGKAHTEKVHVPARPYRVLNNFISNQKMDFKEDLSGIAEMFKTPVKEQPQLTSTCHIAISNSENLLGKQFQGTDSGEEPLLPTSESFGGNVFFSAQNAAKQPSDKCSASPPLRRQCIRENGNVAKTPRNTYKMTSLETKTSDTETEPSKTVSTANRSGRSTEFRNIQKLPVESKSEETNTEIVECILKRGQKATLLQQRREGEMKEIERPFETYKENIELKENDEKMKAMKRSRTWGQKCAPMSDLTDLKSLPDTELMKDTARGQNLLQTQDHAKAPKSEKGKITKMPCQSLQPEPINTPTHTKQQLKASLGKVGVKEELLAVGKFTRTSGETTHTHREPAGDGKSIRTFKESPKQILDPAARVTGMKKWPRTPKEEAQSLEDLAGFKELFQTPGPSEESMTDEKTTKIACKSPPPESVDTPTSTKQWPKRSLRKADVEEEFLALRKLTPSAGKAMLTPKPAGGDEKDIKAFMGTPVQKLDLAGTLPGSKRQLQTPKEKAQALEDLAGFKELFQTPGHTEELVAAGKTTKIPCDSPQSDPVDTPTSTKQRPKRSIRKADVEGELLACRNLMPSAGKAMHTPKPSVGEEKDIIIFVGTPVQKLDLTENLTGSKRRPQTPKEEAQALEDLTGFKELFQTPGHTEEAVAAGKTTKMPCESSPPESADTPTSTRRQPKTPLEKRDVQKELSALKKLTQTSGETTHTDKVPGGEDKSINAFRETAKQKLDPAASVTGSKRHPKTKEKAQPLEDLAGLKELFQTPVCTDKPTTHEKTTKIACRSQPDPVDTPTSSKPQSKRSLRKVDVEEEFFALRKRTPSAGKAMHTPKPAVSGEKNIYAFMGTPVQKLDLTENLTGSKRRLQTPKEKAQALEDLAGFKELFQTRGHTEESMTNDKTAKVACKSSQPDPDKNPASSKRRLKTSLGKVGVKEELLAVGKLTQTSGETTHTHTEPTGDGKSMKAFMESPKQILDSAASLTGSKRQLRTPKGKSEVPEDLAGFIELFQTPSHTKESMTNEKTTKVSYRASQPDLVDTPTSSKPQPKRSLRKADTEEEFLAFRKQTPSAGKAMHTPKPAVGEEKDINTFLGTPVQKLDQPGNLPGSNRRLQTRKEKAQALEELTGFRELFQTPCTDNPTTDEKTTKKILCKSPQSDPADTPTNTKQRPKRSLKKADVEEEFLAFRKLTPSAGKAMHTPKAAVGEEKDINTFVGTPVEKLDLLGNLPGSKRRPQTPKEKAKALEDLAGFKELFQTPGHTEESMTDDKITEVSCKSPQPDPVKTPTSSKQRLKISLGKVGVKEEVLPVGKLTQTSGKTTQTHRETAGDGKSIKAFKESAKQMLDPANYGTGMERWPRTPKEEAQSLEDLAGFKELFQTPDHTEESTTDDKTTKIACKSPPPESMDTPTSTRRRPKTPLGKRDIVEELSALKQLTQTTHTDKVPGDEDKGINVFRETAKQKLDPAASVTGSKRQPRTPKGKAQPLEDLAGLKELFQTPICTDKPTTHEKTTKIACRSPQPDPVGTPTIFKPQSKRSLRKADVEEESLALRKRTPSVGKAMDTPKPAGGDEKDMKAFMGTPVQKLDLPGNLPGSKRWPQTPKEKAQALEDLAGFKELFQTPGTDKPTTDEKTTKIACKSPQPDPVDTPASTKQRPKRNLRKADVEEEFLALRKRTPSAGKAMDTPKPAVSDEKNINTFVETPVQKLDLLGNLPGSKRQPQTPKEKAEALEDLVGFKELFQTPGHTEESMTDDKITEVSCKSPQPESFKTSRSSKQRLKIPLVKVDMKEEPLAVSKLTRTSGETTQTHTEPTGDSKSIKAFKESPKQILDPAASVTGSRRQLRTRKEKARALEDLVDFKELFSAPGHTEESMTIDKNTKIPCKSPPPELTDTATSTKRCPKTRPRKEVKEELSAVERLTQTSGQSTHTHKEPASGDEGIKVLKQRAKKKPNPVEEEPSRRRPRAPKEKAQPLEDLAGFTELSETSGHTQESLTAGKATKIPCESPPLEVVDTTASTKRHLRTRVQKVQVKEEPSAVKFTQTSGETTDADKEPAGEDKGIKALKESAKQTPAPAASVTGSRRRPRAPRESAQAIEDLAGFKDPAAGHTEESMTDDKTTKIPCKSSPELEDTATSSKRRPRTRAQKVEVKEELLAVGKLTQTSGETTHTDKEPVGEGKGTKAFKQPAKRKLDAEDVIGSRRQPRAPKEKAQPLEDLASFQELSQTPGHTEELANGAADSFTSAPKQTPDSGKPLKISRRVLRAPKVEPVGDVVSTRDPVKSQSKSNTSLPPLPFKRGGGKDGSVTGTKRLRCMPAPEEIVEELPASKKQRVAPRARGKSSEPVVIMKRSLRTSAKRIEPAEELNSNDMKTNKEEHKLQDSVPENKGISLRSRRQNKTEAEQQITEVFVLAERIEINRNEKKPMKTSPEMDIQNPDDGARKPIPRDKVTENKRCLRSARQNESSQPKVAEESGGQKSAKVLMQNQKGKGEAGNSDSMCLRSRKTKSQPAASTLESKSVQRVTRSVKRCAENPKKAEDNVCVKKIRTRSHRDSEDI	Literature-reported	Antisense treatment against Ki-67 mRNA inhibits proliferation and tumor growth in vitro and in vivo. Int J Cancer. 2003 Jul 10;105(5):710-6.	.	mRNA	mRNA target	.	.	.	FHA domain; KI67R (NUC007) repeat; Protein phosphatase 1 binding	PF00498; PF08065; PF15276	PF00498; FHA; PF08065; KI67R; PF15276; PP1_bind	.	.	.	.	.	.
TTVXTZ4	Proliferation marker protein Ki-67 (MKI67)	P46013	KI67_HUMAN	.	Antigen identified by monoclonal antibody Ki-67; Antigen Ki67; Antigen KI-67	MKI67	"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."	.	5J28; 2AFF; 1R21	MWPTRRLVTIKRSGVDGPHFPLSLSTCLFGRGIECDIRIQLPVVSKQHCKIEIHEQEAILHNFSSTNPTQVNGSVIDEPVRLKHGDVITIIDRSFRYENESLQNGRKSTEFPRKIREQEPARRVSRSSFSSDPDEKAQDSKAYSKITEGKVSGNPQVHIKNVKEDSTADDSKDSVAQGTTNVHSSEHAGRNGRNAADPISGDFKEISSVKLVSRYGELKSVPTTQCLDNSKKNESPFWKLYESVKKELDVKSQKENVLQYCRKSGLQTDYATEKESADGLQGETQLLVSRKSRPKSGGSGHAVAEPASPEQELDQNKGKGRDVESVQTPSKAVGASFPLYEPAKMKTPVQYSQQQNSPQKHKNKDLYTTGRRESVNLGKSEGFKAGDKTLTPRKLSTRNRTPAKVEDAADSATKPENLSSKTRGSIPTDVEVLPTETEIHNEPFLTLWLTQVERKIQKDSLSKPEKLGTTAGQMCSGLPGLSSVDINNFGDSINESEGIPLKRRRVSFGGHLRPELFDENLPPNTPLKRGEAPTKRKSLVMHTPPVLKKIIKEQPQPSGKQESGSEIHVEVKAQSLVISPPAPSPRKTPVASDQRRRSCKTAPASSSKSQTEVPKRGGRKSGNLPSKRVSISRSQHDILQMICSKRRSGASEANLIVAKSWADVVKLGAKQTQTKVIKHGPQRSMNKRQRRPATPKKPVGEVHSQFSTGHANSPCTIIIGKAHTEKVHVPARPYRVLNNFISNQKMDFKEDLSGIAEMFKTPVKEQPQLTSTCHIAISNSENLLGKQFQGTDSGEEPLLPTSESFGGNVFFSAQNAAKQPSDKCSASPPLRRQCIRENGNVAKTPRNTYKMTSLETKTSDTETEPSKTVSTANRSGRSTEFRNIQKLPVESKSEETNTEIVECILKRGQKATLLQQRREGEMKEIERPFETYKENIELKENDEKMKAMKRSRTWGQKCAPMSDLTDLKSLPDTELMKDTARGQNLLQTQDHAKAPKSEKGKITKMPCQSLQPEPINTPTHTKQQLKASLGKVGVKEELLAVGKFTRTSGETTHTHREPAGDGKSIRTFKESPKQILDPAARVTGMKKWPRTPKEEAQSLEDLAGFKELFQTPGPSEESMTDEKTTKIACKSPPPESVDTPTSTKQWPKRSLRKADVEEEFLALRKLTPSAGKAMLTPKPAGGDEKDIKAFMGTPVQKLDLAGTLPGSKRQLQTPKEKAQALEDLAGFKELFQTPGHTEELVAAGKTTKIPCDSPQSDPVDTPTSTKQRPKRSIRKADVEGELLACRNLMPSAGKAMHTPKPSVGEEKDIIIFVGTPVQKLDLTENLTGSKRRPQTPKEEAQALEDLTGFKELFQTPGHTEEAVAAGKTTKMPCESSPPESADTPTSTRRQPKTPLEKRDVQKELSALKKLTQTSGETTHTDKVPGGEDKSINAFRETAKQKLDPAASVTGSKRHPKTKEKAQPLEDLAGLKELFQTPVCTDKPTTHEKTTKIACRSQPDPVDTPTSSKPQSKRSLRKVDVEEEFFALRKRTPSAGKAMHTPKPAVSGEKNIYAFMGTPVQKLDLTENLTGSKRRLQTPKEKAQALEDLAGFKELFQTRGHTEESMTNDKTAKVACKSSQPDPDKNPASSKRRLKTSLGKVGVKEELLAVGKLTQTSGETTHTHTEPTGDGKSMKAFMESPKQILDSAASLTGSKRQLRTPKGKSEVPEDLAGFIELFQTPSHTKESMTNEKTTKVSYRASQPDLVDTPTSSKPQPKRSLRKADTEEEFLAFRKQTPSAGKAMHTPKPAVGEEKDINTFLGTPVQKLDQPGNLPGSNRRLQTRKEKAQALEELTGFRELFQTPCTDNPTTDEKTTKKILCKSPQSDPADTPTNTKQRPKRSLKKADVEEEFLAFRKLTPSAGKAMHTPKAAVGEEKDINTFVGTPVEKLDLLGNLPGSKRRPQTPKEKAKALEDLAGFKELFQTPGHTEESMTDDKITEVSCKSPQPDPVKTPTSSKQRLKISLGKVGVKEEVLPVGKLTQTSGKTTQTHRETAGDGKSIKAFKESAKQMLDPANYGTGMERWPRTPKEEAQSLEDLAGFKELFQTPDHTEESTTDDKTTKIACKSPPPESMDTPTSTRRRPKTPLGKRDIVEELSALKQLTQTTHTDKVPGDEDKGINVFRETAKQKLDPAASVTGSKRQPRTPKGKAQPLEDLAGLKELFQTPICTDKPTTHEKTTKIACRSPQPDPVGTPTIFKPQSKRSLRKADVEEESLALRKRTPSVGKAMDTPKPAGGDEKDMKAFMGTPVQKLDLPGNLPGSKRWPQTPKEKAQALEDLAGFKELFQTPGTDKPTTDEKTTKIACKSPQPDPVDTPASTKQRPKRNLRKADVEEEFLALRKRTPSAGKAMDTPKPAVSDEKNINTFVETPVQKLDLLGNLPGSKRQPQTPKEKAEALEDLVGFKELFQTPGHTEESMTDDKITEVSCKSPQPESFKTSRSSKQRLKIPLVKVDMKEEPLAVSKLTRTSGETTQTHTEPTGDSKSIKAFKESPKQILDPAASVTGSRRQLRTRKEKARALEDLVDFKELFSAPGHTEESMTIDKNTKIPCKSPPPELTDTATSTKRCPKTRPRKEVKEELSAVERLTQTSGQSTHTHKEPASGDEGIKVLKQRAKKKPNPVEEEPSRRRPRAPKEKAQPLEDLAGFTELSETSGHTQESLTAGKATKIPCESPPLEVVDTTASTKRHLRTRVQKVQVKEEPSAVKFTQTSGETTDADKEPAGEDKGIKALKESAKQTPAPAASVTGSRRRPRAPRESAQAIEDLAGFKDPAAGHTEESMTDDKTTKIPCKSSPELEDTATSSKRRPRTRAQKVEVKEELLAVGKLTQTSGETTHTDKEPVGEGKGTKAFKQPAKRKLDAEDVIGSRRQPRAPKEKAQPLEDLASFQELSQTPGHTEELANGAADSFTSAPKQTPDSGKPLKISRRVLRAPKVEPVGDVVSTRDPVKSQSKSNTSLPPLPFKRGGGKDGSVTGTKRLRCMPAPEEIVEELPASKKQRVAPRARGKSSEPVVIMKRSLRTSAKRIEPAEELNSNDMKTNKEEHKLQDSVPENKGISLRSRRQNKTEAEQQITEVFVLAERIEINRNEKKPMKTSPEMDIQNPDDGARKPIPRDKVTENKRCLRSARQNESSQPKVAEESGGQKSAKVLMQNQKGKGEAGNSDSMCLRSRKTKSQPAASTLESKSVQRVTRSVKRCAENPKKAEDNVCVKKIRTRSHRDSEDI	Literature-reported	"Prognostic value of different cut-off levels of Ki-67 in breast cancer: a systematic review and meta-analysis of 64,196 patients. Breast Cancer Res Treat. 2015 Oct;153(3):477-91."	.	.	.	.	.	.	FHA domain; KI67R (NUC007) repeat; Protein phosphatase 1 binding	PF00498; PF08065; PF15276	PF00498; FHA; PF08065; KI67R; PF15276; PP1_bind	.	.	.	.	.	.
TTEZAUX	MAPK signal-integrating kinase 1 (MKNK1)	Q9BUB5	MKNK1_HUMAN	Protein kinase superfamily. CAMK Ser/Thr protein kinase family	Mnk1; MAP kinase signal-integrating kinase 1	MKNK1	"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."	EC 2.7.11.1	5WVD; 2Y9Q; 2HW6	MVSSQKLEKPIEMGSSEPLPIADGDRRRKKKRRGRATDSLPGKFEDMYKLTSELLGEGAYAKVQGAVSLQNGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKQKHFNEREASRVVRDVAAALDFLHTKDKVSLCHLGWSAMAPSGLTAAPTSLGSSDPPTSASQVAGTTGIAHRDLKPENILCESPEKVSPVKICDFDLGSGMKLNNSCTPITTPELTTPCGSAEYMAPEVVEVFTDQATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRVCQNKLFESIQEGKYEFPDKDWAHISSEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGQAPEKGLPTPQVLQRNSSTMDLTLFAAEAIALNRQLSQHEENELAEEPEALADGLCSMKLSPPCKSRLARRRALAQAGRGEDRSPPTAL	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	hsa04010:MAPK signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04910:Insulin signaling pathway	R-HSA-1295596: Spry regulation of FGF signaling	.	Q9BUB5
TTRECN3	MAP kinase signal-integrating kinase 2 (MKNK2)	Q9HBH9	MKNK2_HUMAN	Protein kinase superfamily. CAMK Ser/Thr protein kinase family	Mnk2; MAPK signal-integrating kinase 2	MKNK2	"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."	EC 2.7.11.1	6CKI; 6CK6; 6CK3; 6CJY; 6CJW	MVQKKPAELQGFHRSFKGQNPFELAFSLDQPDHGDSDFGLQCSARPDMPASQPIDIPDAKKRGKKKKRGRATDSFSGRFEDVYQLQEDVLGEGAHARVQTCINLITSQEYAVKIIEKQPGHIRSRVFREVEMLYQCQGHRNVLELIEFFEEEDRFYLVFEKMRGGSILSHIHKRRHFNELEASVVVQDVASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFDLGSGIKLNGDCSPISTPELLTPCGSAEYMAPEVVEAFSEEASIYDKRCDLWSLGVILYILLSGYPPFVGRCGSDCGWDRGEACPACQNMLFESIQEGKYEFPDKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWVQGCAPENTLPTPMVLQRNSCAKDLTSFAAEAIAMNRQLAQHDEDLAEEEAAGQGQPVLVRATSRCLQLSPPSQSKLAQRRQRASLSSAPVVLVGDHA	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	hsa04010:MAPK signaling pathway; hsa04066:HIF-1 signaling pathway; hsa04910:Insulin signaling pathway	.	.	Q9HBH9
TTITER7	E3 ubiquitin-protein ligase makorin-1 (MKRN1)	Q9UHC7	MKRN1_HUMAN	Carbon-nitrogen ligase	RNF61; RING-type E3 ubiquitin transferase makorin-1; RING finger protein 61	MKRN1	"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."	EC 2.3.2.27	.	MAEAATPGTTATTSGAGAAAATAAAASPTPIPTVTAPSLGAGGGGGGSDGSGGGWTKQVTCRYFMHGVCKEGDNCRYSHDLSDSPYSVVCKYFQRGYCIYGDRCRYEHSKPLKQEEATATELTTKSSLAASSSLSSIVGPLVEMNTGEAESRNSNFATVGAGSEDWVNAIEFVPGQPYCGRTAPSCTEAPLQGSVTKEESEKEQTAVETKKQLCPYAAVGECRYGENCVYLHGDSCDMCGLQVLHPMDAAQRSQHIKSCIEAHEKDMELSFAVQRSKDMVCGICMEVVYEKANPSERRFGILSNCNHTYCLKCIRKWRSAKQFESKIIKSCPECRITSNFVIPSEYWVEEKEEKQKLILKYKEAMSNKACRYFDEGRGSCPFGGNCFYKHAYPDGRREEPQRQKVGTSSRYRAQRRNHFWELIEERENSNPFDNDEEEVVTFELGEMLLMLLAAGGDDELTDSEDEWDLFHDELEDFYDLDL	Literature-reported	Identification of a new target molecule for a cascade therapy of polycystic kidney. Hum Cell. 2003 Jun;16(2):65-72.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-198323: AKT phosphorylates targets in the cytosol; R-HSA-8948751: Regulation of PTEN stability and activity; R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	Q9UHC7
TT362RB	MART-1 melanoma antigen (MLANA)	Q16655	MAR1_HUMAN	.	Protein MelanA; Melanoma antigen recognized by Tcells 1; MLANA; MART1; Antigen SK29AA; Antigen LB39AA	MLANA	"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."	.	6DKP; 6D78; 5NQK; 5NHT; 5E9D	MPREDAHFIYGYPKKGHGHSYTTAEEAAGIGILTVILGVLLLIGCWYCRRRNGYRALMDKSLHVGTQCALTRRCPQEGFDHRDSKVSLQEKNCEPVVPNAPPAYEKLSAEQSPPPYSP	Clinical trial	National Cancer Institute Drug Dictionary (drug id 685201).	25	.	.	.	.	.	.	.	.	.	.	.	.	.	Q16655
TTISG27	DNA mismatch repair protein Mlh1 (MLH1)	P40692	MLH1_HUMAN	.	MutL protein homolog 1; COCA2	MLH1	"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)."	.	5U5P; 4P7A; 3RBN	MSFVAGVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTSIQVIVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQSFEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLKAPPKPCAGNQGTQITVEDLFYNIATRRKALKNPSEEYGKILEVVGRYSVHNAGISFSVKKQGETVADVRTLPNASTVDNIRSIFGNAVSRELIEIGCEDKTLAFKMNGYISNANYSVKKCIFLLFINHRLVESTSLRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEMVKSTTSLTSSSTSGSSDKVYAHQMVRTDSREQKLDAFLQPLSKPLSSQPQAIVTEDKTDISSGRARQQDEEMLELPAPAEVAAKNQSLEGDTTKGTSEMSEKRGPTSSNPRKRHREDSDVEMVEDDSRKEMTAACTPRRRIINLTSVLSLQEEINEQGHEVLREMLHNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPAPLFDLAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAEMLADYFSLEIDEEGNLIGLPLLIDNYVPPLEGLPIFILRLATEVNWDEEKECFESLSKECAMFYSIRKQYISEESTLSGQQSEVPGSIPNSWKWTVEHIVYKALRSHILPPKHFTEDGNILQLANLPDLYKVFERC	Literature-reported	DNA mismatch repair gene MLH1 induces apoptosis in prostate cancer cells. Oncotarget. 2014 Nov 30;5(22):11297-307.	.	.	.	DNA mismatch repair MutL/HexB family.	.	.	"DNA mismatch repair protein, C-terminal domain; DNA mismatch repair protein Mlh1 C-terminus"	PF01119; PF16413	PF01119; DNA_mis_repair; PF16413; Mlh1_C	.	.	hsa01524: Platinum drug resistance; hsa03430: Mismatch repair; hsa03460: Fanconi anemia pathway; hsa05200: Pathways in cancer; hsa05210: Colorectal cancer; hsa05213: Endometrial cancer; hsa05226: Gastric cancer	R-HSA-5358565: Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha); R-HSA-5358606: Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta); R-HSA-5545483: Defective Mismatch Repair Associated With MLH1; R-HSA-5632987: Defective Mismatch Repair Associated With PMS2; R-HSA-6796648: TP53 Regulates Transcription of DNA Repair Genes; R-HSA-912446: Meiotic recombination	.	P40692
TT953CX	Motilin receptor (MLNR)	O43193	MTLR_HUMAN	GPCR rhodopsin	MLNR; Gprotein coupled receptor 38	MLNR	Receptor for motilin.	.	.	MGSPWNGSDGPEGAREPPWPALPPCDERRCSPFPLGALVPVTAVCLCLFVVGVSGNVVTVMLIGRYRDMRTTTNLYLGSMAVSDLLILLGLPFDLYRLWRSRPWVFGPLLCRLSLYVGEGCTYATLLHMTALSVERYLAICRPLRARVLVTRRRVRALIAVLWAVALLSAGPFLFLVGVEQDPGISVVPGLNGTARIASSPLASSPPLWLSRAPPPSPPSGPETAEAAALFSRECRPSPAQLGALRVMLWVTTAYFFLPFLCLSILYGLIGRELWSSRRPLRGPAASGRERGHRQTVRVLLVVVLAFIICWLPFHVGRIIYINTEDSRMMYFSQYFNIVALQLFYLSASINPILYNLISKKYRAAAFKLLLARKSRPRGFHRSRDTAGEVAGDTGGDTVGYTETSANVKTMG	Clinical trial	Discovery of a new class of macrocyclic antagonists to the human motilin receptor. J Med Chem. 2006 Nov 30;49(24):7190-7.	31	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events	.	O43193
TT9Z4YD	Malonyl-CoA decarboxylase (MLYCD)	O95822	DCMC_HUMAN	.	"Malonyl-CoA decarboxylase, mitochondrial; MCD"	MLYCD	"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."	EC 4.1.1.9	4F0X; 2YGW	MRGFGPGLTARRLLPLRLPPRPPGPRLASGQAAGALERAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSECKEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQVLSLVAQFQKNSKL	Literature-reported	Malonyl-CoA decarboxylase inhibition is selectively cytotoxic to human breast cancer cells. Oncogene. 2009 Aug 20;28(33):2979-87.	.	.	.	.	.	.	.	.	.	.	.	hsa00410: beta-Alanine metabolism; hsa00640: Propanoate metabolism; hsa01100: Metabolic pathways; hsa04146: Peroxisome; hsa04152: AMPK signaling pathway; hsa04936: Alcoholic liver disease	R-HSA-390247: Beta-oxidation of very long chain fatty acids; R-HSA-9033241: Peroxisomal protein import	.	O95822
TT5TKPM	Neutral endopeptidase (MME)	P08473	NEP_HUMAN	Peptidase	Skin fibroblast elastase; SFE; Neutral endopeptidase 24.11; Neprilysin; NEP protein; Enkephalinase; EPN; Common acute lymphocytic leukemia antigen; CD10; CALLA; Atriopeptidase	MME	"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."	EC 3.4.24.11	6GID; 5JMY; 4CTH; 2YB9; 2QPJ	MGKSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTIIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW	Clinical trial	2014 FDA drug approvals. Nat Rev Drug Discov. 2015 Feb;14(2):77-81.	31	EC:3.4	Peptidase	peptidase M13 family.	3.4.24.11 	Acting on peptide bonds (peptidases)	Peptidase family M13; Peptidase family M13	PF01431; PF05649	PF01431; Peptidase_M13; PF05649; Peptidase_M13_N	.	.	hsa04614:Renin-angiotensin system; hsa04640:Hematopoietic cell lineage; hsa04974:Protein digestion and absorption; hsa05010:Alzheimer's disease	R-HSA-2022377:Metabolism of Angiotensinogen to Angiotensins	.	P08473
TTMX39J	Matrix metalloproteinase-1 (MMP-1)	P03956	MMP1_HUMAN	Peptidase	Interstitial collagenase; Fibroblast collagenase; CLG	MMP1	"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."	EC 3.4.24.7	966C; 4AYK; 4AUO; 3SHI; 3AYK	MHSFPPLLLLLFWGVVSHSFPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPVVEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN	Successful	AG-3340 (Agouron Pharmaceuticals Inc). IDrugs. 2000 Mar;3(3):336-45.	34	EC:3.4	Peptidase	peptidase M10A family.	3.4.24.7 	Acting on peptide bonds (peptidases)	Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF00045; PF00413; PF01471	PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	hsa03320:PPAR signaling pathway; hsa05200:Pathways in cancer; hsa05219:Bladder cancer; hsa05323:Rheumatoid arthritis	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)	.	P03956
TTXLEG7	Matrix metalloproteinase-10 (MMP-10)	P09238	MMP10_HUMAN	Peptidase	Transin-2; Stromelysin-2; STMY2; SL-2	MMP10	"Activates procollagenase. Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V."	EC 3.4.24.22	4ILW; 3V96; 1Q3A	MMHLAFLVLLCLPVCSAYPLSGAAKEEDSNKDLAQQYLEKYYNLEKDVKQFRRKDSNLIVKKIQGMQKFLGLEVTGKLDTDTLEVMRKPRCGVPDVGHFSSFPGMPKWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRLYEGEADIMISFAVKEHGDFYSFDGPGHSLAHAYPPGPGLYGDIHFDDDEKWTEDASGTNLFLVAAHELGHSLGLFHSANTEALMYPLYNSFTELAQFRLSQDDVNGIQSLYGPPPASTEEPLVPTKSVPSGSEMPAKCDPALSFDAISTLRGEYLFFKDRYFWRRSHWNPEPEFHLISAFWPSLPSYLDAAYEVNSRDTVFIFKGNEFWAIRGNEVQAGYPRGIHTLGFPPTIRKIDAAVSDKEKKKTYFFAADKYWRFDENSQSMEQGFPRLIADDFPGVEPKVDAVLQAFGFFYFFSGSSQFEFDPNARMVTHILKSNSWLHC	Patented-recorded	"Discovery and safety profiling of a potent preclinical candidate, (4-[4-[[(3R)-3-(hydroxycarbamoyl)-8-azaspiro[4.5]decan-3-yl]sulfonyl]phenoxy]-N-methylbenzamide) (CM-352), for the prevention and treatment of hemorrhage. J Med Chem. 2015 Apr 9;58(7):2941-57."	0	EC:3.4	.	peptidase M10A family.	3.4.24.22	Acting on peptide bonds (peptidases)	Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF00045; PF00413; PF01471	PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	.	R-HSA-1442490: Collagen degradation; R-HSA-1474228: Degradation of the extracellular matrix; R-HSA-1592389: Activation of Matrix Metalloproteinases	.	P09238
TTZW4MV	Matrix metalloproteinase-11 (MMP-11)	P24347	MMP11_HUMAN	Peptidase	Stromelysin-3 (ST3) gene; Stromelysin-3; STR-3; STMY3; ST3/MMP11; ST3; SL-3	MMP11	May play an important role in the progression of epithelial malignancies.	EC 3.4.24.-	.	MAPAAWLRSAAARALLPPMLLLLLQPPPLLARALPPDAHHLHAERRGPQPWHAALPSSPAPAPATQEAPRPASSLRPPRCGVPDPSDGLSARNRQKRFVLSGGRWEKTDLTYRILRFPWQLVQEQVRQTMAEALKVWSDVTPLTFTEVHEGRADIMIDFARYWHGDDLPFDGPGGILAHAFFPKTHREGDVHFDYDETWTIGDDQGTDLLQVAAHEFGHVLGLQHTTAAKALMSAFYTFRYPLSLSPDDCRGVQHLYGQPWPTVTSRTPALGPQAGIDTNEIAPLEPDAPPDACEASFDAVSTIRGELFFFKAGFVWRLRGGQLQPGYPALASRHWQGLPSPVDAAFEDAQGHIWFFQGAQYWVYDGEKPVLGPAPLTELGLVRFPVHAALVWGPEKNKIYFFRGRDYWRFHPSTRRVDSPVPRRATDWRGVPSEIDAAFQDADGYAYFLRGRLYWKFDPVKVKALEGFPRLVGPDFFGCAEPANTFL	Literature-reported	Specific targeting of metzincin family members with small-molecule inhibitors: progress toward a multifarious challenge. Bioorg Med Chem. 2008 Oct 1;16(19):8781-94.	0	EC:3.4	Peptidase	peptidase M10A family.	3.4.24.-	Acting on peptide bonds (peptidases)	Hemopexin; Matrixin	PF00045; PF00413	PF00045; Hemopexin; PF00413; Peptidase_M10	.	.	.	R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases	.	P24347
TTXZ0KQ	Matrix metalloproteinase-12 (MMP-12)	P39900	MMP12_HUMAN	Peptidase	Macrophage metalloelastase; Macrophage elastase; MME; ME; HME	MMP12	"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."	EC 3.4.24.65	6EOX; 6ENM; 6ELA; 6EKN; 5N5K	MKFLLILLLQATASGALPLNSSTSLEKNNVLFGERYLEKFYGLEINKLPVTKMKYSGNLMKEKIQEMQHFLGLKVTGQLDTSTLEMMHAPRCGVPDVHHFREMPGGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYGDPKENQRLPNPDNSEPALCDPNLSFDAVTTVGNKIFFFKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNLRPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNKYYYFFQGSNQFEYDFLLQRITKTLKSNSWFGC	Clinical trial	Potential clinical implications of recent matrix metalloproteinase inhibitor design strategies. Expert Rev Proteomics. 2015;12(5):445-7.	17	EC:3.4	Peptidase	peptidase M10A family.	3.4.24.65	Acting on peptide bonds (peptidases)	Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF00045; PF00413; PF01471	PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	.	R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix	.	P39900
TTHY57M	Matrix metalloproteinase-13 (MMP-13)	P45452	MMP13_HUMAN	Peptidase	Matrix metalloproteinase 13; Collagenase-3; Collagenase 3	MMP13	"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."	EC 3.4.24.-	830C; 5UWN; 5UWM; 5UWL; 5UWK	MHPGVLAAFLFLSWTHCRALPLPSGGDEDDLSEEDLQFAERYLRSYYHPTNLAGILKENAASSMTERLREMQSFFGLEVTGKLDDNTLDVMKKPRCGVPDVGEYNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRKFWALNGYDILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVWRYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPANSILWC	Clinical trial	High throughput screening of potentially selective MMP-13 exosite inhibitors utilizing a triple-helical FRET substrate. Bioorg Med Chem. 2009 Feb 1;17(3):990-1005.	25	EC:3.4	Peptidase	peptidase M10A family.	3.4.24.-	Acting on peptide bonds (peptidases)	Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF00045; PF00413; PF01471	PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	"hsa04657: IL-17 signaling pathway; hsa04926: Relaxin signaling pathway; hsa04928: Parathyroid hormone synthesis, secretion and action"	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	.	P45452
TTJ4QE7	Matrix metalloproteinase-14 (MMP-14)	P50281	MMP14_HUMAN	Peptidase	Membrane-type-1 matrix metalloproteinase; Membrane-type matrix metalloproteinase 1; MTMMP1; MT1MMP; MT1-MMP; MT-MMP 1; MMP-X1	MMP14	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.	EC 3.4.24.80	6CM1; 6CLZ; 5H0U; 4QXU; 4P3D	MSPAPRPPRCLLLPLLTLGTALASLGSAQSSSFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQKFYGLQVTGKADADTMKAMRRPRCGVPDKFGAEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGESGFPTKMPPQPRTTSRPSVPDKPKNPTYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGGGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPRRLLYCQRSLLDKV	Clinical trial	Regioselective synthesis of methylated epigallocatechin gallate via nitrobenzenesulfonyl (Ns) protecting group. Bioorg Med Chem Lett. 2009 Aug 1;19(15):4171-4.	25	EC:3.4	Peptidase	peptidase M10A family.	3.4.24.80	Acting on peptide bonds (peptidases)	Domain of unknown function (DUF3377); Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF11857; PF00045; PF00413; PF01471	PF11857; DUF3377; PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	hsa04668:TNF signaling pathway; hsa04912:GnRH signaling pathway	R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases	MetaCyc:ENSG00000157227-MON	P50281
TTNSTO3	Matrix metalloproteinase-15 (MMP-15)	P51511	MMP15_HUMAN	Peptidase	SMCP-2; Membrane-type-2 matrix metalloproteinase; Membrane-type matrix metalloproteinase 2; MTMMP2; MT2MMP; MT2-MMP; MT-MMP 2	MMP15	May activate progelatinase A. Endopeptidase that degrades various components of the extracellular matrix.	EC 3.4.24.-	.	MGSDPSAPGRPGWTGSLLGDREEAARPRLLPLLLVLLGCLGLGVAAEDAEVHAENWLRLYGYLPQPSRHMSTMRSAQILASALAEMQRFYGIPVTGVLDEETKEWMKRPRCGVPDQFGVRVKANLRRRRKRYALTGRKWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYEDIRLRRQKEADIMVLFASGFHGDSSPFDGTGGFLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLRGIQQLYGTPDGQPQPTQPLPTVTPRRPGRPDHRPPRPPQPPPPGGKPERPPKPGPPVQPRATERPDQYGPNICDGDFDTVAMLRGEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPGDISAAYERQDGRFVFFKGDRYWLFREANLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFFFQEDRYWRFNEETQRGDPGYPKPISVWQGIPASPKGAFLSNDAAYTYFYKGTKYWKFDNERLRMEPGYPKSILRDFMGCQEHVEPGPRWPDVARPPFNPHGGAEPGADSAEGDVGDGDGDFGAGVNKDGGSRVVVQMEEVARTVNVVMVLVPLLLLLCVLGLTYALVQMQRKGAPRVLLYCKRSLQEWV	Literature-reported	"Design, synthesis, and structure-activity relationships of macrocyclic hydroxamic acids that inhibit tumor necrosis factor alpha release in vitro and in vivo. J Med Chem. 2001 Aug 2;44(16):2636-60."	0	EC:3.4	.	peptidase M10A family.	3.4.24.-	Acting on peptide bonds (peptidases)	Domain of unknown function (DUF3377); Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF11857; PF00045; PF00413; PF01471	PF11857; DUF3377; PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	"hsa04928: Parathyroid hormone synthesis, secretion and action"	R-HSA-1442490: Collagen degradation; R-HSA-1474228: Degradation of the extracellular matrix; R-HSA-1592389: Activation of Matrix Metalloproteinases	.	P51511
TTNP4CU	Matrix metalloproteinase-16 (MMP-16)	P51512	MMP16_HUMAN	Peptidase	Membrane-type-3 matrix metalloproteinase; Membrane-type matrix metalloproteinase 3; MTMMP3; MT3MMP; MT3-MMP; MT-MMP 3; MMPX2; MMP-X2; C8orf57	MMP16	"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."	EC 3.4.24.-	1RM8	MILLTFSTGRRLDFVHHSGVFFLQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRMSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFHIRRKRYALTGQKWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSELENGKRDVDITIIFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPTRPLPTVPPHRSIPPADPRKNDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLITLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITVWKGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRVKEGHSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV	Literature-reported	"Design, synthesis, and structure-activity relationships of macrocyclic hydroxamic acids that inhibit tumor necrosis factor alpha release in vitro and in vivo. J Med Chem. 2001 Aug 2;44(16):2636-60."	0	EC:3.4	.	peptidase M10A family.	3.4.24.-	Acting on peptide bonds (peptidases)	Domain of unknown function (DUF3377); Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF11857; PF00045; PF00413; PF01471	PF11857; DUF3377; PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	"hsa04928: Parathyroid hormone synthesis, secretion and action; hsa05206: MicroRNAs in cancer"	R-HSA-1592389: Activation of Matrix Metalloproteinases	.	P51512
TTVSZKN	Matrix metalloproteinase-17 (MMP17)	Q9ULZ9	MMP17_HUMAN	Peptidase	Membrane-type-4 matrix metalloproteinase; Membrane-type matrix metalloproteinase 4; MTMMP4; MT4MMP; MT4-MMP; MT-MMP 4; MMP-17	MMP17	"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."	EC 3.4.24.-	.	MRRRAARGPGPPPPGPGLSRLPLPLLLLLALGTRGGCAAPAPAPRAEDLSLGVEWLSRFGYLPPADPTTGQLQTQEELSKAITAMQQFGGLEATGILDEATLALMKTPRCSLPDLPVLTQARRRRQAPAPTKWNKRNLSWRVRTFPRDSPLGHDTVRALMYYALKVWSDIAPLNFHEVAGSAADIQIDFSKADHNDGYPFDGPGGTVAHAFFPGHHHTAGDTHFDDDEAWTFRSSDAHGMDLFAVAVHEFGHAIGLSHVAAAHSIMRPYYQGPVGDPLRYGLPYEDKVRVWQLYGVRESVSPTAQPEEPPLLPEPPDNRSSAPPRKDVPHRCSTHFDAVAQIRGEAFFFKGKYFWRLTRDRHLVSLQPAQMHRFWRGLPLHLDSVDAVYERTSDHKIVFFKGDRYWVFKDNNVEEGYPRPVSDFSLPPGGIDAAFSWAHNDRTYFFKDQLYWRYDDHTRHMDPGYPAQSPLWRGVPSTLDDAMRWSDGASYFFRGQEYWKVLDGELEVAPGYPQSTARDWLVCGDSQADGSVAAGVDAAEGPRAPPGQHDQSRSEDGYEVCSCTSGASSPPGAPGPLVAATMLLLLPPLSPGALWTAAQALTL	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	.	.	.	.	.	.	.	.	.	.	"hsa04928: Parathyroid hormone synthesis, secretion and action"	R-HSA-1592389: Activation of Matrix Metalloproteinases	.	Q9ULZ9
TTLM12X	Matrix metalloproteinase-2 (MMP-2)	P08253	MMP2_HUMAN	Peptidase	TBE-1; Matrix metalloproteinase 2; CLG4A; 72 kDa type IV collagenase; 72 kDa gelatinase	MMP2	"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."	EC 3.4.24.24	3AYU; 1RTG; 1QIB; 1KS0; 1J7M	MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC	Successful	AG-3340 (Agouron Pharmaceuticals Inc). IDrugs. 2000 Mar;3(3):336-45.	34	EC:3.4	Peptidase	peptidase M10A family.	3.4.24.24 	Acting on peptide bonds (peptidases)	Fibronectin type II domain; Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF00040; PF00045; PF00413; PF01471	PF00040; fn2; PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	hsa04670:Leukocyte transendothelial migration; hsa04912:GnRH signaling pathway; hsa04915:Estrogen signaling pathway; hsa05200:Pathways in cancer; hsa05205:Proteoglycans in cancer; hsa05219:Bladder cancer	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	MetaCyc:HS01565-MON	P08253
TTDO3RC	MMP2 messenger RNA (MMP2 mRNA)	P08253	MMP2_HUMAN	mRNA target	TBE-1 (mRNA); Matrix metalloproteinase 2 (mRNA); Gelatinase A (mRNA); CLG4A (mRNA); 72 kDa type IV collagenase (mRNA); 72 kDa gelatinase (mRNA)	MMP2	"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."	EC 3.4.24.24	3AYU; 1RTG; 1QIB; 1KS0; 1J7M	MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC	Literature-reported	NCBI GEO: archive for functional genomics data sets--update. Nucleic Acids Res. 2013 Jan;41(Database issue):D991-5.	.	mRNA	mRNA target	.	.	.	Fibronectin type II domain; Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF00040; PF00045; PF00413; PF01471	PF00040; fn2; PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	hsa01522: Endocrine resistance; hsa04670: Leukocyte transendothelial migration; hsa04912: GnRH signaling pathway; hsa04915: Estrogen signaling pathway; hsa04926: Relaxin signaling pathway; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05219: Bladder cancer; hsa05415: Diabetic cardiomyopathy; hsa05418: Fluid shear stress and atherosclerosis	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; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9009391: Extra-nuclear estrogen signaling	MetaCyc:HS01565-MON	P08253
TTXPTJE	Gelatinase (GEL)	P08253; P14780	MMP2_HUMAN; MMP9_HUMAN	Peptidase	Matrix metalloproteinase GEL; Gelatinase B; Gelatinase A; Collagenase IV; CLG4	MMP2	"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."	.	.	MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC	Patented-recorded	Gelatinase inhibitors: a patent review (2011-2017).Expert Opin Ther Pat. 2018 Jan;28(1):31-46.	15.5	.	.	.	.	.	.	.	.	.	.	hsa01522: Endocrine resistance; hsa04670: Leukocyte transendothelial migration; hsa04912: GnRH signaling pathway; hsa04915: Estrogen signaling pathway; hsa04926: Relaxin signaling pathway; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05219: Bladder cancer; hsa05415: Diabetic cardiomyopathy; hsa05418: Fluid shear stress and atherosclerosis	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; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9009391: Extra-nuclear estrogen signaling	MetaCyc:HS01565-MON	P08253
TTYRF5E	Matrix metalloproteinase-21 (MMP-21)	Q8N119	MMP21_HUMAN	Peptidase	MMP	MMP21	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.	EC 3.4.24.-	.	MLAASIFRPTLLLCWLAAPWPTQPESLFHSRDRSDLEPSPLRQAKPIADLHAAQRFLSRYGWSGVWAAWGPSPEGPPETPKGAALAEAVRRFQRANALPASGELDAATLAAMNRPRCGVPDMRPPPPSAPPSPPGPPPRARSRRSPRAPLSLSRRGWQPRGYPDGGAAQAFSKRTLSWRLLGEALSSQLSVADQRRIVALAFRMWSEVTPLDFREDLAAPGAAVDIKLGFGRGRHLGCPRAFDGSGQEFAHAWRLGDIHFDDDEHFTPPTSDTGISLLKVAVHEIGHVLGLPHTYRTGSIMQPNYIPQEPAFELDWSDRKAIQKLYGSCEGSFDTAFDWIRKERNQYGEVMVRFSTYFFRNSWYWLYENRNNRTRYGDPIQILTGWPGIPTHNIDAFVHIWTWKRDERYFFQGNQYWRYDSDKDQALTEDEQGKSYPKLISEGFPGIPSPLDTAFYDRRQKLIYFFKESLVFAFDVNRNRVLNSYPKRITEVFPAVIPQNHPFRNIDSAYYSYAYNSIFFFKGNAYWKVVNDKDKQQNSWLPANGLFPKKFISEKWFDVCDVHISTLNM	Literature-reported	Selective inhibition of matrix metalloproteinase isozymes and in vivo protection against emphysema by substituted gamma-keto carboxylic acids. J Med Chem. 2006 Jan 26;49(2):456-8.	2.1	EC:3.4	.	peptidase M10A family.	3.4.24.-	Acting on peptide bonds (peptidases)	Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF00045; PF00413; PF01471	PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	.	.	.	Q8N119
TTUZ2L5	Matrix metalloproteinase-3 (MMP-3)	P08254	MMP3_HUMAN	Peptidase	Transin-1; Stromelysin-1; STMY1; SL-1; MMP-3	MMP3	"Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase."	EC 3.4.24.17	6N9D; 6MAV; 4JA1; 4G9L; 4DPE	MKSLPILLLLCVAVCSAYPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPVVKKIREMQKFLGLEVTGKLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGFFYFFTGSSQLEFDPNAKKVTHTLKSNSWLNC	Patented-recorded	Gelatinase inhibitors: a patent review (2011-2017).Expert Opin Ther Pat. 2018 Jan;28(1):31-46.	15.5	EC:3.4	Peptidase	peptidase M10A family.	3.4.24.17	Acting on peptide bonds (peptidases)	Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF00045; PF00413; PF01471	PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	hsa04668:TNF signaling pathway; hsa05202:Transcriptional misregulation in cancer; hsa05323:Rheumatoid arthritis	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	.	P08254
TTLW798	Stromelysin (SL)	P08254; P09238; P24347	MMP3_HUMAN; MMP10_HUMAN; MMP11_HUMAN	Peptidase	Transin; STMY; SL; Matrix metalloproteinase SL	MMP3	"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."	.	.	MKSLPILLLLCVAVCSAYPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPVVKKIREMQKFLGLEVTGKLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGFFYFFTGSSQLEFDPNAKKVTHTLKSNSWLNC	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	.	.	.	.	.	.	.	.	.	.	hsa04657: IL-17 signaling pathway; hsa04668: TNF signaling pathway; hsa05171: Coronavirus disease - COVID-19; hsa05202: Transcriptional misregulation in cancer; hsa05215: Prostate cancer; hsa05323: Rheumatoid arthritis; hsa05417: Lipid and atherosclerosis	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; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-9009391: Extra-nuclear estrogen signaling	.	P08254
TTMTWOS	Matrix metalloproteinase-7 (MMP-7)	P09237	MMP7_HUMAN	Peptidase	Uterine metalloproteinase; Pump-1 protease; PUMP1; Matrin; Matrilysin; MPSL1	MMP7	"Activates procollagenase. Degrades casein, gelatins of types I, III, IV, and V, and fibronectin."	EC 3.4.24.23	5UE5; 5UE2; 2Y6D; 2Y6C; 2MZI	MRLTVLCAVCLLPGSLALPLPQEAGGMSELQWEQAQDYLKRFYLYDSETKNANSLEAKLKEMQKFFGLPITGMLNSRVIEIMQKPRCGVPDVAEYSLFPNSPKWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAPGTGLGGDAHFDEDERWTDGSSLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYGKRSNSRKK	Successful	AG-3340 (Agouron Pharmaceuticals Inc). IDrugs. 2000 Mar;3(3):336-45.	34	EC:3.4	Peptidase	peptidase M10A family.	3.4.24.23	Acting on peptide bonds (peptidases)	Matrixin; Putative peptidoglycan binding domain	PF00413; PF01471	PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	hsa04310:Wnt signaling pathway	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	.	P09237
TTGA1IV	Matrix metalloproteinase-8 (MMP-8)	P22894	MMP8_HUMAN	Peptidase	PMNL-CL; PMNL collagenase; Neutrophil collagenase; CLG1	MMP8	"Can degrade fibrillar type I, II, and III collagens."	EC 3.4.24.34	5H8X; 4QKZ; 3TT4; 3DPF; 3DPE	MFSLKTLPFLLLLHVQISKAFPVSSKEKNTKTVQDYLEKFYQLPSNQYQSTRKNGTNVIVEKLKEMQRFFGLNVTGKPNEETLDMMKKPRCGVPDSGGFMLTPGNPKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDAEETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDIDGIQAIYGLSSNPIQPTGPSTPKPCDPSLTFDAITTLRGEILFFKDRYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWALSGYDILQGYPKDISNYGFPSSVQAIDAAVFYRSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGAFPGIESKVDAVFQQEHFFHVFSGPRYYAFDLIAQRVTRVARGNKWLNCRYG	Clinical trial	Matrix metalloproteinase inhibition lowers mortality and brain injury in experimental pneumococcal meningitis. Infect Immun. 2014 Apr;82(4):1710-8.	25	EC:3.4	Peptidase	peptidase M10A family.	3.4.24.34	Acting on peptide bonds (peptidases)	Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF00045; PF00413; PF01471	PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	.	R-HSA-1442490:Collagen degradation; R-HSA-1474228:Degradation of the extracellular matrix; R-HSA-1592389:Activation of Matrix Metalloproteinases	.	P22894
TT6X50U	Matrix metalloproteinase-9 (MMP-9)	P14780	MMP9_HUMAN	Peptidase	Matrix metalloproteinase 9; GELB; CLG4B; 92 kDa type IV collagenase; 92 kDa gelatinase	MMP9	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.	EC 3.4.24.35	6ESM; 5UE4; 5UE3; 5TH9; 5TH6	MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED	Clinical trial	Synthesis and biological evaluation of curcuminoid pyrazoles as new therapeutic agents in inflammatory bowel disease: effect on matrix metalloprote... Bioorg Med Chem. 2009 Feb 1;17(3):1290-6.	25	EC:3.4	Peptidase	peptidase M10A family.	3.4.24.35	Acting on peptide bonds (peptidases)	Fibronectin type II domain; Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF00040; PF00045; PF00413; PF01471	PF00040; fn2; PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	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	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	.	P14780
TT3TWY8	MMP9 messenger RNA (MMP9 mRNA)	P14780	MMP9_HUMAN	mRNA target	Matrix metalloproteinase 9 (mRNA); Gelatinase B (mRNA); GELB (mRNA); CLG4B (mRNA); 92 kDa type IV collagenase (mRNA); 92 kDa gelatinase (mRNA)	MMP9	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.	EC 3.4.24.35	6ESM; 5UE4; 5UE3; 5TH9; 5TH6	MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED	Literature-reported	NCBI GEO: archive for functional genomics data sets--update. Nucleic Acids Res. 2013 Jan;41(Database issue):D991-5.	.	mRNA	mRNA target	.	.	.	Fibronectin type II domain; Hemopexin; Matrixin; Putative peptidoglycan binding domain	PF00040; PF00045; PF00413; PF01471	PF00040; fn2; PF00045; Hemopexin; PF00413; Peptidase_M10; PF01471; PG_binding_1	.	.	hsa01522: Endocrine resistance; hsa04657: IL-17 signaling pathway; hsa04668: TNF signaling pathway; hsa04670: Leukocyte transendothelial migration; hsa04915: Estrogen signaling pathway; hsa04926: Relaxin signaling pathway; hsa05161: Hepatitis B; hsa05200: Pathways in cancer; hsa05202: Transcriptional misregulation in cancer; hsa05205: Proteoglycans in cancer; hsa05206: MicroRNAs in cancer; hsa05215: Prostate cancer; hsa05219: Bladder cancer; hsa05415: Diabetic cardiomyopathy; hsa05417: Lipid and atherosclerosis; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-1433557: Signaling by SCF-KIT; 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; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6798695: Neutrophil degranulation; R-HSA-9009391: Extra-nuclear estrogen signaling	.	P14780
TTYUK4F	Myelin-associated/oligodendrocyte basic protein (MOBP)	Q13875	MOBP_HUMAN	.	Myelin-associated oligodendrocyte basic protein	MOBP	"May play a role in compacting or stabilizing the myelin sheath, possibly by binding the negatively charged acidic phospholipids of the cytoplasmic membrane."	.	.	MSQKPAKEGPRLSKNQKYSEHFSIHCCPPFTFLNSKKEIVDRKYSICKSGCFYQKKEEDWICCACQKTRTSRRAKSPQRPKQQPAAPPAVVRAPAKPRSPPRSERQPRSPPRSERQPRSPPRSERQPRSPPRSERQPRPRPEVRPPPAKQRPPQKSKQQPRSSPLRGPGASRGGSPVKASRFW	Literature-reported	The central nervous system-specific myelin oligodendrocytic basic protein (MOBP) is encephalitogenic and a potential target antigen in multiple scl... J Neuroimmunol. 2000 Jan 24;102(2):189-98.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-8986944: Transcriptional Regulation by MECP2	.	Q13875
TTH13AB	Cyclic pyranopterin monophosphate synthase (MOCS1)	Q9NZB8	MOCS1_HUMAN	.	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)	MOCS1	"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)."	.	.	MAARPLSRMLRRLLRSSARSCSSGAPVTQPCPGESARAASEEVSRRRQFLREHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFDGNKWNFKKMVSYKEMLDTVRQQWPELEKVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAGMFSISQMKNRPMILIELFLMFPNSPPANPSIFSWDPLHVQGLRPRMSFSSQVATLWKGCRVPQTPPLAQQRLGSGSFQRHYTSRADSDANSKCLSPGSWASAAPSGPQLTSEQLTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSHIQVQLELDSTRHAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRGDFHRA	Clinical trial	ClinicalTrials.gov (NCT02047461) Safety & Efficacy Study of ALXN1101 in Pediatric Patients With MoCD Type A Currently Treated With rcPMP. U.S. National Institutes of Health.	24	.	.	.	.	.	.	.	.	.	.	hsa00790: Folate biosynthesis; hsa01100: Metabolic pathways; hsa01240: Biosynthesis of cofactors	R-HSA-947581: Molybdenum cofactor biosynthesis	.	Q9NZB8
TTQAFX5	Myelin-oligodendrocyte glycoprotein (MOG)	Q16653	MOG_HUMAN	Immunoglobulin	Myelinoligodendrocyte glycoprotein; MOG	MOG	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}.	.	1Q70	MASLSRPSLPSCLCSFLLLLLLQVSSSYAGQFRVIGPRHPIRALVGDEVELPCRISPGKNATGMEVGWYRPPFSRVVHLYRNGKDQDGDQAPEYRGRTELLKDAIGEGKVTLRIRNVRFSDEGGFTCFFRDHSYQEEAAMELKVEDPFYWVSPGVLVLLAVLPVLLLQITVGLIFLCLQYRLRGKLRAEIENLHRTFDPHFLRVPCWKITLFVIVPVLGPLVALIICYNWLHRRLAGQFLEELRNPF	Literature-reported	HLA class II transgenic mice authenticate restriction of myelin oligodendrocyte glycoprotein-specific immune response implicated in multiple sclero... Int Immunol. 2003 Apr;15(4):535-46.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q16653
TTN17BP	2-acylglycerol O-acyltransferase 2 (MOGAT2)	Q3SYC2	MOGT2_HUMAN	.	Acyl-CoA:monoacylglycerol acyltransferase 2; MGAT2; hMGAT2; Diacylglycerol O-acyltransferase candidate 5; hDC5; Diacylglycerol acyltransferase 2-like protein 5; Monoacylglycerol O-acyltransferase 2	MOGAT2	"Catalyzes the formation of diacylglycerol from 2-monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity. Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (PubMed:28420705). {ECO:0000269|PubMed:12621063, ECO:0000269|PubMed:27184406, ECO:0000269|PubMed:28420705}."	EC 2.3.1.22	.	MVEFAPLFMPWERRLQTLAVLQFVFSFLALAEICTVGFIALLFTRFWLLTVLYAAWWYLDRDKPRQGGRHIQAIRCWTIWKYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFANLCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAHILNRKGGGNLLGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSGSWLRYIQNRLQKIMGISLPLFHGRGVFQYSFGLIPYRRPITTVVGKPIEVQKTLHPSEEEVNQLHQRYIKELCNLFEAHKLKFNIPADQHLEFC	Clinical trial	"ClinicalTrials.gov (NCT05247970) A Phase 1 Randomized, Double-blind, Single and Multiple-dose Study to Assess the Safety, Tolerability, Pharmacokinetics, Food Effect, and Drug-Drug Interactions of S-309309 in Healthy and Obese Adult Study Participants. U.S.National Institutes of Health."	.	.	.	.	.	.	.	.	.	.	.	hsa:80168	R-HSA-75109;	.	Q3SYC2;
TTIHYA4	Thrombopoietin receptor (MPL)	P40238	TPOR_HUMAN	Cytokine receptor	TPOR; TPO-R; Proto-oncogene c-Mpl; Myeloproliferative leukemia protein; CD110 antigen; CD110; C-mpl	MPL	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.	.	.	MPSWALFMVTSCLLLAPQNLAQVSSQDVSLLASDSEPLKCFSRTFEDLTCFWDEEEAAPSGTYQLLYAYPREKPRACPLSSQSMPHFGTRYVCQFPDQEEVRLFFPLHLWVKNVFLNQTRTQRVLFVDSVGLPAPPSIIKAMGGSQPGELQISWEEPAPEISDFLRYELRYGPRDPKNSTGPTVIQLIATETCCPALQRPHSASALDQSPCAQPTMPWQDGPKQTSPSREASALTAEGGSCLISGLQPGNSYWLQLRSEPDGISLGGSWGSWSLPVTVDLPGDAVALGLQCFTLDLKNVTCQWQQQDHASSQGFFYHSRARCCPRDRYPIWENCEEEEKTNPGLQTPQFSRCHFKSRNDSIIHILVEVTTAPGTVHSYLGSPFWIHQAVRLPTPNLHWREISSGHLELEWQHPSSWAAQETCYQLRYTGEGHQDWKVLEPPLGARGGTLELRPRSRYRLQLRARLNGPTYQGPWSSWSDPTRVETATETAWISLVTALHLVLGLSAVLGLLLLRWQFPAHYRRLRHALWPSLPDLHRVLGQYLRDTAALSPPKATVSDTCEEVEPSLLEILPKSSERTPLPLCSSQAQMDYRRLQPSCLGTMPLSVCPPMAESGSCCTTHIANHSYLPLSYWQQP	Successful	Emerging drugs for idiopathic thrombocytopenic purpura in adults. Expert Opin Emerg Drugs. 2008 Jun;13(2):237-54.	34	Cytokine receptor	Cytokine receptor	type I cytokine receptor family. Type 1 subfamily.	.	.	"Erythropoietin receptor, ligand binding; Fibronectin type III domain"	PF09067; PF00041	PF09067; EpoR_lig-bind; PF00041; fn3	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04630:Jak-STAT signaling pathway	R-HSA-76009: Platelet Aggregation (Plug Formation)	.	P40238
TTVCZPI	Myeloperoxidase (MPO)	P05164	PERM_HUMAN	Peroxidases	MPO	MPO	"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."	EC 1.11.2.2	6BMT; 6AZP; 5UZU; 5MFA; 5FIW	MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTSLVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLHVALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMCNNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTDQLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFVNCSTLPALNLASWREAS	Clinical trial	"In vitro antibacterial activity of E-101 Solution, a novel myeloperoxidase-mediated antimicrobial, against Gram-positive and Gram-negative pathogens. J Antimicrob Chemother. 2011 Feb;66(2):335-42."	25	.	.	.	.	.	.	.	.	.	.	hsa04145:Phagosome; hsa05202:Transcriptional misregulation in cancer	R-HSA-6798695: Neutrophil degranulation; R-HSA-8941413: Events associated with phagocytolytic activity of PMN cells	MetaCyc:HS00140-MON	P05164
TTKV8W5	HUMAN mannose receptor (MRC1)	P22897	MRC1_HUMAN	Fibronectin protein	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	MRC1	Binds both sulfated and non-sulfated polysaccharide chains. Mediates the endocytosis of glycoproteins by macrophages.	.	5XTW; 5XTS; 1EGI; 1EGG	MRLPLLLVFASVIPGAVLLLDTRQFLIYNEDHKRCVDAVSPSAVQTAACNQDAESQKFRWVSESQIMSVAFKLCLGVPSKTDWVAITLYACDSKSEFQKWECKNDTLLGIKGEDLFFNYGNRQEKNIMLYKGSGLWSRWKIYGTTDNLCSRGYEAMYTLLGNANGATCAFPFKFENKWYADCTSAGRSDGWLWCGTTTDYDTDKLFGYCPLKFEGSESLWNKDPLTSVSYQINSKSALTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSGLWIGLNSLSFNSGWQWSDRSPFRYLNWLPGSPSAEPGKSCVSLNPGKNAKWENLECVQKLGYICKKGNTTLNSFVIPSESDVPTHCPSQWWPYAGHCYKIHRDEKKIQRDALTTCRKEGGDLTSIHTIEELDFIISQLGYEPNDELWIGLNDIKIQMYFEWSDGTPVTFTKWLRGEPSHENNRQEDCVVMKGKDGYWADRGCEWPLGYICKMKSRSQGPEIVEVEKGCRKGWKKHHFYCYMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFVGLRPEKYFWTGLSDIQTKGTFQWTIEEEVRFTHWNSDMPGRKPGCVAMRTGIAGGLWDVLKCDEKAKFVCKHWAEGVTHPPKPTTTPEPKCPEDWGASSRTSLCFKLYAKGKHEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYHKLFWLGLTYGSPSEGFTWSDGSPVSYENWAYGEPNNYQNVEYCGELKGDPTMSWNDINCEHLNNWICQIQKGQTPKPEPTPAPQDNPPVTEDGWVIYKDYQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDAQSAYFIGLLISLDKKFAWMDGSKVDYVSWATGEPNFANEDENCVTMYSNSGFWNDINCGYPNAFICQRHNSSINATTVMPTMPSVPSGCKEGWNFYSNKCFKIFGFMEEERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFSAWTGLNDVNSEHTFLWTDGRGVHYTNWGKGYPGGRRSSLSYEDADCVVIIGGASNEAGKWMDDTCDSKRGYICQTRSDPSLTNPPATIQTDGFVKYGKSSYSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAFAWLQMETSNERVWIALNSNLTDNQYTWTDKWRVRYTNWAADEPKLKSACVYLDLDGYWKTAHCNESFYFLCKRSDEIPATEPPQLPGRCPESDHTAWIPFHGHCYYIESSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEPLKSKTNFWIGLFRNVEGTWLWINNSPVSFVNWNTGDPSGERNDCVALHASSGFWSNIHCSSYKGYICKRPKIIDAKPTHELLTTKADTRKMDPSKPSSNVAGVVIIVILLILTGAGLAAYFFYKKRRVHLPQEGAFENTLYFNSQSSPGTSDMKDLVGNIEQNEHSVI	.	A SARS-CoV-2-Human Protein-Protein Interaction Map Reveals Drug Targets and Potential Drug-Repurposing. March 2020	.	.	.	.	.	.	.	.	.	.	.	hsa04145: Phagosome; hsa05152: Tuberculosis	R-HSA-1236978: Cross-presentation of soluble exogenous antigens (endosomes); R-HSA-9637628: Modulation by Mtb of host immune system	.	P22897
TTMG71U	Mannose receptor (MRC1)	P22897	MRC1_HUMAN	Fibronectin protein	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	MRC1	Binds both sulfated and non-sulfated polysaccharide chains. Mediates the endocytosis of glycoproteins by macrophages.	.	5XTW; 5XTS; 1EGI; 1EGG	MRLPLLLVFASVIPGAVLLLDTRQFLIYNEDHKRCVDAVSPSAVQTAACNQDAESQKFRWVSESQIMSVAFKLCLGVPSKTDWVAITLYACDSKSEFQKWECKNDTLLGIKGEDLFFNYGNRQEKNIMLYKGSGLWSRWKIYGTTDNLCSRGYEAMYTLLGNANGATCAFPFKFENKWYADCTSAGRSDGWLWCGTTTDYDTDKLFGYCPLKFEGSESLWNKDPLTSVSYQINSKSALTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSGLWIGLNSLSFNSGWQWSDRSPFRYLNWLPGSPSAEPGKSCVSLNPGKNAKWENLECVQKLGYICKKGNTTLNSFVIPSESDVPTHCPSQWWPYAGHCYKIHRDEKKIQRDALTTCRKEGGDLTSIHTIEELDFIISQLGYEPNDELWIGLNDIKIQMYFEWSDGTPVTFTKWLRGEPSHENNRQEDCVVMKGKDGYWADRGCEWPLGYICKMKSRSQGPEIVEVEKGCRKGWKKHHFYCYMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFVGLRPEKYFWTGLSDIQTKGTFQWTIEEEVRFTHWNSDMPGRKPGCVAMRTGIAGGLWDVLKCDEKAKFVCKHWAEGVTHPPKPTTTPEPKCPEDWGASSRTSLCFKLYAKGKHEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYHKLFWLGLTYGSPSEGFTWSDGSPVSYENWAYGEPNNYQNVEYCGELKGDPTMSWNDINCEHLNNWICQIQKGQTPKPEPTPAPQDNPPVTEDGWVIYKDYQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDAQSAYFIGLLISLDKKFAWMDGSKVDYVSWATGEPNFANEDENCVTMYSNSGFWNDINCGYPNAFICQRHNSSINATTVMPTMPSVPSGCKEGWNFYSNKCFKIFGFMEEERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFSAWTGLNDVNSEHTFLWTDGRGVHYTNWGKGYPGGRRSSLSYEDADCVVIIGGASNEAGKWMDDTCDSKRGYICQTRSDPSLTNPPATIQTDGFVKYGKSSYSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAFAWLQMETSNERVWIALNSNLTDNQYTWTDKWRVRYTNWAADEPKLKSACVYLDLDGYWKTAHCNESFYFLCKRSDEIPATEPPQLPGRCPESDHTAWIPFHGHCYYIESSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEPLKSKTNFWIGLFRNVEGTWLWINNSPVSFVNWNTGDPSGERNDCVALHASSGFWSNIHCSSYKGYICKRPKIIDAKPTHELLTTKADTRKMDPSKPSSNVAGVVIIVILLILTGAGLAAYFFYKKRRVHLPQEGAFENTLYFNSQSSPGTSDMKDLVGNIEQNEHSVI	Literature-reported	Involvement of mannose receptor in the preventive effects of mannose in lipopolysaccharide-induced acute lung injury. Eur J Pharmacol. 2010 Sep 1;641(2-3):229-37.	.	Fibronectin	Fibronectin	.	.	.	Fibronectin type II domain; Lectin C-type domain; Ricin-type beta-trefoil lectin domain	PF00040; PF00059; PF00652	PF00040; fn2; PF00059; Lectin_C; PF00652; Ricin_B_lectin	.	.	hsa04145: Phagosome; hsa05152: Tuberculosis	R-HSA-1236978: Cross-presentation of soluble exogenous antigens (endosomes); R-HSA-9637628: Modulation by Mtb of host immune system	.	P22897
TTYVR8M	Endocytic receptor Endo180 (MRC2)	Q9Y5P9	MRC2_HUMAN	.	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	MRC2	"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)."	.	5EW6; 5E4L; 5E4K; 5AO6; 5AO5	MGPGRPAPAPWPRHLLRCVLLLGCLHLGRPGAPGDAALPEPNVFLIFSHGLQGCLEAQGGQVRVTPACNTSLPAQRWKWVSRNRLFNLGTMQCLGTGWPGTNTTASLGMYECDREALNLRWHCRTLGDQLSLLLGARTSNISKPGTLERGDQTRSGQWRIYGSEEDLCALPYHEVYTIQGNSHGKPCTIPFKYDNQWFHGCTSTGREDGHLWCATTQDYGKDERWGFCPIKSNDCETFWDKDQLTDSCYQFNFQSTLSWREAWASCEQQGADLLSITEIHEQTYINGLLTGYSSTLWIGLNDLDTSGGWQWSDNSPLKYLNWESDQPDNPSEENCGVIRTESSGGWQNRDCSIALPYVCKKKPNATAEPTPPDRWANVKVECEPSWQPFQGHCYRLQAEKRSWQESKKACLRGGGDLVSIHSMAELEFITKQIKQEVEELWIGLNDLKLQMNFEWSDGSLVSFTHWHPFEPNNFRDSLEDCVTIWGPEGRWNDSPCNQSLPSICKKAGQLSQGAAEEDHGCRKGWTWHSPSCYWLGEDQVTYSEARRLCTDHGSQLVTITNRFEQAFVSSLIYNWEGEYFWTALQDLNSTGSFFWLSGDEVMYTHWNRDQPGYSRGGCVALATGSAMGLWEVKNCTSFRARYICRQSLGTPVTPELPGPDPTPSLTGSCPQGWASDTKLRYCYKVFSSERLQDKKSWVQAQGACQELGAQLLSLASYEEEHFVANMLNKIFGESEPEIHEQHWFWIGLNRRDPRGGQSWRWSDGVGFSYHNFDRSRHDDDDIRGCAVLDLASLQWVAMQCDTQLDWICKIPRGTDVREPDDSPQGRREWLRFQEAEYKFFEHHSTWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKFSRAQEQHWWIGLHTSESDGRFRWTDGSIINFISWAPGKPRPVGKDKKCVYMTASREDWGDQRCLTALPYICKRSNVTKETQPPDLPTTALGGCPSDWIQFLNKCFQVQGQEPQSRVKWSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTFDLWIGLHASQRDFQWVEQEPLMYANWAPGEPSGPSPAPSGNKPTSCAVVLHSPSAHFTGRWDDRSCTEETHGFICQKGTDPSLSPSPAALPPAPGTELSYLNGTFRLLQKPLRWHDALLLCESRNASLAYVPDPYTQAFLTQAARGLRTPLWIGLAGEEGSRRYSWVSEEPLNYVGWQDGEPQQPGGCTYVDVDGAWRTTSCDTKLQGAVCGVSSGPPPPRRISYHGSCPQGLADSAWIPFREHCYSFHMELLLGHKEARQRCQRAGGAVLSILDEMENVFVWEHLQSYEGQSRGAWLGMNFNPKGGTLVWQDNTAVNYSNWGPPGLGPSMLSHNSCYWIQSNSGLWRPGACTNITMGVVCKLPRAEQSSFSPSALPENPAALVVVLMAVLLLLALLTAALILYRRRQSIERGAFEGARYSRSSSSPTEATEKNILVSDMEMNEQQE	Literature-reported	The C-type lectin receptor Endo180 displays internalization and recycling properties distinct from other members of the mannose receptor family. J Biol Chem. 2002 Aug 30;277(35):32320-31.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9UBG0
TTIX6PK	Mas-related G protein-coupled receptor X1 (MRGX1)	Q96LB2	MRGX1_HUMAN	.	Sensory neuron-specific G-protein coupled receptor 3/4; SNSR4; SNSR3; Mas-related G-protein coupled receptor member X1; MRGX1	MRGPRX1	"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."	.	.	MDPTISTLDTELTPINGTEETLCYKQTLSLTVLTCIVSLVGLTGNAVVLWLLGCRMRRNAFSIYILNLAAADFLFLSGRLIYSLLSFISIPHTISKILYPVMMFSYFAGLSFLSAVSTERCLSVLWPIWYRCHRPTHLSAVVCVLLWALSLLRSILEWMLCGFLFSGADSAWCQTSDFITVAWLIFLCVVLCGSSLVLLIRILCGSRKIPLTRLYVTILLTVLVFLLCGLPFGIQFFLFLWIHVDREVLFCHVHLVSIFLSALNSSANPIIYFFVGSFRQRQNRQNLKLVLQRALQDASEVDEGGGQLPEEILELSGSRLEQ	Literature-reported	Targeting human Mas-related G protein-coupled receptor X1 to inhibit persistent pain. Proc Natl Acad Sci U S A. 2017 Mar 7;114(10):E1996-E2005.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q96LB2
TT3YV20	Mas-related gene 2 (MRGX2)	Q96LB1	MRGX2_HUMAN	GPCR rhodopsin	Masrelated Gprotein coupled receptormember X2; MRGPRX2	MRGPRX2	"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}."	.	.	MDPTTPAWGTESTTVNGNDQALLLLCGKETLIPVFLILFIALVGLVGNGFVLWLLGFRMRRNAFSVYVLSLAGADFLFLCFQIINCLVYLSNFFCSISINFPSFFTTVMTCAYLAGLSMLSTVSTERCLSVLWPIWYRCRRPRHLSAVVCVLLWALSLLLSILEGKFCGFLFSDGDSGWCQTFDFITAAWLIFLFMVLCGSSLALLVRILCGSRGLPLTRLYLTILLTVLVFLLCGLPFGIQWFLILWIWKDSDVLFCHIHPVSVVLSSLNSSANPIIYFFVGSFRKQWRLQQPILKLALQRALQDIAEVDHSEGCFRQGTPEMSRSSLV	Literature-reported	NCBI GEO: archive for functional genomics data sets--update. Nucleic Acids Res. 2013 Jan;41(Database issue):D991-5.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q96LB1
TTUQ7WN	Mitochondrial rRNA methyltransferase 2 (MRM2)	Q9UI43 	MRM2_HUMAN	Methyltransferase	"rRNA methyltransferase 2, mitochondrial; Protein ftsJ homolog 2; 16S rRNA [Um1369] 2'-O-methyltransferase; 16S rRNA (uridine(1369)-2'-O)-methyltransferase"	MRM2	"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."	EC 2.1.1.-	2NYU	MAGYLKLVCVSFQRQGFHTVGSRCKNRTGAEHLWLTRHLRDPFVKAAKVESYRCRSAFKLLEVNERHQILRPGLRVLDCGAAPGAWSQVAVQKVNAAGTDPSSPVGFVLGVDLLHIFPLEGATFLCPADVTDPRTSQRILEVLPGRRADVILSDMAPNATGFRDLDHDRLISLCLTLLSVTPDILQPGGTFLCKTWAGSQSRRLQRRLTEEFQNVRIIKPEASRKESSEVYFLATQYHGRKGTVKQ	Successful	In vitro activity of plazomicin against -lactamase-producing carbapenem-resistant Enterobacteriaceae (CRE).J Antimicrob Chemother. 2017 Oct 1;72(10):2792-2795. 	34	.	.	.	.	.	.	.	.	.	.	.	.	.	Q9UI43
TTUE541	Leukocyte surface antigen Leu-16 (CD20)	P11836	CD20_HUMAN	CD20 calcium channel	Membrane-spanning 4-domains subfamily A member 1; Leu-16; Bp35; B-lymphocyte surface antigen B1; B-lymphocyte antigen CD20	MS4A1	"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."	.	3PP4; 3BKY; 2OSL; 1S8B	MTTPRNSVNGTFPAEPMKGPIAMQSGPKPLFRRMSSLVGPTQSFFMRESKTLGAVQIMNGLFHIALGGLLMIPAGIYAPICVTVWYPLWGGIMYIISGSLLAATEKNSRKCLVKGKMIMNSLSLFAAISGMILSIMDILNIKISHFLKMESLNFIRAHTPYINIYNCEPANPSEKNSPSTQYCYSIQSLFLGILSVMLIFAFFQELVIAGIVENEWKRTCSRPKSNIVLLSAEEKKEQTIEIKEEVVGLTETSSQPKNEEDIEIIPIQEEEEEETETNFPEPPQDQESSPIENDSSP	Successful	[Contribution of radioimmunotherapy to the treatment of lymphoma]. Ann Pharm Fr. 2008 Nov-Dec;66(5-6):300-8.	34	TC=1.A.37	CD20 calcium channel	MS4A family.	.	.	CD20-like family	PF04103	PF04103; CD20	1.A.37.1.1	The CD20 Ca<sup>2+</sup> Channel (CD20) Family	hsa04640:Hematopoietic cell lineage	.	.	P11836
TTCAWRT	DNA mismatch repair protein MSH2 (MSH2)	P43246	MSH2_HUMAN	.	hMSH2; MutS protein homolog 2; Mismatch repair gene Msh2	MSH2	"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)."	.	3THZ; 3THY; 3THX; 3THW; 2O8F	MAVQPKETLQLESAAEVGFVRFFQGMPEKPTTTVRLFDRGDFYTAHGEDALLAAREVFKTQGVIKYMGPAGAKNLQSVVLSKMNFESFVKDLLLVRQYRVEVYKNRAGNKASKENDWYLAYKASPGNLSQFEDILFGNNDMSASIGVVGVKMSAVDGQRQVGVGYVDSIQRKLGLCEFPDNDQFSNLEALLIQIGPKECVLPGGETAGDMGKLRQIIQRGGILITERKKADFSTKDIYQDLNRLLKGKKGEQMNSAVLPEMENQVAVSSLSAVIKFLELLSDDSNFGQFELTTFDFSQYMKLDIAAVRALNLFQGSVEDTTGSQSLAALLNKCKTPQGQRLVNQWIKQPLMDKNRIEERLNLVEAFVEDAELRQTLQEDLLRRFPDLNRLAKKFQRQAANLQDCYRLYQGINQLPNVIQALEKHEGKHQKLLLAVFVTPLTDLRSDFSKFQEMIETTLDMDQVENHEFLVKPSFDPNLSELREIMNDLEKKMQSTLISAARDLGLDPGKQIKLDSSAQFGYYFRVTCKEEKVLRNNKNFSTVDIQKNGVKFTNSKLTSLNEEYTKNKTEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAQLDAVVSFAHVSNGAPVPYVRPAILEKGQGRIILKASRHACVEVQDEIAFIPNDVYFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISEYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPKHVIECAKQKALELEEFQYIGESQGYDIMEPAAKKCYLEREQGEKIIQEFLSKVKQMPFTEMSEENITIKLKQLKAEVIAKNNSFVNEIISRIKVTT	Literature-reported	Mismatch repair gene Msh2 modifies the timing of early disease in Hdh(Q111) striatum. Hum Mol Genet. 2003 Feb 1;12(3):273-81.	.	.	.	DNA mismatch repair MutS family.	.	.	MutS domain I; MutS domain II; MutS domain III; MutS family domain IV; MutS domain V	PF01624; PF05188; PF05192; PF05190; PF00488	PF01624; MutS_I; PF05188; MutS_II; PF05192; MutS_III; PF05190; MutS_IV; PF00488; MutS_V	.	.	hsa01524: Platinum drug resistance; hsa03430: Mismatch repair; hsa05200: Pathways in cancer; hsa05210: Colorectal cancer	R-HSA-5358565: Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha); R-HSA-5358606: Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta); R-HSA-5632927: Defective Mismatch Repair Associated With MSH3; R-HSA-5632928: Defective Mismatch Repair Associated With MSH2; R-HSA-5632968: Defective Mismatch Repair Associated With MSH6; R-HSA-6796648: TP53 Regulates Transcription of DNA Repair Genes	.	P43246
TTSM4BA	RNA-binding protein Musashi-1 (MSI1)	O43347	MSI1H_HUMAN	.	RNA-binding protein Musashi homolog 1; Musashi-1	MSI1	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.	.	.	METDAPQPGLASPDSPHDPCKMFIGGLSWQTTQEGLREYFGQFGEVKECLVMRDPLTKRSRGFGFVTFMDQAGVDKVLAQSRHELDSKTIDPKVAFPRRAQPKMVTRTKKIFVGGLSVNTTVEDVKQYFEQFGKVDDAMLMFDKTTNRHRGFGFVTFESEDIVEKVCEIHFHEINNKMVECKKAQPKEVMSPTGSARGRSRVMPYGMDAFMLGIGMLGYPGFQATTYASRSYTGLAPGYTYQFPEFRVERTPLPSAPVLPELTAIPLTAYGPMAAAAAAAAVVRGTGSHPWTMAPPPGSTPSRTGGFLGTTSPGPMAELYGAANQDSGVSSYISAASPAPSTGFGHSLGGPLIATAFTNGYH	Literature-reported	The RNA-binding protein Musashi 1 stabilizes the oncotachykinin 1 mRNA in breast cancer cells to promote cell growth. FASEB J. 2016 Jan;30(1):149-59.	.	.	Musashi family	Musashi family.	.	.	"RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)"	PF00076	PF00076; RRM_1	.	.	hsa03015: mRNA surveillance pathway	R-HSA-9010553: Regulation of expression of SLITs and ROBOs	.	O43347
TTTXQF6	RNA-binding protein Musashi-2 (MSI2)	Q96DH6	MSI2H_HUMAN	.	RNA-binding protein Musashi homolog 2; Musashi-2	MSI2	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.	.	6DBP; 6C8U	MEANGSQGTSGSANDSQHDPGKMFIGGLSWQTSPDSLRDYFSKFGEIRECMVMRDPTTKRSRGFGFVTFADPASVDKVLGQPHHELDSKTIDPKVAFPRRAQPKMVTRTKKIFVGGLSANTVVEDVKQYFEQFGKVEDAMLMFDKTTNRHRGFGFVTFENEDVVEKVCEIHFHEINNKMVECKKAQPKEVMFPPGTRGRARGLPYTMDAFMLGMGMLGYPNFVATYGRGYPGFAPSYGYQFPGFPAAAYGPVAAAAVAAARGSGSNPARPGGFPGANSPGPVADLYGPASQDSGVGNYISAASPQPGSGFGHGIAGPLIATAFTNGYH	Discontinued	The Pluripotency Factor Musashi-2 Is a Novel Target for Lung Cancer Therapy.Ann Am Thorac Soc. 2018 Apr;15(Supplement_2):S124. 	12	.	RNA recognition motif	Musashi family.	.	.	"RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)"	PF00076	PF00076; RRM_1	.	.	hsa03015: mRNA surveillance pathway	R-HSA-9013418: RHOBTB2 GTPase cycle	.	Q96DH6
TT4RXME	Mesothelin (MSLN)	Q13421	MSLN_HUMAN	.	"Prepromegakaryocytepotentiating factor; Pre-pro-megakaryocyte-potentiating factor; Mesothelin, cleaved form; MPF; CAK1 antigen"	MSLN	Membrane-anchored forms may play a role in cellular adhesion.	.	4F3F	MALPTARPLLGSCGTPALGSLLFLLFSLGWVQPSRTLAGETGQEAAPLDGVLANPPNISSLSPRQLLGFPCAEVSGLSTERVRELAVALAQKNVKLSTEQLRCLAHRLSEPPEDLDALPLDLLLFLNPDAFSGPQACTRFFSRITKANVDLLPRGAPERQRLLPAALACWGVRGSLLSEADVRALGGLACDLPGRFVAESAEVLLPRLVSCPGPLDQDQQEAARAALQGGGPPYGPPSTWSVSTMDALRGLLPVLGQPIIRSIPQGIVAAWRQRSSRDPSWRQPERTILRPRFRREVEKTACPSGKKAREIDESLIFYKKWELEACVDAALLATQMDRVNAIPFTYEQLDVLKHKLDELYPQGYPESVIQHLGYLFLKMSPEDIRKWNVTSLETLKALLEVNKGHEMSPQAPRRPLPQVATLIDRFVKGRGQLDKDTLDTLTAFYPGYLCSLSPEELSSVPPSSIWAVRPQDLDTCDPRQLDVLYPKARLAFQNMNGSEYFVKIQSFLGGAPTEDLKALSQQNVSMDLATFMKLRTDAVLPLTVAEVQKLLGPHVEGLKAEERHRPVRDWILRQRQDDLDTLGLGLQGGIPNGYLVLDLSMQEALSGTPCLLGPGPVLTVLALLLASTLA	Clinical trial	"Phase II clinical trial of amatuximab, a chimeric antimesothelin antibody with pemetrexed and cisplatin in advanced unresectable pleural mesothelioma. Clin Cancer Res. 2014 Dec 1;20(23):5927-36."	21	.	Mesothelin	mesothelin family.	.	.	Pre-pro-megakaryocyte potentiating factor precursor (Mesothelin)	PF06060	PF06060; Mesothelin	.	.	.	R-HSA-163125: Post-translational modification: synthesis of GPI-anchored proteins; R-HSA-381426: Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs); R-HSA-8957275: Post-translational protein phosphorylation	.	Q13421
TTYH1ZK	Beta-microseminoprotein (MSMB)	P08118	MSMB_HUMAN	.	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	MSMB	"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."	.	3IX0; 2IZ3	MNVLLGSVVIFATFVTLCNASCYFIPNEGVPGDSTRKCMDLKGNKHPINSEWQTDNCETCTCYETEISCCTLVSTPVGYDKDNCQRIFKKEDCKYIVVEKKDPKKTCSVSEWII	Clinical trial	National Cancer Institute Drug Dictionary (drug id 600185).	17	.	.	.	.	.	.	.	.	.	.	.	.	.	P08118
TT2TDH9	Scavenger receptor A1 (MSR1)	P21757	MSRE_HUMAN	.	Macrophage scavenger receptor; Macrophage acetylated LDL receptor I and II; MSR1; CD204 antigen	MSR1	"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."	.	.	MEQWDHFHNQQEDTDSCSESVKFDARSMTALLPPNPKNSPSLQEKLKSFKAALIALYLLVFAVLIPLIGIVAAQLLKWETKNCSVSSTNANDITQSLTGKGNDSEEEMRFQEVFMEHMSNMEKRIQHILDMEANLMDTEHFQNFSMTTDQRFNDILLQLSTLFSSVQGHGNAIDEISKSLISLNTTLLDLQLNIENLNGKIQENTFKQQEEISKLEERVYNVSAEIMAMKEEQVHLEQEIKGEVKVLNNITNDLRLKDWEHSQTLRNITLIQGPPGPPGEKGDRGPTGESGPRGFPGPIGPPGLKGDRGAIGFPGSRGLPGYAGRPGNSGPKGQKGEKGSGNTLTPFTKVRLVGGSGPHEGRVEILHSGQWGTICDDRWEVRVGQVVCRSLGYPGVQAVHKAAHFGQGTGPIWLNEVFCFGRESSIEECKIRQWGTRACSHSEDAGVTCTL	Literature-reported	"2,4-Bis(octadecanoylamino)benzenesulfonic acid sodium salt as a novel scavenger receptor inhibitor with low molecular weight. Bioorg Med Chem Lett. 2004 Jun 7;14(11):2791-5."	0	.	.	.	.	.	.	.	.	.	.	hsa04145:Phagosome	R-HSA-3000480:Scavenging by Class A Receptors	.	P21757
TT1QUZV	Methionine-R-sulfoxide reductase B1 (MSRB1)	Q9NZV6	MSRB1_HUMAN	MsrB Met sulfoxide reductase family	Selenoprotein X; SelX; SEPX1; MsrB1	MSRB1	"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."	EC 1.8.4.12	3MAO	MSFCSFFGGEVFQNHFEPGVYVCAKCGYELFSSRSKYAHSSPWPAFTETIHADSVAKRPEHNRSEALKVSCGKCGNGLGHEFLNDGPKPGQSRFUIFSSSLKFVPKGKETSASQGH	Literature-reported	Methionine Sulfoxide Reductase B1 Regulates Hepatocellular Carcinoma Cell Proliferation and Invasion via the Mitogen-Activated Protein Kinase Pathw... Oxid Med Cell Longev. 2018 May 10;2018:5287971.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-5676934: Protein repair	.	.
