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GTP-binding nuclear protein Ran (Androgen receptor-associated protein 24) (GTPase Ran) (Ras-like protein TC4) (Ras-related nuclear protein)

 RAN_HUMAN               Reviewed;         216 AA.
P62826; A8K3Z8; P17080; P28746; P28747; Q6IPB2; Q86V08; Q8NI90;
Q9CSP3; Q9CWI7; Q9CZA2; Q9UDJ5; Q9UEU9;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
10-OCT-2018, entry version 183.
RecName: Full=GTP-binding nuclear protein Ran;
AltName: Full=Androgen receptor-associated protein 24 {ECO:0000303|PubMed:10400640};
AltName: Full=GTPase Ran;
AltName: Full=Ras-like protein TC4 {ECO:0000303|PubMed:2108320, ECO:0000303|PubMed:8276887, ECO:0000303|PubMed:8421051};
AltName: Full=Ras-related nuclear protein;
Name=RAN; Synonyms=ARA24 {ECO:0000303|PubMed:10400640};
ORFNames=OK/SW-cl.81;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Teratocarcinoma;
PubMed=2108320; DOI=10.1128/MCB.10.4.1793;
Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P.;
"Characterization of four novel ras-like genes expressed in a human
teratocarcinoma cell line.";
Mol. Cell. Biol. 10:1793-1798(1990).
[2]
SEQUENCE REVISION TO C-TERMINUS.
PubMed=1855255; DOI=10.1016/0092-8674(91)90624-8;
Matsumoto T., Beach D.H.;
"Premature initiation of mitosis in yeast lacking RCC1 or an
interacting GTPase.";
Cell 66:347-360(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF
GLY-19 AND GLN-69.
TISSUE=Brain;
PubMed=8421051; DOI=10.1083/jcb.120.2.313;
Ren M., Drivas G.T., D'Eustachio P., Rush M.G.;
"Ran/TC4: a small nuclear GTP-binding protein that regulates DNA
synthesis.";
J. Cell Biol. 120:313-323(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH AR, AND FUNCTION.
TISSUE=Brain;
PubMed=10400640; DOI=10.1074/jbc.274.29.20229;
Hsiao P.-W., Lin D.-L., Nakao R., Chang C.;
"The linkage of Kennedy's neuron disease to ARA24, the first
identified androgen receptor polyglutamine region-associated
coactivator.";
J. Biol. Chem. 274:20229-20234(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph, Ovary, Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PROTEIN SEQUENCE OF 2-23 AND 143-166, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V., Claeys D.;
Submitted (FEB-2006) to UniProtKB.
[13]
PROTEIN SEQUENCE OF 39-56 AND 153-166, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-216.
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[15]
PROTEIN SEQUENCE OF 65-76; 90-125; 128-147 AND 154-216, INTERACTION
WITH RCC1, AND SUBCELLULAR LOCATION.
TISSUE=Cervix carcinoma;
PubMed=1961752; DOI=10.1073/pnas.88.23.10830;
Bischoff F.R., Ponstingl H.;
"Mitotic regulator protein RCC1 is complexed with a nuclear ras-
related polypeptide.";
Proc. Natl. Acad. Sci. U.S.A. 88:10830-10834(1991).
[16]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8276887;
Melchior F., Paschal B., Evans J., Gerace L.;
"Inhibition of nuclear protein import by nonhydrolyzable analogues of
GTP and identification of the small GTPase Ran/TC4 as an essential
transport factor.";
J. Cell Biol. 123:1649-1659(1993).
[17]
FUNCTION, INTERACTION WITH RCC1, AND MUTAGENESIS OF THR-24 AND GLN-69.
PubMed=7819259;
Klebe C., Bischoff F.R., Ponstingl H., Wittinghofer A.;
"Interaction of the nuclear GTP-binding protein Ran with its
regulatory proteins RCC1 and RanGAP1.";
Biochemistry 34:639-647(1995).
[18]
INTERACTION WITH RANBP1, AND MUTAGENESIS OF 211-ASP--LEU-216.
PubMed=7891706; DOI=10.1128/MCB.15.4.2117;
Ren M., Villamarin A., Shih A., Coutavas E., Moore M.S., Locurcio M.,
Clarke V., Oppenheim J.D., D'Eustachio P., Rush M.G.;
"Separate domains of the Ran GTPase interact with different factors to
regulate nuclear protein import and RNA processing.";
Mol. Cell. Biol. 15:2117-2124(1995).
[19]
FUNCTION, INTERACTION WITH RANBP1 AND KPNB1, AND SUBCELLULAR LOCATION.
PubMed=8896452;
Goerlich D., Pante N., Kutay U., Aebi U., Bischoff F.R.;
"Identification of different roles for RanGDP and RanGTP in nuclear
protein import.";
EMBO J. 15:5584-5594(1996).
[20]
FUNCTION, AND MUTAGENESIS OF THR-24 AND GLN-69.
PubMed=8636225;
Palacios I., Weis K., Klebe C., Mattaj I.W., Dingwall C.;
"RAN/TC4 mutants identify a common requirement for snRNP and protein
import into the nucleus.";
J. Cell Biol. 133:485-494(1996).
[21]
FUNCTION.
PubMed=8692944; DOI=10.1073/pnas.93.14.7059;
Moroianu J., Blobel G., Radu A.;
"Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta
heterodimer by displacing alpha from an overlapping binding site on
beta.";
Proc. Natl. Acad. Sci. U.S.A. 93:7059-7062(1996).
[22]
IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH XPO1.
PubMed=9323133; DOI=10.1016/S0092-8674(00)80371-2;
Fornerod M., Ohno M., Yoshida M., Mattaj I.W.;
"CRM1 is an export receptor for leucine-rich nuclear export signals.";
Cell 90:1051-1060(1997).
[23]
FUNCTION, INTERACTION WITH TNPO1, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF THR-24 AND GLN-69.
