ID RAN_HUMAN Reviewed; 216 AA. AC P62826; A8K3Z8; P17080; P28746; P28747; Q6IPB2; Q86V08; Q8NI90; Q9CSP3; AC Q9CWI7; 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 218. DE RecName: Full=GTP-binding nuclear protein Ran; DE EC=3.6.5.- {ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:8636225}; DE AltName: Full=Androgen receptor-associated protein 24 {ECO:0000303|PubMed:10400640}; DE AltName: Full=GTPase Ran; DE AltName: Full=Ras-like protein TC4 {ECO:0000303|PubMed:2108320, ECO:0000303|PubMed:8276887, ECO:0000303|PubMed:8421051}; DE AltName: Full=Ras-related nuclear protein; GN Name=RAN; Synonyms=ARA24 {ECO:0000303|PubMed:10400640}; GN ORFNames=OK/SW-cl.81; 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], AND TISSUE SPECIFICITY. RC TISSUE=Teratocarcinoma; RX PubMed=2108320; DOI=10.1128/mcb.10.4.1793-1798.1990; RA Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P.; RT "Characterization of four novel ras-like genes expressed in a human RT teratocarcinoma cell line."; RL Mol. Cell. Biol. 10:1793-1798(1990). RN [2] RP SEQUENCE REVISION TO C-TERMINUS. RX PubMed=1855255; DOI=10.1016/0092-8674(91)90624-8; RA Matsumoto T., Beach D.H.; RT "Premature initiation of mitosis in yeast lacking RCC1 or an interacting RT GTPase."; RL Cell 66:347-360(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-19 RP AND GLN-69. RC TISSUE=Brain; RX PubMed=8421051; DOI=10.1083/jcb.120.2.313; RA Ren M., Drivas G.T., D'Eustachio P., Rush M.G.; RT "Ran/TC4: a small nuclear GTP-binding protein that regulates DNA RT synthesis."; RL J. Cell Biol. 120:313-323(1993). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH AR, AND FUNCTION. RC TISSUE=Brain; RX PubMed=10400640; DOI=10.1074/jbc.274.29.20229; RA Hsiao P.-W., Lin D.-L., Nakao R., Chang C.; RT "The linkage of Kennedy's neuron disease to ARA24, the first identified RT androgen receptor polyglutamine region-associated coactivator."; RL J. Biol. Chem. 274:20229-20234(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lymph, Ovary, Skin, and Uterus; 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 [12] RP PROTEIN SEQUENCE OF 2-23 AND 143-166, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Platelet; RA Bienvenut W.V., Claeys D.; RL Submitted (FEB-2006) to UniProtKB. RN [13] RP PROTEIN SEQUENCE OF 39-56 AND 153-166, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-216. RC TISSUE=Colon adenocarcinoma; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that are recognized by tumor-reactive RT CTL generated from TIL of colon cancer patients."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [15] RP PROTEIN SEQUENCE OF 65-76; 90-125; 128-147 AND 154-216, INTERACTION WITH RP RCC1, AND SUBCELLULAR LOCATION. RC TISSUE=Cervix carcinoma; RX PubMed=1961752; DOI=10.1073/pnas.88.23.10830; RA Bischoff F.R., Ponstingl H.; RT "Mitotic regulator protein RCC1 is complexed with a nuclear ras-related RT polypeptide."; RL Proc. Natl. Acad. Sci. U.S.A. 88:10830-10834(1991). RN [16] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=8276887; DOI=10.1083/jcb.123.6.1649; RA Melchior F., Paschal B., Evans J., Gerace L.; RT "Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP RT and identification of the small GTPase Ran/TC4 as an essential transport RT factor."; RL J. Cell Biol. 123:1649-1659(1993). RN [17] RP FUNCTION, INTERACTION WITH RCC1, AND MUTAGENESIS OF THR-24 AND GLN-69. RX PubMed=7819259; DOI=10.1021/bi00002a031; RA Klebe C., Bischoff F.R., Ponstingl H., Wittinghofer A.; RT "Interaction of the nuclear GTP-binding protein Ran with its regulatory RT proteins RCC1 and RanGAP1."; RL Biochemistry 34:639-647(1995). RN [18] RP INTERACTION WITH RANBP1, AND MUTAGENESIS OF 211-ASP--LEU-216. 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 [19] RP FUNCTION, INTERACTION WITH RANBP1 AND KPNB1, AND SUBCELLULAR LOCATION. 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 [20] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-24 AND GLN-69. RX PubMed=8636225; DOI=10.1083/jcb.133.3.485; RA Palacios I., Weis K., Klebe C., Mattaj I.W., Dingwall C.; RT "RAN/TC4 mutants identify a common requirement for snRNP and protein import RT into the nucleus."; RL J. Cell Biol. 133:485-494(1996). RN [21] RP FUNCTION. RX PubMed=8692944; DOI=10.1073/pnas.93.14.7059; RA Moroianu J., Blobel G., Radu A.; RT "Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta RT heterodimer by displacing alpha from an overlapping binding site on beta."; RL Proc. Natl. Acad. Sci. U.S.A. 93:7059-7062(1996). RN [22] RP IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH XPO1. RX PubMed=9323133; DOI=10.1016/s0092-8674(00)80371-2; RA Fornerod M., Ohno M., Yoshida M., Mattaj I.W.; RT "CRM1 is an export receptor for leucine-rich nuclear export signals."; RL Cell 90:1051-1060(1997). RN [23] RP FUNCTION, INTERACTION WITH TNPO1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP THR-24 AND GLN-69. RX PubMed=9351834; DOI=10.1093/emboj/16.21.6535; RA Izaurralde E., Kutay U., von Kobbe C., Mattaj I.W., Goerlich D.; RT "The asymmetric distribution of the constituents of the Ran system is RT essential for transport into and out of the nucleus."; RL EMBO J. 16:6535-6547(1997). RN [24] RP FUNCTION, INTERACTION WITH RANBP1 AND KPNB1, AND SUBUNIT. 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 [25] RP FUNCTION, INTERACTION WITH NUTF2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP GLN-69 AND ARG-76. RX PubMed=9822603; DOI=10.1093/emboj/17.22.6587; RA Ribbeck K., Lipowsky G., Kent H.M., Stewart M., Goerlich D.; RT "NTF2 mediates nuclear import of Ran."; RL EMBO J. 17:6587-6598(1998). RN [26] RP IDENTIFICATION IN A COMPLEX WITH HIV-1 REV; HIV-1 REV RESPONSE ELEMENT AND RP XPO1 (MICROBIAL INFECTION). RX PubMed=9837918; DOI=10.1074/jbc.273.50.33414; RA Askjaer P., Jensen T.H., Nilsson J., Englmeier L., Kjems J.; RT "The specificity of the CRM1-Rev nuclear export signal interaction is RT mediated by RanGTP."; RL J. Biol. Chem. 273:33414-33422(1998). RN [27] RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX, AND IDENTIFICATION IN RP A TRIMERIC EXPORT COMPLEX WITH SNUPN AND XPO1. RX PubMed=10209022; DOI=10.1083/jcb.145.2.255; RA Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U., RA Hartmann E., Luehrmann R., Goerlich D.; RT "CRM1-mediated recycling of snurportin 1 to the cytoplasm."; RL J. Cell Biol. 145:255-264(1999). RN [28] RP FUNCTION, AND MUTAGENESIS OF THR-24 AND GLN-69. RX PubMed=10408446; DOI=10.1038/22133; RA Carazo-Salas R.E., Guarguaglini G., Gruss O.J., Segref A., Karsenti E., RA Mattaj I.W.; RT "Generation of GTP-bound Ran by RCC1 is required for chromatin-induced RT mitotic spindle formation."; RL Nature 400:178-181(1999). RN [29] RP INTERACTION WITH NUTF2, AND SUBCELLULAR LOCATION. RX PubMed=10679025; DOI=10.1091/mbc.11.2.703; RA Steggerda S.M., Black B.E., Paschal B.M.; RT "Monoclonal antibodies to NTF2 inhibit nuclear protein import by preventing RT nuclear translocation of the GTPase Ran."; RL Mol. Biol. Cell 11:703-719(2000). RN [30] RP IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RANBP3 AND XPO1. RX PubMed=11571268; DOI=10.1093/embo-reports/kve200; RA Englmeier L., Fornerod M., Bischoff F.R., Petosa C., Mattaj I.W., Kutay U.; RT "RanBP3 influences interactions between CRM1 and its nuclear protein export RT substrates."; RL EMBO Rep. 2:926-932(2001). RN [31] RP IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RANBP3 AND XPO1. RX PubMed=11425870; DOI=10.1083/jcb.153.7.1391; RA Lindsay M.E., Holaska J.M., Welch K., Paschal B.M., Macara I.G.; RT "Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein RT export."; RL J. Cell Biol. 153:1391-1402(2001). RN [32] RP IDENTIFICATION IN A COMPLEX WITH COPS5; RANBP9 AND DYRK1B. RX PubMed=14500717; DOI=10.1074/jbc.m307556200; RA Zou Y., Lim S., Lee K., Deng X., Friedman E.; RT "Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell RT migration and is negatively regulated by the Met adaptor Ran-binding RT protein M."; RL J. Biol. Chem. 278:49573-49581(2003). RN [33] RP INTERACTION WITH RCC1, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP THR-24 AND GLN-69. RX PubMed=12194828; DOI=10.1016/s0960-9822(02)01076-x; RA Moore W., Zhang C., Clarke P.R.; RT "Targeting of RCC1 to chromosomes is required for proper mitotic spindle RT assembly in human cells."; RL Curr. Biol. 12:1442-1447(2002). RN [34] RP INTERACTION WITH TERT. RX PubMed=12808100; DOI=10.1128/mcb.23.13.4598-4610.2003; RA Haendeler J., Hoffmann J., Brandes R.P., Zeiher A.M., Dimmeler S.; RT "Hydrogen peroxide triggers nuclear export of telomerase reverse RT transcriptase via Src kinase family-dependent phosphorylation of tyrosine RT 707."; RL Mol. Cell. Biol. 23:4598-4610(2003). RN [35] RP IDENTIFICATION IN A COMPLEX WITH HTLV-1 REX; RANBP3 AND XPO1 (MICROBIAL RP INFECTION). RX PubMed=14612415; DOI=10.1128/mcb.23.23.8751-8761.2003; RA Hakata Y., Yamada M., Shida H.; RT "A multifunctional domain in human CRM1 (exportin 1) mediates RanBP3 RT binding and multimerization of human T-cell leukemia virus type 1 Rex RT protein."; RL Mol. Cell. Biol. 23:8751-8761(2003). RN [36] 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 [37] RP INTERACTION WITH RANBP9 AND RANBP10. RX PubMed=14684163; DOI=10.1016/j.bbrc.2003.11.124; RA Wang D., Li Z., Schoen S.R., Messing E.M., Wu G.; RT "A novel MET-interacting protein shares high sequence similarity with RT RanBPM, but fails to stimulate MET-induced Ras/Erk signaling."; RL Biochem. Biophys. Res. Commun. 