RAGP1_MOUSE
ID RAGP1_MOUSE Reviewed; 589 AA.
AC P46061; Q60801; Q6NZB5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Ran GTPase-activating protein 1;
DE Short=RanGAP1;
GN Name=Rangap1; Synonyms=Fug1 {ECO:0000303|PubMed:8314081};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8314081; DOI=10.1101/gad.8.3.265;
RA Degregori J., Russ A., von Melchner H., Rayburn H., Priyaranjan P.,
RA Jenkins N.A., Copeland N.G., Ruley H.E.;
RT "A murine homolog of the yeast RNA1 gene is required for postimplantation
RT development.";
RL Genes Dev. 8:265-276(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC STRAIN=BALB/cJ;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129, and C57BL/6J; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUMOYLATION AT LYS-526, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-526.
RX PubMed=9442102; DOI=10.1083/jcb.140.2.259;
RA Mahajan R., Gerace L., Melchior F.;
RT "Molecular characterization of the SUMO-1 modification of RanGAP1 and its
RT role in nuclear envelope association.";
RL J. Cell Biol. 140:259-270(1998).
RN [6]
RP SUMOYLATION AT LYS-526, SUBCELLULAR LOCATION, INTERACTION WITH RANBP2, AND
RP MUTAGENESIS OF LYS-526 AND PHE-564.
RX PubMed=9456312; DOI=10.1083/jcb.140.3.499;
RA Matunis M.J., Wu J., Blobel G.;
RT "SUMO-1 modification and its role in targeting the Ran GTPase-activating
RT protein, RanGAP1, to the nuclear pore complex.";
RL J. Cell Biol. 140:499-509(1998).
RN [7]
RP PHOSPHORYLATION AT THR-411 AND SER-444, AND MUTAGENESIS OF THR-411 AND
RP SER-444.
RX PubMed=15037602; DOI=10.1083/jcb.200309126;
RA Swaminathan S., Kiendl F., Koerner R., Lupetti R., Hengst L., Melchior F.;
RT "RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains
RT associated with RanBP2 upon NPC disassembly.";
RL J. Cell Biol. 164:965-971(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [9]
RP SUMOYLATION AT LYS-526, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-526.
RX PubMed=16469311; DOI=10.1016/j.yexcr.2005.12.031;
RA Zhu S., Zhang H., Matunis M.J.;
RT "SUMO modification through rapamycin-mediated heterodimerization reveals a
RT dual role for Ubc9 in targeting RanGAP1 to nuclear pore complexes.";
RL Exp. Cell Res. 312:1042-1049(2006).
RN [10]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18305100; DOI=10.1091/mbc.e07-12-1279;
RA Hutten S., Flotho A., Melchior F., Kehlenbach R.H.;
RT "The Nup358-RanGAP complex is required for efficient importin alpha/beta-
RT dependent nuclear import.";
RL Mol. Biol. Cell 19:2300-2310(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441 AND SER-444, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP INTERACTION WITH MYCBP2.
RX PubMed=26304119; DOI=10.1074/jbc.m115.646901;
RA Doerr A., Pierre S., Zhang D.D., Henke M., Holland S., Scholich K.;
RT "MYCBP2 is a guanosine exchange factor for Ran protein and determines its
RT localization in neurons of dorsal root ganglia.";
RL J. Biol. Chem. 290:25620-25635(2015).
RN [14]
RP SUBCELLULAR LOCATION, SUMOYLATION, AND MUTAGENESIS OF 541-LEU--ILE-589 AND
RP 567-LYS--ILE-589.
RX PubMed=26506250; DOI=10.1371/journal.pone.0141309;
RA Cha K., Sen P., Raghunayakula S., Zhang X.D.;
RT "The Cellular Distribution of RanGAP1 Is Regulated by CRM1-Mediated Nuclear
RT Export in Mammalian Cells.";
RL PLoS ONE 10:E0141309-E0141309(2015).
RN [15]
RP DESUMOYLATION.