PubMed=9351834; DOI=10.1093/emboj/16.21.6535;
Izaurralde E., Kutay U., von Kobbe C., Mattaj I.W., Goerlich D.;
"The asymmetric distribution of the constituents of the Ran system is
essential for transport into and out of the nucleus.";
EMBO J. 16:6535-6547(1997).
[24]
FUNCTION, INTERACTION WITH RANBP1 AND KPNB1, AND SUBUNIT.
PubMed=9428644;
Bischoff F.R., Goerlich D.;
"RanBP1 is crucial for the release of RanGTP from importin beta-
related nuclear transport factors.";
FEBS Lett. 419:249-254(1997).
[25]
FUNCTION, INTERACTION WITH NUTF2, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF GLN-69 AND ARG-76.
PubMed=9822603; DOI=10.1093/emboj/17.22.6587;
Ribbeck K., Lipowsky G., Kent H.M., Stewart M., Goerlich D.;
"NTF2 mediates nuclear import of Ran.";
EMBO J. 17:6587-6598(1998).
[26]
IDENTIFICATION IN A COMPLEX WITH HIV-1 REV; HIV-1 REV RESPONSE ELEMENT
AND XPO1 (MICROBIAL INFECTION).
PubMed=9837918; DOI=10.1074/jbc.273.50.33414;
Askjaer P., Jensen T.H., Nilsson J., Englmeier L., Kjems J.;
"The specificity of the CRM1-Rev nuclear export signal interaction is
mediated by RanGTP.";
J. Biol. Chem. 273:33414-33422(1998).
[27]
IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX, AND
IDENTIFICATION IN A TRIMERIC EXPORT COMPLEX WITH SNUPN AND XPO1.
PubMed=10209022; DOI=10.1083/jcb.145.2.255;
Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U.,
Hartmann E., Luehrmann R., Goerlich D.;
"CRM1-mediated recycling of snurportin 1 to the cytoplasm.";
J. Cell Biol. 145:255-264(1999).
[28]
FUNCTION, AND MUTAGENESIS OF THR-24 AND GLN-69.
PubMed=10408446; DOI=10.1038/22133;
Carazo-Salas R.E., Guarguaglini G., Gruss O.J., Segref A.,
Karsenti E., Mattaj I.W.;
"Generation of GTP-bound Ran by RCC1 is required for chromatin-induced
mitotic spindle formation.";
Nature 400:178-181(1999).
[29]
INTERACTION WITH NUTF2, AND SUBCELLULAR LOCATION.
PubMed=10679025; DOI=10.1091/mbc.11.2.703;
Steggerda S.M., Black B.E., Paschal B.M.;
"Monoclonal antibodies to NTF2 inhibit nuclear protein import by
preventing nuclear translocation of the GTPase Ran.";
Mol. Biol. Cell 11:703-719(2000).
[30]
IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RANBP3 AND XPO1.
PubMed=11571268; DOI=10.1093/embo-reports/kve200;
Englmeier L., Fornerod M., Bischoff F.R., Petosa C., Mattaj I.W.,
Kutay U.;
"RanBP3 influences interactions between CRM1 and its nuclear protein
export substrates.";
EMBO Rep. 2:926-932(2001).
[31]
IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RANBP3 AND XPO1.
PubMed=11425870; DOI=10.1083/jcb.153.7.1391;
Lindsay M.E., Holaska J.M., Welch K., Paschal B.M., Macara I.G.;
"Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein
export.";
J. Cell Biol. 153:1391-1402(2001).
[32]
IDENTIFICATION IN A COMPLEX WITH COPS5; RANBP9 AND DYRK1B.
PubMed=14500717; DOI=10.1074/jbc.M307556200;
Zou Y., Lim S., Lee K., Deng X., Friedman E.;
"Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial
cell migration and is negatively regulated by the Met adaptor Ran-
binding protein M.";
J. Biol. Chem. 278:49573-49581(2003).
[33]
INTERACTION WITH RCC1, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF THR-24 AND GLN-69.
PubMed=12194828;
Moore W., Zhang C., Clarke P.R.;
"Targeting of RCC1 to chromosomes is required for proper mitotic
spindle assembly in human cells.";
Curr. Biol. 12:1442-1447(2002).
[34]
INTERACTION WITH TERT.
PubMed=12808100; DOI=10.1128/MCB.23.13.4598-4610.2003;
Haendeler J., Hoffmann J., Brandes R.P., Zeiher A.M., Dimmeler S.;
"Hydrogen peroxide triggers nuclear export of telomerase reverse
transcriptase via Src kinase family-dependent phosphorylation of
tyrosine 707.";
Mol. Cell. Biol. 23:4598-4610(2003).
[35]
IDENTIFICATION IN A COMPLEX WITH HTLV-1 REX; RANBP3 AND XPO1
(MICROBIAL INFECTION).
PubMed=14612415; DOI=10.1128/MCB.23.23.8751-8761.2003;
Hakata Y., Yamada M., Shida H.;
"A multifunctional domain in human CRM1 (exportin 1) mediates RanBP3
binding and multimerization of human T-cell leukemia virus type 1 Rex
protein.";
Mol. Cell. Biol. 23:8751-8761(2003).
[36]
INTERACTION WITH RANBP9 AND RANBP10.
PubMed=14684163; DOI=10.1016/j.bbrc.2003.11.124;
Wang D., Li Z., Schoen S.R., Messing E.M., Wu G.;
"A novel MET-interacting protein shares high sequence similarity with
RanBPM, but fails to stimulate MET-induced Ras/Erk signaling.";
Biochem. Biophys. Res. Commun. 313:320-326(2004).
[37]
IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH XPO1.
PubMed=15574331; DOI=10.1016/j.molcel.2004.11.018;
Petosa C., Schoehn G., Askjaer P., Bauer U., Moulin M., Steuerwald U.,
Soler-Lopez M., Baudin F., Mattaj I.W., Mueller C.W.;
"Architecture of CRM1/Exportin1 suggests how cooperativity is achieved
during formation of a nuclear export complex.";
Mol. Cell 16:761-775(2004).
