RAN_HUMAN
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 03-AUG-2022, entry version 209.
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; Q6LES2: ANXA4; NbExp=3; IntAct=EBI-286642, EBI-10250835;
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; Q5JTY5: CBWD3; NbExp=3; IntAct=EBI-286642, EBI-723434;
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; 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; Q3SX64: ODF3L2; NbExp=3; IntAct=EBI-286642, EBI-6660184;
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; 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};
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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 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 AlphaFoldDB; P62826; -.
DR BMRB; P62826; -.
DR SASBDB; P62826; -.
DR SMR; P62826; -.
DR BioGRID; 111837; 260.
DR CORUM; P62826; -.
DR DIP; DIP-5929N; -.
DR IntAct; P62826; 272.
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).
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 UCD-2DPAGE; P62826; -.
DR EPD; P62826; -.
DR jPOST; P62826; -.
DR MassIVE; P62826; -.
DR MaxQB; P62826; -.
DR PaxDb; P62826; -.
DR PeptideAtlas; P62826; -.
DR PRIDE; P62826; -.
DR ProteomicsDB; 57429; -.
DR TopDownProteomics; P62826; -.
DR Antibodypedia; 19412; 612 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 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; TIVFHRK; -.
DR OrthoDB; 1083175at2759; -.
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; 820 hits in 1060 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 ventricular zone and 206 other tissues.
DR ExpressionAtlas; P62826; baseline and differential.
DR Genevisible; P62826; HS.
DR GO; GO:0005814; C:centriole; 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: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:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; TAS:UniProtKB.
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:0000287; F:magnesium ion binding; IDA:UniProtKB.
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:0006259; P:DNA metabolic process; TAS:UniProtKB.
DR GO; GO:0046039; P:GTP metabolic process; IDA:UniProtKB.
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:0016032; P:viral process; TAS:Reactome.
DR DisProt; DP01364; -.
DR Gene3D; 3.40.50.300; -; 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 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 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 importin-
FT 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 211..215
FT /evidence="ECO:0007829|PDB:2MMC"
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
