RANG_HUMAN
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 03-AUG-2022, entry version 196.
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}.
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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; 83.
DR CORUM; P43487; -.
DR DIP; DIP-35058N; -.
DR IntAct; P43487; 34.
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; P43487; -.
DR PeptideAtlas; P43487; -.
DR PRIDE; P43487; -.
DR ProteomicsDB; 55636; -. [P43487-1]
DR TopDownProteomics; P43487-1; -. [P43487-1]
DR Antibodypedia; 23138; 288 antibodies from 36 providers.
DR DNASU; 5902; -.
DR Ensembl; ENST00000331821.7; ENSP00000327583.3; ENSG00000099901.17. [P43487-1]
DR Ensembl; ENST00000402752.5; ENSP00000384925.1; ENSG00000099901.17. [P43487-2]
DR GeneID; 5902; -.
DR KEGG; hsa:5902; -.
DR UCSC; uc002zro.3; human. [P43487-1]
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; 1154500at2759; -.
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; 199 hits in 1084 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 194 other tissues.
DR ExpressionAtlas; P43487; baseline and differential.
DR Genevisible; P43487; HS.
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; -; 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; PTHR23138; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR PROSITE; PS50196; RANBD1; 1.
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