[38]
IDENTIFICATION IN A COMPLEX WITH RANBP1 AND RANGAP1.
PubMed=16428860;
Takeda E., Hieda M., Katahira J., Yoneda Y.;
"Phosphorylation of RanGAP1 stabilizes its interaction with Ran and
RanBP1.";
Cell Struct. Funct. 30:69-80(2005).
[39]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[40]
FUNCTION, INTERACTION WITH BIRC5, AND MUTAGENESIS OF THR-24 AND
GLN-69.
PubMed=18591255; DOI=10.1128/MCB.02039-07;
Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.;
"A survivin-ran complex regulates spindle formation in tumor cells.";
Mol. Cell. Biol. 28:5299-5311(2008).
[41]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VRK1; VRK2 AND
VRK3.
PubMed=18617507; DOI=10.1074/mcp.M700586-MCP200;
Sanz-Garcia M., Lopez-Sanchez I., Lazo P.A.;
"Proteomics identification of nuclear Ran GTPase as an inhibitor of
human VRK1 and VRK2 (vaccinia-related kinase) activities.";
Mol. Cell. Proteomics 7:2199-2214(2008).
[42]
INTERACTION WITH CAPG AND NUTF2.
PubMed=18266911; DOI=10.1111/j.1600-0854.2008.00720.x;
Van Impe K., Hubert T., De Corte V., Vanloo B., Boucherie C.,
Vandekerckhove J., Gettemans J.;
"A new role for nuclear transport factor 2 and Ran: nuclear import of
CapG.";
Traffic 9:695-707(2008).
[43]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[44]
INTERACTION WITH MAD2L2, AND SUBCELLULAR LOCATION.
PubMed=19753112; DOI=10.1371/journal.pone.0007020;
Medendorp K., van Groningen J.J., Vreede L., Hetterschijt L.,
van den Hurk W.H., de Bruijn D.R., Brugmans L., van Kessel A.G.;
"The mitotic arrest deficient protein MAD2B interacts with the small
GTPase RAN throughout the cell cycle.";
PLoS ONE 4:E7020-E7020(2009).
[45]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-71; LYS-99 AND
LYS-159, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[46]
FUNCTION, AND SUBUNIT.
PubMed=20485264; DOI=10.1038/emboj.2010.89;
Koyama M., Matsuura Y.;
"An allosteric mechanism to displace nuclear export cargo from CRM1
and RanGTP by RanBP1.";
EMBO J. 29:2002-2013(2010).
[47]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[48]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[49]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[52]
INTERACTION WITH MYCBP2.
PubMed=26304119; DOI=10.1074/jbc.M115.646901;
Doerr A., Pierre S., Zhang D.D., Henke M., Holland S., Scholich K.;
"MYCBP2 is a guanosine exchange factor for Ran protein and determines
its localization in neurons of dorsal root ganglia.";
J. Biol. Chem. 290:25620-25635(2015).
[53]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[54]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-71 AND LYS-152, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[55]
FUNCTION, INTERACTION WITH RANGRF AND RCC1, ACETYLATION AT LYS-134,
IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-134.
PubMed=29040603; DOI=10.1093/jmcb/mjx045;
Bao X., Liu H., Liu X., Ruan K., Zhang Y., Zhang Z., Hu Q., Liu Y.,
Akram S., Zhang J., Gong Q., Wang W., Yuan X., Li J., Zhao L., Dou Z.,
Tian R., Yao X., Wu J., Shi Y.;
"Mitosis-specific acetylation tunes Ran effector binding for
chromosome segregation.";
J. Mol. Cell Biol. 10:18-32(2018).
[56]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GDP.
PubMed=7885480; DOI=10.1038/374378a0;
Scheffzek K., Klebe C., Fritz-Wolf K., Kabsch W., Wittinghofer A.;
"Crystal structure of the nuclear Ras-related protein Ran in its GDP-
bound form.";
Nature 374:378-381(1995).
[57] {ECO:0000244|PDB:1IBR}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH GTP ANALOG AND
KPNB1.
PubMed=10367892; DOI=10.1016/S0092-8674(00)80774-6;
Vetter I.R., Arndt A., Kutay U., Goerlich D., Wittinghofer A.;
"Structural view of the Ran-Importin beta interaction at 2.3 A
resolution.";
Cell 97:635-646(1999).
[58] {ECO:0000244|PDB:1QBK}
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH GTP ANALOG AND
KPNB2.
PubMed=10353245; DOI=10.1038/20375;
Chook Y.M., Blobel G.;
"Structure of the nuclear transport complex karyopherin-beta2-Ran x
GppNHp.";
Nature 399:230-237(1999).
[59]
X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) IN COMPLEX WITH GTP ANALOG AND
RANBP2.
PubMed=10078529; DOI=10.1038/17969;
Vetter I.R., Nowak C., Nishimoto T., Kuhlmann J., Wittinghofer A.;
"Structure of a Ran-binding domain complexed with Ran bound to a GTP
analogue: implications for nuclear transport.";
Nature 398:39-46(1999).
[60] {ECO:0000244|PDB:1I2M}
X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH RCC1, FUNCTION,
INTERACTION WITH RCC1, AND MUTAGENESIS OF GLU-70.
PubMed=11336674; DOI=10.1016/S0092-8674(01)00315-4;
Renault L., Kuhlmann J., Henkel A., Wittinghofer A.;
"Structural basis for guanine nucleotide exchange on Ran by the
regulator of chromosome condensation (RCC1).";
Cell 105:245-255(2001).
[61] {ECO:0000244|PDB:1K5D, ECO:0000244|PDB:1K5G}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEXES WITH GTP ANALOGS;
RANBP1 AND FISSION YEAST RANGAP1.
PubMed=11832950; DOI=10.1038/415662a;
Seewald M.J., Korner C., Wittinghofer A., Vetter I.R.;
"RanGAP mediates GTP hydrolysis without an arginine finger.";
Nature 415:662-666(2002).
[62] {ECO:0000244|PDB:3CH5}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH GDP ANALOG AND
NUP153.