TTBQ3OC	Macrophage-stimulating protein receptor (RON)	Q04912	RON_HUMAN	Kinase	p185Ron; Proteintyrosine kinase 8; Macrophagestimulating protein receptor beta chain; Macrophagestimulating protein receptor; MST1R; MSP receptor; CDw136; CD136	MST1R	"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."	EC 2.7.10.1	4QT8; 4FWW; 3PLS	MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVASPLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVTDDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGVGPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRHFPLLVSSSFSRVDLFNGLLGPVQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGQPVQRDVSRLGDHLLFASGDQVFQVPIQGPGCRHFLTCGRCLRAWHFMGCGWCGNMCGQQKECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSGLVPEGTHQVTVGQSPCRPLPKDSSKLRPVPRKDFVEEFECELEPLGTQAVGPTNVSLTVTNMPPGKHFRVDGTSVLRGFSFMEPVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVNGTECLLARVSEGQLLCATPPGATVASVPLSLQVGGAQVPGSWTFQYREDPVVLSISPNCGYINSHITICGQHLTSAWHLVLSFHDGLRAVESRCERQLPEQQLCRLPEYVVRDPQGWVAGNLSARGDGAAGFTLPGFRFLPPPHPPSANLVPLKPEEHAIKFEYIGLGAVADCVGINVTVGGESCQHEFRGDMVVCPLPPSLQLGQDGAPLQVCVDGECHILGRVVRPGPDGVPQSTLLGILLPLLLLVAALATALVFSYWWRRKQLVLPPNLNDLASLDQTAGATPLPILYSGSDYRSGLALPAIDGLDSTTCVHGASFSDSEDESCVPLLRKESIQLRDLDSALLAEVKDVLIPHERVVTHSDRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSALLGDHYVQLPATYMNLGPSTSHEMNVRPEQPQFSPMPGNVRRPRPLSEPPRPT	Clinical trial	"MK-2461, a novel multitargeted kinase inhibitor, preferentially inhibits the activated c-Met receptor. Cancer Res. 2010 Feb 15;70(4):1524-33."	19	.	.	.	.	.	.	.	.	.	.	hsa04020: Calcium signaling pathway	R-HSA-8852405: Signaling by MST1	.	Q04912
TTM8I2X	Myostatin (MSTN)	O14793	GDF8_HUMAN	.	GDF-8	MSTN	Acts specifically as a negative regulator of skeletal muscle growth.	.	5NXS; 5NTU; 5F3H; 5F3B	MQKLQLCVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACTWRQNTKSSRIEAIKIQILSKLRLETAPNISKDVIRQLLPKAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQVDGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVETPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS	Clinical trial	Follistatin Gene Delivery Enhances Muscle Growth and Strength in Nonhuman Primates. Sci Transl Med. 2009 November 11; 1(6): 6ra15.	19	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction	R-HSA-9617828: FOXO-mediated transcription of cell cycle genes	.	O14793
TTSWPH8	Growth/differentiation factor 8 (GDF-8)	O14793	GDF8_HUMAN	Growth factor	GDF8	MSTN	Acts specifically as a negative regulator of skeletal muscle growth.	.	5NXS; 5NTU; 5F3H; 5F3B	MQKLQLCVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACTWRQNTKSSRIEAIKIQILSKLRLETAPNISKDVIRQLLPKAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQVDGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVETPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS	Clinical trial	Myostatin inhibitors as therapies for muscle wasting associated with cancer and other disorders. Curr Opin Support Palliat Care. 2013 November; 7(4): 352-360.	21	Growth factor	Growth factor	TGF-beta family.	.	.	Transforming growth factor beta like domain; TGF-beta propeptide	PF00019; PF00688	PF00019; TGF_beta; PF00688; TGFb_propeptide	.	.	hsa04060: Cytokine-cytokine receptor interaction	R-HSA-9617828: FOXO-mediated transcription of cell cycle genes	.	O14793
TTO4HUS	Metastasis associated gene-1 (MTA1)	Q13330	MTA1_HUMAN	.	Metastasisassociated protein MTA1; Metastasis-associated protein MTA1	MTA1	"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."	.	6G16; 5ICN; 5FXY; 4PC0; 4PBZ	MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSTLIALADKHATLSVCYKAGPGADNGEEGEIEEEMENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTLLADKGEIRVGNRYQADITDLLKEGEEDGRDQSRLETQVWEAHNPLTDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISVNNVKAGVVNGTGAPGQSPGAGRACESCYTTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRSNMSPHGLPARSSGSPKFAMKTRQAFYLHTTKLTRIARRLCREILRPWHAARHPYLPINSAAIKAECTARLPEASQSPLVLKQAVRKPLEAVLRYLETHPRPPKPDPVKSVSSVLSSLTPAKVAPVINNGSPTILGKRSYEQHNGVDGNMKKRLLMPSRGLANHGQARHMGPSRNLLLNGKSYPTKVRLIRGGSLPPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPPRPPPPAPVNDEPIVIED	Literature-reported	Metastasis-associated gene 1 promotes invasion and migration potential of laryngeal squamous cell carcinoma cells. Oncol Lett. 2014 Feb;7(2):399-404.	.	.	.	.	.	.	BAH domain; ELM2 domain; GATA zinc finger; MTA R1 domain; Myb-like DNA-binding domain	PF01426; PF01448; PF00320; PF17226; PF00249	PF01426; BAH; PF01448; ELM2; PF00320; GATA; PF17226; MTA_R1; PF00249; Myb_DNA-binding	.	.	.	R-HSA-3214815: HDACs deacetylate histones; R-HSA-3232118: SUMOylation of transcription factors; R-HSA-427389: ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression; R-HSA-73762: RNA Polymerase I Transcription Initiation; R-HSA-8943724: Regulation of PTEN gene transcription; R-HSA-9679191: Potential therapeutics for SARS	.	Q13330
TTDBX7N	S-methyl-5'-thioadenosine phosphorylase (MTAP)	Q13126	MTAP_HUMAN	Glycosyltransferases	Methylthioadenosine phosphorylase; MTAPase; MTA phosphorylase; MSAP; 5'-methylthioadenosine phosphorylase	MTAP	"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."	EC 2.4.2.28	6DZ3; 6DZ2; 6DZ0; 6DYZ; 5TC8	MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTMRPQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	2	EC:2.4	Pentosyltransferase	PNP/MTAP phosphorylase family. MTAP subfamily.	2.4.2.28 	Glycosyltransferases	Phosphorylase superfamily	PF01048	PF01048; PNP_UDP_1	.	.	hsa00270:Cysteine and methionine metabolism; hsa01100:Metabolic pathways	R-HSA-1237112: Methionine salvage pathway; R-HSA-8950505: Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation	MetaCyc:HS01913-MON	Q13126
TTH6SA5	Metastasis adhesion protein (MTDH)	Q86UE4	LYRIC_HUMAN	.	Protein LYRIC; Metadherin; Lysine-rich CEACAM1 co-isolated protein; LYRIC; Astrocyte elevated gene-1 protein; AEG1; AEG-1; 3D3/LYRIC	MTDH	"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."	.	4QMG	MAARSWQDELAQQAEEGSARLREMLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALGLLLLFLLGYGWAAACAGARKKRRSPPRKREEAAAVPAAAPDDLALLKNLRSEEQKKKNRKKLSEKPKPNGRTVEVAEGEAVRTPQSVTAKQPPEIDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFPVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENLTVNGGGWNEKSVKLSSQISAGEEKWNSVSPASAGKRKTEPSAWSQDTGDANTNGKDWGRSWSDRSIFSGIGSTAEPVSQSTTSDYQWDVSRNQPYIDDEWSGLNGLSSADPNSDWNAPAEEWGNWVDEERASLLKSQEPIPDDQKVSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSTAQDTEELEKEIREDLPVNTSKTRPKQEKAFSLKTISTSDPAEVLVKNSQPIKTLPPATSTEPSVILSKSDSDKSSSQVPPILQETDKSKSNTKQNSVPPSQTKSETSWESPKQIKKKKKARRET	Literature-reported	"AEG-1/MTDH/LYRIC: A Promiscuous Protein Partner Critical in Cancer, Obesity, and CNS Diseases. Adv Cancer Res. 2016;131:97-132."	.	.	.	.	.	.	Lysine-rich CEACAM1 co-isolated protein family	PF15686	PF15686; LYRIC	.	.	.	.	.	Q86UE4
TTTQDEO	Metal regulatory transcription factor 1 (MTF1)	Q14872	MTF1_HUMAN	Zinc-finger	Transcription factor MTF1; MTF1; MREbinding transcription factor	MTF1	Activates the metallothionein I promoter. Binds to the metal responsive element (MRE).	.	.	MGEHSPDNNIIYFEAEEDELTPDDKMLRFVDKNGLVPSSSGTVYDRTTVLIEQDPGTLEDEDDDGQCGEHLPFLVGGEEGFHLIDHEAMSQGYVQHIISPDQIHLTINPGSTPMPRNIEGATLTLQSECPETKRKEVKRYQCTFEGCPRTYSTAGNLRTHQKTHRGEYTFVCNQEGCGKAFLTSYSLRIHVRVHTKEKPFECDVQGCEKAFNTLYRLKAHQRLHTGKTFNCESEGCSKYFTTLSDLRKHIRTHTGEKPFRCDHDGCGKAFAASHHLKTHVRTHTGERPFFCPSNGCEKTFSTQYSLKSHMKGHDNKGHSYNALPQHNGSEDTNHSLCLSDLSLLSTDSELRENSSTTQGQDLSTISPAIIFESMFQNSDDTAIQEDPQQTASLTESFNGDAESVSDVPPSTGNSASLSLPLVLQPGLSEPPQPLLPASAPSAPPPAPSLGPGSQQAAFGNPPALLQPPEVPVPHSTQFAANHQEFLPHPQAPQPIVPGLSVVAGASASAAAVASAVAAPAPPQSTTEPLPAMVQTLPLGANSVLTNNPTITITPTPNTAILQSSLVMGEQNLQWILNGATSSPQNQEQIQQASKVEKVFFTTAVPVASSPGSSVQQIGLSVPVIIIKQEEACQCQCACRDSAKERASSRRKGCSSPPPPEPSPQAPDGPSLQLPAQTFSSAPVPGSSSSTLPSSCEQSRQAETPSDPQTETLSAMDVSEFLSLQSLDTPSNLIPIEALLQGEEEMGLTSSFSK	Literature-reported	Knockout of MTF1 Inhibits the Epithelial to Mesenchymal Transition in Ovarian Cancer Cells. J Cancer. 2018 Nov 11;9(24):4578-4585.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1989781: PPARA activates gene expression; R-HSA-2426168: Activation of gene expression by SREBF (SREBP); R-HSA-5660489: MTF1 activates gene expression	.	Q14872
TTFZW07	NAD-dependent methylenetetrahydrofolate dehydrogenase (NMD)	P13995; Q9H903	MTDC_HUMAN; MTD2L_HUMAN	.	Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase	MTHFD2	"Although its dehydrogenase activity is NAD-specific, it can also utilize NADP at a reduced efficiency."	.	.	MAATSLMSALAARLLQPAHSCSLRLRPFHLAAVRNEAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPASISEEELLNLINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVHDPVTAKPKLVGDVDFEGVRQKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKSKELGVATN	Literature-reported	NAD-dependent methylenetetrahydrofolate dehydrogenase is expressed by immortal cells. J Biol Chem. 1985 Nov 25;260(27):14616-20.	.	.	.	.	.	.	.	.	.	.	.	hsa00670: One carbon pool by folate; hsa01100: Metabolic pathways; hsa01240: Biosynthesis of cofactors	R-HSA-196757: Metabolism of folate and pterines	MetaCyc:HS00858-MON	P13995
TTQWOU1	MTHFR messenger RNA (MTHFR mRNA)	P42898	MTHR_HUMAN	mRNA target	Methylenetetrahydrofolate reductase (mRNA)	MTHFR	"Catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co-substrate for homocysteine remethylation to methionine."	EC 1.5.1.20	6FCX	MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWFSLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYCGLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVKHIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFVKACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIELAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREEDVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKMWGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGILTINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHLVNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYEEESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP	Literature-reported	Therapeutic target database update 2012: a resource for facilitating target-oriented drug discovery. Nucleic Acids Res. 2012 Jan;40(Database issue):D1128-36.	0	mRNA	mRNA target	.	.	.	Methylenetetrahydrofolate reductase	PF02219	PF02219; MTHFR	.	.	hsa00670:One carbon pool by folate; hsa01100:Metabolic pathways; hsa01200:Carbon metabolism	R-HSA-196757:Metabolism of folate and pterines	MetaCyc:HS11117-MON	P42898
TTY2TCU	Myotubularin (MTM1)	Q13496	MTM1_HUMAN	Phosphoric monoester hydrolase	MTM1	MTM1	"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."	EC 3.1.3.95	.	MASASTSKYNSHSLENESIKRTSRDGVNRDLTEAVPRLPGETLITDKEVIYICPFNGPIKGRVYITNYRLYLRSLETDSSLILDVPLGVISRIEKMGGATSRGENSYGLDITCKDMRNLRFALKQEGHSRRDMFEILTRYAFPLAHSLPLFAFLNEEKFNVDGWTVYNPVEEYRRQGLPNHHWRITFINKCYELCDTYPALLVVPYRASDDDLRRVATFRSRNRIPVLSWIHPENKTVIVRCSQPLVGMSGKRNKDDEKYLDVIRETNKQISKLTIYDARPSVNAVANKATGGGYESDDAYHNAELFFLDIHNIHVMRESLKKVKDIVYPNVEESHWLSSLESTHWLEHIKLVLTGAIQVADKVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSFYRSIEGFEILVQKEWISFGHKFASRIGHGDKNHTDADRSPIFLQFIDCVWQMSKQFPTAFEFNEQFLIIILDHLYSCRFGTFLFNCESARERQKVTERTVSLWSLINSNKEKFKNPFYTKEINRVLYPVASMRHLELWVNYYIRWNPRIKQQQPNPVEQRYMELLALRDEYIKRLEELQLANSAKLSDPPTSPSSPSQMMPHVQTHF	Literature-reported	Expression of myotubularin by an adenoviral vector demonstrates its function as a phosphatidylinositol 3-phosphate [PtdIns(3)P] phosphatase in musc... Mol Endocrinol. 2003 Dec;17(12):2448-60.	.	.	.	.	.	.	.	.	.	.	.	hsa00562: Inositol phosphate metabolism; hsa01100: Metabolic pathways; hsa04070: Phosphatidylinositol signaling system	R-HSA-1660499: Synthesis of PIPs at the plasma membrane; R-HSA-1660516: Synthesis of PIPs at the early endosome membrane; R-HSA-1660517: Synthesis of PIPs at the late endosome membrane	.	Q13496
TTHDERA	Myotubularin-related protein 1 (MTMR1)	Q13613	MTMR1_HUMAN	Phosphoric monoester hydrolase	MTMR1	MTMR1	"Lipid phosphatase that has high specificity for phosphatidylinositol 3-phosphate and has no activity with phosphatidylinositol (3,5)-bisphosphate."	EC 3.1.3.95	5C16	MDRPAAAAAAGCEGGGGPNPGPAGGRRPPRAAGGATAGSRQPSVETLDSPTGSHVEWCKQLIAATISSQISGSVTSENVSRDYKALRDGNKLAQMEEAPLFPGESIKAIVKDVMYICPFMGAVSGTLTVTDFKLYFKNVERDPHFILDVPLGVISRVEKIGAQSHGDNSCGIEIVCKDMRNLRLAYKQEEQSKLGIFENLNKHAFPLSNGQALFAFSYKEKFPINGWKVYDPVSEYKRQGLPNESWKISKINSNYEFCDTYPAIIVVPTSVKDDDLSKVAAFRAKGRVPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYLQTIMDANAQSHKLIIFDARQNSVADTNKTKGGGYESESAYPNAELVFLEIHNIHVMRESLRKLKEIVYPSIDEARWLSNVDGTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGWDRTAQLTSLAMLMLDSYYRTIKGFETLVEKEWISFGHRFALRVGHGNDNHADADRSPIFLQFVDCVWQMTRQFPSAFEFNELFLITILDHLYSCLFGTFLCNCEQQRFKEDVYTKTISLWSYINSQLDEFSNPFFVNYENHVLYPVASLSHLELWVNYYVRWNPRMRPQMPIHQNLKELLAVRAELQKRVEGLQREVATRAVSSSSERGSSPSHSATSVHTSV	Literature-reported	Muscle-specific alternative splicing of myotubularin-related 1 gene is impaired in DM1 muscle cells. Hum Mol Genet. 2002 Sep 15;11(19):2297-307.	.	.	.	.	.	.	.	.	.	.	.	hsa00562: Inositol phosphate metabolism; hsa01100: Metabolic pathways; hsa04070: Phosphatidylinositol signaling system	R-HSA-1660499: Synthesis of PIPs at the plasma membrane; R-HSA-9035034: RHOF GTPase cycle	.	Q13613
TTTJF7V	NADH dehydrogenase (MT-ND3)	P03897	NU3M_HUMAN	NADH/NADPH oxidoreductase	ND; NADH-ubiquinone oxidoreductase; NADH; MTND; MT-ND3; MT-ND	MT-ND3	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.	EC 7.1.1.2	5XTD; 5XTC	MNFALILMINTLLALLLMIITFWLPQLNGYMEKSTPYECGFDPMSPARVPFSMKFFLVAITFLLFDLEIALLLPLPWALQTTNLPLMVMSSLLLIIILALSLAYEWLQKGLDWTE	Successful	Mechanism of cadmium-decreased glucuronidation in the rat. Biochem Pharmacol. 1992 Dec 1;44(11):2139-47.	34	.	.	.	.	.	.	.	.	.	.	hsa00190:Oxidative phosphorylation; hsa01100:Metabolic pathways; hsa05012:Parkinson's disease	R-HSA-611105: Respiratory electron transport; R-HSA-6799198: Complex I biogenesis	MetaCyc:HS00032-MON	P03897
TT0WAIE	Melatonin receptor type 1A (MTNR1A)	P48039	MTR1A_HUMAN	GPCR rhodopsin	Mel1a receptor; Mel1AR; Mel-1A-R	MTNR1A	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.	.	6ME5; 6ME4; 6ME3; 6ME2	MQGNGSALPNASQPVLRGDGARPSWLASALACVLIFTIVVDILGNLLVILSVYRNKKLRNAGNIFVVSLAVADLVVAIYPYPLVLMSIFNNGWNLGYLHCQVSGFLMGLSVIGSIFNITGIAINRYCYICHSLKYDKLYSSKNSLCYVLLIWLLTLAAVLPNLRAGTLQYDPRIYSCTFAQSVSSAYTIAVVVFHFLVPMIIVIFCYLRIWILVLQVRQRVKPDRKPKLKPQDFRNFVTMFVVFVLFAICWAPLNFIGLAVASDPASMVPRIPEWLFVASYYMAYFNSCLNAIIYGLLNQNFRKEYRRIIVSLCTARVFFVDSSNDVADRVKWKPSPLMTNNNVVKVDSV	Successful	The human MT1 melatonin receptor stimulates cAMP production in the human neuroblastoma cell line SH-SY5Y cells via a calcium-calmodulin signal transduction pathway. J Neuroendocrinol. 2005 Mar;17(3):170-8.	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	9.A.14.1.3	The G-protein-coupled receptor (GPCR) Family	hsa04080:Neuroactive ligand-receptor interaction; hsa04713:Circadian entrainment	R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418594:G alpha (i) signalling events	.	P48039
TT32JK8	Melatonin receptor type 1B (MTNR1B)	P49286	MTR1B_HUMAN	GPCR rhodopsin	Mel1b receptor; Mel1b melatonin receptor; Mel-1B-R	MTNR1B	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.	.	6ME9; 6ME8; 6ME7; 6ME6	MSENGSFANCCEAGGWAVRPGWSGAGSARPSRTPRPPWVAPALSAVLIVTTAVDVVGNLLVILSVLRNRKLRNAGNLFLVSLALADLVVAFYPYPLILVAIFYDGWALGEEHCKASAFVMGLSVIGSVFNITAIAINRYCYICHSMAYHRIYRRWHTPLHICLIWLLTVVALLPNFFVGSLEYDPRIYSCTFIQTASTQYTAAVVVIHFLLPIAVVSFCYLRIWVLVLQARRKAKPESRLCLKPSDLRSFLTMFVVFVIFAICWAPLNCIGLAVAINPQEMAPQIPEGLFVTSYLLAYFNSCLNAIVYGLLNQNFRREYKRILLALWNPRHCIQDASKGSHAEGLQSPAPPIIGVQHQADAL	Successful	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Ligand id: 7393).	34	PF00001	GPCR rhodopsin	G-protein coupled receptor 1 family.	.	.	7 transmembrane receptor (rhodopsin family)	PF00001	PF00001; 7tm_1	.	.	hsa04080:Neuroactive ligand-receptor interaction; hsa04713:Circadian entrainment	R-HSA-373076:Class A/1 (Rhodopsin-like receptors); R-HSA-418594:G alpha (i) signalling events	.	P49286
TTCJG29	Serine/threonine-protein kinase mTOR (mTOR)	P42345	MTOR_HUMAN	Kinase	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	MTOR	"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."	EC 2.7.11.1	6BCX; 6BCU; 5ZCS; 5WBY; 5WBU	MLGTGPAAATTAATTSSNVSVLQQFASGLKSRNEETRAKAAKELQHYVTMELREMSQEESTRFYDQLNHHIFELVSSSDANERKGGILAIASLIGVEGGNATRIGRFANYLRNLLPSNDPVVMEMASKAIGRLAMAGDTFTAEYVEFEVKRALEWLGADRNEGRRHAAVLVLRELAISVPTFFFQQVQPFFDNIFVAVWDPKQAIREGAVAALRACLILTTQREPKEMQKPQWYRHTFEEAEKGFDETLAKEKGMNRDDRIHGALLILNELVRISSMEGERLREEMEEITQQQLVHDKYCKDLMGFGTKPRHITPFTSFQAVQPQQSNALVGLLGYSSHQGLMGFGTSPSPAKSTLVESRCCRDLMEEKFDQVCQWVLKCRNSKNSLIQMTILNLLPRLAAFRPSAFTDTQYLQDTMNHVLSCVKKEKERTAAFQALGLLSVAVRSEFKVYLPRVLDIIRAALPPKDFAHKRQKAMQVDATVFTCISMLARAMGPGIQQDIKELLEPMLAVGLSPALTAVLYDLSRQIPQLKKDIQDGLLKMLSLVLMHKPLRHPGMPKGLAHQLASPGLTTLPEASDVGSITLALRTLGSFEFEGHSLTQFVRHCADHFLNSEHKEIRMEAARTCSRLLTPSIHLISGHAHVVSQTAVQVVADVLSKLLVVGITDPDPDIRYCVLASLDERFDAHLAQAENLQALFVALNDQVFEIRELAICTVGRLSSMNPAFVMPFLRKMLIQILTELEHSGIGRIKEQSARMLGHLVSNAPRLIRPYMEPILKALILKLKDPDPDPNPGVINNVLATIGELAQVSGLEMRKWVDELFIIIMDMLQDSSLLAKRQVALWTLGQLVASTGYVVEPYRKYPTLLEVLLNFLKTEQNQGTRREAIRVLGLLGALDPYKHKVNIGMIDQSRDASAVSLSESKSSQDSSDYSTSEMLVNMGNLPLDEFYPAVSMVALMRIFRDQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPTFLNVIRVCDGAIREFLFQQLGMLVSFVKSHIRPYMDEIVTLMREFWVMNTSIQSTIILLIEQIVVALGGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTDYASRIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGDALASGPVETGPMKKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQQDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINRVRDKLTGRDFSHDDTLDVPTQVELLIKQATSHENLCQCYIGWCPFW	Successful	Advances in kinase targeting: current clinical use and clinical trials. Trends Pharmacol Sci. 2014 Nov;35(11):604-20.	34	EC:2.7	Kinase	PI3/PI4-kinase family.	2.7.11.1 	Transferring phosphorus-containing groups	Domain of unknown function (DUF3385); FAT domain; FATC domain; FKBP12-rapamycin binding domain ; Phosphatidylinositol 3- and 4-kinase	PF11865; PF02259; PF02260; PF08771; PF00454	PF11865; DUF3385; PF02259; FAT; PF02260; FATC; PF08771; FRB_dom; PF00454; PI3_PI4_kinase	.	.	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	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	.	P42345
TT7HQAF	HUMAN mammalian target of rapamycin (mTOR)	P42345	MTOR_HUMAN	Kinase	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	MTOR	"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."	EC 2.7.11.1	6BCX; 6BCU; 5ZCS; 5WBY; 5WBU	MLGTGPAAATTAATTSSNVSVLQQFASGLKSRNEETRAKAAKELQHYVTMELREMSQEESTRFYDQLNHHIFELVSSSDANERKGGILAIASLIGVEGGNATRIGRFANYLRNLLPSNDPVVMEMASKAIGRLAMAGDTFTAEYVEFEVKRALEWLGADRNEGRRHAAVLVLRELAISVPTFFFQQVQPFFDNIFVAVWDPKQAIREGAVAALRACLILTTQREPKEMQKPQWYRHTFEEAEKGFDETLAKEKGMNRDDRIHGALLILNELVRISSMEGERLREEMEEITQQQLVHDKYCKDLMGFGTKPRHITPFTSFQAVQPQQSNALVGLLGYSSHQGLMGFGTSPSPAKSTLVESRCCRDLMEEKFDQVCQWVLKCRNSKNSLIQMTILNLLPRLAAFRPSAFTDTQYLQDTMNHVLSCVKKEKERTAAFQALGLLSVAVRSEFKVYLPRVLDIIRAALPPKDFAHKRQKAMQVDATVFTCISMLARAMGPGIQQDIKELLEPMLAVGLSPALTAVLYDLSRQIPQLKKDIQDGLLKMLSLVLMHKPLRHPGMPKGLAHQLASPGLTTLPEASDVGSITLALRTLGSFEFEGHSLTQFVRHCADHFLNSEHKEIRMEAARTCSRLLTPSIHLISGHAHVVSQTAVQVVADVLSKLLVVGITDPDPDIRYCVLASLDERFDAHLAQAENLQALFVALNDQVFEIRELAICTVGRLSSMNPAFVMPFLRKMLIQILTELEHSGIGRIKEQSARMLGHLVSNAPRLIRPYMEPILKALILKLKDPDPDPNPGVINNVLATIGELAQVSGLEMRKWVDELFIIIMDMLQDSSLLAKRQVALWTLGQLVASTGYVVEPYRKYPTLLEVLLNFLKTEQNQGTRREAIRVLGLLGALDPYKHKVNIGMIDQSRDASAVSLSESKSSQDSSDYSTSEMLVNMGNLPLDEFYPAVSMVALMRIFRDQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPTFLNVIRVCDGAIREFLFQQLGMLVSFVKSHIRPYMDEIVTLMREFWVMNTSIQSTIILLIEQIVVALGGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTDYASRIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGDALASGPVETGPMKKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQQDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINRVRDKLTGRDFSHDDTLDVPTQVELLIKQATSHENLCQCYIGWCPFW	.	Coronaviruses - drug discovery and therapeutic options. Nat Rev Drug Discov. 2016 May;15(5):327-47.	34	EC:2.7	Kinase	PI3/PI4-kinase family.	2.7.11.1 	Transferring phosphorus-containing groups	Domain of unknown function (DUF3385); FAT domain; FATC domain; FKBP12-rapamycin binding domain ; Phosphatidylinositol 3- and 4-kinase	PF11865; PF02259; PF02260; PF08771; PF00454	PF11865; DUF3385; PF02259; FAT; PF02260; FATC; PF08771; FRB_dom; PF00454; PI3_PI4_kinase	.	.	"hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa01522: Endocrine resistance; hsa04012: ErbB signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04072: Phospholipase D signaling pathway; hsa04136: Autophagy - other; hsa04140: Autophagy - animal; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04152: AMPK signaling pathway; hsa04211: Longevity regulating pathway; hsa04213: Longevity regulating pathway - multiple species; hsa04218: Cellular senescence; hsa04371: Apelin signaling pathway; hsa04613: Neutrophil extracellular trap formation; hsa04630: JAK-STAT signaling pathway; hsa04659: Th17 cell differentiation; hsa04714: Thermogenesis; hsa04910: Insulin signaling pathway; hsa04919: Thyroid hormone signaling pathway; hsa04920: Adipocytokine signaling pathway; hsa04930: Type II diabetes mellitus; hsa04931: Insulin resistance; hsa04935: Growth hormone synthesis, secretion and action; hsa05010: Alzheimer disease; hsa05014: Amyotrophic lateral sclerosis; hsa05016: Huntington disease; hsa05017: Spinocerebellar ataxia; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05131: Shigellosis; hsa05163: Human cytomegalovirus infection; hsa05165: Human papillomavirus infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05206: MicroRNAs in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05210: Colorectal cancer; hsa05212: Pancreatic cancer; hsa05214: Glioma; hsa05215: Prostate cancer; hsa05221: Acute myeloid leukemia; 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; hsa05415: Diabetic cardiomyopathy"	R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1632852: Macroautophagy; R-HSA-165159: MTOR signalling; R-HSA-166208: mTORC1-mediated signalling; R-HSA-3371571: HSF1-dependent transactivation; R-HSA-380972: Energy dependent regulation of mTOR by LKB1-AMPK; 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; R-HSA-6804757: Regulation of TP53 Degradation; R-HSA-8943724: Regulation of PTEN gene transcription; R-HSA-9639288: Amino acids regulate mTORC1	.	P42345
TTX4GLS	Mammalian target of rapamycin complex 1 (mTORC1)	P42345-Q8N122-Q9BVC4-Q96B36-Q8TB45	MTOR_HUMAN-RPTOR_HUMAN-LST8_HUMAN-AKTS1_HUMAN-DPTOR_HUMAN	.	mTORC1; Mechanistic target of rapamycin complex 1	MTOR-RPTORA-MLST8-KT1S1-DEPTOR	"Functions as a nutrient/energy/redox sensor and controls protein synthesis. Activate translation of proteins. Invovled in autophagy, lysosomal damage and reactive oxygen species."	.	.	MNTSPGTVGSDPVILATAGYDHTVRFWQAHSGICTRTVQHQDSQVNALEVTPDRSMIAAAGYQHIRMYDLNSNNPNPIISYDGVNKNIASVGFHEDGRWMYTGGEDCTARIWDLRSRNLQCQRIFQVNAPINCVCLHPNQAELIVGDQSGAIHIWDLKTDHNEQLIPEPEVSITSAHIDPDASYMAAVNSTGNCYVWNLTGGIGDEVTQLIPKTKIPAHTRYALQCRFSPDSTLLATCSADQTCKIWRTSNFSLMTELSIKSGNPGESSRGWMWGCAFSGDSQYIVTASSDNLARLWCVETGEIKREYGGHQKAVVCLAFNDSVLGMLGTGPAAATTAATTSSNVSVLQQFASGLKSRNEETRAKAAKELQHYVTMELREMSQEESTRFYDQLNHHIFELVSSSDANERKGGILAIASLIGVEGGNATRIGRFANYLRNLLPSNDPVVMEMASKAIGRLAMAGDTFTAEYVEFEVKRALEWLGADRNEGRRHAAVLVLRELAISVPTFFFQQVQPFFDNIFVAVWDPKQAIREGAVAALRACLILTTQREPKEMQKPQWYRHTFEEAEKGFDETLAKEKGMNRDDRIHGALLILNELVRISSMEGERLREEMEEITQQQLVHDKYCKDLMGFGTKPRHITPFTSFQAVQPQQSNALVGLLGYSSHQGLMGFGTSPSPAKSTLVESRCCRDLMEEKFDQVCQWVLKCRNSKNSLIQMTILNLLPRLAAFRPSAFTDTQYLQDTMNHVLSCVKKEKERTAAFQALGLLSVAVRSEFKVYLPRVLDIIRAALPPKDFAHKRQKAMQVDATVFTCISMLARAMGPGIQQDIKELLEPMLAVGLSPALTAVLYDLSRQIPQLKKDIQDGLLKMLSLVLMHKPLRHPGMPKGLAHQLASPGLTTLPEASDVGSITLALRTLGSFEFEGHSLTQFVRHCADHFLNSEHKEIRMEAARTCSRLLTPSIHLISGHAHVVSQTAVQVVADVLSKLLVVGITDPDPDIRYCVLASLDERFDAHLAQAENLQALFVALNDQVFEIRELAICTVGRLSSMNPAFVMPFLRKMLIQILTELEHSGIGRIKEQSARMLGHLVSNAPRLIRPYMEPILKALILKLKDPDPDPNPGVINNVLATIGELAQVSGLEMRKWVDELFIIIMDMLQDSSLLAKRQVALWTLGQLVASTGYVVEPYRKYPTLLEVLLNFLKTEQNQGTRREAIRVLGLLGALDPYKHKVNIGMIDQSRDASAVSLSESKSSQDSSDYSTSEMLVNMGNLPLDEFYPAVSMVALMRIFRDQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPTFLNVIRVCDGAIREFLFQQLGMLVSFVKSHIRPYMDEIVTLMREFWVMNTSIQSTIILLIEQIVVALGGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTDYASRIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGDALASGPVETGPMKKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQQDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINRVRDKLTGRDFSHDDTLDVPTQVELLIKQATSHENLCQCYIGWCPFWMESEMLQSPLLGLGEEDEADLTDWNLPLAFMKKRHCEKIEGSKSLAQSWRMKDRMKTVSVALVLCLNVGVDPPDVVKTTPCARLECWIDPLSMGPQKALETIGANLQKQYENWQPRARYKQSLDPTVDEVKKLCTSLRRNAKEERVLFHYNGHGVPRPTVNGEVWVFNKNYTQYIPLSIYDLQTWMGSPSIFVYDCSNAGLIVKSFKQFALQREQELEVAAINPNHPLAQMPLPPSMKNCIQLAACEATELLPMIPDLPADLFTSCLTTPIKIALRWFCMQKCVSLVPGVTLDLIEKIPGRLNDRRTPLGELNWIFTAITDTIAWNVLPRDLFQKLFRQDLLVASLFRNFLLAERIMRSYNCTPVSSPRLPPTYMHAMWQAWDLAVDICLSQLPTIIEEGTAFRHSPFFAEQLTAFQVWLTMGVENRNPPEQLPIVLQVLLSQVHRLRALDLLGRFLDLGPWAVSLALSVGIFPYVLKLLQSSARELRPLLVFIWAKILAVDSSCQADLVKDNGHKYFLSVLADPYMPAEHRTMTAFILAVIVNSYHTGQEACLQGNLIAICLEQLNDPHPLLRQWVAICLGRIWQNFDSARWCGVRDSAHEKLYSLLSDPIPEVRCAAVFALGTFVGNSAERTDHSTTIDHNVAMMLAQLVSDGSPMVRKELVVALSHLVVQYESNFCTVALQFIEEEKNYALPSPATTEGGSLTPVRDSPCTPRLRSVSSYGNIRAVATARSLNKSLQNLSLTEESGGAVAFSPGNLSTSSSASSTLGSPENEEHILSFETIDKMRRASSYSSLNSLIGVSFNSVYTQIWRVLLHLAADPYPEVSDVAMKVLNSIAYKATVNARPQRVLDTSSLTQSAPASPTNKGVHIHQAGGSPPASSTSSSSLTNDVAKQPVSRDLPSGRPGTTGPAGAQYTPHSHQFPRTRKMFDKGPEQTADDADDAAGHKSFISATVQTGFCDWSARYFAQPVMKIPEEHDLESQIRKEREWRFLRNSRVRRQAQQVIQKGITRLDDQIFLNRNPGVPSVVKFHPFTPCIAVADKDSICFWDWEKGEKLDYFHNGNPRYTRVTAMEYLNGQDCSLLLTATDDGAIRVWKNFADLEKNPEMVTAWQGLSDMLPTTRGAGMVVDWEQETGLLMSSGDVRIVRIWDTDREMKVQDIPTGADSCVTSLSCDSHRSLIVAGLGDGSIRVYDRRMALSECRVMTYREHTAWVVKASLQKRPDGHIVSVSVNGDVRIFDPRMPESVNVLQIVKGLTALDIHPQADLIACGSVNQFTAIYNSSGELINNIKYYDGFMGQRVGAISCLAFHPHWPHLAVGSNDYYISVYSVEKRVRMEEGGSTGSAGSDSSTSGSGGAQQRELERMAEVLVTGEQLRLRLHEEKVIKDRRHHLKTYPNCFVAKELIDWLIEHKEASDRETAIKLMQKLADRGIIHHVCDEHKEFKDVKLFYRFRKDDGTFPLDNEVKAFMRGQRLYEKLMSPENTLLQPREEEGVKYERTFMASEFLDWLVQEGEATTRKEAEQLCHRLMEHGIIQHVSNKHPFVDSNLLYQFRMNFRRRRRLMELLNEKSPSSQETHDSPFCLRKQSHDNRKSTSFMSVSPSKEIKIVSAVRRSSMSSCGSSGYFSSSPTLSSSPPVLCNPKSVLKRPVTSEELLTPGAPYARKTFTIVGDAVGWGFVVRGSKPCHIQAVDPSGPAAAAGMKVCQFVVSVNGLNVLHVDYRTVSNLILTGPRTIVMEVMEELECMASGRPEELWEAVVGAAERFRARTGTELVLLTAAPPPPPRPGPCAYAAHGRGALAEAARRCLHDIALAHRAATAARPPAPPPAPQPPSPTPSPPRPTLAREDNEEDEDEPTETETSGEQLGISDNGGLFVMDEDATLQDLPPFCESDPESTDDGSLSEETPAGPPTCSVPPASALPTQQYAKSLPVSVPVWGFKEKRTEARSSDEENGPPSSPDLDRIAASMRALVLREAEDTQVFGDLPRPRLNTSDFQKLKRKY	Clinical trial	Constrained peptides' time to shine. Nat Rev Drug Discov. 2018 Jul 30;17(8):531-533.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	P42345
TTUTO39	Methionine synthase (MTR)	Q99707	METH_HUMAN	Methyltransferase	"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"	MTR	"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."	EC 2.1.1.13	4CCZ; 2O2K	MSPALQDLSQPEGLKKTLRDEINAILQKRIMVLDGGMGTMIQREKLNEEHFRGQEFKDHARPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNMCSAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQAKGLLDGGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQTGEGFVISVSHGEPLCIGLNCALGAAEMRPFIEIIGKCTTAYVLCYPNAGLPNTFGDYDETPSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEAVKNCKPRVPPATAFEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDGMLDGPSAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDDFLEKARKIKKYGAAMVVMAFDEEGQATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFRGMEAIREAMHGVFLYHAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQTQGTGGKKVIQTDEWRNGPVEERLEYALVKGIEKHIIEDTEEARLNQKKYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREETRVLNGTVEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLKDEYFEEIMEEYEDIRQDHYESLKERRYLPLSQARKSGFQMDWLSEPHPVKPTFIGTQVFEDYDLQKLVDYIDWKPFFDVWQLRGKYPNRGFPKIFNDKTVGGEARKVYDDAHNMLNTLISQKKLRARGVVGFWPAQSIQDDIHLYAEAAVPQAAEPIATFYGLRQQAEKDSASTEPYYCLSDFIAPLHSGIRDYLGLFAVACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEELHERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTGIRLTESLAMAPASAVSGLYFSNLKSKYFAVGKISKDQVEDYALRKNISVAEVEKWLGPILGYDTD	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	.	.	.	.	.	.	.	.	.	.	hsa00270: Cysteine and methionine metabolism; hsa00450: Selenocompound metabolism; hsa00670: One carbon pool by folate; hsa01100: Metabolic pathways; hsa01230: Biosynthesis of amino acids	R-HSA-156581: Methylation; R-HSA-1614635: Sulfur amino acid metabolism; R-HSA-3359467: Defective MTRR causes HMAE; R-HSA-3359469: Defective MTR causes HMAG; R-HSA-9013407: RHOH GTPase cycle; R-HSA-9759218: Cobalamin (Cbl) metabolism	MetaCyc:HS04076-MON	Q99707
TTUS1RD	Microsomal triglyceride transfer protein (MTTP)	P55157	MTP_HUMAN	.	Microsomal triglyceride transfer protein large subunit; MTP	MTTP	"Required for the secretion of plasma lipoproteins that contain apolipoprotein B. Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces."	.	.	MILLAVLFLCFISSYSASVKGHTTGLSLNNDRLYKLTYSTEVLLDRGKGKLQDSVGYRISSNVDVALLWRNPDGDDDQLIQITMKDVNVENVNQQRGEKSIFKGKSPSKIMGKENLEALQRPTLLHLIHGKVKEFYSYQNEAVAIENIKRGLASLFQTQLSSGTTNEVDISGNCKVTYQAHQDKVIKIKALDSCKIARSGFTTPNQVLGVSSKATSVTTYKIEDSFVIAVLAEETHNFGLNFLQTIKGKIVSKQKLELKTTEAGPRLMSGKQAAAIIKAVDSKYTAIPIVGQVFQSHCKGCPSLSELWRSTRKYLQPDNLSKAEAVRNFLAFIQHLRTAKKEEILQILKMENKEVLPQLVDAVTSAQTSDSLEAILDFLDFKSDSSIILQERFLYACGFASHPNEELLRALISKFKGSIGSSDIRETVMIITGTLVRKLCQNEGCKLKAVVEAKKLILGGLEKAEKKEDTRMYLLALKNALLPEGIPSLLKYAEAGEGPISHLATTALQRYDLPFITDEVKKTLNRIYHQNRKVHEKTVRTAAAAIILNNNPSYMDVKNILLSIGELPQEMNKYMLAIVQDILRFEMPASKIVRRVLKEMVAHNYDRFSRSGSSSAYTGYIERSPRSASTYSLDILYSGSGILRRSNLNIFQYIGKAGLHGSQVVIEAQGLEALIAATPDEGEENLDSYAGMSAILFDVQLRPVTFFNGYSDLMSKMLSASGDPISVVKGLILLIDHSQELQLQSGLKANIEVQGGLAIDISGAMEFSLWYRESKTRVKNRVTVVITTDITVDSSFVKAGLETSTETEAGLEFISTVQFSQYPFLVCMQMDKDEAPFRQFEKKYERLSTGRGYVSQKRKESVLAGCEFPLHQENSEMCKVVFAPQPDSTSSGWF	Successful	Dyslipidemia and cardiovascular diseases. Curr Opin Lipidol. 2009 Apr;20(2):157-8.	34	.	Vitellogenin lipid transport	.	.	.	Lipoprotein amino terminal region	PF01347	PF01347; Vitellogenin_N	.	.	hsa04975:Fat digestion and absorption	R-HSA-174800:Chylomicron-mediated lipid transport	.	P55157
TTBHFYQ	Mucin-1 (MUC1)	P15941	MUC1_HUMAN	.	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	MUC1	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.	.	6FZR; 6FZQ; 5T78; 5T6P; 2FO4	MTPGTQSPFFLLLLLTVLTVVTGSGHASSTPGGEKETSATQRSSVPSSTEKNAVSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPASGSAATWGQDVTSVPVTRPALGSTTPPAHDVTSAPDNKPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDNRPALGSTAPPVHNVTSASGSASGSASTLVHNGTSARATTTPASKSTPFSIPSHHSDTPTTLASHSTKTDASSTHHSSVPPLTSSNHSTSPQLSTGVSFFFLSFHISNLQFNSSLEDPSTDYYQELQRDISEMFLQIYKQGGFLGLSNIKFRPGSVVVQLTLAFREGTINVHDVETQFNQYKTEAASRYNLTISDVSVSDVPFPFSAQSGAGVPGWGIALLVLVCVLVALAIVYLIALAVCQCRRKNYGQLDIFPARDTYHPMSEYPTYHTHGRYVPPSSTDRSPYEKVSAGNGGSSLSYTNPAVAATSANL	Clinical trial	"Clinical pipeline report, company report or official report of Immunomedics."	25	.	Mucin family	.	.	.	SEA domain	PF01390	PF01390; SEA	.	.	.	R-HSA-5083625: Defective GALNT3 causes HFTC; R-HSA-5083632: Defective C1GALT1C1 causes TNPS; R-HSA-5083636: Defective GALNT12 causes CRCS1; R-HSA-5621480: Dectin-2 family; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-913709: O-linked glycosylation of mucins; R-HSA-977068: Termination of O-glycan biosynthesis	.	P15941
TTGQ6MI	Mucin-15 (MUC15)	Q8N387	MUC15_HUMAN	Mucin	Mucin15; MUC15	MUC15	May play a role in the cell adhesion to the extracellular matrix.	.	.	MLALAKILLISTLFYSLLSGSHGKENQDINTTQNIAEVFKTMENKPISLESEANLNSDKENITTSNLKASHSPPLNLPNNSHGITDFSSNSSAEHSLGSLKPTSTISTSPPLIHSFVSKVPWNAPIADEDLLPISAHPNATPALSSENFTWSLVNDTVKTPDNSSITVSILSSEPTSPSVTPLIVEPSGWLTTNSDSFTGFTPYQEKTTLQPTLKFTNNSKLFPNTSDPQKENRNTGIVFGAILGAILGVSLLTLVGYLLCGKRKTDSFSHRRLYDDRNEPVLRLDNAPEPYDVSFGNSSYYNPTLNDSAMPESEENARDGIPMDDIPPLRTSV	Literature-reported	Expression of mucin 15 in hepatocellular carcinoma and its clinical implications. Nan Fang Yi Ke Da Xue Xue Bao. 2014 Nov;34(11):1611-5.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-5083625: Defective GALNT3 causes HFTC; R-HSA-5083632: Defective C1GALT1C1 causes TNPS; R-HSA-5083636: Defective GALNT12 causes CRCS1; R-HSA-5621480: Dectin-2 family; R-HSA-913709: O-linked glycosylation of mucins; R-HSA-977068: Termination of O-glycan biosynthesis	.	Q8N387
TTC1PS3	Ovarian carcinoma antigen CA125 (MUC16)	Q8WXI7	MUC16_HUMAN	Mucin	Ovarian cancerrelated tumor marker CA125; Mucin16; MUC16; CA125	MUC16	"Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces."	.	.	MLKPSGLPGSSSPTRSLMTGSRSTKATPEMDSGLTGATLSPKTSTGAIVVTEHTLPFTSPDKTLASPTSSVVGRTTQSLGVMSSALPESTSRGMTHSEQRTSPSLSPQVNGTPSRNYPATSMVSGLSSPRTRTSSTEGNFTKEASTYTLTVETTSGPVTEKYTVPTETSTTEGDSTETPWDTRYIPVKITSPMKTFADSTASKENAPVSMTPAETTVTDSHTPGRTNPSFGTLYSSFLDLSPKGTPNSRGETSLELILSTTGYPFSSPEPGSAGHSRISTSAPLSSSASVLDNKISETSIFSGQSLTSPLSPGVPEARASTMPNSAIPFSMTLSNAETSAERVRSTISSLGTPSISTKQTAETILTFHAFAETMDIPSTHIAKTLASEWLGSPGTLGGTSTSALTTTSPSTTLVSEETNTHHSTSGKETEGTLNTSMTPLETSAPGEESEMTATLVPTLGFTTLDSKIRSPSQVSSSHPTRELRTTGSTSGRQSSSTAAHGSSDILRATTSSTSKASSWTSESTAQQFSEPQHTQWVETSPSMKTERPPASTSVAAPITTSVPSVVSGFTTLKTSSTKGIWLEETSADTLIGESTAGPTTHQFAVPTGISMTGGSSTRGSQGTTHLLTRATASSETSADLTLATNGVPVSVSPAVSKTAAGSSPPGGTKPSYTMVSSVIPETSSLQSSAFREGTSLGLTPLNTRHPFSSPEPDSAGHTKISTSIPLLSSASVLEDKVSATSTFSHHKATSSITTGTPEISTKTKPSSAVLSSMTLSNAATSPERVRNATSPLTHPSPSGEETAGSVLTLSTSAETTDSPNIHPTGTLTSESSESPSTLSLPSVSGVKTTFSSSTPSTHLFTSGEETEETSNPSVSQPETSVSRVRTTLASTSVPTPVFPTMDTWPTRSAQFSSSHLVSELRATSSTSVTNSTGSALPKISHLTGTATMSQTNRDTFNDSAAPQSTTWPETSPRFKTGLPSATTTVSTSATSLSATVMVSKFTSPATSSMEATSIREPSTTILTTETTNGPGSMAVASTNIPIGKGYITEGRLDTSHLPIGTTASSETSMDFTMAKESVSMSVSPSQSMDAAGSSTPGRTSQFVDTFSDDVYHLTSREITIPRDGTSSALTPQMTATHPPSPDPGSARSTWLGILSSSPSSPTPKVTMSSTFSTQRVTTSMIMDTVETSRWNMPNLPSTTSLTPSNIPTSGAIGKSTLVPLDTPSPATSLEASEGGLPTLSTYPESTNTPSIHLGAHASSESPSTIKLTMASVVKPGSYTPLTFPSIETHIHVSTARMAYSSGSSPEMTAPGETNTGSTWDPTTYITTTDPKDTSSAQVSTPHSVRTLRTTENHPKTESATPAAYSGSPKISSSPNLTSPATKAWTITDTTEHSTQLHYTKLAEKSSGFETQSAPGPVSVVIPTSPTIGSSTLELTSDVPGEPLVLAPSEQTTITLPMATWLSTSLTEEMASTDLDISSPSSPMSTFAIFPPMSTPSHELSKSEADTSAIRNTDSTTLDQHLGIRSLGRTGDLTTVPITPLTTTWTSVIEHSTQAQDTLSATMSPTHVTQSLKDQTSIPASASPSHLTEVYPELGTQGRSSSEATTFWKPSTDTLSREIETGPTNIQSTPPMDNTTTGSSSSGVTLGIAHLPIGTSSPAETSTNMALERRSSTATVSMAGTMGLLVTSAPGRSISQSLGRVSSVLSESTTEGVTDSSKGSSPRLNTQGNTALSSSLEPSYAEGSQMSTSIPLTSSPTTPDVEFIGGSTFWTKEVTTVMTSDISKSSARTESSSATLMSTALGSTENTGKEKLRTASMDLPSPTPSMEVTPWISLTLSNAPNTTDSLDLSHGVHTSSAGTLATDRSLNTGVTRASRLENGSDTSSKSLSMGNSTHTSMTYTEKSEVSSSIHPRPETSAPGAETTLTSTPGNRAISLTLPFSSIPVEEVISTGITSGPDINSAPMTHSPITPPTIVWTSTGTIEQSTQPLHAVSSEKVSVQTQSTPYVNSVAVSASPTHENSVSSGSSTSSPYSSASLESLDSTISRRNAITSWLWDLTTSLPTTTWPSTSLSEALSSGHSGVSNPSSTTTEFPLFSAASTSAAKQRNPETETHGPQNTAASTLNTDASSVTGLSETPVGASISSEVPLPMAITSRSDVSGLTSESTANPSLGTASSAGTKLTRTISLPTSESLVSFRMNKDPWTVSIPLGSHPTTNTETSIPVNSAGPPGLSTVASDVIDTPSDGAESIPTVSFSPSPDTEVTTISHFPEKTTHSFRTISSLTHELTSRVTPIPGDWMSSAMSTKPTGASPSITLGERRTITSAAPTTSPIVLTASFTETSTVSLDNETTVKTSDILDARKTNELPSDSSSSSDLINTSIASSTMDVTKTASISPTSISGMTASSSPSLFSSDRPQVPTSTTETNTATSPSVSSNTYSLDGGSNVGGTPSTLPPFTITHPVETSSALLAWSRPVRTFSTMVSTDTASGENPTSSNSVVTSVPAPGTWTSVGSTTDLPAMGFLKTSPAGEAHSLLASTIEPATAFTPHLSAAVVTGSSATSEASLLTTSESKAIHSSPQTPTTPTSGANWETSATPESLLVVTETSDTTLTSKILVTDTILFSTVSTPPSKFPSTGTLSGASFPTLLPDTPAIPLTATEPTSSLATSFDSTPLVTIASDSLGTVPETTLTMSETSNGDALVLKTVSNPDRSIPGITIQGVTESPLHPSSTSPSKIVAPRNTTYEGSITVALSTLPAGTTGSLVFSQSSENSETTALVDSSAGLERASVMPLTTGSQGMASSGGIRSGSTHSTGTKTFSSLPLTMNPGEVTAMSEITTNRLTATQSTAPKGIPVKPTSAESGLLTPVSASSSPSKAFASLTTAPPTWGIPQSTLTFEFSEVPSLDTKSASLPTPGQSLNTIPDSDASTASSSLSKSPEKNPRARMMTSTKAISASSFQSTGFTETPEGSASPSMAGHEPRVPTSGTGDPRYASESMSYPDPSKASSAMTSTSLASKLTTLFSTGQAARSGSSSSPISLSTEKETSFLSPTASTSRKTSLFLGPSMARQPNILVHLQTSALTLSPTSTLNMSQEEPPELTSSQTIAEEEGTTAETQTLTFTPSETPTSLLPVSSPTEPTARRKSSPETWASSISVPAKTSLVETTDGTLVTTIKMSSQAAQGNSTWPAPAEETGSSPAGTSPGSPEMSTTLKIMSSKEPSISPEIRSTVRNSPWKTPETTVPMETTVEPVTLQSTALGSGSTSISHLPTGTTSPTKSPTENMLATERVSLSPSPPEAWTNLYSGTPGGTRQSLATMSSVSLESPTARSITGTGQQSSPELVSKTTGMEFSMWHGSTGGTTGDTHVSLSTSSNILEDPVTSPNSVSSLTDKSKHKTETWVSTTAIPSTVLNNKIMAAEQQTSRSVDEAYSSTSSWSDQTSGSDITLGASPDVTNTLYITSTAQTTSLVSLPSGDQGITSLTNPSGGKTSSASSVTSPSIGLETLRANVSAVKSDIAPTAGHLSQTSSPAEVSILDVTTAPTPGISTTITTMGTNSISTTTPNPEVGMSTMDSTPATERRTTSTEHPSTWSSTAASDSWTVTDMTSNLKVARSPGTISTMHTTSFLASSTELDSMSTPHGRITVIGTSLVTPSSDASAVKTETSTSERTLSPSDTTASTPISTFSRVQRMSISVPDILSTSWTPSSTEAEDVPVSMVSTDHASTKTDPNTPLSTFLFDSLSTLDWDTGRSLSSATATTSAPQGATTPQELTLETMISPATSQLPFSIGHITSAVTPAAMARSSGVTFSRPDPTSKKAEQTSTQLPTTTSAHPGQVPRSAATTLDVIPHTAKTPDATFQRQGQTALTTEARATSDSWNEKEKSTPSAPWITEMMNSVSEDTIKEVTSSSSVLRTLNTLDINLESGTTSSPSWKSSPYERIAPSESTTDKEAIHPSTNTVETTGWVTSSEHASHSTIPAHSASSKLTSPVVTTSTREQAIVSMSTTTWPESTRARTEPNSFLTIELRDVSPYMDTSSTTQTSIISSPGSTAITKGPRTEITSSKRISSSFLAQSMRSSDSPSEAITRLSNFPAMTESGGMILAMQTSPPGATSLSAPTLDTSATASWTGTPLATTQRFTYSEKTTLFSKGPEDTSQPSPPSVEETSSSSSLVPIHATTSPSNILLTSQGHSPSSTPPVTSVFLSETSGLGKTTDMSRISLEPGTSLPPNLSSTAGEALSTYEASRDTKAIHHSADTAVTNMEATSSEYSPIPGHTKPSKATSPLVTSHIMGDITSSTSVFGSSETTEIETVSSVNQGLQERSTSQVASSATETSTVITHVSSGDATTHVTKTQATFSSGTSISSPHQFITSTNTFTDVSTNPSTSLIMTESSGVTITTQTGPTGAATQGPYLLDTSTMPYLTETPLAVTPDFMQSEKTTLISKGPKDVSWTSPPSVAETSYPSSLTPFLVTTIPPATSTLQGQHTSSPVSATSVLTSGLVKTTDMLNTSMEPVTNSPQNLNNPSNEILATLAATTDIETIHPSINKAVTNMGTASSAHVLHSTLPVSSEPSTATSPMVPASSMGDALASISIPGSETTDIEGEPTSSLTAGRKENSTLQEMNSTTESNIILSNVSVGAITEATKMEVPSFDATFIPTPAQSTKFPDIFSVASSRLSNSPPMTISTHMTTTQTGSSGATSKIPLALDTSTLETSAGTPSVVTEGFAHSKITTAMNNDVKDVSQTNPPFQDEASSPSSQAPVLVTTLPSSVAFTPQWHSTSSPVSMSSVLTSSLVKTAGKVDTSLETVTSSPQSMSNTLDDISVTSAATTDIETTHPSINTVVTNVGTTGSAFESHSTVSAYPEPSKVTSPNVTTSTMEDTTISRSIPKSSKTTRTETETTSSLTPKLRETSISQEITSSTETSTVPYKELTGATTEVSRTDVTSSSSTSFPGPDQSTVSLDISTETNTRLSTSPIMTESAEITITTQTGPHGATSQDTFTMDPSNTTPQAGIHSAMTHGFSQLDVTTLMSRIPQDVSWTSPPSVDKTSSPSSFLSSPAMTTPSLISSTLPEDKLSSPMTSLLTSGLVKITDILRTRLEPVTSSLPNFSSTSDKILATSKDSKDTKEIFPSINTEETNVKANNSGHESHSPALADSETPKATTQMVITTTVGDPAPSTSMPVHGSSETTNIKREPTYFLTPRLRETSTSQESSFPTDTSFLLSKVPTGTITEVSSTGVNSSSKISTPDHDKSTVPPDTFTGEIPRVFTSSIKTKSAEMTITTQASPPESASHSTLPLDTSTTLSQGGTHSTVTQGFPYSEVTTLMGMGPGNVSWMTTPPVEETSSVSSLMSSPAMTSPSPVSSTSPQSIPSSPLPVTALPTSVLVTTTDVLGTTSPESVTSSPPNLSSITHERPATYKDTAHTEAAMHHSTNTAVTNVGTSGSGHKSQSSVLADSETSKATPLMSTTSTLGDTSVSTSTPNISQTNQIQTEPTASLSPRLRESSTSEKTSSTTETNTAFSYVPTGAITQASRTEISSSRTSISDLDRPTIAPDISTGMITRLFTSPIMTKSAEMTVTTQTTTPGATSQGILPWDTSTTLFQGGTHSTVSQGFPHSEITTLRSRTPGDVSWMTTPPVEETSSGFSLMSPSMTSPSPVSSTSPESIPSSPLPVTALLTSVLVTTTNVLGTTSPEPVTSSPPNLSSPTQERLTTYKDTAHTEAMHASMHTNTAVANVGTSISGHESQSSVPADSHTSKATSPMGITFAMGDTSVSTSTPAFFETRIQTESTSSLIPGLRDTRTSEEINTVTETSTVLSEVPTTTTTEVSRTEVITSSRTTISGPDHSKMSPYISTETITRLSTFPFVTGSTEMAITNQTGPIGTISQATLTLDTSSTASWEGTHSPVTQRFPHSEETTTMSRSTKGVSWQSPPSVEETSSPSSPVPLPAITSHSSLYSAVSGSSPTSALPVTSLLTSGRRKTIDMLDTHSELVTSSLPSASSFSGEILTSEASTNTETIHFSENTAETNMGTTNSMHKLHSSVSIHSQPSGHTPPKVTGSMMEDAIVSTSTPGSPETKNVDRDSTSPLTPELKEDSTALVMNSTTESNTVFSSVSLDAATEVSRAEVTYYDPTFMPASAQSTKSPDISPEASSSHSNSPPLTISTHKTIATQTGPSGVTSLGQLTLDTSTIATSAGTPSARTQDFVDSETTSVMNNDLNDVLKTSPFSAEEANSLSSQAPLLVTTSPSPVTSTLQEHSTSSLVSVTSVPTPTLAKITDMDTNLEPVTRSPQNLRNTLATSEATTDTHTMHPSINTAVANVGTTSSPNEFYFTVSPDSDPYKATSAVVITSTSGDSIVSTSMPRSSAMKKIESETTFSLIFRLRETSTSQKIGSSSDTSTVFDKAFTAATTEVSRTELTSSSRTSIQGTEKPTMSPDTSTRSVTMLSTFAGLTKSEERTIATQTGPHRATSQGTLTWDTSITTSQAGTHSAMTHGFSQLDLSTLTSRVPEYISGTSPPSVEKTSSSSSLLSLPAITSPSPVPTTLPESRPSSPVHLTSLPTSGLVKTTDMLASVASLPPNLGSTSHKIPTTSEDIKDTEKMYPSTNIAVTNVGTTTSEKESYSSVPAYSEPPKVTSPMVTSFNIRDTIVSTSMPGSSEITRIEMESTFSLAHGLKGTSTSQDPIVSTEKSAVLHKLTTGATETSRTEVASSRRTSIPGPDHSTESPDISTEVIPSLPISLGITESSNMTIITRTGPPLGSTSQGTFTLDTPTTSSRAGTHSMATQEFPHSEMTTVMNKDPEILSWTIPPSIEKTSFSSSLMPSPAMTSPPVSSTLPKTIHTTPSPMTSLLTPSLVMTTDTLGTSPEPTTSSPPNLSSTSHEILTTDEDTTAIEAMHPSTSTAATNVETTSSGHGSQSSVLADSEKTKATAPMDTTSTMGHTTVSTSMSVSSETTKIKRESTYSLTPGLRETSISQNASFSTDTSIVLSEVPTGTTAEVSRTEVTSSGRTSIPGPSQSTVLPEISTRTMTRLFASPTMTESAEMTIPTQTGPSGSTSQDTLTLDTSTTKSQAKTHSTLTQRFPHSEMTTLMSRGPGDMSWQSSPSLENPSSLPSLLSLPATTSPPPISSTLPVTISSSPLPVTSLLTSSPVTTTDMLHTSPELVTSSPPKLSHTSDERLTTGKDTTNTEAVHPSTNTAASNVEIPSSGHESPSSALADSETSKATSPMFITSTQEDTTVAISTPHFLETSRIQKESISSLSPKLRETGSSVETSSAIETSAVLSEVSIGATTEISRTEVTSSSRTSISGSAESTMLPEISTTRKIIKFPTSPILAESSEMTIKTQTSPPGSTSESTFTLDTSTTPSLVITHSTMTQRLPHSEITTLVSRGAGDVPRPSSLPVEETSPPSSQLSLSAMISPSPVSSTLPASSHSSSASVTSLLTPGQVKTTEVLDASAEPETSSPPSLSSTSVEILATSEVTTDTEKIHPFSNTAVTKVGTSSSGHESPSSVLPDSETTKATSAMGTISIMGDTSVSTLTPALSNTRKIQSEPASSLTTRLRETSTSEETSLATEANTVLSKVSTGATTEVSRTEAISFSRTSMSGPEQSTMSQDISIGTIPRISASSVLTESAKMTITTQTGPSESTLESTLNLNTATTPSWVETHSIVIQGFPHPEMTTSMGRGPGGVSWPSPPFVKETSPPSSPLSLPAVTSPHPVSTTFLAHIPPSPLPVTSLLTSGPATTTDILGTSTEPGTSSSSSLSTTSHERLTTYKDTAHTEAVHPSTNTGGTNVATTSSGYKSQSSVLADSSPMCTTSTMGDTSVLTSTPAFLETRRIQTELASSLTPGLRESSGSEGTSSGTKMSTVLSKVPTGATTEISKEDVTSIPGPAQSTISPDISTRTVSWFSTSPVMTESAEITMNTHTSPLGATTQGTSTLDTSSTTSLTMTHSTISQGFSHSQMSTLMRRGPEDVSWMSPPLLEKTRPSFSLMSSPATTSPSPVSSTLPESISSSPLPVTSLLTSGLAKTTDMLHKSSEPVTNSPANLSSTSVEILATSEVTTDTEKTHPSSNRTVTDVGTSSSGHESTSFVLADSQTSKVTSPMVITSTMEDTSVSTSTPGFFETSRIQTEPTSSLTLGLRKTSSSEGTSLATEMSTVLSGVPTGATAEVSRTEVTSSSRTSISGFAQLTVSPETSTETITRLPTSSIMTESAEMMIKTQTDPPGSTPESTHTVDISTTPNWVETHSTVTQRFSHSEMTTLVSRSPGDMLWPSQSSVEETSSASSLLSLPATTSPSPVSSTLVEDFPSASLPVTSLLNPGLVITTDRMGISREPGTSSTSNLSSTSHERLTTLEDTVDTEDMQPSTHTAVTNVRTSISGHESQSSVLSDSETPKATSPMGTTYTMGETSVSISTSDFFETSRIQIEPTSSLTSGLRETSSSERISSATEGSTVLSEVPSGATTEVSRTEVISSRGTSMSGPDQFTISPDISTEAITRLSTSPIMTESAESAITIETGSPGATSEGTLTLDTSTTTFWSGTHSTASPGFSHSEMTTLMSRTPGDVPWPSLPSVEEASSVSSSLSSPAMTSTSFFSTLPESISSSPHPVTALLTLGPVKTTDMLRTSSEPETSSPPNLSSTSAEILATSEVTKDREKIHPSSNTPVVNVGTVIYKHLSPSSVLADLVTTKPTSPMATTSTLGNTSVSTSTPAFPETMMTQPTSSLTSGLREISTSQETSSATERSASLSGMPTGATTKVSRTEALSLGRTSTPGPAQSTISPEISTETITRISTPLTTTGSAEMTITPKTGHSGASSQGTFTLDTSSRASWPGTHSAATHRSPHSGMTTPMSRGPEDVSWPSRPSVEKTSPPSSLVSLSAVTSPSPLYSTPSESSHSSPLRVTSLFTPVMMKTTDMLDTSLEPVTTSPPSMNITSDESLATSKATMETEAIQLSENTAVTQMGTISARQEFYSSYPGLPEPSKVTSPVVTSSTIKDIVSTTIPASSEITRIEMESTSTLTPTPRETSTSQEIHSATKPSTVPYKALTSATIEDSMTQVMSSSRGPSPDQSTMSQDISTEVITRLSTSPIKTESTEMTITTQTGSPGATSRGTLTLDTSTTFMSGTHSTASQGFSHSQMTALMSRTPGDVPWLSHPSVEEASSASFSLSSPVMTSSSPVSSTLPDSIHSSSLPVTSLLTSGLVKTTELLGTSSEPETSSPPNLSSTSAEILAITEVTTDTEKLEMTNVVTSGYTHESPSSVLADSVTTKATSSMGITYPTGDTNVLTSTPAFSDTSRIQTKSKLSLTPGLMETSISEETSSATEKSTVLSSVPTGATTEVSRTEAISSSRTSIPGPAQSTMSSDTSMETITRISTPLTRKESTDMAITPKTGPSGATSQGTFTLDSSSTASWPGTHSATTQRFPQSVVTTPMSRGPEDVSWPSPLSVEKNSPPSSLVSSSSVTSPSPLYSTPSGSSHSSPVPVTSLFTSIMMKATDMLDASLEPETTSAPNMNITSDESLAASKATTETEAIHVFENTAASHVETTSATEELYSSSPGFSEPTKVISPVVTSSSIRDNMVSTTMPGSSGITRIEIESMSSLTPGLRETRTSQDITSSTETSTVLYKMPSGATPEVSRTEVMPSSRTSIPGPAQSTMSLDISDEVVTRLSTSPIMTESAEITITTQTGYSLATSQVTLPLGTSMTFLSGTHSTMSQGLSHSEMTNLMSRGPESLSWTSPRFVETTRSSSSLTSLPLTTSLSPVSSTLLDSSPSSPLPVTSLILPGLVKTTEVLDTSSEPKTSSSPNLSSTSVEIPATSEIMTDTEKIHPSSNTAVAKVRTSSSVHESHSSVLADSETTITIPSMGITSAVDDTTVFTSNPAFSETRRIPTEPTFSLTPGFRETSTSEETTSITETSAVLYGVPTSATTEVSMTEIMSSNRIHIPDSDQSTMSPDIITEVITRLSSSSMMSESTQMTITTQKSSPGATAQSTLTLATTTAPLARTHSTVPPRFLHSEMTTLMSRSPENPSWKSSLFVEKTSSSSSLLSLPVTTSPSVSSTLPQSIPSSSFSVTSLLTPGMVKTTDTSTEPGTSLSPNLSGTSVEILAASEVTTDTEKIHPSSSMAVTNVGTTSSGHELYSSVSIHSEPSKATYPVGTPSSMAETSISTSMPANFETTGFEAEPFSHLTSGFRKTNMSLDTSSVTPTNTPSSPGSTHLLQSSKTDFTSSAKTSSPDWPPASQYTEIPVDIITPFNASPSITESTGITSFPESRFTMSVTESTHHLSTDLLPSAETISTGTVMPSLSEAMTSFATTGVPRAISGSGSPFSRTESGPGDATLSTIAESLPSSTPVPFSSSTFTTTDSSTIPALHEITSSSATPYRVDTSLGTESSTTEGRLVMVSTLDTSSQPGRTSSSPILDTRMTESVELGTVTSAYQVPSLSTRLTRTDGIMEHITKIPNEAAHRGTIRPVKGPQTSTSPASPKGLHTGGTKRMETTTTALKTTTTALKTTSRATLTTSVYTPTLGTLTPLNASMQMASTIPTEMMITTPYVFPDVPETTSSLATSLGAETSTALPRTTPSVFNRESETTASLVSRSGAERSPVIQTLDVSSSEPDTTASWVIHPAETIPTVSKTTPNFFHSELDTVSSTATSHGADVSSAIPTNISPSELDALTPLVTISGTDTSTTFPTLTKSPHETETRTTWLTHPAETSSTIPRTIPNFSHHESDATPSIATSPGAETSSAIPIMTVSPGAEDLVTSQVTSSGTDRNMTIPTLTLSPGEPKTIASLVTHPEAQTSSAIPTSTISPAVSRLVTSMVTSLAAKTSTTNRALTNSPGEPATTVSLVTHPAQTSPTVPWTTSIFFHSKSDTTPSMTTSHGAESSSAVPTPTVSTEVPGVVTPLVTSSRAVISTTIPILTLSPGEPETTPSMATSHGEEASSAIPTPTVSPGVPGVVTSLVTSSRAVTSTTIPILTFSLGEPETTPSMATSHGTEAGSAVPTVLPEVPGMVTSLVASSRAVTSTTLPTLTLSPGEPETTPSMATSHGAEASSTVPTVSPEVPGVVTSLVTSSSGVNSTSIPTLILSPGELETTPSMATSHGAEASSAVPTPTVSPGVSGVVTPLVTSSRAVTSTTIPILTLSSSEPETTPSMATSHGVEASSAVLTVSPEVPGMVTSLVTSSRAVTSTTIPTLTISSDEPETTTSLVTHSEAKMISAIPTLAVSPTVQGLVTSLVTSSGSETSAFSNLTVASSQPETIDSWVAHPGTEASSVVPTLTVSTGEPFTNISLVTHPAESSSTLPRTTSRFSHSELDTMPSTVTSPEAESSSAISTTISPGIPGVLTSLVTSSGRDISATFPTVPESPHESEATASWVTHPAVTSTTVPRTTPNYSHSEPDTTPSIATSPGAEATSDFPTITVSPDVPDMVTSQVTSSGTDTSITIPTLTLSSGEPETTTSFITYSETHTSSAIPTLPVSPGASKMLTSLVISSGTDSTTTFPTLTETPYEPETTAIQLIHPAETNTMVPRTTPKFSHSKSDTTLPVAITSPGPEASSAVSTTTISPDMSDLVTSLVPSSGTDTSTTFPTLSETPYEPETTATWLTHPAETSTTVSGTIPNFSHRGSDTAPSMVTSPGVDTRSGVPTTTIPPSIPGVVTSQVTSSATDTSTAIPTLTPSPGEPETTASSATHPGTQTGFTVPIRTVPSSEPDTMASWVTHPPQTSTPVSRTTSSFSHSSPDATPVMATSPRTEASSAVLTTISPGAPEMVTSQITSSGAATSTTVPTLTHSPGMPETTALLSTHPRTETSKTFPASTVFPQVSETTASLTIRPGAETSTALPTQTTSSLFTLLVTGTSRVDLSPTASPGVSAKTAPLSTHPGTETSTMIPTSTLSLGLLETTGLLATSSSAETSTSTLTLTVSPAVSGLSSASITTDKPQTVTSWNTETSPSVTSVGPPEFSRTVTGTTMTLIPSEMPTPPKTSHGEGVSPTTILRTTMVEATNLATTGSSPTVAKTTTTFNTLAGSLFTPLTTPGMSTLASESVTSRTSYNHRSWISTTSSYNRRYWTPATSTPVTSTFSPGISTSSIPSSTAATVPFMVPFTLNFTITNLQYEEDMRHPGSRKFNATERELQGLLKPLFRNSSLEYLYSGCRLASLRPEKDSSATAVDAICTHRPDPEDLGLDRERLYWELSNLTNGIQELGPYTLDRNSLYVNGFTHRSSMPTTSTPGTSTVDVGTSGTPSSSPSPTTAGPLLMPFTLNFTITNLQYEEDMRRTGSRKFNTMESVLQGLLKPLFKNTSVGPLYSGCRLTLLRPEKDGAATGVDAICTHRLDPKSPGLNREQLYWELSKLTNDIEELGPYTLDRNSLYVNGFTHQSSVSTTSTPGTSTVDLRTSGTPSSLSSPTIMAAGPLLVPFTLNFTITNLQYGEDMGHPGSRKFNTTERVLQGLLGPIFKNTSVGPLYSGCRLTSLRSEKDGAATGVDAICIHHLDPKSPGLNRERLYWELSQLTNGIKELGPYTLDRNSLYVNGFTHRTSVPTSSTPGTSTVDLGTSGTPFSLPSPATAGPLLVLFTLNFTITNLKYEEDMHRPGSRKFNTTERVLQTLLGPMFKNTSVGLLYSGCRLTLLRSEKDGAATGVDAICTHRLDPKSPGVDREQLYWELSQLTNGIKELGPYTLDRNSLYVNGFTHWIPVPTSSTPGTSTVDLGSGTPSSLPSPTTAGPLLVPFTLNFTITNLKYEEDMHCPGSRKFNTTERVLQSLLGPMFKNTSVGPLYSGCRLTLLRSEKDGAATGVDAICTHRLDPKSPGVDREQLYWELSQLTNGIKELGPYTLDRNSLYVNGFTHQTSAPNTSTPGTSTVDLGTSGTPSSLPSPTSAGPLLVPFTLNFTITNLQYEEDMHHPGSRKFNTTERVLQGLLGPMFKNTSVGLLYSGCRLTLLRPEKNGAATGMDAICSHRLDPKSPGLNREQLYWELSQLTHGIKELGPYTLDRNSLYVNGFTHRSSVAPTSTPGTSTVDLGTSGTPSSLPSPTTAVPLLVPFTLNFTITNLQYGEDMRHPGSRKFNTTERVLQGLLGPLFKNSSVGPLYSGCRLISLRSEKDGAATGVDAICTHHLNPQSPGLDREQLYWQLSQMTNGIKELGPYTLDRNSLYVNGFTHRSSGLTTSTPWTSTVDLGTSGTPSPVPSPTTTGPLLVPFTLNFTITNLQYEENMGHPGSRKFNITESVLQGLLKPLFKSTSVGPLYSGCRLTLLRPEKDGVATRVDAICTHRPDPKIPGLDRQQLYWELSQLTHSITELGPYTLDRDSLYVNGFTQRSSVPTTSTPGTFTVQPETSETPSSLPGPTATGPVLLPFTLNFTITNLQYEEDMRRPGSRKFNTTERVLQGLLMPLFKNTSVSSLYSGCRLTLLRPEKDGAATRVDAVCTHRPDPKSPGLDRERLYWKLSQLTHGITELGPYTLDRHSLYVNGFTHQSSMTTTRTPDTSTMHLATSRTPASLSGPMTASPLLVLFTINFTITNLRYEENMHHPGSRKFNTTERVLQGLLRPVFKNTSVGPLYSGCRLTLLRPKKDGAATKVDAICTYRPDPKSPGLDREQLYWELSQLTHSITELGPYTLDRDSLYVNGFTQRSSVPTTSIPGTPTVDLGTSGTPVSKPGPSAASPLLVLFTLNFTITNLRYEENMQHPGSRKFNTTERVLQGLLRSLFKSTSVGPLYSGCRLTLLRPEKDGTATGVDAICTHHPDPKSPRLDREQLYWELSQLTHNITELGPYALDNDSLFVNGFTHRSSVSTTSTPGTPTVYLGASKTPASIFGPSAASHLLILFTLNFTITNLRYEENMWPGSRKFNTTERVLQGLLRPLFKNTSVGPLYSGCRLTLLRPEKDGEATGVDAICTHRPDPTGPGLDREQLYLELSQLTHSITELGPYTLDRDSLYVNGFTHRSSVPTTSTGVVSEEPFTLNFTINNLRYMADMGQPGSLKFNITDNVMQHLLSPLFQRSSLGARYTGCRVIALRSVKNGAETRVDLLCTYLQPLSGPGLPIKQVFHELSQQTHGITRLGPYSLDKDSLYLNGYNEPGPDEPPTTPKPATTFLPPLSEATTAMGYHLKTLTLNFTISNLQYSPDMGKGSATFNSTEGVLQHLLRPLFQKSSMGPFYLGCQLISLRPEKDGAATGVDTTCTYHPDPVGPGLDIQQLYWELSQLTHGVTQLGFYVLDRDSLFINGYAPQNLSIRGEYQINFHIVNWNLSNPDPTSSEYITLLRDIQDKVTTLYKGSQLHDTFRFCLVTNLTMDSVLVTVKALFSSNLDPSLVEQVFLDKTLNASFHWLGSTYQLVDIHVTEMESSVYQPTSSSSTQHFYLNFTITNLPYSQDKAQPGTTNYQRNKRNIEDALNQLFRNSSIKSYFSDCQVSTFRSVPNRHHTGVDSLCNFSPLARRVDRVAIYEEFLRMTRNGTQLQNFTLDRSSVLVDGYSPNRNEPLTGNSDLPFWAVILIGLAGLLGVITCLICGVLVTTRRRKKEGEYNVQQQCPGYYQSHLDLEDLQ	Clinical trial	"MUC16 (CA125): tumor biomarker to cancer therapy, a work in progress. Mol Cancer. 2014; 13: 129."	25	.	.	.	.	.	.	.	.	.	.	.	R-HSA-5083625: Defective GALNT3 causes HFTC; R-HSA-5083632: Defective C1GALT1C1 causes TNPS; R-HSA-5083636: Defective GALNT12 causes CRCS1; R-HSA-5621480: Dectin-2 family; R-HSA-913709: O-linked glycosylation of mucins; R-HSA-977068: Termination of O-glycan biosynthesis	.	.