RX PubMed=31088288; DOI=10.1089/ars.2019.7724;
RA Cortes-Montero E., Rodriguez-Munoz M., Sanchez-Blazquez P., Garzon J.;
RT "The Axonal Motor Neuropathy-Related HINT1 Protein Is a Zinc- and
RT Calmodulin-Regulated Cysteine SUMO Protease.";
RL Antioxid. Redox Signal. 31:503-520(2019).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 420-589 IN COMPLEX WITH SUMO1 AND
RP HUMAN UBE2I, AND MUTAGENESIS OF ASN-512; THR-516; ARG-517; ILE-520;
RP HIS-521; MET-522; LEU-524; LEU-525; LYS-526; GLU-528; ASP-529; ILE-531;
RP LEU-537; LEU-560; ALA-563; PHE-564; LYS-567 AND ASN-569.
RX PubMed=11853669; DOI=10.1016/s0092-8674(02)00630-x;
RA Bernier-Villamor V., Sampson D.A., Matunis M.J., Lima C.D.;
RT "Structural basis for E2-mediated SUMO conjugation revealed by a complex
RT between ubiquitin-conjugating enzyme Ubc9 and RanGAP1.";
RL Cell 108:345-356(2002).
CC -!- FUNCTION: GTPase activator for RAN. Converts cytoplasmic GTP-bound RAN
CC to GDP-bound RAN, which is essential for RAN-mediated nuclear import
CC and export (PubMed:18305100). Mediates dissociation of cargo from
CC nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear
CC export (By similarity). Required for postimplantation embryonic
CC development (PubMed:8314081). {ECO:0000250|UniProtKB:P46060,
CC ECO:0000269|PubMed:18305100, ECO:0000269|PubMed:8314081}.
CC -!- SUBUNIT: Homodimer (PubMed:7891706). Interacts with RAN
CC (PubMed:7891706). Forms a complex with RANBP2/NUP358, NXF1 and NXT1 (By
CC similarity). Forms a tight complex in association with RANBP2 and
CC UBE2I/UBC9, the ubiquitin-conjugating enzyme E2 (PubMed:11853669).
CC Interacts with UBE2I; the interaction conjugates SUMO1 to RANGAP1, and
CC subsequently stabilizes interactions of sumoylated RANGAP1 with RANBP2
CC (PubMed:9456312, PubMed:18305100, PubMed:11853669). The complex
CC composed of RANBP2, SUMO1, RANGAP1 and UBE2I associates with nuclear
CC pore complexes (By similarity). Identified in a complex composed of
CC RAN, RANBP2, sumoylated RANGAP1, UBE2I and XPO1 (By similarity).
CC Interacts with TRAF6 (By similarity). Interacts with SUMO1 and SENP1
CC (By similarity). Interacts (when sumoylated) with MYCBP2; interaction
CC inhibits MYCBP2 E3 ubiquitin-protein ligase activity and promotes
CC MYCBP2 translocation to the nucleus (PubMed:26304119).
CC {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:11853669,
CC ECO:0000269|PubMed:18305100, ECO:0000269|PubMed:26304119,
CC ECO:0000269|PubMed:9456312, ECO:0000305|PubMed:7891706}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26506250,
CC ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:26506250}. Nucleus envelope
CC {ECO:0000269|PubMed:16469311, ECO:0000269|PubMed:18305100,
CC ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102,
CC ECO:0000269|PubMed:9456312}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:P46060}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P46060}. Note=Cytoplasmic during interphase
CC (PubMed:26506250). Detected at the nuclear envelope during interphase
CC (PubMed:9442102, PubMed:9456312, PubMed:26506250). Shuttles between
CC nucleus and cytoplasm (PubMed:26506250). Targeted to the nuclear pores
CC after sumoylation. During mitosis, associates with mitotic spindles,
CC but is essentially not detected at the spindle poles. Association with
CC kinetochores appears soon after nuclear envelope breakdown and persists
CC until late anaphase. Mitotic location also requires sumoylation (By
CC similarity). {ECO:0000250|UniProtKB:P46060,
CC ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102,
CC ECO:0000269|PubMed:9456312}.
CC -!- TISSUE SPECIFICITY: Detected in adult brain, liver, kidney, intestine,
CC uterus and ovary. {ECO:0000269|PubMed:8314081}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos at 7.5 dpc, but not at 6 dpc.