PubMed=18611384; DOI=10.1016/j.str.2008.03.014;
Schrader N., Koerner C., Koessmeier K., Bangert J.A., Wittinghofer A.,
Stoll R., Vetter I.R.;
"The crystal structure of the Ran-Nup153ZnF2 complex: a general Ran
docking site at the nuclear pore complex.";
Structure 16:1116-1125(2008).
[63] {ECO:0000244|PDB:3GJ0, ECO:0000244|PDB:3GJ3, ECO:0000244|PDB:3GJ4, ECO:0000244|PDB:3GJ5, ECO:0000244|PDB:3GJ6, ECO:0000244|PDB:3GJ7, ECO:0000244|PDB:3GJ8}
X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 2-216 IN COMPLEX WITH GDP
ANALOG AND NUP153.
PubMed=19505478; DOI=10.1016/j.jmb.2009.06.011;
Partridge J.R., Schwartz T.U.;
"Crystallographic and biochemical analysis of the Ran-binding zinc
finger domain.";
J. Mol. Biol. 391:375-389(2009).
[64] {ECO:0000244|PDB:3GJX}
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH GTP; XPO1 AND
SNUPN, AND IDENTIFICATION IN A COMPLEX WITH XPO1 AND SNUPN.
PubMed=19389996; DOI=10.1126/science.1173388;
Monecke T., Guttler T., Neumann P., Dickmanns A., Gorlich D.,
Ficner R.;
"Crystal structure of the nuclear export receptor CRM1 in complex with
Snurportin1 and RanGTP.";
Science 324:1087-1091(2009).
[65] {ECO:0000244|PDB:5DH9, ECO:0000244|PDB:5DHA, ECO:0000244|PDB:5DHF, ECO:0000244|PDB:5DI9, ECO:0000244|PDB:5DIF}
X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH GTP ANALOG;
CPEB4 NUCLEAR EXPORT SIGNAL AND YEAST HOMOLOGS OF XPO1 AND RANGAP1.
PubMed=26349033; DOI=10.7554/eLife.10034;
Fung H.Y., Fu S.C., Brautigam C.A., Chook Y.M.;
"Structural determinants of nuclear export signal orientation in
binding to exportin CRM1.";
Elife 4:0-0(2015).
[66] {ECO:0000244|PDB:5CIQ, ECO:0000244|PDB:5CIT, ECO:0000244|PDB:5CIW, ECO:0000244|PDB:5CJ2, ECO:0000244|PDB:5CLL, ECO:0000244|PDB:5CLQ}
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEXES WITH GTP ANALOGS
AND RANBP2, FUNCTION, INTERACTION WITH RANBP2, COFACTOR, AND
MUTAGENESIS OF THR-25 AND TYR-39.
PubMed=26272610; DOI=10.1074/jbc.M115.648071;
Rudack T., Jenrich S., Brucker S., Vetter I.R., Gerwert K.,
Kotting C.;
"Catalysis of GTP hydrolysis by small GTPases at atomic detail by
integration of X-ray crystallography, experimental, and theoretical IR
spectroscopy.";
J. Biol. Chem. 290:24079-24090(2015).
[67] {ECO:0000244|PDB:5UWH, ECO:0000244|PDB:5UWI, ECO:0000244|PDB:5UWJ, ECO:0000244|PDB:5UWO, ECO:0000244|PDB:5UWP, ECO:0000244|PDB:5UWQ, ECO:0000244|PDB:5UWR, ECO:0000244|PDB:5UWS, ECO:0000244|PDB:5UWT, ECO:0000244|PDB:5UWU, ECO:0000244|PDB:5UWW}
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH GTP ANALOG AND
THE YEAST HOMOLOGS OF XPO1 AND RANGAP1.
PubMed=28282025; DOI=10.7554/eLife.23961;
Fung H.Y., Fu S.C., Chook Y.M.;
"Nuclear export receptor CRM1 recognizes diverse conformations in
nuclear export signals.";
Elife 6:0-0(2017).
-!- FUNCTION: GTPase involved in nucleocytoplasmic transport,
participating both to the import and the export from the nucleus
of proteins and RNAs (PubMed:10400640, PubMed:8276887,
PubMed:8896452, PubMed:8636225, PubMed:8692944, PubMed:9351834,
PubMed:9428644, PubMed:9822603, PubMed:26272610). Switches between
a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide
exchange and GTP hydrolysis (PubMed:7819259, PubMed:8896452,
PubMed:8636225, PubMed:8692944, PubMed:9351834, PubMed:9428644,
PubMed:9822603, PubMed:29040603, PubMed:11336674,
PubMed:26272610). Nuclear import receptors such as importin beta
bind their substrates only in the absence of GTP-bound RAN and
release them upon direct interaction with GTP-bound RAN, while
export receptors behave in the opposite way. Thereby, RAN controls
cargo loading and release by transport receptors in the proper
compartment and ensures the directionality of the transport
(PubMed:8896452, PubMed:9351834, PubMed:9428644). Interaction with
RANBP1 induces a conformation change in the complex formed by XPO1
and RAN that triggers the release of the nuclear export signal of
cargo proteins (PubMed:20485264). RAN (GTP-bound form) triggers
microtubule assembly at mitotic chromosomes and is required for
normal mitotic spindle assembly and chromosome segregation
(PubMed:10408446, PubMed:29040603). Required for normal progress
through mitosis (PubMed:8421051, PubMed:12194828,
PubMed:29040603). The complex with BIRC5/survivin plays a role in
mitotic spindle formation by serving as a physical scaffold to
help deliver the RAN effector molecule TPX2 to microtubules
(PubMed:18591255). Acts as a negative regulator of the kinase
activity of VRK1 and VRK2 (PubMed:18617507). Enhances AR-mediated
transactivation. Transactivation decreases as the poly-Gln length
within AR increases (PubMed:10400640).