TTVO0JU	Mucin-17 (MUC17)	Q685J3	MUC17_HUMAN	.	MUC-17; Small intestinal mucin-3; MUC-3	MUC17	Probably plays a role in maintaining homeostasis on mucosal surfaces.	.	.	MPRPGTMALCLLTLVLSLLPPQAAAEQDLSVNRAVWDGGGCISQGDVLNRQCQQLSQHVRTGSAANTATGTTSTNVVEPRMYLSCSTNPEMTSIESSVTSDTPGVSSTRMTPTESRTTSESTSDSTTLFPSSTEDTSSPTTPEGTDVPMSTPSEESISSTMAFVSTAPLPSFEAYTSLTYKVDMSTPLTTSTQASSSPTTPESTTIPKSTNSEGSTPLTSMPASTMKVASSEAITLLTTPVEISTPVTISAQASSSPTTAEGPSLSNSAPSGGSTPLTRMPLSVMLVVSSEASTLSTTPAATNIPVITSTEASSSPTTAEGTSIPTSTYTEGSTPLTSTPASTMPVATSEMSTLSITPVDTSTLVTTSTEPSSLPTTAEATSMLTSTLSEGSTPLTNMPVSTILVASSEASTTSTIPVDSKTFVTTASEASSSPTTAEDTSIATSTPSEGSTPLTSMPVSTTPVASSEASNLSTTPVDSKTQVTTSTEASSSPPTAEVNSMPTSTPSEGSTPLTSMSVSTMPVASSEASTLSTTPVDTSTPVTTSSEASSSSTTPEGTSIPTSTPSEGSTPLTNMPVSTRLVVSSEASTTSTTPADSNTFVTTSSEASSSSTTAEGTSMPTSTYSERGTTITSMSVSTTLVASSEASTLSTTPVDSNTPVTTSTEATSSSTTAEGTSMPTSTYTEGSTPLTSMPVNTTLVASSEASTLSTTPVDTSTPVTTSTEASSSPTTADGASMPTSTPSEGSTPLTSMPVSKTLLTSSEASTLSTTPLDTSTHITTSTEASCSPTTTEGTSMPISTPSEGSPLLTSIPVSITPVTSPEASTLSTTPVDSNSPVTTSTEVSSSPTPAEGTSMPTSTYSEGRTPLTSMPVSTTLVATSAISTLSTTPVDTSTPVTNSTEARSSPTTSEGTSMPTSTPGEGSTPLTSMPDSTTPVVSSEARTLSATPVDTSTPVTTSTEATSSPTTAEGTSIPTSTPSEGTTPLTSTPVSHTLVANSEASTLSTTPVDSNTPLTTSTEASSPPPTAEGTSMPTSTPSEGSTPLTRMPVSTTMVASSETSTLSTTPADTSTPVTTYSQASSSSTTADGTSMPTSTYSEGSTPLTSVPVSTRLVVSSEASTLSTTPVDTSIPVTTSTEASSSPTTAEGTSIPTSPPSEGTTPLASMPVSTTLVVSSEANTLSTTPVDSKTQVATSTEASSPPPTAEVTSMPTSTPGERSTPLTSMPVRHTPVASSEASTLSTSPVDTSTPVTTSAETSSSPTTAEGTSLPTSTTSEGSTLLTSIPVSTTLVTSPEASTLLTTPVDTKGPVVTSNEVSSSPTPAEGTSMPTSTYSEGRTPLTSIPVNTTLVASSAISILSTTPVDNSTPVTTSTEACSSPTTSEGTSMPNSNPSEGTTPLTSIPVSTTPVVSSEASTLSATPVDTSTPGTTSAEATSSPTTAEGISIPTSTPSEGKTPLKSIPVSNTPVANSEASTLSTTPVDSNSPVVTSTAVSSSPTPAEGTSIAISTPSEGSTALTSIPVSTTTVASSEINSLSTTPAVTSTPVTTYSQASSSPTTADGTSMQTSTYSEGSTPLTSLPVSTMLVVSSEANTLSTTPIDSKTQVTASTEASSSTTAEGSSMTISTPSEGSPLLTSIPVSTTPVASPEASTLSTTPVDSNSPVITSTEVSSSPTPAEGTSMPTSTYTEGRTPLTSITVRTTPVASSAISTLSTTPVDNSTPVTTSTEARSSPTTSEGTSMPNSTPSEGTTPLTSIPVSTTPVLSSEASTLSATPIDTSTPVTTSTEATSSPTTAEGTSIPTSTLSEGMTPLTSTPVSHTLVANSEASTLSTTPVDSNSPVVTSTAVSSSPTPAEGTSIATSTPSEGSTALTSIPVSTTTVASSETNTLSTTPAVTSTPVTTYAQVSSSPTTADGSSMPTSTPREGRPPLTSIPVSTTTVASSEINTLSTTLADTRTPVTTYSQASSSPTTADGTSMPTPAYSEGSTPLTSMPLSTTLVVSSEASTLSTTPVDTSTPATTSTEGSSSPTTAGGTSIQTSTPSERTTPLAGMPVSTTLVVSSEGNTLSTTPVDSKTQVTNSTEASSSATAEGSSMTISAPSEGSPLLTSIPLSTTPVASPEASTLSTTPVDSNSPVITSTEVSSSPIPTEGTSMQTSTYSDRRTPLTSMPVSTTVVASSAISTLSTTPVDTSTPVTNSTEARSSPTTSEGTSMPTSTPSEGSTPFTSMPVSTMPVVTSEASTLSATPVDTSTPVTTSTEATSSPTTAEGTSIPTSTLSEGTTPLTSIPVSHTLVANSEVSTLSTTPVDSNTPFTTSTEASSPPPTAEGTSMPTSTSSEGNTPLTRMPVSTTMVASFETSTLSTTPADTSTPVTTYSQAGSSPTTADDTSMPTSTYSEGSTPLTSVPVSTMPVVSSEASTHSTTPVDTSTPVTTSTEASSSPTTAEGTSIPTSPPSEGTTPLASMPVSTTPVVSSEAGTLSTTPVDTSTPMTTSTEASSSPTTAEDIVVPISTASEGSTLLTSIPVSTTPVASPEASTLSTTPVDSNSPVVTSTEISSSATSAEGTSMPTSTYSEGSTPLRSMPVSTKPLASSEASTLSTTPVDTSIPVTTSTETSSSPTTAKDTSMPISTPSEVSTSLTSILVSTMPVASSEASTLSTTPVDTRTLVTTSTGTSSSPTTAEGSSMPTSTPGERSTPLTNILVSTTLLANSEASTLSTTPVDTSTPVTTSAEASSSPTTAEGTSMRISTPSDGSTPLTSILVSTLPVASSEASTVSTTAVDTSIPVTTSTEASSSPTTAEVTSMPTSTPSETSTPLTSMPVNHTPVASSEAGTLSTTPVDTSTPVTTSTKASSSPTTAEGIVVPISTASEGSTLLTSIPVSTTPVASSEASTLSTTPVDTSIPVTTSTEGSSSPTTAEGTSMPISTPSEVSTPLTSILVSTVPVAGSEASTLSTTPVDTRTPVTTSAEASSSPTTAEGTSMPISTPGERRTPLTSMSVSTMPVASSEASTLSRTPADTSTPVTTSTEASSSPTTAEGTGIPISTPSEGSTPLTSIPVSTTPVAIPEASTLSTTPVDSNSPVVTSTEVSSSPTPAEGTSMPISTYSEGSTPLTGVPVSTTPVTSSAISTLSTTPVDTSTPVTTSTEAHSSPTTSEGTSMPTSTPSEGSTPLTYMPVSTMLVVSSEDSTLSATPVDTSTPVTTSTEATSSTTAEGTSIPTSTPSEGMTPLTSVPVSNTPVASSEASILSTTPVDSNTPLTTSTEASSSPPTAEGTSMPTSTPSEGSTPLTSMPVSTTTVASSETSTLSTTPADTSTPVTTYSQASSSPPIADGTSMPTSTYSEGSTPLTNMSFSTTPVVSSEASTLSTTPVDTSTPVTTSTEASLSPTTAEGTSIPTSSPSEGTTPLASMPVSTTPVVSSEVNTLSTTPVDSNTLVTTSTEASSSPTIAEGTSLPTSTTSEGSTPLSIMPLSTTPVASSEASTLSTTPVDTSTPVTTSSPTNSSPTTAEVTSMPTSTAGEGSTPLTNMPVSTTPVASSEASTLSTTPVDSNTFVTSSSQASSSPATLQVTTMRMSTPSEGSSSLTTMLLSSTYVTSSEASTPSTPSVDRSTPVTTSTQSNSTPTPPEVITLPMSTPSEVSTPLTIMPVSTTSVTISEAGTASTLPVDTSTPVITSTQVSSSPVTPEGTTMPIWTPSEGSTPLTTMPVSTTRVTSSEGSTLSTPSVVTSTPVTTSTEAISSSATLDSTTMSVSMPMEISTLGTTILVSTTPVTRFPESSTPSIPSVYTSMSMTTASEGSSSPTTLEGTTTMPMSTTSERSTLLTTVLISPISVMSPSEASTLSTPPGDTSTPLLTSTKAGSFSIPAEVTTIRISITSERSTPLTTLLVSTTLPTSFPGASIASTPPLDTSTTFTPSTDTASTPTIPVATTISVSVITEGSTPGTTIFIPSTPVTSSTADVFPATTGAVSTPVITSTELNTPSTSSSSTTTSFSTTKEFTTPAMTTAAPLTYVTMSTAPSTPRTTSRGCTTSASTLSATSTPHTSTSVTTRPVTPSSESSRPSTITSHTIPPTFPPAHSSTPPTTSASSTTVNPEAVTTMTTRTKPSTRTTSFPTVTTTAVPTNTTIKSNPTSTPTVPRTTTCFGDGCQNTASRCKNGGTWDGLKCQCPNLYYGELCEEVVSSIDIGPPETISAQMELTVTVTSVKFTEELKNHSSQEFQEFKQTFTEQMNIVYSGIPEYVGVNITKLRLGSVVVEHDVLLRTKYTPEYKTVLDNATEVVKEKITKVTTQQIMINDICSDMMCFNTTGTQVQNITVTQYDPEEDCRKMAKEYGDYFVVEYRDQKPYCISPCEPGFSVSKNCNLGKCQMSLSGPQCLCVTTETHWYSGETCNQGTQKSLVYGLVGAGVVLMLIILVALLMLVFRSKREVKRQKYRLSQLYKWQEEDSGPAPGTFQNIGFDICQDDDSIHLESIYSNFQPSLRHIDPETKIRIQRPQVMTTSF	Clinical trial	"Clinical pipeline report, company report or official report of Amgen."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-5083625: Defective GALNT3 causes HFTC; R-HSA-5083632: Defective C1GALT1C1 causes TNPS; R-HSA-5083636: Defective GALNT12 causes CRCS1; R-HSA-5621480: Dectin-2 family; R-HSA-913709: O-linked glycosylation of mucins; R-HSA-977068: Termination of O-glycan biosynthesis	.	.
TTEL90S	Tracheobronchial mucin 5A (MUC5AC)	P98088	MUC5A_HUMAN	.	"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"	MUC5AC	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.	.	5AJP; 5AJO; 5AJN	MSVGRRKLALLWALALALACTRHTGHAQDGSSESSYKHHPALSPIARGPSGVPLRGATVFPSLRTIPVVRASNPAHNGRVCSTWGSFHYKTFDGDVFRFPGLCNYVFSEHCGAAYEDFNIQLRRSQESAAPTLSRVLMKVDGVVIQLTKGSVLVNGHPVLLPFSQSGVLIQQSSSYTKVEARLGLVLMWNHDDSLLLELDTKYANKTCGLCGDFNGMPVVSELLSHNTKLTPMEFGNLQKMDDPTDQCQDPVPEPPRNCSTGFGICEELLHGQLFSGCVALVDVGSYLEACRQDLCFCEDTDLLSCVCHTLAEYSRQCTHAGGLPQDWRGPDFCPQKCPNNMQYHECRSPCADTCSNQEHSRACEDHCVAGCFCPEGTVLDDIGQTGCVPVSKCACVYNGAAYAPGATYSTDCTNCTCSGGRWSCQEVPCPGTCSVLGGAHFSTFDGKQYTVHGDCSYVLTKPCDSSAFTVLAELRRCGLTDSETCLKSVTLSLDGAQTVVVIKASGEVFLNQIYTQLPISAANVTIFRPSTFFIIAQTSLGLQLNLQLVPTMQLFMQLAPKLRGQTCGLCGNFNSIQADDFRTLSGVVEATAAAFFNTFKTQAACPNIRNSFEDPCSLSVENEKYAQHWCSQLTDADGPFGRCHAAVKPGTYYSNCMFDTCNCERSEDCLCAALSSYVHACAAKGVQLGGWRDGVCTKPMTTCPKSMTYHYHVSTCQPTCRSLSEGDITCSVGFIPVDGCICPKGTFLDDTGKCVQASNCPCYHRGSMIPNGESVHDSGAICTCTHGKLSCIGGQAPAPVCAAPMVFFDCRNATPGDTGAGCQKSCHTLDMTCYSPQCVPGCVCPDGLVADGEGGCITAEDCPCVHNEASYRAGQTIRVGCNTCTCDSRMWRCTDDPCLATCAVYGDGHYLTFDGQSYSFNGDCEYTLVQNHCGGKDSTQDSFRVVTENVPCGTTGTTCSKAIKIFLGGFELKLSHGKVEVIGTDESQEVPYTIRQMGIYLVVDTDIGLVLLWDKKTSIFINLSPEFKGRVCGLCGNFDDIAVNDFATRSRSVVGDVLEFGNSWKLSPSCPDALAPKDPCTANPFRKSWAQKQCSILHGPTFAACHAHVEPARYYEACVNDACACDSGGDCECFCTAVAAYAQACHEVGLCVSWRTPSICPLFCDYYNPEGQCEWHYQPCGVPCLRTCRNPRGDCLRDVRGLEGCYPKCPPEAPIFDEDKMQCVATCPTPPLPPRCHVHGKSYRPGAVVPSDKNCQSCLCTERGVECTYKAEACVCTYNGQRFHPGDVIYHTTDGTGGCISARCGANGTIERRVYPCSPTTPVPPTTFSFSTPPLVVSSTHTPSNGPSSAHTGPPSSAWPTTAGTSPRTRLPTASASLPPVCGEKCLWSPWMDVSRPGRGTDSGDFDTLENLRAHGYRVCESPRSVECRAEDAPGVPLRALGQRVQCSPDVGLTCRNREQASGLCYNYQIRVQCCTPLPCSTSSSPAQTTPPTTSKTTETRASGSSAPSSTPGTVSLSTARTTPAPGTATSVKKTFSTPSPPPVPATSTSSMSTTAPGTSVVSSKPTPTEPSTSSCLQELCTWTEWIDGSYPAPGINGGDFDTFQNLRDEGYTFCESPRSVQCRAESFPNTPLADLGQDVICSHTEGLICLNKNQLPPICYNYEIRIQCCETVNVCRDITRLPKTVATTRPTPHPTGAQTQTTFTTHMPSASTEQPTATSRGGPTATSVTQGTHTTLVTRNCHPRCTWTKWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAKSHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPRGCHMTSTPGSTSSSPAQTTPSTTSKTTETQASGSSAPSSTPGTVSLSTARTTPAPGTATSVKKTFSTPSPPPVPATSTSSMSTTAPGTSVVSSKPTPTEPSTSSCLQELCTWTEWIDGSYPAPGINGGDFDTFQNLRDEGYTFCESPRSVQCRAESFPNTPLADLGQDVICSHTEGLICLNKNQLPPICYNYEIRIQCCETVNVCRDITRPPKTVATTRPTPHPTGAQTQTTFTTHMPSASTEQPTATSRGGPTATSVTQGTHTTPVTRNCHPRCTWTTWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAKSHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPKGCPVTSTPVTAPSTPSGRATSPTQSTSSWQKSRTTTLVTTSTTSTPQTSTTYAHTTSTTSAPTARTTSAPTTRTTSASPASTTSGPGNTPSPVPTTSTISAPTTSITSAPTTSTTSAPTSSTTSGPGTTPSPVPTTSITSAPTTSTTSAPTTSTTSARTSSTTSATTTSRISGPETTPSPVPTTSTTSATTTSTTSAPTTSTTSAPTSSTTSSPQTSTTSAPTTSTTSGPGTTPSPVPTTSTTSAPTTRTTSAPKSSTTSAATTSTTSGPETTPRPVPTTSTTSSPTTSTTSAPTTSTTSASTTSTTSGAGTTPSPVPTTSTTSAPTTSTTSAPISSTTSATTTSTTSGPGTTPSPVPTTSTTSAPTTSTTSGPGTTPSAVPTTSITSAPTTSTNSAPISSTTSATTTSRISGPETTPSPVPTASTTSASTTSTTSGPGTTPSPVPTTSTISVPTTSTTSASTTSTTSASTTSTTSGPGTTPSPVPTTSTTSAPTTSTTSAPTTSTISAPTTSTTSATTTSTTSAPTPRRTSAPTTSTISASTTSTTSATTTSTTSATTTSTISAPTTSTTLSPTTSTTSTTITSTTSAPISSTTSTPQTSTTSAPTTSTTSGPGTTSSPVPTTSTTSAPTTSTTSAPTTRTTSVPTSSTTSTATTSTTSGPGTTPSPVPTTSTTSAPTTRTTSAPTTSTTSAPTTSTTSAPTSSTTSATTTSTISVPTTSTTSVPGTTPSPVPTTSTISVPTTSTTSASTTSTTSGPGTTPSPVPTTSTTSAPTTSTTSAPTTSTISAPTTSTPSAPTTSTTLAPTTSTTSAPTTSTTSTPTSSTTSSPQTSTTSASTTSITSGPGTTPSPVPTTSTTSAPTTSTTSAATTSTISAPTTSTTSAPTTSTTSASTASKTSGLGTTPSPIPTTSTTSPPTTSTTSASTASKTSGPGTTPSPVPTTSTIFAPRTSTTSASTTSTTPGPGTTPSPVPTTSTASVSKTSTSHVSISKTTHSQPVTRDCHLRCTWTKWFDIDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAESHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPKGCPVTSTPVTAPSTPSGRATSPTQSTSSWQKSRTTTLVTTSTTSTPQTSTTSAPTTSTTSAPTTSTTSAPTTSTTSTPQTSISSAPTSSTTSAPTSSTISARTTSIISAPTTSTTSSPTTSTTSATTTSTTSAPTSSTTSTPQTSKTSAATSSTTSGSGTTPSPVTTTSTASVSKTSTSHVSVSKTTHSQPVTRDCHPRCTWTKWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAKSHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPKGCPVTSTSVTAPSTPSGRATSPTQSTSSWQKSRTTTLVTSSITSTTQTSTTSAPTTSTTPASIPSTTSAPTTSTTSAPTTSTTSAPTTSTTSTPQTTTSSAPTSSTTSAPTTSTISAPTTSTISAPTTSTTSAPTASTTSAPTSTSSAPTTNTTSAPTTSTTSAPITSTISAPTTSTTSTPQTSTISSPTTSTTSTPQTSTTSSPTTSTTSAPTTSTTSAPTTSTTSTPQTSISSAPTSSTTSAPTASTISAPTTSTTSFHTTSTTSPPTSSTSSTPQTSKTSAATSSTTSGSGTTPSPVPTTSTASVSKTSTSHVSVSKTTHSQPVTRDCHPRCTWTKWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAESHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPKGCPVTSTPVTAPSTPSGRATSPTQSTSSWQKSRTTTLVTTSTTSTPQTSTTSAPTTSTIPASTPSTTSAPTTSTTSAPTTSTTSAPTHRTTSGPTTSTTLAPTTSTTSAPTTSTNSAPTTSTISASTTSTISAPTTSTISSPTSSTTSTPQTSKTSAATSSTTSGSGTTPSPVPTTSTTSASTTSTTSAPTTSTTSGPGTTPSPVPSTSTTSAATTSTTSAPTTRTTSAPTSSMTSGPGTTPSPVPTTSTTSAPTTSTTSGPGTTPSPVPTTSTTSAPITSTTSGPGSTPSPVPTTSTTSAPTTSTTSASTASTTSGPGTTPSPVPTTSTTSAPTTRTTSASTASTTSGPGSTPSPVPTTSTTSAPTTRTTPASTASTTSGPGTTPSPVPTTSTTSASTTSTISLPTTSTTSAPITSMTSGPGTTPSPVPTTSTTSAPTTSTTSASTASTTSGPGTTPSPVPTTSTTSAPTTSTTSASTASTTSGPGTSLSPVPTTSTTSAPTTSTTSGPGTTPSPVPTTSTTSAPTTSTTSGPGTTPSPVPTTSTTPVSKTSTSHLSVSKTTHSQPVTSDCHPLCAWTKWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAESHPEVNIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPRGCPVTSVTPYGTSPTNALYPSLSTSMVSASVASTSVASSSVASSSVAYSTQTCFCNVADRLYPAGSTIYRHRDLAGHCYYALCSQDCQVVRGVDSDCPSTTLPPAPATSPSISTSEPVTELGCPNAVPPRKKGETWATPNCSEATCEGNNVISLRPRTCPRVEKPTCANGYPAVKVADQDGCCHHYQCQCVCSGWGDPHYITFDGTYYTFLDNCTYVLVQQIVPVYGHFRVLVDNYFCGAEDGLSCPRSIILEYHQDRVVLTRKPVHGVMTNEIIFNNKVVSPGFRKNGIVVSRIGVKMYATIPELGVQVMFSGLIFSVEVPFSKFANNTEGQCGTCTNDRKDECRTPRGTVVASCSEMSGLWNVSIPDQPACHRPHPTPTTVGPTTVGSTTVGPTTVGSTTVGPTTPPAPCLPSPICQLILSKVFEPCHTVIPPLLFYEGCVFDRCHMTDLDVVCSSLELYAALCASHDICIDWRGRTGHMCPFTCPADKVYQPCGPSNPSYCYGNDSASLGALPEAGPITEGCFCPEGMTLFSTSAQVCVPTGCPRCLGPHGEPVKVGHTVGMDCQECTCEAATWTLTCRPKLCPLPPACPLPGFVPVPAAPQAGQCCPQYSCACNTSRCPAPVGCPEGARAIPTYQEGACCPVQNCSWTVCSINGTLYQPGAVVSSSLCETCRCELPGGPPSDAFVVSCETQICNTHCPVGFEYQEQSGQCCGTCVQVACVTNTSKSPAHLFYPGETWSDAGNHCVTHQCEKHQDGLVVVTTKKACPPLSCSLDEARMSKDGCCRFCPPPPPPYQNQSTCAVYHRSLIIQQQGCSSSEPVRLAYCRGNCGDSSSMYSLEGNTVEHRCQCCQELRTSLRNVTLHCTDGSSRAFSYTEVEECGCMGRRCPAPGDTQHSEEAEPEPSQEAESGSWERGVPVSPMH	Literature-reported	Suppression of MUC5AC expression in human bronchial epithelial cells by interferon-. Allergol Int. 2017 Jan;66(1):75-82.	.	.	.	.	.	.	C8 domain; Mucin-2 protein WxxW repeating region; Trypsin Inhibitor like cysteine rich domain; von Willebrand factor type D domain	PF08742; PF13330; PF01826; PF00094	PF08742; C8; PF13330; Mucin2_WxxW; PF01826; TIL; PF00094; VWD	.	.	hsa04657: IL-17 signaling pathway	R-HSA-5083625: Defective GALNT3 causes HFTC; R-HSA-5083632: Defective C1GALT1C1 causes TNPS; R-HSA-5083636: Defective GALNT12 causes CRCS1; R-HSA-5621480: Dectin-2 family; R-HSA-913709: O-linked glycosylation of mucins; R-HSA-977068: Termination of O-glycan biosynthesis	.	.
TTTLE0A	Mucin-5AC messenger RNA (MUC5AC mRNA)	P98088	MUC5A_HUMAN	mRNA target	"MUC-5AC (mRNA); Gastric mucin (mRNA); Major airway glycoprotein (mRNA); Mucin-5 subtype AC, tracheobronchial (mRNA); Tracheobronchial mucin (mRNA); TBM (mRNA)"	MUC5AC	"Gel-forming glycoprotein of gastric and respiratory tract epithelia that protects the mucosa from infection and chemical damage by binding to inhaled microorganisms and particles that are subsequently removed by the mucociliary system (PubMed:14535999, PubMed:14718370). Interacts with H.pylori in the gastric epithelium, Barrett's esophagus as well as in gastric metaplasia of the duodenum (GMD) (PubMed:14535999). {ECO:0000269|PubMed:14535999, ECO:0000303|PubMed:14535999, ECO:0000303|PubMed:14718370}."	.	5AJN;5AJO;5AJP	MSVGRRKLALLWALALALACTRHTGHAQDGSSESSYKHHPALSPIARGPSGVPLRGATVFPSLRTIPVVRASNPAHNGRVCSTWGSFHYKTFDGDVFRFPGLCNYVFSEHCGAAYEDFNIQLRRSQESAAPTLSRVLMKVDGVVIQLTKGSVLVNGHPVLLPFSQSGVLIQQSSSYTKVEARLGLVLMWNHDDSLLLELDTKYANKTCGLCGDFNGMPVVSELLSHNTKLTPMEFGNLQKMDDPTDQCQDPVPEPPRNCSTGFGICEELLHGQLFSGCVALVDVGSYLEACRQDLCFCEDTDLLSCVCHTLAEYSRQCTHAGGLPQDWRGPDFCPQKCPNNMQYHECRSPCADTCSNQEHSRACEDHCVAGCFCPEGTVLDDIGQTGCVPVSKCACVYNGAAYAPGATYSTDCTNCTCSGGRWSCQEVPCPGTCSVLGGAHFSTFDGKQYTVHGDCSYVLTKPCDSSAFTVLAELRRCGLTDSETCLKSVTLSLDGAQTVVVIKASGEVFLNQIYTQLPISAANVTIFRPSTFFIIAQTSLGLQLNLQLVPTMQLFMQLAPKLRGQTCGLCGNFNSIQADDFRTLSGVVEATAAAFFNTFKTQAACPNIRNSFEDPCSLSVENEKYAQHWCSQLTDADGPFGRCHAAVKPGTYYSNCMFDTCNCERSEDCLCAALSSYVHACAAKGVQLGGWRDGVCTKPMTTCPKSMTYHYHVSTCQPTCRSLSEGDITCSVGFIPVDGCICPKGTFLDDTGKCVQASNCPCYHRGSMIPNGESVHDSGAICTCTHGKLSCIGGQAPAPVCAAPMVFFDCRNATPGDTGAGCQKSCHTLDMTCYSPQCVPGCVCPDGLVADGEGGCITAEDCPCVHNEASYRAGQTIRVGCNTCTCDSRMWRCTDDPCLATCAVYGDGHYLTFDGQSYSFNGDCEYTLVQNHCGGKDSTQDSFRVVTENVPCGTTGTTCSKAIKIFLGGFELKLSHGKVEVIGTDESQEVPYTIRQMGIYLVVDTDIGLVLLWDKKTSIFINLSPEFKGRVCGLCGNFDDIAVNDFATRSRSVVGDVLEFGNSWKLSPSCPDALAPKDPCTANPFRKSWAQKQCSILHGPTFAACHAHVEPARYYEACVNDACACDSGGDCECFCTAVAAYAQACHEVGLCVSWRTPSICPLFCDYYNPEGQCEWHYQPCGVPCLRTCRNPRGDCLRDVRGLEGCYPKCPPEAPIFDEDKMQCVATCPTPPLPPRCHVHGKSYRPGAVVPSDKNCQSCLCTERGVECTYKAEACVCTYNGQRFHPGDVIYHTTDGTGGCISARCGANGTIERRVYPCSPTTPVPPTTFSFSTPPLVVSSTHTPSNGPSSAHTGPPSSAWPTTAGTSPRTRLPTASASLPPVCGEKCLWSPWMDVSRPGRGTDSGDFDTLENLRAHGYRVCESPRSVECRAEDAPGVPLRALGQRVQCSPDVGLTCRNREQASGLCYNYQIRVQCCTPLPCSTSSSPAQTTPPTTSKTTETRASGSSAPSSTPGTVSLSTARTTPAPGTATSVKKTFSTPSPPPVPATSTSSMSTTAPGTSVVSSKPTPTEPSTSSCLQELCTWTEWIDGSYPAPGINGGDFDTFQNLRDEGYTFCESPRSVQCRAESFPNTPLADLGQDVICSHTEGLICLNKNQLPPICYNYEIRIQCCETVNVCRDITRLPKTVATTRPTPHPTGAQTQTTFTTHMPSASTEQPTATSRGGPTATSVTQGTHTTLVTRNCHPRCTWTKWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAKSHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPRGCHMTSTPGSTSSSPAQTTPSTTSKTTETQASGSSAPSSTPGTVSLSTARTTPAPGTATSVKKTFSTPSPPPVPATSTSSMSTTAPGTSVVSSKPTPTEPSTSSCLQELCTWTEWIDGSYPAPGINGGDFDTFQNLRDEGYTFCESPRSVQCRAESFPNTPLADLGQDVICSHTEGLICLNKNQLPPICYNYEIRIQCCETVNVCRDITRPPKTVATTRPTPHPTGAQTQTTFTTHMPSASTEQPTATSRGGPTATSVTQGTHTTPVTRNCHPRCTWTTWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAKSHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPKGCPVTSTPVTAPSTPSGRATSPTQSTSSWQKSRTTTLVTTSTTSTPQTSTTYAHTTSTTSAPTARTTSAPTTRTTSASPASTTSGPGNTPSPVPTTSTISAPTTSITSAPTTSTTSAPTSSTTSGPGTTPSPVPTTSITSAPTTSTTSAPTTSTTSARTSSTTSATTTSRISGPETTPSPVPTTSTTSATTTSTTSAPTTSTTSAPTSSTTSSPQTSTTSAPTTSTTSGPGTTPSPVPTTSTTSAPTTRTTSAPKSSTTSAATTSTTSGPETTPRPVPTTSTTSSPTTSTTSAPTTSTTSASTTSTTSGAGTTPSPVPTTSTTSAPTTSTTSAPISSTTSATTTSTTSGPGTTPSPVPTTSTTSAPTTSTTSGPGTTPSAVPTTSITSAPTTSTNSAPISSTTSATTTSRISGPETTPSPVPTASTTSASTTSTTSGPGTTPSPVPTTSTISVPTTSTTSASTTSTTSASTTSTTSGPGTTPSPVPTTSTTSAPTTSTTSAPTTSTISAPTTSTTSATTTSTTSAPTPRRTSAPTTSTISASTTSTTSATTTSTTSATTTSTISAPTTSTTLSPTTSTTSTTITSTTSAPISSTTSTPQTSTTSAPTTSTTSGPGTTSSPVPTTSTTSAPTTSTTSAPTTRTTSVPTSSTTSTATTSTTSGPGTTPSPVPTTSTTSAPTTRTTSAPTTSTTSAPTTSTTSAPTSSTTSATTTSTISVPTTSTTSVPGTTPSPVPTTSTISVPTTSTTSASTTSTTSGPGTTPSPVPTTSTTSAPTTSTTSAPTTSTISAPTTSTPSAPTTSTTLAPTTSTTSAPTTSTTSTPTSSTTSSPQTSTTSASTTSITSGPGTTPSPVPTTSTTSAPTTSTTSAATTSTISAPTTSTTSAPTTSTTSASTASKTSGLGTTPSPIPTTSTTSPPTTSTTSASTASKTSGPGTTPSPVPTTSTIFAPRTSTTSASTTSTTPGPGTTPSPVPTTSTASVSKTSTSHVSISKTTHSQPVTRDCHLRCTWTKWFDIDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAESHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPKGCPVTSTPVTAPSTPSGRATSPTQSTSSWQKSRTTTLVTTSTTSTPQTSTTSAPTTSTTSAPTTSTTSAPTTSTTSTPQTSISSAPTSSTTSAPTSSTISARTTSIISAPTTSTTSSPTTSTTSATTTSTTSAPTSSTTSTPQTSKTSAATSSTTSGSGTTPSPVTTTSTASVSKTSTSHVSVSKTTHSQPVTRDCHPRCTWTKWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAKSHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPKGCPVTSTSVTAPSTPSGRATSPTQSTSSWQKSRTTTLVTSSITSTTQTSTTSAPTTSTTPASIPSTTSAPTTSTTSAPTTSTTSAPTTSTTSTPQTTTSSAPTSSTTSAPTTSTISAPTTSTISAPTTSTTSAPTASTTSAPTSTSSAPTTNTTSAPTTSTTSAPITSTISAPTTSTTSTPQTSTISSPTTSTTSTPQTSTTSSPTTSTTSAPTTSTTSAPTTSTTSTPQTSISSAPTSSTTSAPTASTISAPTTSTTSFHTTSTTSPPTSSTSSTPQTSKTSAATSSTTSGSGTTPSPVPTTSTASVSKTSTSHVSVSKTTHSQPVTRDCHPRCTWTKWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAESHPEVSIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPKGCPVTSTPVTAPSTPSGRATSPTQSTSSWQKSRTTTLVTTSTTSTPQTSTTSAPTTSTIPASTPSTTSAPTTSTTSAPTTSTTSAPTHRTTSGPTTSTTLAPTTSTTSAPTTSTNSAPTTSTISASTTSTISAPTTSTISSPTSSTTSTPQTSKTSAATSSTTSGSGTTPSPVPTTSTTSASTTSTTSAPTTSTTSGPGTTPSPVPSTSTTSAATTSTTSAPTTRTTSAPTSSMTSGPGTTPSPVPTTSTTSAPTTSTTSGPGTTPSPVPTTSTTSAPITSTTSGPGSTPSPVPTTSTTSAPTTSTTSASTASTTSGPGTTPSPVPTTSTTSAPTTRTTSASTASTTSGPGSTPSPVPTTSTTSAPTTRTTPASTASTTSGPGTTPSPVPTTSTTSASTTSTISLPTTSTTSAPITSMTSGPGTTPSPVPTTSTTSAPTTSTTSASTASTTSGPGTTPSPVPTTSTTSAPTTSTTSASTASTTSGPGTSLSPVPTTSTTSAPTTSTTSGPGTTPSPVPTTSTTSAPTTSTTSGPGTTPSPVPTTSTTPVSKTSTSHLSVSKTTHSQPVTSDCHPLCAWTKWFDVDFPSPGPHGGDKETYNNIIRSGEKICRRPEEITRLQCRAESHPEVNIEHLGQVVQCSREEGLVCRNQDQQGPFKMCLNYEVRVLCCETPRGCPVTSVTPYGTSPTNALYPSLSTSMVSASVASTSVASSSVASSSVAYSTQTCFCNVADRLYPAGSTIYRHRDLAGHCYYALCSQDCQVVRGVDSDCPSTTLPPAPATSPSISTSEPVTELGCPNAVPPRKKGETWATPNCSEATCEGNNVISLRPRTCPRVEKPTCANGYPAVKVADQDGCCHHYQCQCVCSGWGDPHYITFDGTYYTFLDNCTYVLVQQIVPVYGHFRVLVDNYFCGAEDGLSCPRSIILEYHQDRVVLTRKPVHGVMTNEIIFNNKVVSPGFRKNGIVVSRIGVKMYATIPELGVQVMFSGLIFSVEVPFSKFANNTEGQCGTCTNDRKDECRTPRGTVVASCSEMSGLWNVSIPDQPACHRPHPTPTTVGPTTVGSTTVGPTTVGSTTVGPTTPPAPCLPSPICQLILSKVFEPCHTVIPPLLFYEGCVFDRCHMTDLDVVCSSLELYAALCASHDICIDWRGRTGHMCPFTCPADKVYQPCGPSNPSYCYGNDSASLGALPEAGPITEGCFCPEGMTLFSTSAQVCVPTGCPRCLGPHGEPVKVGHTVGMDCQECTCEAATWTLTCRPKLCPLPPACPLPGFVPVPAAPQAGQCCPQYSCACNTSRCPAPVGCPEGARAIPTYQEGACCPVQNCSWTVCSINGTLYQPGAVVSSSLCETCRCELPGGPPSDAFVVSCETQICNTHCPVGFEYQEQSGQCCGTCVQVACVTNTSKSPAHLFYPGETWSDAGNHCVTHQCEKHQDGLVVVTTKKACPPLSCSLDEARMSKDGCCRFCPPPPPPYQNQSTCAVYHRSLIIQQQGCSSSEPVRLAYCRGNCGDSSSMYSLEGNTVEHRCQCCQELRTSLRNVTLHCTDGSSRAFSYTEVEECGCMGRRCPAPGDTQHSEEAEPEPSQEAESGSWERGVPVSPMH	Clinical trial	ClinicalTrials.gov (NCT05292950) A Phase 1/2a Study Evaluating the Effects of ARO-MUC5AC Inhalation Solution in Healthy Subjects and Patients With Muco-Obstructive Lung Disease. U.S.National Institutes of Health.	.	.	.	.	.	.	.	.	.	.	.	hsa:4586	R-HSA-5083625;R-HSA-5083632;R-HSA-5083636;R-HSA-5621480;R-HSA-913709;R-HSA-977068;	.	.
TT6SA0X	Muscle-specific kinase receptor (MUSK)	O15146	MUSK_HUMAN	.	"Muscle-specific tyrosine-protein kinase receptor; Muscle, skeletal receptor tyrosine-protein kinase; MuSK"	MUSK	"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)."	EC 2.7.10.1	.	MRELVNIPLVHILTLVAFSGTEKLPKAPVITTPLETVDALVEEVATFMCAVESYPQPEISWTRNKILIKLFDTRYSIRENGQLLTILSVEDSDDGIYCCTANNGVGGAVESCGALQVKMKPKITRPPINVKIIEGLKAVLPCTTMGNPKPSVSWIKGDSPLRENSRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGTAYSKVVKLEVEVFARILRAPESHNVTFGSFVTLHCTATGIPVPTITWIENGNAVSSGSIQESVKDRVIDSRLQLFITKPGLYTCIATNKHGEKFSTAKAAATISIAEWSKPQKDNKGYCAQYRGEVCNAVLAKDALVFLNTSYADPEEAQELLVHTAWNELKVVSPVCRPAAEALLCNHIFQECSPGVVPTPIPICREYCLAVKELFCAKEWLVMEEKTHRGLYRSEMHLLSVPECSKLPSMHWDPTACARLPHLDYNKENLKTFPPMTSSKPSVDIPNLPSSSSSSFSVSPTYSMTVIISIMSSFAIFVLLTITTLYCCRRRKQWKNKKRESAAVTLTTLPSELLLDRLHPNPMYQRMPLLLNPKLLSLEYPRNNIEYVRDIGEGAFGRVFQARAPGLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDNPNIVKLLGVCAVGKPMCLLFEYMAYGDLNEFLRSMSPHTVCSLSHSDLSMRAQVSSPGPPPLSCAEQLCIARQVAAGMAYLSERKFVHRDLATRNCLVGENMVVKIADFGLSRNIYSADYYKANENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGLQPYYGMAHEEVIYYVRDGNILSCPENCPVELYNLMRLCWSKLPADRPSFTSIHRILERMCERAEGTVSV	Literature-reported	In vitro and in vivo evaluation of 6-aminopyrazolyl-pyridine-3-carbonitriles as JAK2 kinase inhibitors. Bioorg Med Chem Lett. 2011 May 15;21(10):2958-61.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-3000178: ECM proteoglycans	.	O15146
TTCQ21Y	Methylmalonyl-CoA mutase (MMUT)	P22033	MUTA_HUMAN	Intramolecular transferases	Methylmalonyl-CoA isomerase; MUT; MCM	MUT	"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."	EC 5.4.99.2	3BIC; 2XIQ; 2XIJ	MLRAKNQLFLLSPHYLRQVKESSGSRLIQQRLLHQQQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESKEITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLEKKQQSV	Successful	Vitamin B12. Nippon Rinsho. 1999 Oct;57(10):2205-10.	34	.	.	.	.	.	.	.	.	.	.	"hsa00280:Valine, leucine and isoleucine degradation; hsa00630:Glyoxylate and dicarboxylate metabolism; hsa00640:Propanoate metabolism; hsa01100:Metabolic pathways; hsa01200:Carbon metabolism"	"R-HSA-196741:Cobalamin (Cbl, vitamin B12) transport and metabolism"	MetaCyc:HS07322-MON	P22033
TTNB0ZK	Adenine DNA glycosylase (MUTYH)	Q9UIF7	MUTYH_HUMAN	.	hMYH; MutY homolog; MYH	MUTYH	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.	EC 3.2.2.31	3N5N; 1X51	MTPLVSRLSRLWAIMRKPRAAVGSGHRKQAASQEGRQKHAKNNSQAKPSACDGMIAECPGAPAGLARQPEEVVLQASVSSYHLFRDVAEVTAFRGSLLSWYDQEKRDLPWRRRAEDEMDLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLLASGSLSGSPDVEECAPNTGQCHLCLPPSEPWDQTLGVVNFPRKASRKPPREESSATCVLEQPGALGAQILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKALLQELQRWAGPLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVFRVYQGQQPGTCMGSKRSQVSSPCSRKKPRMGQQVLDNFFRSHISTDAHSLNSAAQ	Literature-reported	Aberrant base excision repair pathway of oxidatively damaged DNA: Implications for degenerative diseases. Free Radic Biol Med. 2017 Jun;107:266-277.	.	.	.	.	.	.	.	.	.	.	.	hsa03410: Base excision repair	R-HSA-110330: Recognition and association of DNA glycosylase with site containing an affected purine; R-HSA-110331: Cleavage of the damaged purine; R-HSA-110357: Displacement of DNA glycosylase by APEX1; R-HSA-9608287: Defective MUTYH substrate binding; R-HSA-9608290: Defective MUTYH substrate processing	.	Q9UIF7
TT1E5A4	Marburg virus NP messenger RNA (MV NP mRNA)	P27588	NCAP_MABVM	mRNA target	Protein N (mRNA); Nucleoprotein (mRNA); Nucleocapsid protein (mRNA)	MV NP mRNA	"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."	.	6APP; 5T3W; 4W2Q; 4W2O	MDLHSLLELGTKPTAPHVRNKKVILFDTNHQVSICNQIIDAINSGIDLGDLLEGGLLTLCVEHYYNSDKDKFNTSPVAKYLRDAGYEFDVIKNADATRFLDVSPNEPHYSPLILALKTLESTESQRGRIGLFLSFCSLFLPKLVVGDRASIEKALRQVTVHQEQGIVTYPNHWLTTGHMKVIFGILRSSFILKFVLIHQGVNLVTGHDAYDSIISNSVGQTRFSGLLIVKTVLEFILQKTDSGVTLHPLVRTSKVKNEVASFKQALSNLARHGEYAPFARVLNLSGINNLEHGLYPQLSAIALGVATAHGSTLAGVNVGEQYQQLREAAHDAEVKLQRRHEHQEIQAIAEDDEERKILEQFHLQKTEITHSQTLAVLSQKREKLARLAAEIENNIVEDQGFKQSQNRVSQSFLNDPTPVEVTVQARPMNRPTALPPPVDDKIEHESTEDSSSSSSFVDLNDPFALLNEDEDTLDDSVMIPGTTSREFQGIPEPPRQSQDLNNSQGKQEDESTNRIKKQFLRYQELPPVQEDDESEYTTDSQESIDQPGSDNEQGVDLPPPPLYAQEKRQDPIQHPAANPQDPFGSIGDVNGDILEPIRSPSSPSAPQEDTRMREAYELSPDFTNDEDNQQNWPQRVVTKKGRTFLYPNDLLQTNPPESLITALVEEYQNPVSAKELQADWPDMSFDERRHVAMNL	Clinical trial	AVI-7288 for Marburg Virus in Nonhuman Primates and Humans. N Engl J Med. 2015 Jul 23;373(4):339-48.	17	mRNA	mRNA target	.	.	.	Ebola nucleoprotein	PF05505	PF05505; Ebola_NP	.	.	.	.	.	.
TTE5J6X	Diphosphomevalonate decarboxylase (MVD)	P53602	MVD1_HUMAN	Carbon-carbon lyase	Mevalonate pyrophosphate decarboxylase; Mevalonate (diphospho)decarboxylase; Mevalonate (diphospho)Diphosphomevalonate decarboxylasedecarboxylase; MVD	MVD	Performs the first committed step in the biosynthesis of isoprenes.	EC 4.1.1.33	3D4J	MASEKPLAAVTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLHQDQLKTTTTAVISKDFTEDRIWLNGREEDVGQPRLQACLREIRCLARKRRNSRDGDPLPSSLSCKVHVASVNNFPTAAGLASSAAGYACLAYTLARVYGVESDLSEVARRGSGSACRSLYGGFVEWQMGEQADGKDSIARQVAPESHWPELRVLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPARMAEMARCIRERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNAHHGDTKVAYTFDAGPNAVIFTLDDTVAEFVAAVWHGFPPGSNGDTFLKGLQVRPAPLSAELQAALAMEPTPGGVKYIIVTQVGPGPQILDDPCAHLLGPDGLPKPAA	Literature-reported	"Human mevalonate diphosphate decarboxylase: characterization, investigation of the mevalonate diphosphate binding site, and crystal structure. Arch Biochem Biophys. 2008 Dec 1;480(1):58-67."	0	.	.	.	.	.	.	.	.	.	.	hsa00900: Terpenoid backbone biosynthesis; hsa01100: Metabolic pathways	R-HSA-191273:Cholesterol biosynthesis; R-HSA-2426168:Activation of gene expression by SREBF (SREBP)	MetaCyc:ENSG00000167508-MON	P53602
TT5DFHW	Mevalonate kinase (MVK)	Q03426	KIME_HUMAN	Kinase	POROK3; MVLK; LRBP	MVK	"Catalyzes the phosphorylation of mevalonate to mevalonate 5-phosphate, a key step in isoprenoid and cholesterol biosynthesis."	EC 2.7.1.36	2R3V	MLSEVLLVSAPGKVILHGEHAVVHGKVALAVSLNLRTFLRLQPHSNGKVDLSLPNIGIKRAWDVARLQSLDTSFLEQGDVTTPTSEQVEKLKEVAGLPDDCAVTERLAVLAFLYLYLSICRKQRALPSLDIVVWSELPPGAGLGSSAAYSVCLAAALLTVCEEIPNPLKDGDCVNRWTKEDLELINKWAFQGERMIHGNPSGVDNAVSTWGGALRYHQGKISSLKRSPALQILLTNTKVPRNTRALVAGVRNRLLKFPEIVAPLLTSIDAISLECERVLGEMGEAPAPEQYLVLEELIDMNQHHLNALGVGHASLDQLCQVTRARGLHSKLTGAGGGGCGITLLKPGLEQPEVEATKQALTSCGFDCLETSIGAPGVSIHSATSLDSRVQQALDGL	Literature-reported	Post-translational regulation of mevalonate kinase by intermediates of the cholesterol and nonsterol isoprene biosynthetic pathways. J Lipid Res. 1997 Nov;38(11):2216-23.	0	EC:2.7	.	GHMP kinase family. Mevalonate kinase subfamily.	2.7.1.36 	Transferring phosphorus-containing groups	GHMP kinases C terminal ; GHMP kinases N terminal domain	PF08544; PF00288	PF08544; GHMP_kinases_C; PF00288; GHMP_kinases_N	.	.	hsa00900: Terpenoid backbone biosynthesis; hsa01100: Metabolic pathways; hsa04146: Peroxisome	R-HSA-191273: Cholesterol biosynthesis; R-HSA-2426168: Activation of gene expression by SREBF (SREBP)	MetaCyc:ENSG00000110921-MON	Q03426
TT8V13P	Myb messenger RNA (MYB mRNA)	P10242	MYB_HUMAN	mRNA target	Transcriptional activator Myb (mRNA); Proto-oncogene c-Myb (mRNA)	MYB	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'.	.	.	MARRPRHSIYSSDEDDEDFEMCDHDYDGLLPKSGKRHLGKTRWTREEDEKLKKLVEQNGTDDWKVIANYLPNRTDVQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPEVKKTSWTEEEDRIIYQAHKRLGNRWAEIAKLLPGRTDNAIKNHWNSTMRRKVEQEGYLQESSKASQPAVATSFQKNSHLMGFAQAPPTAQLPATGQPTVNNDYSYYHISEAQNVSSHVPYPVALHVNIVNVPQPAAAAIQRHYNDEDPEKEKRIKELELLLMSTENELKGQQVLPTQNHTCSYPGWHSTTIADHTRPHGDSAPVSCLGEHHSTPSLPADPGSLPEESASPARCMIVHQGTILDNVKNLLEFAETLQFIDSFLNTSSNHENSDLEMPSLTSTPLIGHKLTVTTPFHRDQTVKTQKENTVFRTPAIKRSILESSPRTPTPFKHALAAQEIKYGPLKMLPQTPSHLVEDLQDVIKQESDESGIVAEFQENGPPLLKKIKQEVESPTDKSGNFFCSHHWEGDSLNTQLFTQTSPVADAPNILTSSVLMAPASEDEDNVLKAFTVPKNRSLASPLQPCSSTWEPASCGKMEEQMTSSSQARKYVNAFSARTLVM	Clinical trial	Genta obtains orphan drug designation for C-Myb Antisense (LR3001) in chronic myelocytic leukemia. Genta. 2005.	21	mRNA	mRNA target	.	.	.	"C-myb, C-terminal; LMSTEN motif; Myb-like DNA-binding domain"	PF09316; PF07988; PF00249	PF09316; Cmyb_C; PF07988; LMSTEN; PF00249; Myb_DNA-binding	.	.	hsa04151:PI3K-Akt signaling pathway; hsa05166:HTLV-I infection	R-HSA-983231:Factors involved in megakaryocyte development and platelet production	.	P10242
TT9WOBN	Cardiac myosin (MYBPC3)	Q14896	MYPC3_HUMAN	Immunoglobulin	"Myosinbinding protein C, cardiactype; Myosin-binding protein C, cardiac-type; Cprotein, cardiac muscle isoform; Cardiac MyBPC; Cardiac MyBP-C; C-protein, cardiac muscle isoform"	MYBPC3	"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."	.	6G2T; 6CXJ; 6CXI; 5K6P; 3CX2	MPEPGKKPVSAFSKKPRSVEVAAGSPAVFEAETERAGVKVRWQRGGSDISASNKYGLATEGTRHTLTVREVGPADQGSYAVIAGSSKVKFDLKVIEAEKAEPMLAPAPAPAEATGAPGEAPAPAAELGESAPSPKGSSSAALNGPTPGAPDDPIGLFVMRPQDGEVTVGGSITFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQPAFTGSYRCEVSTKDKFDCSNFNLTVHEAMGTGDLDLLSAFRRTSLAGGGRRISDSHEDTGILDFSSLLKKRDSFRTPRDSKLEAPAEEDVWEILRQAPPSEYERIAFQYGVTDLRGMLKRLKGMRRDEKKSTAFQKKLEPAYQVSKGHKIRLTVELADHDAEVKWLKNGQEIQMSGSKYIFESIGAKRTLTISQCSLADDAAYQCVVGGEKCSTELFVKEPPVLITRPLEDQLVMVGQRVEFECEVSEEGAQVKWLKDGVELTREETFKYRFKKDGQRHHLIINEAMLEDAGHYALCTSGGQALAELIVQEKKLEVYQSIADLMVGAKDQAVFKCEVSDENVRGVWLKNGKELVPDSRIKVSHIGRVHKLTIDDVTPADEADYSFVPEGFACNLSAKLHFMEVKIDFVPRQEPPKIHLDCPGRIPDTIVVVAGNKLRLDVPISGDPAPTVIWQKAITQGNKAPARPAPDAPEDTGDSDEWVFDKKLLCETEGRVRVETTKDRSIFTVEGAEKEDEGVYTVTVKNPVGEDQVNLTVKVIDVPDAPAAPKISNVGEDSCTVQWEPPAYDGGQPILGYILERKKKKSYRWMRLNFDLIQELSHEARRMIEGVVYEMRVYAVNAIGMSRPSPASQPFMPIGPPSEPTHLAVEDVSDTTVSLKWRPPERVGAGGLDGYSVEYCPEGCSEWVAALQGLTEHTSILVKDLPTGARLLFRVRAHNMAGPGAPVTTTEPVTVQEILQRPRLQLPRHLRQTIQKKVGEPVNLLIPFQGKPRPQVTWTKEGQPLAGEEVSIRNSPTDTILFIRAARRVHSGTYQVTVRIENMEDKATLVLQVVDKPSPPQDLRVTDAWGLNVALEWKPPQDVGNTELWGYTVQKADKKTMEWFTVLEHYRRTHCVVPELIIGNGYYFRVFSQNMVGFSDRAATTKEPVFIPRPGITYEPPNYKALDFSEAPSFTQPLVNRSVIAGYTAMLCCAVRGSPKPKISWFKNGLDLGEDARFRMFSKQGVLTLEIRKPCPFDGGIYVCRATNLQGEARCECRLEVRVPQ	Clinical trial	"CK-1827452, a sarcomere-directed cardiac myosin activator for acute and chronic heart disease. IDrugs. 2009 Apr;12(4):243-51."	25	Immunoglobulin	Immunoglobulin superfamily	immunoglobulin superfamily. MyBP family.	.	.	Fibronectin type III domain; Immunoglobulin I-set domain; Tri-helix bundle domain	PF00041; PF07679; PF18362	PF00041; fn3; PF07679; I-set; PF18362; THB	.	.	hsa05410:Hypertrophic cardiomyopathy (HCM); hsa05414:Dilated cardiomyopathy	R-HSA-390522:Striated Muscle Contraction	.	Q14896
TTNQ5ZP	Myc messenger RNA (MYC mRNA)	P01106	MYC_HUMAN	mRNA target	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)	MYC	"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'."	.	6G6L; 6G6K; 6G6J; 6C4U; 5I50	MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA	Clinical trial	Efficacy of a phosphorodiamidate morpholino oligomer antisense compound in the inhibition of corneal transplant rejection in a rat cornea transplant model. J Ocul Pharmacol Ther. 2012 Apr;28(2):194-201.	21	mRNA	mRNA target	.	.	.	Helix-loop-helix DNA-binding domain; Myc leucine zipper domain; Myc amino-terminal region	PF00010; PF02344; PF01056	PF00010; HLH; PF02344; Myc-LZ; PF01056; Myc_N	.	.	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	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	MetaCyc:ENSG00000136997-MON	P01106
TTZILNJ	Proto-oncogene c-Myc (MYC)	P01106	MYC_HUMAN	.	Transcription factor p64; Myc proto-oncogene protein; Class E basic helix-loop-helix protein 39; BHLHE39	MYC	"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."	.	6G6L; 6G6K; 6G6J; 6C4U; 5I50	MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA	Literature-reported	Diversity-oriented synthesis: exploring the intersections between chemistry and biology. Nat Chem Biol. 2005 Jul;1(2):74-84.	0	.	.	.	.	.	Helix-loop-helix DNA-binding domain; Myc leucine zipper domain; Myc amino-terminal region	PF00010; PF02344; PF01056	PF00010; HLH; PF02344; Myc-LZ; PF01056; Myc_N	.	.	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	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	MetaCyc:ENSG00000136997-MON	P01106
TTUCT4J	Mycobacterium Aminoglycoside 2'-N-acetyltransferase (MycB aac)	P0A5N0	AAC2_MYCTU	Acyltransferase	Aminoglycoside 2'-N-acetyltransferase; AAC(2')-Ic	MycB aac	"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."	EC 2.3.1.-	1M4I; 1M4G; 1M4D; 1M44	MHTQVHTARLVHTADLDSETRQDIRQMVTGAFAGDFTETDWEHTLGGMHALIWHHGAIIAHAAVIQRRLIYRGNALRCGYVEGVAVRADWRGQRLVSALLDAVEQVMRGAYQLGALSSSARARRLYASRGWLPWHGPTSVLAPTGPVRTPDDDGTVFVLPIDISLDTSAELMCDWRAGDVW	Literature-reported	Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates. Nat Struct Biol. 2002 Sep;9(9):653-8.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P9WQG9
TTGDAE5	Mycobacterium Alkylhydroperoxidase AhpD (MycB ahpD)	Q57353	AHPD_MYCTU	.	Alkylhydroperoxidase AhpD; Alkyl hydroperoxide reductase AhpD	MycB ahpD	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.	.	1ME5; 1LW1; 1KNC; 1GU9	MSIEKLKAALPEYAKDIKLNLSSITRSSVLDQEQLWGTLLASAAATRNPQVLADIGAEATDHLSAAARHAALGAAAIMGMNNVFYRGRGFLEGRYDDLRPGLRMNIIANPGIPKANFELWSFAVSAINGCSHCLVAHEHTLRTVGVDREAIFEALKAAAIVSGVAQALATIEALSPS	Literature-reported	"The crystal structure of Mycobacterium tuberculosis alkylhydroperoxidase AhpD, a potential target for antitubercular drug design. J Biol Chem. 2002 May 31;277(22):20033-40."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P9WQB5
TT6TMZU	Mycobacterium Biosynthetic alanine racemase (MycB alr)	P94967	ALR_MYCSM	Racemases and epimerases	D-alanine racemase; Alr; Alanine racemase; AlaR	MycB alr	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.	EC 5.1.1.1	.	MQTTEPMTPPAPLASAQTVIDLGAIDHNVRVLRELAGSADVMAVVKADAYGHGALPVARTALAAGAAALGVATIPEALALREGGITAPVLAWLHPPGTDFAPAIAADVEVAVSSRRQLEQVTAAAAEVGRTATVTVKVDTGLSRNGVGAADYPEVLDVLRRAQADGAIRVRGLMSHLVHGDDPENPFNGLQGQRLADMRVYAREHGVDYEVAHLCNSPAAMTRPDLAFEMVRPGISLYGLSPIPERGDMGLRPAMTLKCPVALVRSVHAGDGVSYGHRWVADRDTTLGLLPIGYADGVYRALSGRIDVLIKGRRRRAVGRICMDQFVVDLGPDADDVAVGDDAILFGPGANGEPTAQDWAELLDTIHYEVVTSPRGRVTRTYLPAGQQD	Successful	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	P94967
TTVH0YQ	Mycobacterium Fusion protein Rv2608-Rv3619-Rv3620-Rv1813 (MycB antigens)	P9WHZ5-P0DOA7-P9WNI3-P9WLS1	PPE42_MYCTU-ESXV_MYCTU-ESXW_MYCTU-Y1813_MYCTU	.	Mycobacterium Fusion protein PPE42-esxV-esxW-MTY16F9.01	MycB antigens	Invovled in immune response.	.	.	MTSRFMTDPHAMRDMAGRFEVHAQTVEDEARRMWASAQNISGAGWSGMAEATSLDTMTQMNQAFRNIVNMLHGVRDGLVRDANNYEQQEQASQQILSSMTINYQFGDVDAHGAMIRAQAGSLEAEHQAIISDVLTASDFWGGAGSAACQGFITQLGRNFQVIYEQANAHGQKVQAAGNNMAQTDSAVGSSWAMNFAVLPPEVNSARIFAGAGLGPMLAAASAWDGLAEELHAAAGSFASVTTGLAGDAWHGPASLAMTRAASPYVGWLNTAAGQAAQAAGQARLAASAFEATLAATVSPAMVAANRTRLASLVAANLLGQNAPAIAAAEAEYEQIWAQDVAAMFGYHSAASAVATQLAPIQEGLQQQLQNVLAQLASGNLGSGNVGVGNIGNDNIGNANIGFGNRGDANIGIGNIGDRNLGIGNTGNWNIGIGITGNGQIGFGKPANPDVLVVGNGGPGVTALVMGGTDSLLPLPNIPLLEYAARFITPVHPGYTATFLETPSQFFPFTGLNSLTYDVSVAQGVTNLHTAIMAQLAAGNEVVVFGTSQSATIATFEMRYLQSLPAHLRPGLDELSFTLTGNPNRPDGGILTRFGFSIPQLGFTLSGATPADAYPTVDYAFQYDGVNDFPKYPLNVFATANAIAGILFLHSGLIALPPDLASGVVQPVSSPDVLTTYILLPSQDLPLLVPLRAIPLLGNPLADLIQPDLRVLVELGYDRTAHQDVPSPFGLFPDVDWAEVAADLQQGAVQGVNDALSGLGLPPPWQPALPRLFMITNLRRRTAMAAAGLGAALGLGILLVPTVDAHLANGSMSEVMMSEIAGLPIPPIIHYGAIAYAPSGASGKAWHQRTPARAEQVALEKCGDKTCKVVSRFTRCGAVAYNGSKYQGGTGLTRRAAEDDAVNRLEGGRIVNWACN	Clinical trial	US patent application no. US20150182612 A1.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	P9WHZ5
TTJ4AN0	Mycobacterium Shikimate kinase (MycB aroK)	G0TQ18	G0TQ18_MYCCP	.	Shikimate kinase; MycB SK	MycB aroK	Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.	.	.	MAPKAVLVGLPGSGKSTIGRRLAKALGVSLLDTDVAIEQRTGRSIADIFATDGEQEFRRIEEDVVRAALADHDGVLSLGGGAVTSPGVRAALAGHTVVYLEISAAEGVRRTGGNTVRPLLAGPDRAEKYRALMAKRAPLYRRVATMRVDTNRRNPGAVVRYILSRLQVPSPSEAAT	Literature-reported	"Shikimate kinase, a protein target for drug design. Curr Med Chem. 2014;21(5):592-604."	.	.	.	.	.	.	.	.	.	.	.	"mce00400: Phenylalanine, tyrosine and tryptophan biosynthesis; mce01100: Metabolic pathways; mce01110: Biosynthesis of secondary metabolites; mce01230: Biosynthesis of amino acids"	.	.	.
