ID RAN_MOUSE Reviewed; 216 AA. AC P62827; P17080; P28746; P28747; Q3U954; Q811M2; Q86V08; Q9CSP3; Q9CWI7; AC Q9CZA2; Q9UDJ5; Q9UEU9; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 190. DE RecName: Full=GTP-binding nuclear protein Ran; DE EC=3.6.5.- {ECO:0000250|UniProtKB:P62826}; DE AltName: Full=GTPase Ran; DE AltName: Full=Ras-like protein TC4; DE AltName: Full=Ras-related nuclear protein; GN Name=Ran; Synonyms=Rasl2-8; 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], AND TISSUE SPECIFICITY. RC TISSUE=Testis; RX PubMed=7849398; DOI=10.1007/bf00411457; RA Coutavas E.E., Hsieh C.M., Ren M., Drivas G.T., Rush M.G., RA D'Eustachio P.D.; RT "Tissue-specific expression of Ran isoforms in the mouse."; RL Mamm. Genome 5:623-628(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C3H/HeJ; TISSUE=Spleen; RX PubMed=8890215; DOI=10.1128/iai.64.11.4612-4617.1996; RA Kang A.D., Wong P.M., Chen H., Castagna R., Chung S.W., Sultzer B.M.; RT "Restoration of lipopolysaccharide-mediated B-cell response after RT expression of a cDNA encoding a GTP-binding protein."; RL Infect. Immun. 64:4612-4617(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C3H/HeJ; RX PubMed=10500213; DOI=10.1073/pnas.96.20.11543; RA Wong P.M.C., Kang A., Chen H., Yuan Q., Fan P., Sultzer B.M., Kan Y.W., RA Chung S.-W.; RT "Lps(d)/Ran of endotoxin-resistant C3H/HeJ mice is defective in mediating RT lipopolysaccharide endotoxin responses."; RL Proc. Natl. Acad. Sci. U.S.A. 96:11543-11548(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=BALB/cJ, C57BL/6J, and NOD; RC TISSUE=Bone marrow, Embryo, Embryonic stem cell, Thymus, and Tongue; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-70. RC TISSUE=Kidney; RX PubMed=1555775; DOI=10.1016/0378-1119(92)90387-5; RA Chavrier P., Simons K., Zerial M.; RT "The complexity of the Rab and Rho GTP-binding protein subfamilies revealed RT by a PCR cloning approach."; RL Gene 112:261-264(1992). RN [7] RP PROTEIN SEQUENCE OF 2-23; 57-71 AND 143-152, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic fibroblast; RA Bienvenut W.V., Sandilands E., Serrels B., Brunton V.G., Frame M.C.; RL Submitted (FEB-2008) to UniProtKB. RN [8] RP INTERACTION WITH RANBP1. 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 [9] RP INTERACTION WITH RANBP1. RX PubMed=9428644; DOI=10.1016/s0014-5793(97)01467-1; RA Bischoff F.R., Goerlich D.; RT "RanBP1 is crucial for the release of RanGTP from importin beta-related RT nuclear transport factors."; RL FEBS Lett. 419:249-254(1997). RN [10] RP INTERACTION WITH RANGRF, AND MUTAGENESIS OF GLN-69. RX PubMed=10811801; DOI=10.1074/jbc.c000252200; RA Steggerda S.M., Paschal B.M.; RT "The mammalian Mog1 protein is a guanine nucleotide release factor for RT Ran."; RL J. Biol. Chem. 275:23175-23180(2000). RN [11] RP INTERACTION WITH RANBP10, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-24 RP AND GLN-69. RX PubMed=18347012; DOI=10.1074/jbc.m709397200; RA Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr., RA Shivdasani R.A.; RT "RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates RT noncentrosomal microtubules."; RL J. Biol. Chem. 283:14109-14119(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-159, SUCCINYLATION [LARGE SCALE RP ANALYSIS] AT LYS-159, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [14] 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 [15] RP INTERACTION WITH NEMP1 AND KPNB1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP THR-24; THR-42 AND GLN-69. RX PubMed=25946333; DOI=10.1371/journal.pone.0127271; RA Shibano T., Mamada H., Hakuno F., Takahashi S., Taira M.; RT "The inner nuclear membrane protein Nemp1 is a new type of RanGTP-binding RT protein in eukaryotes."; RL PLoS ONE 10:E0127271-E0127271(2015). CC -!