{ECO:0000269|PubMed:10400640, ECO:0000269|PubMed:10408446,
ECO:0000269|PubMed:11336674, ECO:0000269|PubMed:12194828,
ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:18617507,
ECO:0000269|PubMed:20485264, ECO:0000269|PubMed:29040603,
ECO:0000269|PubMed:7819259, ECO:0000269|PubMed:8276887,
ECO:0000269|PubMed:8421051, ECO:0000269|PubMed:8636225,
ECO:0000269|PubMed:8692944, ECO:0000269|PubMed:8896452,
ECO:0000269|PubMed:9351834, ECO:0000269|PubMed:9428644,
ECO:0000269|PubMed:9822603, ECO:0000305|PubMed:26272610}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:26272610};
Note=Mg(2+) interacts primarily with the phosphate groups of the
bound guanine nucleotide. {ECO:0000269|PubMed:26272610};
-!- SUBUNIT: Monomer. Interacts with RANGAP1, which promotes RAN-
mediated GTP hydrolysis (PubMed:7819259, PubMed:9428644).
Interacts with KPNB1 (PubMed:8896452, PubMed:9428644,
PubMed:10367892). Interaction with KPNB1 inhibits RANGAP1-mediated
stimulation of GTPase activity (PubMed:9428644). Interacts with
RCC1 which promotes the exchange of RAN-bound GDP by GTP
(PubMed:1961752, PubMed:7819259, PubMed:12194828,
PubMed:11336674). Interaction with KPNB1 inhibits RCC1-mediated
exchange of RAN-bound GDP by GTP (PubMed:8896452). Interacts (GTP-
bound form) with TNPO1; the interaction is direct
(PubMed:9351834). Interacts with KPNB1 and with TNPO1; both
inhibit RAN GTPase activity (PubMed:8896452, PubMed:9428644).
Interacts (via C-terminus) with RANBP1, which alleviates the
inhibition of RAN GTPase activity (PubMed:7891706, PubMed:8896452,
PubMed:9428644, PubMed:11832950). Interacts with RANGRF, which
promotes the release of bound guanine nucleotide
(PubMed:29040603). RANGRF and RCC1 compete for an overlapping
binding site on RAN (PubMed:29040603). Identified in a complex
with KPNA2 and CSE1L; interaction with RANBP1 mediates
dissociation of RAN from this complex (PubMed:9428644).
Interaction with both RANBP1 and KPNA2 promotes dissociation of
the complex between RAN and KPNB1 (PubMed:9428644). Identified in
a complex composed of RAN, RANGAP1 and RANBP1 (PubMed:16428860).
Identified in a complex that contains TNPO1, RAN and RANBP1
(PubMed:9428644). Identified in a nuclear export complex with XPO1
(PubMed:9323133, PubMed:15574331, PubMed:10209022). Found in a
nuclear export complex with RANBP3 and XPO1 (PubMed:11571268,
PubMed:11425870). Interacts with RANBP2/NUP358 (PubMed:10078529,
PubMed:26272610). Interaction with RANBP1 or RANBP2 induces a
conformation change in the complex formed by XPO1 and RAN that
triggers the release of the nuclear export signal of cargo
proteins (PubMed:20485264). Component of a nuclear export receptor
complex composed of KPNB1, RAN, SNUPN and XPO1 (PubMed:10209022,
PubMed:19389996). Found in a nuclear export complex with RAN, XPO5
and pre-miRNA (By similarity). Interacts (GTP-bound form) with
XPO5 (By similarity). Part of a complex consisting of RANBP9, RAN,
DYRK1B and COPS5 (PubMed:14500717). Interacts with RANBP9 and
RANBP10 (PubMed:14684163). Interacts in its GTP-bound form with
BIRC5/survivin at S and M phases of the cell cycle
(PubMed:18591255). Interacts with TERT; the interaction requires
hydrogen peroxide-mediated phosphorylation of TERT and transports
TERT to the nucleus (PubMed:12808100). Interacts with MAD2L2
(PubMed:19753112). Interacts with VRK1 and VRK3 (PubMed:18617507).
Interacts with isoform 1 and isoform 2 of VRK2 (PubMed:18617507).
Interacts with NEMP1 and KPNB1 (By similarity). Interacts (GDP-
bound form) with NUTF2; regulates RAN nuclear import
(PubMed:9822603, PubMed:10679025, PubMed:18266911). Interacts with
CAPG; mediates CAPG nuclear import (PubMed:10679025,
PubMed:18266911). Interacts with NUP153 (PubMed:18611384,
PubMed:19505478). Interacts with the AR N-terminal poly-Gln
region; the interaction with AR is inversely correlated with the
poly-Gln length (PubMed:10400640). Interacts with MYCBP2, which
promotes RAN-mediated GTP hydrolysis (PubMed:26304119).
{ECO:0000250|UniProtKB:P62825, ECO:0000250|UniProtKB:P62827,
ECO:0000269|PubMed:10078529, ECO:0000269|PubMed:10209022,
ECO:0000269|PubMed:10400640, ECO:0000269|PubMed:10679025,
ECO:0000269|PubMed:11336674, ECO:0000269|PubMed:11425870,
ECO:0000269|PubMed:11571268, ECO:0000269|PubMed:11832950,
ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:12808100,
ECO:0000269|PubMed:14500717, ECO:0000269|PubMed:14684163,
ECO:0000269|PubMed:15574331, ECO:0000269|PubMed:16428860,
ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:18611384,
ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:19389996,
ECO:0000269|PubMed:19505478, ECO:0000269|PubMed:1961752,
ECO:0000269|PubMed:19753112, ECO:0000269|PubMed:20485264,
ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26304119,
ECO:0000269|PubMed:29040603, ECO:0000269|PubMed:7819259,
ECO:0000269|PubMed:7891706, ECO:0000269|PubMed:8896452,
ECO:0000269|PubMed:9323133, ECO:0000269|PubMed:9351834,
ECO:0000269|PubMed:9428644, ECO:0000269|PubMed:9822603}.
-!- SUBUNIT: (Microbial infection) In case of HIV-1 infection, found
in a complex with HIV-1 Rev, RNAs containing a Rev response
element (RRE) and XPO1. {ECO:0000269|PubMed:9837918}.
-!- SUBUNIT: (Microbial infection) Found in a complex with HTLV-1 Rex,
RANBP3 and XPO1. {ECO:0000269|PubMed:14612415}.
-!- INTERACTION:
Q8WVL7:ANKRD49; NbExp=2; IntAct=EBI-286642, EBI-9381820;
O15392:BIRC5; NbExp=7; IntAct=EBI-286642, EBI-518823;
O94829:IPO13; NbExp=13; IntAct=EBI-286642, EBI-747310;
P49791:Nup153 (xeno); NbExp=5; IntAct=EBI-286642, EBI-6140533;
P61970:NUTF2; NbExp=5; IntAct=EBI-286642, EBI-591778;
Q8WUF5:PPP1R13L; NbExp=9; IntAct=EBI-286642, EBI-5550163;
P18754:RCC1; NbExp=6; IntAct=EBI-286642, EBI-992720;
Q13625:TP53BP2; NbExp=5; IntAct=EBI-286642, EBI-77642;
Q99986:VRK1; NbExp=12; IntAct=EBI-286642, EBI-1769146;
Q86Y07-1:VRK2; NbExp=2; IntAct=EBI-286642, EBI-1207633;
Q86Y07-5:VRK2; NbExp=2; IntAct=EBI-286642, EBI-1207649;
Q6P5F9:Xpo1 (xeno); NbExp=3; IntAct=EBI-286642, EBI-2550236;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10679025,
ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:8421051,
ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9351834,
ECO:0000269|PubMed:9822603}. Nucleus envelope
{ECO:0000269|PubMed:8896452, ECO:0000269|PubMed:9822603}.
Cytoplasm, cytosol {ECO:0000269|PubMed:8276887}. Cytoplasm
{ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:12194828,
ECO:0000269|PubMed:9822603}. Melanosome
{ECO:0000269|PubMed:17081065}. Note=Predominantly nuclear during
interphase (PubMed:8421051, PubMed:12194828, PubMed:10679025).
Becomes dispersed throughout the cytoplasm during mitosis
(PubMed:8421051, PubMed:12194828). Identified by mass spectrometry
in melanosome fractions from stage I to stage IV
(PubMed:17081065). {ECO:0000269|PubMed:10679025,
ECO:0000269|PubMed:12194828, ECO:0000269|PubMed:17081065,
ECO:0000269|PubMed:8421051}.
-!- TISSUE SPECIFICITY: Expressed in a variety of tissues.
{ECO:0000269|PubMed:2108320}.
-!- PTM: Acetylation by KAT5 at Lys-134 is increased during mitosis,
impairs RANGRF binding and enhances RCC1 binding.
{ECO:0000269|PubMed:29040603}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB93486.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RANID4203912q24.html";
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EMBL; M31469; AAA36546.1; -; mRNA.
EMBL; AF052578; AAC05840.1; -; mRNA.
EMBL; AF054183; AAC99400.1; -; mRNA.
EMBL; AF501887; AAM15923.1; -; mRNA.
EMBL; BT007271; AAP35935.1; -; mRNA.
EMBL; CR450347; CAG29343.1; -; mRNA.
EMBL; AK290763; BAF83452.1; -; mRNA.
EMBL; AK312466; BAG35373.1; -; mRNA.
EMBL; CH471054; EAW98516.1; -; Genomic_DNA.
EMBL; BC004272; AAH04272.3; -; mRNA.
EMBL; BC014518; AAH14518.1; -; mRNA.
EMBL; BC014901; AAH14901.1; -; mRNA.
EMBL; BC016654; AAH16654.1; -; mRNA.
EMBL; BC051908; AAH51908.2; -; mRNA.
EMBL; BC072000; AAH72000.1; -; mRNA.
EMBL; AB062399; BAB93486.1; ALT_INIT; mRNA.
CCDS; CCDS9271.1; -.
PIR; A44393; TVHUC3.
RefSeq; NP_001287725.1; NM_001300796.1.
RefSeq; NP_001287726.1; NM_001300797.1.
RefSeq; NP_006316.1; NM_006325.4.
UniGene; Hs.10842; -.
PDB; 1I2M; X-ray; 1.76 A; A/C=1-216.
PDB; 1IBR; X-ray; 2.30 A; A/C=1-216.
PDB; 1K5D; X-ray; 2.70 A; A/D/G/J=1-216.
PDB; 1K5G; X-ray; 3.10 A; A/D/G/J=1-216.
PDB; 1QBK; X-ray; 3.00 A; C=1-216.
PDB; 1RRP; X-ray; 2.96 A; A/C=8-211.
PDB; 2MMC; NMR; -; A=1-216.
PDB; 2MMG; NMR; -; A=1-216.
PDB; 2N1B; NMR; -; A=1-216.
PDB; 3CH5; X-ray; 2.10 A; A=1-216.
PDB; 3EA5; X-ray; 2.50 A; A/C=1-216.
PDB; 3GJ0; X-ray; 1.48 A; A/B=2-216.
PDB; 3GJ3; X-ray; 1.79 A; A=2-216.
PDB; 3GJ4; X-ray; 2.15 A; A/C=2-216.
PDB; 3GJ5; X-ray; 1.79 A; A/C=2-216.
PDB; 3GJ6; X-ray; 2.70 A; A=2-216.
PDB; 3GJ7; X-ray; 1.93 A; A/C=2-216.
PDB; 3GJ8; X-ray; 1.82 A; A/C=2-216.
PDB; 3GJX; X-ray; 2.50 A; C/F=1-216.
PDB; 3NBY; X-ray; 3.42 A; C/F=5-180.
PDB; 3NBZ; X-ray; 2.80 A; C/F=5-180.
PDB; 3NC0; X-ray; 2.90 A; C/F=5-180.
PDB; 3NC1; X-ray; 3.35 A; C=1-180.
PDB; 3ZJY; X-ray; 3.60 A; A/D/F=1-180.