TT0S4IF	Mycobacterium Glyoxylase CFP32 (MycB cfp32)	P9WIR3	CFP32_MYCTU	.	MycB Putative glyoxylase CFP32; 27 kDa antigen Cfp30B	MycB cfp32	"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."	.	3OXH	MPKRSEYRQGTPNWVDLQTTDQSAAKKFYTSLFGWGYDDNPVPGGGGVYSMATLNGEAVAAIAPMPPGAPEGMPPIWNTYIAVDDVDAVVDKVVPGGGQVMMPAFDIGDAGRMSFITDPTGAAVGLWQANRHIGATLVNETGTLIWNELLTDKPDLALAFYEAVVGLTHSSMEIAAGQNYRVLKAGDAEVGGCMEPPMPGVPNHWHVYFAVDDADATAAKAAAAGGQVIAEPADIPSVGRFAVLSDPQGAIFSVLKPAPQQ	Literature-reported	The Mycobacterium tuberculosis complex-restricted gene cfp32 encodes an expressed protein that is detectable in tuberculosis patients and is positi... Infect Immun. 2003 Dec;71(12):6871-83.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P9WIR3
TTKQU18	Mycobacterium 27kDa antigen Cfp30B (MycB cfp32)	O53774	CF30_MYCTU	.	MycB Putative glyoxylase CF30	MycB cfp32	"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."	.	3OXH	MPKRSEYRQGTPNWVDLQTTDQSAAKKFYTSLFGWGYDDNPVPGGGGVYSMATLNGEAVAAIAPMPPGAPEGMPPIWNTYIAVDDVDAVVDKVVPGGGQVMMPAFDIGDAGRMSFITDPTGAAVGLWQANRHIGATLVNETGTLIWNELLTDKPDLALAFYEAVVGLTHSSMEIAAGQNYRVLKAGDAEVGGCMEPPMPGVPNHWHVYFAVDDADATAAKAAAAGGQVIAEPADIPSVGRFAVLSDPQGAIFSVLKPAPQQ	Literature-reported	The Mycobacterium tuberculosis complex-restricted gene cfp32 encodes an expressed protein that is detectable in tuberculosis patients and is positi... Infect Immun. 2003 Dec;71(12):6871-83.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT08ESN	Mycobacterium Mycolic acid synthase (MycB cma)	P9WPB7; P9WPB5; P9WPB3	CMAS1_MYCTU; CMAS2_MYCTU; CMAS3_MYCTU	.	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	MycB cmaA1	"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."	.	.	MPDELKPHFANVQAHYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVEKYDVNVVGLTLSKNQANHVQQLVANSENLRSKRVLLAGWEQFDEPVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVMLLHTITGLHPKEIHERGLPMSFTFARFLKFIVTEIFPGGRLPSIPMVQECASANGFTVTRVQSLQPHYAKTLDLWSAALQANKGQAIALQSEEVYERYMKYLTGCAEMFRIGYIDVNQFTCQK	Successful	Role of long-chain acyl-CoAs in the regulation of mycolic acid biosynthesis in mycobacteria. Open Biol. 2017 Jul;7(7). pii: 170087.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P9WPB7
TTBK0PU	Mycobacterium Cytochrome p450 121 (MycB cyp121)	P0A515	CP121_MYCBO	Paired donor oxygen oxidoreductase	Cytochrome P450 MT2; Cytochrome P450 121	MycB cyp121	Catalyzes the formation of an intramolecular C-C bond between two tyrosyl carbon atoms of Cyy.	EC 1.14.-.-	5EDT	MTATVLLEVPFSARGDRIPDAVAELRTREPIRKVRTITGAEAWLVSSYALCTQVLEDRRFSMKETAAAGAPRLNALTVPPEVVNNMGNIADAGLRKAVMKAITPKAPGLEQFLRDTANSLLDNLITEGAPADLRNDFADPLATALHCKVLGIPQEDGPKLFRSLSIAFMSSADPIPAAKINWDRDIEYMAGILENPNITTGLMGELSRLRKDPAYSHVSDELFATIGVTFFGAGVISTGSFLTTALISLIQRPQLRNLLHEKPELIPAGVEELLRINLSFADGLPRLATADIQVGDVLVRKGELVLVLLEGANFDPEHFPNPGSIELDRPNPTSHLAFGRGQHFCPGSALGRRHAQIGIEALLKKMPGVDLAVPIDQLVWRTRFQRRIPERLPVLW	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P0A515
TTCS3P1	Mycobacterium D-alanine-D-alanine ligase A (MycB ddl)	P9WP31	DDL_MYCTU	Carbon-nitrogen ligase	ddlA; D-alanylalanine synthetase A; D-Ala-D-Ala ligase A	MycB ddl	Cell wall formation.	EC 6.3.2.4	3LWB	MSANDRRDRRVRVAVVFGGRSNEHAISCVSAGSILRNLDSRRFDVIAVGITPAGSWVLTDANPDALTITNRELPQVKSGSGTELALPADPRRGGQLVSLPPGAGEVLESVDVVFPVLHGPYGEDGTIQGLLELAGVPYVGAGVLASAVGMDKEFTKKLLAADGLPVGAYAVLRPPRSTLHRQECERLGLPVFVKPARGGSSIGVSRVSSWDQLPAAVARARRHDPKVIVEAAISGRELECGVLEMPDGTLEASTLGEIRVAGVRGREDSFYDFATKYLDDAAELDVPAKVDDQVAEAIRQLAIRAFAAIDCRGLARVDFFLTDDGPVINEINTMPGFTTISMYPRMWAASGVDYPTLLATMIETTLARGVGLH	Successful	"Self-protection mechanism in D-cycloserine-producing Streptomyces lavendulae. Gene cloning, characterization, and kinetics of its alanine racemase ... J Biol Chem. 2004 Oct 29;279(44):46143-52."	34	.	.	.	.	.	.	.	.	.	.	mtu00473:D-Alanine metabolism; mtu00550:Peptidoglycan biosynthesis; mtu01100:Metabolic pathways; mtu01502:Vancomycin resistance	.	MetaCyc:G185E-7236-MON	P9WP31
TTT8SED	Mycobacterium D-alanine-D-alanine ligase (MycB ddl)	P9WP30	DDL_MYCTO	Carbon-nitrogen ligase	ddl; D-alanylalanine synthetase; D-alanine:D-alanine ligase; D-Ala-D-Ala ligase	MycB ddl	Cell wall formation.	EC 6.3.2.4	.	MSANDRRDRRVRVAVVFGGRSNEHAISCVSAGSILRNLDSRRFDVIAVGITPAGSWVLTDANPDALTITNRELPQVKSGSGTELALPADPRRGGQLVSLPPGAGEVLESVDVVFPVLHGPYGEDGTIQGLLELAGVPYVGAGVLASAVGMDKEFTKKLLAADGLPVGAYAVLRPPRSTLHRQECERLGLPVFVKPARGGSSIGVSRVSSWDQLPAAVARARRHDPKVIVEAAISGRELECGVLEMPDGTLEASTLGEIRVAGVRGREDSFYDFATKYLDDAAELDVPAKVDDQVAEAIRQLAIRAFAAIDCRGLARVDFFLTDDGPVINEINTMPGFTTISMYPRMWAASGVDYPTLLATMIETALARGVGLH	Successful	D-Ala-D-Ala ligases from glycopeptide antibiotic-producing organisms are highly homologous to the enterococcal vancomycin-resistance ligases VanA and VanB. Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6480-3.	34	.	.	.	.	.	.	.	.	.	.	mtc00473:D-Alanine metabolism; mtc00550:Peptidoglycan biosynthesis; mtc01100:Metabolic pathways; mtc01502:Vancomycin resistance	.	.	P9WP30
TTB91WX	Mycobacterium Arabinosyltransferase A (MycB embA)	P71485	EMBA_MYCAV	.	Probable arabinosyltransferase A	MycB embA	Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan.	EC 2.4.2.-	.	MPHDGKQRSQRIPRSVAAVAGIAGLLLCLAVPLLPVRQTTATVLWPQGTVDGHVSQITAPLVSGAPRALDISIPCPAVATLPADGGLVVSTLPPGGMDAGKNGLFVRANKDVVVVAFRDTVAAVAQRPAVAAGACSVLHAWADAGAAGAEFVGIPGAAGTLPAEKKPQVGGIFTDLKVPAGPGLSARVDIDTRFITAPTVLKQIVMVLGTLAVLTAIVALAVLDRRSRGGGTLINWRSPIAWLSRYRPGTHLANWRRVGLATWIADAAVLATLLLWHVVGATSSDDGYNLTIARVAPKAGYLVDYYRYFGTTDAPFDWYLGLLSRLASVSTAGVWMRLPATLAGIGCWLIISHWVLRRLGPGRGGLAANRVAVFTAGAVFVAAWLPFNNGLRPEPLIALGVLVTWMLVERAIALQRLAPAAVAVVVALLTATLAPQGLIAVAALLTGARAVAQAIRRRRASDGLLAPLAVLAAALSLILVVVFRSQTVATVLESARIKYKVGPTIAWYQDWLRYYFLTVESNPDGSMARRFAVLVMLLCLFGMLVILLRRGHVPGVASGPRWRLIGTTAVGLLLLTFTPTKWAVQFGAFAGLAGALGALTAFACSRIGLHNRRNLTLYVTALLFVLAWATSGINGWFYVGNYGVPWYDIQPVIASHPVTSMFLTLSIITGLLAAWQHFRMDYAGHTEVKDSRRNRVLASTPLLVVATIMVVGEVASLTKGAVFRYPLYTTGKANLAAIASGLSPTSCAMADDVLAEPDANAGMLQPLPGQTFGPDGPLGGVNPVGFKPDGVGDDLQSDPVVTKPGLVNSDASPNKPNVAYSDSAGTAGGKGPVGVNGSHAALPFGLDPARTPVMGSYGENSLAATATSAWYQLPPRTPDRPLVVVSAAGAIWSYKEDGTFTYGQSLKLQWGVARPDGSTVPLAEVQPIDIGPQPAWRNLRFPLAWAPPEANVARIVAYDPNLSSEQWFAFTPPRVPVTETLQQLIGSQTPVMMDIATAANFPCQRPFSEHLGVAELPAYRILPDRKQTAASSNLWQSSEAGGPFLFLQALLRTSTIPTYLRGDWYRDWGSVEQYFRLVPADQAPDAAIEQGVMTVHGWSRQGPIRALP	Literature-reported	The embAB genes of Mycobacterium avium encode an arabinosyl transferase involved in cell wall arabinan biosynthesis that is the target for the anti... Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11919-24.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P71485
TTSBUH3	Mycobacterium Arabinosyltransferase B (MycB embB)	P71486	EMBB_MYCAV	.	Probable arabinosyltransferase B	MycB embB	Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan.	EC 2.4.2.-	.	MSVSTVGGDVRVTRWVATIAGLIGFVLSVATPLLPVVQTTATLNWPQGGQLNSVTAPLISLTPVDLTATVPCSLVRDLPPGGGVILSTGPKKGKDAALNALFVVAHGKRVDVTDRNVVIASASRDQVAGAGCSRIEIASTRAGTFATFVGLTDPAGKPLGGGFPDPNLRPQIVGVFTDLTGPAPAGLKLSATIDTRFSTTPTTLKLAAMVTAILATIVALVALWRLDQLDGHRMRRLIPANWRTFTLADVAVIFGFVLWHVIGANSSDDGYILGMARVADRAGYMSNYFRWFGSPEDPFGWYYNLLALMTHVSDASLWMRLPDLFAGIVCWLLLSREVLPRLGPAVAASRPANWAAGMVLLTAWMPFDNGLRPEPIIALGSLVTYVLIERSMRYSRLTPAALAVITAAFTLGVQPTGLIAVAALVAGGRPILRILVRRHRVVGTWPLVAPMLAAGTVILTVVFADQTLATVLEATRIRTAIGPSQAWYTENLRYYYLILPTVDGSLSRRFGFLITALCLFTAVFIMLRRKRIPGVARGPAWRLMGVIFGTMFFLMFTPTKWVHHFGLFAAVGAAMAALTTVLVSPAVLGWSRNRMAFLAALLFMMALCFATTNGWWYVSSYGVPFNSTMPKIGGITVSTVFFSMFVAAALYAIWLHFASREHGEGRLARALTAAPVPLAAGFMALVFIASMVAGIVRQYPTYSNAWDNLREFSGGCGLADDVLVEPDSNVGYMTPLGGDYGPLGPLGGQHPVGFSPNGVPEHTVAEAIRITPNQPGTDYDWDAPTKLSAPGINGSTVPLPYGLDAARVPLAGSYTTGAQQQSRLTSAWYRLPAPDDGHPLVVVTAAGKIAGNSVLHHHTDGQTVVLEYGRPGPGGDIVPAGRLVPYDLYGEQPKAWRNLRFARSDMPADTVAVRVVAEDLSLTPEDWIAVTPPRVPEMRSLQEYVGSTQPVLMDWAVGLAFPCQQPMLHVNGVTEIPKFRITPDYTAKKMDTDTWEDGTNGGLLGITDLLLRAHVMSTYLSHDWGRDWGSLRRFETIADAHPAQLDLGTATRTGWWSPGPIRIKP	Literature-reported	The embAB genes of Mycobacterium avium encode an arabinosyl transferase involved in cell wall arabinan biosynthesis that is the target for the anti... Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11919-24.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P71486
TT1Q8GP	Mycobacterium Arabinosyltransferase C (MycB embC)	P9WNL5	EMBC_MYCTU	.	Probable arabinosyltransferase C	MycB embC	Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan.	EC 2.4.2.-	3PTY	MATEAAPPRIAVRLPSTSVRDAGANYRIARYVAVVAGLLGAVLAIATPLLPVNQTTAQLNWPQNGTFASVEAPLIGYVATDLNITVPCQAAAGLAGSQNTGKTVLLSTVPKQAPKAVDRGLLLQRANDDLVLVVRNVPLVTAPLSQVLGPTCQRLTFTAHADRVAAEFVGLVQGPNAEHPGAPLRGERSGYDFRPQIVGVFTDLAGPAPPGLSFSASVDTRYSSSPTPLKMAAMILGVALTGAALVALHILDTADGMRHRRFLPARWWSTGGLDTLVIAVLVWWHFVGANTSDDGYILTMARVSEHAGYMANYYRWFGTPEAPFGWYYDLLALWAHVSTASIWMRLPTLAMALTCWWVISREVIPRLGHAVKTSRAAAWTAAGMFLAVWLPLDNGLRPEPIIALGILLTWCSVERAVATSRLLPVAIACIIGALTLFSGPTGIASIGALLVAIGPLRTILHRRSRRFGVLPLVAPILAAATVTAIPIFRDQTFAGEIQANLLKRAVGPSLKWFDEHIRYERLFMASPDGSIARRFAVLALVLALAVSVAMSLRKGRIPGTAAGPSRRIIGITIISFLAMMFTPTKWTHHFGVFAGLAGSLGALAAVAVTGAAMRSRRNRTVFAAVVVFVLALSFASVNGWWYVSNFGVPWSNSFPKWRWSLTTALLELTVLVLLLAAWFHFVANGDGRRTARPTRFRARLAGIVQSPLAIATWLLVLFEVVSLTQAMISQYPAWSVGRSNLQALAGKTCGLAEDVLVELDPNAGMLAPVTAPLADALGAGLSEAFTPNGIPADVTADPVMERPGDRSFLNDDGLITGSEPGTEGGTTAAPGINGSRARLPYNLDPARTPVLGSWRAGVQVPAMLRSGWYRLPTNEQRDRAPLLVVTAAGRFDSREVRLQWATDEQAAAGHHGGSMEFADVGAAPAWRNLRAPLSAIPSTATQVRLVADDQDLAPQHWIALTPPRIPRVRTLQNVVGAADPVFLDWLVGLAFPCQRPFGHQYGVDETPKWRILPDRFGAEANSPVMDHNGGGPLGITELLMRATTVASYLKDDWFRDWGALQRLTPYYPDAQPADLNLGTVTRSGLWSPAPLRRG	Successful	The arabinosyltransferase EmbC is inhibited by ethambutol in Mycobacterium tuberculosis. Antimicrob Agents Chemother. 2009 Oct;53(10):4138-46.	34	.	.	.	.	.	.	.	.	.	.	mtu00571: Lipoarabinomannan (LAM) biosynthesis	.	MetaCyc:G185E-8089-MON	P9WNL5
TTHP87B	Mycobacterium 6kDa early secretory antigenic target (MycB esxA)	P9WNK7	ESXA_MYCTU	.	ESAT-6; 6 kDa early secretory antigenic target	MycB esxA	"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)."	.	3FAV; 1WA8	MTEQQWNFAGIEAAASAIQGNVTSIHSLLDEGKQSLTKLAAAWGGSGSEAYQGVQQKWDATATELNNALQNLARTISEAGQAMASTEGNVTGMFA	Literature-reported	Mycobacterium tuberculosis ESAT6 induces IFN- gene expression in Macrophages via TLRs-mediated signaling. Cytokine. 2018 Apr;104:104-109.	.	.	.	.	.	.	.	.	.	.	.	mtu05152: Tuberculosis	R-HSA-9636667: Manipulation of host energy metabolism; R-HSA-9637628: Modulation by Mtb of host immune system	.	P9WNK7
TTAGENB	Mycobacterium Malonyl-CoA:acyl carrier transacylase (MycB fabD)	P63459	FABD_MYCBO	Acyltransferase	Malonyl CoA-acyl carrier protein transacylase; MCT	MycB fabD	"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."	EC 2.3.1.39	.	MIALLAPGQGSQTEGMLSPWLQLPGAADQIAAWSKAADLDLARLGTTASTEEITDTAVAQPLIVAATLLAHQELARRCVLAGKDVIVAGHSVGEIAAYAIAGVIAADDAVALAATRGAEMAKACATEPTGMSAVLGGDETEVLSRLEQLDLVPANRNAAGQIVAAGRLTALEKLAEDPPAKARVRALGVAGAFHTEFMAPALDGFAAAAANIATADPTATLLSNRDGKPVTSAAAAMDTLVSQLTQPVRWDLCTATLREHTVTAIVEFPPAGTLSGIAKRELRGVPARAVKSPADLDELANL	Literature-reported	"Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuber... J Biol Chem. 2001 Jul 27;276(30):27967-74."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P63459
TTB859L	Mycobacterium Beta-ketoacyl-ACP reductase (MycB fabG1)	P9WGT3	FABG_MYCTU	.	Beta-ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; 3-oxoacyl-[acyl-carrier-protein] reductase FabG1; 3-ketoacyl-acyl carrier protein reductase	MycB fabG1	"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."	.	2NTN; 1UZN; 1UZM; 1UZL	MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH	Literature-reported	Ligand-induced fit in mycobacterial MabA: the sequence-specific C-terminus locks the conformational change. Proteins. 2005 Aug 15;60(3):392-400.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZYJ8U	Mycobacterium Antigen complex 85A (MycB fbpA)	P9WQP3	A85A_MYCTU	Acyltransferase	Fibronectinbinding protein A; Fbps A; Diacylglycerol acyltransferase/mycolyltransferase Ag85A; Antigen 85 complex A; Ag85A; AcylCoA:diacylglycerol acyltransferase; 85A	MycB fbpA	"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."	.	1SFR	MQLVDRVRGAVTGMSRRLVVGAVGAALVSGLVGAVGGTATAGAFSRPGLPVEYLQVPSPSMGRDIKVQFQSGGANSPALYLLDGLRAQDDFSGWDINTPAFEWYDQSGLSVVMPVGGQSSFYSDWYQPACGKAGCQTYKWETFLTSELPGWLQANRHVKPTGSAVVGLSMAASSALTLAIYHPQQFVYAGAMSGLLDPSQAMGPTLIGLAMGDAGGYKASDMWGPKEDPAWQRNDPLLNVGKLIANNTRVWVYCGNGKPSDLGGNNLPAKFLEGFVRTSNIKFQDAYNAGGGHNGVFDFPDSGTHSWEYWGAQLNAMKPDLQRALGATPNTGPAPQGA	Clinical trial	"MVA-85A, a novel candidate booster vaccine for the prevention of tuberculosis in children and adults. Curr Opin Mol Ther. 2010 Feb;12(1):124-34."	21	.	.	.	.	.	.	.	.	.	.	mtu00561:Glycerolipid metabolism; mtu01100:Metabolic pathways	.	MetaCyc:G185E-8100-MON	P9WQP3
TTF8O7H	Mycobacterium 30kDa major secretory protein (MycB fbpB)	P31952	A85B_MYCTU	Acyltransferase	Mycolyl transferase 85B; Fibronectin-binding protein B; Extracellular alpha-antigen; Antigen 85B; Antigen 85 complex B; Ag85B; 85B; 30 kDa extracellular protein	MycB fbpB	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).	.	5TS1; 5TRZ; 1F0P; 1F0N	MTDVSRKIRAWGRRLMIGTAAAVVLPGLVGLAGGAATAGAFSRPGLPVEYLQVPSPSMGRDIKVQFQSGGNNSPAVYLLDGLRAQDDYNGWDINTPAFEWYYQSGLSIVMPVGGQSSFYSDWYSPACGKAGCQTYKWETFLTSELPQWLSANRAVKPTGSAAIGLSMAGSSAMILAAYHPQQFIYAGSLSALLDPSQGMGPSLIGLAMGDAGGYKAADMWGPSSDPAWERNDPTQQIPKLVANNTRLWVYCGNGTPNELGGANIPAEFLENFVRSSNLKFQDAYNAAGGHNAVFNFPPNGTHSWEYWGAQLNAMKGDLQSSLGAG	Literature-reported	An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30 kDa major secretory pr... J Mol Biol. 2001 Mar 23;307(2):671-81.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P9WQP1
TTTO9MF	Mycobacterium Alpha-glucan:maltose-phosphate maltosyltransferase (MycB glgE)	P9WQ17	GLGE_MYCTU	Glycosyl transferase	"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"	MycB glgE	"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."	.	.	MSGRAIGTETEWWVPGRVEIDDVAPVVSCGVYPAKAVVGEVVPVSAAVWREGHEAVAATLVVRYLGVRYPHLTDRPRARVLPTPSEPQQRVKPLLIPMTSGQEPFVFHGQFTPDRVGLWTFRVDGWGDPIHTWRHGLIAKLDAGQGETELSNDLLVGAVLLERAATGVPRGLRDPLLAAAAALRTPGDPVTRTALALTPEIEELLADYPLRDLVTRGEQFGVWVDRPLARFGAWYEMFPRSTGGWDDDGNPVHGTFATAAAELPRIAGMGFDVVYLPPIHPIGKVHRKGRNNSPTAAPTDVGSPWAIGSDEGGHDTVHPSLGTIDDFDDFVSAARDLGMEVALDLALQCAPDHPWAREHRQWFTELPDGTIAYAENPPKKYQDIYPLNFDNDPEGLYDEVLRVVQHWVNHGVKFFRVDNPHTKPPNFWAWLIAQVKTVDPDVLFLSEAFTPPARQYGLAKLGFTQSYSYFTWRTTKWELTEFGNQIAELADYRRPNLFVNTPDILHAVLQHNGPGMFAIRAVLAATMSPAWGMYCGYELFEHRAVREGSEEYLDSEKYELRPRDFASALDQGRSLQPFITRLNIIRRLHPAFQQLRTIHFHHVDNDALLAYSKFDPATGDCVLVVVTLNAFGPEEATLWLDMAALGMEDYDRFWVRDEITGEEYQWGQANYIRIDPARAVAHIINMPAVPYESRNTLLRRR	Literature-reported	The significance of GlgE as a new target for tuberculosis. Drug News Perspect. 2010 Dec;23(10):619-24.	.	.	.	.	.	.	.	.	.	.	.	mtu00500: Starch and sucrose metabolism; mtu01100: Metabolic pathways	.	MetaCyc:G185E-5506-MON	P9WQ17
TTOZVUM	Mycobacterium Phosphoglucosamine mutase (MycB glmM)	A5U8B7	GLMM_MYCTA	Intramolecular transferases	glmM of Mycobacterium tuberculosis	MycB glmM	Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.	EC 5.4.2.10	.	MGRLFGTDGVRGVANRELTAELALALGAAAARRLSRSGAPGRRVAVLGRDPRASGEMLEAAVIAGLTSEGVDALRVGVLPTPAVAYLTGAYDADFGVMISASHNPMPDNGIKIFGPGGHKLDDDTEDQIEDLVLGVSRGPGLRPAGAGIGRVIDAEDATERYLRHVAKAATARLDDLAVVVDCAHGAASSAAPRAYRAAGARVIAINAEPNGRNINDGCGSTHLDPLRAAVLAHRADLGLAHDGDADRCLAVDANGDLVDGDAIMVVLALAMKEAGELACNTLVATVMSNLGLHLAMRSAGVTVRTTAVGDRYVLEELRAGDYSLGGEQSGHIVMPALGSTGDGIVTGLRLMTRMVQTGSSLSDLASAMRTLPQVLINVEVVDKATAAAAPSVRTAVEQAAAELGDTGRILLRPSGTEPMIRVMVEAADEGVAQRLAATVADAVSTAR	Literature-reported	Effect of phosphoglucosamine mutase on biofilm formation and antimicrobial susceptibilities in M. smegmatis glmM gene knockdown strain. PLoS One. 2013 Apr 10;8(4):e61589.	.	.	.	.	.	.	.	.	.	.	.	mra00520: Amino sugar and nucleotide sugar metabolism; mra01100: Metabolic pathways; mra01250: Biosynthesis of nucleotide sugars	.	.	A5U8B7
TT8R2M4	Mycobacterium Bifunctional protein GlmU (MycB glmU)	P9WMN3	GLMU_MYCTU	.	Bifunctional protein GlmU	MycB glmU	"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."	.	4HCQ; 4G87; 4G3S; 4G3Q; 4G3P	MTFPGDTAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADTLGRTIDVALQDRPLGTGHAVLCGLSALPDDYAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIVEQTDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQLAELASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGASVVRTHGSSSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSKRRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQRKRPGSPAAQASKRASEMACQQPTQPPDADQTP	Literature-reported	UDP-GlcNAc pathway: Potential target for inhibitor discovery against M. tuberculosis. Eur J Pharm Sci. 2016 Feb 15;83:62-70.	.	.	.	.	.	.	.	.	.	.	.	mtu00520: Amino sugar and nucleotide sugar metabolism; mtu00541: O-Antigen nucleotide sugar biosynthesis; mtu01100: Metabolic pathways; mtu01250: Biosynthesis of nucleotide sugars	.	.	P9WMN3
TTHJWVK	Mycobacterium Bisphosphoglycerate phosphoglycerate mutase (MycB gpmI)	P47669	GPMI_MYCGE	Intramolecular transferases	gpmI; Phosphoglyceromutase; Phosphoglycerate mutase; IPGM; BPG-independent PGAM	MycB gpmI	Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.	.	.	MHKKVLLAILDGYGISNAIYGNAVQNANTPMLDELINSYPCVLLDASGEAVGLPMGQIGNSEVGHLNIGAGRVVYTGLSLINQHIKDRSFFANKAFLKTIEHVEKNHSKIHLIGLFSNGGVHSHNEHLLALIELFSKHAKVVLHLFGDGRDVAPCSLKQDLEKLMIFLKNYPNVVIGTIGGRYYGMDRDQRWDREMIAYKALLGVSKNKFNDPIGYIETQYQNQITDEFIYPAINANLNSDQFALNNNDGVIFFNFRPDRARQMSHLIFNSNYYNYQPELKRKENLFFVTMMNYEGIVPSEFAFPPQTIKNSLGEVIANNNLKQLRIAETEKYAHVTFFFDGGFEVNLSNETKTLIPSLKVATYDLAPEMSCKAITDALLEKLNNFDFTVLNFANPDMVGHTGNYQACIKALEALDVQIKRIVDFCKANQITMFLTADHGNAEVMIDNNNNPVTKHTINPVPFVCTDKNVNFNQTGILANIAPTILEYLNLSKPKEMTAKSLLKNNN	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	"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"	.	.	P47669
TTVQGI2	Mycobacterium Heat shock protein 65 (MycB groL2)	P0A521	CH602_MYCBO	.	Protein Cpn60-2; Heat shock protein 65; GroEL protein 2; Cell wall protein A; Antigen A; 65 kDa antigen; 60 kDa chaperonin 2	MycB groL2	Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	.	.	MAKTIAYDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKGAKEVETKEQIAATAAISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDPERQEAVLEDPYILLVSSKVSTVKDLLPLLEKVIGAGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISEEVGLTLENADLSLLGKARKVVVTKDETTIVEGAGDTDAIAGRVAQIRQEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVTLLQAAPTLDELKLEGDEATGANIVKVALEAPLKQIAFNSGLEPGVVAEKVRNLPAGHGLNAQTGVYEDLLAAGVADPVKVTRSALQNAASIAGLFLTTEAVVADKPEKEKASVPGGGDMGGMDF	Discontinued	"Activity of HspE7, a novel immunotherapy, in patients with anogenital warts. Dis Colon Rectum. 2002 Apr;45(4):502-7."	9	.	.	.	.	.	.	.	.	.	.	.	.	.	P0A521
TTU3AL1	Mycobacterium Meta-cleavage product hydrolase (MycB HsaD)	P9WNH5	HSAD_MYCTU	.	"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"	MycB HsaD	"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)."	EC 3.7.1.17	5JZS; 5JZB; 2WUG; 2WUF; 2WUE	MTATEELTFESTSRFAEVDVDGPLKLHYHEAGVGNDQTVVLLHGGGPGAASWTNFSRNIAVLARHFHVLAVDQPGYGHSDKRAEHGQFNRYAAMALKGLFDQLGLGRVPLVGNSLGGGTAVRFALDYPARAGRLVLMGPGGLSINLFAPDPTEGVKRLSKFSVAPTRENLEAFLRVMVYDKNLITPELVDQRFALASTPESLTATRAMGKSFAGADFEAGMMWREVYRLRQPVLLIWGREDRVNPLDGALVALKTIPRAQLHVFGQCGHWVQVEKFDEFNKLTIEFLGGGR	Literature-reported	Investigation of the mycobacterial enzyme HsaD as a potential novel target for anti-tubercular agents using a fragment-based drug design approach. Br J Pharmacol. 2017 Jul;174(14):2209-2224.	.	.	.	.	.	.	.	.	.	.	.	mtu00984: Steroid degradation; mtu01100: Metabolic pathways; mtu01120: Microbial metabolism in diverse environments; mtu01220: Degradation of aromatic compounds	.	MetaCyc:G185E-7847-MON	P9WNH5
TT58ZYW	Mycobacterium Isocitrate lyase (MycB icl)	P9WKK7	ACEA_MYCTU	Carbon-carbon lyase	Isocitratase; Isocitrase; ICL	MycB icl	"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."	EC 4.1.3.1	5DQL; 1F8M; 1F8I; 1F61	MSVVGTPKSAEQIQQEWDTNPRWKDVTRTYSAEDVVALQGSVVEEHTLARRGAEVLWEQLHDLEWVNALGALTGNMAVQQVRAGLKAIYLSGWQVAGDANLSGHTYPDQSLYPANSVPQVVRRINNALQRADQIAKIEGDTSVENWLAPIVADGEAGFGGALNVYELQKALIAAGVAGSHWEDQLASEKKCGHLGGKVLIPTQQHIRTLTSARLAADVADVPTVVIARTDAEAATLITSDVDERDQPFITGERTREGFYRTKNGIEPCIARAKAYAPFADLIWMETGTPDLEAARQFSEAVKAEYPDQMLAYNCSPSFNWKKHLDDATIAKFQKELAAMGFKFQFITLAGFHALNYSMFDLAYGYAQNQMSAYVELQEREFAAEERGYTATKHQREVGAGYFDRIATTVDPNSSTTALTGSTEEGQFH	Literature-reported	"Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis. Nat Struct Biol. 2000 Aug;7(8):663-8."	0	.	.	.	.	.	.	.	.	.	.	mtu00630:Glyoxylate and dicarboxylate metabolism; mtu01100:Metabolic pathways; mtu01110:Biosynthesis of secondary metabolites; mtu01120:Microbial metabolism in diverse environments; mtu01200:Carbon metabolism	.	MetaCyc:G185E-4594-MON	P9WKK7
TTPH97Y	Mycobacterium 3-oxoacyl-[acyl-carrier-protein] synthase 1 (MycB kasA)	P9WQD9	FAB1_MYCTU	Acyltransferase	kasA; KAS 1; Beta-ketoacyl-ACP synthase 1	MycB kasA	Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-acp.	EC 2.3.1.41	5LD8; 2WGG; 2WGF; 2WGE; 2WGD	MSQPSTANGGFPSVVVTAVTATTSISPDIESTWKGLLAGESGIHALEDEFVTKWDLAVKIGGHLKDPVDSHMGRLDMRRMSYVQRMGKLLGGQLWESAGSPEVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIRVAGCDQAAVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFGRY	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	MetaCyc:G185E-6461-MON	.
TT46T5G	Mycobacterium Leucine-tRNA ligase (MycB leuS)	P9WFV1	SYL_MYCTU	.	Leucyl-tRNA synthetase; LeuRS	MycB leuS	.	EC 6.1.1.4	.	MTESPTAGPGGVPRADDADSDVPRYRYTAELAARLERTWQENWARLGTFNVPNPVGSLAPPDGAAVPDDKLFVQDMFPYPSGEGLHVGHPLGYIATDVYARYFRMVGRNVLHALGFDAFGLPAEQYAVQTGTHPRTRTEANVVNFRRQLGRLGFGHDSRRSFSTTDVDFYRWTQWIFLQIYNAWFDTTANKARPISELVAEFESGARCLDGGRDWAKLTAGERADVIDEYRLVYRADSLVNWCPGLGTVLANEEVTADGRSDRGNFPVFRKRLRQWMMRITAYADRLLDDLDVLDWPEQVKTMQRNWIGRSTGAVALFSARAASDDGFEVDIEVFTTRPDTLFGATYLVLAPEHDLVDELVAASWPAGVNPLWTYGGGTPGEAIAAYRRAIAAKSDLERQESREKTGVFLGSYAINPANGEPVPIFIADYVLAGYGTGAIMAVPGHDQRDWDFARAFGLPIVEVIAGGNISESAYTGDGILVNSDYLNGMSVPAAKRAIVDRLESAGRGRARIEFKLRDWLFARQRYWGEPFPIVYDSDGRPHALDEAALPVELPDVPDYSPVLFDPDDADSEPSPPLAKATEWVHVDLDLGDGLKPYSRDTNVMPQWAGSSWYELRYTDPHNSERFCAKENEAYWMGPRPAEHGPDDPGGVDLYVGGAEHAVLHLLYSRFWHKVLYDLGHVSSREPYRRLVNQGYIQAYAYTDARGSYVPAEQVIERGDRFVYPGPDGEVEVFQEFGKIGKSLKNSVSPDEICDAYGADTLRVYEMSMGPLEASRPWATKDVVGAYRFLQRVWRLVVDEHTGETRVADGVELDIDTLRALHRTIVGVSEDFAALRNNTATAKLIEYTNHLTKKHRDAVPRAAVEPLVQMLAPLAPHIAEELWLRLGNTTSLAHGPFPKADAAYLVDETVEYPVQVNGKVRGRVVVAADTDEETLKAAVLTDEKVQAFLAGATPRKVIVVAGRLVNLVI	Clinical trial	"Discovery of a Potent and Specific M. tuberculosis Leucyl-tRNA Synthetase Inhibitor: (S)-3-(Aminomethyl)-4-chloro-7-(2-hydroxyethoxy)benzo[c][1,2]oxaborol-1(3H)-ol (GSK656). J Med Chem. 2017 Oct 12;60(19):8011-8026."	.	.	.	.	.	.	.	.	.	.	.	mtu00970: Aminoacyl-tRNA biosynthesis	.	.	P9WFV1
TTTU2LD	Mycobacterium Primase (MycB ligD)	P9WNV3	LIGD_MYCTU	.	NHEJ DNA repair protein D; NHEJ DNA polymerase; Multifunctional non-homologous end joining DNA repair protein LigD; Mt-Lig	MycB ligD	"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."	.	4MKY; 3PKY; 2R9L; 2IRY; 2IRX	MGSASEQRVTLTNADKVLYPATGTTKSDIFDYYAGVAEVMLGHIAGRPATRKRWPNGVDQPAFFEKQLALSAPPWLSRATVAHRSGTTTYPIIDSATGLAWIAQQAALEVHVPQWRFVAEPGSGELNPGPATRLVFDLDPGEGVMMAQLAEVARAVRDLLADIGLVTFPVTSGSKGLHLYTPLDEPVSSRGATVLAKRVAQRLEQAMPALVTSTMTKSLRAGKVFVDWSQNSGSKTTIAPYSLRGRTHPTVAAPRTWAELDDPALRQLSYDEVLTRIARDGDLLERLDADAPVADRLTRYRRMRDASKTPEPIPTAKPVTGDGNTFVIQEHHARRPHYDFRLECDGVLVSWAVPKNLPDNTSVNHLAIHTEDHPLEYATFEGAIPSGEYGAGKVIIWDSGTYDTEKFHDDPHTGEVIVNLHGGRISGRYALIRTNGDRWLAHRLKNQKDQKVFEFDNLAPMLATHGTVAGLKASQWAFEGKWDGYRLLVEADHGAVRLRSRSGRDVTAEYPQLRALAEDLADHHVVLDGEAVVLDSSGVPSFSQMQNRGRDTRVEFWAFDLLYLDGRALLGTRYQDRRKLLETLANATSLTVPELLPGDGAQAFACSRKHGWEGVIAKRRDSRYQPGRRCASWVKDKHWNTQEVVIGGWRAGEGGRSSGVGSLLMGIPGPGGLQFAGRVGTGLSERELANLKEMLAPLHTDESPFDVPLPARDAKGITYVKPALVAEVRYSEWTPEGRLRQSSWRGLRPDKKPSEVVRE	Literature-reported	Thermally denaturing high-performance liquid chromatography analysis of primase activity. Anal Biochem. 2004 Sep 15;332(2):330-6.	.	.	.	.	.	.	.	.	.	.	.	mtu03450: Non-homologous end-joining	.	.	P9WNV3
TTTLB3R	Mycobacterium Membrane protein mmpL3 (MycB mmpL3)	P9WJV5	MMPL3_MYCTU	.	Trehalose monomycolate exporter MmpL3; TMM exporter MmpL3	MycB mmpL3	Transports trehalose monomycolate (TMM) across the inner membrane. Could also be part of a heme-iron acquisition system.	.	.	MFAWWGRTVYRYRFIVIGVMVALCLGGGVFGLSLGKHVTQSGFYDDGSQSVQASVLGDQVYGRDRSGHIVAIFQAPAGKTVDDPAWSKKVVDELNRFQQDHPDQVLGWAGYLRASQATGMATADKKYTFVSIPLKGDDDDTILNNYKAIAPDLQRLDGGTVKLAGLQPVAEALTGTIATDQRRMEVLALPLVAVVLFFVFGGVIAAGLPVMVGGLCIAGALGIMRFLAIFGPVHYFAQPVVSLIGLGIAIDYGLFIVSRFREEIAEGYDTETAVRRTVITAGRTVTFSAVLIVASAIGLLLFPQGFLKSLTYATIASVMLSAILSITVLPACLGILGKHVDALGVRTLFRVPFLANWKISAAYLNWLADRLQRTKTREEVEAGFWGKLVNRVMKRPVLFAAPIVIIMILLIIPVGKLSLGGISEKYLPPTNSVRQAQEEFDKLFPGYRTNPLTLVIQTSNHQPVTDAQIADIRSKAMAIGGFIEPDNDPANMWQERAYAVGASKDPSVRVLQNGLINPADASKKLTELRAITPPKGITVLVGGTPALELDSIHGLFAKMPLMVVILLTTTIVLMFLAFGSVVLPIKATLMSALTLGSTMGILTWIFVDGHFSKWLNFTPTPLTAPVIGLIIALVFGLSTDYEVFLVSRMVEARERGMSTQEAIRIGTAATGRIITAAALIVAVVAGAFVFSDLVMMKYLAFGLMAALLLDATVVRMFLVPSVMKLLGDDCWWAPRWARRLQTRIGLGEIHLPDERKRPVSNGRPARPPVTAGLVAARAAGDPRPPHDPTHPLAESPRPARSSPASSPELTPALEATAAPAAPSGASTTRMQIGSSTEPPTTRLAAAGRSVQSPASTPPPTPTPPSAPSAGQTRAMPLAANRSTDAAGDPAEPTAALPIIRSDGDDSEAATEQLNARGTSDKTRQRRRGGGALSAQDLLRREGRL	Clinical trial	"SQ109 targets MmpL3, a membrane transporter of trehalose monomycolate involved in mycolic acid donation to the cell wall core of Mycobacterium tuberculosis. Antimicrob Agents Chemother. 2012 Apr;56(4):1797-809."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	P9WJV5
TTLYJGT	Mycobacterium Immunogenic protein MPT63/MPB63 (MycB mpt63)	P97175	MP63_MYCTU	.	Immunogenic protein MPT63; Antigen MPT63; 16 kDa immunoprotective extracellular protein	MycB mpt63	A secreted protein of unknown function that is specific to mycobacteria.	.	1LMI	MKLTTMIKTAVAVVAMAAIATFAAPVALAAYPITGKLGSELTMTDTVGQVVLGWKVSDLKSSTAVIPGYPVAGQVWEATATVNAIRGSVTPAVSQFNARTADGINYRVLWQAAGPDTISGATIPQGEQSTGKIYFDVTGPSPTIVAMNNGMEDLLIWEP	Literature-reported	Crystal structure of a major secreted protein of Mycobacterium tuberculosis-MPT63 at 1.5-A resolution. Protein Sci. 2002 Dec;11(12):2887-93.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P9WIP1
TTH29K0	Mycobacterium Nicotinate-nucleotide pyrophosphorylase (MycB nadC)	P9WJJ7	NADC_MYCTU	Pentosyltransferase	nadC; Quinolinic acid phosphoribosyltransferase; Quinolinate phosphoribosyltransferase [decarboxylating]; QAPRTase	MycB nadC	Involved in the catabolism of quinolinic acid (QA).	EC 2.4.2.19	1QPR; 1QPQ; 1QPO; 1QPN	MGLSDWELAAARAAIARGLDEDLRYGPDVTTLATVPASATTTASLVTREAGVVAGLDVALLTLNEVLGTNGYRVLDRVEDGARVPPGEALMTLEAQTRGLLTAERTMLNLVGHLSGIATATAAWVDAVRGTKAKIRDTRKTLPGLRALQKYAVRTGGGVNHRLGLGDAALIKDNHVAAAGSVVDALRAVRNAAPDLPCEVEVDSLEQLDAVLPEKPELILLDNFAVWQTQTAVQRRDSRAPTVMLESSGGLSLQTAATYAETGVDYLAVGALTHSVRVLDIGLDM	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	mtu00760:Nicotinate and nicotinamide metabolism; mtu01100:Metabolic pathways	.	.	P9WJJ7
TTUHP04	Mycobacterium Phosphatidyl-myo-inositol mannosyltransferase (MycB pimA)	P9WMZ5	PIMA_MYCTU	.	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	MycB pimA	"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."	.	.	MRIGMICPYSFDVPGGVQSHVLQLAEVMRTRGHLVSVLAPASPHAALPDYFVSGGRAVPIPYNGSVARLRFGPATHRKVKKWLAHGDFDVLHLHEPNAPSLSMLALNIAEGPIVATFHTSTTKSLTLTVFQGILRPMHEKIVGRIAVSDLARRWQMEALGSDAVEIPNGVDVDSFASAARLDGYPRQGKTVLFLGRYDEPRKGMAVLLDALPKVVQRFPDVQLLIVGHGDADQLRGQAGRLAAHLRFLGQVDDAGKASAMRSADVYCAPNTGGESFGIVLVEAMAAGTAVVASDLDAFRRVLRDGEVGHLVPVDPPDLQAAALADGLIAVLENDVLRERYVAAGNAAVRRYDWSVVASQIMRVYETVAGSGAKVQVAS	Literature-reported	The phosphatidyl-myo-inositol mannosyltransferase PimA is essential for Mycobacterium tuberculosis growth in vitro and in vivo. J Bacteriol. 2014 Oct;196(19):3441-51.	.	.	.	.	.	.	.	.	.	.	.	mtu00571: Lipoarabinomannan (LAM) biosynthesis; mtu01100: Metabolic pathways	.	.	P9WMZ5
TTS6XJE	Mycobacterium Serine/threonine-protein kinase PknB (MycB pknB)	P9WI81	PKNB_MYCTU	.	pknB; Serine/threonineprotein kinase PknB	MycB pknB	"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."	.	6I2P; 6B2P; 5U94; 5E0Z; 5E0Y	MTTPSHLSDRYELGEILGFGGMSEVHLARDLRLHRDVAVKVLRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAETPAGPLPYIVMEYVDGVTLRDIVHTEGPMTPKRAIEVIADACQALNFSHQNGIIHRDVKPANIMISATNAVKVMDFGIARAIADSGNSVTQTAAVIGTAQYLSPEQARGDSVDARSDVYSLGCVLYEVLTGEPPFTGDSPVSVAYQHVREDPIPPSARHEGLSADLDAVVLKALAKNPENRYQTAAEMRADLVRVHNGEPPEAPKVLTDAERTSLLSSAAGNLSGPRTDPLPRQDLDDTDRDRSIGSVGRWVAVVAVLAVLTVVVTIAINTFGGITRDVQVPDVRGQSSADAIATLQNRGFKIRTLQKPDSTIPPDHVIGTDPAANTSVSAGDEITVNVSTGPEQREIPDVSTLTYAEAVKKLTAAGFGRFKQANSPSTPELVGKVIGTNPPANQTSAITNVVIIIVGSGPATKDIPDVAGQTVDVAQKNLNVYGFTKFSQASVDSPRPAGEVTGTNPPAGTTVPVDSVIELQVSKGNQFVMPDLSGMFWVDAEPRLRALGWTGMLDKGADVDAGGSQHNRVVYQNPPAGTGVNRDGIITLRFGQ	Literature-reported	A novel drug discovery concept for tuberculosis: inhibition of bacterial and host cell signalling. Immunol Lett. 2008 Mar 15;116(2):225-31.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	P9WI81
TT7MHK2	Mycobacterium Polyketide synthase (MycB pks2)	P9WQE9	PHAS_MYCTU	.	Polyketide synthase pks2; Phthioceranic/hydroxyphthioceranic acid synthase	MycB pks2	Catalyzes the synthesis of the hepta- and octamethyl phthioceranic acids and/or hydroxyphthioceranic acids that are the major acyl constituents of sulfolipids.	EC 2.3.1.-	.	MGLGSAASGTGADRGAWTLAEPRVTPVAVIGMACRLPGGIDSPELLWKALLRGDDLITEVPPDRWDCDEFYDPQPGVPGRTVCKWGGFLDNPADFDCEFFGIGEREAIAIDPQQRLLLETSWEAMEHAGLTQQTLAGSATGVFAGVTHGDYTMVAADAKQLEEPYGYLGNSFSMASGRVAYAMRLHGPAITVDTACSSGLTAVHMACRSLHEGESDVALAGGVALMLEPRKAAAGSALGMLSPTGRCRAFDVAADGFVSGEGCAVVVLKRLPDALADGDRILAVIRGTSANQDGHTVNIATPSQPAQVAAYRAALAAGGVDAATVGMVEAHGPGTPIGDPIEYASVSEVYGVDGPCALASVKTNFGHTQSTAGVLGLIKVVLALKHGVVPRNLHFTRLPDEIAGITTNLFVPEVTTPWPTNGRQVPRRAAVSSYGFSGTNVHAVVEQAPQTEAQPHAASTPPTGTPALFTLSASSADALRQTAQRLTDWIQQHADSLVLSDLAYTLARRRTHRSVRTAVIASSVDELIAGLGEVADGDTVYQPAVGQDDRGPVWLFSGQGSQWAAMGADLLTNESVFAATVAELEPLIAAESGFSVTEAMTAPETVTGIDRVQPTIFAMQVALAATMAAYGVRPGAVIGHSMGESAAAVVAGVLSAEDGVRVICRRSKLMATIAGSAAMASVELPALAVQSELTALGIDDVVVAVVTAPQSTVIAGGTESVRKLVDIWERRDVLARAVAVDVASHSPQVDPILDELIAALADLNPKAPEIPYYSATLFDPREAPACDARYWADNLRHTVRFSAAVRSALDDGYRVFAELSPHPLLTHAVDQIAGSVGMPVAALAGMRREQPLPLGLRRLLTDLHNAGAAVDFSVLCPQGRLVDAPLPAWSHRFLFYDREGVDNRSPGGSTVAVHPLLGAHVRLPEEPERHAWQADVGTATLPWLGDHRIHNVAALPGAAYCEMALSAARAVLGEQSEVRDMRFEAMLLLDDQTPVSTVATVTSPGVVDFAVEALQEGVGHHLRRASAVLQQVSGECEPPAYDMASLLEAHPCRVDGEDLRRQFDKHGVQYGPAFTGLAVAYVAEDATATMLAEVALPGSIRSQQGLYAIHPALLDACFQSVGAHPDSQSVGSGLLVPLGVRRVRAYAPVRTARYCYTRVTKVELVGVEADIDVLDAHGTVLLAVCGLRIGTGVSERDKHNRVLNERLLTIEWHQRELPEMDPSGAGKWLLISDCAASDVTATRLADAFREHSAACTTMRWPLHDDQLAAADQLRDQVGSDEFSGVVVLTGSNTGTPHQGSADRGAEYVRRLVGIARELSDLPGAVPRMYVVTRGAQRVLADDCVNLEQGGLRGLLRTIGAEHPHLRATQIDVDEQTGVEQLARQLLATSEEDETAWRDNEWYVARLCPTPLRPQERRTIVADHQQSGMRLQIRTPGDMQTIELAAFHRVPPGPGQIEVAVRASSVNFADVLIAFGRYPSFEGHLPQLGTDFAGVVTAVGPGVTDHKVGDHVGGMSPNGCWGTFVTCDARLAATLPPGLGDAQAAAVTTAHATAWYGLHELARIRAGDTVLIHSGTGGVGQAAIAIARAAGAEIFATAGTPQRRELLRNMGIEHVYDSRSIEFAEQIRRDTNGRGVDVVLNSVTGAAQLAGLKLLAFRGRFVEIGKRDIYGDTKLGLFPFRRNLSFYAVDLGLLSATHPEELRDLLGTVYRLTAAGELPMPQSTHYPLVEAATAIRVMGNAEHTGKLVLHIPQTGKSLVTLPPEQAQVFRPDGSYIITGGLGGLGLFLAEKMAAAGCGRIVLNSRTQPTQKMRETIEAIAAMGSEVVVECGDIAQPGTAERLVATAVATGLPVRGVLHAAAVVEDATLANITDELLARDWAPKVHGAWELHEATSGQPLDWFCLFSSAAALTGSPGQSAYSAANSWLDAFAHWRQAQGLPATAIAWGAWSDIGQLGWWSASPARASALEESNYTAITPDEGAYAFEALLRHNRVYTGYAPVIGAPWLVAFAERSRFFEVFSSSNGSGTSKFRVELNELPRDEWPARLRQLVAEQVSLILRRTVDPDRPLPEYGLDSLGALELRTRIETETGIRLAPKNVSATVRGLADHLYEQLAPDDAPAAALSSQ	Literature-reported	A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms. Proc Natl Acad Sci U S A. 2004 Jan 6;101(1):314-9.	.	.	.	.	.	.	.	.	.	.	.	.	.	MetaCyc:G185E-8121-MON	P9WQE9
TT19LDW	Mycobacterium Polyphosphate kinase (MycB ppk)	O33127	PPK1_MYCLE	Kinase	Polyphosphoric acid kinase; PPK; ATP-polyphosphate phosphotransferase	MycB ppk	Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).	.	.	MMSNDLLVTDIEAEARTEENIWHSDNSALAAPPAATTSASQDQLPDDRYLNRESSWLDFNARVLALAADNSLPLLERAKFLAIFASNLDEFYMVRVAGLKRRDEMDLSVRSADGLTPREQLSRIGEQTQWIASRHARVFLDSVLPALGEEGIYIVTWTDLDQAERDQLSTYFNEQVFPVLTPLAVDPAHPFPFVSGLSLNLAVTVKQPEDGTQHFARVKVPNNVDRFVELANRGAVRDTSAGDEGQLIHRFLPMEELIAAFLPVLFPGTEIVEHHAFRITRNADFEVEEDRDEDLLQALERELARRRFGSPVRLEIADDMTESMLELLLRELDVHPSDVIEVPGLLDLSSLWQIYGLDRPALKDRAFIPDTHPAFAERETPKSIFATLREGDVLVHHPYHSFATSVQRFIEQATADPDVLAIKQTLYRTSGDSPIVLALIEAAEAGKQVVALVEIKARFDEQANIRWARALEHAGVHVVYGIVGLKTHCKTCLVVRREGPTIRRYCHIGTGNYNSKTARLYEDVGLLTAAPDIGADLTDLFNSLTGYSRKLAYRNLLVAPYGIRRGIIERVEREVAAHRESGPQTGKGLIRLKMNALVDEQVIDALYRASQAGVRVEVVVRGICALRPGTEGFSENIFVRSILGRFLEHSRIIHFRAIDEFWIGSADMMHRNLDRRVEVLAQVKDSRLTAQLDELLKSALDPFTRCWELRPDGQWTASPQKGQQVRDHQESLMERHRSR	Literature-reported	Establishing Virulence Associated Polyphosphate Kinase 2 as a drug target for Mycobacterium tuberculosis. Sci Rep. 2016 Jun 9;6:26900.	.	.	.	.	.	.	.	.	.	.	.	mle00190: Oxidative phosphorylation; mle03018: RNA degradation	.	.	O33127
TTFZAYL	Mycobacterium Phosphopantetheinyl transferase (MycB pptT)	O33336	O33336_MYCTU	.	Phosphopantetheinyl transferase PptT (CoA:APO-[ACP]pantetheinephosphotransferase) (CoA:APO-[acyl-carrier protein]pantetheinephosphotransferase)	MycB pptT	"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."	.	4U89; 4QVH; 4QJK	MTVGTLVASVLPATVFEDLAYAELYSDPPGLTPLPEEAPLIARSVAKRRNEFITVRHCARIALDQLGVPPAPILKGDKGEPCWPDGMVGSLTHCAGYRGAVVGRRDAVRSVGIDAEPHDVLPNGVLDAISLPAERADMPRTMPAALHWDRILFCAKEATYKAWFPLTKRWLGFEDAHITFETDSTGWTGRFVSRILIDGSTLSGPPLTTLRGRWSVERGLVLTAIVL	Literature-reported	Opposing reactions in coenzyme A metabolism sensitize Mycobacterium tuberculosis to enzyme inhibition. Science. 2019 Feb 1;363(6426). pii: eaau8959.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT19K0L	Mycobacterium Proton pump (MycB Prop)	A0A1Q4HQH4	A0A1Q4HQH4_9MYCO	.	Nicotinamide nucleotide transhydrogenase subunit beta; NAD(P) transhydrogenase subunit beta	MycB Prop	The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.	.	.	MNYLVTVLYIISFALFIYGLMGLTGPKTAVRGNLIAAVGMAIAVAATLIKIRHTESWVLIIAGLVVGVALGVPPARYTKMTAMPQLVAFFNGVGGGTVALIALSEFIETKGFSAFQHGESPTVHIVVASLFAAIIGSISFWGSIIAFGKLQEIISGSPIGFGKAQQPINLLLLAAAVAAAVVIGLGAHPGTGGVALWWMIGLLAAAGVLGLMVVLPIGGADMPVVISLLNAMTGLSAAAAGLALNNTAMIVAGMIVGASGSILTNLMAKAMNRSIPAIVAGGFGGGGVAPSGGGGGDKHVKATSAADAAIQMAYANQVIVVPGYGLAVAQAQHAVKDMASLLEDKGVPVKYAIHPVAGRMPGHMNVLLAEAEVDYDAMKDMDDINDEFARTDVAIVIGANDVTNPAARNEQSSPIYGMPILNVDRAKSVIVLKRSMNSGFAGIDNPLFYADGTTMLFGDAKKSVTEVAEELKAL	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. 2015	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTI0TCK	Mycobacterium CDP-diacylglycerol-inositol phosphatidyltransferase (MycB pssA)	P9WPG1	PSS_MYCTU	Kinase	pssA; PtdIns synthase; Phosphatidylinositol synthase; PI synthase	MycB pssA	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.	EC 2.7.8.8	.	MIGKPRGRRGVNLQILPSAMTVLSICAGLTAIKFALEHQPKAAMALIAAAAILDGLDGRVARILDAQSRMGAEIDSLADAVNFGVTPALVLYVSMLSKWPVGWVVVLLYAVCVVLRLARYNALQDDGTQPAYAHEFFVGMPAPAGAVSMIGLLALKMQFGEGWWTSGWFLSFWVTGTSILLVSGIPMKKMHAVSVPPNYAAALLAVLAICAAAAVLAPYLLIWVIIIAYMCHIPFAVRSQRWLAQHPEVWDDKPKQRRAVRRASRRAHPYRPSMARLGLRKPGRRL	Clinical trial	Phosphatidylinositol synthesis in mycobacteria. Biochim Biophys Acta. 1999 Jan 4;1436(3):437-50.	31	.	.	.	.	.	.	.	.	.	.	"mtu00260: Glycine, serine and threonine metabolism; mtu00564: Glycerophospholipid metabolism; mtu01100: Metabolic pathways; mtu01110: Biosynthesis of secondary metabolites"	.	.	P9WPG1
TTV7Y40	Mycobacterium Orotidine phosphate decarboxylase (MycB pyrF)	P9WIU2	PYRF_MYCTO	Carbon-carbon lyase	Orotidine 5'-phosphate decarboxylase; OMPdecase; OMPDCase; OMP decarboxylase	MycB pyrF	"Catalyzes the decarboxylation of orotidine monophosphate (OMP), producing uridine monophosphate (UMP)."	EC 4.1.1.23	.	MTGFGLRLAEAKARRGPLCLGIDPHPELLRGWDLATTADGLAAFCDICVRAFADFAVVKPQVAFFESYGAAGFAVLERTIAELRAADVLVLADAKRGDIGATMSAYATAWVGDSPLAADAVTASPYLGFGSLRPLLEVAAAHGRGVFVLAATSNPEGAAVQNAAADGRSVAQLVVDQVGAANEAAGPGPGSIGVVVGATAPQAPDLSAFTGPVLVPGVGVQGGRPEALGGLGGAASSQLLPAVAREVLRAGPGVPELRAAGERMRDAVAYLAAV	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	mtc00240: Pyrimidine metabolism; mtc01100: Metabolic pathways; mtc01240: Biosynthesis of cofactors	.	.	P9WIU2
TTKGY3F	Mycobacterium DTDP-dehydrorhamnose epimerase rmlC (MycB rmlC)	P9WH11	RMLC_MYCTU	Racemases and epimerases	"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"	MycB rmlC	"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."	EC 5.1.3.13	2IXC; 1UPI; 1PM7	MKARELDVPGAWEITPTIHVDSRGLFFEWLTDHGFRAFAGHSLDVRQVNCSVSSAGVLRGLHFAQLPPSQAKYVTCVSGSVFDVVVDIREGSPTFGRWDSVLLDDQDRRTIYVSEGLAHGFLALQDNSTVMYLCSAEYNPQREHTICATDPTLAVDWPLVDGAAPSLSDRDAAAPSFEDVRASGLLPRWEQTQRFIGEMRGT	Literature-reported	How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6.	0	.	.	.	.	.	.	.	.	.	.	mtu00521: Streptomycin biosynthesis; mtu00523: Polyketide sugar unit biosynthesis; mtu00541: O-Antigen nucleotide sugar biosynthesis; mtu01100: Metabolic pathways; mtu01110: Biosynthesis of secondary metabolites; mtu01250: Biosynthesis of nucleotide sugars	.	.	P9WH11
TT79JGK	Mycobacterium RNA polymerase (MycB RNAP)	P9WGZ1; P9WGY9; P9WGY7; P9WGY5	RPOA_MYCTU; RPOB_MYCTU; RPOC_MYCTU; RPOZ_MYCTU	.	Transcriptase; RNAP; RNA polymerase; Mycobacterium DNA-directed RNA polymerase	MycB rpoA	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	.	.	MLISQRPTLSEDVLTDNRSQFVIEPLEPGFGYTLGNSLRRTLLSSIPGAAVTSIRIDGVLHEFTTVPGVKEDVTEIILNLKSLVVSSEEDEPVTMYLRKQGPGEVTAGDIVPPAGVTVHNPGMHIATLNDKGKLEVELVVERGRGYVPAVQNRASGAEIGRIPVDSIYSPVLKVTYKVDATRVEQRTDFDKLILDVETKNSISPRDALASAGKTLVELFGLARELNVEAEGIEIGPSPAEADHIASFALPIDDLDLTVRSYNCLKREGVHTVGELVARTESDLLDIRNFGQKSIDEVKIKLHQLGLSLKDSPPSFDPSEVAGYDVATGTWSTEGAYDEQDYAETEQL	Successful	Rifamycin action on RNA polymerase in antibiotic-tolerant Mycobacterium tuberculosis results in differentially detectable populations.Proc Natl Acad Sci U S A. 2017 Jun 13;114(24):E4832-E4840. 	34	.	.	.	.	.	.	.	.	.	.	mtu00230:Purine metabolism; mtu00240:Pyrimidine metabolism; mtu01100:Metabolic pathways; mtu03020:RNA polymerase	R-HSA-9639775: Antimicrobial action and antimicrobial resistance in Mtb	.	P9WGZ1
TTNOTDM	Mycobacterium DNA-dependent RNA polymerase beta (MycB rpoB)	Q7X2I2	Q7X2I2_MYCTX	.	DNA-dependent RNA polymerase beta subunit	MycB rpoB	Transcribes the message carried by DNA. Has important implications in transcriptional regulation.	.	.	TVPGGVEVPVETDDIDHFGNRRLRTVGELIQNQIRVGMSRMERVVRERMTTQDVEAITPQTLINIRPVVAAIKEFFGTSQLSQFMDQNNPLSGLTHKRRLWALGPGGLSRERAGLEVRDVHPS	Literature-reported	The distribution of fitness effects of beneficial mutations in Pseudomonas aeruginosa. PLoS Genet. 2009 Mar;5(3):e1000406.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYVRWD	Mycobacterium Sensor-like histidine kinase senX3 (MycB senX3)	Q11155	SENX3_MYCTU	.	SenX3; Rv0490; MTCY20G9.16	MycB senX3	Probably forms part of a two-component regulatory system senx3/regx3. Phosphorylates regx3.	EC 2.7.13.3	.	MTVFSALLLAGVLSALALAVGGAVGMRLTSRVVEQRQRVATEWSGITVSQMLQCIVTLMPLGAAVVDTHRDVVYLNERAKELGLVRDRQLDDQAWRAARQALGGEDVEFDLSPRKRSATGRSGLSVHGHARLLSEEDRRFAVVFVHDQSDYARMEAARRDFVANVSHELKTPVGAMALLAEALLASADDSETVRRFAEKVLIEANRLGDMVAELIELSRLQGAERLPNMTDVDVDTIVSEAISRHKVAADNADIEVRTDAPSNLRVLGDQTLLVTALANLVSNAIAYSPRGSLVSISRRRRGANIEIAVTDRGIGIAPEDQERVFERFFRGDKARSRATGGSGLGLAIVKHVAANHDGTIRVWSKPGTGSTFTLALPALIEAYHDDERPEQAREPELRSNRSQREEELSR	Literature-reported	A two-component signal transduction system with a PAS domain-containing sensor is required for virulence of Mycobacterium tuberculosis in mice. Biochem Biophys Res Commun. 2004 Jan 30;314(1):259-67.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P9WGK5
TT0Z3HD	Mycobacterium Sphingomyelinase (MycB spmT)	P9WKQ1	SMASE_MYCTU	SpmT family	SMase	MycB spmT	"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."	EC 3.1.4.12	.	MDYAKRIGQVGALAVVLGVGAAVTTHAIGSAAPTDPSSSSTDSPVDACSPLGGSASSLAAIPGASVPQVGVRQVDPGSIPDDLLNALIDFLAAVRNGLVPIIENRTPVANPQQVSVPEGGTVGPVRFDACDPDGNRMTFAVRERGAPGGPQHGIVTVDQRTASFIYTADPGFVGTDTFSVNVSDDTSLHVHGLAGYLGPFHGHDDVATVTVFVGNTPTDTISGDFSMLTYNIAGLPFPLSSAILPRFFYTKEIGKRLNAYYVANVQEDFAYHQFLIKKSKMPSQTPPEPPTLLWPIGVPFSDGLNTLSEFKVQRLDRQTWYECTSDNCLTLKGFTYSQMRLPGGDTVDVYNLHTNTGGGPTTNANLAQVANYIQQNSAGRAVIVTGDFNARYSDDQSALLQFAQVNGLTDAWVQVEHGPTTPPFAPTCMVGNECELLDKIFYRSGQGVTLQAVSYGNEAPKFFNSKGEPLSDHSPAVVGFHYVADNVAVR	Literature-reported	Secretory sphingomyelinase in health and disease. Biol Chem. 2015 Jun;396(6-7):707-36.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	P9WKQ1
TT5B8AX	Mycobacterium Thymidine monophosphate kinase (MycB tmk)	P9WKE1	KTHY_MYCTU	Kinase	tmk; Thymidylic kinase; Thymidylic acid kinase; Thymidylate monophosphate kinase; Thymidylate kinase; Thymidine 5'-monophosphate kinase; TMPK; Deoxythymidine 5'-monophosphate kinase; DTMPkinase	MycB tmk	"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."	EC 2.7.4.9	5NRQ; 5NRN; 5NR7; 5NQ5; 4UNS	MLIAIEGVDGAGKRTLVEKLSGAFRAAGRSVATLAFPRYGQSVAADIAAEALHGEHGDLASSVYAMATLFALDRAGAVHTIQGLCRGYDVVILDRYVASNAAYSAARLHENAAGKAAAWVQRIEFARLGLPKPDWQVLLAVSAELAGERSRGRAQRDPGRARDNYERDAELQQRTGAVYAELAAQGWGGRWLVVGADVDPGRLAATLAPPDVPS	Literature-reported	Thymidylate kinase as target enzyme for 5'-deoxythymidine and various 5'-deoxy-5'-halogeno pyrimidine nucleosides. Acta Biol Med Ger. 1969;23(6):Suppl:K 19+.	0	.	.	.	.	.	.	.	.	.	.	mtu00240:Pyrimidine metabolism; mtu01100:Metabolic pathways	.	MetaCyc:G185E-7521-MON	P9WKE1
TTVW4XU	MYCBP messenger RNA (MYCBP mRNA)	Q99417	MYCBP_HUMAN	mRNA target	c-Myc-binding protein (mRNA); Associate of Myc 1 (mRNA); AMY1 (mRNA); AMY-1 (mRNA)	MYCBP	Stimulates the activation of E box-dependent transcription by MYC. May control the transcriptional activity of MYC.	.	2YY0	MAHYKAADSKREQFRRYLEKSGVLDTLTKVLVALYEEPEKPNSALDFLKHHLGAATPENPEIELLRLELAEMKEKYEAIVEENKKLKAKLAQYEPPQEEKRAE	Clinical trial	National Cancer Institute Drug Dictionary (drug id 759983).	19	mRNA	mRNA target	.	.	.	.	.	.	.	.	.	.	.	Q99417
TT9JBY5	N-myc proto-oncogene protein (MYCN)	P04198	MYCN_HUMAN	.	bHLHe37; NMYC; N-myc; Class E basic helix-loop-helix protein 37	MYCN	Positively regulates the transcription of MYCNOS in neuroblastoma cells.	.	5G1X	MPSCSTSTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWGSPAEEDAFGLGGLGGLTPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAGRAGAALPAELAHPAAECVDPAVVFPFPVNKREPAPVPAAPASAPAAGPAVASGAGIAAPAGAPGVAPPRPGGRQTSGGDHKALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQHNYAAPSPYVESEDAPPQKKIKSEASPRPLKSVIPPKAKSLSPRNSDSEDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQLLLEKEKLQARQQQLLKKIEHARTC	Literature-reported	Where pathology meets molecular biology: N-myc amplification in human neuroblastoma as a paradigm for the clinical use of an oncogene alteration. Verh Dtsch Ges Pathol. 1994;78:26-33.	.	.	.	.	.	.	Helix-loop-helix DNA-binding domain; Myc amino-terminal region	PF00010; PF01056	PF00010; HLH; PF01056; Myc_N	.	.	hsa05202: Transcriptional misregulation in cancer	R-HSA-201556: Signaling by ALK	.	P04198
TTB6Q2O	Myeloid differentiation primary response protein MyD88 (MYD88)	Q99836	MYD88_HUMAN	.	MyD88	MYD88	"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."	.	4EO7; 4DOM; 3MOP; 2Z5V; 2JS7	MAAGGPGAGSAAPVSSTSSLPLAALNMRVRRRLSLFLNVRTQVAADWTALAEEMDFEYLEIRQLETQADPTGRLLDAWQGRPGASVGRLLELLTKLGRDDVLLELGPSIEEDCQKYILKQQQEEAEKPLQVAAVDSSVPRTAELAGITTLDDPLGHMPERFDAFICYCPSDIQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSIASELIEKRCRRMVVVVSDDYLQSKECDFQTKFALSLSPGAHQKRLIPIKYKAMKKEFPSILRFITVCDYTNPCTKSWFWTRLAKALSLP	Literature-reported	Myeloid-MyD88 Contributes to Ethanol-Induced Liver Injury in Mice Linking Hepatocellular Death to Inflammation. Alcohol Clin Exp Res. 2017 Apr;41(4):719-726.	.	.	.	.	.	.	Death domain; TIR domain	PF00531; PF01582	PF00531; Death; PF01582; TIR	.	.	hsa04010: MAPK signaling pathway; hsa04064: NF-kappa B signaling pathway; hsa04620: Toll-like receptor signaling pathway; hsa04621: NOD-like receptor signaling pathway; hsa04936: Alcoholic liver disease; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05133: Pertussis; hsa05134: Legionellosis; hsa05135: Yersinia infection; hsa05140: Leishmaniasis; hsa05142: Chagas disease; hsa05143: African trypanosomiasis; hsa05144: Malaria; hsa05145: Toxoplasmosis; hsa05152: Tuberculosis; hsa05161: Hepatitis B; hsa05162: Measles; hsa05164: Influenza A; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05171: Coronavirus disease - COVID-19; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer; hsa05417: Lipid and atherosclerosis	"R-HSA-1236974: ER-Phagosome pathway; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-166058: MyD88:MAL(TIRAP) cascade initiated on plasma membrane; R-HSA-1810476: RIP-mediated NFkB activation via ZBP1; R-HSA-209543: p75NTR recruits signalling complexes; R-HSA-3134963: DEx/H-box helicases activate type I IFN and inflammatory cytokines production; 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-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-9020702: Interleukin-1 signaling; 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"	.	Q99836
TTBIL13	Myosin-2 (MYH2)	Q9UKX2	MYH2_HUMAN	Myosin-kinesin ATPase	"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"	MYH2	Required for cytoskeleton organization. Muscle contraction.	.	.	MSSDSELAVFGEAAPFLRKSERERIEAQNRPFDAKTSVFVAEPKESFVKGTIQSREGGKVTVKTEGGATLTVKDDQVFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQLITRTQARCRGFLARVEYQRMVERREAIFCIQYNIRSFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE	Literature-reported	Myosin 2 is a key Rho kinase target necessary for the local concentration of E-cadherin at cell-cell contacts. Mol Biol Cell. 2005 Oct;16(10):4531-42.	.	Myosin-kinesin ATPase	.	TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.	.	.	Myosin head (motor domain); Myosin N-terminal SH3-like domain; Myosin tail	PF00063; PF02736; PF01576	PF00063; Myosin_head; PF02736; Myosin_N; PF01576; Myosin_tail_1	.	.	.	R-HSA-2029482: Regulation of actin dynamics for phagocytic cup formation; R-HSA-9664422: FCGR3A-mediated phagocytosis	.	Q9UKX2
TTNIMDP	Myosin-7 (MYH7)	P12883	MYH7_HUMAN	TRAFAC class myosin-kinesin ATPase	"Myosin heavy chain, cardiac muscle beta isoform; Myosin heavy chain slow isoform; Myosin heavy chain 7; MyHCslow; MyHCbeta; MYH7"	MYH7	Muscle contraction.	.	5WME; 5WLZ; 5WLQ; 5WJB; 5WJ7	MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSANFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLARMEYKKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNEE	Clinical trial	EIAV-based retinal gene therapy in the shaker1 mouse model for usher syndrome type 1B: development of UshStat. PLoS One. 2014 Apr 4;9(4):e94272.	19	.	.	.	.	.	.	.	.	.	.	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	R-HSA-1445148:Translocation of GLUT4 to the plasma membrane	.	P12883
TT18ETS	Myosin light kinase (MYLK)	Q15746	MYLK_HUMAN	Kinase	"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"	MYLK	"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)."	EC 2.7.11.18	6C6M; 5JTH; 5JQA; 2YR3; 2K0F	MGDVKLVASSHISKTSLSVDPSRVDSMPLTEAPAFILPPRNLCIKEGATAKFEGRVRGYPEPQVTWHRNGQPITSGGRFLLDCGIRGTFSLVIHAVHEEDRGKYTCEATNGSGARQVTVELTVEGSFAKQLGQPVVSKTLGDRFSAPAVETRPSIWGECPPKFATKLGRVVVKEGQMGRFSCKITGRPQPQVTWLKGNVPLQPSARVSVSEKNGMQVLEIHGVNQDDVGVYTCLVVNGSGKASMSAELSIQGLDSANRSFVRETKATNSDVRKEVTNVISKESKLDSLEAAAKSKNCSSPQRGGSPPWAANSQPQPPRESKLESCKDSPRTAPQTPVLQKTSSSITLQAARVQPEPRAPGLGVLSPSGEERKRPAPPRPATFPTRQPGLGSQDVVSKAANRRIPMEGQRDSAFPKFESKPQSQEVKENQTVKFRCEVSGIPKPEVAWFLEGTPVRRQEGSIEVYEDAGSHYLCLLKARTRDSGTYSCTASNAQGQLSCSWTLQVERLAVMEVAPSFSSVLKDCAVIEGQDFVLQCSVRGTPVPRITWLLNGQPIQYARSTCEAGVAELHIQDALPEDHGTYTCLAENALGQVSCSAWVTVHEKKSSRKSEYLLPVAPSKPTAPIFLQGLSDLKVMDGSQVTMTVQVSGNPPPEVIWLHNGNEIQESEDFHFEQRGTQHSLCIQEVFPEDTGTYTCEAWNSAGEVRTQAVLTVQEPHDGTQPWFISKPRSVTASLGQSVLISCAIAGDPFPTVHWLRDGKALCKDTGHFEVLQNEDVFTLVLKKVQPWHAGQYEILLKNRVGECSCQVSLMLQNSSARALPRGREPASCEDLCGGGVGADGGGSDRYGSLRPGWPARGQGWLEEEDGEDVRGVLKRRVETRQHTEEAIRQQEVEQLDFRDLLGKKVSTKTLSEDDLKEIPAEQMDFRANLQRQVKPKTVSEEERKVHSPQQVDFRSVLAKKGTSKTPVPEKVPPPKPATPDFRSVLGGKKKLPAENGSSSAETLNAKAVESSKPLSNAQPSGPLKPVGNAKPAETLKPMGNAKPAETLKPMGNAKPDENLKSASKEELKKDVKNDVNCKRGHAGTTDNEKRSESQGTAPAFKQKLQDVHVAEGKKLLLQCQVSSDPPATIIWTLNGKTLKTTKFIILSQEGSLCSVSIEKALPEDRGLYKCVAKNDAGQAECSCQVTVDDAPASENTKAPEMKSRRPKSSLPPVLGTESDATVKKKPAPKTPPKAAMPPQIIQFPEDQKVRAGESVELFGKVTGTQPITCTWMKFRKQIQESEHMKVENSENGSKLTILAARQEHCGCYTLLVENKLGSRQAQVNLTVVDKPDPPAGTPCASDIRSSSLTLSWYGSSYDGGSAVQSYSIEIWDSANKTWKELATCRSTSFNVQDLLPDHEYKFRVRAINVYGTSEPSQESELTTVGEKPEEPKDEVEVSDDDEKEPEVDYRTVTINTEQKVSDFYDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWLMKDTKNMEAKKLSKDRMKKYMARRKWQKTGNAVRAIGRLSSMAMISGLSGRKSSTGSPTSPLNAEKLESEEDVSQAFLEAVAEEKPHVKPYFSKTIRDLEVVEGSAARFDCKIEGYPDPEVVWFKDDQSIRESRHFQIDYDEDGNCSLIISDVCGDDDAKYTCKAVNSLGEATCTAELIVETMEEGEGEGEEEEE	Clinical trial	"ME-3407, a new antiulcer agent, inhibits acid secretion by interfering with redistribution of H(+)-K(+)-ATPase. Am J Physiol. 1997 May;272(5 Pt 1):G1122-34."	21	EC:2.7	Kinase	protein kinase superfamily. CAMK Ser/Thr protein kinase family.	2.7.11.18	Transferring phosphorus-containing groups	Fibronectin type III domain; Immunoglobulin I-set domain; Protein kinase domain	PF00041; PF07679; PF00069	PF00041; fn3; PF07679; I-set; PF00069; Pkinase	.	.	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	R-HSA-445355:Smooth Muscle Contraction	.	Q15746
TTHLGB2	Myosin light chain kinase 2 (MYLK2)	Q9H1R3	MYLK2_HUMAN	.	MYLK2	MYLK2	Implicated in the level of global muscle contraction and cardiac function. Phosphorylates a specific serine in the N-terminus of a myosin light chain.	EC 2.7.11.18	3KF9; 2LV6	MATENGAVELGIQNPSTDKAPKGPTGERPLAAGKDPGPPDPKKAPDPPTLKKDAKAPASEKGDGTLAQPSTSSQGPKGEGDRGGGPAEGSAGPPAALPQQTATPETSVKKPKAEQGASGSQDPGKPRVGKKAAEGQAAARRGSPAFLHSPSCPAIISSSEKLLAKKPPSEASELTFEGVPMTHSPTDPRPAKAEEGKNILAESQKEVGEKTPGQAGQAKMQGDTSRGIEFQAVPSEKSEVGQALCLTAREEDCFQILDDCPPPPAPFPHRMVELRTGNVSSEFSMNSKEALGGGKFGAVCTCMEKATGLKLAAKVIKKQTPKDKEMVLLEIEVMNQLNHRNLIQLYAAIETPHEIVLFMEYIEGGELFERIVDEDYHLTEVDTMVFVRQICDGILFMHKMRVLHLDLKPENILCVNTTGHLVKIIDFGLARRYNPNEKLKVNFGTPEFLSPEVVNYDQISDKTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLSGNWYFDEETFEAVSDEAKDFVSNLIVKDQRARMNAAQCLAHPWLNNLAEKAKRCNRRLKSQILLKKYLMKRRWKKNFIAVSAANRFKKISSSGALMALGV	Literature-reported	"Discovery of 7-methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3-dihydro-1H-indol-5-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine (GSK2606414), a potent and selective first-in-class inhibitor of protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK). J Med Chem. 2012 Aug 23;55(16):7193-207."	0	.	.	.	.	.	.	.	.	.	.	hsa04020: Calcium signaling pathway; hsa04022: cGMP-PKG signaling pathway; hsa04270: Vascular smooth muscle contraction; hsa04371: Apelin signaling pathway; hsa04510: Focal adhesion; hsa04611: Platelet activation; hsa04810: Regulation of actin cytoskeleton; hsa04921: Oxytocin signaling pathway; hsa04971: Gastric acid secretion	.	.	Q9H1R3
TTENSOI	Nucleoprotein (N)	P0DTC9	NCAP_SARS2	.	N; Nucleocapsid protein; NC; Protein N	N	"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 (PubMed:33264373). Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. {ECO:0000269|PubMed:32974389, ECO:0000269|PubMed:33264373}.; May block host chemokine function in vivo, facilitating viral replication and transmission (PubMed:35921414). Acts by being secreted into the extracellular space where it competes to host chemokines for binding to host glycosaminoglycans (GAG) (PubMed:35921414). {ECO:0000269|PubMed:35921414}.; May induce inflammasome responses in cultured cells and mice. Acts by interacting with host NLRP3 to facilitate inflammasome assembly, which induces cytokine release that may play a role in COVID lung injury. {ECO:0000269|PubMed:34341353}."	.	6M3M;6VYO;6WJI;6WKP;6WZO;6WZQ;6YI3;6YUN;6ZCO;7ACS;7ACT;7C22;7CDZ;7CE0;7CR5;7DE1;7F2B;7F2E;7KGO;7KGP;7KGQ;7KGR;7KGS;7KGT;7LGD;7LTU;7LUX;7LUZ;7LV2;7N0I;7N0R;7N3C;7N3D;7O05;7O35;7O36;7PKU;7QIK;7QIP;7R98;7SD4;7STR;7STS;7SUE;7SUO;7UW3;7UXX;7UXZ;7VBD;7VBE;7VBF;7VNU;7WKJ;7WZO;7XWX;7XWZ;7XX1;7XXK;7ZIT;8DNT;8FD5;8FG2	MSDNGPQNQRNAPRITFGGPSDSTGSNQNGERSGARSKQRRPQGLPNNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANKDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRNSSRNSTPGSSRGTSPARMAGNGGDAALALLLLDRLNQLESKMSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFPPTEPKKDKKKKADETQALPQRQKKQQTVTLLPAADLDDFSKQLQQSMSSADSTQA	Clinical trial	"Clinical pipeline report, company report or official report of Pfizer"	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-1257604;R-HSA-168638;R-HSA-168928;R-HSA-389357;R-HSA-445989;R-HSA-5218920;R-HSA-9020702;R-HSA-909733;R-HSA-9694322;R-HSA-9694614;R-HSA-9694631;R-HSA-9694635;R-HSA-9694786;R-HSA-9705671;R-HSA-9733458;R-HSA-9755779;	.	.