CC {ECO:0000269|PubMed:8314081}.
CC -!- PTM: Phosphorylation occurs before nuclear envelope breakdown and
CC continues throughout mitosis. Phosphorylated by the M-phase kinase
CC cyclin B/Cdk1, in vitro. Differential timimg of dephosphorylation
CC occurs during phases of mitosis. The phosphorylated form remains
CC associated with RANBP2/NUP358 and the SUMO E2-conjugating enzyme,
CC UBE2I, on nuclear pore complex (NPC) diassembly and during mitosis.
CC {ECO:0000269|PubMed:15037602}.
CC -!- PTM: Sumoylated (PubMed:26506250, PubMed:11853669). Sumoylation is
CC necessary for targeting to the nuclear envelope (NE) (PubMed:16469311).
CC Sumoylation is necessary for association with mitotic spindles and
CC kinetochores during mitosis (By similarity). Also required for
CC interaction with RANBP2 and is mediated by UBE2I (PubMed:9456312,
CC PubMed:11853669). Desumoylated by HINT1 (PubMed:31088288).
CC {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:11853669,
CC ECO:0000269|PubMed:16469311, ECO:0000269|PubMed:26506250,
CC ECO:0000269|PubMed:31088288, ECO:0000269|PubMed:9456312}.
CC -!- DISRUPTION PHENOTYPE: Embryonic development is arrested around 6 dpc.
CC {ECO:0000269|PubMed:8314081}.
CC -!- SIMILARITY: Belongs to the RNA1 family. {ECO:0000305}.
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DR EMBL; U08110; AAA17681.1; -; mRNA.
DR EMBL; U20857; AAB60517.1; -; Genomic_RNA.
DR EMBL; AK146670; BAE27347.1; -; mRNA.
DR EMBL; AK159009; BAE34767.1; -; mRNA.
DR EMBL; AK159525; BAE35154.1; -; mRNA.
DR EMBL; BC066213; AAH66213.1; -; mRNA.
DR EMBL; BC071200; AAH71200.1; -; mRNA.
DR CCDS; CCDS27670.1; -.
DR PIR; A36983; A36983.
DR PIR; T52070; T52070.
DR RefSeq; NP_001139646.1; NM_001146174.1.
DR RefSeq; NP_035371.4; NM_011241.4.
DR PDB; 1KPS; X-ray; 2.50 A; B/D=420-589.
DR PDBsum; 1KPS; -.
DR AlphaFoldDB; P46061; -.
DR SMR; P46061; -.
DR BioGRID; 202583; 40.
DR ComplexPortal; CPX-4921; E3 ligase (RANBP2) complex.
DR DIP; DIP-17024N; -.
DR ELM; P46061; -.
DR IntAct; P46061; 7.
DR MINT; P46061; -.
DR STRING; 10090.ENSMUSP00000126849; -.
DR iPTMnet; P46061; -.
DR PhosphoSitePlus; P46061; -.
DR SwissPalm; P46061; -.
DR EPD; P46061; -.
DR jPOST; P46061; -.
DR MaxQB; P46061; -.
DR PaxDb; P46061; -.
DR PeptideAtlas; P46061; -.
DR PRIDE; P46061; -.
DR ProteomicsDB; 300391; -.
DR Antibodypedia; 3803; 403 antibodies from 41 providers.
DR DNASU; 19387; -.
DR Ensembl; ENSMUST00000052374; ENSMUSP00000057771; ENSMUSG00000022391.
DR Ensembl; ENSMUST00000170134; ENSMUSP00000126849; ENSMUSG00000022391.
DR Ensembl; ENSMUST00000171115; ENSMUSP00000130046; ENSMUSG00000022391.
DR GeneID; 19387; -.
DR KEGG; mmu:19387; -.
DR UCSC; uc007wxa.2; mouse.
DR CTD; 5905; -.
DR MGI; MGI:103071; Rangap1.
DR VEuPathDB; HostDB:ENSMUSG00000022391; -.
DR eggNOG; KOG1909; Eukaryota.
DR GeneTree; ENSGT00440000039203; -.