- FUNCTION: GTPase involved in nucleocytoplasmic transport, participating CC both to the import and the export from the nucleus of proteins and CC RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state CC by nucleotide exchange and GTP hydrolysis. Nuclear import receptors CC such as importin beta bind their substrates only in the absence of GTP- CC bound RAN and release them upon direct interaction with GTP-bound RAN, CC while export receptors behave in the opposite way. Thereby, RAN CC controls cargo loading and release by transport receptors in the proper CC compartment and ensures the directionality of the transport. CC Interaction with RANBP1 induces a conformation change in the complex CC formed by XPO1 and RAN that triggers the release of the nuclear export CC signal of cargo proteins. RAN (GTP-bound form) triggers microtubule CC assembly at mitotic chromosomes and is required for normal mitotic CC spindle assembly and chromosome segregation. Required for normal CC progress through mitosis. The complex with BIRC5/survivin plays a role CC in mitotic spindle formation by serving as a physical scaffold to help CC deliver the RAN effector molecule TPX2 to microtubules. Acts as a CC negative regulator of the kinase activity of VRK1 and VRK2. Enhances CC AR-mediated transactivation. {ECO:0000250|UniProtKB:P62826}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000250|UniProtKB:P62826}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P62826}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P62826}; CC Note=Mg(2+) interacts primarily with the phosphate groups of the bound CC guanine nucleotide. {ECO:0000250|UniProtKB:P62826}; CC -!- SUBUNIT: Monomer. Interacts with RANGAP1, which promotes RAN-mediated CC GTP hydrolysis. Interacts with KPNB1. Interaction with KPNB1 inhibits CC RANGAP1-mediated stimulation of GTPase activity. Interacts with RCC1 CC which promotes the exchange of RAN-bound GDP by GTP. Interaction with CC KPNB1 inhibits RCC1-mediated exchange of RAN-bound GDP by GTP. CC Interacts (GTP-bound form) with TNPO1; the interaction is direct. CC Interacts (GTP-bound form) with TNPO3; the interaction is direct. CC Interacts with KPNB1 and with TNPO1; both inhibit RAN GTPase activity CC (By similarity). Interacts (via C-terminus) with RANBP1, which CC alleviates the inhibition of RAN GTPase activity (PubMed:7891706, CC PubMed:9428644). Interacts with RANGRF, which promotes the release of CC bound guanine nucleotide (PubMed:10811801). RANGRF and RCC1 compete for CC an overlapping binding site on RAN. Identified in a complex with KPNA2 CC and CSE1L; interaction with RANBP1 mediates dissociation of RAN from CC this complex. Interaction with both RANBP1 and KPNA2 promotes CC dissociation of the complex between RAN and KPNB1. Identified in a CC complex composed of RAN, RANGAP1 and RANBP1. Identified in a complex CC that contains TNPO1, RAN and RANBP1. Identified in a nuclear export CC complex with XPO1. Found in a nuclear export complex with RANBP3 and CC XPO1. Interacts with RANBP2/NUP358. Interaction with RANBP1 or RANBP2 CC induces a conformation change in the complex formed by XPO1 and RAN CC that triggers the release of the nuclear export signal of cargo CC proteins. Component of a nuclear export receptor complex composed of CC KPNB1, RAN, SNUPN and XPO1 (By similarity). Found in a nuclear export CC complex with RAN, XPO5 and pre-miRNA (By similarity). Interacts (GTP- CC bound form) with XPO5 (By similarity). Part of a complex consisting of CC RANBP9, RAN, DYRK1B and COPS5 (By similarity). Interacts with RANBP9 CC and RANBP10 (PubMed:18347012). Interacts in its GTP-bound form with CC BIRC5/survivin at S and M phases of the cell cycle. Interacts with CC TERT; the interaction requires hydrogen peroxide-mediated CC phosphorylation of TERT and transports TERT to the nucleus. Interacts CC with MAD2L2. Interacts with VRK1 and VRK3. Interacts with VRK2 (By CC similarity). Interacts with NEMP1 and KPNB1 (PubMed:25946333). CC Interacts (GDP-bound form) with NUTF2; regulates RAN nuclear import. CC Interacts with CAPG; mediates CAPG nuclear import. Interacts with CC NUP153. Interacts with the AR N-terminal poly-Gln region; the CC interaction with AR is inversely correlated with the poly-Gln length CC (By similarity). Interacts with MYCBP2, which promotes RAN-mediated GTP CC hydrolysis (PubMed:26304119). Interacts with EPG5 (By similarity). CC {ECO:0000250|UniProtKB:P62825, ECO:0000250|UniProtKB:P62826, CC ECO:0000269|PubMed:10811801, ECO:0000269|PubMed:18347012, CC ECO:0000269|PubMed:25946333, ECO:0000269|PubMed:26304119, CC ECO:0000269|PubMed:7891706, ECO:0000269|PubMed:9428644}. CC -!- INTERACTION: CC P62827; Q6ZQE4: Nemp1; NbExp=7; IntAct=EBI-286564, EBI-12595939; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18347012, CC ECO:0000269|PubMed:25946333}. Nucleus envelope CC {ECO:0000269|PubMed:25946333}. Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P62826}. Cytoplasm CC {ECO:0000269|PubMed:18347012}. Melanosome CC {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during CC interphase. Becomes dispersed throughout the cytoplasm during mitosis CC (By similarity). Identified by mass spectrometry in melanosome CC fractions from stage I to stage IV (By similarity). CC {ECO:0000250|UniProtKB:P62826}. CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues, including CC testis. {ECO:0000269|PubMed:7849398}. CC -!- PTM: Acetylation by KAT5 at Lys-134 is increased during mitosis, CC impairs RANGRF binding and enhances RCC1 binding. Acetylation at Lys-37 CC enhances the association with nuclear export components. Deacetylation CC of Lys-37 by SIRT7 regulates the nuclear export of NF-kappa-B subunit CC RELA/p65. {ECO:0000250|UniProtKB:P62826}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family. CC {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; L32751; AAA64247.1; -; mRNA. DR EMBL; S83456; AAB50841.1; -; mRNA. DR EMBL; AF159256; AAD45343.1; -; mRNA. DR EMBL; AK010569; BAB27034.1; -; mRNA. DR EMBL; AK010672; BAB27105.1; -; mRNA. DR EMBL; AK012268; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK012844; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK075900; BAC36040.1; -; mRNA. DR EMBL; AK087974; BAC40068.1; -; mRNA. DR EMBL; AK151341; BAE30319.1; -; mRNA. DR EMBL; AK151937; BAE30813.1; -; mRNA. DR EMBL; AK153197; BAE31797.1; -; mRNA. DR EMBL; AK153411; BAE31971.1; -; mRNA. DR EMBL; AK160647; BAE35939.1; -; mRNA. DR EMBL; AK167040; BAE39208.1; -; mRNA. DR EMBL; AK168183; BAE40143.1; -; mRNA. DR EMBL; BC014829; AAH14829.3; -; mRNA. DR EMBL; BC083356; AAH83356.1; -; mRNA. DR EMBL; M79316; AAK14838.1; -; mRNA. DR CCDS; CCDS19693.1; -. DR PIR; I57020; I57020. DR PIR; JH0654; JH0654. DR RefSeq; NP_033417.1; NM_009391.3. DR RefSeq; XP_006504343.1; XM_006504280.3. DR AlphaFoldDB; P62827; -. DR BMRB; P62827; -. DR SMR; P62827; -. DR BioGRID; 202580; 59. DR IntAct; P62827; 6. DR MINT; P62827; -. DR STRING; 10090.ENSMUSP00000106975; -. DR GlyGen; P62827; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62827; -. DR PhosphoSitePlus; P62827; -. DR SwissPalm; P62827; -. DR REPRODUCTION-2DPAGE; P62827; -. DR CPTAC; non-CPTAC-3936; -. DR EPD; P62827; -. DR jPOST; P62827; -. DR MaxQB; P62827; -. DR PaxDb; 10090-ENSMUSP00000031383; -. DR PeptideAtlas; P62827; -. DR ProteomicsDB; 255095; -. DR Pumba; P62827; -. DR DNASU; 19384; -. DR Ensembl; ENSMUST00000031383.14; ENSMUSP00000031383.8; ENSMUSG00000029430.14. DR Ensembl; ENSMUST00000111343.2; ENSMUSP00000106975.2; ENSMUSG00000029430.14. DR GeneID; 19384; -. DR KEGG; mmu:19384; -. DR UCSC; uc008zsr.1; mouse. DR AGR; MGI:1333112; -. DR CTD; 5901; -. DR MGI; MGI:1333112; Ran. DR VEuPathDB; HostDB:ENSMUSG00000029430; -. DR eggNOG; KOG0096; Eukaryota. DR GeneTree; ENSGT00940000153786; -. DR HOGENOM; CLU_041217_13_0_1; -. DR InParanoid; P62827; -. DR OMA; GEIKFDC; -. DR OrthoDB; 5471873at2759; -. DR PhylomeDB; P62827; -. DR TreeFam; TF106302; -. DR Reactome; R-MMU-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF). DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs. DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation. DR BioGRID-ORCS; 19384; 32 hits in 81 CRISPR screens. DR ChiTaRS; Ran; mouse. DR PRO; PR:P62827; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; P62827; Protein. DR Bgee; ENSMUSG00000029430; Expressed in mesodermal cell in embryo and 285 other cell types or tissues. DR GO; GO:0005814; C:centriole; ISO:MGI. DR GO; GO:0000785; C:chromatin; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0001673; C:male germ cell nucleus; ISO:MGI. DR GO; GO:0002177; C:manchette; ISO:MGI. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0030496; C:midbody; ISO:MGI. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0005643; C:nuclear pore; ISO:MGI. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0055037; C:recycling endosome; ISO:MGI. DR GO; GO:0042565; C:RNA nuclear export complex; ISO:MGI. DR GO; GO:0036126; C:sperm flagellum; ISO:MGI. DR GO; GO:0045505; F:dynein intermediate chain binding; ISO:MGI. DR GO; GO:0003925; F:G protein activity; ISO:MGI. DR GO; GO:0019003; F:GDP binding; ISO:MGI. DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB. DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB. DR GO; GO:0061676; F:importin-alpha family protein binding; ISO:MGI. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0070883; F:pre-miRNA binding; IEA:Ensembl. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071389; P:cellular response to mineralocorticoid stimulus; IEA:Ensembl. DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB. DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl. DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI. DR GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB. DR GO; GO:0006606; P:protein import into nucleus; IDA:MGI. DR GO; GO:0008104; P:protein localization; IMP:MGI. DR GO; GO:1902570; P:protein localization to nucleolus; ISO:MGI. DR GO; GO:0031503; P:protein-containing complex localization; IMP:MGI. DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; ISO:MGI. DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; ISO:MGI. DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central. DR GO; GO:0061015; P:snRNA import into nucleus; ISS:UniProtKB. DR GO; GO:0007286; P:spermatid development; IEA:Ensembl. DR CDD; cd00877; Ran; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR002041; Ran_GTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR24071:SF0; GTP-BINDING NUCLEAR PROTEIN RAN; 1. DR PANTHER; PTHR24071; RAN GTPASE; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00627; GTPRANTC4. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51418; RAN; 1. DR Genevisible; P62827; MM. PE 1: Evidence at protein level; KW Acetylation; Cell cycle; Cell division; Cytoplasm; KW Direct protein sequencing; GTP-binding; Hydrolase; Isopeptide bond; KW Magnesium; Metal-binding; Mitosis; Nucleotide-binding; Nucleus; KW Phosphoprotein; Protein transport; Reference proteome; Transport; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.7" FT CHAIN 2..216 FT /note="GTP-binding nuclear protein Ran" FT /id="PRO_0000208697" FT REGION 211..216 FT /note="Interaction with RANBP1" FT /evidence="ECO:0000250|UniProtKB:P62826" FT BINDING 18..25 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62825" FT BINDING 36..42 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62825" FT BINDING 68 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62825" FT BINDING 122..125 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62825" FT BINDING 150..152 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62825" FT SITE 69 FT /note="Essential for GTP hydrolysis" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.7" FT MOD_RES 24 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 37 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 60 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 71 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 99 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 134 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 159 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 159 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT CROSSLNK 71 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P62826" FT CROSSLNK 71 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P62826" FT CROSSLNK 152 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MUTAGEN 24 FT /note="T->N: No effect on RANBP10-binding. Loss of FT interaction with NEMP1." FT /evidence="ECO:0000269|PubMed:18347012, FT ECO:0000269|PubMed:25946333" FT MUTAGEN 42 FT /note="T->A: Loss of interaction with NEMP1." FT /evidence="ECO:0000269|PubMed:25946333" FT MUTAGEN 69 FT /note="Q->L: Strongly decreases interaction with RANGRF. FT Partial decrease in RANBP10-binding. No effect on FT interaction with NEMP1 and KPNB1." FT /evidence="ECO:0000269|PubMed:10811801, FT ECO:0000269|PubMed:18347012, ECO:0000269|PubMed:25946333" FT CONFLICT 9 FT /note="V -> G (in Ref. 4; BAB27105)" FT /evidence="ECO:0000305" FT CONFLICT 43 FT /note="L -> P (in Ref. 4; BAB27105)" FT /evidence="ECO:0000305" FT CONFLICT 49 FT /note="P -> T (in Ref. 6; AAK14838)" FT /evidence="ECO:0000305" SQ SEQUENCE 216 AA; 24423 MW; D5C9B7275C34BCE0 CRC64; MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL VFHTNRGPIK FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLIG DPNLEFVAMP ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEDDDL //