Details of Drug Off-Target (DOT)

General Information of Drug Off-Target (DOT) (ID: OTFG5CVF)

• DOT Name: E3 SUMO-protein ligase RanBP2 (RANBP2)
• Synonyms: EC 2.3.2.-; 358 kDa nucleoporin; Nuclear pore complex protein Nup358; Nucleoporin Nup358; Ran-binding protein 2; RanBP2; p270
• Gene Name: RANBP2
• Related Disease:
  Malaria
  Paralysis
  Acute myelomonocytic leukemia M4
  Adult glioblastoma
  Advanced cancer
  Autoimmune disease
  Carcinoma
  Cholangiocarcinoma
  Chromosomal disorder
  Classic Hodgkin lymphoma
  Colon cancer
  Colon carcinoma
  Colorectal carcinoma
  Familial acute necrotizing encephalopathy
  Glioblastoma multiforme
  Glioma
  Hematologic disease
  Huntington disease
  Hypopigmentation of the skin
  Insulinoma
  Malignant glioma
  Meningioma
  Microphthalmia
  Myelodysplastic syndrome
  Neoplasm
  Ocular cancer
  Plasma cell myeloma
  Sciatica/lumbar radicular pain
  Trichorhinophalangeal syndrome type II
  Vibrio cholerae infection
  Vitiligo
  Amyotrophic lateral sclerosis
  Encephalitis
  Frontotemporal dementia
  Pick disease
  Dowling-Degos disease
  Follicular lymphoma
  Leigh syndrome
  Malignant soft tissue neoplasm
  Nervous system disease
  Sarcoma
• UniProt ID: RBP2_HUMAN
• PDB ID: 1RRP; 1XKE; 1Z5S; 2LAS; 3UIN; 3UIO; 3UIP; 4GA0; 4I9Y; 4L6E; 4LQW; 5CLL; 5CLQ; 7MNJ; 7MNK; 7MNL; 7MNM; 7MNN; 7MNO; 7MNP; 7MNQ; 7MNR; 7MNS; 7MNT; 7MNU; 7MNV; 7MNW; 7MNX; 7MNY; 7MNZ; 7R5J; 7R5K
• EC Number: 2.3.2.-
• Pfam ID: PF12185 ; PF00160 ; PF00638 ; PF00641
• Sequence:
  MRRSKADVERYIASVQGSTPSPRQKSMKGFYFAKLYYEAKEYDLAKKYICTYINVQERDP
  KAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYWLER
  AAKLFPGSPAIYKLKEQLLDCEGEDGWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKR
  LKDAVAHCHEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYA
  NLMLLTLSTRDVQESRELLQSFDSALQSVKSLGGNDELSATFLEMKGHFYMHAGSLLLKM
  GQHSSNVQWRALSELAALCYLIAFQVPRPKIKLIKGEAGQNLLEMMACDRLSQSGHMLLN
  LSRGKQDFLKEIVETFANKSGQSALYDALFSSQSPKDTSFLGSDDIGNIDVREPELEDLT
  RYDVGAIRAHNGSLQHLTWLGLQWNSLPALPGIRKWLKQLFHHLPHETSRLETNAPESIC
  ILDLEVFLLGVVYTSHLQLKEKCNSHHSSYQPLCLPLPVCKQLCTERQKSWWDAVCTLIH
  RKAVPGNVAKLRLLVQHEINTLRAQEKHGLQPALLVHWAECLQKTGSGLNSFYDQREYIG
  RSVHYWKKVLPLLKIIKKKNSIPEPIDPLFKHFHSVDIQASEIVEYEEDAHITFAILDAV
  NGNIEDAVTAFESIKSVVSYWNLALIFHRKAEDIENDALSPEEQEECKNYLRKTRDYLIK
  IIDDSDSNLSVVKKLPVPLESVKEMLNSVMQELEDYSEGGPLYKNGSLRNADSEIKHSTP
  SPTRYSLSPSKSYKYSPKTPPRWAEDQNSLLKMICQQVEAIKKEMQELKLNSSNSASPHR
  WPTENYGPDSVPDGYQGSQTFHGAPLTVATTGPSVYYSQSPAYNSQYLLRPAANVTPTKG
  PVYGMNRLPPQQHIYAYPQQMHTPPVQSSSACMFSQEMYGPPALRFESPATGILSPRGDD
  YFNYNVQQTSTNPPLPEPGYFTKPPIAAHASRSAESKTIEFGKTNFVQPMPGEGLRPSLP
  TQAHTTQPTPFKFNSNFKSNDGDFTFSSPQVVTQPPPAAYSNSESLLGLLTSDKPLQGDG
  YSGAKPIPGGQTIGPRNTFNFGSKNVSGISFTENMGSSQQKNSGFRRSDDMFTFHGPGKS
  VFGTPTLETANKNHETDGGSAHGDDDDDGPHFEPVVPLPDKIEVKTGEEDEEEFFCNRAK
  LFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGS
  DRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSILKAPGTNVAMASNQAV
  RIVKEPTSHDNKDICKSDAGNLNFEFQVAKKEGSWWHCNSCSLKNASTAKKCVSCQNLNP
  SNKELVGPPLAETVFTPKTSPENVQDRFALVTPKKEGHWDCSICLVRNEPTVSRCIACQN
  TKSANKSGSSFVHQASFKFGQGDLPKPINSDFRSVFSTKEGQWDCSACLVQNEGSSTKCA
  ACQNPRKQSLPATSIPTPASFKFGTSETSKTLKSGFEDMFAKKEGQWDCSSCLVRNEANA
  TRCVACQNPDKPSPSTSVPAPASFKFGTSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNE
  ASATKCIACQNPGKQNQTTSAVSTPASSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEA
  SATKCIACQNPGKQNQTTSAVSTPASSETSKAPKSGFEGMFTKKEGQWDCSVCLVRNEAS
  ATKCIACQCPSKQNQTTAISTPASSEISKAPKSGFEGMFIRKGQWDCSVCCVQNESSSLK
  CVACDASKPTHKPIAEAPSAFTLGSEMKLHDSSGSQVGTGFKSNFSEKASKFGNTEQGFK
  FGHVDQENSPSFMFQGSSNTEFKSTKEGFSIPVSADGFKFGISEPGNQEKKSEKPLENGT
  GFQAQDISGQKNGRGVIFGQTSSTFTFADLAKSTSGEGFQFGKKDPNFKGFSGAGEKLFS
  SQYGKMANKANTSGDFEKDDDAYKTEDSDDIHFEPVVQMPEKVELVTGEEDEKVLYSQRV
  KLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSG
  SDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRLLLDIPLQTPHKLVDT
  GRAAKLIQRAEEMKSGLKDFKTFLTNDQTKVTEEENKGSGTGAAGASDTTIKPNPENTGP
  TLEWDNYDLREDALDDSVSSSSVHASPLASSPVRKNLFRFGESTTGFNFSFKSALSPSKS
  PAKLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLPDLVEVSSGEENEQVVFSHRAKLY
  RYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTER
  VWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTAQEKDSLITPHVSRSSTPR
  ESPCGKIAVAVLEETTRERTDVIQGDDVADATSEVEVSSTSETTPKAVVSPPKFVFGSES
  VKSIFSSEKSKPFAFGNSSATGSLFGFSFNAPLKSNNSETSSVAQSGSESKVEPKKCELS
  KNSDIEQSSDSKVKNLFASFPTEESSINYTFKTPEKAKEKKKPEDSPSDDDVLIVYELTP
  TAEQKALATKLKLPPTFFCYKNRPDYVSEEEEDDEDFETAVKKLNGKLYLDGSEKCRPLE
  ENTADNEKECIIVWEKKPTVEEKAKADTLKLPPTFFCGVCSDTDEDNGNGEDFQSELQKV
  QEAQKSQTEEITSTTDSVYTGGTEVMVPSFCKSEEPDSITKSISSPSVSSETMDKPVDLS
  TRKEIDTDSTSQGESKIVSFGFGSSTGLSFADLASSNSGDFAFGSKDKNFQWANTGAAVF
  GTQSVGTQSAGKVGEDEDGSDEEVVHNEDIHFEPIVSLPEVEVKSGEEDEEILFKERAKL
  YRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSN
  NALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQNLMKLQKGHVSLAAELSK
  ETNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKGFGFKNSIFHRVIPDF
  VCQGGDITKHDGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAE
  HLDFKHVVFGFVKDGMDTVKKIESFGSPKGSVCRRITITECGQI
• Function: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Binds single-stranded RNA (in vitro). May bind DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Inhibits EIF4E-dependent mRNA export. Sumoylates PML at 'Lys-490' which is essential for the proper assembly of PML-NB. Recruits BICD2 to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae during G2 phase of cell cycle. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity.
• KEGG Pathway:
  Nucleocytoplasmic transport (hsa03013)
  Viral life cycle - HIV-1 (hsa03250)
  Amyotrophic lateral sclerosis (hsa05014)
• Reactome Pathway:
  Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal (R-HSA-141444)
  Transport of the SLBP independent Mature mRNA (R-HSA-159227)
  Transport of the SLBP Dependant Mature mRNA (R-HSA-159230)
  Transport of Mature mRNA Derived from an Intronless Transcript (R-HSA-159231)
  Transport of Mature mRNA derived from an Intron-Containing Transcript (R-HSA-159236)
  Rev-mediated nuclear export of HIV RNA (R-HSA-165054)
  Transport of Ribonucleoproteins into the Host Nucleus (R-HSA-168271)
  NS1 Mediated Effects on Host Pathways (R-HSA-168276)
  Viral Messenger RNA Synthesis (R-HSA-168325)
  NEP/NS2 Interacts with the Cellular Export Machinery (R-HSA-168333)
  Regulation of Glucokinase by Glucokinase Regulatory Protein (R-HSA-170822)
  Nuclear import of Rev protein (R-HSA-180746)
  Vpr-mediated nuclear import of PICs (R-HSA-180910)
  snRNP Assembly (R-HSA-191859)
  Separation of Sister Chromatids (R-HSA-2467813)
  Resolution of Sister Chromatid Cohesion (R-HSA-2500257)
  SUMOylation of DNA damage response and repair proteins (R-HSA-3108214)
  SUMOylation of ubiquitinylation proteins (R-HSA-3232142)
  Nuclear Pore Complex (NPC) Disassembly (R-HSA-3301854)
  Regulation of HSF1-mediated heat shock response (R-HSA-3371453)
  SUMOylation of SUMOylation proteins (R-HSA-4085377)
  SUMOylation of chromatin organization proteins (R-HSA-4551638)
  SUMOylation of RNA binding proteins (R-HSA-4570464)
  SUMOylation of DNA replication proteins (R-HSA-4615885)
  Transcriptional regulation by small RNAs (R-HSA-5578749)
  Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) (R-HSA-5619107)
  RHO GTPases Activate Formins (R-HSA-5663220)
  tRNA processing in the nucleus (R-HSA-6784531)
  Mitotic Prometaphase (R-HSA-68877)
  HCMV Early Events (R-HSA-9609690)
  HCMV Late Events (R-HSA-9610379)
  EML4 and NUDC in mitotic spindle formation (R-HSA-9648025)
  SARS-CoV-2 activates/modulates innate and adaptive immune responses (R-HSA-9705671)
  Signaling by ALK fusions and activated point mutants (R-HSA-9725370)
  ISG15 antiviral mechanism (R-HSA-1169408)

Molecular Interaction Atlas (MIA) of This DOT

41 Disease(s) Related to This DOT

Disease Name	Disease ID	Evidence Level	Mode of Inheritance	REF
Malaria	DISQ9Y50	Definitive	Biomarker	[1]
Paralysis	DISF9I3O	Definitive	Genetic Variation	[2]
Acute myelomonocytic leukemia M4	DISRRMV2	Strong	Biomarker	[3]
Adult glioblastoma	DISVP4LU	Strong	Biomarker	[4]
Advanced cancer	DISAT1Z9	Strong	Altered Expression	[5]
Autoimmune disease	DISORMTM	Strong	Biomarker	[6]
Carcinoma	DISH9F1N	Strong	Biomarker	[7]
Cholangiocarcinoma	DIS71F6X	Strong	Biomarker	[8]
Chromosomal disorder	DISM5BB5	Strong	Biomarker	[9]
Classic Hodgkin lymphoma	DISV1LU6	Strong	Biomarker	[10]
Colon cancer	DISVC52G	Strong	Altered Expression	[11]
Colon carcinoma	DISJYKUO	Strong	Altered Expression	[11]
Colorectal carcinoma	DIS5PYL0	Strong	Biomarker	[12]
Familial acute necrotizing encephalopathy	DISPCVGG	Strong	Autosomal dominant	[13]
Glioblastoma multiforme	DISK8246	Strong	Biomarker	[4]
Glioma	DIS5RPEH	Strong	Altered Expression	[14]
Hematologic disease	DIS9XD9A	Strong	Biomarker	[3]
Huntington disease	DISQPLA4	Strong	Biomarker	[10]
Hypopigmentation of the skin	DIS39YKC	Strong	Biomarker	[15]
Insulinoma	DISIU1JS	Strong	Altered Expression	[16]
Malignant glioma	DISFXKOV	Strong	Biomarker	[17]
Meningioma	DISPT4TG	Strong	Altered Expression	[14]
Microphthalmia	DISGEBES	Strong	Altered Expression	[18]
Myelodysplastic syndrome	DISYHNUI	Strong	Biomarker	[19]
Neoplasm	DISZKGEW	Strong	Biomarker	[20]
Ocular cancer	DISV2EVE	Strong	Biomarker	[21]
Plasma cell myeloma	DIS0DFZ0	Strong	Biomarker	[22]
Sciatica/lumbar radicular pain	DIS01KTQ	Strong	Genetic Variation	[23]
Trichorhinophalangeal syndrome type II	DISW4YZ1	Strong	Biomarker	[24]
Vibrio cholerae infection	DISW7E3U	Strong	Altered Expression	[25]
Vitiligo	DISR05SL	Strong	Biomarker	[26]
Amyotrophic lateral sclerosis	DISF7HVM	moderate	Biomarker	[27]
Encephalitis	DISLD1RL	moderate	Genetic Variation	[28]
Frontotemporal dementia	DISKYHXL	moderate	Genetic Variation	[29]
Pick disease	DISP6X50	moderate	Genetic Variation	[29]
Dowling-Degos disease	DISGTTEP	Limited	Biomarker	[30]
Follicular lymphoma	DISVEUR6	Limited	Genetic Variation	[31]
Leigh syndrome	DISWQU45	Limited	Autosomal dominant	[32]
Malignant soft tissue neoplasm	DISTC6NO	Limited	Genetic Variation	[33]
Nervous system disease	DISJ7GGT	Limited	Biomarker	[34]
Sarcoma	DISZDG3U	Limited	Genetic Variation	[33]