TTMN4HY	N-acylethanolamine-hydrolyzing acidamidase (NAAA)	Q02083	NAAA_HUMAN	Carbon-nitrogen hydrolase	Nacylsphingosine amidohydrolaselike; Nacylethanolaminehydrolyzing acid amidase subunit beta; NAAA; Acid ceramidaselike protein; ASAHlike protein	NAAA	"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."	EC 3.5.1.-	6DXX; 6DXW	MRTADREARPGLPSLLLLLLAGAGLSAASPPAAPRFNVSLDSVPELRWLPVLRHYDLDLVRAAMAQVIGDRVPKWVHVLIGKVVLELERFLPQPFTGEIRGMCDFMNLSLADCLLVNLAYESSVFCTSIVAQDSRGHIYHGRNLDYPFGNVLRKLTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPHKFTVSGDERDKGWWWENAIAALFRRHIPVSWLIRATLSESENFEAAVGKLAKTPLIADVYYIVGGTSPREGVVITRNRDGPADIWPLDPLNGAWFRVETNYDHWKPAPKEDDRRTSAIKALNATGQANLSLEALFQILSVVPVYNNFTIYTTVMSAGSPDKYMTRIRNPSRK	Literature-reported	Selective N-acylethanolamine-hydrolyzing acid amidase inhibition reveals a key role for endogenous palmitoylethanolamide in inflammation. Proc Natl Acad Sci U S A. 2009 Dec 8;106(49):20966-71.	0	.	.	.	.	.	.	.	.	.	.	.	R-HSA-112310: Neurotransmitter release cycle	MetaCyc:ENSG00000138744-MON	Q02083
TTUWQLT	Glutamate carboxypeptidase III (NAALAD2)	Q9Y3Q0	NALD2_HUMAN	Peptidase	NAALADase II; NAALAD2	NAALAD2	Has N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Also exhibits a dipeptidyl-peptidase IV type activity. Inactivate the peptide neurotransmitter N- acetylaspartylglutamate.	EC 3.4.17.21	3FF3; 3FEE; 3FED; 3FEC	MAESRGRLYLWMCLAAALASFLMGFMVGWFIKPLKETTTSVRYHQSIRWKLVSEMKAENIKSFLRSFTKLPHLAGTEQNFLLAKKIQTQWKKFGLDSAKLVHYDVLLSYPNETNANYISIVDEHETEIFKTSYLEPPPDGYENVTNIVPPYNAFSAQGMPEGDLVYVNYARTEDFFKLEREMGINCTGKIVIARYGKIFRGNKVKNAMLAGAIGIILYSDPADYFAPEVQPYPKGWNLPGTAAQRGNVLNLNGAGDPLTPGYPAKEYTFRLDVEEGVGIPRIPVHPIGYNDAEILLRYLGGIAPPDKSWKGALNVSYSIGPGFTGSDSFRKVRMHVYNINKITRIYNVVGTIRGSVEPDRYVILGGHRDSWVFGAIDPTSGVAVLQEIARSFGKLMSKGWRPRRTIIFASWDAEEFGLLGSTEWAEENVKILQERSIAYINSDSSIEGNYTLRVDCTPLLYQLVYKLTKEIPSPDDGFESKSLYESWLEKDPSPENKNLPRINKLGSGSDFEAYFQRLGIASGRARYTKNKKTDKYSSYPVYHTIYETFELVEKFYDPTFKKQLSVAQLRGALVYELVDSKIIPFNIQDYAEALKNYAASIYNLSKKHDQQLTDHGVSFDSLFSAVKNFSEAASDFHKRLIQVDLNNPIAVRMMNDQLMLLERAFIDPLGLPGKLFYRHIIFAPSSHNKYAGESFPGIYDAIFDIENKANSRLAWKEVKKHISIAAFTIQAAAGTLKEVL	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-8963693: Aspartate and asparagine metabolism	.	Q9Y3Q0
TT4AQ5F	Nucleus accumbens-associated protein 1 (NACC1)	Q96RE7	NACC1_HUMAN	.	NAC1; NAC-1; BTBD14B; BTB/POZ domain-containing protein 14B	NACC1	"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."	.	4U2N; 3GA1	MAQTLQMEIPNFGNSILECLNEQRLQGLYCDVSVVVKGHAFKAHRAVLAASSSYFRDLFNNSRSAVVELPAAVQPQSFQQILSFCYTGRLSMNVGDQFLLMYTAGFLQIQEIMEKGTEFFLKVSSPSCDSQGLHAEEAPSSEPQSPVAQTSGWPACSTPLPLVSRVKTEQQESDSVQCMPVAKRLWDSGQKEAGGGGNGSRKMAKFSTPDLAANRPHQPPPPQQAPVVAAAQPAVAAGAGQPAGGVAAAGGVVSGPSTSERTSPGTSSAYTSDSPGSYHNEEDEEEDGGEEGMDEQYRQICNMYTMYSMMNVGQTAEKVEALPEQVAPESRNRIRVRQDLASLPAELINQIGNRCHPKLYDEGDPSEKLELVTGTNVYITRAQLMNCHVSAGTRHKVLLRRLLASFFDRNTLANSCGTGIRSSTNDPRRKPLDSRVLHAVKYYCQNFAPNFKESEMNAIAADMCTNARRVVRKSWMPKVKVLKAEDDAYTTFISETGKIEPDMMGVEHGFETASHEGEAGPSAEALQ	Literature-reported	Nucleus accumbens-associated protein-1 promotes glycolysis and survival of hypoxic tumor cells via the HDAC4-HIF-1 axis. Oncogene. 2017 Jul 20;36(29):4171-4181.	.	.	.	.	.	.	BEN domain; BTB/POZ domain	PF10523; PF00651	PF10523; BEN; PF00651; BTB	.	.	.	.	.	Q96RE7
TTVKOPM	NEDD8-activating enzyme (NAE)	Q13564; Q8TBC4	ULA1_HUMAN; UBA3_HUMAN	.	NEDD8-activating enzyme E1	NAE1	"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."	.	.	MAQLGKLLKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAEAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEHPVIESHPDNALEDLRLDKPFPELREHFQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQGILKNENGAPEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPSFWILARALKEFVAKEGQGNLPVRGTIPDMIADSGKYIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEKELKLLCSNSAFLRVVRCRSLAEEYGLDTINKDEIISSMDNPDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLKSCLTGFLQEYGLSVMVKDDYVHEFCRYGAAEPHTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATFQL	Clinical trial	Targeting Cullin-RING ligases by MLN4924 induces autophagy via modulating the HIF1-REDD1-TSC1-mTORC1-DEPTOR axis.Cell Death Dis.2012 Sep 6;3:e386.	25	.	.	.	.	.	.	.	.	.	.	hsa05010: Alzheimer disease	R-HSA-8951664: Neddylation	MetaCyc:ENSG00000159593-MON	Q13564
TTDM6HZ	Alpha-N-acetylglucosaminidase (NAGLU)	P54802	ANAG_HUMAN	Glycosylase	UFHSD1; NAGLU; NAG; N-acetyl-alpha-glucosaminidase; Alpha-N-acetylglucosaminidase82 kDa form; Alpha-N-acetylglucosaminidase77 kDa form	NAGLU	Involved in the degradation of heparan sulfate.	EC 3.2.1.50	4XWH	MEAVAVAAAVGVLLLAGAGGAAGDEAREAAAVRALVARLLGPGPAADFSVSVERALAAKPGLDTYSLGGGGAARVRVRGSTGVAAAAGLHRYLRDFCGCHVAWSGSQLRLPRPLPAVPGELTEATPNRYRYYQNVCTQSYSFVWWDWARWEREIDWMALNGINLALAWSGQEAIWQRVYLALGLTQAEINEFFTGPAFLAWGRMGNLHTWDGPLPPSWHIKQLYLQHRVLDQMRSFGMTPVLPAFAGHVPEAVTRVFPQVNVTKMGSWGHFNCSYSCSFLLAPEDPIFPIIGSLFLRELIKEFGTDHIYGADTFNEMQPPSSEPSYLAAATTAVYEAMTAVDTEAVWLLQGWLFQHQPQFWGPAQIRAVLGAVPRGRLLVLDLFAESQPVYTRTASFQGQPFIWCMLHNFGGNHGLFGALEAVNGGPEAARLFPNSTMVGTGMAPEGISQNEVVYSLMAELGWRKDPVPDLAAWVTSFAARRYGVSHPDAGAAWRLLLRSVYNCSGEACRGHNRSPLVRRPSLQMNTSIWYNRSDVFEAWRLLLTSAPSLATSPAFRYDLLDLTRQAVQELVSLYYEEARSAYLSKELASLLRAGGVLAYELLPALDEVLASDSRFLLGSWLEQARAAAVSEAEADFYEQNSRYQLTLWGPEGNILDYANKQLAGLVANYYTPRWRLFLEALVDSVAQGIPFQQHQFDKNVFQLEQAFVLSKQRYPSQPRGDTVDLAKKIFLKYYPRWVAGSW	Successful	Development of bFGF-Chitosan Matrices and Their Interactions with Human Dermal Fibroblast Cells. J Biomater Sci Polym Ed. 2009;20(10):1335-51.	34	.	.	.	.	.	.	.	.	.	.	hsa00531:Glycosaminoglycan degradation; hsa01100:Metabolic pathways; hsa04142:Lysosome	R-HSA-2024096:HS-GAG degradation	.	P54802
TTD1WIG	Nicotinamide phosphoribosyltransferase (NAMPT)	P43490	NAMPT_HUMAN	Glycosyltransferases	Visfatin; PreBcell colonyenhancing factor 1; PreB cellenhancing factor; Pre-B-cell colony-enhancing factor 1; Pre-B cell-enhancing factor; PBEF1; PBEF; Nampt; NAmPRTase	NAMPT	"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."	EC 2.4.2.12	6B76; 6B75; 6AZJ; 6ATB; 6.00E+68	MNPAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKLRKVKYEETVFYGLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKGWNYILEKYDGHLPIEIKAVPEGFVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETSGNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGLALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIVSRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINTLQEIVEGMKQKMWSIENIAFGSGGGLLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVADPNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGQDLLHTVFKNGKVTKSYSFDEIRKNAQLNIELEAAHH	Clinical trial	Anticancer agent CHS-828 inhibits cellular synthesis of NAD. Biochem Biophys Res Commun. 2008 Mar 21;367(4):799-804.	21	EC:2.4	Pentosyltransferase	NAPRTase family.	2.4.2.12	Glycosyltransferases	Domain of unknown function (DUF5598); Nicotinate phosphoribosyltransferase (NAPRTase) family	PF18127; PF04095	PF18127; DUF5598; PF04095; NAPRTase	.	.	hsa00760:Nicotinate and nicotinamide metabolism; hsa01100:Metabolic pathways	"R-HSA-1368108:BMAL1:CLOCK,NPAS2 activates circadian gene expression"	.	P43490
TTFMCB6	NAPE-hydrolyzing phospholipase D (NAPE-PLD)	Q6IQ20	NAPEP_HUMAN	.	NAPE-PLD; N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D; N-acyl phosphatidylethanolamine phospholipase D; C7orf18	NAPEPLD	"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)."	EC 3.1.4.54	4QN9	MDENESNQSLMTSSQYPKEAVRKRQNSARNSGASDSSRFSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNPSIPNVLRWLIMEKDHSSVPSSKEELDKELPVLKPYFITNPEEAGVREAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDAVLISHNHYDHLDYNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHTDVQTKKSMAIHWGTFALANEHYLEPPVKLNEALERYGLNAEDFFVLKHGESRYLNNDDENF	Literature-reported	Intestinal epithelial N-acylphosphatidylethanolamine phospholipase D links dietary fat to metabolic adaptations in obesity and steatosis. Nat Commun. 2019 Jan 28;10(1):457.	.	.	.	.	.	.	.	.	.	.	.	hsa04723: Retrograde endocannabinoid signaling	"R-HSA-2466712: Biosynthesis of A2E, implicated in retinal degradation"	MetaCyc:ENSG00000161048-MON	Q6IQ20
TTVR1FW	FHA-HIT-interacting protein	.	PNCB_HUMAN	Single Protein	Nicotinate phosphoribosyltransferase; NAPRTase; Nicotinate phosphoribosyltransferase domain-containing protein 1; FHIP; NAPRT1	NAPRT	"Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Helps prevent cellular oxidative stress via its role in NAD biosynthesis."	.	.	MAAEQDPEARAAARPLLTDLYQATMALGYWRAGRARDAAEFELFFRRCPFGGAFALAAGLRDCVRFLRAFRLRDADVQFLASVLPPDTDPAFFEHLRALDCSEVTVRALPEGSLAFPGVPLLQVSGPLLVVQLLETPLLCLVSYASLVATNAARLRLIAGPEKRLLEMGLRRAQGPDGGLTASTYSYLGGFDSSSNVLAGQLRGVPVAGTLAHSFVTSFSGSEVPPDPMLAPAAGEGPGVDLAAKAQVWLEQVCAHLGLGVQEPHPGERAAFVAYALAFPRAFQGLLDTYSVWRSGLPNFLAVALALGELGYRAVGVRLDSGDLLQQAQEIRKVFRAAAAQFQVPWLESVLIVVSNNIDEEALARLAQEGSEVNVIGIGTSVVTCPQQPSLGGVYKLVAVGGQPRMKLTEDPEKQTLPGSKAAFRLLGSDGSPLMDMLQLAEEPVPQAGQELRVWPPGAQEPCTVRPAQVEPLLRLCLQQGQLCEPLPSLAESRALAQLSLSRLSPEHRRLRSPAQYQVVLSERLQALVNSLCAGQSP	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q6XQN6
TT1K6Q4	Arylamine N-acetyltransferase (NAT)	P18440; P11245	ARY1_HUMAN; ARY2_HUMAN	Acyltransferase	NAT; N-acetyltransferase; Arylamide acetylase; AAC	NAT1	"Could have a role in acetylating, and hence inactivating, the antitubercular drug isoniazid."	.	.	MDIEAYLERIGYKKSRNKLDLETLTDILQHQIRAVPFENLNIHCGDAMDLGLEAIFDQVVRRNRGGWCLQVNHLLYWALTTIGFETTMLGGYVYSTPAKKYSTGMIHLLLQVTIDGRNYIVDAGFGRSYQMWQPLELISGKDQPQVPCVFRLTEENGFWYLDQIRREQYIPNEEFLHSDLLEDSKYRKIYSFTLKPRTIEDFESMNTYLQTSPSSVFTSKSFCSLQTPDGVHCLVGFTLTHRRFNYKDNTDLIEFKTLSEEEIEKVLKNIFNISLQRKLVPKHGDRFFTI	Literature-reported	"Selective small molecule inhibitors of the potential breast cancer marker, human arylamine N-acetyltransferase 1, and its murine homologue, mouse a... Bioorg Med Chem. 2009 Jan 15;17(2):905-18."	0	.	.	.	.	.	.	.	.	.	.	hsa00232: Caffeine metabolism; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa05204: Chemical carcinogenesis - DNA adducts	R-HSA-156582: Acetylation; R-HSA-9753281: Paracetamol ADME	.	P18440
TTVXPHT	Neural cell adhesion molecule 1 (NCAM1)	P13591	NCAM1_HUMAN	.	NCAM-1; NCAM; N-CAM-1; MSK39; CD56	NCAM1	"This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc."	.	5LKN; 5AEA; 3MTR; 2VKX; 2VKW	MLQTKDLIWTLFFLGTAVSLQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQKLMFKNAPTPQEFREGEDAVIVCDVVSSLPPTIIWKHKGRDVILKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGRILARGEINFKDIQVIVNVPPTIQARQNIVNATANLGQSVTLVCDAEGFPEPTMSWTKDGEQIEQEEDDEKYIFSDDSSQLTIKKVDKNDEAEYICIAENKAGEQDATIHLKVFAKPKITYVENQTAMELEEQVTLTCEASGDPIPSITWRTSTRNISSEEKASWTRPEKQETLDGHMVVRSHARVSSLTLKSIQYTDAGEYICTASNTIGQDSQSMYLEVQYAPKLQGPVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQESLEFILVQADTPSSPSIDQVEPYSSTAQVQFDEPEATGGVPILKYKAEWRAVGEEVWHSKWYDAKEASMEGIVTIVGLKPETTYAVRLAALNGKGLGEISAASEFKTQPVQGEPSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVRYRALSSEWKPEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQGKSKAAHFVFRTSAQPTAIPANGSPTSGLSTGAIVGILIVIFVLLLVVVDITCYFLNKCGLFMCIAVNLCGKAGPGAKGKDMEEGKAAFSKDESKEPIVEVRTEEERTPNHDGGKHTEPNETTPLTEPEKGPVEAKPECQETETKPAPAEVKTVPNDATQTKENESKA	Clinical trial	ClinicalTrials.gov (NCT03222674) Multi-CAR T Cell Therapy for Acute Myeloid Leukemia	19	.	.	.	.	.	Fibronectin type III domain; Immunoglobulin I-set domain	PF00041; PF07679	PF00041; fn3; PF07679; I-set	.	.	hsa04514:Cell adhesion molecules (CAMs); hsa05020:Prion diseases	R-HSA-3000178: ECM proteoglycans; R-HSA-375165: NCAM signaling for neurite out-growth; R-HSA-419037: NCAM1 interactions; R-HSA-445144: Signal transduction by L1; R-HSA-5673001: RAF/MAP kinase cascade; R-HSA-877300: Interferon gamma signaling	.	P13591
TTZ4JC3	Neutrophil cytosol factor 1 (NCF1)	P14598	NCF1_HUMAN	.	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	NCF1	"NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production)."	.	1WLP; 1W70; 1UEC; 1OV3; 1O7K	MGDTFIRHIALLGFEKRFVPSQHYVYMFLVKWQDLSEKVVYRRFTEIYEFHKTLKEMFPIEAGAINPENRIIPHLPAPKWFDGQRAAENRQGTLTEYCSTLMSLPTKISRCPHLLDFFKVRPDDLKLPTDNQTKKPETYLMPKDGKSTATDITGPIILQTYRAIANYEKTSGSEMALSTGDVVEVVEKSESGWWFCQMKAKRGWIPASFLEPLDSPDETEDPEPNYAGEPYVAIKAYTAVEGDEVSLLEGEAVEVIHKLLDGWWVIRKDDVTGYFPSMYLQKSGQDVSQAQRQIKRGAPPRRSSIRNAHSIHQRSRKRLSQDAYRRNSVRFLQQRRRQARPGPQSPGSPLEEERQTQRSKPQPAVPPRPSADLILNRCSESTKRKLASAV	Literature-reported	The vascular NAD(P)H oxidases as therapeutic targets in cardiovascular diseases. Trends Pharmacol Sci. 2003 Sep;24(9):471-8.	.	.	.	.	.	.	"SH3 terminal domain of 2nd SH3 on Neutrophil cytosol factor 1; NADPH oxidase subunit p47Phox, C terminal domain; PX domain; SH3 domain"	PF16621; PF08944; PF00787; PF00018	PF16621; NECFESHC; PF08944; p47_phox_C; PF00787; PX; PF00018; SH3_1	.	.	hsa04062: Chemokine signaling pathway; hsa04145: Phagosome; hsa04380: Osteoclast differentiation; hsa04613: Neutrophil extracellular trap formation; hsa04666: Fc gamma R-mediated phagocytosis; hsa04670: Leukocyte transendothelial migration; hsa05020: Prion disease; hsa05140: Leishmaniasis; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05415: Diabetic cardiomyopathy; hsa05417: Lipid and atherosclerosis; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-1222556: ROS and RNS production in phagocytes; R-HSA-1236973: Cross-presentation of particulate exogenous antigens (phagosomes); R-HSA-3299685: Detoxification of Reactive Oxygen Species; R-HSA-4420097: VEGFA-VEGFR2 Pathway; R-HSA-5668599: RHO GTPases Activate NADPH Oxidases; R-HSA-9013149: RAC1 GTPase cycle; R-HSA-9013404: RAC2 GTPase cycle; R-HSA-9013423: RAC3 GTPase cycle	.	P14598
TTMA3VF	NCK adaptor protein 1 (NCK1)	P16333	NCK1_HUMAN	.	SH2/SH3 adaptor protein NCKalpha; SH2/SH3 adaptor protein NCK-alpha; Nck1; Nck-1; NCK; Cytoplasmic protein NCK1	NCK1	"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."	.	2JW4; 2JS2; 2JS0; 2CUB; 2CI9	MAEEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKSWWRVRNSMNKTGFVPSNYVERKNSARKASIVKNLKDTLGIGKVKRKPSVPDSASPADDSFVDPGERLYDLNMPAYVKFNYMAEREDELSLIKGTKVIVMEKCSDGWWRGSYNGQVGWFPSNYVTEEGDSPLGDHVGSLSEKLAAVVNNLNTGQVLHVVQALYPFSSSNDEELNFEKGDVMDVIEKPENDPEWWKCRKINGMVGLVPKNYVTVMQNNPLTSGLEPSPPQCDYIRPSLTGKFAGNPWYYGKVTRHQAEMALNERGHEGDFLIRDSESSPNDFSVSLKAQGKNKHFKVQLKETVYCIGQRKFSTMEELVEHYKKAPIFTSEQGEKLYLVKHLS	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	SH2 domain; SH3 domain; Variant SH3 domain	PF00017; PF00018; PF14604	PF00017; SH2; PF00018; SH3_1; PF14604; SH3_9	.	.	hsa04012: ErbB signaling pathway; hsa04360: Axon guidance; hsa04660: T cell receptor signaling pathway; hsa05130: Pathogenic Escherichia coli infection	R-HSA-186763: Downstream signal transduction; R-HSA-202433: Generation of second messenger molecules; R-HSA-2029482: Regulation of actin dynamics for phagocytic cup formation; R-HSA-373753: Nephrin family interactions; R-HSA-418885: DCC mediated attractive signaling; R-HSA-428540: Activation of RAC1; R-HSA-4420097: VEGFA-VEGFR2 Pathway; R-HSA-5663213: RHO GTPases Activate WASPs and WAVEs; R-HSA-9013420: RHOU GTPase cycle; R-HSA-9013424: RHOV GTPase cycle; R-HSA-9664422: FCGR3A-mediated phagocytosis; R-HSA-983695: Antigen activates B Cell Receptor (BCR) leading to generation of second messengers	.	P16333
TTK1V5Q	Nucleolin messenger RNA (NCL mRNA)	P19338	NUCL_HUMAN	mRNA target	Protein C23 (mRNA); Nucleolin (mRNA)	NCL	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.	.	2KRR; 2FC9; 2FC8	MVKLAKAGKNQGDPKKMAPPPKEVEEDSEDEEMSEDEEDDSSGEEVVIPQKKGKKAAATSAKKVVVSPTKKVAVATPAKKAAVTPGKKAAATPAKKTVTPAKAVTTPGKKGATPGKALVATPGKKGAAIPAKGAKNGKNAKKEDSDEEEDDDSEEDEEDDEDEDEDEDEIEPAAMKAAAAAPASEDEDDEDDEDDEDDDDDEEDDSEEEAMETTPAKGKKAAKVVPVKAKNVAEDEDEEEDDEDEDDDDDEDDEDDDDEDDEEEEEEEEEEPVKEAPGKRKKEMAKQKAAPEAKKQKVEGTEPTTAFNLFVGNLNFNKSAPELKTGISDVFAKNDLAVVDVRIGMTRKFGYVDFESAEDLEKALELTGLKVFGNEIKLEKPKGKDSKKERDARTLLAKNLPYKVTQDELKEVFEDAAEIRLVSKDGKSKGIAYIEFKTEADAEKTFEEKQGTEIDGRSISLYYTGEKGQNQDYRGGKNSTWSGESKTLVLSNLSYSATEETLQEVFEKATFIKVPQNQNGKSKGYAFIEFASFEDAKEALNSCNKREIEGRAIRLELQGPRGSPNARSQPSKTLFVKGLSEDTTEETLKESFDGSVRARIVTDRETGSSKGFGFVDFNSEEDAKAAKEAMEDGEIDGNKVTLDWAKPKGEGGFGGRGGGRGGFGGRGGGRGGRGGFGGRGRGGFGGRGGFRGGRGGGGDHKPQGKKTKFE	Literature-reported	"US patent application no. 6,165,786, Antisense modulation of nucleolin expression."	0	mRNA	mRNA target	.	.	.	"RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)"	PF00076	PF00076; RRM_1	.	.	hsa05130:Pathogenic Escherichia coli infection	R-HSA-6791226: Major pathway of rRNA processing in the nucleolus and cytosol	.	P19338
TTCSZH7	Nucleolin (NCL)	P19338	NUCL_HUMAN	.	Protein C23	NCL	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.	.	2KRR; 2FC9; 2FC8	MVKLAKAGKNQGDPKKMAPPPKEVEEDSEDEEMSEDEEDDSSGEEVVIPQKKGKKAAATSAKKVVVSPTKKVAVATPAKKAAVTPGKKAAATPAKKTVTPAKAVTTPGKKGATPGKALVATPGKKGAAIPAKGAKNGKNAKKEDSDEEEDDDSEEDEEDDEDEDEDEDEIEPAAMKAAAAAPASEDEDDEDDEDDEDDDDDEEDDSEEEAMETTPAKGKKAAKVVPVKAKNVAEDEDEEEDDEDEDDDDDEDDEDDDDEDDEEEEEEEEEEPVKEAPGKRKKEMAKQKAAPEAKKQKVEGTEPTTAFNLFVGNLNFNKSAPELKTGISDVFAKNDLAVVDVRIGMTRKFGYVDFESAEDLEKALELTGLKVFGNEIKLEKPKGKDSKKERDARTLLAKNLPYKVTQDELKEVFEDAAEIRLVSKDGKSKGIAYIEFKTEADAEKTFEEKQGTEIDGRSISLYYTGEKGQNQDYRGGKNSTWSGESKTLVLSNLSYSATEETLQEVFEKATFIKVPQNQNGKSKGYAFIEFASFEDAKEALNSCNKREIEGRAIRLELQGPRGSPNARSQPSKTLFVKGLSEDTTEETLKESFDGSVRARIVTDRETGSSKGFGFVDFNSEEDAKAAKEAMEDGEIDGNKVTLDWAKPKGEGGFGGRGGGRGGFGGRGGGRGGRGGFGGRGRGGFGGRGGFRGGRGGGGDHKPQGKKTKFE	Clinical trial	Targeting G-quadruplexes in gene promoters: a novel anticancer strategy . Nat Rev Drug Discov. 2011 April; 10(4): 261-275.	21	.	RNA recognition motif	.	.	.	"RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)"	PF00076	PF00076; RRM_1	.	.	hsa05130: Pathogenic Escherichia coli infection	R-HSA-6791226: Major pathway of rRNA processing in the nucleolus and cytosol	.	P19338
TT124R0	Nuclear receptor coactivator 3 (NCOA3)	Q9Y6Q9	NCOA3_HUMAN	Acyltransferase	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	NCOA3	"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."	EC 2.3.1.48	6ES7; 3L3Z; 3L3X; 1KBH	MSGLGENLDPLASDSRKRKLPCDTPGQGLTCSGEKRRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKTISNDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYNILHEEDRKDFLKNLPKSTVNGVSWTNETQRQKSHTFNCRMLMKTPHDILEDINASPEMRQRYETMQCFALSQPRAMMEEGEDLQSCMICVARRITTGERTFPSNPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRCIQRFFSLNDGQSWSQKRHYQEAYLNGHAETPVYRFSLADGTIVTAQTKSKLFRNPVTNDRHGFVSTHFLQREQNGYRPNPNPVGQGIRPPMAGCNSSVGGMSMSPNQGLQMPSSRAYGLADPSTTGQMSGARYGGSSNIASLTPGPGMQSPSSYQNNNYGLNMSSPPHGSPGLAPNQQNIMISPRNRGSPKIASHQFSPVAGVHSPMASSGNTGNHSFSSSSLSALQAISEGVGTSLLSTLSSPGPKLDNSPNMNITQPSKVSNQDSKSPLGFYCDQNPVESSMCQSNSRDHLSDKESKESSVEGAENQRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDSSCKESSVSVTSPSGVSSSTSGGVSSTSNMHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSITSCGDGNVVKQEQLSPKKKENNALLRYLLDRDDPSDALSKELQPQVEGVDNKMSQCTSSTIPSSSQEKDPKIKTETSEEGSGDLDNLDAILGDLTSSDFYNNSISSNGSHLGTKQQVFQGTNSLGLKSSQSVQSIRPPYNRAVSLDSPVSVGSSPPVKNISAFPMLPKQPMLGGNPRMMDSQENYGSSMGGPNRNVTVTQTPSSGDWGLPNSKAGRMEPMNSNSMGRPGGDYNTSLPRPALGGSIPTLPLRSNSIPGARPVLQQQQQMLQMRPGEIPMGMGANPYGQAAASNQLGSWPDGMLSMEQVSHGTQNRPLLRNSLDDLVGPPSNLEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPELVNQGQALEPKQDAFQGQEAAVMMDQKAGLYGQTYPAQGPPMQGGFHLQGQSPSFNSMMNQMNQQGNFPLQGMHPRANIMRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALELKMENPTAGGAAVMRPMMQPQVSSQQGFLNAQMVAQRSRELLSHHFRQQRVAMMMQQQQQQQQQQQQQQQQQQQQQQQQQQQQQTQAFSPPPNVTASPSMDGLLAGPTMPQAPPQQFPYQPNYGMGQQPDPAFGRVSSPPNAMMSSRMGPSQNPMMQHPQAASIYQSSEMKGWPSGNLARNSSFSQQQFAHQGNPAVYSMVHMNGSSGHMGQMNMNPMPMSGMPMGPDQKYC	Literature-reported	In silico identification and biochemical evaluation of novel inhibitors of NRH:quinone oxidoreductase 2 (NQO2). Bioorg Med Chem Lett. 2010 Dec 15;20(24):7331-6.	0	EC:2.3	Acyltransferase	SRC/p160 nuclear receptor coactivator family.	2.3.1.48	Acyltransferases	Domain of unknown function (DUF1518) ; Domain of unknown function (DUF4927); Nuclear receptor coactivator; PAS fold; Steroid receptor coactivator	PF07469; PF16279; PF08815; PF00989; PF08832	PF07469; DUF1518; PF16279; DUF4927; PF08815; Nuc_rec_co-act; PF00989; PAS; PF08832; SRC-1	.	.	hsa04919:Thyroid hormone signaling pathway	R-HSA-1989781:PPARA activates gene expression; R-HSA-381340:Transcriptional regulation of white adipocyte differentiation; R-HSA-5687128:MAPK6/MAPK4 signaling	.	Q9Y6Q9
TT8OY02	ARA70 messenger RNA (NCOA4 mRNA)	Q13772	NCOA4_HUMAN	mRNA target	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)	NCOA4	Ligand-independent coactivator of the peroxisome proliferator-activated receptor (PPAR) gamma. Enhances the androgen receptor transcriptional activity in prostate cancer cells.	.	1T5Z	MNTFQDQSGSSSNREPLLRCSDARRDLELAIGGVLRAEQQIKDNLREVKAQIHSCISRHLECLRSREVWLYEQVDLIYQLKEETLQQQAQQLYSLLGQFNCLTHQLECTQNKDLANQVSVCLERLGSLTLKPEDSTVLLFEADTITLRQTITTFGSLKTIQIPEHLMAHASSANIGPFLEKRGCISMPEQKSASGIVAVPFSEWLLGSKPASGYQAPYIPSTDPQDWLTQKQTLENSQTSSRACNFFNNVGGNLKGLENWLLKSEKSSYQKCNSHSTTSSFSIEMEKVGDQELPDQDEMDLSDWLVTPQESHKLRKPENGSRETSEKFKLLFQSYNVNDWLVKTDSCTNCQGNQPKGVEIENLGNLKCLNDHLEAKKPLSTPSMVTEDWLVQNHQDPCKVEEVCRANEPCTSFAECVCDENCEKEALYKWLLKKEGKDKNGMPVEPKPEPEKHKDSLNMWLCPRKEVIEQTKAPKAMTPSRIADSFQVIKNSPLSEWLIRPPYKEGSPKEVPGTEDRAGKQKFKSPMNTSWCSFNTADWVLPGKKMGNLSQLSSGEDKWLLRKKAQEVLLNSPLQEEHNFPPDHYGLPAVCDLFACMQLKVDKEKWLYRTPLQM	Literature-reported	"US patent application no. 6,255,110, Antisense modulation of ARA70 expression."	0	mRNA	mRNA target	.	.	.	Nuclear coactivator	PF12489	PF12489; ARA70	.	.	hsa05200:Pathways in cancer; hsa05216:Thyroid cancer	.	.	Q13772
TT39EZT	Nuclear receptor coactivator 4 (NCOA4)	Q13772	NCOA4_HUMAN	.	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	NCOA4	Ligand-independent coactivator of the peroxisome proliferator-activated receptor (PPAR) gamma. Enhances the androgen receptor transcriptional activity in prostate cancer cells.	.	1T5Z	MNTFQDQSGSSSNREPLLRCSDARRDLELAIGGVLRAEQQIKDNLREVKAQIHSCISRHLECLRSREVWLYEQVDLIYQLKEETLQQQAQQLYSLLGQFNCLTHQLECTQNKDLANQVSVCLERLGSLTLKPEDSTVLLFEADTITLRQTITTFGSLKTIQIPEHLMAHASSANIGPFLEKRGCISMPEQKSASGIVAVPFSEWLLGSKPASGYQAPYIPSTDPQDWLTQKQTLENSQTSSRACNFFNNVGGNLKGLENWLLKSEKSSYQKCNSHSTTSSFSIEMEKVGDQELPDQDEMDLSDWLVTPQESHKLRKPENGSRETSEKFKLLFQSYNVNDWLVKTDSCTNCQGNQPKGVEIENLGNLKCLNDHLEAKKPLSTPSMVTEDWLVQNHQDPCKVEEVCRANEPCTSFAECVCDENCEKEALYKWLLKKEGKDKNGMPVEPKPEPEKHKDSLNMWLCPRKEVIEQTKAPKAMTPSRIADSFQVIKNSPLSEWLIRPPYKEGSPKEVPGTEDRAGKQKFKSPMNTSWCSFNTADWVLPGKKMGNLSQLSSGEDKWLLRKKAQEVLLNSPLQEEHNFPPDHYGLPAVCDLFACMQLKVDKEKWLYRTPLQM	Literature-reported	Reducing the agonist activity of antiandrogens by a dominant-negative androgen receptor coregulator ARA70 in prostate cancer cells. J Biol Chem. 2003 May 30;278(22):19619-26.	.	.	.	.	.	.	Nuclear coactivator	PF12489	PF12489; ARA70	.	.	hsa04216: Ferroptosis; hsa05200: Pathways in cancer; hsa05216: Thyroid cancer	.	.	Q13772
TTQNRJM	Natural cytotoxic triggering receptor 1 (NCR1)	O76036	NCTR1_HUMAN	.	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	NCR1	Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis.	.	1P6F; 1OLL	MSSTLPALLCVGLCLSQRISAQQQTLPKPFIWAEPHFMVPKEKQVTICCQGNYGAVEYQLHFEGSLFAVDRPKPPERINKVKFYIPDMNSRMAGQYSCIYRVGELWSEPSNLLDLVVTEMYDTPTLSVHPGPEVISGEKVTFYCRLDTATSMFLLLKEGRSSHVQRGYGKVQAEFPLGPVTTAHRGTYRCFGSYNNHAWSFPSEPVKLLVTGDIENTSLAPEDPTFPADTWGTYLLTTETGLQKDHALWDHTAQNLLRMGLAFLVLVALVWFLVEDWLSRKRTRERASRASTWEGRRRLNTQTL	Literature-reported	Innate immunity in multiple sclerosis white matter lesions: expression of natural cytotoxicity triggering receptor 1 (NCR1). J Neuroinflammation. 2012 Jan 2;9:1.	.	.	.	.	.	.	.	.	.	.	.	hsa04650: Natural killer cell mediated cytotoxicity	R-HSA-198933: Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell	.	O76036
TTRU1NG	Mitochondrial complex I (NDUFA13)	Q9P0J0	NDUAD_HUMAN	.	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	NDUFA13	"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."	.	5XTI; 5XTH; 5XTD; 5XTC; 5XTB	MAASKVKQDMPPPGGYGPIDYKRNLPRRGLSGYSMLAIGIGTLIYGHWSIMKWNRERRRLQIEDFEARIALLPLLQAETDRRTLQMLRENLEEEAIIMKDVPDWKVGESVFHTTRWVPPLIGELYGLRTTEEALHASHGFMWYT	Clinical trial	The next generation of cardiac positron emission tomography imaging agents: discovery of flurpiridaz F-18 for detection of coronary disease. Semin Nucl Med. 2011 Jul;41(4):305-13.	25	.	.	complex I NDUFA13 subunit family.	.	.	GRIM-19 protein	PF06212	PF06212; GRIM-19	.	.	hsa00190: Oxidative phosphorylation; hsa01100: Metabolic pathways; hsa04714: Thermogenesis; hsa04723: Retrograde endocannabinoid signaling; hsa04932: Non-alcoholic fatty liver disease; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05014: Amyotrophic lateral sclerosis; hsa05016: Huntington disease; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05415: Diabetic cardiomyopathy	R-HSA-611105: Respiratory electron transport; R-HSA-6799198: Complex I biogenesis	MetaCyc:HS05364-MON	Q9P0J0
TTCHGVF	HUMAN NADH:ubiquinone oxidoreductase complex assembly factor 2 (NDUFAF2)	Q8N183	NDUF2_HUMAN	Complex I NDUFA12 subunit family	NDUFA12-like protein; NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2; Myc-induced mitochondrial protein ; MMTN ; Mimitin ; B17.2-like; B17.2L	NDUFAF2	"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."	.	.	MGWSQDLFRALWRSLSREVKEHVGTDQFGNKYYYIPQYKNWRGQTIREKRIVEAANKKEVDYEAGDIPTEWEAWIRRTRKTPPTMEEILKNEKHREEIKIKSQDFYEKEKLLSKETSEELLPPPVQTQIKGHASAPYFGKEEPSVAPSSTGKTFQPGSWMPRDGKSHNQ	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa04714: Thermogenesis	R-HSA-6799198: Complex I biogenesis	.	Q8N183
TTBYJ39	HUMAN NADH:ubiquinone oxidoreductase subunit B9 (NDUFB9)	Q9Y6M9	NDUB9_HUMAN	Complex I LYR family	NADH-ubiquinone oxidoreductase B22 subunit; NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9; LYR motif-containing protein 3; Complex I-B22; CI-B22	NDUFB9	"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."	.	5XTC; 5XTD; 5XTH; 5XTI	MAFLASGPYLTHQQKVLRLYKRALRHLESWCVQRDKYRYFACLMRARFEEHKNEKDMAKATQLLKEAEEEFWYRQHPQPYIFPDSPGGTSYERYDCYKVPEWCLDDWHPSEKAMYPDYFAKREQWKKLRRESWEREVKQLQEETPPGGPLTEALPPARKEGDLPPLWWYIVTRPRERPM	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	hsa00190: Oxidative phosphorylation; hsa01100: Metabolic pathways; hsa04714: Thermogenesis; hsa04723: Retrograde endocannabinoid signaling; hsa04932: Non-alcoholic fatty liver disease; hsa05010: Alzheimer disease; hsa05012: Parkinson disease; hsa05014: Amyotrophic lateral sclerosis; hsa05016: Huntington disease; hsa05020: Prion disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05415: Diabetic cardiomyopathy	R-HSA-611105: Respiratory electron transport; R-HSA-6799198: Complex I biogenesis	MetaCyc:HS07466-MON	Q9Y6M9
TTPO9EG	Nectin cell adhesion molecule 4 (NECTIN4)	Q96NY8	NECT4_HUMAN	.	Poliovirus receptor-related protein 4; PVRL4; PRR4; Nectin-4; LNIR; Ig superfamily receptor LNIR	NECTIN4	"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."	.	4JJH; 4GJT; 4FRW	MPLSLGAEMWGPEAWLLLLLLLASFTGRCPAGELETSDVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQELALLHSKYGLHVSPAYEGRVEQPPPPRNPLDGSVLLRNAVQADEGEYECRVSTFPAGSFQARLRLRVLVPPLPSLNPGPALEEGQGLTLAASCTAEGSPAPSVTWDTEVKGTTSSRSFKHSRSAAVTSEFHLVPSRSMNGQPLTCVVSHPGLLQDQRITHILHVSFLAEASVRGLEDQNLWHIGREGAMLKCLSEGQPPPSYNWTRLDGPLPSGVRVDGDTLGFPPLTTEHSGIYVCHVSNEFSSRDSQVTVDVLDPQEDSGKQVDLVSASVVVVGVIAALLFCLLVVVVVLMSRYHRRKAQQMTQKYEEELTLTRENSIRRLHSHHTDPRSQPEESVGLRAEGHPDSLKDNSSCSVMSEEPEGRSYSTLTTVREIETQTELLSPGSGRAEEEEDQDEGIKQAMNHFVQENGTLRAKPTGNGIYINGRGHLV	Successful	2011 Pipeline of Seattle Genetics.	17	.	.	nectin family.	.	.	CD80-like C2-set immunoglobulin domain ; Immunoglobulin V-set domain	PF08205; PF07686	PF08205; C2-set_2; PF07686; V-set	.	.	hsa04520:Adherens junction	R-HSA-418990:Adherens junctions interactions	.	Q96NY8
TT1QU6G	E3 ubiquitin-protein ligase NEDD4 (NEDD4)	P46934	NEDD4_HUMAN	.	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	NEDD4	"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)."	EC 2.3.2.26	5C91; 5C7J; 5AHT; 4N7H; 4N7F	MAQSLRLHFAARRSNTYPLSETSGDDLDSHVHMCFKRPTRISTSNVVQMKLTPRQTALAPLIKENVQSQERSSVPSSENVNKKSSCLQISLQPTRYSGYLQSSNVLADSDDASFTCILKDGIYSSAVVDNELNAVNDGHLVSSPAICSGSLSNFSTSDNGSYSSNGSDFGSCASITSGGSYTNSVISDSSSYTFPPSDDTFLGGNLPSDSTSNRSVPNRNTTPCEIFSRSTSTDPFVQDDLEHGLEIMKLPVSRNTKIPLKRYSSLVIFPRSPSTTRPTSPTSLCTLLSKGSYQTSHQFIISPSEIAHNEDGTSAKGFLSTAVNGLRLSKTICTPGEVRDIRPLHRKGSLQKKIVLSNNTPRQTVCEKSSEGYSCVSVHFTQRKAATLDCETTNGDCKPEMSEIKLNSDSEYIKLMHRTSACLPSSQNVDCQININGELERPHSQMNKNHGILRRSISLGGAYPNISCLSSLKHNCSKGGPSQLLIKFASGNEGKVDNLSRDSNRDCTNELSNSCKTRDDFLGQVDVPLYPLPTENPRLERPYTFKDFVLHPRSHKSRVKGYLRLKMTYLPKTSGSEDDNAEQAEELEPGWVVLDQPDAACHLQQQQEPSPLPPGWEERQDILGRTYYVNHESRRTQWKRPTPQDNLTDAENGNIQLQAQRAFTTRRQISEETESVDNRESSENWEIIREDEATMYSNQAFPSPPPSSNLDVPTHLAEELNARLTIFGNSAVSQPASSSNHSSRRGSLQAYTFEEQPTLPVLLPTSSGLPPGWEEKQDERGRSYYVDHNSRTTTWTKPTVQATVETSQLTSSQSSAGPQSQASTSDSGQQVTQPSEIEQGFLPKGWEVRHAPNGRPFFIDHNTKTTTWEDPRLKIPAHLRGKTSLDTSNDLGPLPPGWEERTHTDGRIFYINHNIKRTQWEDPRLENVAITGPAVPYSRDYKRKYEFFRRKLKKQNDIPNKFEMKLRRATVLEDSYRRIMGVKRADFLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLHKPITLHDMESVDSEYYNSLRWILENDPTELDLRFIIDEELFGQTHQHELKNGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSANHQVIQWFWKAVLMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQSFTVEQWGTPEKLPRAHTCFNRLDLPPYESFEELWDKLQMAIENTQGFDGVD	Literature-reported	NEDD4: a promising target for cancer therapy. Curr Cancer Drug Targets. 2014;14(6):549-56.	.	.	.	.	.	.	.	.	.	.	.	hsa04120:Ubiquitin mediated proteolysis; hsa04144:Endocytosis; hsa04530:Tight junction; hsa05169:Epstein-Barr virus infection	R-HSA-1169408: ISG15 antiviral mechanism; R-HSA-1253288: Downregulation of ERBB4 signaling; R-HSA-8948747: Regulation of PTEN localization; R-HSA-8948751: Regulation of PTEN stability and activity; R-HSA-983168: Antigen processing: Ubiquitination & Proteasome degradation	.	P46934
TTNDC4K	Ubiquitin-like protein Nedd8 (NEDD8)	Q15843	NEDD8_HUMAN	Ubiquitin family	Neural precursor cell expressed developmentally down-regulated protein 8; Neddylin; NEDD-8	NEDD8	"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."	.	4P5O; 4HCP; 4FBJ; 4F8C; 3GZN	MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGGGGLRQ	Clinical trial	"Promoting tumorigenesis in nasopharyngeal carcinoma, NEDD8 serves as a potential theranostic target.Cell Death Dis. 2017 Jun 1;8(6):e2834. "	25	.	.	.	.	.	.	.	.	.	.	.	R-HSA-2173789: TGF-beta receptor signaling activates SMADs; R-HSA-5689603: UCH proteinases; R-HSA-8856825: Cargo recognition for clathrin-mediated endocytosis; R-HSA-8951664: Neddylation; R-HSA-917937: Iron uptake and transport	.	Q15843
TT1UREA	Enhancer of filamentation 1 (NEDD9)	Q14511	CASL_HUMAN	.	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	NEDD9	"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."	.	5X3S; 2L81	MKYKNLMARALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWLCSLHGRQGIVPGNRVKLLIGPMQETASSHEQPASGLMQQTFGQQKLYQVPNPQAAPRDTIYQVPPSYQNQGIYQVPTGHGTQEQEVYQVPPSVQRSIGGTSGPHVGKKVITPVRTGHGYVYEYPSRYQKDVYDIPPSHTTQGVYDIPPSSAKGPVFSVPVGEIKPQGVYDIPPTKGVYAIPPSACRDEAGLREKDYDFPPPMRQAGRPDLRPEGVYDIPPTCTKPAGKDLHVKYNCDIPGAAEPVARRHQSLSPNHPPPQLGQSVGSQNDAYDVPRGVQFLEPPAETSEKANPQERDGVYDVPLHNPPDAKGSRDLVDGINRLSFSSTGSTRSNMSTSSTSSKESSLSASPAQDKRLFLDPDTAIERLQRLQQALEMGVSSLMALVTTDWRCYGYMERHINEIRTAVDKVELFLKEYLHFVKGAVANAACLPELILHNKMKRELQRVEDSHQILSQTSHDLNECSWSLNILAINKPQNKCDDLDRFVMVAKTVPDDAKQLTTTINTNAEALFRPGPGSLHLKNGPESIMNSTEYPHGGSQGQLLHPGDHKAQAHNKALPPGLSKEQAPDCSSSDGSERSWMDDYDYVHLQGKEEFERQQKELLEKENIMKQNKMQLEHHQLSQFQLLEQEITKPVENDISKWKPSQSLPTTNSGVSAQDRQLLCFYYDQCETHFISLLNAIDALFSCVSSAQPPRIFVAHSKFVILSAHKLVFIGDTLTRQVTAQDIRNKVMNSSNQLCEQLKTIVMATKMAALHYPSTTALQEMVHQVTDLSRNAQLFKRSLLEMATF	Literature-reported	"Effects of human enhancer of filamentation 1 (HEF1) gene on the proliferation, invasion and metastasis of bladder cancer cells. J BUON. 2018 May-Jun;23(3):782-786."	.	.	.	CAS family.	.	.	Crk-Associated Substrate C-terminal domain; Serine rich protein interaction domain; Variant SH3 domain	PF12026; PF08824; PF14604	PF12026; CAS_C; PF08824; Serine_rich; PF14604; SH3_9	.	.	.	.	.	Q14511
TTO5QT2	NIMA-related kinase 1 (NEK1)	Q96PY6	NEK1_HUMAN	.	Serine/threonine-protein kinase Nek1; Renal carcinoma antigen NY-REN-55; NimA-related protein kinase 1; Never in mitosis A-related kinase 1; KIAA1901	NEK1	"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."	EC 2.7.11.1	4B9D; 4APC	MEKYVRLQKIGEGSFGKAILVKSTEDGRQYVIKEINISRMSSKEREESRREVAVLANMKHPNIVQYRESFEENGSLYIVMDYCEGGDLFKRINAQKGVLFQEDQILDWFVQICLALKHVHDRKILHRDIKSQNIFLTKDGTVQLGDFGIARVLNSTVELARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYELCTLKHAFEAGSMKNLVLKIISGSFPPVSLHYSYDLRSLVSQLFKRNPRDRPSVNSILEKGFIAKRIEKFLSPQLIAEEFCLKTFSKFGSQPIPAKRPASGQNSISVMPAQKITKPAAKYGIPLAYKKYGDKKLHEKKPLQKHKQAHQTPEKRVNTGEERRKISEEAARKRRLEFIEKEKKQKDQIISLMKAEQMKRQEKERLERINRAREQGWRNVLSAGGSGEVKAPFLGSGGTIAPSSFSSRGQYEHYHAIFDQMQQQRAEDNEAKWKREIYGRGLPERGILPGVRPGFPYGAAGHHHFPDADDIRKTLKRLKAVSKQANANRQKGQLAVERAKQVEEFLQRKREAMQNKARAEGHMVYLARLRQIRLQNFNERQQIKAKLRGEKKEANHSEGQEGSEEADMRRKKIESLKAHANARAAVLKEQLERKRKEAYEREKKVWEEHLVAKGVKSSDVSPPLGQHETGGSPSKQQMRSVISVTSALKEVGVDSSLTDTRETSEEMQKTNNAISSKREILRRLNENLKAQEDEKGKQNLSDTFEINVHEDAKEHEKEKSVSSDRKKWEAGGQLVIPLDELTLDTSFSTTERHTVGEVIKLGPNGSPRRAWGKSPTDSVLKILGEAELQLQTELLENTTIRSEISPEGEKYKPLITGEKKVQCISHEINPSAIVDSPVETKSPEFSEASPQMSLKLEGNLEEPDDLETEILQEPSGTNKDESLPCTITDVWISEEKETKETQSADRITIQENEVSEDGVSSTVDQLSDIHIEPGTNDSQHSKCDVDKSVQPEPFFHKVVHSEHLNLVPQVQSVQCSPEESFAFRSHSHLPPKNKNKNSLLIGLSTGLFDANNPKMLRTCSLPDLSKLFRTLMDVPTVGDVRQDNLEIDEIEDENIKEGPSDSEDIVFEETDTDLQELQASMEQLLREQPGEEYSEEEESVLKNSDVEPTANGTDVADEDDNPSSESALNEEWHSDNSDGEIASECECDSVFNHLEELRLHLEQEMGFEKFFEVYEKIKAIHEDEDENIEICSKIVQNILGNEHQHLYAKILHLVMADGAYQEDNDE	Literature-reported	Aminopyrazine inhibitors binding to an unusual inactive conformation of the mitotic kinase Nek2: SAR and structural characterization. J Med Chem. 2010 Nov 11;53(21):7682-98.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	Q96PY6
TT3VZ24	NIMA-related kinase 2 (NEK2)	P51955	NEK2_HUMAN	Kinase	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	NEK2	"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."	EC 2.7.11.1	6H0O; 5M57; 5M55; 5M53; 5M51	MPSRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCEGGDLASVITKGTKERQYLDEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPLIADLVADEQRRNLERRGRQLGEPEKSQDSSPVLSELKLKEIQLQERERALKAREERLEQKEQELCVRERLAEDKLARAENLLKNYSLLKERKFLSLASNPELLNLPSSVIKKKVHFSGESKENIMRSENSESQLTSKSKCKDLKKRLHAAQLRAQALSDIEKNYQLKSRQILGMR	Literature-reported	Design of potent thiophene inhibitors of polo-like kinase 1 with improved solubility and reduced protein binding. Bioorg Med Chem Lett. 2009 Mar 15;19(6):1694-7.	0	EC:2.7	.	protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	.	.	.	R-HSA-179409: APC-Cdc20 mediated degradation of Nek2A; 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-380320: Recruitment of NuMA to mitotic centrosomes; R-HSA-5620912: Anchoring of the basal body to the plasma membrane; R-HSA-8854518: AURKA Activation by TPX2	.	P51955
TT8I2M7	Serine/threonine-protein kinase Nek6 (NEK6)	Q9HC98	NEK6_HUMAN	.	Protein kinase SID6-1512; NimA-related protein kinase 6; Never in mitosis A-related kinase 6	NEK6	"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."	EC 2.7.11.1	.	MAGQPGHMPHGGSSNNLCHTLGPVHPPDPQRHPNTLSFRCSLADFQIEKKIGRGQFSEVYKATCLLDRKTVALKKVQIFEMMDAKARQDCVKEIGLLKQLNHPNIIKYLDSFIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSETTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPLPGEHYSEKLRELVSMCICPDPHQRPDIGYVHQVAKQMHIWMSST	Literature-reported	Nek6 mediates human cancer cell transformation and is a potential cancer therapeutic target. RETRACTED ARTICLESee: Retraction NoticeMol Cancer Res. 2010 May;8(5):717-28.	.	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-2980767: Activation of NIMA Kinases NEK9, NEK6, NEK7; R-HSA-3301854: Nuclear Pore Complex (NPC) Disassembly; R-HSA-9648025: EML4 and NUDC in mitotic spindle formation"	.	Q9HC98
TTHOI91	NIMA-related kinase 6 (NEK6)	Q9HC98	NEK6_HUMAN	Kinase	Serine/threonine-protein kinase Nek6; Protein kinase SID6-1512; NimA-related protein kinase 6; Never in mitosis A-related kinase 6	NEK6	"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."	EC 2.7.11.1	.	MAGQPGHMPHGGSSNNLCHTLGPVHPPDPQRHPNTLSFRCSLADFQIEKKIGRGQFSEVYKATCLLDRKTVALKKVQIFEMMDAKARQDCVKEIGLLKQLNHPNIIKYLDSFIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSETTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPLPGEHYSEKLRELVSMCICPDPHQRPDIGYVHQVAKQMHIWMSST	Literature-reported	Substituted 2H-isoquinolin-1-one as potent Rho-Kinase inhibitors. Part 1: Hit-to-lead account. Bioorg Med Chem Lett. 2010 Jun 1;20(11):3235-9.	0	EC:2.7	.	protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily.	2.7.11.1	Transferring phosphorus-containing groups	Protein kinase domain	PF00069	PF00069; Pkinase	1.I.1.1.3	The Eukaryotic Nuclear Pore Complex (E-NPC) Family	.	"R-HSA-2980767: Activation of NIMA Kinases NEK9, NEK6, NEK7; R-HSA-3301854: Nuclear Pore Complex (NPC) Disassembly; R-HSA-9648025: EML4 and NUDC in mitotic spindle formation"	.	Q9HC98
TTJ5SWP	NIMA-related kinase 7 (NEK7)	Q8TDX7	NEK7_HUMAN	.	Serine/threonine-protein kinase Nek7; NimA-related protein kinase 7; Never in mitosis A-related kinase 7	NEK7	"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."	EC 2.7.11.1	6GT1; 5DE2; 2WQN; 2WQM	MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDVTYVYDVAKRMHACTASS	Literature-reported	Substituted 2H-isoquinolin-1-one as potent Rho-Kinase inhibitors. Part 1: Hit-to-lead account. Bioorg Med Chem Lett. 2010 Jun 1;20(11):3235-9.	0	.	.	.	.	.	.	.	.	.	.	hsa04621: NOD-like receptor signaling pathway	"R-HSA-2980767: Activation of NIMA Kinases NEK9, NEK6, NEK7; R-HSA-3301854: Nuclear Pore Complex (NPC) Disassembly; R-HSA-9648025: EML4 and NUDC in mitotic spindle formation"	.	Q8TDX7
TT8AH9I	Serine/threonine-protein kinase Nek8 (NEK8)	Q86SG6	NEK8_HUMAN	Protein kinase superfamily. NEK Ser/Thr protein kinase family	Nima-related protein kinase 12a; NimA-related protein kinase 8; Never in mitosis A-related kinase 8; NEK12A; JCK	NEK8	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.	EC 2.7.11.1	.	MEKYERIRVVGRGAFGIVHLCLRKADQKLVIIKQIPVEQMTKEERQAAQNECQVLKLLNHPNVIEYYENFLEDKALMIAMEYAPGGTLAEFIQKRCNSLLEEETILHFFVQILLALHHVHTHLILHRDLKTQNILLDKHRMVVKIGDFGISKILSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMSGTFAPISDRYSPELRQLVLSLLSLEPAQRPPLSHIMAQPLCIRALLNLHTDVGSVRMRRAEKSVAPSNTGSRTTSVRCRGIPRGPVRPAIPPPLSSVYAWGGGLGTPLRLPMLNTEVVQVAAGRTQKAGVTRSGRLILWEAPPLGAGGGSLLPGAVEQPQPQFISRFLEGQSGVTIKHVACGDFFTACLTDRGIIMTFGSGSNGCLGHGSLTDISQPTIVEALLGYEMVQVACGASHVLALSTERELFAWGRGDSGRLGLGTRESHSCPQQVPMPPGQEAQRVVCGIDSSMILTVPGQALACGSNRFNKLGLDHLSLGEEPVPHQQVEEALSFTLLGSAPLDQEPLLSIDLGTAHSAAVTASGDCYTFGSNQHGQLGTNTRRGSRAPCKVQGLEGIKMAMVACGDAFTVAIGAESEVYSWGKGARGRLGRRDEDAGLPRPVQLDETHPYTVTSVSCCHGNTLLAVRSVTDEPVPP	Literature-reported	"Nek8, a NIMA family kinase member, is overexpressed in primary human breast tumors. Gene. 2004 Mar 17;328:135-42."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q86SG6
TTM57AW	HUMAN NIMA related kinase 9 (NEK9)	Q8TD19	NEK9_HUMAN	Kinase	Serine/threonine-protein kinase Nek9; NimA-related protein kinase 9; NimA-related kinase 8; Never in mitosis A-related kinase 9; Nercc1 kinase; Nek8	NEK9	"Human protein NIMA related kinase 9 interacts with SARS-CoV-2 Nsp9 protein with high significance, which indicates NEK9 as a potential therapeutic target."	EC 2.7.11.1	3ZKE; 3ZKF	MSVLGEYERHCDSINSDFGSESGGCGDSSPGPSASQGPRAGGGAAEQEELHYIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSEKERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTLNIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAMEVDSSQYSLELIQMVHSCLDQDPEQRPTADELLDRPLLRKRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQKLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIRQVSCGDDFTVCVTDEGQLYAFGSDYYGCMGVDKVAGPEVLEPMQLNFFLSNPVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQKVDVPKALIIVAVQCGCDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDERGRLLTFGCNKCGQLGVGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHTILIVEKVLNSKTIRSNSSGLSIGTVFQSSSPGGGGGGGGGEEEDSQQESETPDPSGGFRGTMEADRGMEGLISPTEAMGNSNGASSSCPGWLRKELENAEFIPMPDSPSPLSAAFSESEKDTLPYEELQGLKVASEAPLEHKPQVEASSPRLNPAVTCAGKGTPLTPPACACSSLQVEVERLQGLVLKCLAEQQKLQQENLQIFTQLQKLNKKLEGGQQVGMHSKGTQTAKEEMEMDPKPDLDSDSWCLLGTDSCRPSL	.	A SARS-CoV-2 Protein Interaction Map Reveals Targets for Drug Repurposing. Nature. 2020 Apr 30.  doi: 10.1038/s41586-020-2286-9.	.	.	.	.	.	.	.	.	.	.	.	.	"R-HSA-2980767: Activation of NIMA Kinases NEK9, NEK6, NEK7; R-HSA-3301854: Nuclear Pore Complex (NPC) Disassembly; R-HSA-9648025: EML4 and NUDC in mitotic spindle formation"	.	Q8TD19
TT7H4BF	Nel-related protein 1 (NELL1)	Q92832	NELL1_HUMAN	.	NELL1; NEL-like protein 1	NELL1	Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization.	.	.	MPMDLILVVWFCVCTARTVVGFGMDPDLQMDIVTELDLVNTTLGVAQVSGMHNASKAFLFQDIEREIHAAPHVSEKLIQLFRNKSEFTILATVQQKPSTSGVILSIRELEHSYFELESSGLRDEIRYHYIHNGKPRTEALPYRMADGQWHKVALSVSASHLLLHVDCNRIYERVIDPPDTNLPPGINLWLGQRNQKHGLFKGIIQDGKIIFMPNGYITQCPNLNHTCPTCSDFLSLVQGIMDLQELLAKMTAKLNYAETRLSQLENCHCEKTCQVSGLLYRDQDSWVDGDHCRNCTCKSGAVECRRMSCPPLNCSPDSLPVHIAGQCCKVCRPKCIYGGKVLAEGQRILTKSCRECRGGVLVKITEMCPPLNCSEKDHILPENQCCRVCRGHNFCAEGPKCGENSECKNWNTKATCECKSGYISVQGDSAYCEDIDECAAKMHYCHANTVCVNLPGLYRCDCVPGYIRVDDFSCTEHDECGSGQHNCDENAICTNTVQGHSCTCKPGYVGNGTICRAFCEEGCRYGGTCVAPNKCVCPSGFTGSHCEKDIDECSEGIIECHNHSRCVNLPGWYHCECRSGFHDDGTYSLSGESCIDIDECALRTHTCWNDSACINLAGGFDCLCPSGPSCSGDCPHEGGLKHNGQVWTLKEDRCSVCSCKDGKIFCRRTACDCQNPSADLFCCPECDTRVTSQCLDQNGHKLYRSGDNWTHSCQQCRCLEGEVDCWPLTCPNLSCEYTAILEGECCPRCVSDPCLADNITYDIRKTCLDSYGVSRLSGSVWTMAGSPCTTCKCKNGRVCCSVDFECLQNN	Literature-reported	Combining Smoothened Agonist and NEL-Like Protein-1 Enhances Bone Healing. Plast Reconstr Surg. 2017 Jun;139(6):1385-1396.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q92832
TTHZ752	Nestin (NES)	P48681	NEST_HUMAN	.	Nbla00170	NES	"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."	.	.	MEGCMGEESFQMWELNRRLEAYLARVKALEEQNELLSAELGGLRAQSADTSWRAHADDELAALRALVDQRWREKHAAEVARDNLAEELEGVAGRCQQLRLARERTTEEVARNRRAVEAEKCARAWLSSQVAELERELEALRVAHEEERVGLNAQAACAPRCPAPPRGPPAPAPEVEELARRLGEAWRGAVRGYQERVAHMETSLGQARERLGRAVQGAREGRLELQQLQAERGGLLERRAALEQRLEGRWQERLRATEKFQLAVEALEQEKQGLQSQIAQVLEGRQQLAHLKMSLSLEVATYRTLLEAENSRLQTPGGGSKTSLSFQDPKLELQFPRTPEGRRLGSLLPVLSPTSLPSPLPATLETPVPAFLKNQEFLQARTPTLASTPIPPTPQAPSPAVDAEIRAQDAPLSLLQTQGGRKQAPEPLRAEARVAIPASVLPGPEEPGGQRQEASTGQSPEDHASLAPPLSPDHSSLEAKDGESGGSRVFSICRGEGEGQIWGLVEKETAIEGKVVSSLQQEIWEEEDLNRKEIQDSQVPLEKETLKSLGEEIQESLKTLENQSHETLERENQECPRSLEEDLETLKSLEKENKELLKDVEVVRPLEKEAVGQLKPTGKEDTQTLQSLQKENQELMKSLEGNLETFLFPGTENQELVSSLQENLESLTALEKENQEPLRSPEVGDEEALRPLTKENQEPLRSLEDENKEAFRSLEKENQEPLKTLEEEDQSIVRPLETENHKSLRSLEEQDQETLRTLEKETQQRRRSLGEQDQMTLRPPEKVDLEPLKSLDQEIARPLENENQEFLKSLKEESVEAVKSLETEILESLKSAGQENLETLKSPETQAPLWTPEEINQGAMNPLEKEIQEPLESVEVNQETFRLLEEENQESLRSLGAWNLENLRSPEEVDKESQRNLEEEENLGKGEYQESLRSLEEEGQELPQSADVQRWEDTVEKDQELAQESPPGMAGVENEDEAELNLREQDGFTGKEEVVEQGELNATEEVWIPGEGHPESPEPKEQRGLVEGASVKGGAEGLQDPEGQSQQVGAPGLQAPQGLPEAIEPLVEDDVAPGGDQASPEVMLGSEPAMGESAAGAEPGPGQGVGGLGDPGHLTREEVMEPPLEEESLEAKRVQGLEGPRKDLEEAGGLGTEFSELPGKSRDPWEPPREGREESEAEAPRGAEEAFPAETLGHTGSDAPSPWPLGSEEAEEDVPPVLVSPSPTYTPILEDAPGPQPQAEGSQEASWGVQGRAEALGKVESEQEELGSGEIPEGPQEEGEESREESEEDELGETLPDSTPLGFYLRSPTSPRWDPTGEQRPPPQGETGKEGWDPAVLASEGLEAPPSEKEEGEEGEEECGRDSDLSEEFEDLGTEAPFLPGVPGEVAEPLGQVPQLLLDPAAWDRDGESDGFADEEESGEEGEEDQEEGREPGAGRWGPGSSVGSLQALSSSQRGEFLESDSVSVSVPWDDSLRGAVAGAPKTALETESQDSAEPSGSEEESDPVSLEREDKVPGPLEIPSGMEDAGPGADIIGVNGQGPNLEGKSQHVNGGVMNGLEQSEEVGQGMPLVSEGDRGSPFQEEEGSALKTSWAGAPVHLGQGQFLKFTQREGDRESWSSGED	Literature-reported	Nestin: a novel angiogenesis marker and possible target for tumor angiogenesis. World J Gastroenterol. 2013 Jan 7;19(1):42-8.	.	.	Intermediate filament family	intermediate filament family.	.	.	Intermediate filament protein	PF00038	PF00038; Filament	.	.	.	.	.	P48681
TTZIK7P	Neurofibromin-2 (NF2)	P35240	MERL_HUMAN	.	Schwannomin; Schwannomerlin; SCH; Moesin-ezrin-radixin-like protein; Merlin	NF2	"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."	.	6CDS; 4ZRJ; 4ZRI; 3U8Z; 1H4R	MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSDRGGSSKHNTIKKLTLQSAKSRVAFFEEL	Literature-reported	Identification of the cis-acting region in the NF2 gene promoter as a potential target for mutation and methylation-dependent silencing in schwannoma. Genes Cells. 2001 May;6(5):441-54.	.	.	.	.	.	.	.	.	.	.	.	hsa04390: Hippo signaling pathway; hsa04392: Hippo signaling pathway - multiple species; hsa04530: Tight junction	R-HSA-2029482: Regulation of actin dynamics for phagocytic cup formation; R-HSA-5627123: RHO GTPases activate PAKs	.	P35240
TTA6ZN2	Nuclear factor erythroid 2-related factor 2 (Nrf2)	Q16236	NF2L2_HUMAN	Basic leucine zipper bZIP	"Nuclear factor, erythroid derived 2, like 2; NRF2; NFE2-related factor 2; NF-E2-related factor 2; HEBP1"	NFE2L2	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.	.	5WFV; 4IFL; 3ZGC; 2LZ1; 2FLU	MMDLELPPPGLPSQQDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN	Clinical trial	National Cancer Institute Drug Dictionary (drug id 756624).	21	bZIP	BZIP Maf transcription factor	bZIP family. CNC subfamily.	.	.	bZIP Maf transcription factor	PF03131	PF03131; bZIP_Maf	.	.	hsa04141:Protein processing in endoplasmic reticulum	R-HSA-8951664: Neddylation; R-HSA-9679191: Potential therapeutics for SARS; R-HSA-9707587: Regulation of HMOX1 expression and activity; R-HSA-9707616: Heme signaling; R-HSA-9755511: KEAP1-NFE2L2 pathway; R-HSA-9759194: Nuclear events mediated by NFE2L2; R-HSA-9762114: GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2	.	Q16236