313:320-326(2004). RN [38] RP IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH XPO1. RX PubMed=15574331; DOI=10.1016/j.molcel.2004.11.018; RA Petosa C., Schoehn G., Askjaer P., Bauer U., Moulin M., Steuerwald U., RA Soler-Lopez M., Baudin F., Mattaj I.W., Mueller C.W.; RT "Architecture of CRM1/Exportin1 suggests how cooperativity is achieved RT during formation of a nuclear export complex."; RL Mol. Cell 16:761-775(2004). RN [39] RP IDENTIFICATION IN A COMPLEX WITH RANBP1 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 [40] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [41] RP FUNCTION, AND MUTAGENESIS OF GLN-69. RX PubMed=17209048; DOI=10.1074/jbc.m607180200; RA Yamashita D., Komori H., Higuchi Y., Yamaguchi T., Osumi T., Hirose F.; RT "Human DNA replication-related element binding factor (hDREF) self- RT association via hATC domain is necessary for its nuclear accumulation and RT DNA binding."; RL J. Biol. Chem. 282:7563-7575(2007). RN [42] RP FUNCTION, INTERACTION WITH BIRC5, AND MUTAGENESIS OF THR-24 AND GLN-69. RX PubMed=18591255; DOI=10.1128/mcb.02039-07; RA Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.; RT "A survivin-ran complex regulates spindle formation in tumor cells."; RL Mol. Cell. Biol. 28:5299-5311(2008). RN [43] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VRK1; VRK2 AND VRK3. RX PubMed=18617507; DOI=10.1074/mcp.m700586-mcp200; RA Sanz-Garcia M., Lopez-Sanchez I., Lazo P.A.; RT "Proteomics identification of nuclear Ran GTPase as an inhibitor of human RT VRK1 and VRK2 (vaccinia-related kinase) activities."; RL Mol. Cell. Proteomics 7:2199-2214(2008). RN [44] RP INTERACTION WITH CAPG AND NUTF2. RX PubMed=18266911; DOI=10.1111/j.1600-0854.2008.00720.x; RA Van Impe K., Hubert T., De Corte V., Vanloo B., Boucherie C., RA Vandekerckhove J., Gettemans J.; RT "A new role for nuclear transport factor 2 and Ran: nuclear import of RT CapG."; RL Traffic 9:695-707(2008). RN [45] 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 [46] RP INTERACTION WITH MAD2L2, AND SUBCELLULAR LOCATION. RX PubMed=19753112; DOI=10.1371/journal.pone.0007020; RA Medendorp K., van Groningen J.J., Vreede L., Hetterschijt L., RA van den Hurk W.H., de Bruijn D.R., Brugmans L., van Kessel A.G.; RT "The mitotic arrest deficient protein MAD2B interacts with the small GTPase RT RAN throughout the cell cycle."; RL PLoS ONE 4:E7020-E7020(2009). RN [47] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-71; LYS-99 AND LYS-159, RP AND 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 [48] RP FUNCTION, AND SUBUNIT. 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 [49] 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 [50] 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=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [51] 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=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [52] RP INTERACTION WITH TNPO3, AND MUTAGENESIS OF GLN-69. RX PubMed=23878195; DOI=10.1074/jbc.m113.484345; RA Taltynov O., Demeulemeester J., Christ F., De Houwer S., Tsirkone V.G., RA Gerard M., Weeks S.D., Strelkov S.V., Debyser Z.; RT "Interaction of transportin-SR2 with Ras-related nuclear protein (Ran) RT GTPase."; RL J. Biol. Chem. 288:25603-25613(2013). RN [53] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [54] RP IDENTIFICATION BY 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 [55] RP INTERACTION WITH MENGO ENCEPHALOMYOCARDITIS VIRUS LEADER PROTEIN (MICROBIAL RP INFECTION). RX PubMed=25331866; DOI=10.1073/pnas.1411098111; RA Bacot-Davis V.R., Ciomperlik J.J., Basta H.A., Cornilescu C.C., RA Palmenberg A.C.; RT "Solution structures of Mengovirus Leader protein, its phosphorylated RT derivatives, and in complex with nuclear transport regulatory protein, RT RanGTPase."; RL Proc. Natl. Acad. Sci. U.S.A. 111:15792-15797(2014). RN [56] 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 [57] 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 [58] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-71 AND LYS-152, AND RP IDENTIFICATION BY MASS 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 [59] RP INTERACTION WITH EPG5. RX PubMed=29130391; DOI=10.1080/15548627.2017.1389356; RA Piano Mortari E., Folgiero V., Marcellini V., Romania P., Bellacchio E., RA D'Alicandro V., Bocci C., Carrozzo R., Martinelli D., Petrini S., RA Axiotis E., Farroni C., Locatelli F., Schara U., Pilz D.T., Jungbluth H., RA Dionisi-Vici C., Carsetti R.; RT "The Vici syndrome protein EPG5 regulates intracellular nucleic acid RT trafficking linking autophagy to innate and adaptive immunity."; RL Autophagy 14:22-37(2018). RN [60] RP FUNCTION, INTERACTION WITH RANGRF AND RCC1, ACETYLATION AT LYS-134, RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-134. RX PubMed=29040603; DOI=10.1093/jmcb/mjx045; RA Bao X., Liu H., Liu X., Ruan K., Zhang Y., Zhang Z., Hu Q., Liu Y., RA Akram S., Zhang J., Gong Q., Wang W., Yuan X., Li J., Zhao L., Dou Z., RA Tian R., Yao X., Wu J., Shi Y.; RT "Mitosis-specific acetylation tunes Ran effector binding for chromosome RT segregation."; RL J. Mol. Cell Biol. 10:18-32(2018). RN [61] RP ACETYLATION AT LYS-37, DEACETYLATION, SUBCELLULAR LOCATION, AND MUTAGENESIS RP OF LYS-37. RX PubMed=31075303; DOI=10.1016/j.bbamcr.2019.05.001; RA Sobuz S.U., Sato Y., Yoshizawa T., Karim F., Ono K., Sawa T., Miyamoto Y., RA Oka M., Yamagata K.; RT "SIRT7 regulates the nuclear export of NF-kappaB p65 by deacetylating RT Ran."; RL Biochim. Biophys. Acta 1866:1355-1367(2019). RN [62] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GDP. RX PubMed=7885480; DOI=10.1038/374378a0; RA Scheffzek K., Klebe C., Fritz-Wolf K., Kabsch W., Wittinghofer A.; RT "Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound RT form."; RL Nature 374:378-381(1995). RN [63] {ECO:0007744|PDB:1IBR} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH GTP ANALOG AND RP KPNB1. RX PubMed=10367892; DOI=10.1016/s0092-8674(00)80774-6; RA Vetter I.R., Arndt A., Kutay U., Goerlich D., Wittinghofer A.; RT "Structural view of the Ran-Importin beta interaction at 2.3 A RT resolution."; RL Cell 97:635-646(1999). RN [64] {ECO:0007744|PDB:1QBK} RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH GTP ANALOG AND KPNB2. RX PubMed=10353245; DOI=10.1038/20375; RA Chook Y.M., Blobel G.; RT "Structure of the nuclear transport complex karyopherin-beta2-Ran x RT GppNHp."; RL Nature 399:230-237(1999). RN [65] RP X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) IN COMPLEX WITH GTP ANALOG AND RP RANBP2. RX PubMed=10078529; DOI=10.1038/17969; RA Vetter I.R., Nowak C., Nishimoto T., Kuhlmann J., Wittinghofer A.; RT "Structure of a Ran-binding domain complexed with Ran bound to a GTP RT analogue: implications for nuclear transport."; RL Nature 398:39-46(1999). RN [66] {ECO:0007744|PDB:1I2M} RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH RCC1, FUNCTION, RP INTERACTION WITH RCC1, AND MUTAGENESIS OF GLU-70. RX PubMed=11336674; DOI=10.1016/s0092-8674(01)00315-4; RA Renault L., Kuhlmann J., Henkel A., Wittinghofer A.; RT "Structural basis for guanine nucleotide exchange on Ran by the regulator RT of chromosome condensation (RCC1)."; RL Cell 105:245-255(2001). RN [67] {ECO:0007744|PDB:1K5D, ECO:0007744|PDB:1K5G} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEXES WITH GTP ANALOGS; RP RANBP1 AND FISSION YEAST 