RAN_MOUSE
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 03-AUG-2022, entry version 182.
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, Pancreas,
RC 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}.
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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; 56.
DR IntAct; P62827; 6.
DR MINT; P62827; -.
DR STRING; 10090.ENSMUSP00000031383; -.
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; P62827; -.
DR PeptideAtlas; P62827; -.
DR PRIDE; P62827; -.
DR ProteomicsDB; 255095; -.
DR DNASU; 19384; -.
DR Ensembl; ENSMUST00000031383; ENSMUSP00000031383; ENSMUSG00000029430.
DR Ensembl; ENSMUST00000111343; ENSMUSP00000106975; ENSMUSG00000029430.
DR GeneID; 19384; -.
DR KEGG; mmu:19384; -.
DR UCSC; uc008zsr.1; mouse.
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; TIVFHRK; -.
DR OrthoDB; 1083175at2759; -.
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; 31 hits in 77 CRISPR screens.
DR ChiTaRS; Ran; mouse.
DR PRO; PR:P62827; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P62827; protein.
DR Bgee; ENSMUSG00000029430; Expressed in ectoplacental cone and 282 other tissues.
DR Genevisible; P62827; MM.
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: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; ISO:MGI.
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:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
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:0043393; P:regulation of protein binding; ISO: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 Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR24071; PTHR24071; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00627; GTPRANTC4.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51418; RAN; 1.
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