This DOT Affected the Drug Response of 1 Drug(s)

Drug Name	Drug ID	Highest Status	Interaction	REF
Arsenic	DMTL2Y1	Approved	E3 SUMO-protein ligase RanBP2 (RANBP2) increases the response to substance of Arsenic.	[47]

4 Drug(s) Affected the Post-Translational Modifications of This DOT

Drug Name	Drug ID	Highest Status	Interaction	REF
Valproate	DMCFE9I	Approved	Valproate increases the methylation of E3 SUMO-protein ligase RanBP2 (RANBP2).	[35]
TAK-243	DM4GKV2	Phase 1	TAK-243 decreases the sumoylation of E3 SUMO-protein ligase RanBP2 (RANBP2).	[45]
PMID28870136-Compound-52	DMFDERP	Patented	PMID28870136-Compound-52 affects the phosphorylation of E3 SUMO-protein ligase RanBP2 (RANBP2).	[46]
Coumarin	DM0N8ZM	Investigative	Coumarin affects the phosphorylation of E3 SUMO-protein ligase RanBP2 (RANBP2).	[46]

10 Drug(s) Affected the Gene/Protein Processing of This DOT

Drug Name	Drug ID	Highest Status	Interaction	REF
Ciclosporin	DMAZJFX	Approved	Ciclosporin decreases the expression of E3 SUMO-protein ligase RanBP2 (RANBP2).	[36]
Tretinoin	DM49DUI	Approved	Tretinoin decreases the expression of E3 SUMO-protein ligase RanBP2 (RANBP2).	[37]
Acetaminophen	DMUIE76	Approved	Acetaminophen decreases the expression of E3 SUMO-protein ligase RanBP2 (RANBP2).	[38]
Ivermectin	DMDBX5F	Approved	Ivermectin decreases the expression of E3 SUMO-protein ligase RanBP2 (RANBP2).	[39]
Vorinostat	DMWMPD4	Approved	Vorinostat increases the expression of E3 SUMO-protein ligase RanBP2 (RANBP2).	[40]
Testosterone	DM7HUNW	Approved	Testosterone decreases the expression of E3 SUMO-protein ligase RanBP2 (RANBP2).	[41]
Selenium	DM25CGV	Approved	Selenium decreases the expression of E3 SUMO-protein ligase RanBP2 (RANBP2).	[42]
Testosterone enanthate	DMB6871	Approved	Testosterone enanthate affects the expression of E3 SUMO-protein ligase RanBP2 (RANBP2).	[43]
Azacitidine	DMTA5OE	Approved	Azacitidine increases the expression of E3 SUMO-protein ligase RanBP2 (RANBP2).	[44]
Tocopherol	DMBIJZ6	Phase 2	Tocopherol decreases the expression of E3 SUMO-protein ligase RanBP2 (RANBP2).	[42]

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