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 [68] {ECO:0007744|PDB:3CH5} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH GDP ANALOG AND RP NUP153. RX PubMed=18611384; DOI=10.1016/j.str.2008.03.014; RA Schrader N., Koerner C., Koessmeier K., Bangert J.A., Wittinghofer A., RA Stoll R., Vetter I.R.; RT "The crystal structure of the Ran-Nup153ZnF2 complex: a general Ran docking RT site at the nuclear pore complex."; RL Structure 16:1116-1125(2008). RN [69] {ECO:0007744|PDB:3GJ0, ECO:0007744|PDB:3GJ3, ECO:0007744|PDB:3GJ4, ECO:0007744|PDB:3GJ5, ECO:0007744|PDB:3GJ6, ECO:0007744|PDB:3GJ7, ECO:0007744|PDB:3GJ8} RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 2-216 IN COMPLEX WITH GDP ANALOG RP AND NUP153. RX PubMed=19505478; DOI=10.1016/j.jmb.2009.06.011; RA Partridge J.R., Schwartz T.U.; RT "Crystallographic and biochemical analysis of the Ran-binding zinc finger RT domain."; RL J. Mol. Biol. 391:375-389(2009). RN [70] {ECO:0007744|PDB:3GJX} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH GTP; XPO1 AND SNUPN, RP AND IDENTIFICATION IN A COMPLEX WITH XPO1 AND SNUPN. RX PubMed=19389996; DOI=10.1126/science.1173388; RA Monecke T., Guttler T., Neumann P., Dickmanns A., Gorlich D., Ficner R.; RT "Crystal structure of the nuclear export receptor CRM1 in complex with RT Snurportin1 and RanGTP."; RL Science 324:1087-1091(2009). RN [71] {ECO:0007744|PDB:4OL0} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF MUTANT ASN-69 IN COMPLEX WITH GTP RP AND TNPO3, AND MUTAGENESIS OF GLN-69. RX PubMed=24915079; DOI=10.1107/s2053230x14009492; RA Tsirkone V.G., Beutels K.G., Demeulemeester J., Debyser Z., Christ F., RA Strelkov S.V.; RT "Structure of transportin SR2, a karyopherin involved in human disease, in RT complex with Ran."; RL Acta Crystallogr. F 70:723-729(2014). RN [72] {ECO:0007744|PDB:4C0Q} RP X-RAY CRYSTALLOGRAPHY (3.42 ANGSTROMS) OF 2-216 IN COMPLEX WITH GTP AND RP TNPO3. RX PubMed=24449914; DOI=10.1073/pnas.1320755111; RA Maertens G.N., Cook N.J., Wang W., Hare S., Gupta S.S., Oztop I., Lee K., RA Pye V.E., Cosnefroy O., Snijders A.P., KewalRamani V.N., Fassati A., RA Engelman A., Cherepanov P.; RT "Structural basis for nuclear import of splicing factors by human RT Transportin 3."; RL Proc. Natl. Acad. Sci. U.S.A. 111:2728-2733(2014). RN [73] {ECO:0007744|PDB:5DH9, ECO:0007744|PDB:5DHA, ECO:0007744|PDB:5DHF, ECO:0007744|PDB:5DI9, ECO:0007744|PDB:5DIF} RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH GTP ANALOG; CPEB4 RP NUCLEAR EXPORT SIGNAL AND YEAST HOMOLOGS OF XPO1 AND RANGAP1. RX PubMed=26349033; DOI=10.7554/elife.10034; RA Fung H.Y., Fu S.C., Brautigam C.A., Chook Y.M.; RT "Structural determinants of nuclear export signal orientation in binding to RT exportin CRM1."; RL Elife 4:0-0(2015). RN [74] {ECO:0007744|PDB:5CIQ, ECO:0007744|PDB:5CIT, ECO:0007744|PDB:5CIW, ECO:0007744|PDB:5CJ2, ECO:0007744|PDB:5CLL, ECO:0007744|PDB:5CLQ} RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEXES WITH GTP ANALOGS AND RP RANBP2, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RANBP2, COFACTOR, RP AND MUTAGENESIS OF THR-25 AND TYR-39. RX PubMed=26272610; DOI=10.1074/jbc.m115.648071; RA Rudack T., Jenrich S., Brucker S., Vetter I.R., Gerwert K., Kotting C.; RT "Catalysis of GTP hydrolysis by small GTPases at atomic detail by RT integration of X-ray crystallography, experimental, and theoretical IR RT spectroscopy."; RL J. Biol. Chem. 290:24079-24090(2015). RN [75] {ECO:0007744|PDB:5DLQ} RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 5-180 IN COMPLEX WITH XPO4 AND RP EIF5A, AND FUNCTION. RX PubMed=27306458; DOI=10.1038/ncomms11952; RA Aksu M., Trakhanov S., Goerlich D.; RT "Structure of the exportin Xpo4 in complex with RanGTP and the hypusine- RT containing translation factor eIF5A."; RL Nat. Commun. 7:11952-11952(2016). RN [76] {ECO:0007744|PDB:5UWH, ECO:0007744|PDB:5UWI, ECO:0007744|PDB:5UWJ, ECO:0007744|PDB:5UWO, ECO:0007744|PDB:5UWP, ECO:0007744|PDB:5UWQ, ECO:0007744|PDB:5UWR, ECO:0007744|PDB:5UWS, ECO:0007744|PDB:5UWT, ECO:0007744|PDB:5UWU, ECO:0007744|PDB:5UWW} RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH GTP ANALOG AND THE RP YEAST HOMOLOGS OF XPO1 AND RANGAP1. RX PubMed=28282025; DOI=10.7554/elife.23961; RA Fung H.Y., Fu S.C., Chook Y.M.; RT "Nuclear export receptor CRM1 recognizes diverse conformations in nuclear RT export signals."; RL Elife 6:0-0(2017). CC -!- FUNCTION: GTPase involved in nucleocytoplasmic transport, participating CC both to the import and the export from the nucleus of proteins and RNAs CC (PubMed:10400640, PubMed:8276887, PubMed:8896452, PubMed:8636225, CC PubMed:8692944, PubMed:9351834, PubMed:9428644, PubMed:9822603, CC PubMed:17209048, PubMed:26272610, PubMed:27306458). Switches between a CC cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange CC and GTP hydrolysis (PubMed:7819259, PubMed:8896452, PubMed:8636225, CC PubMed:8692944, PubMed:9351834, PubMed:9428644, PubMed:9822603, CC PubMed:29040603, PubMed:11336674, PubMed:26272610). Nuclear import CC receptors such as importin beta bind their substrates only in the CC absence of GTP-bound RAN and release them upon direct interaction with CC GTP-bound RAN, while export receptors behave in the opposite way. CC Thereby, RAN controls cargo loading and release by transport receptors CC in the proper compartment and ensures the directionality of the CC transport (PubMed:8896452, PubMed:9351834, PubMed:9428644). Interaction CC with RANBP1 induces a conformation change in the complex formed by XPO1 CC and RAN that triggers the release of the nuclear export signal of cargo CC proteins (PubMed:20485264). RAN (GTP-bound form) triggers microtubule CC assembly at mitotic chromosomes and is required for normal mitotic CC spindle assembly and chromosome segregation (PubMed:10408446, CC PubMed:29040603). Required for normal progress through mitosis CC (PubMed:8421051, PubMed:12194828, PubMed:29040603). The complex with CC BIRC5/survivin plays a role in mitotic spindle formation by serving as CC a physical scaffold to help deliver the RAN effector molecule TPX2 to CC microtubules (PubMed:18591255). Acts as a negative regulator of the CC kinase activity of VRK1 and VRK2 (PubMed:18617507). Enhances AR- CC mediated transactivation. Transactivation decreases as the poly-Gln CC length within AR increases (PubMed:10400640). CC {ECO:0000269|PubMed:10400640, ECO:0000269|PubMed:10408446, CC ECO:0000269|PubMed:11336674, ECO:0000269|PubMed:12194828, CC ECO:0000269|PubMed:17209048, ECO:0000269|PubMed:18591255, CC ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:20485264, CC ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:27306458, CC ECO:0000269|PubMed:29040603, ECO:0000269|PubMed:7819259, CC ECO:0000269|PubMed:8276887, ECO:0000269|PubMed:8421051, CC ECO:0000269|PubMed:8636225, ECO:0000269|PubMed:8692944, CC ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9351834, CC ECO:0000269|PubMed:9428644, ECO:0000269|PubMed:9822603, CC ECO:0000305|PubMed:26272610}. 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:0000269|PubMed:26272610, ECO:0000269|PubMed:8636225}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:8636225}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:26272610}; CC Note=Mg(2+) interacts primarily with the phosphate groups of the bound CC guanine nucleotide. {ECO:0000269|PubMed:26272610}; CC -!- SUBUNIT: Monomer. Interacts with RANGAP1, which promotes RAN-mediated CC GTP hydrolysis (PubMed:7819259, PubMed:9428644). Interacts with KPNB1 CC (PubMed:8896452, PubMed:9428644, PubMed:10367892). Interaction with CC KPNB1 inhibits RANGAP1-mediated stimulation of GTPase activity CC (PubMed:9428644). Interacts with RCC1 which promotes the exchange of CC RAN-bound GDP by GTP (PubMed:1961752, PubMed:7819259, PubMed:12194828, CC PubMed:11336674). Interaction with KPNB1 inhibits RCC1-mediated CC exchange of RAN-bound GDP by GTP (PubMed:8896452). Interacts (GTP-bound CC form) with TNPO1; the interaction is direct (PubMed:9351834). Interacts CC (GTP-bound form) with TNPO3; the interaction is direct CC (PubMed:23878195, PubMed:24915079, PubMed:24449914). Interacts with CC KPNB1 and with TNPO1; both inhibit RAN GTPase activity (PubMed:8896452, CC PubMed:9428644). Interacts (via C-terminus) with RANBP1, which CC alleviates the inhibition of RAN GTPase activity (PubMed:7891706, CC PubMed:8896452, PubMed:9428644, PubMed:11832950). Interacts with CC RANGRF, which promotes the release of bound guanine nucleotide CC (PubMed:29040603). RANGRF and RCC1 compete for an overlapping binding CC site on RAN (PubMed:29040603). Identified in a complex with KPNA2 and CC CSE1L; interaction with RANBP1 mediates dissociation of RAN from this CC complex (PubMed:9428644). Interaction with both RANBP1 and KPNA2 CC promotes dissociation of the complex between RAN and KPNB1 CC (PubMed:9428644). Identified in a complex composed of RAN, RANGAP1 and CC RANBP1 (PubMed:16428860). Identified in a complex that contains TNPO1, CC RAN and RANBP1 (PubMed:9428644). Identified in a nuclear export complex CC with XPO1 (PubMed:9323133, PubMed:15574331, PubMed:10209022). Found in CC a nuclear export complex with RANBP3 and XPO1 (PubMed:11571268, CC PubMed:11425870). Interacts with RANBP2/NUP358 (PubMed:10078529, CC PubMed:26272610). Interaction with RANBP1 or RANBP2 induces a CC conformation change in the complex formed by XPO1 and RAN that triggers CC the release of the nuclear export signal of cargo proteins CC (PubMed:20485264). Component of a nuclear export receptor complex CC composed of KPNB1, RAN, SNUPN and XPO1 (PubMed:10209022, CC PubMed:19389996). Found in a nuclear export complex with RAN, XPO5 and CC pre-miRNA (By similarity). Interacts (GTP-bound form) with XPO5 (By CC similarity). Part of a complex consisting of RANBP9, RAN, DYRK1B and CC COPS5 (PubMed:14500717). Interacts with RANBP9 and RANBP10 CC (PubMed:14684163). Interacts in its GTP-bound form with BIRC5/survivin CC at S and M phases of the cell cycle (PubMed:18591255). Interacts with CC TERT; the interaction requires hydrogen peroxide-mediated CC phosphorylation of TERT and transports TERT to the nucleus CC (PubMed:12808100). Interacts with MAD2L2 (PubMed:19753112). Interacts CC with VRK1 and VRK3 (PubMed:18617507). Interacts with isoform 1 and CC isoform 2 of VRK2 (PubMed:18617507). Interacts with NEMP1 and KPNB1 (By CC similarity). Interacts (GDP-bound form) with NUTF2; regulates RAN CC nuclear import (PubMed:9822603, PubMed:10679025, PubMed:18266911). CC Interacts with CAPG; mediates CAPG nuclear import (PubMed:10679025, CC PubMed:18266911). Interacts with NUP153 (PubMed:18611384, CC PubMed:19505478). Interacts with the AR N-terminal poly-Gln region; the CC interaction with AR is inversely correlated with the poly-Gln length CC (PubMed:10400640). Interacts with MYCBP2, which promotes RAN-mediated CC GTP hydrolysis (PubMed:26304119). Interacts with EPG5 CC (PubMed:29130391). {ECO:0000250|UniProtKB:P62825, CC ECO:0000250|UniProtKB:P62827, ECO:0000269|PubMed:10078529, CC ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:10400640, CC ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:11336674, CC ECO:0000269|PubMed:11425870, ECO:0000269|PubMed:11571268, CC ECO:0000269|PubMed:11832950, ECO:0000269|PubMed:12194828, CC ECO:0000269|PubMed:12808100, ECO:0000269|PubMed:14500717, CC ECO:0000269|PubMed:14684163, ECO:0000269|PubMed:15574331, CC ECO:0000269|PubMed:16428860, ECO:0000269|PubMed:18591255, CC ECO:0000269|PubMed:18611384, ECO:0000269|PubMed:18617507, CC ECO:0000269|PubMed:19389996, ECO:0000269|PubMed:19505478, CC ECO:0000269|PubMed:1961752, ECO:0000269|PubMed:19753112, CC ECO:0000269|PubMed:20485264, ECO:0000269|PubMed:23878195, CC ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24915079, CC ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26304119, CC ECO:0000269|PubMed:29040603, ECO:0000269|PubMed:29130391, CC ECO:0000269|PubMed:7819259, ECO:0000269|PubMed:7891706, CC ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9323133, CC ECO:0000269|PubMed:9351834, ECO:0000269|PubMed:9428644, CC ECO:0000269|PubMed:9822603}. CC -!- SUBUNIT: (Microbial infection) In case of HIV-1 infection, found in a CC complex with HIV-1 Rev, RNAs containing a Rev response element (RRE) CC and XPO1. {ECO:0000269|PubMed:9837918}. CC -!- SUBUNIT: (Microbial infection) Found in a complex with HTLV-1 Rex, CC RANBP3 and XPO1. {ECO:0000269|PubMed:14612415}. CC -!- SUBUNIT: (Microbial infection) Interacts with Mengo CC encephalomyocarditis virus Leader protein; the complex L-RAN recruits CC cellular kinases responsible for the L-induced nucleocytoplasmic CC trafficking inhibition. {ECO:0000269|PubMed:25331866}. CC -!- INTERACTION: CC P62826; Q9Y614: ACTL7B; NbExp=3; IntAct=EBI-286642, EBI-25835070; CC P62826; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-286642, EBI-18899653; CC P62826; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-286642, EBI-10173507; CC P62826; Q96MA6: AK8; NbExp=3; IntAct=EBI-286642, EBI-8466265; CC P62826; Q96Q83-2: ALKBH3; NbExp=3; IntAct=EBI-286642, EBI-9089544; CC P62826; Q9Y303-2: AMDHD2; NbExp=3; IntAct=EBI-286642, EBI-12323557; CC P62826; Q8WVL7: ANKRD49; NbExp=2; IntAct=EBI-286642, EBI-9381820; CC P62826; P09525: ANXA4; NbExp=3; IntAct=EBI-286642, EBI-2556852; CC P62826; Q8WW27: APOBEC4; NbExp=3; IntAct=EBI-286642, EBI-25836284; CC P62826; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-286642, EBI-5280499; CC P62826; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-286642, EBI-10254793; CC P62826; Q9H0Y0: ATG10; NbExp=3; IntAct=EBI-286642, EBI-1048913; CC P62826; Q14032: BAAT; NbExp=3; IntAct=EBI-286642, EBI-8994378; CC P62826; P06276: BCHE; NbExp=3; IntAct=EBI-286642, EBI-7936069; CC P62826; O15392: BIRC5; NbExp=7; IntAct=EBI-286642, EBI-518823; CC P62826; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-286642, EBI-10693038; CC P62826; Q96Q07-2: BTBD9; NbExp=3; IntAct=EBI-286642, EBI-22006737; CC P62826; Q9H0W9-3: C11orf54; NbExp=3; IntAct=EBI-286642, EBI-12108466; CC P62826; Q13901: C1D; NbExp=3; IntAct=EBI-286642, EBI-3844053; CC P62826; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-286642, EBI-18036948; CC P62826; P17655: CAPN2; NbExp=3; IntAct=EBI-286642, EBI-1028956; CC P62826; P20807-4: CAPN3; NbExp=3; IntAct=EBI-286642, EBI-11532021; CC P62826; O00257-3: CBX4; NbExp=3; IntAct=EBI-286642, EBI-4392727; CC P62826; Q9NNX6-10: CD209; NbExp=3; IntAct=EBI-286642, EBI-12300031; CC P62826; O95674: CDS2; NbExp=3; IntAct=EBI-286642, EBI-3913685; CC P62826; Q494V2-2: CFAP100; NbExp=3; IntAct=EBI-286642, EBI-11953200; CC P62826; Q8WUX9: CHMP7; NbExp=3; IntAct=EBI-286642, EBI-749253; CC P62826; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-286642, EBI-744045; CC P62826; Q3SX64: CIMAP1D; NbExp=3; IntAct=EBI-286642, EBI-6660184; CC P62826; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-286642, EBI-25836090; CC P62826; Q96BR5: COA7; NbExp=3; IntAct=EBI-286642, EBI-6269632; CC P62826; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-286642, EBI-713677; CC P62826; Q9UKG9-2: CROT; NbExp=3; IntAct=EBI-286642, EBI-25835363; CC P62826; P35222: CTNNB1; NbExp=3; IntAct=EBI-286642, EBI-491549; CC P62826; Q9H2U1-3: DHX36; NbExp=3; IntAct=EBI-286642, EBI-25868628; CC P62826; Q96EY1-3: DNAJA3; NbExp=3; IntAct=EBI-286642, EBI-11526226; CC P62826; Q92782-2: DPF1; NbExp=3; IntAct=EBI-286642, EBI-23669343; CC P62826; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-286642, EBI-724653; CC P62826; Q658K8: EEF1DP3; NbExp=3; IntAct=EBI-286642, EBI-10248874; CC P62826; O00472: ELL2; NbExp=3; IntAct=EBI-286642, EBI-395274; CC P62826; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-286642, EBI-25835236; CC P62826; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-286642, EBI-8468186; CC P62826; Q6ZNL6: FGD5; NbExp=3; IntAct=EBI-286642, EBI-7962481; CC P62826; P06241: FYN; NbExp=3; IntAct=EBI-286642, EBI-515315; CC P62826; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-286642, EBI-9088619; CC P62826; Q49A26-4: GLYR1; NbExp=3; IntAct=EBI-286642, EBI-12143817; CC P62826; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-286642, EBI-2868501; CC P62826; P62805: H4C9; NbExp=2; IntAct=EBI-286642, EBI-302023; CC P62826; Q9BT25: HAUS8; NbExp=3; IntAct=EBI-286642, EBI-2558143; CC P62826; Q9NRZ9-6: HELLS; NbExp=3; IntAct=EBI-286642, EBI-12003732; CC P62826; P42858: HTT; NbExp=6; IntAct=EBI-286642, EBI-466029; CC P62826; O94829: IPO13; NbExp=13; IntAct=EBI-286642, EBI-747310; CC P62826; P0C870: JMJD7; NbExp=3; IntAct=EBI-286642, EBI-9090173; CC P62826; Q9UK76: JPT1; NbExp=3; IntAct=EBI-286642, EBI-720411; CC P62826; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-286642, EBI-743960; CC P62826; Q8TBB5-2: KLHDC4; NbExp=3; IntAct=EBI-286642, EBI-21838933; CC P62826; Q8N1A0: KRT222; NbExp=3; IntAct=EBI-286642, EBI-8473062; CC P62826; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-286642, EBI-25835523; CC P62826; Q8N0U6: LINC00518; NbExp=3; IntAct=EBI-286642, EBI-10264791; CC P62826; Q16609: LPAL2; NbExp=3; IntAct=EBI-286642, EBI-10238012; CC P62826; Q8IYG6: LRRC56; NbExp=3; IntAct=EBI-286642, EBI-14752528; CC P62826; P27338: MAOB; NbExp=3; IntAct=EBI-286642, EBI-3911344; CC P62826; A6NJ78-4: METTL15; NbExp=3; IntAct=EBI-286642, EBI-10174029; CC P62826; A0A0A0MR05: MLST8; NbExp=3; IntAct=EBI-286642, EBI-25835557; CC P62826; Q6IN84-2: MRM1; NbExp=3; IntAct=EBI-286642, EBI-25835707; CC P62826; A2RUH7: MYBPHL; NbExp=3; IntAct=EBI-286642, EBI-9088235; CC P62826; P36639-4: NUDT1; NbExp=3; IntAct=EBI-286642, EBI-25834643; CC P62826; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-286642, EBI-741048; CC P62826; P61970: NUTF2; NbExp=6; IntAct=EBI-286642, EBI-591778; CC P62826; Q6N063-2: OGFOD2; NbExp=3; IntAct=EBI-286642, EBI-22006224; CC P62826; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-286642, EBI-25830200; CC P62826; Q9H8K7: PAAT; NbExp=3; IntAct=EBI-286642, EBI-714785; CC P62826; O15534: PER1; NbExp=3; IntAct=EBI-286642, EBI-2557276; CC P62826; Q9BUL5: PHF23; NbExp=3; IntAct=EBI-286642, EBI-722852; CC P62826; Q14181: POLA2; NbExp=3; IntAct=EBI-286642, EBI-712752; CC P62826; P0DPB6: POLR1D; NbExp=3; IntAct=EBI-286642, EBI-359498; CC P62826; P36954: POLR2I; NbExp=3; IntAct=EBI-286642, EBI-395202; CC P62826; Q07869: PPARA; NbExp=3; IntAct=EBI-286642, EBI-78615; CC P62826; O60927: PPP1R11; NbExp=3; IntAct=EBI-286642, EBI-1048104; CC P62826; Q8WUF5: PPP1R13L; NbExp=9; IntAct=EBI-286642, EBI-5550163; CC P62826; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-286642, EBI-25835994; CC P62826; Q8WUD1-2: RAB2B; NbExp=3; IntAct=EBI-286642, EBI-25835884; CC P62826; P49792: RANBP2; NbExp=4; IntAct=EBI-286642, EBI-973138; CC P62826; Q9HD47-3: RANGRF; NbExp=3; IntAct=EBI-286642, EBI-9089733; CC P62826; Q09028: RBBP4; NbExp=3; IntAct=EBI-286642, EBI-620823; CC P62826; P18754: RCC1; NbExp=15; IntAct=EBI-286642, EBI-992720; CC P62826; Q04206: RELA; NbExp=3; IntAct=EBI-286642, EBI-73886; CC P62826; P47804-3: RGR; NbExp=3; IntAct=EBI-286642, EBI-25834767; CC P62826; Q15382: RHEB; NbExp=3; IntAct=EBI-286642, EBI-1055287; CC P62826; Q8N5U6: RNF10; NbExp=3; IntAct=EBI-286642, EBI-714023; CC P62826; P62701: RPS4X; NbExp=3; IntAct=EBI-286642, EBI-354303; CC P62826; Q96IZ7: RSRC1; NbExp=3; IntAct=EBI-286642, EBI-712189; CC P62826; Q66K80: RUSC1-AS1; NbExp=3; IntAct=EBI-286642, EBI-10248967; CC P62826; P22307-3: SCP2; NbExp=3; IntAct=EBI-286642, EBI-25834804; CC P62826; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-286642, EBI-9089805; CC P62826; Q8IYM2: SLFN12; NbExp=3; IntAct=EBI-286642, EBI-2822550; CC P62826; Q86US8: SMG6; NbExp=3; IntAct=EBI-286642, EBI-3232100; CC P62826; P37840: SNCA; NbExp=3; IntAct=EBI-286642, EBI-985879; CC P62826; Q96H20: SNF8; NbExp=3; IntAct=EBI-286642, EBI-747719; CC P62826; Q13573: SNW1; NbExp=3; IntAct=EBI-286642, EBI-632715; CC P62826; Q496A3: SPATS1; NbExp=3; IntAct=EBI-286642, EBI-3923692; CC P62826; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-286642, EBI-5235340; CC P62826; Q9C004: SPRY4; NbExp=3; IntAct=EBI-286642, EBI-354861; CC P62826; Q5W111-2: SPRYD7; NbExp=3; IntAct=EBI-286642, EBI-12408727; CC P62826; Q96BD6: SPSB1; NbExp=3; IntAct=EBI-286642, EBI-2659201; CC P62826; Q92797-2: SYMPK; NbExp=3; IntAct=EBI-286642, EBI-21560407; CC P62826; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-286642, EBI-11123832; CC P62826; O15273: TCAP; NbExp=3; IntAct=EBI-286642, EBI-954089; CC P62826; Q86WV5: TEN1; NbExp=3; IntAct=EBI-286642, EBI-2562799; CC P62826; Q96A09: TENT5B; NbExp=3; IntAct=EBI-286642, EBI-752030; CC P62826; P54274-2: TERF1; NbExp=3; IntAct=EBI-286642, EBI-711018; CC P62826; Q9UIK5-2: TMEFF2; NbExp=3; IntAct=EBI-286642, EBI-25835153; CC P62826; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-286642, EBI-10242677; CC P62826; O14787-2: TNPO2; NbExp=3; IntAct=EBI-286642, EBI-12076664; CC P62826; Q12888: TP53BP1; NbExp=3; IntAct=EBI-286642, EBI-396540; CC P62826; Q13625: TP53BP2; NbExp=5; IntAct=EBI-286642, EBI-77642; CC P62826; P36406: TRIM23; NbExp=3; IntAct=EBI-286642, EBI-740098; CC P62826; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-286642, EBI-11525489; CC P62826; P49459: UBE2A; NbExp=3; IntAct=EBI-286642, EBI-2339348; CC P62826; P09936: UCHL1; NbExp=3; IntAct=EBI-286642, EBI-714860; CC P62826; Q9P1Q0-4: VPS54; NbExp=3; IntAct=EBI-286642, EBI-25835297; CC P62826; Q99986: VRK1; NbExp=12; IntAct=EBI-286642, EBI-1769146; CC P62826; Q86Y07-1: VRK2; NbExp=2; IntAct=EBI-286642, EBI-1207633; CC P62826; Q86Y07-5: VRK2; NbExp=2; IntAct=EBI-286642, EBI-1207649; CC P62826; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-286642, EBI-10316321; CC P62826; Q9BQA1: WDR77; NbExp=3; IntAct=EBI-286642, EBI-1237307; CC P62826; Q9UIA9: XPO7; NbExp=3; IntAct=EBI-286642, EBI-286668; CC P62826; O43592: XPOT; NbExp=3; IntAct=EBI-286642, EBI-286683; CC P62826; O95070: YIF1A; NbExp=3; IntAct=EBI-286642, EBI-2799703; CC P62826; O43829: ZBTB14; NbExp=3; IntAct=EBI-286642, EBI-10176632; CC P62826; Q8IWT0-2: ZBTB8OS; NbExp=3; IntAct=EBI-286642, EBI-12956041; CC P62826; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-286642, EBI-14104088; CC P62826; Q05CR2: ZNF248; NbExp=3; IntAct=EBI-286642, EBI-25835471; CC P62826; Q96LX8: ZNF597; NbExp=3; IntAct=EBI-286642, EBI-9091553; CC P62826; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-286642, EBI-18036029; CC P62826; Q5JTY5: ZNG1C; NbExp=3; IntAct=EBI-286642, EBI-723434; CC P62826; A0A384MDV8; NbExp=3; IntAct=EBI-286642, EBI-25834468; CC P62826; B7Z3E8; NbExp=3; IntAct=EBI-286642, EBI-25831617; CC P62826; Q86V28; NbExp=3; IntAct=EBI-286642, EBI-10259496; CC P62826; P49791: Nup153; Xeno; NbExp=5; IntAct=EBI-286642, EBI-6140533; CC P62826; Q6P5F9: Xpo1; Xeno; NbExp=3; IntAct=EBI-286642, EBI-2550236; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10679025, CC ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:18617507, CC ECO:0000269|PubMed:1961752, ECO:0000269|PubMed:19753112, CC ECO:0000269|PubMed:31075303, ECO:0000269|PubMed:8421051, CC ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9351834, CC ECO:0000269|PubMed:9822603}. Nucleus envelope CC {ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9822603}. Cytoplasm, CC cytosol {ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:8276887}. CC Cytoplasm {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:12194828, CC ECO:0000269|PubMed:9822603}. Melanosome {ECO:0000269|PubMed:17081065}. CC Note=Predominantly nuclear during interphase (PubMed:8421051, CC PubMed:12194828, PubMed:10679025). Becomes dispersed throughout the CC cytoplasm during mitosis (PubMed:8421051, PubMed:12194828). Identified CC by mass spectrometry in melanosome fractions from stage I to stage IV CC (PubMed:17081065). {ECO:0000269|PubMed:10679025, CC ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:17081065, CC ECO:0000269|PubMed:8421051}. CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues. CC {ECO:0000269|PubMed:2108320}. CC -!- PTM: Acetylation by KAT5 at Lys-134 is increased during mitosis, CC impairs RANGRF binding and enhances RCC1 binding (PubMed:29040603). CC Acetylation at Lys-37 enhances the association with nuclear export CC components (PubMed:31075303). Deacetylation of Lys-37 by SIRT7 CC regulates the nuclear export of NF-kappa-B subunit RELA/p65 CC (PubMed:31075303). {ECO:0000269|PubMed:29040603, CC ECO:0000269|PubMed:31075303}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB93486.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; M31469; AAA36546.1; -; mRNA. DR EMBL; AF052578; AAC05840.1; -; mRNA. DR EMBL; AF054183; AAC99400.1; -; mRNA. DR EMBL; AF501887; AAM15923.1; -; mRNA. DR EMBL; BT007271; AAP35935.1; -; mRNA. DR EMBL; CR450347; CAG29343.1; -; mRNA. DR EMBL; AK290763; BAF83452.1; -; mRNA. DR EMBL; AK312466; BAG35373.1; -; mRNA. DR EMBL; CH471054; EAW98516.1; -; Genomic_DNA. DR EMBL; BC004272; AAH04272.3; -; mRNA. DR EMBL; BC014518; AAH14518.1; -; mRNA. DR EMBL; BC014901; AAH14901.1; -; mRNA. DR EMBL; BC016654; AAH16654.1; -; mRNA. DR EMBL; BC051908; AAH51908.2; -; mRNA. DR EMBL; BC072000; AAH72000.1; -; mRNA. DR EMBL; AB062399; BAB93486.1; ALT_INIT; mRNA. DR CCDS; CCDS9271.1; -. DR PIR; A44393; TVHUC3. DR RefSeq; NP_001287725.1; NM_001300796.1. DR RefSeq; NP_001287726.1; NM_001300797.1. DR RefSeq; NP_006316.1; NM_006325.4. DR PDB; 1I2M; X-ray; 1.76 A; A/C=1-216. DR PDB; 1IBR; X-ray; 2.30 A; A/C=1-216. DR PDB; 1K5D; X-ray; 2.70 A; A/D/G/J=1-216. DR PDB; 1K5G; X-ray; 3.10 A; A/D/G/J=1-216. DR PDB; 1QBK; X-ray; 3.00 A; C=1-216. DR PDB; 1RRP; X-ray; 2.96 A; A/C=8-211. DR PDB; 2MMC; NMR; -; A=1-216. DR PDB; 2MMG; NMR; -; A=1-216. DR PDB; 2N1B; NMR; -; A=1-216. DR PDB; 3CH5; X-ray; 2.10 A; A=1-216. DR PDB; 3EA5; X-ray; 2.50 A; A/C=1-216. DR PDB; 3GJ0; X-ray; 1.48 A; A/B=2-216. DR PDB; 3GJ3; X-ray; 1.79 A; A=2-216. DR PDB; 3GJ4; X-ray; 2.15 A; A/C=2-216. DR PDB; 3GJ5; X-ray; 1.79 A; A/C=2-216. DR PDB; 3GJ6; X-ray; 2.70 A; A=2-216. DR PDB; 3GJ7; X-ray; 1.93 A; A/C=2-216. DR PDB; 3GJ8; X-ray; 1.82 A; A/C=2-216. DR PDB; 3GJX; X-ray; 2.50 A; C/F=1-216. DR PDB; 3NBY; X-ray; 3.42 A; C/F=5-180. DR PDB; 3NBZ; X-ray; 2.80 A; C/F=5-180. DR PDB; 3NC0; X-ray; 2.90 A; C/F=5-180. DR PDB; 3NC1; X-ray; 3.35 A; C=1-180. DR PDB; 3ZJY; X-ray; 3.60 A; A/D/F=1-180. DR PDB; 4C0Q; X-ray; 3.42 A; C/D=2-216. DR PDB; 4GMX; X-ray; 2.10 A; A=1-216. DR PDB; 4GPT; X-ray; 2.22 A; A=1-216. DR PDB; 4HAT; X-ray; 1.78 A; A=1-216. DR PDB; 4HAU; X-ray; 2.00 A; A=1-216. DR PDB; 4HAV; X-ray; 2.00 A; A=1-216. DR PDB; 4HAW; X-ray; 1.90 A; A=1-216. DR PDB; 4HAX; X-ray; 2.28 A; A=1-216. DR PDB; 4HAY; X-ray; 2.30 A; A=1-216. DR PDB; 4HAZ; X-ray; 1.90 A; A=1-216. DR PDB; 4HB0; X-ray; 2.20 A; A=1-216. DR PDB; 4HB2; X-ray; 1.80 A; A=1-216. DR PDB; 4HB3; X-ray; 2.80 A; A=1-216. DR PDB; 4HB4; X-ray; 2.05 A; A=1-216. DR PDB; 4OL0; X-ray; 2.90 A; A=1-216. DR PDB; 4WVF; X-ray; 1.80 A; A=1-216. DR PDB; 5CIQ; X-ray; 1.65 A; A/B=1-216. DR PDB; 5CIT; X-ray; 1.75 A; A/B=1-216. DR PDB; 5CIW; X-ray; 1.75 A; A/B=1-216. DR PDB; 5CJ2; X-ray; 1.75 A; A/B/C/D/E/F/G/H=1-216. DR PDB; 5CLL; X-ray; 2.45 A; A/C=1-191. DR PDB; 5CLQ; X-ray; 3.20 A; A/C=1-216. DR PDB; 5DH9; X-ray; 2.55 A; A=1-216. DR PDB; 5DHA; X-ray; 2.95 A; A=1-216. DR PDB; 5DHF; X-ray; 2.29 A; A=1-216. DR PDB; 5DI9; X-ray; 2.28 A; A=1-216. DR PDB; 5DIF; X-ray; 2.09 A; A=1-216. DR PDB; 5DIS; X-ray; 2.85 A; B=8-179. DR PDB; 5DLQ; X-ray; 3.20 A; C/D=5-180. DR PDB; 5FYQ; X-ray; 3.00 A; C/D=31-43. DR PDB; 5JLJ; X-ray; 2.50 A; A=1-216. DR PDB; 5UWH; X-ray; 2.26 A; A=1-216. DR PDB; 5UWI; X-ray; 2.14 A; A=1-216. DR PDB; 5UWJ; X-ray; 2.22 A; A=1-216. DR PDB; 5UWO; X-ray; 2.35 A; A=1-216. DR PDB; 5UWP; X-ray; 2.05 A; A=1-216. DR PDB; 5UWQ; X-ray; 2.28 A; A=1-216. DR PDB; 5UWR; X-ray; 2.24 A; A=1-216. DR PDB; 5UWS; X-ray; 2.40 A; A=1-216. DR PDB; 5UWT; X-ray; 2.34 A; A=1-216. DR PDB; 5UWU; X-ray; 2.24 A; A=1-216. DR PDB; 5UWW; X-ray; 2.15 A; A=1-216. DR PDB; 5YRO; X-ray; 2.40 A; A=1-216. DR PDB; 5YST; X-ray; 2.04 A; A=1-216. DR PDB; 5YSU; X-ray; 2.30 A; A=1-216. DR PDB; 5YTB; X-ray; 2.30 A; A=1-216. DR PDB; 5ZPU; X-ray; 2.60 A; A=1-216. DR PDB; 6A38; X-ray; 2.69 A; A=1-216. DR PDB; 6A3A; X-ray; 2.30 A; A=1-216. DR PDB; 6A3B; X-ray; 2.51 A; A=1-216. DR PDB; 6A3C; X-ray; 2.35 A; A=1-216. DR PDB; 6A3E; X-ray; 2.70 A; A=1-216. DR PDB; 6CIT; X-ray; 2.03 A; A=1-216. DR PDB; 6KFT; X-ray; 2.51 A; A=1-216. DR PDB; 6LQ9; X-ray; 2.50 A; A=1-216. DR PDB; 6M60; X-ray; 2.17 A; A=1-216. DR PDB; 6M6X; X-ray; 2.88 A; A=1-216. DR PDB; 6Q82; X-ray; 2.99 A; B=5-180. DR PDB; 6Q84; X-ray; 3.70 A; B/E=5-180. DR PDB; 6TVO; X-ray; 3.20 A; B=1-180. DR PDB; 6X2M; X-ray; 2.35 A; A=1-216. DR PDB; 6X2O; X-ray; 2.55 A; A=1-216. DR PDB; 6X2P; X-ray; 2.40 A; A=1-216. DR PDB; 6X2R; X-ray; 2.30 A; A=1-216. DR PDB; 6X2S; X-ray; 2.50 A; A=1-216. DR PDB; 6X2U; X-ray; 2.20 A; A=1-216. DR PDB; 6X2V; X-ray; 2.82 A; A=1-216. DR PDB; 6X2W; X-ray; 3.00 A; A=1-216. DR PDB; 6X2X; X-ray; 2.46 A; A=1-216. DR PDB; 6X2Y; X-ray; 2.30 A; A=1-216. DR PDB; 6XJP; X-ray; 2.80 A; A=1-216. DR PDB; 6XJR; X-ray; 1.94 A; A=1-216. DR PDB; 6XJS; X-ray; 1.94 A; A=1-216. DR PDB; 6XJT; X-ray; 2.41 A; A=1-216. DR PDB; 6XJU; X-ray; 2.19 A; A=1-216. DR PDB; 7B51; X-ray; 2.58 A; B=1-180. DR PDB; 7CND; X-ray; 1.80 A; A=1-216. DR PDB; 7DBG; X-ray; 2.06 A; A=1-216. DR PDB; 7L5E; X-ray; 1.94 A; A=1-216. DR PDB; 7MNP; X-ray; 2.05 A; A/C=1-216. DR PDB; 7MNQ; X-ray; 2.05 A; A=1-216. DR PDB; 7MNR; X-ray; 1.80 A; A=1-216. DR PDB; 7MNS; X-ray; 2.10 A; A=1-216. DR PDB; 7MNT; X-ray; 2.45 A; A/C=1-216. DR PDB; 7MNU; X-ray; 2.00 A; A=1-216. DR PDB; 7MNV; X-ray; 1.80 A; A=1-216. DR PDB; 7MNW; X-ray; 2.40 A; A/C/E/G=1-216. DR PDB; 7MNX; X-ray; 2.40 A; A/C/E/G/I/K=1-216. DR PDB; 7MNY; X-ray; 2.70 A; A/C/E/G/I/K=1-216. DR PDB; 7MNZ; X-ray; 2.35 A; A/C/E/G/I/K=1-215. DR PDB; 7MO0; X-ray; 2.45 A; A/C=1-216. DR PDB; 7MO1; X-ray; 1.60 A; A=1-216. DR PDB; 7MO2; X-ray; 1.65 A; A/C=1-216. DR PDB; 7MO3; X-ray; 2.05 A; A/C=1-216. DR PDB; 7MO4; X-ray; 2.40 A; A/C=1-216. DR PDB; 7MO5; X-ray; 1.55 A; A=1-216. DR PDB; 7YPZ; X-ray; 2.15 A; A=1-216. DR PDB; 8HQ3; X-ray; 2.10 A; A=1-216. DR PDB; 8HQ6; X-ray; 2.03 A; A=1-216. DR PDB; 8UX1; EM; 2.50 A; K=1-216. DR PDBsum; 1I2M; -. DR PDBsum; 1IBR; -. DR PDBsum; 1K5D; -. DR PDBsum; 1K5G; -. DR PDBsum; 1QBK; -. DR PDBsum; 1RRP; -. DR PDBsum; 2MMC; -. DR PDBsum; 2MMG; -. DR PDBsum; 2N1B; -. DR PDBsum; 3CH5; -. DR PDBsum; 3EA5; -. DR PDBsum; 3GJ0; -. DR PDBsum; 3GJ3; -. DR PDBsum; 3GJ4; -. DR PDBsum; 3GJ5; -. DR PDBsum; 3GJ6; -. DR PDBsum; 3GJ7; -. DR PDBsum; 3GJ8; -. DR PDBsum; 3GJX; -. DR PDBsum; 3NBY; -. DR PDBsum; 3NBZ; -. DR PDBsum; 3NC0; -. DR PDBsum; 3NC1; -. DR PDBsum; 3ZJY; -. DR PDBsum; 4C0Q; -. DR PDBsum; 4GMX; -. DR PDBsum; 4GPT; -. DR PDBsum; 4HAT; -. DR PDBsum; 4HAU; -. DR PDBsum; 4HAV; -. DR PDBsum; 4HAW; -. DR PDBsum; 4HAX; -. DR PDBsum; 4HAY; -. DR PDBsum; 4HAZ; -. DR PDBsum; 4HB0; -. DR PDBsum; 4HB2; -. DR PDBsum; 4HB3; -. DR PDBsum; 4HB4; -. DR PDBsum; 4OL0; -. DR PDBsum; 4WVF; -. DR PDBsum; 5CIQ; -. DR PDBsum; 5CIT; -. DR PDBsum; 5CIW; -. DR PDBsum; 5CJ2; -. DR PDBsum; 5CLL; -. DR PDBsum; 5CLQ; -. DR PDBsum; 5DH9; -. DR PDBsum; 5DHA; -. DR PDBsum; 5DHF; -. DR PDBsum; 5DI9; -. DR PDBsum; 5DIF; -. DR PDBsum; 5DIS; -. DR PDBsum; 5DLQ; -. DR PDBsum; 5FYQ; -. DR PDBsum; 5JLJ; -. DR PDBsum; 5UWH; -. DR PDBsum; 5UWI; -. DR PDBsum; 5UWJ; -. DR PDBsum; 5UWO; -. DR PDBsum; 5UWP; -. DR PDBsum; 5UWQ; -. DR PDBsum; 5UWR; -. DR PDBsum; 5UWS; -. DR PDBsum; 5UWT; -. DR PDBsum; 5UWU; -. DR PDBsum; 5UWW; -. DR PDBsum; 5YRO; -. DR PDBsum; 5YST; -. DR PDBsum; 5YSU; -. DR PDBsum; 5YTB; -. DR PDBsum; 5ZPU; -. DR PDBsum; 6A38; -. DR PDBsum; 6A3A; -. DR PDBsum; 6A3B; -. DR PDBsum; 6A3C; -. DR PDBsum; 6A3E; -. DR PDBsum; 6CIT; -. DR PDBsum; 6KFT; -. DR PDBsum; 6LQ9; -. DR PDBsum; 6M60; -. DR PDBsum; 6M6X; -. DR PDBsum; 6Q82; -. DR PDBsum; 6Q84; -. DR PDBsum; 6TVO; -. DR PDBsum; 6X2M; -. DR PDBsum; 6X2O; -. DR PDBsum; 6X2P; -. DR PDBsum; 6X2R; -. DR PDBsum; 6X2S; -. DR PDBsum; 6X2U; -. DR PDBsum; 6X2V; -. DR PDBsum; 6X2W; -. DR PDBsum; 6X2X; -. DR PDBsum; 6X2Y; -. DR PDBsum; 6XJP; -. DR PDBsum; 6XJR; -. DR PDBsum; 6XJS; -. DR PDBsum; 6XJT; -. DR PDBsum; 6XJU; -. DR PDBsum; 7B51; -. DR PDBsum; 7CND; -. DR PDBsum; 7DBG; -. DR PDBsum; 7L5E; -. DR PDBsum; 7MNP; -. DR PDBsum; 7MNQ; -. DR PDBsum; 7MNR; -. DR PDBsum; 7MNS; -. DR PDBsum; 7MNT; -. DR PDBsum; 7MNU; -. DR PDBsum; 7MNV; -. DR PDBsum; 7MNW; -. DR PDBsum; 7MNX; -. DR PDBsum; 7MNY; -. DR PDBsum; 7MNZ; -. DR PDBsum; 7MO0; -. DR PDBsum; 7MO1; -. DR PDBsum; 7MO2; -. DR PDBsum; 7MO3; -. DR PDBsum; 7MO4; -. DR PDBsum; 7MO5; -. DR PDBsum; 7YPZ; -. DR PDBsum; 8HQ3; -. DR PDBsum; 8HQ6; -. DR PDBsum; 8UX1; -. DR AlphaFoldDB; P62826; -. DR BMRB; P62826; -. DR EMDB; EMD-42685; -. DR EMDB; EMD-6231; -. DR SASBDB; P62826; -. DR SMR; P62826; -. DR BioGRID; 111837; 420. DR CORUM; P62826; -. DR DIP; DIP-5929N; -. DR IntAct; P62826; 273. DR MINT; P62826; -. DR STRING; 9606.ENSP00000446215; -. DR ChEMBL; CHEMBL1741190; -. DR DrugBank; DB04315; Guanosine-5'-Diphosphate. DR TCDB; 9.A.60.1.1; the small nuclear rna exporter (snrna-e) family. DR GlyGen; P62826; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62826; -. DR PhosphoSitePlus; P62826; -. DR SwissPalm; P62826; -. DR BioMuta; RAN; -. DR DMDM; 51338598; -. DR OGP; P62826; -. DR REPRODUCTION-2DPAGE; P62826; -. DR EPD; P62826; -. DR jPOST; P62826; -. DR MassIVE; P62826; -. DR MaxQB; P62826; -. DR PaxDb; 9606-ENSP00000446215; -. DR PeptideAtlas; P62826; -. DR ProteomicsDB; 57429; -. DR Pumba; P62826; -. DR TopDownProteomics; P62826; -. DR Antibodypedia; 19412; 658 antibodies from 42 providers. DR DNASU; 5901; -. DR Ensembl; ENST00000392369.6; ENSP00000376176.2; ENSG00000132341.12. DR Ensembl; ENST00000543796.6; ENSP00000446215.1; ENSG00000132341.12. DR GeneID; 5901; -. DR KEGG; hsa:5901; -. DR