PDB; 4C0Q; X-ray; 3.42 A; C/D=2-216.
PDB; 4GMX; X-ray; 2.10 A; A=1-216.
PDB; 4GPT; X-ray; 2.22 A; A=1-216.
PDB; 4HAT; X-ray; 1.78 A; A=1-216.
PDB; 4HAU; X-ray; 2.00 A; A=1-216.
PDB; 4HAV; X-ray; 2.00 A; A=1-216.
PDB; 4HAW; X-ray; 1.90 A; A=1-216.
PDB; 4HAX; X-ray; 2.28 A; A=1-216.
PDB; 4HAY; X-ray; 2.30 A; A=1-216.
PDB; 4HAZ; X-ray; 1.90 A; A=1-216.
PDB; 4HB0; X-ray; 2.20 A; A=1-216.
PDB; 4HB2; X-ray; 1.80 A; A=1-216.
PDB; 4HB3; X-ray; 2.80 A; A=1-216.
PDB; 4HB4; X-ray; 2.05 A; A=1-216.
PDB; 4OL0; X-ray; 2.90 A; A=1-216.
PDB; 4WVF; X-ray; 1.80 A; A=1-216.
PDB; 5CIQ; X-ray; 1.65 A; A/B=1-216.
PDB; 5CIT; X-ray; 1.75 A; A/B=1-216.
PDB; 5CIW; X-ray; 1.75 A; A/B=1-216.
PDB; 5CJ2; X-ray; 1.75 A; A/B/C/D/E/F/G/H=1-216.
PDB; 5CLL; X-ray; 2.45 A; A/C=1-191.
PDB; 5CLQ; X-ray; 3.20 A; A/C=1-216.
PDB; 5DH9; X-ray; 2.55 A; A=1-216.
PDB; 5DHA; X-ray; 2.95 A; A=1-216.
PDB; 5DHF; X-ray; 2.29 A; A=1-216.
PDB; 5DI9; X-ray; 2.28 A; A=1-216.
PDB; 5DIF; X-ray; 2.09 A; A=1-216.
PDB; 5DIS; X-ray; 2.85 A; B=8-179.
PDB; 5DLQ; X-ray; 3.20 A; C/D=5-180.
PDB; 5FYQ; X-ray; 3.00 A; C/D=31-43.
PDB; 5JLJ; X-ray; 2.50 A; A=1-216.
PDB; 5UWH; X-ray; 2.26 A; A=1-216.
PDB; 5UWI; X-ray; 2.14 A; A=1-216.
PDB; 5UWJ; X-ray; 2.22 A; A=1-216.
PDB; 5UWO; X-ray; 2.35 A; A=1-216.
PDB; 5UWP; X-ray; 2.05 A; A=1-216.
PDB; 5UWQ; X-ray; 2.28 A; A=1-216.
PDB; 5UWR; X-ray; 2.24 A; A=1-216.
PDB; 5UWS; X-ray; 2.40 A; A=1-216.
PDB; 5UWT; X-ray; 2.34 A; A=1-216.
PDB; 5UWU; X-ray; 2.24 A; A=1-216.
PDB; 5UWW; X-ray; 2.15 A; A=1-216.
PDB; 6CIT; X-ray; 2.03 A; A=1-216.
PDBsum; 1I2M; -.
PDBsum; 1IBR; -.
PDBsum; 1K5D; -.
PDBsum; 1K5G; -.
PDBsum; 1QBK; -.
PDBsum; 1RRP; -.
PDBsum; 2MMC; -.
PDBsum; 2MMG; -.
PDBsum; 2N1B; -.
PDBsum; 3CH5; -.
PDBsum; 3EA5; -.
PDBsum; 3GJ0; -.
PDBsum; 3GJ3; -.
PDBsum; 3GJ4; -.
PDBsum; 3GJ5; -.
PDBsum; 3GJ6; -.
PDBsum; 3GJ7; -.
PDBsum; 3GJ8; -.
PDBsum; 3GJX; -.
PDBsum; 3NBY; -.
PDBsum; 3NBZ; -.
PDBsum; 3NC0; -.
PDBsum; 3NC1; -.
PDBsum; 3ZJY; -.
PDBsum; 4C0Q; -.
PDBsum; 4GMX; -.
PDBsum; 4GPT; -.
PDBsum; 4HAT; -.
PDBsum; 4HAU; -.
PDBsum; 4HAV; -.
PDBsum; 4HAW; -.
PDBsum; 4HAX; -.
PDBsum; 4HAY; -.
PDBsum; 4HAZ; -.
PDBsum; 4HB0; -.
PDBsum; 4HB2; -.
PDBsum; 4HB3; -.
PDBsum; 4HB4; -.
PDBsum; 4OL0; -.
PDBsum; 4WVF; -.
PDBsum; 5CIQ; -.
PDBsum; 5CIT; -.
PDBsum; 5CIW; -.
PDBsum; 5CJ2; -.
PDBsum; 5CLL; -.
PDBsum; 5CLQ; -.
PDBsum; 5DH9; -.
PDBsum; 5DHA; -.
PDBsum; 5DHF; -.
PDBsum; 5DI9; -.
PDBsum; 5DIF; -.
PDBsum; 5DIS; -.
PDBsum; 5DLQ; -.
PDBsum; 5FYQ; -.
PDBsum; 5JLJ; -.
PDBsum; 5UWH; -.
PDBsum; 5UWI; -.
PDBsum; 5UWJ; -.
PDBsum; 5UWO; -.
PDBsum; 5UWP; -.
PDBsum; 5UWQ; -.
PDBsum; 5UWR; -.
PDBsum; 5UWS; -.
PDBsum; 5UWT; -.
PDBsum; 5UWU; -.
PDBsum; 5UWW; -.
PDBsum; 6CIT; -.
ProteinModelPortal; P62826; -.
SMR; P62826; -.
BioGrid; 111837; 158.
CORUM; P62826; -.
DIP; DIP-5929N; -.
IntAct; P62826; 104.
