ID RANG_HUMAN Reviewed; 201 AA. AC P43487; Q53EY3; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 205. DE RecName: Full=Ran-specific GTPase-activating protein; DE AltName: Full=Ran-binding protein 1; DE Short=RanBP1; GN Name=RANBP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION, RP INTERACTION WITH RAN, AND SUBUNIT. RX PubMed=7882974; DOI=10.1002/j.1460-2075.1995.tb07049.x; RA Bischoff F.R., Krebber H., Smirnova E., Dong W., Ponstingl H.; RT "Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP RT binding protein RanBP1."; RL EMBO J. 14:705-715(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION IN A COMPLEX WITH RP RAN AND RCC1, AND FUNCTION. RC TISSUE=Blood; RX PubMed=7616957; DOI=10.1007/bf00290397; RA Hayashi N., Yokoyama N., Seki T., Azuma Y., Ohba T., Nishimoto T.; RT "RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits RCC1 via RT Ran/TC4."; RL Mol. Gen. Genet. 247:661-669(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Coronary arterial endothelium; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [6] RP INTERACTION WITH RAN. RX PubMed=7891706; DOI=10.1128/mcb.15.4.2117; RA Ren M., Villamarin A., Shih A., Coutavas E., Moore M.S., Locurcio M., RA Clarke V., Oppenheim J.D., D'Eustachio P., Rush M.G.; RT "Separate domains of the Ran GTPase interact with different factors to RT regulate nuclear protein import and RNA processing."; RL Mol. Cell. Biol. 15:2117-2124(1995). RN [7] RP INTERACTION WITH RAN. RX PubMed=8896452; DOI=10.1002/j.1460-2075.1996.tb00943.x; RA Goerlich D., Pante N., Kutay U., Aebi U., Bischoff F.R.; RT "Identification of different roles for RanGDP and RanGTP in nuclear protein RT import."; RL EMBO J. 15:5584-5594(1996). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [9] RP IDENTIFICATION IN A COMPLEX WITH RAN AND RANGAP1. RX PubMed=16428860; DOI=10.1247/csf.30.69; RA Takeda E., Hieda M., Katahira J., Yoneda Y.; RT "Phosphorylation of RanGAP1 stabilizes its interaction with Ran and RT RanBP1."; RL Cell Struct. Funct. 30:69-80(2005). RN [10] RP FUNCTION. RX PubMed=17671426; DOI=10.4161/cc.6.15.4487; RA Li H.Y., Ng W.P., Wong C.H., Iglesias P.A., Zheng Y.; RT "Coordination of chromosome alignment and mitotic progression by the RT chromosome-based Ran signal."; RL Cell Cycle 6:1886-1895(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; THR-18 AND SER-21, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150 AND LYS-183, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [15] RP FUNCTION. RX PubMed=20485264; DOI=10.1038/emboj.2010.89; RA Koyama M., Matsuura Y.; RT "An allosteric mechanism to displace nuclear export cargo from CRM1 and RT RanGTP by RanBP1."; RL EMBO J. 29:2002-2013(2010). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-188, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-190, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-190, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [25] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-190, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [26] {ECO:0007744|PDB:1K5D, ECO:0007744|PDB:1K5G} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH RAN AND THE FISSION RP YEAST ORTHOLOG OF RANGAP1. RX PubMed=11832950; DOI=10.1038/415662a; RA Seewald M.J., Korner C., Wittinghofer A., Vetter I.R.; RT "RanGAP mediates GTP hydrolysis without an arginine finger."; RL Nature 415:662-666(2002). RN [27] RP VARIANT [LARGE SCALE ANALYSIS] ASP-16. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Plays a role in RAN-dependent nucleocytoplasmic transport. CC Alleviates the TNPO1-dependent inhibition of RAN GTPase activity and CC mediates the dissociation of RAN from proteins involved in transport CC into the nucleus (By similarity). Induces a conformation change in the CC complex formed by XPO1 and RAN that triggers the release of the nuclear CC export signal of cargo proteins (PubMed:20485264). Promotes the CC disassembly of the complex formed by RAN and importin beta. Promotes CC dissociation of RAN from a complex with KPNA2 and CSE1L (By CC similarity). Required for normal mitotic spindle assembly and normal CC progress through mitosis via its effect on RAN (PubMed:17671426). Does CC not increase the RAN GTPase activity by itself, but increases GTP CC hydrolysis mediated by RANGAP1 (PubMed:7882974). Inhibits RCC1- CC dependent exchange of RAN-bound GDP by GTP (PubMed:7882974, CC PubMed:7616957). {ECO:0000250|UniProtKB:P34022, CC ECO:0000269|PubMed:17671426, ECO:0000269|PubMed:20485264, CC ECO:0000269|PubMed:7616957, ECO:0000269|PubMed:7882974}. CC -!- SUBUNIT: Interacts with RAN (via C-terminus of GTP-bound form) but not CC with GDP-bound RAN (PubMed:7882974, PubMed:7891706, PubMed:8896452). CC Identified in a complex composed of RAN, RANGAP1 and RANBP1 CC (PubMed:16428860, PubMed:11832950). Identified in a complex that CC contains TNPO1, RAN and RANBP1. Identified in a complex that contains CC CSE1L, KPNA2, RAN and RANBP1 (By similarity). Identified in a complex CC with nucleotide-free RAN and RCC1 (PubMed:7882974, PubMed:7616957). CC {ECO:0000250|UniProtKB:P34022, ECO:0000269|PubMed:11832950, CC ECO:0000269|PubMed:16428860, ECO:0000269|PubMed:7616957, CC ECO:0000269|PubMed:7882974, ECO:0000269|PubMed:7891706, CC ECO:0000269|PubMed:8896452}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P43487-1; Sequence=Displayed; CC Name=2; CC IsoId=P43487-2; Sequence=VSP_055104; CC -!- SIMILARITY: Belongs to the RANBP1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X83617; CAA58592.1; -; mRNA. DR EMBL; D38076; BAA07269.1; -; mRNA. DR EMBL; CR456556; CAG30442.1; -; mRNA. DR EMBL; AK223506; BAD97226.1; -; mRNA. DR EMBL; AC006547; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS13775.1; -. [P43487-1] DR CCDS; CCDS63408.1; -. [P43487-2] DR PIR; S54290; S54290. DR RefSeq; NP_001265568.1; NM_001278639.1. DR RefSeq; NP_001265569.1; NM_001278640.1. [P43487-2] DR RefSeq; NP_002873.1; NM_002882.3. [P43487-1] DR PDB; 1K5D; X-ray; 2.70 A; B/E/H/K=1-201. DR PDB; 1K5G; X-ray; 3.10 A; B/E/H/K=1-201. DR PDBsum; 1K5D; -. DR PDBsum; 1K5G; -. DR AlphaFoldDB; P43487; -. DR SMR; P43487; -. DR BioGRID; 111838; 176. DR CORUM; P43487; -. DR DIP; DIP-35058N; -. DR IntAct; P43487; 39. DR MINT; P43487; -. DR STRING; 9606.ENSP00000401564; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB12695; Phenethyl Isothiocyanate. DR GlyGen; P43487; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P43487; -. DR PhosphoSitePlus; P43487; -. DR SwissPalm; P43487; -. DR BioMuta; RANBP1; -. DR DOSAC-COBS-2DPAGE; P43487; -. DR OGP; P43487; -. DR REPRODUCTION-2DPAGE; IPI00414127; -. DR EPD; P43487; -. DR jPOST; P43487; -. DR MassIVE; P43487; -. DR MaxQB; P43487; -. DR PaxDb; 9606-ENSP00000401564; -. DR PeptideAtlas; P43487; -. DR ProteomicsDB; 55636; -. [P43487-1] DR Pumba; P43487; -. DR TopDownProteomics; P43487-1; -. [P43487-1] DR Antibodypedia; 23138; 318 antibodies from 36 providers. DR DNASU; 5902; -. DR Ensembl; ENST00000331821.8; ENSP00000327583.3; ENSG00000099901.18. [P43487-1] DR Ensembl; ENST00000402752.5; ENSP00000384925.1; ENSG00000099901.18. [P43487-2] DR GeneID; 5902; -. DR KEGG; hsa:5902; -. DR UCSC; uc002zro.3; human. [P43487-1] DR AGR; HGNC:9847; -. DR CTD; 5902; -. DR DisGeNET; 5902; -. DR GeneCards; RANBP1; -. DR HGNC; HGNC:9847; RANBP1. DR HPA; ENSG00000099901; Low tissue specificity. DR MIM; 601180; gene. DR neXtProt; NX_P43487; -. DR OpenTargets; ENSG00000099901; -. DR PharmGKB; PA34206; -. DR VEuPathDB; HostDB:ENSG00000099901; -. DR eggNOG; KOG0864; Eukaryota. DR GeneTree; ENSGT00900000141073; -. DR InParanoid; P43487; -. DR OrthoDB; 158765at2759; -. DR PhylomeDB; P43487; -. DR PathwayCommons; P43487; -. DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA. DR SignaLink; P43487; -. DR BioGRID-ORCS; 5902; 224 hits in 1171 CRISPR screens. DR ChiTaRS; RANBP1; human. DR EvolutionaryTrace; P43487; -. DR GeneWiki; RANBP1; -. DR GenomeRNAi; 5902; -. DR Pharos; P43487; Tbio. DR PRO; PR:P43487; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; P43487; Protein. DR Bgee; ENSG00000099901; Expressed in ganglionic eminence and 196 other cell types or tissues. DR ExpressionAtlas; P43487; baseline and differential. DR GO; GO:0005813; C:centrosome; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005635; C:nuclear envelope; TAS:Reactome. DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; TAS:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IMP:GO_Central. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0031267; F:small GTPase binding; TAS:ProtInc. DR GO; GO:0006913; P:nucleocytoplasmic transport; IEA:InterPro. DR GO; GO:0046604; P:positive regulation of mitotic centrosome separation; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB. DR CDD; cd13179; RanBD_RanBP1; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR IDEAL; IID00337; -. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR000156; Ran_bind_dom. DR InterPro; IPR045255; RanBP1-like. DR InterPro; IPR045256; RanBP1_RanBD. DR PANTHER; PTHR23138; RAN BINDING PROTEIN; 1. DR PANTHER; PTHR23138:SF87; RANBD1 DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00638; Ran_BP1; 1. DR SMART; SM00160; RanBD; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50196; RANBD1; 1. DR Genevisible; P43487; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW GTPase activation; Isopeptide bond; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..201 FT /note="Ran-specific GTPase-activating protein" FT /id="PRO_0000213667" FT DOMAIN 26..164 FT /note="RanBD1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164" FT REGION 1..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 163..201 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..23 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 13 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 18 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 21 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 150 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 150 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P34022" FT MOD_RES 183 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 188 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 190 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT VAR_SEQ 169 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7616957, ECO:0000303|Ref.4" FT /id="VSP_055104" FT VARIANT 16 FT /note="E -> D (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036567" FT VARIANT 145 FT /note="A -> V (in dbSNP:rs5746863)" FT /id="VAR_053629" FT CONFLICT 61 FT /note="E -> V (in Ref. 5; BAD97226)" FT /evidence="ECO:0000305" FT STRAND 48..58 FT /evidence="ECO:0007829|PDB:1K5D" FT STRAND 67..79 FT /evidence="ECO:0007829|PDB:1K5D" FT STRAND 81..83 FT /evidence="ECO:0007829|PDB:1K5D" FT STRAND 86..92 FT /evidence="ECO:0007829|PDB:1K5D" FT TURN 93..95 FT /evidence="ECO:0007829|PDB:1K5D" FT STRAND 98..103 FT /evidence="ECO:0007829|PDB:1K5D" FT STRAND 117..127 FT /evidence="ECO:0007829|PDB:1K5D" FT STRAND 134..141 FT /evidence="ECO:0007829|PDB:1K5D" FT HELIX 145..165 FT /evidence="ECO:0007829|PDB:1K5D" SQ SEQUENCE 201 AA; 23310 MW; 05FC9B35DADA48C9 CRC64; MAAAKDTHED HDTSTENTDE SNHDPQFEPI VSLPEQEIKT LEEDEEELFK MRAKLFRFAS ENDLPEWKER GTGDVKLLKH KEKGAIRLLM RRDKTLKICA NHYITPMMEL KPNAGSDRAW VWNTHADFAD ECPKPELLAI RFLNAENAQK FKTKFEECRK EIEEREKKAG SGKNDHAEKV AEKLEALSVK EETKEDAEEK Q //