DR HOGENOM; CLU_028747_2_0_1; -.
DR InParanoid; P46061; -.
DR OMA; WGVDELD; -.
DR OrthoDB; 1357476at2759; -.
DR PhylomeDB; P46061; -.
DR TreeFam; TF318283; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 19387; 28 hits in 74 CRISPR screens.
DR ChiTaRS; Rangap1; mouse.
DR EvolutionaryTrace; P46061; -.
DR PRO; PR:P46061; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P46061; protein.
DR Bgee; ENSMUSG00000022391; Expressed in dorsal pancreas and 257 other tissues.
DR ExpressionAtlas; P46061; baseline and differential.
DR Genevisible; P46061; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:1904115; C:axon cytoplasm; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:1990723; C:cytoplasmic periphery of the nuclear pore complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0106068; C:SUMO ligase complex; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISO:MGI.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISO:MGI.
DR GO; GO:1904117; P:cellular response to vasopressin; IEA:Ensembl.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; ISO:MGI.
DR GO; GO:0051168; P:nuclear export; IC:ComplexPortal.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; ISO:MGI.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.40.200; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR009109; Ran_GTPase_activating_1_C.
DR InterPro; IPR036720; RanGAP1_C_sf.
DR Pfam; PF13516; LRR_6; 3.
DR Pfam; PF07834; RanGAP1_C; 1.
DR SUPFAM; SSF69099; SSF69099; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW GTPase activation; Isopeptide bond; Kinetochore; Leucine-rich repeat;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT CHAIN 2..589
FT /note="Ran GTPase-activating protein 1"
FT /id="PRO_0000056738"
FT REPEAT 48..71
FT /note="LRR 1"
FT REPEAT 111..134
FT /note="LRR 2"
FT REPEAT 207..230
FT /note="LRR 3"
FT REPEAT 235..258
FT /note="LRR 4"
FT REPEAT 292..315
FT /note="LRR 5"
FT REPEAT 320..343
FT /note="LRR 6"
FT REGION 357..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..566
FT /note="Important for accumulation in the nucleus"
FT /evidence="ECO:0000269|PubMed:26506250"
FT MOTIF 525..528
FT /note="SUMO conjugation"
FT /evidence="ECO:0000250"
FT COMPBIAS 359..402
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 564
FT /note="Hydrophobic interaction with UBE2I"
FT /evidence="ECO:0000250"
FT SITE 567
FT /note="Hydrophobic interaction with UBE2I"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT MOD_RES 411
FT /note="Phosphothreonine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15037602,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 526
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT CROSSLNK 454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT CROSSLNK 526
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 526
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT CROSSLNK 526
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P46060"
FT MUTAGEN 411
FT /note="T->D: Greatly reduced phosphorylation by CDK1 or
FT CDK2. Completely abolished phosphorylation by CDK1 or CDK2;
FT when associated with D-444."
FT /evidence="ECO:0000269|PubMed:15037602"
FT MUTAGEN 444
FT /note="S->D: Little change in phosphorylation by CDK1 or
FT CDK2. Completely abolished phosphorylation by CDK1 or CDK2;
FT when associated with D-411."
FT /evidence="ECO:0000269|PubMed:15037602"
FT MUTAGEN 512
FT /note="N->A: No effect on UBE2I binding nor on
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 516
FT /note="T->A: No effect on UBE2I binding nor on
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 517
FT /note="R->A: No effect on UBE2I binding nor on
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 520
FT /note="I->A: No effect on UBE2I binding nor on
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 521
FT /note="H->A: No effect on UBE2I binding nor on
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 522
FT /note="M->A: No effect on UBE2I binding nor on
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 524
FT /note="L->A: No sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 525
FT /note="L->A: Disrupted binding to UBE2I, and no
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 526
FT /note="K->A: No UBE2I binding nor sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669,
FT ECO:0000269|PubMed:16469311, ECO:0000269|PubMed:9442102,
FT ECO:0000269|PubMed:9456312"
FT MUTAGEN 526
FT /note="K->R: Absence of sumoylation. Not targeted to the
FT nuclear envelope rim nor to nuclear pore complexes.
FT Disrupted sumoylation. No interaction with SUMO1; when
FT associated with A-564 and with or without SUMO1 A-97."
FT /evidence="ECO:0000269|PubMed:11853669,
FT ECO:0000269|PubMed:16469311, ECO:0000269|PubMed:9442102,
FT ECO:0000269|PubMed:9456312"
FT MUTAGEN 528
FT /note="E->A: No UBE2I binding nor sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 529
FT /note="D->A: No effect on UBE2I binding nor on
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 531
FT /note="I->A: No effect on UBE2I binding nor on
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 537
FT /note="L->A: No effect on UBE2I binding nor on
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 541..589
FT /note="Missing: Abolishes accumulation in the nucleus."
FT /evidence="ECO:0000269|PubMed:26506250"
FT MUTAGEN 560
FT /note="L->A: No effect on UBE2I binding nor on
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 563
FT /note="A->L: No effect on UBE2I binding nor on
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 564
FT /note="F->A: No UBE2I binding nor sumoylation. Not targeted
FT to nuclear pore complexes; when associated with R-526."
FT /evidence="ECO:0000269|PubMed:11853669,
FT ECO:0000269|PubMed:9456312"
FT MUTAGEN 567..589
FT /note="Missing: No effect on accumulation in the nucleus."
FT /evidence="ECO:0000269|PubMed:26506250"
FT MUTAGEN 567
FT /note="K->A: No UBE2I binding nor sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT MUTAGEN 569
FT /note="N->A: No effect on UBE2I binding nor on
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:11853669"
FT CONFLICT 181
FT /note="A -> R (in Ref. 1; AAA17681)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="S -> L (in Ref. 2; AAB60517)"
FT /evidence="ECO:0000305"
FT HELIX 436..441
FT /evidence="ECO:0007829|PDB:1KPS"
FT HELIX 445..450
FT /evidence="ECO:0007829|PDB:1KPS"
FT HELIX 455..461
FT /evidence="ECO:0007829|PDB:1KPS"
FT HELIX 468..480
FT /evidence="ECO:0007829|PDB:1KPS"
FT HELIX 486..505
FT /evidence="ECO:0007829|PDB:1KPS"
FT HELIX 511..521
FT /evidence="ECO:0007829|PDB:1KPS"
FT HELIX 538..549
FT /evidence="ECO:0007829|PDB:1KPS"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:1KPS"
FT HELIX 558..565
FT /evidence="ECO:0007829|PDB:1KPS"
FT HELIX 577..588
FT /evidence="ECO:0007829|PDB:1KPS"
SQ SEQUENCE 589 AA; 63531 MW; 775ADE3A53EFD558 CRC64;
MASEDIAKLA ETLAKTQVAG GQLSFKGKGL KLNTAEDAKD VIKEIEEFDG LEALRLEGNT
VGVEAARVIA KALEKKSELK RCHWSDMFTG RLRSEIPPAL ISLGEGLITA GAQLVELDLS
DNAFGPDGVR GFEALLKSPA CFTLQELKLN NCGMGIGGGK ILAAALTECH RKSSAQGKPL
ALKVFVAGRN RLENDGATAL AEAFGIIGTL EEVHMPQNGI NHPGVTALAQ AFAINPLLRV
INLNDNTFTE KGGVAMAETL KTLRQVEVIN FGDCLVRSKG AVAIADAVRG GLPKLKELNL
SFCEIKRDAA LVVAEAVADK AELEKLDLNG NALGEEGCEQ LQEVMDSFNM AKVLASLSDD
EGEDEDEEEE GEEDDEEEED EEDEEDDDEE EEEQEEEEEP PQRGSGEEPA TPSRKILDPN
SGEPAPVLSS PTPTDLSTFL SFPSPEKLLR LGPKVSVLIV QQTDTSDPEK VVSAFLKVAS
VFRDDASVKT AVLDAIDALM KKAFSCSSFN SNTFLTRLLI HMGLLKSEDK IKAIPSLHGP
LMVLNHVVRQ DYFPKALAPL LLAFVTKPNG ALETCSFARH NLLQTLYNI