TTUIZKC	DNA-binding factor KBF1 (p105)	P19838	NFKB1_HUMAN	.	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	NFKB1	"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."	.	3GUT; 2O61; 2DBF; 1SVC; 1NFI	MAEDDPYLGRPEQMFHLDPSLTHTIFNPEVFQPQMALPTDGPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLMPNFSDSFGGGSGAGAGGGGMFGSGGGGGGTGSTGPGYSFPHYGFPTYGGITFHPGTTKSNAGMKHGTMDTESKKDPEGCDKSDDKNTVNLFGKVIETTEQDQEPSEATVGNGEVTLTYATGTKEESAGVQDNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDHPNGDGLNAIHLAMMSNSLPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAALLKAAGADPLVENFEPLYDLDDSWENAGEDEGVVPGTTPLDMATSWQVFDILNGKPYEPEFTSDDLLAQGDMKQLAEDVKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQAASSPVKTTSQAHSLPLSPASTRQQIDELRDSDSVCDSGVETSFRKLSFTESLTSGASLLTLNKMPHDYGQEGPLEGKI	Clinical trial	Identification of p54(nrb) and the 14-3-3 Protein HS1 as TNF-alpha-inducible genes related to cell cycle control and apoptosis in human arterial endothelial cells. J Biochem Mol Biol. 2005 Jul 31;38(4):447-56.	21	.	.	.	.	.	Ankyrin repeats (3 copies); Death domain; Rel homology dimerisation domain; Rel homology DNA-binding domain	PF12796; PF00531; PF16179; PF00554	PF12796; Ank_2; PF00531; Death; PF16179; RHD_dimer; PF00554; RHD_DNA_bind	.	.	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)	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	.	P19838
TTSXVID	Nuclear factor NF-kappa-B (NFKB)	P19838; Q00653; Q04206; Q01201; Q04864	NFKB1_HUMAN; NFKB2_HUMAN; TF65_HUMAN; RELB_HUMAN; REL_HUMAN	.	Nuclear factor of kappa light polypeptide gene enhancer in B-cells; DNA-binding factor KBF	NFKB1	"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."	.	.	MAEDDPYLGRPEQMFHLDPSLTHTIFNPEVFQPQMALPTDGPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLMPNFSDSFGGGSGAGAGGGGMFGSGGGGGGTGSTGPGYSFPHYGFPTYGGITFHPGTTKSNAGMKHGTMDTESKKDPEGCDKSDDKNTVNLFGKVIETTEQDQEPSEATVGNGEVTLTYATGTKEESAGVQDNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDHPNGDGLNAIHLAMMSNSLPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAALLKAAGADPLVENFEPLYDLDDSWENAGEDEGVVPGTTPLDMATSWQVFDILNGKPYEPEFTSDDLLAQGDMKQLAEDVKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQAASSPVKTTSQAHSLPLSPASTRQQIDELRDSDSVCDSGVETSFRKLSFTESLTSGASLLTLNKMPHDYGQEGPLEGKI	Successful	Emerging drugs for rheumatoid arthritis. Expert Opin Emerg Drugs. 2008 Mar;13(1):175-96.	34	.	.	.	.	.	Ankyrin repeats (3 copies); Death domain; Rel homology dimerisation domain; Rel homology DNA-binding domain	PF12796; PF00531; PF16179; PF00554	PF12796; Ank_2; PF00531; Death; PF16179; RHD_dimer; PF00554; RHD_DNA_bind	.	.	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	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	.	P19838
TTKLNRV	NFKB messenger RNA (NFKB mRNA)	Q00653	NFKB2_HUMAN	mRNA target	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)	NFKB2	"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."	.	5ZMC; 4OT9; 3DO7; 2D96; 1A3Q	MESCYNPGLDGIIEYDDFKLNSSIVEPKEPAPETADGPYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSELGICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSRPQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSKSPGASNLKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDENGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVFLQLKRKRGGDVSDSKQFTYYPLVEDKEEVQRKRRKALPTFSQPFGGGSHMGGGSGGAAGGYGGAGGGGSLGFFPSSLAYSPYQSGAGPMGCYPGGGGGAQMAATVPSRDSGEEAAEPSAPSRTPQCEPQAPEMLQRAREYNARLFGLAQRSARALLDYGVTADARALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIEQIVYVIHHAQDLGVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGAPAVPQLLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEELGLVTHLVTKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPLPSPPTSDSDSDSEGPEKDTRSSFRGHTPLDLTCSTKVKTLLLNAAQNTMEPPLTPPSPAGPGLSLGDTALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRGPETRDKLPSTAEVKEDSAYGSQSVEQEAEKLGPPPEPPGGLCHGHPQPQVH	Clinical trial	"News and Analysis. Nature Reviews Drug Discovery 12, 179 (March 2013)."	25	mRNA	mRNA target	.	.	.	Ankyrin repeats (3 copies); Death domain; Rel homology dimerisation domain; Rel homology DNA-binding domain	PF12796; PF00531; PF16179; PF00554	PF12796; Ank_2; PF00531; Death; PF16179; RHD_dimer; PF00554; RHD_DNA_bind	.	.	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	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	.	Q00653
TTSHAEB	NF-kappa-B inhibitor alpha (NFKBIA)	P25963	IKBA_HUMAN	.	I-kappa-B-alpha; IkB-alpha; IkappaBalpha; Major histocompatibility complex enhancer-binding protein MAD3	NFKBIA	"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."	.	.	MFQAAERPQEWAMEGPRDGLKKERLLDDRHDSGLDSMKDEEYEQMVKELQEIRLEPQEVPRGSEPWKQQLTEDGDSFLHLAIIHEEKALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTPHLHSILKATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQLTWGRPSTRIQQQLGQLTLENLQMLPESEDEESYDTESEFTEFTEDELPYDDCVFGGQRLTL	Clinical trial	"Protective effect of Indole-3-carbinol, an NF-B inhibitor in experimental paradigm of Parkinson's disease: In silico and in vivo studies. Brain Behav Immun. 2020 Nov;90:108-137."	.	.	.	.	.	.	.	.	.	.	.	hsa04024: cAMP signaling pathway; hsa04062: Chemokine signaling pathway; hsa04064: NF-kappa B 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; hsa04625: C-type lectin receptor signaling pathway; hsa04657: IL-17 signaling pathway; hsa04658: Th1 and Th2 cell differentiation; hsa04659: Th17 cell differentiation; hsa04660: T cell receptor signaling pathway; hsa04662: B cell receptor signaling pathway; hsa04668: TNF signaling pathway; hsa04722: Neurotrophin signaling pathway; hsa04920: Adipocytokine signaling pathway; hsa04926: Relaxin signaling pathway; hsa04931: Insulin resistance; hsa04936: Alcoholic liver disease; hsa05120: Epithelial cell signaling in Helicobacter pylori infection; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05134: Legionellosis; hsa05135: Yersinia infection; hsa05140: Leishmaniasis; hsa05142: Chagas disease; hsa05145: Toxoplasmosis; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05162: Measles; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05203: Viral carcinogenesis; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05215: Prostate cancer; hsa05220: Chronic myeloid leukemia; hsa05222: Small cell lung cancer; hsa05235: PD-L1 expression and PD-1 checkpoint pathway in cancer; hsa05417: Lipid and atherosclerosis	R-HSA-1169091: Activation of NF-kappaB in B cells; R-HSA-1810476: RIP-mediated NFkB activation via ZBP1; R-HSA-202424: Downstream TCR signaling; R-HSA-209560: NF-kB is activated and signals survival; R-HSA-2871837: FCERI mediated NF-kB activation; R-HSA-445989: TAK1-dependent IKK and NF-kappa-B activation; R-HSA-4755510: SUMOylation of immune response proteins; R-HSA-5603029: IkBA variant leads to EDA-ID; R-HSA-5607764: CLEC7A (Dectin-1) signaling; R-HSA-5689880: Ub-specific processing proteases; R-HSA-9020702: Interleukin-1 signaling; R-HSA-933542: TRAF6 mediated NF-kB activation	.	P25963
TTDN3LF	Nerve growth factor (NGF)	P01138	NGF_HUMAN	Growth factor	NGFB; Beta-nerve growth factor; Beta-NGF	NGF	"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)."	.	5JZ7; 4ZBN; 4EDX; 4EDW; 2IFG	MSMLFYTLITAFLIGIQAEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNITVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRSSSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFETKCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTACVCVLSRKAVRRA	Clinical trial	Fate of novel painkiller mAbs hangs in balance.Nat Biotechnol.2011 Mar;29(3):173-4.	24	Growth factor	Growth factor	NGF-beta family.	.	.	Nerve growth factor family	PF00243	PF00243; NGF	.	.	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	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	.	P01138
TTEDJN4	Low-affinity nerve growth factor receptor (NGFR)	P08138	TNR16_HUMAN	Cytokine receptor	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	NGFR	"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."	.	5ZGG; 3EWV; 2N97; 2N83; 2N80	MGAGATGRAMDGPRLLLLLLLGVSLGGAKEACPTGLYTHSGECCKACNLGEGVAQPCGANQTVCEPCLDSVTFSDVVSATEPCKPCTECVGLQSMSAPCVEADDAVCRCAYGYYQDETTGRCEACRVCEAGSGLVFSCQDKQNTVCEECPDGTYSDEANHVDPCLPCTVCEDTERQLRECTRWADAECEEIPGRWITRSTPPEGSDSTAPSTQEPEAPPEQDLIASTVAGVVTTVMGSSQPVVTRGTTDNLIPVYCSILAAVVVGLVAYIAFKRWNSCKQNKQGANSRPVNQTPPPEGEKLHSDSGISVDSQSLHDQQPHTQTASGQALKGDGGLYSSLPPAKREEVEKLLNGSAGDTWRHLAGELGYQPEHIDSFTHEACPVRALLASWATQDSATLDALLAALRRIQRADLVESLCSESTATSPV	Successful	2018 FDA drug approvals.Nat Rev Drug Discov. 2019 Feb;18(2):85-89. 	34	Cytokine receptor	Cytokine receptor	.	.	.	Death domain; Tumor necrosis factor receptor member 16 trans-membrane domain; TNFR/NGFR cysteine-rich region	PF00531; PF18422; PF00020	PF00531; Death; PF18422; TNFR_16_TM; PF00020; TNFR_c6	.	.	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	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	.	P08138
TT0T5HK	Immunoglobulin gamma-1 heavy NIE (NIE)	P0DOX5	IGG1_HUMAN	.	Immunoglobulin gamma-1 heavy chain NIE	NIE	"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)."	.	6OGE; 6N35; 6N32; 6N2X; 6MUB	QVQLVQSGGGVVQPGRSLRLSCAASGFTFSRYTIHWVRQAPGKGLEWVAVMSYNGNNKHYADSVNGRFTISRNDSKNTLYLNMNSLRPEDTAVYYCARIRDTAMFFAHWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	.	.	.	P0DOX5
TT789FN	Nischarin (NISCH)	Q9Y2I1	NISCH_HUMAN	.	NISCH; I1R	NISCH	"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. ."	.	3P0C	MATARTFGPEREAEPAKEARVVGSELVDTYTVYIIQVTDGSHEWTVKHRYSDFHDLHEKLVAERKIDKNLLPPKKIIGKNSRSLVEKREKDLEVYLQKLLAAFPGVTPRVLAHFLHFHFYEINGITAALAEELFEKGEQLLGAGEVFAIGPLQLYAVTEQLQQGKPTCASGDAKTDLGHILDFTCRLKYLKVSGTEGPFGTSNIQEQLLPFDLSIFKSLHQVEISHCDAKHIRGLVASKPTLATLSVRFSATSMKEVLVPEASEFDEWEPEGTTLEGPVTAVIPTWQALTTLDLSHNSVSEIDESVKLIPKIEFLDLSHNGLLVVDNLQHLYNLVHLDLSYNKLSSLEGLHTKLGNIKTLNLAGNLLESLSGLHKLYSLVNLDLRDNRIEQMEEVRSIGSLPCLEHVSLLNNPLSIIPDYRTKVLAQFGERASEVCLDDTVTTEKELDTVEVLKAIQKAKEVKSKLSNPEKKGGEDSRLSAAPCIRPSSSPPTVAPASASLPQPILSNQGIMFVQEEALASSLSSTDSLTPEHQPIAQGCSDSLESIPAGQAASDDLRDVPGAVGGASPEHAEPEVQVVPGSGQIIFLPFTCIGYTATNQDFIQRLSTLIRQAIERQLPAWIEAANQREEGQGEQGEEEDEEEEEEEDVAENRYFEMGPPDVEEEEGGGQGEEEEEEEEDEEAEEERLALEWALGADEDFLLEHIRILKVLWCFLIHVQGSIRQFAACLVLTDFGIAVFEIPHQESRGSSQHILSSLRFVFCFPHGDLTEFGFLMPELCLVLKVRHSENTLFIISDAANLHEFHADLRSCFAPQHMAMLCSPILYGSHTSLQEFLRQLLTFYKVAGGCQERSQGCFPVYLVYSDKRMVQTAAGDYSGNIEWASCTLCSAVRRSCCAPSEAVKSAAIPYWLLLTPQHLNVIKADFNPMPNRGTHNCRNRNSFKLSRVPLSTVLLDPTRSCTQPRGAFADGHVLELLVGYRFVTAIFVLPHEKFHFLRVYNQLRASLQDLKTVVIAKTPGTGGSPQGSFADGQPAERRASNDQRPQEVPAEALAPAPAEVPAPAPAAASASGPAKTPAPAEASTSALVPEETPVEAPAPPPAEAPAQYPSEHLIQATSEENQIPSHLPACPSLRHVASLRGSAIIELFHSSIAEVENEELRHLMWSSVVFYQTPGLEVTACVLLSTKAVYFVLHDGLRRYFSEPLQDFWHQKNTDYNNSPFHISQCFVLKLSDLQSVNVGLFDQHFRLTGSTPMQVVTCLTRDSYLTHCFLQHLMVVLSSLERTPSPEPVDKDFYSEFGNKTTGKMENYELIHSSRVKFTYPSEEEIGDLTFTVAQKMAEPEKAPALSILLYVQAFQVGMPPPGCCRGPLRPKTLLLTSSEIFLLDEDCVHYPLPEFAKEPPQRDRYRLDDGRRVRDLDRVLMGYQTYPQALTLVFDDVQGHDLMGSVTLDHFGEVPGGPARASQGREVQWQVFVPSAESREKLISLLARQWEALCGRELPVELTG	Literature-reported	"Expression of Nischarin negatively correlates with estrogen receptor and alters apoptosis, migration and invasion in human breast cancer. Biochem Biophys Res Commun. 2017 Mar 11;484(3):536-542."	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-9013149: RAC1 GTPase cycle; R-HSA-9696264: RND3 GTPase cycle; R-HSA-9696270: RND2 GTPase cycle	.	Q9Y2I1
TTUN4L1	Imidazoline receptor 1 (IR1)	Q9Y2I1	NISCH_HUMAN	.	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	NISCH	"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."	.	3P0C	MATARTFGPEREAEPAKEARVVGSELVDTYTVYIIQVTDGSHEWTVKHRYSDFHDLHEKLVAERKIDKNLLPPKKIIGKNSRSLVEKREKDLEVYLQKLLAAFPGVTPRVLAHFLHFHFYEINGITAALAEELFEKGEQLLGAGEVFAIGPLQLYAVTEQLQQGKPTCASGDAKTDLGHILDFTCRLKYLKVSGTEGPFGTSNIQEQLLPFDLSIFKSLHQVEISHCDAKHIRGLVASKPTLATLSVRFSATSMKEVLVPEASEFDEWEPEGTTLEGPVTAVIPTWQALTTLDLSHNSVSEIDESVKLIPKIEFLDLSHNGLLVVDNLQHLYNLVHLDLSYNKLSSLEGLHTKLGNIKTLNLAGNLLESLSGLHKLYSLVNLDLRDNRIEQMEEVRSIGSLPCLEHVSLLNNPLSIIPDYRTKVLAQFGERASEVCLDDTVTTEKELDTVEVLKAIQKAKEVKSKLSNPEKKGGEDSRLSAAPCIRPSSSPPTVAPASASLPQPILSNQGIMFVQEEALASSLSSTDSLTPEHQPIAQGCSDSLESIPAGQAASDDLRDVPGAVGGASPEHAEPEVQVVPGSGQIIFLPFTCIGYTATNQDFIQRLSTLIRQAIERQLPAWIEAANQREEGQGEQGEEEDEEEEEEEDVAENRYFEMGPPDVEEEEGGGQGEEEEEEEEDEEAEEERLALEWALGADEDFLLEHIRILKVLWCFLIHVQGSIRQFAACLVLTDFGIAVFEIPHQESRGSSQHILSSLRFVFCFPHGDLTEFGFLMPELCLVLKVRHSENTLFIISDAANLHEFHADLRSCFAPQHMAMLCSPILYGSHTSLQEFLRQLLTFYKVAGGCQERSQGCFPVYLVYSDKRMVQTAAGDYSGNIEWASCTLCSAVRRSCCAPSEAVKSAAIPYWLLLTPQHLNVIKADFNPMPNRGTHNCRNRNSFKLSRVPLSTVLLDPTRSCTQPRGAFADGHVLELLVGYRFVTAIFVLPHEKFHFLRVYNQLRASLQDLKTVVIAKTPGTGGSPQGSFADGQPAERRASNDQRPQEVPAEALAPAPAEVPAPAPAAASASGPAKTPAPAEASTSALVPEETPVEAPAPPPAEAPAQYPSEHLIQATSEENQIPSHLPACPSLRHVASLRGSAIIELFHSSIAEVENEELRHLMWSSVVFYQTPGLEVTACVLLSTKAVYFVLHDGLRRYFSEPLQDFWHQKNTDYNNSPFHISQCFVLKLSDLQSVNVGLFDQHFRLTGSTPMQVVTCLTRDSYLTHCFLQHLMVVLSSLERTPSPEPVDKDFYSEFGNKTTGKMENYELIHSSRVKFTYPSEEEIGDLTFTVAQKMAEPEKAPALSILLYVQAFQVGMPPPGCCRGPLRPKTLLLTSSEIFLLDEDCVHYPLPEFAKEPPQRDRYRLDDGRRVRDLDRVLMGYQTYPQALTLVFDDVQGHDLMGSVTLDHFGEVPGGPARASQGREVQWQVFVPSAESREKLISLLARQWEALCGRELPVELTG	Literature-reported	The I1-imidazoline receptor: from binding site to therapeutic target in cardiovascular disease. J Hypertens Suppl. 1997 Jan;15(1):S9-23.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-9013149: RAC1 GTPase cycle; R-HSA-9696264: RND3 GTPase cycle; R-HSA-9696270: RND2 GTPase cycle	.	Q9Y2I1
TT1E0JK	Homeobox protein Nkx-3.1 (NKX3-1)	Q99801	NKX31_HUMAN	.	NKX3A; NKX31; NKX3.1; Homeobox protein Nkx3.1; Homeobox protein NK3 homolog A; Homeobox protein NK-3 homolog A	NKX3-1	"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."	.	2L9R	MLRVPEPRPGEAKAEGAAPPTPSKPLTSFLIQDILRDGAQRQGGRTSSQRQRDPEPEPEPEPEGGRSRAGAQNDQLSTGPRAAPEEAETLAETEPERHLGSYLLDSENTSGALPRLPQTPKQPQKRSRAAFSHTQVIELERKFSHQKYLSAPERAHLAKNLKLTETQVKIWFQNRRYKTKRKQLSSELGDLEKHSSLPALKEEAFSRASLVSVYNSYPYYPYLYCVGSWSPAFW	Literature-reported	NKX3.1 as a marker of prostatic origin in metastatic tumors. Am J Surg Pathol. 2010 Aug;34(8):1097-105.	.	.	.	NK-3 homeobox family.	.	.	Homeodomain	PF00046	PF00046; Homeodomain	.	.	hsa05200: Pathways in cancer; hsa05215: Prostate cancer	.	.	Q99801
TTWZC78	Caterpiller protein 16.1 (NLRC5)	Q86WI3	NLRC5_HUMAN	NLRP family	Nucleotide-binding oligomerization domain protein 4; Nucleotide-binding oligomerization domain protein 27; NOD4; NOD27; CLR16.1	NLRC5	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.	.	.	MDPVGLQLGNKNLWSCLVRLLTKDPEWLNAKMKFFLPNTDLDSRNETLDPEQRVILQLNKLHVQGSDTWQSFIHCVCMQLEVPLDLEVLLLSTFGYDDGFTSQLGAEGKSQPESQLHHGLKRPHQSCGSSPRRKQCKKQQLELAKKYLQLLRTSAQQRYRSQIPGSGQPHAFHQVYVPPILRRATASLDTPEGAIMGDVKVEDGADVSISDLFNTRVNKGPRVTVLLGKAGMGKTTLAHRLCQKWAEGHLNCFQALFLFEFRQLNLITRFLTPSELLFDLYLSPESDHDTVFQYLEKNADQVLLIFDGLDEALQPMGPDGPGPVLTLFSHLCNGTLLPGCRVMATSRPGKLPACLPAEAAMVHMLGFDGPRVEEYVNHFFSAQPSREGALVELQTNGRLRSLCAVPALCQVACLCLHHLLPDHAPGQSVALLPNMTQLYMQMVLALSPPGHLPTSSLLDLGEVALRGLETGKVIFYAKDIAPPLIAFGATHSLLTSFCVCTGPGHQQTGYAFTHLSLQEFLAALHLMASPKVNKDTLTQYVTLHSRWVQRTKARLGLSDHLPTFLAGLASCTCRPFLSHLAQGNEDCVGAKQAAVVQVLKKLATRKLTGPKVVELCHCVDETQEPELASLTAQSLPYQLPFHNFPLTCTDLATLTNILEHREAPIHLDFDGCPLEPHCPEALVGCGQIENLSFKSRKCGDAFAEALSRSLPTMGRLQMLGLAGSKITARGISHLVKALPLCPQLKEVSFRDNQLSDQVVLNIVEVLPHLPRLRKLDLSSNSICVSTLLCLARVAVTCPTVRMLQAREADLIFLLSPPTETTAELQRAPDLQESDGQRKGAQSRSLTLRLQKCQLQVHDAEALIALLQEGPHLEEVDLSGNQLEDEGCRLMAEAASQLHIARKLDLSNNGLSVAGVHCVLRAVSACWTLAELHISLQHKTVIFMFAQEPEEQKGPQERAAFLDSLMLQMPSELPLSSRRMRLTHCGLQEKHLEQLCKALGGSCHLGHLHLDFSGNALGDEGAARLAQLLPGLGALQSLNLSENGLSLDAVLGLVRCFSTLQWLFRLDISFESQHILLRGDKTSRDMWATGSLPDFPAAAKFLGFRQRCIPRSLCLSECPLEPPSLTRLCATLKDCPGPLELQLSCEFLSDQSLETLLDCLPQLPQLSLLQLSQTGLSPKSPFLLANTLSLCPRVKKVDLRSLHHATLHFRSNEEEEGVCCGRFTGCSLSQEHVESLCWLLSKCKDLSQVDLSANLLGDSGLRCLLECLPQVPISGLLDLSHNSISQESALYLLETLPSCPRVREASVNLGSEQSFRIHFSREDQAGKTLRLSECSFRPEHVSRLATGLSKSLQLTELTLTQCCLGQKQLAILLSLVGRPAGLFSLRVQEPWADRARVLSLLEVCAQASGSVTEISISETQQQLCVQLEFPRQEENPEAVALRLAHCDLGAHHSLLVGQLMETCARLQQLSLSQVNLCEDDDASSLLLQSLLLSLSELKTFRLTSSCVSTEGLAHLASGLGHCHHLEELDLSNNQFDEEGTKALMRALEGKWMLKRLDLSHLLLNSSTLALLTHRLSQMTCLQSLRLNRNSIGDVGCCHLSEALRAATSLEELDLSHNQIGDAGVQHLATILPGLPELRKIDLSGNSISSAGGVQLAESLVLCRRLEELMLGCNALGDPTALGLAQELPQHLRVLHLPFSHLGPGGALSLAQALDGSPHLEEISLAENNLAGGVLRFCMELPLLRQIDLVSCKIDNQTAKLLTSSFTSCPALEVILLSWNLLGDEAAAELAQVLPQMGRLKRVDLEKNQITALGAWLLAEGLAQGSSIQVIRLWNNPIPCDMAQHLKSQEPRLDFAFFDNQPQAPWGT	Literature-reported	NLRC5/CITA: A Key Player in Cancer Immune Surveillance. Trends Cancer. 2017 Jan;3(1):28-38.	.	.	.	.	.	.	.	.	.	.	.	.	R-HSA-168928: DDX58/IFIH1-mediated induction of interferon-alpha/beta; R-HSA-936440: Negative regulators of DDX58/IFIH1 signaling	.	Q86WI3
TTQX29T	NLR pyrin domain containing 1 (NLRP1)	Q9C000	NLRP1_HUMAN	.	"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"	NLRP1	"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."	.	5Y3S; 4IM6; 4IFP; 3KAT; 1PN5	MAGGAWGRLACYLEFLKKEELKEFQLLLANKAHSRSSSGETPAQPEKTSGMEVASYLVAQYGEQRAWDLALHTWEQMGLRSLCAQAQEGAGHSPSFPYSPSEPHLGSPSQPTSTAVLMPWIHELPAGCTQGSERRVLRQLPDTSGRRWREISASLLYQALPSSPDHESPSQESPNAPTSTAVLGSWGSPPQPSLAPREQEAPGTQWPLDETSGIYYTEIREREREKSEKGRPPWAAVVGTPPQAHTSLQPHHHPWEPSVRESLCSTWPWKNEDFNQKFTQLLLLQRPHPRSQDPLVKRSWPDYVEENRGHLIEIRDLFGPGLDTQEPRIVILQGAAGIGKSTLARQVKEAWGRGQLYGDRFQHVFYFSCRELAQSKVVSLAELIGKDGTATPAPIRQILSRPERLLFILDGVDEPGWVLQEPSSELCLHWSQPQPADALLGSLLGKTILPEASFLITARTTALQNLIPSLEQARWVEVLGFSESSRKEYFYRYFTDERQAIRAFRLVKSNKELWALCLVPWVSWLACTCLMQQMKRKEKLTLTSKTTTTLCLHYLAQALQAQPLGPQLRDLCSLAAEGIWQKKTLFSPDDLRKHGLDGAIISTFLKMGILQEHPIPLSYSFIHLCFQEFFAAMSYVLEDEKGRGKHSNCIIDLEKTLEAYGIHGLFGASTTRFLLGLLSDEGEREMENIFHCRLSQGRNLMQWVPSLQLLLQPHSLESLHCLYETRNKTFLTQVMAHFEEMGMCVETDMELLVCTFCIKFSRHVKKLQLIEGRQHRSTWSPTMVVLFRWVPVTDAYWQILFSVLKVTRNLKELDLSGNSLSHSAVKSLCKTLRRPRCLLETLRLAGCGLTAEDCKDLAFGLRANQTLTELDLSFNVLTDAGAKHLCQRLRQPSCKLQRLQLVSCGLTSDCCQDLASVLSASPSLKELDLQQNNLDDVGVRLLCEGLRHPACKLIRLGLDQTTLSDEMRQELRALEQEKPQLLIFSRRKPSVMTPTEGLDTGEMSNSTSSLKRQRLGSERAASHVAQANLKLLDVSKIFPIAEIAEESSPEVVPVELLCVPSPASQGDLHTKPLGTDDDFWGPTGPVATEVVDKEKNLYRVHFPVAGSYRWPNTGLCFVMREAVTVEIEFCVWDQFLGEINPQHSWMVAGPLLDIKAEPGAVEAVHLPHFVALQGGHVDTSLFQMAHFKEEGMLLEKPARVELHHIVLENPSFSPLGVLLKMIHNALRFIPVTSVVLLYHRVHPEEVTFHLYLIPSDCSIRKAIDDLEMKFQFVRIHKPPPLTPLYMGCRYTVSGSGSGMLEILPKELELCYRSPGEDQLFSEFYVGHLGSGIRLQVKDKKDETLVWEALVKPGDLMPATTLIPPARIAVPSPLDAPQLLHFVDQYREQLIARVTSVEVVLDKLHGQVLSQEQYERVLAENTRPSQMRKLFSLSQSWDRKCKDGLYQALKETHPHLIMELWEKGSKKGLLPLSS	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1768).	0	.	.	.	.	.	.	.	.	.	.	hsa04621: NOD-like receptor signaling pathway	R-HSA-844455: The NLRP1 inflammasome	.	Q9C000
TT4EN8X	Caterpiller protein 1.1 (NLRP3)	Q96P20	NLRP3_HUMAN	.	"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"	NLRP3	"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."	.	3QF2; 2NAQ	MKMASTRCKLARYLEDLEDVDLKKFKMHLEDYPPQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAKRDEPKWGSDNARVSNPTVICQEDSIEEEWMGLLEYLSRISICKMKKDYRKKYRKYVRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQQEREQELLAIGKTKTCESPVSPIKMELLFDPDDEHSEPVHTVVFQGAAGIGKTILARKMMLDWASGTLYQDRFDYLFYIHCREVSLVTQRSLGDLIMSCCPDPNPPIHKIVRKPSRILFLMDGFDELQGAFDEHIGPLCTDWQKAERGDILLSSLIRKKLLPEASLLITTRPVALEKLQHLLDHPRHVEILGFSEAKRKEYFFKYFSDEAQARAAFSLIQENEVLFTMCFIPLVCWIVCTGLKQQMESGKSLAQTSKTTTAVYVFFLSSLLQPRGGSQEHGLCAHLWGLCSLAADGIWNQKILFEESDLRNHGLQKADVSAFLRMNLFQKEVDCEKFYSFIHMTFQEFFAAMYYLLEEEKEGRTNVPGSRLKLPSRDVTVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCKISQQIRLELLKWIEVKAKAKKLQIQPSQLELFYCLYEMQEEDFVQRAMDYFPKIEINLSTRMDHMVSSFCIENCHRVESLSLGFLHNMPKEEEEEEKEGRHLDMVQCVLPSSSHAACSHGLVNSHLTSSFCRGLFSVLSTSQSLTELDLSDNSLGDPGMRVLCETLQHPGCNIRRLWLGRCGLSHECCFDISLVLSSNQKLVELDLSDNALGDFGIRLLCVGLKHLLCNLKKLWLVSCCLTSACCQDLASVLSTSHSLTRLYVGENALGDSGVAILCEKAKNPQCNLQKLGLVNSGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLKQQSCLLQNLGLSEMYFNYETKSALETLQEEKPELTVVFEPSW	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	NLRP family.	.	.	Fish-specific NACHT associated domain; Leucine Rich repeat; NACHT domain; NLRC4 helical domain HD2; NOD2 winged helix domain; PAAD/DAPIN/Pyrin domain	PF14484; PF13516; PF05729; PF17776; PF17779; PF02758	PF14484; FISNA; PF13516; LRR_6; PF05729; NACHT; PF17776; NLRC4_HD2; PF17779; NOD2_WH; PF02758; PYRIN	.	.	hsa04217: Necroptosis; hsa04621: NOD-like receptor signaling pathway; hsa04625: C-type lectin receptor signaling pathway; hsa05130: Pathogenic Escherichia coli infection; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05133: Pertussis; hsa05135: Yersinia infection; hsa05164: Influenza A; hsa05171: Coronavirus disease - COVID-19; hsa05417: Lipid and atherosclerosis	R-HSA-5689901: Metalloprotease DUBs; R-HSA-844456: The NLRP3 inflammasome; R-HSA-9660826: Purinergic signaling in leishmaniasis infection; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses; R-HSA-9707564: Cytoprotection by HMOX1	.	Q96P20
TTKT026	NLR family member X1 (NLRX1)	Q86UT6	NLRX1_HUMAN	NLRP family	Caterpiller protein 11.3; CLR11.3; Nucleotide-binding oligomerization domain protein 5; Nucleotide-binding oligomerization domain protein 9	NLRX1	"Participates in antiviral signaling. Acts as a negative regulator of MAVS-mediated antiviral responses, through the inhibition of the virus-induced RLH (RIG-like helicase)-MAVS interaction (PubMed:18200010). Instead, promotes autophagy by interacting with TUFM and subsequently recruiting the autophagy-related proteins ATG5 and ATG12 (PubMed:22749352). Regulates also MAVS-dependent NLRP3 inflammasome activation to attenuate apoptosis (PubMed:27393910). Has no inhibitory function on NF-kappa-B signaling pathway, but enhances NF-kappa-B and JUN N-terminal kinase dependent signaling through the production of reactive oxygen species (PubMed:18219313). Regulates viral mediated-inflammation and energy metabolism in a sex-dependent manner (By similarity). In females, prevents uncontrolled inflammation and energy metabolism and thus, may contribute to the sex differences observed in infectious and inflammatory diseases (By similarity). {ECO:0000250|UniProtKB:Q3TL44, ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:18219313, ECO:0000269|PubMed:22749352, ECO:0000269|PubMed:27393910}."	.	3UN9	MRWGHHLPRASWGSGFRRALQRPDDRIPFLIHWSWPLQGERPFGPPRAFIRHHGSSVDSAPPPGRHGRLFPSASATEAIQRHRRNLAEWFSRLPREERQFGPTFALDTVHVDPVIRESTPDELLRPPAELALEHQPPQAGLPPLALSQLFNPDACGRRVQTVVLYGTVGTGKSTLVRKMVLDWCYGRLPAFELLIPFSCEDLSSLGPAPASLCQLVAQRYTPLKEVLPLMAAAGSHLLFVLHGLEHLNLDFRLAGTGLCSDPEEPQEPAAIIVNLLRKYMLPQASILVTTRPSAIGRIPSKYVGRYGEICGFSDTNLQKLYFQLRLNQPYCGYAVGGSGVSATPAQRDHLVQMLSRNLEGHHQIAAACFLPSYCWLVCATLHFLHAPTPAGQTLTSIYTSFLRLNFSGETLDSTDPSNLSLMAYAARTMGKLAYEGVSSRKTYFSEEDVCGCLEAGIRTEEEFQLLHIFRRDALRFFLAPCVEPGRAGTFVFTVPAMQEYLAALYIVLGLRKTTLQKVGKEVAELVGRVGEDVSLVLGIMAKLLPLRALPLLFNLIKVVPRVFGRMVGKSREAVAQAMVLEMFREEDYYNDDVLDQMGASILGVEGPRRHPDEPPEDEVFELFPMFMGGLLSAHNRAVLAQLGCPIKNLDALENAQAIKKKLGKLGRQVLPPSELLDHLFFHYEFQNQRFSAEVLSSLRQLNLAGVRMTPVKCTVVAAVLGSGRHALDEVNLASCQLDPAGLRTLLPVFLRARKLGLQLNSLGPEACKDLRDLLLHDQCQITTLRLSNNPLTAAGVAVLMEGLAGNTSVTHLSLLHTGLGDEGLELLAAQLDRNRQLQELNVAYNGAGDTAALALARAAREHPSLELLHLYFNELSSEGRQVLRDLGGAAEGGARVVVSLTEGTAVSEYWSVILSEVQRNLNSWDRARVQRHLELLLRDLEDSRGATLNPWRKAQLLRVEGEVRALLEQLGSSGS	Clinical trial	"Exploratory studies with NX-13: oral toxicity and pharmacokinetics in rodents of an orally active, gut-restricted first-in-class therapeutic for IBD that targets NLRX1. Drug Chem Toxicol. 2022 Jan;45(1):209-214."	.	.	.	.	.	.	.	.	.	.	.	hsa:79671	R-HSA-168928;R-HSA-936440;R-HSA-9758274;	.	Q86UT6;
TTHYDUM	Bombesin receptor (BS)	P28336; P30550; P32247	NMBR_HUMAN; GRPR_HUMAN; BRS3_HUMAN	GPCR rhodopsin	BB	NMBR	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.	.	.	MPSKSLSNLSVTTGANESGSVPEGWERDFLPASDGTTTELVIRCVIPSLYLLIITVGLLGNIMLVKIFITNSAMRSVPNIFISNLAAGDLLLLLTCVPVDASRYFFDEWMFGKVGCKLIPVIQLTSVGVSVFTLTALSADRYRAIVNPMDMQTSGALLRTCVKAMGIWVVSVLLAVPEAVFSEVARISSLDNSSFTACIPYPQTDELHPKIHSVLIFLVYFLIPLAIISIYYYHIAKTLIKSAHNLPGEYNEHTKKQMETRKRLAKIVLVFVGCFIFCWFPNHILYMYRSFNYNEIDPSLGHMIVTLVARVLSFGNSCVNPFALYLLSESFRRHFNSQLCCGRKSYQERGTSYLLSSSAVRMTSLKSNAKNMVTNSVLLNGHSMKQEMAL	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 38).	17	PF00001	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-375276:Peptide ligand-binding receptors; R-HSA-416476:G alpha (q) signalling events	.	P28336
TTDY8JH	Nucleoside diphosphate kinase A (NM23-H1)	P15531	NDKA_HUMAN	Kinase	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	NME1	"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."	EC 2.7.4.6	5UI4; 4ENO; 3L7U; 2HVE; 2HVD	MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAEKEIGLWFHPEELVDYTSCAQNWIYE	Literature-reported	Metastasis suppressor Nm23-H1 inhibits STAT3 signaling via a negative feedback mechanism. Biochem Biophys Res Commun. 2013 May 10;434(3):541-6.	.	EC:2.7	Kinase	NDK family.	2.7.4.6	Transferring phosphorus-containing groups	Nucleoside diphosphate kinase	PF00334	PF00334; NDK	.	.	hsa00230: Purine metabolism; hsa00240: Pyrimidine metabolism; hsa00983: Drug metabolism - other enzymes; hsa01100: Metabolic pathways; hsa01232: Nucleotide metabolism; hsa01240: Biosynthesis of cofactors	R-HSA-499943: Interconversion of nucleotide di- and triphosphates; R-HSA-9748787: Azathioprine ADME	MetaCyc:ENSG00000011052-MON	P15531
TTHSVK0	Thioredoxin-like protein 2b (NME9)	Q86XW9	TXND6_HUMAN	.	Txl-2; Thioredoxin-like protein 2; Thioredoxin domain-containing protein 6; NME9	NME9	May be a regulator of microtubule physiology.	.	.	MGSRKKEIALQVNISTQELWEEMLSSKGLTVVDVYQGWCGPCKPVVSLFQKMRIEVGLDLLHFALAEADRLDVLEKYRGKCEPTFLFYAGGELVAVVRGANAPLLQKTILDQLEAEKKVLAEGRERKVIKDEALSDEDECVSHGKNNGEDEDMVSSERTCTLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRTEGFEDVVTTWRTVMGPRDPNVARREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLFPSLKFSDKDTEAPQGGEAEATAGPTEALCFPEDVD	Literature-reported	Thioredoxin-like protein 2b facilitates colon cancer cell proliferation and inhibits apoptosis via NF-B pathway. Cancer Lett. 2015 Jul 28;363(2):119-26.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	Q86XW9
TTI7T1Q	Neuromedin-U receptor 1 (NMUR1)	Q9HB89	NMUR1_HUMAN	.	NMU-R1; GPR66; G-protein coupled receptor FM-3; G-protein coupled receptor 66	NMUR1	Receptor for the neuromedin-U and neuromedin-S neuropeptides.	.	.	MTPLCLNCSVLPGDLYPGGARNPMACNGSAARGHFDPEDLNLTDEALRLKYLGPQQTELFMPICATYLLIFVVGAVGNGLTCLVILRHKAMRTPTNYYLFSLAVSDLLVLLVGLPLELYEMWHNYPFLLGVGGCYFRTLLFEMVCLASVLNVTALSVERYVAVVHPLQARSMVTRAHVRRVLGAVWGLAMLCSLPNTSLHGIRQLHVPCRGPVPDSAVCMLVRPRALYNMVVQTTALLFFCLPMAIMSVLYLLIGLRLRRERLLLMQEAKGRGSAAARSRYTCRLQQHDRGRRQVTKMLFVLVVVFGICWAPFHADRVMWSVVSQWTDGLHLAFQHVHVISGIFFYLGSAANPVLYSLMSSRFRETFQEALCLGACCHRLRPRHSSHSLSRMTTGSTLCDVGSLGSWVHPLAGNDGPEAQQETDPS	Literature-reported	Discovery of selective hexapeptide agonists to human neuromedin U receptors types 1 and 2. J Med Chem. 2014 Aug 14;57(15):6583-93.	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-416476: G alpha (q) signalling events; R-HSA-418594: G alpha (i) signalling events	.	Q9HB89
TT2L6C5	Neuromedin-U receptor 2 (NMUR2)	Q9GZQ4	NMUR2_HUMAN	.	TGR1; NMU2R; NMU-R2; G-protein coupled receptor TGR-1; G-protein coupled receptor FM-4	NMUR2	Receptor for the neuromedin-U and neuromedin-S neuropeptides.	.	.	MSGMEKLQNASWIYQQKLEDPFQKHLNSTEEYLAFLCGPRRSHFFLPVSVVYVPIFVVGVIGNVLVCLVILQHQAMKTPTNYYLFSLAVSDLLVLLLGMPLEVYEMWRNYPFLFGPVGCYFKTALFETVCFASILSITTVSVERYVAILHPFRAKLQSTRRRALRILGIVWGFSVLFSLPNTSIHGIKFHYFPNGSLVPGSATCTVIKPMWIYNFIIQVTSFLFYLLPMTVISVLYYLMALRLKKDKSLEADEGNANIQRPCRKSVNKMLFVLVLVFAICWAPFHIDRLFFSFVEEWSESLAAVFNLVHVVSGVFFYLSSAVNPIIYNLLSRRFQAAFQNVISSFHKQWHSQHDPQLPPAQRNIFLTECHFVELTEDIGPQFPCQSSMHNSHLPAALSSEQMSRTNYQSFHFNKT	Literature-reported	Discovery and pharmacological characterization of a small-molecule antagonist at neuromedin U receptor NMUR2. J Pharmacol Exp Ther. 2009 Jul;330(1):268-75.	0	.	.	.	.	.	.	.	.	.	.	hsa04080: Neuroactive ligand-receptor interaction	R-HSA-375276: Peptide ligand-binding receptors; R-HSA-416476: G alpha (q) signalling events; R-HSA-418594: G alpha (i) signalling events	.	Q9GZQ4
TTKIH76	Pyridine nucleotide transhydrogenase (NNT)	Q13423	NNTM_HUMAN	.	"Nicotinamide nucleotide transhydrogenase; NAD(P) transhydrogenase, mitochondrial"	NNT	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.	EC 7.1.1.1	1U31; 1PT9; 1DJL	MANLLKTVVTGCSCPLLSNLGSCKGLRVKKDFLRTFYTHQELWCKAPVKPGIPYKQLTVGVPKEIFQNEKRVALSPAGVQNLVKQGFNVVVESGAGEASKFSDDHYRVAGAQIQGAKEVLASDLVVKVRAPMVNPTLGVHEADLLKTSGTLISFIYPAQNPELLNKLSQRKTTVLAMDQVPRVTIAQGYDALSSMANIAGYKAVVLAANHFGRFFTGQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAIVRGFDTRAAALEQFKSLGAEPLEVDLKESGEGQGGYAKEMSKEFIEAEMKLFAQQCKEVDILISTALIPGKKAPVLFNKEMIESMKEGSVVVDLAAEAGGNFETTKPGELYIHKGITHIGYTDLPSRMATQASTLYSNNITKLLKAISPDKDNFYFDVKDDFDFGTMGHVIRGTVVMKDGKVIFPAPTPKNIPQGAPVKQKTVAELEAEKAATITPFRKTMSTASAYTAGLTGILGLGIAAPNLAFSQMVTTFGLAGIVGYHTVWGVTPALHSPLMSVTNAISGLTAVGGLALMGGHLYPSTTSQGLAALAAFISSVNIAGGFLVTQRMLDMFKRPTDPPEYNYLYLLPAGTFVGGYLAALYSGYNIEQIMYLGSGLCCVGALAGLSTQGTARLGNALGMIGVAGGLAATLGVLKPGPELLAQMSGAMALGGTIGLTIAKRIQISDLPQLVAAFHSLVGLAAVLTCIAEYIIEYPHFATDAAANLTKIVAYLGTYIGGVTFSGSLIAYGKLQGLLKSAPLLLPGRHLLNAGLLAASVGGIIPFMVDPSFTTGITCLGSVSALSAVMGVTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNLLTIVGALIGSSGAILSYIMCVAMNRSLANVILGGYGTTSTAGGKPMEISGTHTEINLDNAIDMIREANSIIITPGYGLCAAKAQYPIADLVKMLTEQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDIVLEMDEINHDFPDTDLVLVIGANDTVNSAAQEDPNSIIAGMPVLEVWKSKQVIVMKRSLGVGYAAVDNPIFYKPNTAMLLGDAKKTCDALQAKVRESYQK	Literature-reported	Nicotinamide nucleotide transhydrogenase (Nnt) links the substrate requirement in brain mitochondria for hydrogen peroxide removal to the thioredox... J Biol Chem. 2014 May 30;289(22):15611-20.	.	.	.	.	.	.	.	.	.	.	.	hsa00760: Nicotinate and nicotinamide metabolism; hsa01100: Metabolic pathways	R-HSA-71403: Citric acid cycle (TCA cycle)	MetaCyc:HS03639-MON	Q13423
TTYSRXM	Pattern recognition receptor NOD1 (NOD1)	Q9Y239	NOD1_HUMAN	.	Nucleotide-binding oligomerization domain-containing protein 1; Caspase recruitment domain-containing protein 4; CARD4	NOD1	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.	.	4JQW; 4E9M; 2NZ7; 2NSN; 2DBD	MEEQGHSEMEIIPSESHPHIQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDLRPWLLEIGFSPSLLTQSKVVVNTDPVSRYTQQLRHHLGRDSKFVLCYAQKEELLLEEIYMDTIMELVGFSNESLGSLNSLACLLDHTTGILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESDRLCLQDLLFKHYCYPERDPEEVFAFLLRFPHVALFTFDGLDELHSDLDLSRVPDSSCPWEPAHPLVLLANLLSGKLLKGASKLLTARTGIEVPRQFLRKKVLLRGFSPSHLRAYARRMFPERALQDRLLSQLEANPNLCSLCSVPLFCWIIFRCFQHFRAAFEGSPQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPVETLHAGRDTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELGPGGDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMPPAGAATTSCYPPFLPFQCLQGSGPAREDLFKNKDHFQFTNLFLCGLLSKAKQKLLRHLVPAAALRRKRKALWAHLFSSLRGYLKSLPRVQVESFNQVQAMPTFIWMLRCIYETQSQKVGQLAARGICANYLKLTYCNACSADCSALSFVLHHFPKRLALDLDNNNLNDYGVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLIKPEEAKVYEDEKRIICF	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 1762).	0	.	.	.	.	.	Caspase recruitment domain; Leucine Rich repeat; NACHT domain; NLRC4 helical domain HD2; NOD2 winged helix domain	PF00619; PF13516; PF05729; PF17776; PF17779	PF00619; CARD; PF13516; LRR_6; PF05729; NACHT; PF17776; NLRC4_HD2; PF17779; NOD2_WH	.	.	hsa04621: NOD-like receptor signaling pathway; hsa05120: Epithelial cell signaling in Helicobacter pylori infection; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05133: Pertussis	R-HSA-168638: NOD1/2 Signaling Pathway; R-HSA-445989: TAK1-dependent IKK and NF-kappa-B activation; 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-5689896: Ovarian tumor domain proteases; R-HSA-9020702: Interleukin-1 signaling; R-HSA-9705671: SARS-CoV-2 activates/modulates innate and adaptive immune responses	.	Q9Y239
TTYPUHA	Pattern recognition receptor NOD2 (NOD2)	Q9HC29	NOD2_HUMAN	.	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	NOD2	"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."	.	.	MGEEGGSASHDEEERASVLLGHSPGCEMCSQEAFQAQRSQLVELLVSGSLEGFESVLDWLLSWEVLSWEDYEGFHLLGQPLSHLARRLLDTVWNKGTWACQKLIAAAQEAQADSQSPKLHGCWDPHSLHPARDLQSHRPAIVRRLHSHVENMLDLAWERGFVSQYECDEIRLPIFTPSQRARRLLDLATVKANGLAAFLLQHVQELPVPLALPLEAATCKKYMAKLRTTVSAQSRFLSTYDGAETLCLEDIYTENVLEVWADVGMAGPPQKSPATLGLEELFSTPGHLNDDADTVLVVGEAGSGKSTLLQRLHLLWAAGQDFQEFLFVFPFSCRQLQCMAKPLSVRTLLFEHCCWPDVGQEDIFQLLLDHPDRVLLTFDGFDEFKFRFTDRERHCSPTDPTSVQTLLFNLLQGNLLKNARKVVTSRPAAVSAFLRKYIRTEFNLKGFSEQGIELYLRKRHHEPGVADRLIRLLQETSALHGLCHLPVFSWMVSKCHQELLLQEGGSPKTTTDMYLLILQHFLLHATPPDSASQGLGPSLLRGRLPTLLHLGRLALWGLGMCCYVFSAQQLQAAQVSPDDISLGFLVRAKGVVPGSTAPLEFLHITFQCFFAAFYLALSADVPPALLRHLFNCGRPGNSPMARLLPTMCIQASEGKDSSVAALLQKAEPHNLQITAAFLAGLLSREHWGLLAECQTSEKALLRRQACARWCLARSLRKHFHSIPPAAPGEAKSVHAMPGFIWLIRSLYEMQEERLARKAARGLNVGHLKLTFCSVGPTECAALAFVLQHLRRPVALQLDYNSVGDIGVEQLLPCLGVCKALYLRDNNISDRGICKLIECALHCEQLQKLALFNNKLTDGCAHSMAKLLACRQNFLALRLGNNYITAAGAQVLAEGLRGNTSLQFLGFWGNRVGDEGAQALAEALGDHQSLRWLSLVGNNIGSVGAQALALMLAKNVMLEELCLEENHLQDEGVCSLAEGLKKNSSLKILKLSNNCITYLGAEALLQALERNDTILEVWLRGNTFSLEEVDKLGCRDTRLLL	Clinical trial	DOI: 10.1371/journal.pone.0087712	21	.	.	.	.	.	Caspase recruitment domain; Leucine Rich repeat; NACHT domain; NLRC4 helical domain HD2; NOD2 winged helix domain	PF00619; PF13516; PF05729; PF17776; PF17779	PF00619; CARD; PF13516; LRR_6; PF05729; NACHT; PF17776; NLRC4_HD2; PF17779; NOD2_WH	.	.	hsa04621:NOD-like receptor signaling pathway; hsa04668:TNF signaling pathway; hsa05131:Shigellosis; hsa05152:Tuberculosis; hsa05321:Inflammatory bowel disease (IBD)	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	.	Q9HC29
TTK2O1Q	Nodal homolog (NODAL)	Q96S42	NODAL_HUMAN	Growth factor	nodal growth differentiation factor; HTX5	NODAL	Essential for mesoderm formation and axial patterning during embryonic development.	.	4N1D	MHAHCLPFLLHAWWALLQAGAATVATALLRTRGQPSSPSPLAYMLSLYRDPLPRADIIRSLQAEDVAVDGQNWTFAFDFSFLSQQEDLAWAELRLQLSSPVDLPTEGSLAIEIFHQPKPDTEQASDSCLERFQMDLFTVTLSQVTFSLGSMVLEVTRPLSKWLKHPGALEKQMSRVAGECWPRPPTPPATNVLLMLYSNLSQEQRQLGGSTLLWEAESSWRAQEGQLSWEWGKRHRRHHLPDRSQLCRKVKFQVDFNLIGWGSWIIYPKQYNAYRCEGECPNPVGEEFHPTNHAYIQSLLKRYQPHRVPSTCCAPVKTKPLSMLYVDNGRVLLDHHKDMIVEECGCL	Literature-reported	Elevated expression of Nodal and YAP1 is associated with poor prognosis of gastric adenocarcinoma. J Cancer Res Clin Oncol. 2016 Aug;142(8):1765-73.	.	Growth factor	Transforming growth factor	TGF-beta family.	.	.	Transforming growth factor beta like domain	PF00019	PF00019; TGF_beta	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04350: TGF-beta signaling pathway; hsa04550: Signaling pathways regulating pluripotency of stem cells	R-HSA-1181150: Signaling by NODAL; R-HSA-1433617: Regulation of signaling by NODAL	.	Q96S42
TT95SOA	Interferon alpha (IFNA)	Family	NOUNIPROTAC	.	IFN-A	IFNA	"Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase."	.	.	.	Successful	"Clinical pipeline report, company report or official report of Hemispherx Biopharma."	34	.	.	.	.	.	.	.	.	.	.	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	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	.	.
TTCAQMW	Inosine-5'-monophosphate dehydrogenase (IMPDH)	Family	NOUNIPROTAC	Short-chain dehydrogenases reductase	.	IMPDH	.	.	.	.	Successful	"Mycophenolate mofetil, an inhibitor of inosine monophosphate dehydrogenase, causes a paradoxical elevation of GTP in erythrocytes of renal transplant patients. Clin Sci (Lond). 2004 Jul;107(1):63-8."	34	.	.	.	.	.	.	.	.	.	.	hsa00230:Purine metabolism; hsa00983:Drug metabolism - other enzymes; hsa01100:Metabolic pathways	R-HSA-73817:Purine ribonucleoside monophosphate biosynthesis	.	.
TTMY6L1	Fatty acid-binding protein (FABP)	Family	NOUNIPROTAC	.	Fatty acid binding protein	FABP	.	.	.	.	Patented-recorded	Fatty acid binding protein (FABP) inhibitors: a patent review (2012-2015).Expert Opin Ther Pat. 2016 Jul;26(7):767-76.	15.5	.	Calycin superfamily	.	.	.	.	.	.	.	.	"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"	R-HSA-70263:Gluconeogenesis; R-HSA-70614:Amino acid synthesis and interconversion (transamination)	.	.
TTJSZTB	Nicotinic acetylcholine receptor (nAChR)	Family	NOUNIPROTAC	Ion transport	nAChR; Nicotinergic acetylcholine receptor	nAChR	"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."	.	.	.	Successful	Mecamylamine (Inversine): an old antihypertensive with new research directions. J Hum Hypertens. 2002 Jul;16(7):453-7.	34	.	.	.	.	.	.	.	.	.	.	hsa04080:Neuroactive ligand-receptor interaction	R-HSA-629587:Highly sodium permeable acetylcholine nicotinic receptors; R-HSA-629594:Highly calcium permeable postsynaptic nicotinic acetylcholine receptors	.	.
TTRK8B9	Sodium channel unspecific (NaC)	Family	NOUNIPROTAC	.	.	NaC	"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."	.	.	.	Successful	Lacosamide: a new approach to target voltage-gated sodium currents in epileptic disorders. CNS Drugs. 2009;23(7):555-68. 	34	.	.	.	.	.	.	.	.	.	.	hsa04728:Dopaminergic synapse	R-HSA-445095:Interaction between L1 and Ankyrins	.	.
TTOXS3C	Muscarinic acetylcholine receptor (CHRM)	Family	NOUNIPROTAC	.	.	CHRM	"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."	.	.	.	Successful	Competitive and non-competitive antagonism exhibited by 'selective' antagonists at atrial and ileal muscarinic receptor subtypes. Br J Pharmacol. 1987 Apr;90(4):701-7.	34	.	.	.	.	.	.	.	.	.	.	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	R-HSA-390648:Muscarinic acetylcholine receptors; R-HSA-399997:Acetylcholine regulates insulin secretion; R-HSA-416476:G alpha (q) signalling events	.	.
TTYFKSZ	Tubulin beta (TUBB)	Family	NOUNIPROTAC	Tubulin family	Major cysteine proteinase; Cysteine proteinase cruzipain; Cruzaine; Congopain; Beta-tubulin	TUBB	"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."	.	.	.	Successful	Antiproliferating activity of the mitotic inhibitor pironetin against vindesine- and paclitaxel-resistant human small cell lung cancer H69 cells. Anticancer Res. 2007 Mar-Apr;27(2):729-36.	34	.	.	.	.	.	.	.	.	.	.	hsa04145:Phagosome; hsa04540:Gap junction; hsa05130:Pathogenic Escherichia coli infection	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	.	.
TTE4BSY	Bromodomain and extraterminal domain protein (BET)	Family	NOUNIPROTAC	.	Bromodomain and Extra Terminal protein	BET	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	19	.	.	.	.	.	.	.	.	.	.	hsa04130:SNARE interactions in vesicular transport	R-HSA-204005:COPII (Coat Protein 2) Mediated Vesicle Transport	.	.
TT8KLPT	C-C chemokine receptor (CCR)	Family	NOUNIPROTAC	.	Chemokine (C-C motif) receptor	CCR	"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."	.	.	.	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Target id: 67).	0	.	.	.	.	.	.	.	.	.	.	hsa04060:Cytokine-cytokine receptor interaction; hsa04062:Chemokine signaling pathway	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	.	.
TT9K83W	Tubulin receptor (TUBR)	NO-UNIPROT	NOUNIPROTAC	.	Tubulin protein	TUBR	"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."	.	.	.	Clinical trial	ClinicalTrials.gov (NCT01869933) Phase I Study Assessing the Ocular and Systemic Safety and Tolerability of OC-10X. U.S. National Institutes of Health.	17	.	Tubulin family	.	.	.	.	.	.	.	.	hsa04145:Phagosome; hsa04540:Gap junction; hsa05130:Pathogenic Escherichia coli infection	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	.	.
TTRPDBG	Inhibitor of nuclear factor kappa-B kinase (IKK)	Family	NOUNIPROTAC	.	IB kinase; IkappaB kinase; IKK	IKK	"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."	.	.	.	Patented-recorded	Novel NF-B inhibitors: a patent review (2011 - 2014).Expert Opin Ther Pat. 2015 Mar;25(3):319-34.	15.5	.	Protein kinase superfamily. Ser/Thr protein kinase family	.	.	.	.	.	.	.	.	.	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	.	.
TTAJU0S	Interleukin 2 receptor (IL2R)	Family	NOUNIPROTAC	Cytokine receptor	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	IL2R	"Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15. Common subunit for the receptors for a variety of interleukins."	.	.	.	Successful	Optimizing denileukin diftitox (Ontak) therapy. Future Oncol. 2008 Aug;4(4):457-69.	34	Cytokine receptor	.	type I cytokine receptor family. Type 5 subfamily.	.	.	"Interleukin-6 receptor alpha chain, binding"	PF09240	PF09240; IL6Ra-bind	.	.	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	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	.	.
TTROQ37	MAPK/ERK kinase kinase (MAP3K)	Family	NOUNIPROTAC	Kinase	.	MAP3K	"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."	.	.	.	Successful	Radium 223 dichloride for prostate cancer treatment. Drug Des Devel Ther. 2017 Sep 6;11:2643-2651.	34	.	.	.	.	.	.	.	.	.	.	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	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	.	.
TTDP1UC	Fatty acid amide hydrolase (FAAH)	Family	NOUNIPROTAC	.	Oleamidehydrolase; Anandamide amidohydrolase	FAAH	"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."	.	.	.	Successful	The general anesthetic propofol increases brain N-arachidonylethanolamine (anandamide) content and inhibits fatty acid amide hydrolase. Br J Pharmacol. 2003 Jul;139(5):1005-13.	34	.	Carbon nitrogen hydrolase	.	.	.	.	.	.	.	.	hsa04723:Retrograde endocannabinoid signaling	.	.	.
TTUBJQ3	Neural cell adhesion molecule (NCAM)	Family	NOUNIPROTAC	Immunoglobulin	.	NCAM	.	.	.	.	Clinical trial	"Lorvotuzumab mertansine, a CD56-targeting antibody-drug conjugate with potent antitumor activity against small cell lung cancer in human xenograft models. MAbs. 2014 Mar-Apr;6(2):556-66."	21	.	.	.	.	.	.	.	.	.	.	hsa04514:Cell adhesion molecules (CAMs); hsa05020:Prion diseases	.	.	.
TTQ29KF	Voltage-gated potassium channel Kv7 (KCNQ)	Family	NOUNIPROTAC	Voltage-gated ion channel	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	KCNQ	.	.	.	.	Clinical trial	The Kv7 potassium channel activator flupirtine affects clinical excitability parameters of myelinated axons in isolated rat sural nerve. J Peripher Nerv Syst. 2010 Mar;15(1):63-72.	21	.	.	.	.	.	.	.	.	.	.	hsa04261:Adrenergic signaling in cardiomyocytes; hsa04725:Cholinergic synapse; hsa04971:Gastric acid secretion; hsa04972:Pancreatic secretion; hsa04974:Protein digestion and absorption; hsa05110:Vibrio cholerae infection	.	.	.
TTFQVUT	NADPH oxidase (NOX)	Family	NOUNIPROTAC	.	.	NOX	"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."	.	.	.	Clinical trial	Nicotinamide Adenine Dinucleotide Phosphate Oxidase (NOX) in Experimental Liver Fibrosis: GKT137831 as a Novel Potential Therapeutic Agent. Hepatology. 2012 December; 56(6): 2316-2327.	21	.	.	.	.	.	.	.	.	.	.	hsa04066:HIF-1 signaling pathway; hsa04145:Phagosome; hsa04380:Osteoclast differentiation; hsa04670:Leukocyte transendothelial migration	.	.	.
TT70SZ3	Sodium/hydrogen exchanger (SLC)	Family	NOUNIPROTAC	.	.	SLC	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.	.	.	.	Literature-reported	"Protective effect of FR183998, a Na+/H+ exchanger inhibitor, and its inhibition of iNOS induction in hepatic ischemia-reperfusion injury in rats. Shock. 2008 Sep;30(3):311-7."	2	.	.	.	.	.	.	.	.	.	.	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	.	.	.
TTU593I	Neurokinin receptor (NKR)	Family	NOUNIPROTAC	.	.	NKR	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.	.	.	.	Literature-reported	"US patent application no. 2008,0039,404, Bifunctional analgesic compounds for opioid receptor agonists and neurokinin-1 receptor antagonists."	2	.	.	.	.	.	.	.	.	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa05162:Measles	.	.	.
TTYSN63	5-HT 2 receptor (5HT2R)	Family	NOUNIPROTAC	GPCR rhodopsin	Serotonin receptor 2; 5-hydroxytryptamine receptor 2; 5-HT2 receptor	5HT2R	"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."	.	.	.	Successful	Pharmacological effects of zotepine and other antipsychotics on the central 5-HT2 receptors. Pharmacopsychiatry. 1993 Mar;26(2):53-8.	34	PF00001	.	.	.	.	.	.	.	.	.	hsa04020:Calcium signaling pathway; hsa04080:Neuroactive ligand-receptor interaction; hsa04540:Gap junction; hsa04726:Serotonergic synapse; hsa04750:Inflammatory mediator regulation of TRP channels	.	.	.
TTGN1ZA	Angiotensin II receptor (AGTR)	Family	NOUNIPROTAC	.	.	AGTR	Receptor for angiotensin II. Mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system.	.	.	.	Clinical trial	"CYT-006-AngQb, a vaccine against angiotensin II for the potential treatment of hypertension. Curr Opin Investig Drugs. 2009 Mar;10(3):269-75."	21	.	.	.	.	.	.	.	.	.	.	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	.	.	.
TTVJ1D8	Vascular endothelial growth factor receptor (VEGFR)	Family	NOUNIPROTAC	Kinase	.	VEGFR	.	.	.	.	Successful	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	34	.	.	.	.	.	.	.	.	.	.	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	.	.	.