MANE-Select; ENST00000543796.6; ENSP00000446215.1; NM_006325.5; NP_006316.1. DR UCSC; uc001uir.4; human. DR AGR; HGNC:9846; -. DR CTD; 5901; -. DR DisGeNET; 5901; -. DR GeneCards; RAN; -. DR HGNC; HGNC:9846; RAN. DR HPA; ENSG00000132341; Low tissue specificity. DR MIM; 601179; gene. DR neXtProt; NX_P62826; -. DR OpenTargets; ENSG00000132341; -. DR PharmGKB; PA34205; -. DR VEuPathDB; HostDB:ENSG00000132341; -. DR eggNOG; KOG0096; Eukaryota. DR GeneTree; ENSGT00940000153786; -. DR InParanoid; P62826; -. DR OMA; GEIKFDC; -. DR OrthoDB; 5471873at2759; -. DR PhylomeDB; P62826; -. DR TreeFam; TF106302; -. DR PathwayCommons; P62826; -. DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA. DR Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF). DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery. DR Reactome; R-HSA-180746; Nuclear import of Rev protein. DR Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis. DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs. DR Reactome; R-HSA-6784531; tRNA processing in the nucleus. DR Reactome; R-HSA-9615933; Postmitotic nuclear pore complex (NPC) reformation. DR SignaLink; P62826; -. DR SIGNOR; P62826; -. DR BioGRID-ORCS; 5901; 855 hits in 1140 CRISPR screens. DR ChiTaRS; RAN; human. DR EvolutionaryTrace; P62826; -. DR GeneWiki; Ran_(biology); -. DR GenomeRNAi; 5901; -. DR Pharos; P62826; Tchem. DR PRO; PR:P62826; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P62826; Protein. DR Bgee; ENSG00000132341; Expressed in primordial germ cell in gonad and 208 other cell types or tissues. DR ExpressionAtlas; P62826; baseline and differential. DR GO; GO:0005814; C:centriole; IDA:UniProtKB. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl. DR GO; GO:0002177; C:manchette; IEA:Ensembl. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0005643; C:nuclear pore; NAS:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA. DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB. DR GO; GO:0042565; C:RNA nuclear export complex; IDA:BHF-UCL. DR GO; GO:0036126; C:sperm flagellum; IEA:Ensembl. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0003682; F:chromatin binding; TAS:UniProtKB. DR GO; GO:0045505; F:dynein intermediate chain binding; IEA:Ensembl. DR GO; GO:0003925; F:G protein activity; IDA:UniProt. DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0061676; F:importin-alpha family protein binding; IEA:Ensembl. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl. 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:0006259; P:DNA metabolic process; TAS:UniProtKB. DR GO; GO:0046039; P:GTP metabolic process; IDA:UniProtKB. DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl. DR GO; GO:0000278; P:mitotic cell cycle; TAS:UniProtKB. DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB. DR GO; GO:0007052; P:mitotic spindle organization; TAS:UniProtKB. DR GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:ParkinsonsUK-UCL. DR GO; GO:0035281; P:pre-miRNA export from nucleus; IC:BHF-UCL. DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB. DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB. DR GO; GO:1902570; P:protein localization to nucleolus; IMP:UniProtKB. DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:ParkinsonsUK-UCL. DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:ParkinsonsUK-UCL. DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central. DR GO; GO:0061015; P:snRNA import into nucleus; IMP:UniProtKB. DR GO; GO:0007286; P:spermatid development; IEA:Ensembl. DR GO; GO:0016032; P:viral process; TAS:Reactome. DR CDD; cd00877; Ran; 1. DR DisProt; DP01364; -. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR IDEAL; IID00162; -. 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 UCD-2DPAGE; P62826; -. DR Genevisible; P62826; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell cycle; Cell division; Cytoplasm; KW Direct protein sequencing; GTP-binding; Host-virus interaction; Hydrolase; KW Isopeptide bond; Magnesium; Metal-binding; Mitosis; Nucleotide-binding; KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Transport; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..216 FT /note="GTP-binding nuclear protein Ran" FT /id="PRO_0000208696" FT REGION 211..216 FT /note="Interaction with RANBP1" FT /evidence="ECO:0000269|PubMed:7891706" FT BINDING 18..25 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:10078529, FT ECO:0000269|PubMed:10353245, ECO:0000269|PubMed:10367892, FT ECO:0000269|PubMed:11832950, ECO:0000269|PubMed:18611384, FT ECO:0000269|PubMed:19389996, ECO:0000269|PubMed:19505478, FT ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24915079, FT ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26349033, FT ECO:0000269|PubMed:28282025, ECO:0000269|PubMed:7885480, FT ECO:0007744|PDB:1IBR, ECO:0007744|PDB:1K5G, FT ECO:0007744|PDB:1RRP, ECO:0007744|PDB:3CH5, FT ECO:0007744|PDB:3GJ0, ECO:0007744|PDB:3GJ3, FT ECO:0007744|PDB:3GJ4, ECO:0007744|PDB:3GJ5, FT ECO:0007744|PDB:3GJ6, ECO:0007744|PDB:3GJ7, FT ECO:0007744|PDB:3GJ8, ECO:0007744|PDB:3GJX, FT ECO:0007744|PDB:3NBY, ECO:0007744|PDB:3NBZ, FT ECO:0007744|PDB:3NC0, ECO:0007744|PDB:3NC1, FT ECO:0007744|PDB:3ZJY, ECO:0007744|PDB:4C0Q, FT ECO:0007744|PDB:4OL0, ECO:0007744|PDB:5CIQ, FT ECO:0007744|PDB:5CIT, ECO:0007744|PDB:5CIW, FT ECO:0007744|PDB:5CLQ, ECO:0007744|PDB:5DH9, FT ECO:0007744|PDB:5DHA, ECO:0007744|PDB:5DHF, FT ECO:0007744|PDB:5DI9, ECO:0007744|PDB:5DIF, FT ECO:0007744|PDB:5DIS, ECO:0007744|PDB:5DLQ, FT ECO:0007744|PDB:5UWH, ECO:0007744|PDB:5UWI, FT ECO:0007744|PDB:5UWJ, ECO:0007744|PDB:5UWO, FT ECO:0007744|PDB:5UWP, ECO:0007744|PDB:5UWQ, FT ECO:0007744|PDB:5UWR, ECO:0007744|PDB:5UWS, FT ECO:0007744|PDB:5UWT, ECO:0007744|PDB:5UWU, FT ECO:0007744|PDB:5UWW" FT BINDING 36..42 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:10078529, FT ECO:0000269|PubMed:10353245, ECO:0000269|PubMed:10367892, FT ECO:0000269|PubMed:11832950, ECO:0000269|PubMed:19389996, FT ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24915079, FT ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26349033, FT ECO:0000269|PubMed:28282025, ECO:0000269|PubMed:7885480, FT ECO:0007744|PDB:1IBR, ECO:0007744|PDB:1K5D, FT ECO:0007744|PDB:1QBK, ECO:0007744|PDB:1RRP, FT ECO:0007744|PDB:3GJX, ECO:0007744|PDB:3NBY, FT ECO:0007744|PDB:3NBZ, ECO:0007744|PDB:3NC0, FT ECO:0007744|PDB:3NC1, ECO:0007744|PDB:3ZJY, FT ECO:0007744|PDB:4C0Q, ECO:0007744|PDB:4OL0, FT ECO:0007744|PDB:5CLL, ECO:0007744|PDB:5CLQ, FT ECO:0007744|PDB:5DH9, ECO:0007744|PDB:5DHA, FT ECO:0007744|PDB:5DHF, ECO:0007744|PDB:5DI9, FT ECO:0007744|PDB:5DIF, ECO:0007744|PDB:5DIS, FT ECO:0007744|PDB:5DLQ, ECO:0007744|PDB:5JLJ, FT ECO:0007744|PDB:5UWH, ECO:0007744|PDB:5UWI, FT ECO:0007744|PDB:5UWJ, ECO:0007744|PDB:5UWO, FT ECO:0007744|PDB:5UWP, ECO:0007744|PDB:5UWQ, FT ECO:0007744|PDB:5UWR, ECO:0007744|PDB:5UWS, FT ECO:0007744|PDB:5UWT, ECO:0007744|PDB:5UWU, FT ECO:0007744|PDB:5UWW" FT BINDING 68 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:10078529, FT ECO:0000269|PubMed:10353245, ECO:0000269|PubMed:10367892, FT ECO:0000269|PubMed:11832950, ECO:0000269|PubMed:18611384, FT ECO:0000269|PubMed:19389996, ECO:0000269|PubMed:19505478, FT ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24915079, FT ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26349033, FT ECO:0000269|PubMed:28282025, ECO:0000269|PubMed:7885480, FT ECO:0007744|PDB:1IBR, ECO:0007744|PDB:1K5D, FT ECO:0007744|PDB:1QBK, ECO:0007744|PDB:1RRP, FT ECO:0007744|PDB:3GJX, ECO:0007744|PDB:3NBY, FT ECO:0007744|PDB:3NBZ, ECO:0007744|PDB:3NC0, FT ECO:0007744|PDB:3NC1, ECO:0007744|PDB:3ZJY, FT ECO:0007744|PDB:4C0Q, ECO:0007744|PDB:4OL0, FT ECO:0007744|PDB:5DH9, ECO:0007744|PDB:5DHA, FT ECO:0007744|PDB:5DHF, ECO:0007744|PDB:5DI9, FT ECO:0007744|PDB:5DIF, ECO:0007744|PDB:5DIS, FT ECO:0007744|PDB:5DLQ, ECO:0007744|PDB:5JLJ, FT ECO:0007744|PDB:5UWH, ECO:0007744|PDB:5UWI, FT ECO:0007744|PDB:5UWJ, ECO:0007744|PDB:5UWO, FT ECO:0007744|PDB:5UWP, ECO:0007744|PDB:5UWQ, FT ECO:0007744|PDB:5UWR, ECO:0007744|PDB:5UWS, FT ECO:0007744|PDB:5UWT, ECO:0007744|PDB:5UWU, FT ECO:0007744|PDB:5UWW" FT BINDING 122..125 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:10078529, FT ECO:0000269|PubMed:10353245, ECO:0000269|PubMed:10367892, FT ECO:0000269|PubMed:11832950, ECO:0000269|PubMed:18611384, FT ECO:0000269|PubMed:19389996, ECO:0000269|PubMed:19505478, FT ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24915079, FT ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26349033, FT ECO:0000269|PubMed:28282025, ECO:0000269|PubMed:7885480, FT ECO:0007744|PDB:1IBR, ECO:0007744|PDB:1K5D, FT ECO:0007744|PDB:1QBK, ECO:0007744|PDB:1RRP, FT ECO:0007744|PDB:3CH5, ECO:0007744|PDB:3GJ0, FT ECO:0007744|PDB:3GJ3, ECO:0007744|PDB:3GJ4, FT ECO:0007744|PDB:3GJ5, ECO:0007744|PDB:3GJ6, FT ECO:0007744|PDB:3GJ7, ECO:0007744|PDB:3GJ8, FT ECO:0007744|PDB:3GJX, ECO:0007744|PDB:3NBY, FT ECO:0007744|PDB:3NBZ, ECO:0007744|PDB:3NC0, FT ECO:0007744|PDB:3NC1, ECO:0007744|PDB:3ZJY, FT ECO:0007744|PDB:4C0Q, ECO:0007744|PDB:4OL0, FT ECO:0007744|PDB:5CIQ, ECO:0007744|PDB:5CIT, FT ECO:0007744|PDB:5CIW, ECO:0007744|PDB:5CJ2, FT ECO:0007744|PDB:5CLL, ECO:0007744|PDB:5DH9, FT ECO:0007744|PDB:5DHA, ECO:0007744|PDB:5DHF, FT ECO:0007744|PDB:5DI9, ECO:0007744|PDB:5DIF, FT ECO:0007744|PDB:5DIS, ECO:0007744|PDB:5DLQ, FT ECO:0007744|PDB:5JLJ, ECO:0007744|PDB:5UWH, FT ECO:0007744|PDB:5UWI, ECO:0007744|PDB:5UWJ, FT ECO:0007744|PDB:5UWO, ECO:0007744|PDB:5UWP, FT ECO:0007744|PDB:5UWQ, ECO:0007744|PDB:5UWR, FT ECO:0007744|PDB:5UWS, ECO:0007744|PDB:5UWT, FT ECO:0007744|PDB:5UWU, ECO:0007744|PDB:5UWW" FT BINDING 150..152 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:10078529, FT ECO:0000269|PubMed:10353245, ECO:0000269|PubMed:10367892, FT ECO:0000269|PubMed:11832950, ECO:0000269|PubMed:18611384, FT ECO:0000269|PubMed:19389996, ECO:0000269|PubMed:19505478, FT ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24915079, FT ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26349033, FT ECO:0000269|PubMed:28282025, ECO:0000269|PubMed:7885480, FT ECO:0007744|PDB:1K5G, ECO:0007744|PDB:3CH5, FT ECO:0007744|PDB:3GJ0, ECO:0007744|PDB:3GJ3, FT ECO:0007744|PDB:3GJ4, ECO:0007744|PDB:3GJ5, FT ECO:0007744|PDB:3GJ6, ECO:0007744|PDB:3GJ7, FT ECO:0007744|PDB:3GJ8, ECO:0007744|PDB:3GJX, FT ECO:0007744|PDB:3NBY, ECO:0007744|PDB:3NBZ, FT ECO:0007744|PDB:3NC0, ECO:0007744|PDB:3NC1, FT ECO:0007744|PDB:3ZJY, ECO:0007744|PDB:4C0Q, FT ECO:0007744|PDB:4OL0, ECO:0007744|PDB:5CIQ, FT ECO:0007744|PDB:5CIT, ECO:0007744|PDB:5CIW, FT ECO:0007744|PDB:5CJ2, ECO:0007744|PDB:5CLL, FT ECO:0007744|PDB:5CLQ, ECO:0007744|PDB:5DH9, FT ECO:0007744|PDB:5DHA, ECO:0007744|PDB:5DHF, FT ECO:0007744|PDB:5DI9, ECO:0007744|PDB:5DIF, FT ECO:0007744|PDB:5DIS, ECO:0007744|PDB:5DLQ, FT ECO:0007744|PDB:5JLJ, ECO:0007744|PDB:5UWH, FT ECO:0007744|PDB:5UWI, ECO:0007744|PDB:5UWJ, FT ECO:0007744|PDB:5UWO, ECO:0007744|PDB:5UWP, FT ECO:0007744|PDB:5UWQ, ECO:0007744|PDB:5UWR, FT ECO:0007744|PDB:5UWS, ECO:0007744|PDB:5UWT, FT ECO:0007744|PDB:5UWU, ECO:0007744|PDB:5UWW" FT SITE 69 FT /note="Essential for GTP hydrolysis" FT /evidence="ECO:0000269|PubMed:18591255, FT ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:8636225" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 24 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 37 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:31075303" FT MOD_RES 60 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 71 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 99 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 134 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:29040603" FT MOD_RES 159 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 159 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62827" FT CROSSLNK 71 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 71 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT CROSSLNK 152 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT MUTAGEN 19 FT /note="G->V: Blocks DNA replication; when associated with FT L-69." FT /evidence="ECO:0000269|PubMed:8421051" FT MUTAGEN 24 FT /note="T->L: Has low binding affinity for GTP and GDP. FT Almost completely abolishes interaction with BIRC5." FT /evidence="ECO:0000269|PubMed:18591255" FT MUTAGEN 24 FT /note="T->N: Has low binding affinity for GTP and GDP. FT Decreases nuclear import of proteins and RNA. Stabilizes FT the interaction with RCC1. No effect on nuclear location FT during interphase. Loss of activity in triggering FT microtubule assembly at mitotic chromosomes." FT /evidence="ECO:0000269|PubMed:10408446, FT ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:7819259, FT ECO:0000269|PubMed:8636225, ECO:0000269|PubMed:9351834" FT MUTAGEN 25 FT /note="T->A: Minor effect on the interaction with the alpha FT phosphate group of bound GTP." FT /evidence="ECO:0000269|PubMed:26272610" FT MUTAGEN 37 FT /note="K->Q: Mimics acetylation; enhances the nuclear FT export of RELA/p65." FT /evidence="ECO:0000269|PubMed:31075303" FT MUTAGEN 37 FT /note="K->R: Decreased acetylation." FT /evidence="ECO:0000269|PubMed:31075303" FT MUTAGEN 39 FT /note="Y->A: Abolishes steric hindrance that traps the FT essential Q-69 in an unreactive position, and causes slow FT GTP hydrolysis in wild-type. Loss of one hydrogen bond with FT the gamma phosphate group of bound GTP." FT /evidence="ECO:0000269|PubMed:26272610" FT MUTAGEN 69 FT /note="Q->L: Strongly decreased GTPase activity. Probably FT locked in the GTP-bound form. Loss of interaction with FT NUTF2. Decreases nuclear location and leads to cytoplasmic FT location during interphase. Loss of function in FT importin-mediated protein nuclear import. High activity in FT triggering microtubule assembly at mitotic chromosomes. FT Blocks DNA replication; when associated with V-19." FT /evidence="ECO:0000269|PubMed:10408446, FT ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:17209048, FT ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:7819259, FT ECO:0000269|PubMed:8421051, ECO:0000269|PubMed:8636225, FT ECO:0000269|PubMed:9351834, ECO:0000269|PubMed:9822603" FT MUTAGEN 69 FT /note="Q->N: Unable to hydrolyze GTP. Increases binding to FT BIRC5 and promotes exaggerated spindle formation." FT /evidence="ECO:0000269|PubMed:18591255, FT ECO:0000269|PubMed:23878195, ECO:0000269|PubMed:24915079" FT MUTAGEN 70 FT /note="E->A: Strongly decreases the relase of bound GDP." FT /evidence="ECO:0000269|PubMed:11336674" FT MUTAGEN 76 FT /note="R->E: Probable loss of interaction with NUTF2. Loss FT of transport to the nucleus." FT /evidence="ECO:0000269|PubMed:9822603" FT MUTAGEN 134 FT /note="K->Q: Loss of normal mitotic chromosome segregation FT and defective mitotic spindle orientation." FT /evidence="ECO:0000269|PubMed:29040603" FT MUTAGEN 134 FT /note="K->R: Loss of normal mitotic chromosome segregation FT and formation of sister chromatid bridges." FT /evidence="ECO:0000269|PubMed:29040603" FT MUTAGEN 211..216 FT /note="Missing: No effect on GTPase activity. Abolishes FT interaction with RANBP1." FT /evidence="ECO:0000269|PubMed:7891706" FT CONFLICT 2 FT /note="A -> T (in Ref. 11; AAH72000)" FT /evidence="ECO:0000305" FT CONFLICT 181 FT /note="A -> C (in Ref. 5; AAC99400)" FT /evidence="ECO:0000305" FT TURN 2..5 FT /evidence="ECO:0007829|PDB:2MMG" FT STRAND 10..17 FT /evidence="ECO:0007829|PDB:3GJ0" FT STRAND 18..22 FT /evidence="ECO:0007829|PDB:1QBK" FT HELIX 23..27 FT /evidence="ECO:0007829|PDB:3GJ0" FT HELIX 31..35 FT /evidence="ECO:0007829|PDB:3GJ0" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:3GJ0" FT TURN 41..44 FT /evidence="ECO:0007829|PDB:3GJ0" FT STRAND 45..54 FT /evidence="ECO:0007829|PDB:3GJ0" FT STRAND 57..66 FT /evidence="ECO:0007829|PDB:3GJ0" FT HELIX 69..71 FT /evidence="ECO:0007829|PDB:3GJ0" FT HELIX 74..76 FT /evidence="ECO:0007829|PDB:1K5D" FT HELIX 77..80 FT /evidence="ECO:0007829|PDB:3GJ0" FT STRAND 85..91 FT /evidence="ECO:0007829|PDB:3GJ0" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:1RRP" FT HELIX 95..99 FT /evidence="ECO:0007829|PDB:3GJ0" FT HELIX 101..111 FT /evidence="ECO:0007829|PDB:3GJ0" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:5CJ2" FT STRAND 117..122 FT /evidence="ECO:0007829|PDB:3GJ0" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:3GJ0" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:3GJ0" FT HELIX 138..142 FT /evidence="ECO:0007829|PDB:3GJ0" FT STRAND 145..148 FT /evidence="ECO:0007829|PDB:3GJ0" FT TURN 151..154 FT /evidence="ECO:0007829|PDB:3GJ0" FT TURN 156..158 FT /evidence="ECO:0007829|PDB:3GJ0" FT HELIX 159..169 FT /evidence="ECO:0007829|PDB:3GJ0" FT STRAND 176..178 FT /evidence="ECO:0007829|PDB:3GJ0" FT TURN 185..187 FT /evidence="ECO:0007829|PDB:1QBK" FT HELIX 191..205 FT /evidence="ECO:0007829|PDB:3GJ0" FT HELIX 210..212 FT /evidence="ECO:0007829|PDB:7MNX" 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 //