TTKIAM5	NF-kappa-B messenger RNA (NFKB mRNA)	Family	NOUNIPROTAC	mRNA target	mRNA of NF-kappaB; NF-kappaB mRNA	NFKB mRNA	"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."	.	.	.	Clinical trial	Antisense oligonucleotide therapy for urologic tumors. Curr Urol Rep. 2003 Feb;4(1):60-9.	25	mRNA	.	.	.	.	.	.	.	.	.	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)	.	.	.
TT1APCZ	Phosphodiesterase 7 (PDE7)	Q13946; Q9NP56	PDE7A_HUMAN; PDE7B_HUMAN	.	.	PDE7	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of Omeros."	.	.	.	.	.	.	.	.	.	.	.	hsa00230: Purine metabolism; hsa01100: Metabolic pathways; hsa05032: Morphine addiction	R-HSA-418555: G alpha (s) signalling events	.	Q13946
TTRMIZ7	Peroxisome proliferator-activated receptor (PPAR)	Q07869; Q03181; P37231	PPARA_HUMAN; PPARD_HUMAN; PPARG_HUMAN	.	.	PPAR	.	.	.	.	Clinical trial	Pan-PPAR agonist IVA337 is effective in experimental lung fibrosis and pulmonary hypertension. Ann Rheum Dis. 2017 Nov;76(11):1931-1940.	.	.	.	.	.	.	.	.	.	.	.	hsa03320: PPAR signaling pathway; hsa04024: cAMP signaling pathway; hsa04920: Adipocytokine signaling pathway; hsa04922: Glucagon signaling pathway; hsa04931: Insulin resistance; hsa04932: Non-alcoholic fatty liver disease; hsa04936: Alcoholic liver disease; hsa05160: Hepatitis C; hsa05207: Chemical carcinogenesis - receptor activation; hsa05415: Diabetic cardiomyopathy	"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-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 PPARalpha; R-HSA-400253: Circadian Clock; R-HSA-4090294: SUMOylation of intracellular receptors; R-HSA-9707564: Cytoprotection by HMOX1; R-HSA-9707616: Heme signaling"	.	Q07869
TT34ECM	Cell cycle (CC)	Pathway/Process	NOUNIPROTAC	.	.	CC	.	.	.	.	Clinical trial	"BZL101, a phytochemical extract from the Scutellaria barbata plant, disrupts proliferation of human breast and prostate cancer cells through distinct mechanisms dependent on the cancer cell phenotype. Cancer Biol Ther. 2010 Aug 15;10(4):397-405."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZJD1B	Acetylcholine release (Ach rele)	Pathway/Process	NOUNIPROTAC	.	.	Ach rele	.	.	.	.	Successful	Mullard A: 2010 FDA drug approvals. Nat Rev Drug Discov. 2011 Feb;10(2):82-5.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTD3BVN	Axon loss (AXL)	Pathway/Process	NOUNIPROTAC	.	.	AXL	.	.	.	.	Literature-reported	Axon pathology in neurological disease: a neglected therapeutic target. Trends Neurosci. 2002 Oct;25(10):532-7.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQ2GJ0	Plasmodial phospholipid metabolism (PPP metab)	Pathway/Process	NOUNIPROTAC	.	.	PPP metab	.	.	.	.	Clinical trial	"Transport and pharmacodynamics of albitiazolium, an antimalarial drug candidate. Br J Pharmacol. 2012 August; 166(8): 2263-2276."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMDQIJ	Oxalate absorption (Oxalate absor)	Pathway/Process	NOUNIPROTAC	.	.	Oxalate absor	.	.	.	.	Clinical trial	Hyperoxaluria: a gut-kidney axis. Kidney Int. 2011 Dec;80(11):1146-58.	3	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMPGNS	Leukotriene biosynthesis (LT synth)	Pathway/Process	NOUNIPROTAC	.	Leukotriene synthesis	LT synth	.	.	.	.	Literature-reported	Regulation of leukotriene biosynthesis. Cancer Metastasis Rev. 1994 Dec;13(3-4):257-67.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXKQIV	Energy metabolism (Energy metab)	Pathway/Process	NOUNIPROTAC	.	.	Energy metab	.	.	.	.	Literature-reported	Hepatic Control of Energy Metabolism via the Autonomic Nervous System. J Atheroscler Thromb. 2017 Jan 1;24(1):14-18.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTEWNM1	IL-1 synthesis/release (IL-1 synth/rele)	Pathway/Process	NOUNIPROTAC	.	.	IL-1 synth/rele	.	.	.	.	Clinical trial	Effects of flezelastine and its enantiomers on LPS-induced IL-1 beta generation in vitro and LPS-induced pyrexia in vivo. Agents Actions. 1994 Mar;41(1-2):99-100.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNHYJL	Ketogenesis (KG)	Pathway/Process	NOUNIPROTAC	.	.	KG	.	.	.	.	Clinical trial	"Study of the ketogenic agent AC-1202 in mild to moderate Alzheimer's disease: a randomized, double-blind, placebo-controlled, multicenter trial. Nutr Metab (Lond). 2009 Aug 10;6:31."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMCA52	Viral Maturation (VM)	Pathway/Process	NOUNIPROTAC	.	.	VM	.	.	.	.	Clinical trial	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800037762)"	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3BLGR	STAT3-Beta-catenin pathway (SBC pathway)	Pathway/Process	NOUNIPROTAC	.	.	SBC pathway	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTTD45S	Neurotransmitter release (NT rele)	Pathway/Process	NOUNIPROTAC	.	.	NT rele	.	.	.	.	Clinical trial	"Effects of an indene-derivative, TN-871, on synaptic transmission in a sympathetic ganglion: presynaptic actions on neurotransmitter release. Bull Tokyo Med Dent Univ. 1995 Mar;42(1):19-29."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT7KY5U	Histamine/peptide leukotriene release (His/p-LT rele)	Pathway/Process	NOUNIPROTAC	.	.	His/p-LT rele	.	.	.	.	Clinical trial	"Effects of quinotolast, a new orally active antiallergic drug, on experimental allergic models. Jpn J Pharmacol. 1993 Sep;63(1):73-81."	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT01UPE	Cytomegalovirus Replication (CMV replication)	Pathway/Process	NOUNIPROTAC	.	.	CMV replication	.	.	.	.	Discontinued	A Systematic Screen for CDK4/6 Substrates Links FOXM1 Phosphorylation to Senescence Suppression in Cancer Cells. Cancer Cell. 2011 November 15; 20(5): 620-634.	5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTRA79S	Cholesterol synthesis (Chole synth)	Pathway/Process	NOUNIPROTAC	.	.	Chole synth	.	.	.	.	Successful	"Clinical pipeline report, company report or official report of Esperion Therapeutics."	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXLO8T	Potential penetration (PP)	Pathway/Process	NOUNIPROTAC	.	.	PP	.	.	.	.	Literature-reported	"Effectiveness of pirotiodecane, absorption enhancer, on nasal absorption in rabbits. Drug Metab Pharmacokinet. 2005 Feb;20(1):65-71."	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTV0YFR	Lipid peroxidation (LPO)	Pathway/Process	NOUNIPROTAC	.	.	LPO	.	.	.	.	Clinical trial	"A neuroprotective agent, T-817MA (1-{3-[2-(1-benzothiophen-5-yl)ethoxy]propyl} azetidin-3-ol maleate), prevents 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced neurotoxicity in mice. Neuropharmacology. 2008 Oct;55(5):654-60."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTC3JYS	TNF alpha synthesis (TNFA synthesis)	Pathway/Process	NOUNIPROTAC	.	Tumor necrosis factor alpha synthesis	TNFA synthesis	.	.	.	.	Literature-reported	Tumor necrosis factor alpha polymorphisms are associated with Parkinson's disease age at onset. Neurosci Lett. 2017 Sep 29;658:133-136.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTABD5E	DNA replication (DNA repli)	Pathway/Process	NOUNIPROTAC	.	.	DNA repli	.	.	.	.	Successful	2017 FDA drug approvals.Nat Rev Drug Discov. 2018 Feb;17(2):81-85. 	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTTPKA5	Thyroid hormone synthesis (TH synth)	Pathway/Process	NOUNIPROTAC	.	.	TH synth	.	.	.	.	Literature-reported	Thyroid hormone synthesis: a potential target of a Chinese herbal formula Haizao Yuhu Decoction acting on iodine-deficient goiter. Oncotarget. 2016 Aug 9;7(32):51699-51712.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTV8N19	Immune checkpoint (ICH)	Pathway/Process	NOUNIPROTAC	.	.	ICH	.	.	.	.	Clinical trial	Deal watch: Genentech dives deeper into the next wave of cancer immunotherapies. Nat Rev Drug Discov. 2014 Dec;13(12):879.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTPVYKI	Signal transduction unspecific (ST)	Pathway/Process	NOUNIPROTAC	.	.	ST	.	.	.	.	Clinical trial	"Enhanced anticancer activity of a combination of docetaxel and Aneustat (OMN54) in a patient-derived, advanced prostate cancer tissue xenograft model. Mol Oncol. 2014 Mar;8(2):311-22."	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTU8Q3Y	Plasmodium Gametocytogenesis (Plasm Gamet)	Pathway/Process	NOUNIPROTAC	.	.	Plasm Gamet	.	.	.	.	Literature-reported	Initiation of gametocytogenesis at very low parasite density in Plasmodium falciparum infection. J Infect Dis. 2017 Apr 1;215(7):1167-1174.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT470F3	TNF alpha production (TNFA produ)	Pathway/Process	NOUNIPROTAC	.	Tumor necrosis factor alpha production	TNFA produ	.	.	.	.	Clinical trial	Particulate beta-glucan induces TNF-alpha production in wound macrophages via a redox-sensitive NF- beta-dependent pathway. Wound Repair Regen. 2011 May-Jun;19(3):411-9.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUPO71	Mast cell degranulation pathway (MCD pathway)	Pathway/Process	NOUNIPROTAC	.	.	MCD pathway	.	.	.	.	Literature-reported	Mast cell stabilisers. Eur J Pharmacol. 2016 May 5;778:158-68.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOV74C	Bone metabolism (Bone metab)	Pathway/Process	NOUNIPROTAC	.	.	Bone metab	.	.	.	.	Discontinued	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800030958)"	5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT63CB1	Food intake (FI)	Pathway/Process	NOUNIPROTAC	.	.	FI	.	.	.	.	Discontinued	Analysis of the anorectic efficacy of HMR1426 in rodents and its effects on gastric emptying in rats. Int J Obes Relat Metab Disord. 2004 Feb;28(2):211-21.	5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT40BO8	Late inward sodium current (LISC)	Pathway/Process	NOUNIPROTAC	.	.	LISC	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of Gilead."	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTDIBYJ	Angiogenesis/myeloma cell growth (AMCG)	Pathway/Process	NOUNIPROTAC	.	.	AMCG	.	.	.	.	Successful	Radium 223 dichloride for prostate cancer treatment. Drug Des Devel Ther. 2017 Sep 6;11:2643-2651.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTSTYLU	Growth hormone secretion (GH secr)	Pathway/Process	NOUNIPROTAC	.	.	GH secr	.	.	.	.	Clinical trial	"Growth hormone response in man to L-692,429, a novel nonpeptide mimic of growth hormone-releasing peptide-6. J Clin Endocrinol Metab. 1993 Nov;77(5):1393-7."	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTV9MQG	Gamma-aminobutyric acid uptake (GABAU)	Pathway/Process	NOUNIPROTAC	.	GABA uptake	GABAU	.	.	.	.	Successful	Glutamate- and GABA-based CNS therapeutics. Curr Opin Pharmacol. 2006 Feb;6(1):7-17.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUBNVO	DNA synthesis (DNA synth)	Pathway/Process	NOUNIPROTAC	.	.	DNA synth	.	.	.	.	Successful	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT1AVS7	Second phase insulin secretion (SPI secr)	Pathway/Process	NOUNIPROTAC	.	.	SPI secr	.	.	.	.	Clinical trial	"AGI-1067, a novel antioxidant and anti-inflammatory agent, enhances insulin release and protects mouse islets. Mol Cell Endocrinol. 2010 Jul 29;323(2):246-55."	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT20DOQ	Hydroxy radical elimination (HYRE)	Pathway/Process	NOUNIPROTAC	.	.	HYRE	.	.	.	.	Clinical trial	"Creatinine and HMH (5-hydroxy-1-methylhydantoin, NZ-419) as intrinsic hydroxyl radical scavengers. Drug Discov Ther. 2011 Aug;5(4):162-75."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTC0BEN	Oxidative stress (OS)	Pathway/Process	NOUNIPROTAC	.	.	OS	.	.	.	.	Clinical trial	"Protective effect of SUN N8075, a free radical scavenger, against excessive light-induced retinal damage in mice. Biol Pharm Bull. 2014;37(3):424-30."	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZ1DV7	Mitochondrial function (MF)	Pathway/Process	NOUNIPROTAC	.	.	MF	.	.	.	.	Clinical trial	The therapeutic role of creatine in Huntington's disease. Pharmacol Ther. 2005 Nov;108(2):193-207.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT7KPH1	MAPK/ERK signaling pathway (MAPK pathway)	Pathway/Process	NOUNIPROTAC	.	.	MAPK pathway	.	.	.	.	Clinical trial	"US patent application no. 2006,0270,742, Compositions and methods for the treatment of neurodegenerative diseases."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2QPV9	Aryl hydrocarbon receptor signaling pathway (AhR pathway)	Pathway/Process	NOUNIPROTAC	.	.	AhR pathway	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of AFP464."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTEI6SF	IKB-beta-NFKB signaling pathway (IKBB-NFKB pathway)	Pathway/Process	NOUNIPROTAC	.	.	IKBB-NFKB pathway	.	.	.	.	Literature-reported	Inhibiting IB-NFB signaling attenuates the expression of select pro-inflammatory genes. J Cell Sci. 2015 Jun 1;128(11):2143-55.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8G3Z7	Serotoninnorepinephrinedopamine reuptake (SNDR)	Pathway/Process	NOUNIPROTAC	.	.	SNDR	.	.	.	.	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. 2015	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT4IN7L	Histamine release (His rele)	Pathway/Process	NOUNIPROTAC	.	.	His rele	.	.	.	.	Clinical trial	Cytoprotective effects of CI-959 in the rat gastric mucosa: modulation of leukocyte adhesion. Gastroenterology. 1995 Oct;109(4):1224-33.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT0QZ8R	cAMP formation (cAMP form)	Pathway/Process	NOUNIPROTAC	.	.	cAMP form	.	.	.	.	Clinical trial	"ucb 11056, a new potential nootropic drug, amplifies induced cyclic AMP formation in rat brain tissue. J Neurochem. 1993 Dec;61(6):2256-61."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTB8Y9K	Angiogenesis (AGG)	Pathway/Process	NOUNIPROTAC	.	.	AGG	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTLK6DR	Cyclin D1 synthesis (CCND1 synthesis)	Pathway/Process	NOUNIPROTAC	.	Cyclin D1 biosynthesis	CCND1 synthesis	.	.	.	.	Clinical trial	Reduction of heat-induced haemotoxicity in a hyperthermic purging protocol of murine acute myeloid leukaemic stem cells by AcSDKP. Br J Haematol. 1997 Dec;99(3):692-8.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTX1JEN	JNK signaling pathway (JNK pathway)	Pathway/Process	NOUNIPROTAC	.	.	JNK pathway	.	.	.	.	Clinical trial	"US patent application no. 2006,0270,742, Compositions and methods for the treatment of neurodegenerative diseases."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTC4QIX	Pro-inflammatory autologous messenger (PAM)	Pathway/Process	NOUNIPROTAC	.	.	PAM	.	.	.	.	Literature-reported	Oxidative induction of pro-inflammatory cytokine formation by human monocyte-derived macrophages following exposure to manganese in vitro. J Immunotoxicol. 2015 Jan-Mar;12(1):98-103.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT0AD7X	Bacterial Quorum sensing (Bact BQS)	Pathway/Process	NOUNIPROTAC	.	.	Bact BQS	.	.	.	.	Literature-reported	Mathematical Modelling of Bacterial Quorum Sensing: A Review. Bull Math Biol. 2016 Aug;78(8):1585-639.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT26HJ8	Eosinophil/lymphocyte-rich accumulation (ELR accum)	Pathway/Process	NOUNIPROTAC	.	.	ELR accum	.	.	.	.	Clinical trial	"Preclinical evaluation of anti-inflammatory activities of the novel pyrrolopyrimidine PNU-142731A, a potential treatment for asthma. J Pharmacol Exp Ther. 1999 Jul;290(1):188-95."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJ6ESR	Catecholamine uptake (CA uptake)	Pathway/Process	NOUNIPROTAC	.	.	CA uptake	.	.	.	.	Literature-reported	Catecholamine uptake blockade in anaesthetized dogs: influence on cardiovascular responses. J Pharm Pharmacol. 1979 Nov;31(11):761-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3KL5X	Ubiquitin-proteasome pathway (UP pathway)	Pathway/Process	NOUNIPROTAC	.	.	UP pathway	.	.	.	.	Literature-reported	Second generation proteasome inhibitors: carfilzomib and immunoproteasome-specific inhibitors (IPSIs). Curr Cancer Drug Targets. 2011 Mar;11(3):285-95.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTBC12P	Sonic hedgehog pathway (Shh pathway)	Pathway/Process	NOUNIPROTAC	.	.	Shh pathway	.	.	.	.	Literature-reported	Sonic hedgehog signalling pathway: a complex network. Ann Neurosci. 2014 Jan;21(1):28-31.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZ7WFL	Glucose metabolism (Glucose metab)	Pathway/Process	NOUNIPROTAC	.	.	Glucose metab	.	.	.	.	Clinical trial	"Herbal constituent sequoyitol improves hyperglycemia and glucose intolerance by targeting hepatocytes, adipocytes, and beta-cells. Am J Physiol Endocrinol Metab. 2012 April 15; 302(8): E932-E940."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT4EWFY	TNF/IL-10 release (TNF/IL10 rele)	Pathway/Process	NOUNIPROTAC	.	.	TNF/IL10 rele	.	.	.	.	Clinical trial	"PCT-233, a novel modulator of pro- and anti-inflammatory cytokine production. Clin Exp Immunol. 2004 Mar;135(3):440-7."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYIJX1	Autophagy (AUT)	Pathway/Process	NOUNIPROTAC	.	.	AUT	.	.	.	.	Literature-reported	Targeting autophagy in cancer. Nat Rev Cancer. 2017 Sep;17(9):528-542.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNRF4L	Histone synthesis (Histone synth)	Pathway/Process	NOUNIPROTAC	.	.	Histone synth	.	.	.	.	Discontinued	Immunostimulatory action of L-4-oxalysine counteracts immunosuppression induced by alpha-fetoprotein. Eur J Pharmacol. 1998 Jun 12;351(1):105-11.	5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTVX670	Protein translation (hPT)	Pathway/Process	NOUNIPROTAC	.	.	hPT	.	.	.	.	Literature-reported	Translation Initiation Factors: Reprogramming Protein Synthesis in Cancer. Trends Cell Biol. 2016 Dec;26(12):918-933.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2VX74	Bacterial Protein synthesis (Bact PROS)	Pathway/Process	NOUNIPROTAC	.	.	Bact PROS	.	.	.	.	Clinical trial	"Cellular pharmacodynamics of the novel biaryloxazolidinone radezolid: studies with infected phagocytic and nonphagocytic cells, using Staphylococcus aureus, Staphylococcus epidermidis, Listeria monocytogenes, and Legionella pneumophila. Antimicrob Agents Chemother. 2010 Jun;54(6):2549-59."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYNBIE	Hepatic oligosaccharide/glycolipid storage (HOGS)	Pathway/Process	NOUNIPROTAC	.	.	HOGS	.	.	.	.	Literature-reported	Hepatic storage of oligosaccharides and glycolipids in a cat affected with GM1 gangliosidosis. Biochem J. 1978 Dec 1;175(3):945-53.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTBD054	Inflammation pathogenesis (IP)	Pathway/Process	NOUNIPROTAC	.	.	IP	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of Hutchison Medi Pharma."	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTFPSHI	Wnt signaling pathway (Wnt pathway)	Pathway/Process	NOUNIPROTAC	.	.	Wnt pathway	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT14TBN	Cyclin E/cdk2 pathway (CCNE2/CDK2 pathway)	Pathway/Process	NOUNIPROTAC	.	Cyclin E/CDK2 pathway signalling	CCNE2/CDK2 pathway	.	.	.	.	Literature-reported	Expression of cyclin E in resting and activated B-chronic lymphocytic leukaemia cells: cyclin E/cdk2 as a potential therapeutic target. Br J Haematol. 2004 Apr;125(2):141-8.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTSI7BV	Glycolysis (GLYS)	Pathway/Process	NOUNIPROTAC	.	.	GLYS	.	.	.	.	Literature-reported	Glycolysis inhibition as a cancer treatment and its role in an anti-tumour immune response. Biochim Biophys Acta. 2016 Aug;1866(1):87-105.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZGF8B	Tau protein aggregation (TauA)	Pathway/Process	NOUNIPROTAC	.	.	TauA	.	.	.	.	Clinical trial	Successes and Failures for Drugs in Late-Stage Development for Alzheimer's Disease. Correction in: volume 31 on page 81.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNA5ZS	Cholesterol absorption (Chole absorp)	Pathway/Process	NOUNIPROTAC	.	.	Chole absorp	.	.	.	.	Clinical trial	Intestinal and Hepatic Niemann-Pick C1-Like 1. Correction in: Diabetes Metab J. 2013 December; 37(6): 486-487.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTSB7ZR	Trigeminal ganglion stimulation-induced response (TGSR)	Pathway/Process	NOUNIPROTAC	.	.	TGSR	.	.	.	.	Clinical trial	Tonabersat (SB-220453) a novel benzopyran with anticonvulsant properties attenuates trigeminal nerve-induced neurovascular reflexes. Br J Pharmacol. 2001 April; 132(7): 1549-1557.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3J5ZI	Cell mediated immunity response (CMIR)	Pathway/Process	NOUNIPROTAC	.	.	CMIR	.	.	.	.	Successful	Flu myths: dispelling the myths associated with live attenuated influenza vaccine. Mayo Clin Proc. 2008 Jan;83(1):77-84.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTEWTCR	Adenine synthesis (Adeni synth)	Pathway/Process	NOUNIPROTAC	.	.	Adeni synth	.	.	.	.	Clinical trial	Circadian pharmacology of L-alanosine (SDX-102) in mice. Mol Cancer Ther. 2006 Feb;5(2):337-46.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT0DWYQ	Tumour metastasis (Tmet)	Pathway/Process	NOUNIPROTAC	.	Metastasis; Cancer metastasis	Tmet	.	.	.	.	Literature-reported	Molecular insights into tumour metastasis: tracing the dominant events. J Pathol. 2017 Apr;241(5):567-577.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTE6DMK	Ligand-nuclear hormone receptor interaction (LNHRI)	Pathway/Process	NOUNIPROTAC	.	.	LNHRI	.	.	.	.	Literature-reported	"Rapid, portable detection of endocrine disrupting chemicals through ligand-nuclear hormone receptor interactions. Analyst. 2017 Dec 4;142(24):4595-4600."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTV4B1Y	Src tyrosine kinase signaling pathway (Src pathway)	Pathway/Process	NOUNIPROTAC	.	.	Src pathway	.	.	.	.	Literature-reported	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Ligand id: 7957).	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHQGFL	PMN apoptosis and chemotaxis (PMNAC)	Pathway/Process	NOUNIPROTAC	.	.	PMNAC	.	.	.	.	Clinical trial	Attenuation of interleukin 8-induced nasal inflammation by an inhibitor peptide. Am J Respir Crit Care Med. 2001 Apr;163(5):1198-205.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUO9SZ	Nitric oxide elimination (NOE)	Pathway/Process	NOUNIPROTAC	.	.	NOE	.	.	.	.	Clinical trial	"Inhibition of nitrosylation, nitration, lymphocyte proliferation, and gene expression in acute and delayed cardiac allograft rejection by an orally active dithiocarbamate. J Cardiovasc Pharmacol. 2004 Apr;43(4):522-30."	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTX2AYW	RNA synthesis (hRNA synth)	Pathway/Process	NOUNIPROTAC	.	.	hRNA synth	.	.	.	.	Successful	Role of magnesium ion in mithramycin-DNA interaction: binding of mithramycin-Mg2+ complexes with DNA. Biochemistry. 1995 Jan 31;34(4):1376-85.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTD2MLN	Natural killer cell activation (NKA)	Pathway/Process	NOUNIPROTAC	.	.	NKA	.	.	.	.	Successful	"Virulizin, a novel immunotherapy agent, activates NK cells through induction of IL-12 expression in macrophages. Cancer Immunol Immunother. 2005 Nov;54(11):1115-26."	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT61VTP	Cholesterol uptake (Chole uptake)	Pathway/Process	NOUNIPROTAC	.	.	Chole uptake	.	.	.	.	Clinical trial	"Comparison of synthetic saponin cholesterol absorption inhibitors in rabbits: evidence for a non-stoichiometric, intestinal mechanism of action. J Lipid Res. 1999 Mar;40(3):464-74."	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTAXYDF	TLR signaling pathway (TLR pathway)	Pathway/Process	NOUNIPROTAC	.	.	TLR pathway	.	.	.	.	Literature-reported	TLR signaling in B-cell development and activation. Cell Mol Immunol. 2013 Mar;10(2):103-6.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJXYQ6	Monoamine uptake (MA uptake)	Pathway/Process	NOUNIPROTAC	.	Monoamine(MA) uptake	MA uptake	.	.	.	.	Literature-reported	"The antidepressant agents desipramine, fluoxetine, fluvoxamine and norzimelidine inhibit uptake of [3H]noradrenaline and [3H]5-hydroxytryptamine in slices of human and rat cortical brain tissue. Brain Res. 1983 Sep 19;275(1):99-104."	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT4LXBC	Hedgehog signaling pathway (HS pathway)	Pathway/Process	NOUNIPROTAC	.	.	HS pathway	.	.	.	.	Successful	2018 FDA drug approvals.Nat Rev Drug Discov. 2019 Feb;18(2):85-89. 	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTS3GIJ	Heterotrimeric G-protein signaling pathway (HGP pathway)	Pathway/Process	NOUNIPROTAC	.	.	HGP pathway	.	.	.	.	Literature-reported	Inhibition of heterotrimeric G protein signaling by a small molecule acting on Galpha subunit. J Biol Chem. 2009 Oct 16;284(42):29136-45.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTKAWRQ	JAK-STAT signaling pathway (JAK-STAT pathway)	Pathway/Process	NOUNIPROTAC	.	.	JAK-STAT pathway	.	.	.	.	Clinical trial	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Ligand id: 7972).	19	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXL3MF	Lymphoid cell adhesion molecule expression (LCDME)	Pathway/Process	NOUNIPROTAC	.	.	LCDME	.	.	.	.	Successful	Anapsos (Polypodium leucotomos) modulates lymphoid cells and the expression of adhesion molecules. Pharmacol Res. 2002 Aug;46(2):185-90.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTGD6BY	TNF-alpha/IL-1 beta production (TNFA/IL1B produ)	Pathway/Process	NOUNIPROTAC	.	.	TNFA/IL1B produ	.	.	.	.	Clinical trial	"KE-758, an active metabolite of the new anti-rheumatic drug KE-298, suppresses production of tumor necrosis factor-alpha and interleukin-1 beta in THP-1, a human monocyte cell line. Drugs Exp Clin Res. 2002;28(5):197-205."	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTE5Q4N	VWF-dependent platelet-collagen conversion (VDDPCC)	Pathway/Process	NOUNIPROTAC	.	.	VDDPCC	.	.	.	.	Clinical trial	Antithrombotic effects of saratin on human atherosclerotic plaques. Thromb Haemost. 2004 Jul;92(1):191-200.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTGPK5Y	T(H2) cytokine production (TH2 produ)	Pathway/Process	NOUNIPROTAC	.	.	TH2 produ	.	.	.	.	Successful	Suplatast tosilate inhibits goblet-cell metaplasia of airway epithelium in sensitized mice. J Allergy Clin Immunol. 2000 Apr;105(4):739-45.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXT2VN	NF-kappa-B-p38 signaling pathway (NFKB-p38 pathway)	Pathway/Process	NOUNIPROTAC	.	.	NFKB-p38 pathway	.	.	.	.	Clinical trial	"Effects of the immunomodulator, VGX-1027, in endotoxin-induced uveitis in Lewis rats. Br J Pharmacol. 2008 Nov;155(5):722-30."	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTU5CF1	Actin polymerization (Actin poly)	Pathway/Process	NOUNIPROTAC	.	.	Actin poly	.	.	.	.	Clinical trial	Chronic hypoxia differentially up-regulates protein kinase C-mediated ovine uterine arterial contraction via actin polymerization signaling in pregnancy. Biol Reprod. 2012 Dec 21;87(6):142.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTW6MKR	Calcium release (Ca rele)	Pathway/Process	NOUNIPROTAC	.	.	Ca rele	.	.	.	.	Clinical trial	"NPC-15199, a novel anti-inflammatory agent, mobilizes intracellular Ca2+ in bladder female transitional carcinoma (BFTC) cells. Chin J Physiol. 2000 Mar 31;43(1):29-33."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT438XZ	Cyclin D1/E2F pathway (CCND1/E2F pathway)	Pathway/Process	NOUNIPROTAC	.	Cyclin D1/E2F pathway signalling	CCND1/E2F pathway	.	.	.	.	Discontinued	"Inhibition of the cyclin D1/E2F pathway by PCA-4230, a potent repressor of cellular proliferation. Br J Pharmacol. 2001 April; 132(7): 1597-1605."	5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTLIZBJ	Protein synthesis (hPRO synth)	Pathway/Process	NOUNIPROTAC	.	.	hPRO synth	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJAY96	Polymorphonuclear neutrophil adhesion (PMNA)	Pathway/Process	NOUNIPROTAC	.	.	PMNA	.	.	.	.	Discontinued	NPC 15669-modulated human polymorphonuclear neutrophil functional responsiveness: effects on receptor-coupled signal transduction. Br J Pharmacol. 1995 Apr;114(8):1694-702.	3	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT6AS9F	Protein phosphorylation (PP)	Pathway/Process	NOUNIPROTAC	.	.	PP	.	.	.	.	Literature-reported	"Anxiolytic 2,3-benzodiazepines, their specific binding to the basal ganglia. Prog Neurobiol. 2000 Mar;60(4):309-42."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8YUAD	P450-dependent ergosterol synthesis (PDE synth)	Pathway/Process	NOUNIPROTAC	.	.	PDE synth	.	.	.	.	Discontinued	"Saperconazole: a selective inhibitor of the cytochrome P-450-dependent ergosterol synthesis in Candida albicans, Aspergillus fumigatus and Trichophyton mentagrophytes. Mycoses. 1990 Jul-Aug;33(7-8):335-52."	5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZSDKE	Carcinogenesis (Tumorigenesis)	Pathway/Process	NOUNIPROTAC	.	Biogenesis of tumor	Tumorigenesis	.	.	.	.	Literature-reported	The role of stromal fibroblasts in lung carcinogenesis: A target for chemoprevention Int J Cancer. 2016 Jan 1;138(1):30-44.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTPW8EF	Synaptic transmission (ST)	Pathway/Process	NOUNIPROTAC	.	.	ST	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHVQ4N	Tubulin polymerization (TubP)	Pathway/Process	NOUNIPROTAC	.	.	TubP	.	.	.	.	Successful	URL: http://www.guidetopharmacology.org Nucleic Acids Res. 2015 Oct 12. pii: gkv1037. The IUPHAR/BPS Guide to PHARMACOLOGY in 2016: towards curated quantitative interactions between 1300 protein targets and 6000 ligands. (Ligand id: 7957).	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTX1Z4P	Prostaglandin metabolism (PG metab)	Pathway/Process	NOUNIPROTAC	.	.	PG metab	.	.	.	.	Literature-reported	HMGB1 promotes hair growth via the modulation of prostaglandin metabolism. Sci Rep. 2019 Apr 30;9(1):6660.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNDGAR	Advanced glycation end-product pathway (AGE pathway)	Pathway/Process	NOUNIPROTAC	.	.	AGE pathway	.	.	.	.	Literature-reported	Advanced glycation end-products produced systemically and by macrophages: A common contributor to inflammation and degenerative diseases. Pharmacol Ther. 2017 Sep;177:44-55.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTAUG8D	Human immunodeficiency virus Transmission (HIV Tran)	Pathway/Process	NOUNIPROTAC	.	.	HIV Tran	.	.	.	.	Clinical trial	Short Communication: Enhancement of HIV Infection by Cellulose Sulfate. AIDS Res Hum Retroviruses. 2008 July; 24(7): 925-929.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT15T2Q	Inflammatory mediator release (IM rele)	Pathway/Process	NOUNIPROTAC	.	.	IM rele	.	.	.	.	Literature-reported	Induction of inflammatory mediators (histamine and leukotrienes) from rat peritoneal mast cells and human granulocytes by Pseudomonas aeruginosa st... Infect Immun. 1989 Jul;57(7):2187-95.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTTEJMY	Tromboxane A2 synthesis (TA2 synth)	Pathway/Process	NOUNIPROTAC	.	.	TA2 synth	.	.	.	.	Successful	Tolerability of imidazole salycilate in aspirin-sensitive patients. Allergy Proc. 1995 Sep-Oct;16(5):251-4.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTDLJ0S	Interleukin-12 signaling pathway (IL12 pathway)	Pathway/Process	NOUNIPROTAC	.	.	IL12 pathway	.	.	.	.	Literature-reported	"Signal transducer and activation of transcription (STAT) 4beta, a shorter isoform of interleukin-12-induced STAT4, is preferentially activated by e... Endocrinology. 2009 Mar;150(3):1310-20."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTF63Z1	Cell differentiation (CD)	Pathway/Process	NOUNIPROTAC	.	.	CD	.	.	.	.	Clinical trial	"Fujifilm Initiates Phase I Clinical Trial in Japan for the Anticancer Agent ""FF-10501"" in Patients with Relapsed or Refractory Myelodysplastic Syndromes. FUJIFILM Corporation. June 6, 2013."	19	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8WZ3Q	Mitochondrial gene transcription (MGT)	Pathway/Process	NOUNIPROTAC	.	.	MGT	.	.	.	.	Discontinued	Down-regulation of mitochondrial gene expression by the anti-tumor arotinoid mofarotene (Ro 40-8757). Int J Cancer. 1994 Sep 15;58(6):891-7.	3	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT62Q7D	LPS-miR-34a-CCL22 axis (LmCa)	Pathway/Process	NOUNIPROTAC	.	.	LmCa	.	.	.	.	Literature-reported	LPS-miR-34a-CCL22 axis contributes to regulatory T cell recruitment in periapical lesions. Biochem Biophys Res Commun. 2015 May 8;460(3):733-40.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTCDKBP	Non-steroidal androgen synthesis (NSAD synth)	Pathway/Process	NOUNIPROTAC	.	.	NSAD synth	.	.	.	.	Literature-reported	"Orteronel (TAK-700), a novel non-steroidal 17,20-lyase inhibitor: effects on steroid synthesis in human and monkey adrenal cells and serum steroid levels in cynomolgus monkeys. J Steroid Biochem Mol Biol. 2012 Apr;129(3-5):115-28."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTLYHN8	CXCL5/CXCR2 axis (CXCL5/CXCR2 axis)	Pathway/Process	NOUNIPROTAC	.	C-X-C motif chemokine 5/C-X-C motif chemokine receptor 2 axis	CXCL5/CXCR2 axis	.	.	.	.	Literature-reported	CXCL5/CXCR2 axis promotes bladder cancer cell migration and invasion by activating PI3K/AKT-induced upregulation of MMP2/MMP9. Int J Oncol. 2015 Aug;47(2):690-700.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTM852O	S100A6/p38/MAPK signaling pathway (SpM pathway)	Pathway/Process	NOUNIPROTAC	.	.	SpM pathway	.	.	.	.	Literature-reported	S100A6 promotes cell proliferation in human nasopharyngeal carcinoma via the p38/MAPK signaling pathway. Mol Carcinog. 2017 Mar;56(3):972-984.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTGQUFK	PI3K/AKT/mTOR pathway (PAm pathway)	Pathway/Process	NOUNIPROTAC	.	.	PAm pathway	.	.	.	.	Successful	The genomic landscape of nasopharyngeal carcinoma.Nat Genet. 2014 Aug;46(8):866-71.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTKA5LP	HGF/Met signaling pathway (HGF/Met pathway)	Pathway/Process	NOUNIPROTAC	.	.	HGF/Met pathway	.	.	.	.	Successful	"Met tyrosine kinase inhibitor, PF-2341066, suppresses growth and invasion of nasopharyngeal carcinoma.Drug Des Devel Ther. 2015 Aug 26;9:4897-907."	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT7GJ9D	Glutamate release (GLU rele)	Pathway/Process	NOUNIPROTAC	.	.	GLU rele	.	.	.	.	Literature-reported	The uptake and release of glutamate at the crayfish neuromuscular junction. J Physiol. 1984 Sep;354:69-78.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMR83K	Hepatitis B virus Reverse transcriptase priming/DNA synthesis (HBV RTP/DS)	Pathway/Process	NOUNIPROTAC	.	.	HBV RTP/DS	.	.	.	.	Clinical trial	Noncompetitive Inhibition of Hepatitis B Virus Reverse Transcriptase Protein Priming and DNA Synthesis by the Nucleoside Analog Clevudine. Correction in: Antimicrob Agents Chemother. 2013 November; 57(11): 5788.	19	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT9X7H4	Beta-hematin formation (BHF)	Pathway/Process	NOUNIPROTAC	.	.	BHF	.	.	.	.	Successful	Lack of association of the S769N mutation in Plasmodium falciparum SERCA (PfATP6) with resistance to artemisinins. Antimicrob Agents Chemother. 2012 May;56(5):2546-52.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTK3Q4W	NFE2-related factor 2 pathway (Nrf2 pathway)	Pathway/Process	NOUNIPROTAC	.	.	Nrf2 pathway	.	.	.	.	Successful	Radium 223 dichloride for prostate cancer treatment. Drug Des Devel Ther. 2017 Sep 6;11:2643-2651.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTL3N71	Virus Replication (Viru Repli)	Pathway/Process	NOUNIPROTAC	.	.	Viru Repli	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYJL7K	Sodium/potassium transport (Na/K trans)	Pathway/Process	NOUNIPROTAC	.	.	Na/K trans	.	.	.	.	Clinical trial	"US patent application no. 8,067,031, Compositions and systems for forming crosslinked biomaterials and associated methods of preparation and use."	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8579I	Tumor necrosis factor synthesis (TNF synth)	Pathway/Process	NOUNIPROTAC	.	.	TNF synth	.	.	.	.	Literature-reported	Small molecule activators of the Nrf2-HO-1 antioxidant axis modulate heme metabolism and inflammation in BV2 microglia cells. Pharmacol Res. 2013 Oct;76:132-48.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTF1HJC	Ergosterol synthesis (EG synth)	Pathway/Process	NOUNIPROTAC	.	.	EG synth	.	.	.	.	Literature-reported	The 3-hydroxy-3-methylglutaryl coenzyme-A reductases from fungi: a proposal as a therapeutic target and as a study model. Rev Iberoam Micol. 2014 Jan-Mar;31(1):81-5.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTT1MCF	Permeability pathway (NP pathway)	Pathway/Process	NOUNIPROTAC	.	NPPs	NP pathway	.	.	.	.	Literature-reported	Novel molecular targets for antimalarial drug development. Chem Biol Drug Des. 2008 Apr;71(4):287-97.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5TOX7	Human immunodeficiency virus Maturation (HIV Mat)	Pathway/Process	NOUNIPROTAC	.	.	HIV Mat	.	.	.	.	Clinical trial	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800037762)"	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTR3ZY2	Human immunodeficiency virus Cell fusion (HIV CF)	Pathway/Process	NOUNIPROTAC	.	.	HIV CF	.	.	.	.	Literature-reported	Enfuvirtide (T20)-Based Lipopeptide Is a Potent HIV-1 Cell Fusion Inhibitor: Implications for Viral Entry and Inhibition. J Virol. 2017 Aug 24;91(18). pii: e00831-17.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTRPO9Z	TNF-alpha signaling pathway (TNFA pathway)	Pathway/Process	NOUNIPROTAC	Viral DNA polymerase	.	TNFA pathway	.	.	.	.	Clinical trial	"Phase 1 safety and immunogenicity evaluation of ADVAX, a multigenic, DNA-based clade C/B' HIV-1 candidate vaccine. PLoS One. 2010 Jan 25;5(1):e8617."	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT6K9BV	Cdc-like kinase (CLK)	P49759; P49760; P49761; Q9HAZ1	CLK1_HUMAN; CLK2_HUMAN; CLK3_HUMAN; CLK4_HUMAN	.	.	CLK	.	.	.	.	Clinical trial	"SM09419, a Novel, Small-Molecule CDC-like Kinase (CLK) Inhibitor, Demonstrates Strong Inhibition of the Wnt Signaling Pathway and Antitumor Effects in FMS-like Tyrosine Kinase 3 (FLT3)-Mutant Acute Myeloid Leukemia Models. Blood; 2019,134 (Supplement_1):1377."	.	.	.	.	.	.	.	.	.	.	.	hsa05134: Legionellosis	.	.	P49759
TT7OGZP	Casein kinase 1 (CK1)	P48729; P48730; P49674; Q9HCP0; P78368; Q9Y6M4	KC1A_HUMAN; KC1D_HUMAN; KC1E_HUMAN; KC1G1_HUMAN; KC1G2_HUMAN; KC1G3_HUMAN	.	.	CK1	.	.	.	.	Preclinical	Crystal structures of two aminoglycoside kinases bound with a eukaryotic protein kinase inhibitor. PLoS One. 2011 May 9;6(5):e19589.	.	.	.	.	.	.	.	.	.	.	.	hsa04310: Wnt signaling pathway; hsa04340: Hedgehog signaling pathway; hsa05010: Alzheimer disease; hsa05022: Pathways of neurodegeneration - multiple diseases; hsa05165: Human papillomavirus infection; hsa05224: Breast cancer; hsa05225: Hepatocellular carcinoma; hsa05226: Gastric cancer	R-HSA-195253: Degradation of beta-catenin by the destruction complex; R-HSA-196299: Beta-catenin phosphorylation cascade; R-HSA-4641262: Disassembly of the destruction complex and recruitment of AXIN to the membrane; R-HSA-5339716: Signaling by GSK3beta mutants; R-HSA-5358747: CTNNB1 S33 mutants aren't phosphorylated; R-HSA-5358749: CTNNB1 S37 mutants aren't phosphorylated; R-HSA-5358751: CTNNB1 S45 mutants aren't phosphorylated; R-HSA-5358752: CTNNB1 T41 mutants aren't phosphorylated; R-HSA-5467337: APC truncation mutants have impaired AXIN binding; R-HSA-5467340: AXIN missense mutants destabilize the destruction complex; R-HSA-5467348: Truncations of AMER1 destabilize the destruction complex; R-HSA-5610783: Degradation of GLI2 by the proteasome; R-HSA-5610785: GLI3 is processed to GLI3R by the proteasome; R-HSA-5635838: Activation of SMO; R-HSA-9694631: Maturation of nucleoprotein	.	P48729
TTQ7UAP	RAC serine/threonine-protein kinase (AKT)	P31749; P31751; Q9Y243	AKT1_HUMAN; AKT2_HUMAN; AKT3_HUMAN	.	.	AKT	.	.	.	.	Clinical trial	"Targeting AKT1-E17K and the PI3K/AKT Pathway with an Allosteric AKT Inhibitor, ARQ 092. PLoS One. 2015 Oct 15;10(10):e0140479."	.	.	.	.	.	.	.	.	.	.	.	"hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa01522: Endocrine resistance; hsa01524: Platinum drug resistance; 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; hsa04072: Phospholipase D signaling pathway; hsa04140: Autophagy - animal; hsa04150: mTOR signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04152: AMPK signaling pathway; hsa04210: Apoptosis; hsa04211: Longevity regulating pathway; hsa04213: Longevity regulating pathway - multiple species; hsa04218: Cellular senescence; hsa04261: Adrenergic signaling in cardiomyocytes; hsa04370: VEGF signaling pathway; hsa04371: Apelin signaling pathway; hsa04380: Osteoclast differentiation; hsa04510: Focal adhesion; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa04611: Platelet activation; hsa04613: Neutrophil extracellular trap formation; hsa04620: Toll-like receptor signaling pathway; hsa04625: C-type lectin 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; hsa04926: Relaxin signaling pathway; hsa04929: GnRH secretion; hsa04931: Insulin resistance; hsa04932: Non-alcoholic fatty liver disease; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa04935: Growth hormone synthesis, secretion and action; hsa04936: Alcoholic liver disease; hsa04973: Carbohydrate digestion and absorption; hsa05010: Alzheimer disease; hsa05017: Spinocerebellar ataxia; hsa05131: Shigellosis; hsa05132: Salmonella infection; hsa05135: Yersinia infection; hsa05142: Chagas disease; hsa05145: Toxoplasmosis; hsa05152: Tuberculosis; hsa05160: Hepatitis C; hsa05161: Hepatitis B; hsa05162: Measles; hsa05163: Human cytomegalovirus infection; hsa05164: Influenza A; hsa05165: Human papillomavirus infection; hsa05166: Human T-cell leukemia virus 1 infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05168: Herpes simplex virus 1 infection; hsa05169: Epstein-Barr virus infection; hsa05170: Human immunodeficiency virus 1 infection; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; 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; 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; hsa05415: Diabetic cardiomyopathy; hsa05417: Lipid and atherosclerosis; hsa05418: Fluid shear stress and atherosclerosis"	"R-HSA-111447: Activation of BAD and translocation to mitochondria; R-HSA-1257604: PIP3 activates AKT signaling; R-HSA-1358803: Downregulation of ERBB2:ERBB3 signaling; R-HSA-1445148: Translocation of SLC2A4 (GLUT4) to the plasma membrane; R-HSA-1474151: Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation; R-HSA-165159: MTOR signalling; 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 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-450385: Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA; 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; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-6804757: Regulation of TP53 Degradation; R-HSA-6804758: Regulation of TP53 Activity through Acetylation; R-HSA-6804759: Regulation of TP53 Activity through Association with Co-factors; R-HSA-6811558: PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling; R-HSA-69202: Cyclin E associated events during G1/S transition; R-HSA-69656: Cyclin A:Cdk2-associated events at S phase entry; R-HSA-8849469: PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1; R-HSA-8876198: RAB GEFs exchange GTP for GDP on RABs; R-HSA-8941332: RUNX2 regulates genes involved in cell migration; R-HSA-8948751: Regulation of PTEN stability and activity; R-HSA-9009391: Extra-nuclear estrogen signaling; R-HSA-9604323: Negative regulation of NOTCH4 signaling; R-HSA-9607240: FLT3 Signaling; R-HSA-9614399: Regulation of localization of FOXO transcription factors; R-HSA-9634638: Estrogen-dependent nuclear events downstream of ESR-membrane signaling; R-HSA-9755511: KEAP1-NFE2L2 pathway; R-HSA-9755779: SARS-CoV-2 targets host intracellular signalling and regulatory pathways"	.	P31749
TTG68FB	Interleukine 12 (IL-12)	P29459; P29460	IL12A_HUMAN; IL12B_HUMAN	.	.	IL-12	.	.	.	.	Clinical trial	Intratumoral delivery of tavokinogene telseplasmid yields systemic immune responses in metastatic melanoma patients. Ann Oncol. 2020 Apr;31(4):532-540.	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04620: Toll-like receptor signaling pathway; hsa04622: RIG-I-like receptor signaling pathway; hsa04625: C-type lectin receptor signaling pathway; hsa04630: JAK-STAT signaling pathway; hsa04658: Th1 and Th2 cell differentiation; hsa04936: Alcoholic liver disease; hsa04940: Type I diabetes mellitus; hsa05133: Pertussis; hsa05134: Legionellosis; hsa05140: Leishmaniasis; hsa05142: Chagas disease; hsa05143: African trypanosomiasis; hsa05144: Malaria; hsa05145: Toxoplasmosis; hsa05146: Amoebiasis; hsa05152: Tuberculosis; hsa05162: Measles; hsa05164: Influenza A; hsa05168: Herpes simplex virus 1 infection; hsa05171: Coronavirus disease - COVID-19; hsa05200: Pathways in cancer; hsa05321: Inflammatory bowel disease; hsa05330: Allograft rejection; hsa05417: Lipid and atherosclerosis	R-HSA-6783783: Interleukin-10 signaling; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-8984722: Interleukin-35 Signalling; R-HSA-9020591: Interleukin-12 signaling	.	P29459
TTRG4QN	Activin receptor type II (ACVR2)	P27037; Q13705	AVR2A_HUMAN; AVR2B_HUMAN	.	.	ACVR2	.	.	.	.	Clinical trial	"Effects of bimagrumab, an activin receptor type II inhibitor, on pituitary neurohormonal axes. Clin Endocrinol (Oxf). 2018 Jun;88(6):908-919."	.	.	.	.	.	.	.	.	.	.	.	hsa04060: Cytokine-cytokine receptor interaction; hsa04350: TGF-beta signaling pathway; hsa04550: Signaling pathways regulating pluripotency of stem cells; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-1181150: Signaling by NODAL; R-HSA-1433617: Regulation of signaling by NODAL; R-HSA-1502540: Signaling by Activin; R-HSA-201451: Signaling by BMP	.	P27037
TT9HKJA	Vascular endothelial growth factor (VEGF)	P15692; P49765; P49767; O43915	VEGFA_HUMAN; VEGFB_HUMAN; VEGFC_HUMAN; VEGFD_HUMAN	Growth factor	Vascular endothelial cell growth factor	VEGF	.	.	.	.	Successful	"Nasopharyngeal carcinoma: Current treatment options and future directions. J Nasopharyng Carcinoma, 2014, 1(16): e16."	34	.	.	.	.	.	.	.	.	.	.	hsa01521: EGFR tyrosine kinase inhibitor resistance; hsa04010: MAPK signaling pathway; hsa04014: Ras signaling pathway; hsa04015: Rap1 signaling pathway; hsa04020: Calcium signaling pathway; hsa04066: HIF-1 signaling pathway; hsa04151: PI3K-Akt signaling pathway; hsa04370: VEGF signaling pathway; hsa04510: Focal adhesion; hsa04926: Relaxin signaling pathway; hsa04933: AGE-RAGE signaling pathway in diabetic complications; hsa05163: Human cytomegalovirus infection; hsa05165: Human papillomavirus infection; hsa05167: Kaposi sarcoma-associated herpesvirus infection; hsa05200: Pathways in cancer; hsa05205: Proteoglycans in cancer; hsa05206: MicroRNAs in cancer; hsa05207: Chemical carcinogenesis - receptor activation; hsa05208: Chemical carcinogenesis - reactive oxygen species; hsa05211: Renal cell carcinoma; hsa05212: Pancreatic cancer; hsa05219: Bladder cancer; hsa05323: Rheumatoid arthritis; hsa05418: Fluid shear stress and atherosclerosis	R-HSA-114608: Platelet degranulation; R-HSA-1234158: Regulation of gene expression by Hypoxia-inducible Factor; R-HSA-194138: Signaling by VEGF; R-HSA-194313: VEGF ligand-receptor interactions; R-HSA-195399: VEGF binds to VEGFR leading to receptor dimerization; R-HSA-4420097: VEGFA-VEGFR2 Pathway; R-HSA-5218921: VEGFR2 mediated cell proliferation; R-HSA-6785807: Interleukin-4 and Interleukin-13 signaling; R-HSA-8866910: TFAP2 (AP-2) family regulates transcription of growth factors and their receptors; R-HSA-9679191: Potential therapeutics for SARS	.	P15692
TTJOCTY	Tropomyosin receptor kinase (Trk)	P04629; Q16620; Q16288	NTRK1_HUMAN; NTRK2_HUMAN; NTRK3_HUMAN	.	.	Trk	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of AnHeart Therapeutics."	.	.	.	.	.	.	.	.	.	.	.	hsa04010: MAPK signaling pathway; hsa04014: Ras signaling pathway; hsa04020: Calcium signaling pathway; hsa04151: PI3K-Akt signaling pathway; 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	R-HSA-167021: PLC-gamma1 signalling; R-HSA-167044: Signalling to RAS; R-HSA-170968: Frs2-mediated activation; R-HSA-170984: ARMS-mediated activation; R-HSA-177504: Retrograde neurotrophin signalling; R-HSA-187024: NGF-independant TRKA activation; R-HSA-187042: TRKA activation by NGF; R-HSA-187706: Signalling to p38 via RIT and RIN; R-HSA-198203: PI3K/AKT activation; R-HSA-198745: Signalling to STAT3	.	P04629
TT0OV9N	Haematin (HA)	Other molecule	NOUNIPROTAC	.	.	HA	.	.	.	.	Clinical trial	Insights into the mechanism of action of ferroquine. Relationship between physicochemical properties and antiplasmodial activity. Mol Pharm. 2005 May-Jun;2(3):185-93.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUDR0C	Iron (Fe)	Other molecule	NOUNIPROTAC	.	.	Fe	.	.	.	.	Successful	2011 FDA drug approvals. Nat Rev Drug Discov. 2012 Feb 1;11(2):91-4.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZ1SWF	Uric acid (URA)	Other molecule	NOUNIPROTAC	.	.	URA	.	.	.	.	Successful	Mullard A: 2010 FDA drug approvals. Nat Rev Drug Discov. 2011 Feb;10(2):82-5.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT0DBAO	Polyamine unspecific (PLA)	Other molecule	NOUNIPROTAC	.	.	PLA	.	.	.	.	Discontinued	"Antitumor activity of a novel synthetic polyamine analogue, N,N'-bis-[3-(ethylamino)-propyl]-1-7-heptane diamine: potentiation by polyamine oxidase inhibitors. Anticancer Res. 1990 Sep-Oct;10(5A):1281-7."	3	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT698WO	Plasmodium Deoxyribonucleic acid (Malaria DNA)	Other molecule	NOUNIPROTAC	.	.	Malaria DNA	.	.	.	.	Successful	Direct detection of falciparum and non-falciparum malaria DNA from a drop of blood with high sensitivity by the dried-LAMP system. Parasit Vectors. 2017 Jan 13;10(1):26.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTULV0X	Reactive oxygen species (ROS)	Other molecule	NOUNIPROTAC	.	.	ROS	.	.	.	.	Successful	Tafenoquine: First Global Approval.Drugs. 2018 Sep;78(14):1517-1523. 	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT9W3FO	Monosialic ganglioside 2 (GM2)	Other Molecule	NOUNIPROTAC	.	Gamma-M2; GM2	GM2	Crystallins are the dominant structural components of the vertebrate eye lens.	.	.	.	Literature-reported	Ganglioside characterization of a cell line displaying motor neuron-like phenotype: GM2 as a possible major ganglioside in motor neurons. J Neurol Sci. 1995 Aug;131(2):111-8.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTE6QWF	Staphylococcus Capsular polysaccharide CP5 (Stap-coc CP5)	Other molecule	NOUNIPROTAC	.	.	Stap-coc CP5	.	.	.	.	Clinical trial	ClinicalTrials.gov (NCT01364571) Evaluation of a Single Vaccination With One of Three Ascending Dose Levels of a 4-Antigen Staphylococcus Aureus Vaccine (SA4Ag) in Healthy Adults Aged 18 to <65 Years. U.S. National Institutes of Health.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT4ESMB	Pseudomonas Lipopolysaccharide (Pseudo LPS)	Other molecule	NOUNIPROTAC	.	.	Pseudo LPS	.	.	.	.	Clinical trial	Antibacterial antibodies gain traction. Nat Rev Drug Discov. 2015 Nov;14(11):737-8. 	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTAD7UL	Superoxide anion (SPA)	Other molecule	NOUNIPROTAC	.	.	SPA	.	.	.	.	Clinical trial	Evaluation of superoxide scavenging activity of OPC-14117 by electron spin resonance technique. Free Radic Res Commun. 1991;15(4):223-30.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTT28H3	Plasmodium 80S ribosome (Malaria 80S)	Other molecule	NOUNIPROTAC	.	.	Malaria 80S	.	.	.	.	Successful	An ultrastructural study of the effects of mefloquine on malaria parasites. Am J Trop Med Hyg. 1987 Jan;36(1):9-14.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT4823K	Virus Deoxyribonucleic acid (Viru DNA)	Other molecule	NOUNIPROTAC	.	.	Viru DNA	.	.	.	.	Successful	Functions of DNA damage machinery in the innate immune response to DNA virus infection. Curr Opin Virol. 2015 Dec;15:56-62.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3NH7G	Human immunodeficiency virus Deoxyribonucleic acid (HIV DNA)	Other molecule	NOUNIPROTAC	.	.	HIV DNA	.	.	.	.	Clinical trial	"WO patent application no. 2006,0835,53, Diketo acids with nucleobase scaffolds: anti-hiv replication inhibitors targeted at hiv integrase."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTB0SC6	Potassium (K)	Other molecule	NOUNIPROTAC	.	.	K	.	.	.	.	Successful	"Evaluation of the efficacy and safety of RLY5016, a polymeric potassium binder, in a double-blind, placebo-controlled study in patients with chronic heart failure (the PEARL-HF) trial. Eur Heart J. 2011 Apr;32(7):820-8."	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQKWA4	Fungal Cell membrane ergosterol (Fung CME)	Other molecule	NOUNIPROTAC	.	.	Fung CME	.	.	.	.	Successful	Comparative molecular dynamics simulations of amphotericin B-cholesterol/ergosterol membrane channels. Biochim Biophys Acta. 2002 Dec 23;1567(1-2):63-78.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTX1CE3	High density lipoprotein (HDL)	Other molecule	NOUNIPROTAC	.	HDL	HDL	.	.	.	.	Literature-reported	High density lipoproteins (HDLs) and atherosclerosis; the unanswered questions. Atherosclerosis. 2003 Jun;168(2):195-211.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHL1EA	G-quadruplex DNA (GQDNA)	Other molecule	NOUNIPROTAC	.	.	GQDNA	.	.	.	.	Literature-reported	G-quadruplex DNA: a potential target for anti-cancer drug design. Trends Pharmacol Sci. 2000 Apr;21(4):136-42.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTVUKJI	Cyclic nucleotide (CN)	Other Molecule	NOUNIPROTAC	.	cNMP	CN	.	.	.	.	Literature-reported	The role of cyclic nucleotide signaling pathways in cancer: targets for prevention and treatment. Cancers (Basel). 2014 Feb 26;6(1):436-58.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXPQW1	Hormone unspecific (HOM)	Other molecule	NOUNIPROTAC	.	.	HOM	.	.	.	.	Clinical trial	ClinicalTrials.gov (NCT01872078) A Study of AZD4901 in Females With Polycystic Ovary Syndrome. U.S. National Institutes of Health.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTS1W4A	Bacterial Deoxyribonucleic acid (Bact DNA)	Other molecule	NOUNIPROTAC	.	.	Bact DNA	.	.	.	.	Successful	Interaction between hydroxystilbamidine and DNA. I. Binding isotherms and thermodynamics of the association. Biochim Biophys Acta. 1975 Sep 12;407(1):24-42.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYTVXF	Hyaluronic acid (HA)	Other molecule	NOUNIPROTAC	.	.	HA	.	.	.	.	Successful	Safety results of two phase III trials of an intravitreous injection of highly purified ovine hyaluronidase (Vitrase) for the management of vitreous hemorrhage. Am J Ophthalmol. 2005 Oct;140(4):585-97.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHL6YX	Progesterone (PG)	Other molecule	NOUNIPROTAC	.	.	PG	.	.	.	.	Clinical trial	Randomized phase II study of lonaprisan as second-line therapy for progesterone receptor-positive breast cancer. Ann Oncol. 2013 Oct;24(10):2543-8.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTX81QL	Toxic methotrexate (TM)	Other molecule	NOUNIPROTAC	.	.	TM	.	.	.	.	Successful	Nat Rev Drug Discov. 2013 Feb;12(2):87-90.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTB1TZG	Schistosoma Deoxyribonucleic acid (Schist DNA)	Other molecule	NOUNIPROTAC	.	.	Schist DNA	.	.	.	.	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT27K59	Platelet activating factor (PAF)	Other molecule	NOUNIPROTAC	.	PAF	PAF	.	.	.	.	Literature-reported	Pinusolide from the leaves of Biota orientalis as potent platelet activating factor antagonist. Planta Med. 1999 Feb;65(1):39-42.	2.1	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT4SVB7	Staphylococcus Capsular polysaccharide CP8 (Stap-coc CP8)	Other molecule	NOUNIPROTAC	.	.	Stap-coc CP8	.	.	.	.	Clinical trial	ClinicalTrials.gov (NCT01364571) Evaluation of a Single Vaccination With One of Three Ascending Dose Levels of a 4-Antigen Staphylococcus Aureus Vaccine (SA4Ag) in Healthy Adults Aged 18 to <65 Years. U.S. National Institutes of Health.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT80ARU	Ganglioside GD2 (GD2)	Other Molecule	NOUNIPROTAC	.	Ganglioside G2; GD2	GD2	.	.	.	.	Clinical trial	ClinicalTrials.gov (NCT02765243) Anti-GD2 4th Generation CART Cells Targeting Refractory and/or Recurrent Neuroblastoma	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOVXHF	Human Deoxyribonucleic acid minor groove (hDNA min)	Other molecule	NOUNIPROTAC	.	.	hDNA min	.	.	.	.	Successful	"Brostallicin (PNU-166196), a new minor groove DNA binder: preclinical and clinical activity. Expert Opin Investig Drugs. 2009 Dec;18(12):1939-46."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTK938H	Cytomegalovirus Deoxyribonucleic acid (CMV DNA)	Other molecule	NOUNIPROTAC	.	.	CMV DNA	.	.	.	.	Clinical trial	"VCL-CB01, an injectable bivalent plasmid DNA vaccine for potential protection against CMV disease and infection. Curr Opin Mol Ther. 2009 Oct;11(5):572-8."	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZYW5V	Hepatitis C virus Deoxyribonucleic acid (HCV DNA)	Other molecule	NOUNIPROTAC	.	.	HCV DNA	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of Inovio Pharmaceuticals."	19	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8X5NO	Calcium (Ca)	Other molecule	NOUNIPROTAC	.	.	Ca	.	.	.	.	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTY1GPO	Human Deoxyribonucleic acid major groove (hDNA maj)	Other molecule	NOUNIPROTAC	.	.	hDNA maj	.	.	.	.	Successful	Natural products as sources of new drugs over the last 25 years. J Nat Prod. 2007 Mar;70(3):461-77.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTDCBO2	Endotoxin (LPS)	Other Molecule	NOUNIPROTAC	.	Endotoxin (lipopolysaccharide)	LPS	.	.	.	.	Literature-reported	Endotoxin as a drug target. Crit Care Med. 2003 Jan;31(1 Suppl):S57-64.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTGXKP7	Samarium (SAM)	Other molecule	NOUNIPROTAC	.	.	SAM	.	.	.	.	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHOTF6	Phosphate (PHO)	Other molecule	NOUNIPROTAC	.	.	PHO	.	.	.	.	Successful	2004 approvals: the demise of the blockbuster. Nat Rev Drug Discov. 2005 Feb;4(2):93-4.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUTN1I	Human Deoxyribonucleic acid (hDNA)	Other molecule	NOUNIPROTAC	.	.	hDNA	.	.	.	.	Successful	"Carmustine-induced toxicity, DNA crosslinking and O6-methylguanine-DNA methyltransferase activity in two human lung cancer cell lines. Eur J Cancer. 1991;27(12):1658-62."	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZEX7Y	Malondialdehyde (MDA)	Other molecule	NOUNIPROTAC	.	.	MDA	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT0C9DV	Toxic reactive metabolite (TRM)	Other molecule	NOUNIPROTAC	.	.	TRM	.	.	.	.	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. 2015	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTAFD3Y	Poly-N-acetyl glucosamine (PNAG)	Other molecule	NOUNIPROTAC	.	.	PNAG	.	.	.	.	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT4P0T6	Potassium-competitive acid (PCA)	Other molecule	NOUNIPROTAC	.	.	PCA	.	.	.	.	Literature-reported	Potassium-competitive acid blockers: Advanced therapeutic option for acid-related diseases. Pharmacol Ther. 2016 Dec;168:12-22.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTC6RJ7	Intermediate-density lipoprotein (IDL)	Other molecule	NOUNIPROTAC	.	.	IDL	.	.	.	.	Literature-reported	New dimension of statin action on ApoB atherogenicity. Clin Cardiol. 2003 Jan;26(1 Suppl 1):I7-10.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8E7Z0	Free radical (FRD)	Other molecule	NOUNIPROTAC	.	.	FRD	.	.	.	.	Clinical trial	"NXY-059, a free radical--trapping agent, substantially lessens the functional disability resulting from cerebral ischemia in a primate species. Stroke. 2001 Jan;32(1):190-8."	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXQYT6	T-cells (T-cells)	Organelle/Cell	NOUNIPROTAC	.	T cells	T-cells	.	.	.	.	Clinical trial	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. 2015	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTO0YVN	Leukocyte (WBC)	Organelle/Cell	NOUNIPROTAC	.	Human leukocyte	WBC	.	.	.	.	Clinical trial	"WO patent application no. 2005,0792,17, Oligonucleotide decoys and methods of use."	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2AMHT	Mitochondrial membrane (MIM)	Organelle/Cell	NOUNIPROTAC	.	.	MIM	.	.	.	.	Literature-reported	Mitochondria as a target in treatment. Environ Mol Mutagen. 2010 Jun;51(5):462-75.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTIEJ8U	Helper-inducer T-lymphocyte (HITL)	Organelle/Cell	NOUNIPROTAC	.	.	HITL	.	.	.	.	Clinical trial	"WO patent application no. 2013,1850,32, Nanotherapeutics for drug targeting."	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTT6K3S	Endothelium of blood vessels (Endothelium)	Organelle/Cell	NOUNIPROTAC	.	Endothelium of blood vessels	Endothelium	.	.	.	.	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. 2015	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYA7V2	Prostate cance cell (PCC)	Organelle/Cell	NOUNIPROTAC	.	.	PCC	.	.	.	.	Clinical trial	"17alpha-alkynyl 3alpha, 17beta-androstanediol non-clinical and clinical pharmacology, pharmacokinetics and metabolism. Invest New Drugs. 2012 Feb;30(1):59-78."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJ073B	Ribosome (hRBS)	Organelle/Cell	NOUNIPROTAC	.	.	hRBS	.	.	.	.	Clinical trial	Gateways to clinical trials. Methods Find Exp Clin Pharmacol. 2009 Nov;31(9):597-633.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTT04VN	Adrenergic neuron (AD neuro)	Organelle/Cell	NOUNIPROTAC	.	.	AD neuro	.	.	.	.	Successful	Characterization of bradykinin-induced endothelium-independent contraction in equine basilar artery. J Vet Pharmacol Ther. 2009 Jun;32(3):264-70.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXT4D5	Bacterial Cell membrane (Bact CM)	Organelle/Cell	NOUNIPROTAC	.	.	Bact CM	.	.	.	.	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTAH0B3	Fungal Cell membrane (Fung CM)	Organelle/Cell	NOUNIPROTAC	.	.	Fung CM	.	.	.	.	Successful	Natamycin blocks fungal growth by binding specifically to ergosterol without permeabilizing the membrane. J Biol Chem. 2008 Mar 7;283(10):6393-401.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTWR6YK	PI3-kinase (PIK3C)	NOUNIPROTAC	Family	.	.	PIK3C	.	.	.	.	Literature-reported	"A novel phosphatidylinositol 3-kinase (PI3K) inhibitor directs a potent FOXO-dependent, p53-independent cell cycle arrest phenotype characterized by the differential induction of a subset of FOXO-regulated genes. Breast Cancer Res. 2014 Dec 9;16(6):482."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT6S84O	Human immunodeficiency virus Trans-activation response element (HIV TAR RNA element)	NO-UNIPROT	NOUNIPROTAC	mRNA target	HIV TAR element	HIV TAR RNA element	.	.	.	.	Clinical trial	Design and development of antisense drugs. Expert Opin. Drug Discov. 2008 3(10):1189-1207.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXWCK2	Hepatitis C virus Internal ribosome entry site messenger RNA (HCV IRES mRNA)	NO-UNIPROT	NOUNIPROTAC	mRNA target	mRNA of HCV IRES	HCV IRES mRNA	.	.	.	.	Discontinued	Design and development of antisense drugs. Expert Opin. Drug Discov. 2008 3(10):1189-1207.	5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTPHW9Y	Ascaris NADH-fumarate reductase (Asc OSM)	NO-UNIPROT	NOUNIPROTAC	.	.	Asc OSM	.	.	.	.	Literature-reported	Mitochondrial fumarate reductase as a target of chemotherapy: from parasites to cancer cells. Biochim Biophys Acta. 2012 May;1820(5):643-51.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTFCQYU	Sinus node I(f) channel (SA node IfC)	NO-UNIPROT	NOUNIPROTAC	.	.	SA node IfC	.	.	.	.	Successful	Ivabradine - the first selective sinus node If channel inhibitor in the treatment of stable angina. Int J Clin Pract. 2006 February; 60(2): 222-228.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTWYIT3	Acetaminophen binding protein 58kDa (ABP58)	NO-UNIPROT	NOUNIPROTAC	.	.	ABP58	.	.	.	.	Literature-reported	Evidence suggesting the 58-kDa acetaminophen binding protein is a preferential target for acetaminophen electrophile. Fundam Appl Toxicol. 1996 Jul;32(1):79-86.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQDJCS	Streptococcus Capsular antigen (Stre CA)	NO-UNIPROT	NOUNIPROTAC	.	.	Stre CA	.	.	.	.	Literature-reported	Review: current and new generation pneumococcal vaccines. J Infect. 2014 Oct;69(4):309-25.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTPXOQN	Gastric carcinoma-associated antigen MG7 (MG7)	NO-UNIPROT	NOUNIPROTAC	.	MG7-Ag	MG7	.	.	.	.	Clinical trial	ClinicalTrials.gov (NCT02862704) A Study of MG7 Redirected Autologous T Cells for Advanced MG7 Positive Liver Metastases(MG7-CART)	19	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTH7Z83	Tumor-associated carbohydrate antigen KH-1 (KH-1)	NO-UNIPROT	NOUNIPROTAC	.	Antigen KH-1	KH-1	.	.	.	.	Literature-reported	Constructing an adenocarcinoma vaccine: immunization of mice with synthetic KH-1 nonasaccharide stimulates anti-KH-1 and anti-Le(y) antibodies. Int J Cancer. 2002 May 10;99(2):207-12.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTSJMN8	Immunoproteasome complex (IP)	NO-UNIPROT	NOUNIPROTAC	.	i-proteasome complex	IP	.	.	.	.	Patented-recorded	A patent review of immunoproteasome inhibitors.Expert Opin Ther Pat. 2018 Jul;28(7):517-540.	15.5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTBFHXC	Feto-acinar pancreatic protein (FAPP)	NO-UNIPROT	NOUNIPROTAC	.	.	FAPP	.	.	.	.	Literature-reported	"Clinical pipeline report, company report or official report of Gimv."	2	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5XVD6	Intracellular nitroreductase (INR)	NO-UNIPROT	NOUNIPROTAC	.	.	INR	.	.	.	.	Clinical trial	A phase I study of SR-4554 via intravenous administration for noninvasive investigation of tumor hypoxia by magnetic resonance spectroscopy in patients with malignancy. Clin Cancer Res. 2003 Nov 1;9(14):5101-12.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT7FTES	Endothelium-derived hyperpolarizing factor (EDHF)	NO-UNIPROT	NOUNIPROTAC	.	EDHF	EDHF	.	.	.	.	Literature-reported	Calcium dobesilate potentiates endothelium-derived hyperpolarizing factor-mediated relaxation of human penile resistance arteries. Br J Pharmacol. 2003 Jun;139(4):854-62.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTSBFYK	Estramustine binding protein (EMBP)	NO-UNIPROT	NOUNIPROTAC	.	.	EMBP	.	.	.	.	Successful	Estramustine binding protein in primary tumours and metastases of malignant melanoma. Melanoma Res. 1994 Dec;4(6):401-5.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTGFDOM	Leukotriene E4 receptor (LTE4R)	NO-UNIPROT	NOUNIPROTAC	.	LTE4 receptor	LTE4R	.	.	.	.	Literature-reported	"Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTF5WCR	Endogenous gut peptide (EGP)	NO-UNIPROT	NOUNIPROTAC	.	.	EGP	.	.	.	.	Clinical trial	Investigational drugs in Phase II clinical trials for the treatment of obesity: implications for future development of novel therapies. Expert Opin Investig Drugs. 2014 Aug;23(8):1055-66.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTIJ5EB	Bacterial RNA polymerase switch region (Bact RNAP-SR)	NO-UNIPROT	NOUNIPROTAC	.	.	Bact RNAP-SR	.	.	.	.	Successful	Bacillus subtilis tolerance of moderate concentrations of rifampin involves the sigma(B)-dependent general and multiple stress response. J Bacteriol. 2002 Jan;184(2):459-67.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3WAD0	HLA-A02/AFP complex (HLA-A02/AFP)	NO-UNIPROT	NOUNIPROTAC	.	HLA-A2/AFP complex	HLA-A02/AFP	.	.	.	.	Clinical trial	ClinicalTrials.gov (NCT03349255) Clinical Study of ET1402L1-CAR T Cells in AFP Expressing Hepatocellular Carcinoma	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYG378	Tuftsin receptor (TR)	NO-UNIPROT	NOUNIPROTAC	.	.	TR	.	.	.	.	Clinical trial	"WO patent application no. 2013,1850,32, Nanotherapeutics for drug targeting."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQ5XI3	Glycoprotein Ib-IX-V receptor (GPIbIXV)	NO-UNIPROT	NOUNIPROTAC	.	Glycoprotein Ib-IX-V; Glycoprotein (GP) Ib-IX-V; GP Ib-IX-V	GPIbIXV	.	.	.	.	Literature-reported	Glycoprotein Ib-IX-V. Int J Biochem Cell Biol. 2003 Aug;35(8):1170-4.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTSFNKW	Tumor antigen NGcGM3 (NGcGM3)	NO-UNIPROT	NOUNIPROTAC	.	Tumor antigen N-glycolyl-GM3	NGcGM3	.	.	.	.	Clinical trial	Racotumomab: an anti-idiotype vaccine related to N-glycolyl-containing gangliosides - preclinical and clinical data. Front Oncol. 2012; 2: 150.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTDM9GW	Hepatitis C virus Nucleoside triphosphatase (HCV NTP)	NO-UNIPROT	NOUNIPROTAC	.	Nucleoside-triphosphatase; Nucleoside triphosphate phosphohydrolase; NTPase; MJ0226	HCV NTP	"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."	.	.	.	Literature-reported	Nucleotide triphosphatase/helicase of hepatitis C virus as a target for antiviral therapy. Antiviral Res. 2002 Sep;55(3):397-412.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT6EYVN	Peripheral carotid chemoreceptor (PCC)	NO-UNIPROT	NOUNIPROTAC	.	.	PCC	.	.	.	.	Successful	Ovalbumin sensitization alters the ventilatory responses to chemical challenges in guinea pigs. J Appl Physiol (1985). 2005 Nov;99(5):1782-8.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTTG60L	CAP-dependent endonuclease (CDE)	NO-UNIPROT	NOUNIPROTAC	.	.	CDE	.	.	.	.	Discontinued	"Synthesis of natural flutimide and analogous fully substituted pyrazine-2,6-diones, endonuclease inhibitors of influenza virus. J Org Chem. 2001 Aug 10;66(16):5504-16."	5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNSUK0	Protein thiol group (PTG)	NO-UNIPROT	NOUNIPROTAC	.	.	PTG	.	.	.	.	Discontinued	Antieosinophilic activity of orazipone. Mol Pharmacol. 2006 Jun;69(6):1861-70.	3	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOASGR	Neuroepithelial receptor (NR)	NO-UNIPROT	NOUNIPROTAC	.	.	NR	.	.	.	.	Clinical trial	Patents by Assignee Pherin Corporation.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTPV9O1	Cancer stemness kinase (CSK)	NO-UNIPROT	NOUNIPROTAC	.	.	CSK	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTR6P2Z	Imidazoline I2 receptor (I2R)	NO-UNIPROT	NOUNIPROTAC	.	.	I2R	.	.	.	.	Literature-reported	Antinociceptive effects of imidazoline I2 receptor agonists in the formalin test in rats. Behav Pharmacol. 2016 Jun;27(4):377-83.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTV75BJ	Carbohydrate antigen Lewis-Y (Lewis-Y)	NO-UNIPROT	NOUNIPROTAC	.	Lewis-Y carbohydrate antigen; Lewis-Y	Lewis-Y	.	.	.	.	Clinical trial	ClinicalTrials.gov (NCT03198052) HER2/Mesothelin/Lewis-Y/PSCA/MUC1/PD-L1/CD80/86-CAR-T Cells Immunotherapy Against Cancers	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTX35ZM	Tumor-associated glycoprotein 72 (TAG-72)	NO-UNIPROT	NOUNIPROTAC	.	.	TAG-72	.	.	.	.	Successful	Indium-111 satumomab pendetide: the first FDA-approved monoclonal antibody for tumor imaging. J Nucl Med Technol. 1998 Sep;26(3):155-63; quiz 170-1.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTA5LWY	M1-prime segment of membrane-expressed IgE (M1 IgE)	NO-UNIPROT	NOUNIPROTAC	.	.	M1 IgE	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of Genentech (2011)."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTFNSPC	Mechanistic target of rapamycin complex 3 (mTORC3)	NO-UNIPROT	NOUNIPROTAC	.	.	mTORC3	.	.	.	.	Literature-reported	ETV7 is an essential component of a rapamycin-insensitive mTOR complex in cancer. Sci Adv. 2018 Sep 12;4(9):eaar3938.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUIFO6	Human immunodeficiency virus Adenovector Ad35 (HIV Ad35)	NO-UNIPROT	NOUNIPROTAC	.	.	HIV Ad35	.	.	.	.	Clinical trial	ClinicalTrials.gov (NCT00123968) Safety of and Immune Response to an HIV-1 Vaccine (VRC-HIVDNA016-00-VP) and a Vaccine Booster (VRC-HIVADV014-00-VP) in HIV Uninfected East African Adults. U.S. National Institutes of Health.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT9GOIR	Streptococcus Diphtheria protein (Stre DIPP)	NO-UNIPROT	NOUNIPROTAC	.	.	Stre DIPP	.	.	.	.	Successful	Patent WO2013131983 A1.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTC6JZQ	Haemophilus influenzae CRM197 (Hae-influ CRM197)	NO-UNIPROT	NOUNIPROTAC	.	.	Hae-influ CRM197	.	.	.	.	Clinical trial	ClinicalTrials.gov (NCT02140047) Exploratory Clinical Study of MT-2301. U.S. National Institutes of Health.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYHBSN	Nerve/glial antigen-2 (NG2)	NO-UNIPROT	NOUNIPROTAC	.	Tubulin protein	NG2	.	.	.	.	Literature-reported	Nerve/Glial Antigen 2: A Novel Target for Anti-Tumor Therapy in Colorectal Cancer. Digestion. 2017;96(1):60-66.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQ1DP3	CoA-independent transacylase (CIT)	NO-UNIPROT	NOUNIPROTAC	Acyltransferase	Glycerophospholipid arachidonoyl-transferase(CoA-independent); Coenzyme A-independent transacylase; CoA-IT; 1-alkylglycerophosphocholine Acyltransferase	CIT	.	.	.	.	Literature-reported	Anti-CD3 and concanavalin A-induced human T cell proliferation is associated with an increased rate of arachidonate-phospholipid remodeling. Lack o... J Biol Chem. 2001 May 18;276(20):17568-75.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT1HM0R	Kappa myeloma antigen (KMA)	NO-UNIPROT	NOUNIPROTAC	Kappa myeloma antigen	.	KMA	.	.	.	.	Clinical trial	MDX-1097 induces antibody-dependent cellular cytotoxicity against kappa multiple myeloma cells and its activity is augmented by lenalidomide. Br J Haematol. 2015 May;169(3):333-43.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTAVH2G	Cytochrome P450 2B2 (CYP2B2)	NO-UNIPROT	NOUNIPROTAC	Paired donor oxygen oxidoreductase	Cytochrome P450E; Cytochrome P450 PB4; Cyp2b2; Cyp2b-2; CYPIIB2	CYP2B2	"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."	.	.	.	Literature-reported	"DrugBank: a knowledgebase for drugs, drug actions and drug targets. Nucleic Acids Res. 2008 Jan;36(Database issue):D901-6."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTGF64I	microRNA hsa-miR-199a (MIR199a)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR199a	.	.	.	.	Literature-reported	MiR-199a suppresses prostate cancer paclitaxel resistance by targeting YES1. World J Urol. 2018 Mar;36(3):357-365.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTBXRSK	microRNA hsa-miR-132 (MIR132)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR132	.	.	.	.	Literature-reported	Advances in Roles of miR-132 in the Nervous System. Front Pharmacol. 2017 Oct 25;8:770.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3ULBR	microRNA hsa-miR-191 (MIR191)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR191	.	.	.	.	Literature-reported	hsa-miR-191 is a candidate oncogene target for hepatocellular carcinoma therapy. Cancer Res. 2010 Oct 15;70(20):8077-87.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJCBTE	microRNA hsa-miR-1269a (MIR1269a)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR1269a	.	.	.	.	Literature-reported	MiR-1269a acts as an onco-miRNA in non-small cell lung cancer via down-regulating SOX6. Eur Rev Med Pharmacol Sci. 2018 Aug;22(15):4888-4897.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTVPGU3	microRNA hsa-miR-100 (MIR100)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR100	.	.	.	.	Literature-reported	"Potential role of miR-100 in cancer diagnosis, prognosis, and therapy. Tumour Biol. 2015 Mar;36(3):1403-9."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTSXL1N	microRNA hsa-miR-130b (MIR130b)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR130b	.	.	.	.	Literature-reported	miR-130b targets NKD2 and regulates the Wnt signaling to promote proliferation and inhibit apoptosis in osteosarcoma cells. Biochem Biophys Res Commun. 2016 Mar 18;471(4):479-85.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYJH6B	microRNA hsa-miR-455 (MIR455)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR455	.	.	.	.	Literature-reported	miR-455 inhibits breast cancer cell proliferation through targeting CDK14. Eur J Pharmacol. 2017 Jul 15;807:138-143.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTC3TFX	microRNA hsa-miR-181a (MIR181a)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR181a	.	.	.	.	Literature-reported	Inhibition of miR-181a protects female mice from transient focal cerebral ischemia by targeting astrocyte estrogen receptor-. Mol Cell Neurosci. 2017 Jul;82:118-125.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT9ZCFQ	microRNA hsa-miR-9 (MIR9)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR9	.	.	.	.	Literature-reported	miR-124 and miR-9 mediated downregulation of HDAC5 promotes neurite development through activating MEF2C-GPM6A pathway. J Cell Physiol. 2018 Jan;233(1):673-687.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTD81JK	microRNA hsa-miR-152 (MIR152)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR152	.	.	.	.	Literature-reported	miR-152 as a tumor suppressor microRNA: Target recognition and regulation in cancer. Oncol Lett. 2016 Jun;11(6):3911-3916.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQSK01	microRNA hsa-miR-183 (MIR183)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR183	.	.	.	.	Literature-reported	MiR-21 and miR-183 can simultaneously target SOCS6 and modulate growth and invasion of hepatocellular carcinoma (HCC) cells. Eur Rev Med Pharmacol Sci. 2015 Sep;19(17):3208-17.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYAR63	microRNA hsa-miR-1280 (MIR1280)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR1280	.	.	.	.	Literature-reported	tRF/miR-1280 Suppresses Stem Cell-like Cells and Metastasis in Colorectal Cancer. Cancer Res. 2017 Jun 15;77(12):3194-3206.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT9IGC3	microRNA hsa-miR-621 (MIR621)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR621	.	.	.	.	Literature-reported	Downregulated miR-621 promotes cell proliferation via targeting CAPRIN1 in hepatocellular carcinoma. Am J Cancer Res. 2018 Oct 1;8(10):2116-2129.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTEHZXM	microRNA hsa-miR-30d (MIR30d)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR30d	.	.	.	.	Literature-reported	miR-30d is related to asbestos exposure and inhibits migration and invasion in NCI-H2452 cells. FEBS Open Bio. 2017 Aug 30;7(10):1469-1479.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT68KIU	microRNA hsa-miR-371-5p (MIR371-5p)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR371-5p	.	.	.	.	Literature-reported	miR-371-5p suppresses the proliferative and migratory capacity of human nasopharyngeal carcinoma by targeting BCL2. Oncol Lett. 2018 Jun;15(6):9209-9215.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTL2KO8	Small nucleolar RNA 40 (snoRNA40)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	snoRNA40	.	.	.	.	Literature-reported	Identification of ncRNAs as potential therapeutic targets in multiple sclerosis through differential ncRNA - mRNA network analysis. BMC Genomics. 2015 Mar 28;16:250.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2J1RT	microRNA hsa-miR-212 (MIR212)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR212	.	.	.	.	Literature-reported	Effect of miR-212 targeting TCF7L2 on the proliferation and metastasis of cervical cancer. Eur Rev Med Pharmacol Sci. 2017 Jan;21(2):219-226.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJLWTC	microRNA hsa-miR-182 (MIR182)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR182	.	.	.	.	Literature-reported	Contradicting roles of miR-182 in both NK cells and their host target hepatocytes in HCV. Immunol Lett. 2016 Jan;169:52-60.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJVKAN	microRNA hsa-miR-26a (MIR26a)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR26a	.	.	.	.	Literature-reported	MiR-26a and miR-26b mediate osteoarthritis progression by targeting FUT4 via NF-B signaling pathway. Int J Biochem Cell Biol. 2018 Jan;94:79-88.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT6HUWO	microRNA hsa-miR-129-5p (MIR129-5p)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR129-5p	.	.	.	.	Literature-reported	MiR-129-5p suppresses gastric cancer cell invasion and proliferation by inhibiting COL1A1. Biochem Cell Biol. 2018 Feb;96(1):19-25.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTRZTXD	microRNA hsa-miR-96 (MIR96)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR96	.	.	.	.	Literature-reported	"miR-96 targets SOX6 and promotes proliferation, migration, and invasion of hepatocellular carcinoma. Biochem Cell Biol. 2018 Jun;96(3):365-371."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTH12DY	microRNA hsa-miR-185 (MIR185)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR185	.	.	.	.	Literature-reported	MiR-185 inhibits 3T3-L1 cell differentiation by targeting SREBP-1. Biosci Biotechnol Biochem. 2017 Sep;81(9):1747-1754.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT7OE0A	microRNA hsa-miR-194 (MIR194)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR194	.	.	.	.	Literature-reported	miR-194 targets RBX1 gene to modulate proliferation and migration of gastric cancer cells. Tumour Biol. 2015 Apr;36(4):2393-401.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3NJX2	microRNA hsa-miR-329 (MIR329)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR329	.	.	.	.	Literature-reported	MiR-329 suppresses osteosarcoma development by downregulating Rab10. FEBS Lett. 2016 Sep;590(17):2973-81.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTIB5L1	microRNA hsa-miR-375 (MIR375)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR375	.	.	.	.	Literature-reported	miR-375 Regulates Invasion-Related Proteins Vimentin and L-Plastin. Am J Pathol. 2017 Jul;187(7):1523-1536.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMDPH8	Long intergenic noncoding RNA AATBC (lincRNA AATBC)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	lincRNA AATBC	.	.	.	.	Literature-reported	Knockdown of a novel lincRNA AATBC suppresses proliferation and induces apoptosis in bladder cancer. Oncotarget. 2015 Jan 20;6(2):1064-78.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTEA1FT	microRNA hsa-miR-133a (MIR133a)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR133a	.	.	.	.	Literature-reported	miR-133a acts as a tumor suppressor in colorectal cancer by targeting eIF4A1. Tumour Biol. 2017 May;39(5):1010428317698389.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTG8INV	microRNA hsa-miR-134 (MIR134)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR134	.	.	.	.	Literature-reported	miR-134: A Human Cancer Suppressor Mol Ther Nucleic Acids. 2017 Mar 17;6:140-149.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTO60BY	microRNA hsa-miR-29b (MIR29b)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR29b	.	.	.	.	Clinical trial	miR-29b contributes to multiple types of muscle atrophy. Nat Commun. 2017 May 25;8:15201.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTC9EYH	microRNA hsa-miR-30a (MIR30a)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR30a	.	.	.	.	Literature-reported	miR-30a as Potential Therapeutics by Targeting TET1 through Regulation of Drp-1 Promoter Hydroxymethylation in Idiopathic Pulmonary Fibrosis. Int J Mol Sci. 2017 Mar 15;18(3). pii: E633.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTFWOHQ	microRNA hsa-miR-22 (MIR22)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR22	.	.	.	.	Literature-reported	miR-22 Is a Novel Mediator of Vascular Smooth Muscle Cell Phenotypic Modulation and Neointima Formation. Circulation. 2018 Apr 24;137(17):1824-1841.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8TPWV	microRNA hsa-miR-509 (MIR509)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR509	.	.	.	.	Literature-reported	MALAT1 Promotes the Proliferation and Metastasis of Osteosarcoma Cells By Activating the Rac1/JNK Pathway Via Targeting MiR-509. Oncol Res. 2018 Apr 27. doi: 10.3727/096504017X14957939026111.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQRLOF	microRNA hsa-miR-105 (MIR105)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR105	.	.	.	.	Literature-reported	miR-105/Runx2 axis mediates FGF2-induced ADAMTS expression in osteoarthritis cartilage. J Mol Med (Berl). 2016 Jun;94(6):681-94.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQYUF5	microRNA hsa-miR-10b (MIR10b)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR10b	.	.	.	.	Literature-reported	miR-10b is a prognostic marker in clear cell renal cell carcinoma. J Clin Pathol. 2017 Oct;70(10):854-859.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT96IGO	microRNA hsa-miR-34 (MIR34)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR34	.	.	.	.	Clinical trial	Interpreting expression profiles of cancers by genome-wide survey of breadth of expression in normal tissues. Genomics 2005 Aug;86(2):127-41.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYJRBQ	microRNA hsa-miR-429 (MIR429)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR429	.	.	.	.	Literature-reported	MiR-429 suppresses glioblastoma multiforme by targeting SOX2. Cell Biochem Funct. 2017 Jul;35(5):260-268.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2H4DE	microRNA hsa-miR-18a (MIR18a)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR18a	.	.	.	.	Literature-reported	miR-18a induces myotubes atrophy by down-regulating IgfI. Int J Biochem Cell Biol. 2017 Sep;90:145-154.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMH5GE	microRNA hsa-miR-107 (MIR107)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR107	.	.	.	.	Literature-reported	Depleted tumor suppressor miR-107 in plasma relates to tumor progression and is a novel therapeutic target in pancreatic cancer. Sci Rep. 2017 Jul 18;7(1):5708.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTF5CVU	microRNA hsa-miR-210 (MIR210)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR210	.	.	.	.	Literature-reported	miR-210: a therapeutic target in cancer. Expert Opin Ther Targets. 2013 Jan;17(1):21-8.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3STGE	Small nucleolar RNA 78 (snoRNA78)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	snoRNA78	.	.	.	.	Literature-reported	Small nucleolar RNA 78 promotes the tumorigenesis in non-small cell lung cancer. J Exp Clin Cancer Res. 2015 May 15;34:49.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT47RZK	microRNA hsa-miR-302a (MIR302a)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR302a	.	.	.	.	Literature-reported	MiR-302a sensitizes leukemia cells to etoposide by targeting Rad52. Oncotarget. 2017 May 16;8(43):73884-73891.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTX2ITC	microRNA hsa-miR-572 (MIR572)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR572	.	.	.	.	Literature-reported	MiR-572 prompted cell proliferation of human ovarian cancer cells by suppressing PPP2R2C expression. Biomed Pharmacother. 2016 Feb;77:92-7.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTI4ERV	microRNA hsa-miR-30d-5p (MIR30d-5p)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR30d-5p	.	.	.	.	Literature-reported	miR-30d-5p Plays an Important Role in Autophagy and Apoptosis in Developing Rat Brains After Hypoxic-Ischemic Injury. J Neuropathol Exp Neurol. 2017 Aug 1;76(8):709-719.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTN4D5H	HOXA distal transcript antisense RNA (HOTTIP)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	HOTTIP	.	.	.	.	Literature-reported	The long noncoding RNA HOXA transcript at the distal tip promotes colorectal cancer growth partially via silencing of p21 expression. Tumour Biol. 2016 Jun;37(6):7431-40.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTY04XD	microRNA hsa-miR-1207-5p (MIR1207-5p)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR1207-5p	.	.	.	.	Literature-reported	hnRNPK-regulated PTOV1-AS1 modulates heme oxygenase-1 expression via miR-1207-5p. BMB Rep. 2017 Apr;50(4):220-225.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTFDOTL	microRNA hsa-miR-486 (MIR486)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR486	.	.	.	.	Literature-reported	MicroRNA 486 is a potentially novel target for the treatment of spinal cord injury. Brain. 2012 Apr;135(Pt 4):1237-52.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQOPIA	microRNA hsa-miR-144 (MIR144)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR144	.	.	.	.	Literature-reported	Hepatic miR-33a/miR-144 and their target gene ABCA1 are associated with steatohepatitis in morbidly obese subjects. Liver Int. 2016 Sep;36(9):1383-91.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOPT8D	microRNA hsa-miR-181c (MIR181c)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR181c	.	.	.	.	Literature-reported	miR-181c protects CsA-induced renal damage and fibrosis through inhibiting EMT. FEBS Lett. 2017 Nov;591(21):3588-3599.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJAFT2	microRNA hsa-miR-122 (MIR122)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR122	.	.	.	.	Literature-reported	Coordination of insulin and Notch pathway activities by microRNA miR-305 mediates adaptive homeostasis in the intestinal stem cells of the Drosophi... Genes Dev. 2014 Nov 1;28(21):2421-31.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTA2G3P	microRNA hsa-miR-33 (MIR33)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR33	.	.	.	.	Literature-reported	MiR-33 may be a Biological Marker for Coronary Heart Disease. Clin Lab. 2018 Oct 1;64(10):1755-1760.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8LA9O	microRNA hsa-miR-101 (MIR101)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR101	.	.	.	.	Literature-reported	MiR-101: a potential therapeutic target of cancers. Am J Transl Res. 2018 Nov 15;10(11):3310-3321.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2C5LO	microRNA hsa-miR-146a (MIR146a)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR146a	.	.	.	.	Literature-reported	The chemokine scavenging receptor D6/ACKR2 is a target of miR-146a in thyroid cancer. Genes Cancer. 2017 May;8(5-6):577-588.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZQYV0	microRNA hsa-miR-373 (MIR373)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR373	.	.	.	.	Literature-reported	MiR-205 and MiR-373 Are Associated with Aggressive Human Mucinous Colorectal Cancer. PLoS One. 2016 Jun 6;11(6):e0156871.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTP03CE	Hepatitis C virus microRNA miR-122 (HCV MIR122)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	HCV MIR122	.	.	.	.	Clinical trial	Company report (Isis Pharmaceuticals)	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOW189	microRNA hsa-miR-148a (MIR148a)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR148a	.	.	.	.	Literature-reported	miR-148a inhibits colitis and colitis-associated tumorigenesis in mice. Cell Death Differ. 2017 Dec;24(12):2199-2209.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT1W5LN	microRNA hsa-miR-143 (MIR143)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR143	.	.	.	.	Literature-reported	miR-143 and miR-145 inhibit gastric cancer cell migration and metastasis by suppressing MYO6. Cell Death Dis. 2017 Oct 12;8(10):e3101.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTR7S2C	microRNA hsa-miR-29c (MIR29c)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR29c	.	.	.	.	Literature-reported	The role of miR-29c/B7-H3 axis in children with allergic asthma. J Transl Med. 2018 Aug 3;16(1):218.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZJ0Q6	microRNA hsa-miR-206 (MIR206)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR206	.	.	.	.	Literature-reported	miR-206 Mediates YAP-Induced Cardiac Hypertrophy and Survival. Circ Res. 2015 Oct 23;117(10):891-904.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTF7CL8	microRNA hsa-miR-218 (MIR218)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR218	.	.	.	.	Literature-reported	miR-218 inhibited tumor angiogenesis by targeting ROBO1 in gastric cancer. Gene. 2017 Jun 5;615:42-49.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNDIAX	microRNA hsa-miR-214 (MIR214)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR214	.	.	.	.	Literature-reported	miR-214 promotes osteoclastogenesis by targeting Pten/PI3k/Akt pathway. RNA Biol. 2015;12(3):343-53.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3N0YA	microRNA hsa-miR-939 (MIR939)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR939	.	.	.	.	Literature-reported	Decreased expression of miR-939 contributes to chemoresistance and metastasis of gastric cancer via dysregulation of SLC34A2 and Raf/MEK/ERK pathway. Mol Cancer. 2017 Jan 23;16(1):18.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMK5ZC	H19 imprinted maternally expressed transcript (H19)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	H19	.	.	.	.	Literature-reported	The H19 gene: regulation and function of a non-coding RNA. Cytogenet Genome Res. 2006;113(1-4):188-93.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8EM6Q	microRNA hsa-miR-296 (MIR296)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR296	.	.	.	.	Literature-reported	miR-296 inhibits the metastasis and epithelial-mesenchymal transition of colorectal cancer by targeting S100A4. BMC Cancer. 2017 Feb 16;17(1):140.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQD4FU	microRNA hsa-miR-664 (MIR664)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR664	.	.	.	.	Literature-reported	Overexpression of miR-664 is associated with enhanced osteosarcoma cell migration and invasion ability via targeting SOX7. Clin Exp Med. 2017 Feb;17(1):51-58.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTKH1NI	microRNA hsa-miR-21 (MIR21)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR21	.	.	.	.	Literature-reported	"miR-21, An Oncogenic Target miRNA for Cancer Therapy: Molecular Mechanisms and Recent Advancements in Chemo and Radio-resistance. Curr Gene Ther. 2017;16(6):375-389."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT6ZE4S	microRNA hsa-miR-223-3p (MIR223-3p)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR223-3p	.	.	.	.	Literature-reported	MiR-223-3p inhibits angiogenesis and promotes resistance to cetuximab in head and neck squamous cell carcinoma. Oncotarget. 2017 Jul 11;8(34):57174-57186.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT1GNRQ	microRNA hsa-miR-155 (MIR155)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR155	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTIWTFQ	microRNA hsa-miR-709 (MIR709)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR709	.	.	.	.	Literature-reported	MicroRNA-709 Mediates Acute Tubular Injury through Effects on Mitochondrial Function. J Am Soc Nephrol. 2018 Feb;29(2):449-461.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTKZVCO	microRNA hsa-miR-7 (MIR7)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR7	.	.	.	.	Literature-reported	"Identification of direct target genes of miR-7, miR-9, miR-96, and miR-182 in the human breast cancer cell lines MCF-7 and MDA-MB-231. Mol Cell Probes. 2017 Aug;34:45-52."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTIWODE	microRNA hsa-miR-451 (MIR451)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR451	.	.	.	.	Literature-reported	MiR-451 as a new tumor marker for gastric cancer. Oncotarget. 2017 Apr 19;8(34):56542-56545.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUCLSH	microRNA hsa-miR-23a (MIR23a)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR23a	.	.	.	.	Literature-reported	miR-23a acts as an oncogene in pancreatic carcinoma by targeting FOXP2. J Investig Med. 2018 Mar;66(3):676-683.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMRFN9	microRNA hsa-miR-197-3p (MIR197-3p)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR197-3p	.	.	.	.	Literature-reported	MicroRNA-197-3p acts as a prognostic marker and inhibits cell invasion in hepatocellular carcinoma. Oncol Lett. 2019 Feb;17(2):2317-2327.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTKMAOQ	microRNA hsa-miR-492 (MIR492)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR492	.	.	.	.	Literature-reported	MiR-492 regulates metastatic properties of hepatoblastoma via CD44. Liver Int. 2018 Jul;38(7):1280-1291.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTEA4LW	Long intergenic noncoding RNA p21 (lincRNA p21)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	lincRNA p21	.	.	.	.	Literature-reported	Long intergenic noncoding RNA-p21 inhibits apoptosis by decreasing PUMA expression in non-small cell lung cancer. J Int Med Res. 2019 Jan;47(1):481-493.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8VA5M	Epstein-Barr virus microRNA miR-BART1 (EBV MIRBART1)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	EBV MIRBART1	.	.	.	.	Literature-reported	EBV-miR-BART1 is involved in regulating metabolism-associated genes in nasopharyngeal carcinoma. Biochem Biophys Res Commun. 2013 Jun 21;436(1):19-24.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8AJ6S	microRNA hsa-miR-188 (MIR188)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR188	.	.	.	.	Literature-reported	miR-188 promotes senescence of lineage-negative bone marrow cells by targeting MAP3K3 expression. FEBS Lett. 2017 Aug;591(15):2290-2298.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTB7DYX	microRNA hsa-miR-1271 (MIR1271)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR1271	.	.	.	.	Literature-reported	"miR-1271 regulates cisplatin resistance of human gastric cancer cell lines by targeting IGF1R, IRS1, mTOR, and BCL2. Anticancer Agents Med Chem. 2014;14(6):884-91."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTDGEIH	microRNA hsa-miR-200c (MIR200c)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR200c	.	.	.	.	Literature-reported	"miR-200c: a versatile watchdog in cancer progression, EMT, and drug resistance. J Mol Med (Berl). 2016 Jun;94(6):629-44."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTI7YU2	microRNA hsa-miR-205 (MIR205)	microRNA/lncRNA	NOUNIPROTAC	Non-coding RNA target	.	MIR205	.	.	.	.	Literature-reported	Upregulation of MiR-205 transcriptionally suppresses SMAD4 and PTEN and contributes to human ovarian cancer progression. Sci Rep. 2017 Feb 1;7:41330.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQMWCG	Human immunodeficiency virus RNA (HIV RNA)	microRNA/lncRNA	NOUNIPROTAC	.	.	HIV RNA	.	.	.	.	Literature-reported	Specificity of neomycin analogues bound to the packaging region of human immunodeficiency virus type 1 RNA. Bioorg Med Chem. 2004 Apr 15;12(8):1835-43.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTPFQ0C	HOX transcript antisense RNA (HOTAIR)	microRNA/lncRNA	NOUNIPROTAC	.	.	HOTAIR	.	.	.	.	Literature-reported	Expression level and clinical significance of HOX transcript antisense intergenic RNA in cervical cancer: a meta-analysis. Sci Rep. 2016 Nov 29;6:38047.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTIA0J5	Bacterial 70S ribosomal RNA (Bact 70S rRNA)	microRNA/lncRNA	NOUNIPROTAC	.	.	Bact 70S rRNA	.	.	.	.	Successful	Interaction between the ribosomal subunits: 16S rRNA suppressors of the lethal DeltaA1916 mutation in the 23S rRNA of Escherichia coli. Mol Genet Genomics. 2007 Sep;278(3):307-15.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUWYEA	Bacterial 50S ribosomal RNA (Bact 50S rRNA)	microRNA/lncRNA	NOUNIPROTAC	.	.	Bact 50S rRNA	"Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA."	.	.	.	Successful	2014 FDA drug approvals. Nat Rev Drug Discov. 2015 Feb;14(2):77-81.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOVFH2	Bacterial 30S ribosomal RNA (Bact 30S rRNA)	microRNA/lncRNA	NOUNIPROTAC	.	.	Bact 30S rRNA	.	.	.	.	Successful	The antibiotic Furvina targets the P-site of 30S ribosomal subunits and inhibits translation initiation displaying start codon bias. Nucleic Acids Res. 2012 Nov 1;40(20):10366-74.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTIXJ2S	microRNA hsa-miR-92 (MIR92)	microRNA/lncRNA	NOUNIPROTAC	.	.	MIR92	.	.	.	.	Clinical trial	Efficiency and Target Derepression of Anti-miR-92a: Results of a First in Human Study. Nucleic Acid Ther. 2020 Dec;30(6):335-345.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT38DW5	Bacterial 16S ribosomal RNA (Bact 16S rRNA)	microRNA/lncRNA	NOUNIPROTAC	.	RrnS; Plastid 16S rRNA; 16S rRNA	Bact 16S rRNA	.	.	.	.	Successful	Antistaphylococcal activity of gentamicin. Minerva Med. 1975 Dec 8;66(84):4505-26.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTNSXG2	Human immunodeficiency virus TAR RNA (HIV TAR-RNA)	microRNA/lncRNA	NOUNIPROTAC	.	.	HIV TAR-RNA	.	.	.	.	Literature-reported	RNA as a target for small molecules. Curr Opin Chem Biol. 2000 Dec;4(6):678-86.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMGJ19	microRNA hsa-miR-17 (MIR17)	microRNA/lncRNA	NOUNIPROTAC	.	.	MIR17	.	.	.	.	Clinical trial	Discovery and preclinical evaluation of anti-miR-17 oligonucleotide RGLS4326 for the treatment of polycystic kidney disease. Nat Commun. 2019 Sep 12;10(1):4148.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTLFGBV	Bacterial 23S ribosomal RNA (Bact 23S rRNA)	microRNA/lncRNA	NOUNIPROTAC	.	RrnL; Plastid 23S rRNA	Bact 23S rRNA	.	.	.	.	Successful	Genome sequencing of linezolid-resistant Streptococcus pneumoniae mutants reveals novel mechanisms of resistance. Genome Res. 2009 Jul;19(7):1214-23.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTR6NV2	Lactobacillus 16S rRNA (Lacto 16RNA)	microRNA/lncRNA	NOUNIPROTAC	.	.	Lacto 16RNA	.	.	.	.	Literature-reported	Lactobacillus casei Shirota Supplementation Does Not Restore Gut Microbiota Composition and Gut Barrier in Metabolic Syndrome: A Randomized Pilot S... PLoS One. 2015 Oct 28;10(10):e0141399.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZALHD	Protein kinase C messenger RNA (PKC mRNA)	Family	NOUNIPROTAC	mRNA target	mRNA of PKC	PKC mRNA	.	.	.	.	Literature-reported	Technology evaluation: ISIS-3521. Curr Opin Mol Ther. 1999 Jun;1(3):393-8.	.	mRNA	.	.	.	.	.	.	.	.	.	.	.	.	.
TTH754E	Lentivirus messenger RNA (Lentivirus mRNA)	Family	NOUNIPROTAC	mRNA target	mRNA of Lentivirus	Lentivirus mRNA	.	.	.	.	Literature-reported	Effect of targeted silencing of hTERT mRNA by lentivirus-mediated siRNA on A549 lung cancer cells in vitro. Mol Biol Rep. 2013 Jan;40(1):605-16.	.	mRNA	.	.	.	.	.	.	.	.	.	.	.	.	.
TTDW3Z2	Telomerase messenger RNA (Telomerase mRNA)	Family	NOUNIPROTAC	mRNA target	mRNA of Terminal transferase	Telomerase mRNA	.	.	.	.	Discontinued	Combination therapy of 2-5A antisense against telomerase RNA and cisplatin for malignant gliomas. Int J Oncol. 2001 Jun;18(6):1287-92.	5	mRNA	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMQ2WK	Protein kinase A1 messenger RNA (PKA mRNA)	Family	NOUNIPROTAC	mRNA target	mRNA of PKA	PKA mRNA	.	.	.	.	Literature-reported	"Combined targeted inhibition of bcl-2, bcl-XL, epidermal growth factor receptor, and protein kinase A type I causes potent antitumor, apoptotic, and antiangiogenic activity. Clin Cancer Res. 2003 Feb;9(2):866-71."	.	mRNA	.	.	.	.	.	.	.	.	.	.	.	.	.
TTSXP1G	Protein kinase A alpha messenger RNA (PKA-alpha mRNA)	Family	NOUNIPROTAC	mRNA target	mRNA of PKA alpha	PKA-alpha mRNA	.	.	.	.	Literature-reported	Antitumor activity and pharmacokinetics of a mixed-backbone antisense oligonucleotide targeted to the RIalpha subunit of protein kinase A after oral administration. Proc Natl Acad Sci U S A. 1999 Nov23;96(24):13989-94.	0	mRNA	.	.	.	.	.	.	.	.	.	.	.	.	.
TT43YWN	Hepatitis B virus messenger RNA (HBV mRNA)	Family	NOUNIPROTAC	mRNA target	mRNA of HBV protein	HBV mRNA	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of ISIS Pharmaceuticals."	21	mRNA	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXQFV2	Protein kinase A Ri alpha messenger RNA (PKA-Ri-alpha mRNA)	Family	NOUNIPROTAC	mRNA target	mRNA of PKA Ri alpha	PKA-Ri-alpha mRNA	.	.	.	.	Literature-reported	Antitumor activity and pharmacokinetics of a mixed-backbone antisense oligonucleotide targeted to the RIalpha subunit of protein kinase A after oral administration. Proc Natl Acad Sci U S A. 1999 Nov23;96(24):13989-94.	0	mRNA	.	.	.	.	.	.	.	.	.	.	.	.	.
TTC50YZ	Inflammatory cytokine messenger RNA (Cytokine mRNA)	Family	NOUNIPROTAC	mRNA target	mRNA of Inflammatory cytokine	Cytokine mRNA	.	.	.	.	Literature-reported	Predictive value of intratumour inflammatory cytokine mRNA levels of hepatocellular carcinoma patients and activation of two distinct pathways gove... Cytokine. 2019 Jul;119:81-89.	.	mRNA	.	.	.	.	.	.	.	.	.	.	.	.	.
TTU8HT1	Ubiquitin-activating enzyme (UBA)	Family	NOUNIPROTAC	.	.	UBA	.	.	.	.	Clinical trial	National Cancer Institute Drug Dictionary (drug id 757275).	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT53E8H	Amine oxidase (AO)	Family	NOUNIPROTAC	.	Amine oxidase (copper-containing); AOC	AO	.	.	.	.	Literature-reported	Novel monoamine oxidase inhibitors: a patent review (2012 - 2014).Expert Opin Ther Pat. 2015 Jan;25(1):91-110.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTSBIMH	GPCR frizzled protein unspecific (GPCRF)	Family	NOUNIPROTAC	.	.	GPCRF	.	.	.	.	Literature-reported	Frizzled Receptors in Development and Disease. Curr Top Dev Biol. 2016;117:113-39.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTCY4SB	Aurora kinase (AURK)	Family	NOUNIPROTAC	.	Serine/threonine kinase	AURK	.	.	.	.	Clinical trial	Cyclin-dependent kinase inhibitors for cancer therapy: a patent review (2009 - 2014).Expert Opin Ther Pat. 2015;25(9):953-70.	15.5	.	Protein kinase superfamily. Ser/Thr protein kinase family	.	.	.	.	.	.	.	.	.	.	.	.
TTZBFA0	Protease unspecific (PRO)	Family	NOUNIPROTAC	.	.	PRO	.	.	.	.	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. 2015	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUS05D	Nucleoside DNA polymerase (DPOL)	Family	NOUNIPROTAC	.	.	DPOL	.	.	.	.	Clinical trial	Progress in the Development of New Therapies for Herpesvirus Infections. Curr Opin Virol. 2011 December 1; 1(6): 548-554.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3ZIJL	JNK-interacting protein peptide (pepJIP)	Family	NOUNIPROTAC	.	pepJIP	pepJIP	.	.	.	.	Patented-recorded	c-Jun N-terminal kinase inhibitors: a patent review (2010 - 2014).Expert Opin Ther Pat. 2015;25(8):849-72.	15.5	.	JIP scaffold family	.	.	.	.	.	.	.	.	.	.	.	.
TTZC3G5	Lysine-specific histone demethylase (LSD)	Family	NOUNIPROTAC	.	.	LSD	.	.	.	.	Literature-reported	Lysine-specific histone demethylases in normal and malignant hematopoiesis. Exp Hematol. 2016 Sep;44(9):778-782.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTWFZ1N	Dopamine receptor (DR)	Family	NOUNIPROTAC	.	Human dopamine receptor	DR	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	.	G-protein coupled receptor 1 family	.	.	.	.	.	.	.	.	.	.	.	.
TTKA1M6	Catenin (CTNN)	Family	NOUNIPROTAC	.	.	CTNN	.	.	.	.	Literature-reported	beta-catenin is a target for the ubiquitin-proteasome pathway. EMBO J. 1997 Jul 1;16(13):3797-804.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTO32GK	P-glycoprotein (P-GP)	Family	NOUNIPROTAC	.	.	P-GP	.	.	.	.	Discontinued	Communication between multiple drug binding sites on P-glycoprotein. Mol Pharmacol. 2000 Sep;58(3):624-32.	3	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5WKM8	ATP phosphatase (ATPase)	Family	NOUNIPROTAC	.	.	ATPase	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYCILE	Vasopressin receptor (VR)	Family	NOUNIPROTAC	.	Human vasopressin receptor	VR	.	.	.	.	Successful	Vasopressin V2 (SR121463A) and V1a (SR49059) receptor antagonists both inhibit desmopressin vasorelaxing activity. Eur J Pharmacol. 1999 Nov 3;383(3):287-90.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTCLA5K	Type II transmembrane serine proteases (TTSP)	Family	NOUNIPROTAC	.	.	TTSP	.	.	.	.	Literature-reported	The role of type II transmembrane serine protease-mediated signaling in cancer. FEBS J. 2017 May;284(10):1421-1436.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT60D9N	GPCR rhodopsin protein unspecific (GPCRA)	Family	NOUNIPROTAC	.	.	GPCRA	.	.	.	.	Literature-reported	G Protein-Coupled Receptors as Targets for Approved Drugs: How Many Targets and How Many Drugs Mol Pharmacol. 2018 Apr;93(4):251-258.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTO3HT7	Transforming growth factor beta (TGFB)	Family	NOUNIPROTAC	.	TGF-beta	TGFB	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTX1OI0	Galectin (LGALS)	Family	NOUNIPROTAC	.	.	LGALS	.	.	.	.	Clinical trial	"GCS-100, a novel galectin-3 antagonist, modulates MCL-1, NOXA, and cell cycle to induce myeloma cell death. Blood. 2010 May 13;115(19):3939-48."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTPZ7AG	Oxidoreductase unspecific (OR)	Family	NOUNIPROTAC	.	.	OR	.	.	.	.	Successful	Reaction mechanism of azoreductases suggests convergent evolution with quinone oxidoreductases. Protein Cell. 2010 Aug;1(8):780-90.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUX68I	Hypoxia-inducible factor 1 (HIF-1)	Family	NOUNIPROTAC	.	HIF-1	HIF-1	.	.	.	.	Patented-recorded	Hypoxia-inducible factor (HIF) inhibitors: a patent survey (2011-2015).Expert Opin Ther Pat. 2016;26(3):309-22.	15.5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTWLEZV	Aminopeptidase (AMP)	Family	NOUNIPROTAC	.	.	AMP	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTGWSKE	Bacterial Transpeptidase (Bact TPP)	Family	NOUNIPROTAC	.	.	Bact TPP	.	.	.	.	Literature-reported	Lipid II overproduction allows direct assay of transpeptidase inhibition by -lactams. Nat Chem Biol. 2017 Jul;13(7):793-798.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTDB5IS	Receptor unspecific (Rec)	Family	NOUNIPROTAC	.	.	Rec	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of Biotest."	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTG3K2U	Lipoxygenase (ALOX)	Family	NOUNIPROTAC	.	.	ALOX	.	.	.	.	Clinical trial	"Hydroxylamine analogs of 2,6-di-t-butylphenols: dual inhibitors of cyclooxygenase and 5-lipoxygenase or selective 5-lipoxygenase inhibitors. Bioorg Med Chem. 1995 Apr;3(4):403-10."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3C1VN	Enzyme unspecific (Enz)	Family	NOUNIPROTAC	.	.	Enz	.	.	.	.	Successful	"Methionine and cysteine affect glutathione level, glutathione-related enzyme activities and the expression of glutathione S-transferase isozymes in rat hepatocytes. J Nutr. 1997 Nov;127(11):2135-41."	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT0RGE9	Lysine-specific demethylase 4 (KDM4)	Family	NOUNIPROTAC	.	KDM4	KDM4	.	.	.	.	Patented-recorded	KDM4 histone demethylase inhibitors for anti-cancer agents: a patent review.Expert Opin Ther Pat. 2015 Feb;25(2):135-44.	15.5	.	JHDM3 histone demethylase family	.	.	.	.	.	.	.	.	.	.	.	.
TTC8NQ2	Lyase unspecific (LYA)	Family	NOUNIPROTAC	.	.	LYA	.	.	.	.	Clinical trial	"J Clin Oncol 30, 2012 (suppl; abstr e15167)."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2XHSJ	Secretory phospholipase A2 (sPLA2)	Family	NOUNIPROTAC	.	.	sPLA2	.	.	.	.	Clinical trial	Varespladib. Am J Cardiovasc Drugs. 2011;11(2):137-43.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOD7B3	Retinoic acid receptor (RAR)	Family	NOUNIPROTAC	.	Retinoic acid receptor	RAR	.	.	.	.	Successful	Retinoid agonist isotretinoin ameliorates obstructive renal injury. J Urol. 2003 Oct;170(4 Pt 1):1398-402.	34	.	Nuclear hormone receptor family	.	.	.	.	.	.	.	.	.	.	.	.
TTSCO7R	NAD-dependent deacetylase sirtuin (SIRT)	Family	NOUNIPROTAC	.	NAD+-dependent deacetylase SIRT	SIRT	.	.	.	.	Patented-recorded	Sirtuin modulators: an updated patent review (2012 - 2014).Expert Opin Ther Pat. 2015 Jan;25(1):5-15.	15.5	.	Sirtuin family	.	.	.	.	.	.	.	.	.	.	.	.
TTYHPRQ	Sodium pump (NaP)	Family	NOUNIPROTAC	.	.	NaP	.	.	.	.	Successful	Medicinal plants in therapy. Bull World Health Organ. 1985;63(6):965-81.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTRBPLN	DNA-binding protein inhibitor (ID)	Family	NOUNIPROTAC	.	.	ID	.	.	.	.	Literature-reported	"Increased hypermethylation of glutathione S-transferase P1, DNA-binding protein inhibitor, death associated protein kinase and paired box protein-5... Asian Pac J Cancer Prev. 2015;16(2):541-9."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTGMYVE	Phosphofructokinase 2 (PFK2)	Family	NOUNIPROTAC	.	.	PFK2	.	.	.	.	Clinical trial	A Pentadecapeptide Fragment of Islet Neogenesis-Associated Protein Increases Beta-Cell Mass and Reverses Diabetes in C57BL/6J Mice. Ann Surg. 2004 November; 240(5): 875-884.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTWFC4G	Netrin (NET)	Family	NOUNIPROTAC	.	.	NET	.	.	.	.	Clinical trial	"Striatal delivery of neurturin by CERE-120, an AAV2 vector for the treatment of dopaminergic neuron degeneration in Parkinson's disease. Mol Ther. 2007 Jan;15(1):62-8."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3J1EK	Zinc finger protein (ZNF)	Family	NOUNIPROTAC	.	.	ZNF	.	.	.	.	Clinical trial	"US patent application no. 2005,0239,723, Compositions and methods useful for treatment of acne."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5SZDC	Serine/threonine-protein phosphatase (PSP)	Family	NOUNIPROTAC	.	Protein serine/threonine phosphatase	PSP	.	.	.	.	Patented-recorded	Serine/Threonine Phosphatases in Atrial Fibrillation. J Mol Cell Cardiol. 2017 Feb;103:110-120.	.	.	PPP phosphatase family	.	.	.	.	.	.	.	.	.	.	.	.
TT3M2WO	Sphingosine kinase (SphK)	Family	NOUNIPROTAC	.	SphK	SphK	.	.	.	.	Patented-recorded	Sphingosine kinase inhibitors: a review of patent literature (2006-2015).Expert Opin Ther Pat. 2016 Dec;26(12):1409-1416.	15.5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTHKJLN	DNA-directed RNA polymerase (RNAP)	Family	NOUNIPROTAC	.	.	RNAP	.	.	.	.	Successful	Contribution of rpoB mutations to development of rifamycin cross-resistance in Mycobacterium tuberculosis. Antimicrob Agents Chemother. 1998 Jul;42(7):1853-7.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTBA9I1	Hematopoietic protein-tyrosine phosphatase (PTPN)	Family	NOUNIPROTAC	.	.	PTPN	.	.	.	.	Literature-reported	Hematopoietic cell phosphatase is recruited to CD22 following B cell antigen receptor ligation. J Biol Chem. 1995 Sep 1;270(35):20305-8.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT0LF7H	Fibroblast growth factor receptor (FGFR)	Family	NOUNIPROTAC	.	FGF receptor	FGFR	.	.	.	.	Successful	Tumor angiogenesis as a therapeutic target. Drug Discov Today. 2001 Oct 1;6(19):1005-1024.	31	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5WVU2	mRNA-decapping enzyme (DCP)	Family	NOUNIPROTAC	.	.	DCP	.	.	.	.	Literature-reported	Targeting Poxvirus Decapping Enzymes and mRNA Decay to Generate an Effective Oncolytic Virus. Mol Ther Oncolytics. 2018 Jan 31;8:71-81.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTBH0LA	Alpha-secretase (ASE)	Family	NOUNIPROTAC	.	.	ASE	.	.	.	.	Literature-reported	Alpha-secretase as a therapeutic target. Curr Alzheimer Res. 2007 Sep;4(4):412-7.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUPDWN	Cholinergic receptor unspecific (CHR)	Family	NOUNIPROTAC	.	.	CHR	.	.	.	.	Successful	Bradycardia produced by pyridostigmine and physostigmine. Can J Anaesth. 1997 Dec;44(12):1286-92.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTQSFTZ	Phosphoprotein phosphatases 1 (PP1)	Family	NOUNIPROTAC	.	Protein phosphatase 1	PP1	.	.	.	.	Patented-recorded	Ligands for Ser/Thr phosphoprotein phosphatases: a patent review (2005-2015).Expert Opin Ther Pat. 2016;26(3):389-407.	15.5	.	PPP phosphatase family	.	.	.	.	.	.	.	.	.	.	.	.
TT5BDCY	TGF-beta receptor (TGFBR)	Family	NOUNIPROTAC	.	.	TGFBR	.	.	.	.	Clinical trial	Phase I study of GC1008 (fresolimumab): a human anti-transforming growth factor-beta (TGF) monoclonal antibody in patients with advanced malignant melanoma or renal cell carcinoma.PLoS One.2014 Mar 11;9(3):e90353.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZTEFH	Major histocompatibility complex (MHC)	Family	NOUNIPROTAC	.	.	MHC	.	.	.	.	Discontinued	Molecular features of the hepatitis B virus nucleocapsid T-cell epitope 18-27: interaction with HLA and T-cell receptor. Hepatology. 1997 Oct;26(4):1027-34.	5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTEMV5X	Serine protease unspecific (SP)	Family	NOUNIPROTAC	.	.	SP	.	.	.	.	Successful	Randomized controlled trials of aprotinin in cardiac surgery: could clinical equipoise have stopped the bleeding Clin Trials. 2005;2(3):218-29; discussion 229-32.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2GPK3	DNA topoisomerase (TOP)	Family	NOUNIPROTAC	.	.	TOP	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2GVH5	Isomerase unspecific (IsoM)	Family	NOUNIPROTAC	.	.	IsoM	.	.	.	.	Discontinued	"Beneficial effect of CV-4151 (Isbogrel), a thromboxane A2 synthase inhibitor, in a rat middle cerebral artery thrombosis model. Thromb Res. 1995 Jul 1;79(1):95-107."	10	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT3V81G	Nuclear receptor unspecific (NR)	Family	NOUNIPROTAC	.	.	NR	.	.	.	.	Clinical trial	"Dehydroepiandrosterone activates endothelial cell nitric-oxide synthase by a specific plasma membrane receptor coupled to Galpha(i2,3). J Biol Chem. 2002 Jun 14;277(24):21379-88."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTI7S12	Glutamine receptor (GluR)	Family	NOUNIPROTAC	.	.	GluR	.	.	.	.	Successful	Natural products as sources of new drugs over the last 25 years. J Nat Prod. 2007 Mar;70(3):461-77.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTXEVN8	Transforming protein Rho (RHO)	Family	NOUNIPROTAC	.	.	RHO	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTVH35R	Opsin (OP)	Family	NOUNIPROTAC	.	.	OP	.	.	.	.	Literature-reported	The opsin repertoire of the European lancelet: a window into light detection in a basal chordate. Int J Dev Biol. 2017;61(10-11-12):763-772.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT0YOTH	Immunoglobulin gamma Fc receptor (FCGR)	Family	NOUNIPROTAC	.	.	FCGR	.	.	.	.	Literature-reported	The IgG Fc contains distinct Fc receptor (FcR) binding sites: the leukocyte receptors Fc gamma RI and Fc gamma RIIa bind to a region in the Fc dist... J Immunol. 2000 May 15;164(10):5313-8.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5JCZL	GDNF receptor complexes (GDNFR)	Family	NOUNIPROTAC	.	.	GDNFR	Receptor for GDNF. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor.	.	.	.	Literature-reported	GDNF family receptor complexes are emerging drug targets. Trends Pharmacol Sci. 2007 Feb;28(2):68-74.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTN4QDT	Opioid receptor (OPR)	Family	NOUNIPROTAC	.	Opioid receptor	OPR	.	.	.	.	Successful	Methadone treatment and its dangers. Medicina (Kaunas). 2009;45(5):419-25.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOMNR9	Somatostatin receptor (SSTR)	Family	NOUNIPROTAC	.	.	SSTR	.	.	.	.	Clinical trial	Peptide receptor radionuclide therapy with 177Lu-DOTATATE for patients with somatostatin receptor-expressing neuroendocrine tumors: the first US phase 2 experience. Pancreas. 2014 May;43(4):518-25.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTTM6W8	Melanin-concentrating hormone receptor (MCHR)	Family	NOUNIPROTAC	.	MCH receptor	MCHR	.	.	.	.	Literature-reported	Emerging drugs for obesity: linking novel biological mechanisms to pharmaceutical pipelines. Expert Opin Emerg Drugs. 2005 Aug;10(3):643-60.	2.1	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTX2N1T	Transferase unspecific (TF)	Family	NOUNIPROTAC	.	.	TF	.	.	.	.	Successful	"Antioxidant properties of remaxol, reamberin, and ademetionine in patients with drug-induced liver injury on the background of antituberculous therapy. Eksp Klin Farmakol. 2013;76(4):45-8."	31	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTFH2RS	FK506-binding protein (FKBP)	Family	NOUNIPROTAC	.	.	FKBP	.	.	.	.	Clinical trial	"Analysis of FK506, timcodar (VX-853) and FKBP51 and FKBP52 chaperones in control of glucocorticoid receptor activity and phosphorylation. Pharmacol Res Perspect. 2014 December; 2(6): e00076."	19	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2DLFI	Lysosphingolipid receptor (LSPR)	Family	NOUNIPROTAC	.	.	LSPR	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTGFK5X	Protein kinase unspecific (PK)	Family	NOUNIPROTAC	.	.	PK	.	.	.	.	Clinical trial	"Synthesis and evaluation of carbamoylmethylene linked prodrugs of BMS-582949, a clinical p38alpha inhibitor. Bioorg Med Chem Lett. 2013 May 15;23(10):3028-33."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTTWGIX	Leukotriene receptor (LTR)	Family	NOUNIPROTAC	.	Human leukotriene receptor	LTR	.	.	.	.	Clinical trial	"Effect of the leukotriene LTD4/LTE4 antagonist, SR 2640, in ulcerative colitis: an open clinical study. Prostaglandins Leukot Essent Fatty Acids. 1991 Mar;42(3):181-4."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZH7FT	Gluten (GLEN)	Family	NOUNIPROTAC	.	.	GLEN	.	.	.	.	Literature-reported	Stereotyped antibody responses target posttranslationally modified gluten in celiac disease. JCI Insight. 2017 Sep 7;2(17). pii: 93961.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT34I9F	Neoplasm antigen (NA)	Family	NOUNIPROTAC	.	.	NA	.	.	.	.	Clinical trial	National Cancer Institute Drug Dictionary (drug id 663436).	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTPFZJ1	Vasopressin V1 receptor (V1R)	Family	NOUNIPROTAC	.	Vasopressin receptor 1; ADH V1 receptor	V1R	.	.	.	.	Successful	"Human pain thresholds after the application of lypressin, a vasopressin analogue. Pharmacol Toxicol. 1987 Jul;61(1):16-9."	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOP3CH	Immunoglobulin unspecific (Ig)	Family	NOUNIPROTAC	.	.	Ig	.	.	.	.	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services. 2015	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZRQHU	Monocyte derived cytokine (MDC)	Family	NOUNIPROTAC	.	.	MDC	.	.	.	.	Literature-reported	A system for assessment of monokine gene expression using human whole blood. Genet Anal. 1995 Mar;12(1):39-43.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJP4SM	Bacterial Penicillin binding protein (Bact PBP)	Family	NOUNIPROTAC	.	.	Bact PBP	Cell wall formation.	.	.	.	Successful	"Role of penicillin-binding protein 2 (PBP2) in the antibiotic susceptibility and cell wall cross-linking of Staphylococcus aureus: evidence for the cooperative functioning of PBP2, PBP4, and PBP2A. JBacteriol. 2005 Mar;187(5):1815-24."	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT8CYO4	Endopeptidase (ENP)	Family	NOUNIPROTAC	.	.	ENP	.	.	.	.	Successful	"A comprehensive review of the pharmacodynamics, pharmacokinetics, and clinical effects of the neutral endopeptidase inhibitor racecadotril. Front Pharmacol. 2012 May 30;3:93."	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTEBCY8	Poly [ADP-ribose] polymerase (PARP)	Family	NOUNIPROTAC	.	Poly-ADP-ribose polymerase	PARP	.	.	.	.	Successful	2014 FDA drug approvals. Nat Rev Drug Discov. 2015 Feb;14(2):77-81.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT2QROC	Guanosine phosphotransferase (GPTase)	Family	NOUNIPROTAC	.	.	GPTase	.	.	.	.	Literature-reported	"Identification, partial purification and inhibition by guanine analogues of a novel enzymic activity which phosphorylates guanosine to GMP in the p... Biochem J. 1994 Mar 1;298 ( Pt 2):289-94."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTYJQTF	Immunoglobulin E (IgE)	Family	NOUNIPROTAC	.	IgE	IgE	.	.	.	.	Clinical trial	"International Nonproprietary Names for Pharmaceutical Substances (INN). WHO Drug Information, Vol. 25, No. 4, 2011"	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT9RTYG	Neuropeptide receptor (NPR)	Family	NOUNIPROTAC	.	.	NPR	.	.	.	.	Clinical trial	NNZ-2566 treatment inhibits neuroinflammation and pro-inflammatory cytokine expression induced by experimental penetrating ballistic-like brain injury in rats. J Neuroinflammation. 2009 Aug 5;6:19.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTANY71	AdoHcy hydrolase (SAHase)	Family	NOUNIPROTAC	.	AdoHcyase	SAHase	.	.	.	.	Literature-reported	Anti-HIV-1 activity of 3-deaza-adenosine analogs. Inhibition of S-adenosylhomocysteine hydrolase and nucleotide congeners. Eur J Biochem. 2003 Sep;270(17):3507-17.	2	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTE3PC9	Hepatitis C virus Non-structural 5 (HCV NS5)	Family	NOUNIPROTAC	.	.	HCV NS5	.	.	.	.	Clinical trial	Genotype and Subtype Profiling of PSI-7977 as a Nucleotide Inhibitor of Hepatitis C Virus. Antimicrob Agents Chemother. 2012 June; 56(6): 3359-3368.	19	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMNI76	Calcium-activated potassium channel (KCN)	Family	NOUNIPROTAC	.	Ca-activated K channel	KCN	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.	.	.	.	Successful	Chlorzoxazone inhibits contraction of rat thoracic aorta. Eur J Pharmacol. 2006 Sep 18;545(2-3):161-6.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTBLN9S	Sulfur mustard-stimulated protease (SMSP)	Family	NOUNIPROTAC	.	.	SMSP	.	.	.	.	Literature-reported	Sulfur mustard-stimulated protease: a target for antivesicant drugs. J Appl Toxicol. 2002 Mar-Apr;22(2):139-40.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZHSBO	Cytomegalovirus Terminase (CMV TRM)	Family	NOUNIPROTAC	.	.	CMV TRM	.	.	.	.	Successful	2017 FDA drug approvals.Nat Rev Drug Discov. 2018 Feb;17(2):81-85. 	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTR1XF8	Deoxyribonuclease (DNASE)	Family	NOUNIPROTAC	.	.	DNASE	.	.	.	.	Literature-reported	Deoxyribonuclease inhibitors. Eur J Med Chem. 2014 Dec 17;88:101-11.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTVC5K6	Estradiol 17 beta-dehydrogenase (17-beta-HSD)	Family	NOUNIPROTAC	.	.	17-beta-HSD	.	.	.	.	Literature-reported	"Trusted, scientifically sound profiles of drug programs, clinical trials, safety reports, and company deals, written by scientists. Springer. 2015. Adis Insight (drug id 800015540)"	2	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTVBH9I	TNF receptor-associated factor (TRAF)	Family	NOUNIPROTAC	.	TRAF; TNF-receptor-associated factor	TRAF	.	.	.	.	Literature-reported	TNF-receptor-associated factors as targets for drug development. Expert Opin Ther Targets. 2003 Jun;7(3):411-25.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTH6N8T	Cytochrome P450 3 (CYP3)	Family	NOUNIPROTAC	.	.	CYP3	.	.	.	.	Literature-reported	Phylogenetic analysis of the cytochrome P450 3 (CYP3) gene family. J Mol Evol. 2003 Aug;57(2):200-11.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5WF6D	Inflammatory cytokine (IC)	Family	NOUNIPROTAC	.	.	IC	.	.	.	.	Literature-reported	Inflammatory Cytokines and Alzheimer's Disease: A Review from the Perspective of Genetic Polymorphisms. Neurosci Bull. 2016 Oct;32(5):469-80.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTBMAOZ	Regulatory protein unspecific (RGP)	Family	NOUNIPROTAC	.	.	RGP	.	.	.	.	Clinical trial	Visilizumab induces apoptosis of mucosal T lymphocytes in ulcerative colitis through activation of caspase 3 and 8 dependent pathways. Clin Immunol. 2008 Jun;127(3):322-9.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTOK0LR	Toll-like receptor (TLR)	Family	NOUNIPROTAC	.	Toll-like receptor	TLR	.	.	.	.	Clinical trial	"UbiVac's DRibble, autophagosome-enriched vaccines: Applications for cancer and infectious disease. UbiVac. 2013."	21	.	Toll-like receptor family	.	.	.	.	.	.	.	.	.	.	.	.
TTV57E8	Interleukin receptor (ILR)	Family	NOUNIPROTAC	.	Interleukin receptor	ILR	.	.	.	.	Literature-reported	The interleukin-6 receptor as a target for prevention of coronary heart disease: a mendelian randomisation analysis. Lancet. 2012 Mar 31;379(9822):1214-24.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTG712R	Calprotectin (CP)	Family	NOUNIPROTAC	.	S100A9/S100A8; MRP8/MRP14 complex; MRP-8/MRP-14; Leucocyte protein L1; L1 protein; L1 antigen; Cytosolic protein complex L1	CP	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.	.	.	.	Literature-reported	"Calprotectin (S100A8/S100A9), an inflammatory protein complex from neutrophils with a broad apoptosis-inducing activity. Biol Pharm Bull. 2003 Jun;26(6):753-60."	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTTB3L1	Alpha-crystallin (CRYA)	Family	NOUNIPROTAC	.	.	CRYA	.	.	.	.	Preclinical	Different alpha crystallin expression in human age-related and congenital cataract lens epithelium. BMC Ophthalmol. 2016 May 28;16:67.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTML2WA	Tubulin (TUB)	Family	NOUNIPROTAC	.	Human tubulin	TUB	"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."	.	.	.	Successful	Mullard A: 2010 FDA drug approvals. Nat Rev Drug Discov. 2011 Feb;10(2):82-5.	34	.	Tubulin	.	.	.	.	.	.	.	.	.	.	.	.
TTJSQEF	Tyrosine-protein kinase (PTK)	Family	NOUNIPROTAC	.	Protein-tyrosine kinase; PTK	PTK	.	.	.	.	Successful	2018 FDA drug approvals.Nat Rev Drug Discov. 2019 Feb;18(2):85-89. 	34	.	Protein kinase superfamily. Tyr protein kinase family	.	.	.	.	.	.	.	.	.	.	.	.
TTQWUPT	Thyroid hormone receptor (THR)	Family	NOUNIPROTAC	.	.	THR	.	.	.	.	Clinical trial	Diiodothyropropionic Acid (DITPA) in the Treatment of MCT8 Deficiency	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUNARX	Carbonic anhydrase (CA)	Family	NOUNIPROTAC	.	Carbonate dehydratase	CA	.	.	.	.	Successful	Carbonic anhydrase inhibitors. Interaction of indapamide and related diuretics with 12 mammalian isozymes and X-ray crystallographic studies for th... Bioorg Med Chem Lett. 2008 Apr 15;18(8):2567-73.	34	.	Carbon-oxygen lyases	.	.	.	.	.	.	.	.	.	.	.	.
TT94IAG	Cannabinoid receptor (CB)	Family	NOUNIPROTAC	.	.	CB	.	.	.	.	Successful	(-)-Cannabidiol antagonizes cannabinoid receptor agonists and noradrenaline in the mouse vas deferens. Eur J Pharmacol. 2002 Dec 5;456(1-3):99-106.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTE8XGQ	Large subunit Cp complex Cdc68p (CDC68)	Family	NOUNIPROTAC	.	Cdc68p; CDC68	CDC68	.	.	.	.	Literature-reported	Validation of Cdc68p as a novel antifungal target. Arch Microbiol. 2002 Dec;178(6):428-36.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTMYPOH	Tumor-associated peptide (TAP)	Family	NOUNIPROTAC	.	Tumor associated peptide	TAP	.	.	.	.	Literature-reported	CD8+ T cells against multiple tumor-associated antigens in peripheral blood of midgut carcinoid patients. Cancer Immunol Immunother. 2008 Mar;57(3):399-409.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTEOSZT	Melanocortin receptor (MCR)	Family	NOUNIPROTAC	.	Melanocortin receptor	MCR	.	.	.	.	Clinical trial	Wikipedia: Bremelanotide	23	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5HONZ	Calcium channel unspecific (CaC)	Family	NOUNIPROTAC	.	.	CaC	.	.	.	.	Successful	Influence of bupropion and calcium channel antagonists on the nicotine-induced memory-related response of mice in the elevated plus maze. Pharmacol Rep. 2009 Mar-Apr;61(2):236-44.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT9B4N3	Prostaglandin receptor (PTGR)	Family	NOUNIPROTAC	.	.	PTGR	.	.	.	.	Successful	Comparison of the vasoactive effects of the docosanoid unoprostone and selected prostanoids on isolated perfused retinal arterioles. Invest Ophthalmol Vis Sci. 2001 Jun;42(7):1499-504.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTKAPQ1	Cholecystokinin receptor (CCKR)	Family	NOUNIPROTAC	.	.	CCKR	.	.	.	.	Literature-reported	"CN patent application no. 102481276, Chemosensory receptor ligand-based therapies."	2	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTA6KF7	C-X-C chemokine receptor (CXCR)	Family	NOUNIPROTAC	.	.	CXCR	.	.	.	.	Literature-reported	Constitutively active chemokine CXC receptors. Adv Pharmacol. 2014;70:265-301.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTRF7Q8	Natural killer cell receptor (NKCR)	Family	NOUNIPROTAC	.	.	NKCR	.	.	.	.	Clinical trial	In vitro stimulation with HBV therapeutic vaccine candidate Nasvac activates B and T cells from chronic hepatitis B patients and healthy donors. Mol Immunol. 2015 Feb;63(2):320-7.	25	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJQFBG	HIF-prolyl hydroxylase (HPH)	Family	NOUNIPROTAC	.	.	HPH	.	.	.	.	Successful	Drugs@FDA. U.S. Food and Drug Administration. U.S. Department of Health & Human Services.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTRAXK5	Aminotransferase (AT)	Family	NOUNIPROTAC	.	.	AT	.	.	.	.	Clinical trial	Expansion of the clavulanic acid gene cluster: identification and in vivo functional analysis of three new genes required for biosynthesis of clavulanic acid by Streptomyces clavuligerus. J Bacteriol. 2000 Jul;182(14):4087-95.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT79AOF	Transient receptor potential channel (TRP channel)	Family	NOUNIPROTAC	.	.	TRP channel	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTA6ZER	Immunoglobulin G1k (IgG1k)	Family	NOUNIPROTAC	.	.	IgG1k	.	.	.	.	Clinical trial	Advances in Sickle Cell Therapies in the Hydroxyurea Era. Mol Med. 2014; 20(Suppl 1): S37-S42.	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTRBUYN	Ribonuclease (RNase)	Family	NOUNIPROTAC	.	.	RNase	.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of Nanotherapeutics."	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTTMZSG	Clostridium difficile Toxin (CD tox)	Family	NOUNIPROTAC	.	.	CD tox	.	.	.	.	Clinical trial	Emerging therapies for Clostridium difficile infection - focus on fidaxomicin. Infect Drug Resist. 2013; 6: 41-53.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT1OQ4F	NEDD4-like E3 ubiquitin-protein ligase WWP (WWP)	Family	NOUNIPROTAC	.	.	WWP	.	.	.	.	Literature-reported	WW-Domain Containing Protein Roles in Breast Tumorigenesis. Front Oncol. 2018 Dec 13;8:580.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTI2WET	Platelet-derived growth factor receptor (PDGFR)	Family	NOUNIPROTAC	.	Platelet-derived growth factor receptor tyrosine kinase; PDGFR kinase; PDGF-R	PDGFR	.	.	.	.	Successful	A comparison of physicochemical property profiles of marketed oral drugs and orally bioavailable anti-cancer protein kinase inhibitors in clinical development. Curr Top Med Chem. 2007;7(14):1408-22.	34	.	Protein kinase superfamily. Tyr protein kinase family	.	.	.	.	.	.	.	.	.	.	.	.
TTB094Z	Adrenomedullin receptor (AMR)	Family	NOUNIPROTAC	.	.	AMR	.	.	.	.	Literature-reported	Characterization of the adrenomedullin receptor acting as the target of a new radiopharmaceutical biomolecule for lung imaging. Eur J Pharmacol. 2009 Sep 1;617(1-3):118-23.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT9PNO1	TRAIL receptor (TRAIL-R)	Family	NOUNIPROTAC	.	.	TRAIL-R	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.	.	.	.	Clinical trial	"Clinical pipeline report, company report or official report of the Pharmaceutical Research and Manufacturers of America (PhRMA)"	17	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTJNPTK	Plasmodium Cysteine protease falcipain (Malaria CPF)	Family	NOUNIPROTAC	.	.	Malaria CPF	.	.	.	.	Literature-reported	Falcipain inhibition as a promising antimalarial target. Curr Top Med Chem. 2012;12(5):408-44.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTM7WCE	Ion channel unspecific (IC)	Family	NOUNIPROTAC	.	.	IC	.	.	.	.	Clinical trial	Lundbeck: leading the way in the treatment of CNS disorders.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTWOCZI	Cation channel sperm-associated protein (CatSper)	Family	NOUNIPROTAC	.	Chemokine (C-C motif) receptor	CatSper	"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."	.	.	.	Literature-reported	The CatSper channel mediates progesterone-induced Ca2+ influx in human sperm. Nature. 2011 Mar 17;471(7338):382-6.	0	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5BN70	Nucleoside transporter (SLC)	Family	NOUNIPROTAC	.	.	SLC	.	.	.	.	Discontinued	"Studies of the nucleoside transporter inhibitor, draflazine, in the human myocardium. Br J Pharmacol. 1994 May;112(1):137-42."	5	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTZWSN5	Amyloid precursor protein (APP)	Family	NOUNIPROTAC	.	.	APP	.	.	.	.	Literature-reported	The Intracellular Domain of Amyloid Precursor Protein is a Potential Therapeutic Target in Alzheimer's Disease. Curr Drug Discov Technol. 2014;11(4):243-58.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTG91S4	Heat shock protein (HSP)	Family	NOUNIPROTAC	.	.	HSP	.	.	.	.	Clinical trial	Heat shock proteins (HSPs) based anti-cancer vaccines. Curr Mol Med. 2012 Nov 1;12(9):1183-97.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTCYAXN	Chloride channel unspecific (ClC)	Family	NOUNIPROTAC	.	.	ClC	.	.	.	.	Successful	Haemonchus contortus: selection at a glutamate-gated chloride channel gene in ivermectin- and moxidectin-selected strains. Exp Parasitol. 1998 Sep;90(1):42-8.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT92RXQ	ATP-sensitive potassium channel (KATP channel)	Family	NOUNIPROTAC	.	.	KATP channel	.	.	.	.	Literature-reported	Diverse roles of K(ATP) channels learned from Kir6.2 genetically engineered mice. Diabetes. 2000 Mar;49(3):311-8.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT6HNB8	Stretch-gated ion channel (MSC)	Family	NOUNIPROTAC	.	.	MSC	.	.	.	.	Literature-reported	Mechanosensitive channels: what can they do and how do they do it Structure. 2011 Oct 12;19(10):1356-69.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTV2CN0	Interferon receptor (IFNR)	Family	NOUNIPROTAC	.	Interferon receptor	IFNR	.	.	.	.	Clinical trial	Interferon in HDV infection. Antiviral Res. 1994 Jul;24(2-3):165-74.	21	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTV8ETH	Protein prenyl transferase (PPTF)	Family	NOUNIPROTAC	.	.	PPTF	.	.	.	.	Literature-reported	Spectroscopic study of fluorescent peptides for prenyl transferase assays. J Pharm Biomed Anal. 2005 Mar 9;37(3):417-22.	2	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTUN7MC	T-cell surface glycoprotein CD3 (CD3)	Family	NOUNIPROTAC	.	Cluster of differentiation 3	CD3	.	.	.	.	Successful	2014 FDA drug approvals. Nat Rev Drug Discov. 2015 Feb;14(2):77-81.	34	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TTD0CAZ	Aspartic protease (ASPP)	Family	NOUNIPROTAC	.	.	ASPP	.	.	.	.	Literature-reported	Aspartic protease inhibitors containing tertiary alcohol transition-state mimics. Eur J Med Chem. 2015 Jan 27;90:462-90.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT5TFXR	Relaxin receptor (RXFP)	Family	NOUNIPROTAC	.	.	RXFP	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.	.	.	.	Literature-reported	The relaxin receptor as a therapeutic target - perspectives from evolution and drug targeting. Pharmacol Ther. 2018 Jul;187:114-132.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
TT32XQJ	Monoamine oxidase (MAO)	Family	NOUNIPROTAC	.	Human monoamine oxidase	MAO	.	.