MINT; P62826; -.
STRING; 9606.ENSP00000376176; -.
ChEMBL; CHEMBL3885569; -.
DrugBank; DB04315; Guanosine-5'-Diphosphate.
TCDB; 9.A.60.1.1; the small nuclear rna exporter (snrna-e).
iPTMnet; P62826; -.
PhosphoSitePlus; P62826; -.
SwissPalm; P62826; -.
BioMuta; RAN; -.
DMDM; 51338598; -.
OGP; P62826; -.
REPRODUCTION-2DPAGE; P62826; -.
UCD-2DPAGE; P62826; -.
EPD; P62826; -.
MaxQB; P62826; -.
PaxDb; P62826; -.
PeptideAtlas; P62826; -.
PRIDE; P62826; -.
ProteomicsDB; 57429; -.
TopDownProteomics; P62826; -.
DNASU; 5901; -.
Ensembl; ENST00000392369; ENSP00000376176; ENSG00000132341.
Ensembl; ENST00000543796; ENSP00000446215; ENSG00000132341.
GeneID; 5901; -.
KEGG; hsa:5901; -.
UCSC; uc001uir.4; human.
CTD; 5901; -.
DisGeNET; 5901; -.
EuPathDB; HostDB:ENSG00000132341.11; -.
GeneCards; RAN; -.
HGNC; HGNC:9846; RAN.
HPA; HPA063353; -.
MIM; 601179; gene.
neXtProt; NX_P62826; -.
OpenTargets; ENSG00000132341; -.
PharmGKB; PA34205; -.
eggNOG; KOG0096; Eukaryota.
eggNOG; ENOG410XNRS; LUCA.
GeneTree; ENSGT00840000129836; -.
HOVERGEN; HBG107376; -.
InParanoid; P62826; -.
KO; K07936; -.
PhylomeDB; P62826; -.
TreeFam; TF106302; -.
Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
Reactome; R-HSA-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF).
Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
Reactome; R-HSA-180746; Nuclear import of Rev protein.
Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-6784531; tRNA processing in the nucleus.
SignaLink; P62826; -.
SIGNOR; P62826; -.
ChiTaRS; RAN; human.
EvolutionaryTrace; P62826; -.
GeneWiki; Ran_(biology); -.
GenomeRNAi; 5901; -.
PRO; PR:P62826; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000132341; Expressed in 226 organ(s), highest expression level in testis.
ExpressionAtlas; P62826; baseline and differential.
Genevisible; P62826; HS.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005643; C:nuclear pore; NAS:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0042565; C:RNA nuclear export complex; IDA:BHF-UCL.
GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0003682; F:chromatin binding; TAS:UniProtKB.
GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; NAS:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006259; P:DNA metabolic process; TAS:UniProtKB.
GO; GO:0046039; P:GTP metabolic process; IDA:UniProtKB.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0010586; P:miRNA metabolic process; TAS:Reactome.
GO; GO:0000278; P:mitotic cell cycle; TAS:UniProtKB.
GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB.
GO; GO:0007052; P:mitotic spindle organization; TAS:UniProtKB.
GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0035281; P:pre-miRNA export from nucleus; IC:BHF-UCL.
GO; GO:0006611; P:protein export from nucleus; IDA:BHF-UCL.
GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
GO; GO:0000060; P:protein import into nucleus, translocation; IMP:UniProtKB.
GO; GO:1902570; P:protein localization to nucleolus; IMP:UniProtKB.
GO; GO:0045540; P:regulation of cholesterol biosynthetic process; TAS:Reactome.
GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:ParkinsonsUK-UCL.
GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:ParkinsonsUK-UCL.
GO; GO:0061015; P:snRNA import into nucleus; IMP:UniProtKB.
GO; GO:0006409; P:tRNA export from nucleus; TAS:Reactome.
GO; GO:0016032; P:viral process; TAS:Reactome.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR002041; Ran_GTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
PANTHER; PTHR24071; PTHR24071; 1.
Pfam; PF00071; Ras; 1.
PRINTS; PR00627; GTPRANTC4.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51418; RAN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell cycle; Cell division;
Complete proteome; Cytoplasm; Direct protein sequencing; GTP-binding;
Host-virus interaction; Isopeptide bond; Magnesium; Metal-binding;
Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
Protein transport; Reference proteome; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.12}.
CHAIN 2 216 GTP-binding nuclear protein Ran.
/FTId=PRO_0000208696.
NP_BIND 18 25 GTP. {ECO:0000244|PDB:1IBR,
ECO:0000244|PDB:1K5G,
ECO:0000244|PDB:1RRP,
ECO:0000244|PDB:3CH5,
ECO:0000244|PDB:3GJ0,
ECO:0000244|PDB:3GJ3,
ECO:0000244|PDB:3GJ4,
ECO:0000244|PDB:3GJ5,
ECO:0000244|PDB:3GJ6,
ECO:0000244|PDB:3GJ7,
ECO:0000244|PDB:3GJ8,
ECO:0000244|PDB:3GJX,
ECO:0000244|PDB:3NBY,
ECO:0000244|PDB:3NBZ,
ECO:0000244|PDB:3NC0,
ECO:0000244|PDB:3NC1,
ECO:0000244|PDB:3ZJY,
ECO:0000244|PDB:4C0Q,
ECO:0000244|PDB:4OL0,
ECO:0000244|PDB:5CIQ,
ECO:0000244|PDB:5CIT,
ECO:0000244|PDB:5CIW,
ECO:0000244|PDB:5CLQ,
ECO:0000244|PDB:5DH9,
ECO:0000244|PDB:5DHA,
ECO:0000244|PDB:5DHF,
ECO:0000244|PDB:5DI9,
ECO:0000244|PDB:5DIF,
ECO:0000244|PDB:5DIS,
ECO:0000244|PDB:5DLQ,
ECO:0000244|PDB:5UWH,
ECO:0000244|PDB:5UWI,
ECO:0000244|PDB:5UWJ,
ECO:0000244|PDB:5UWO,
ECO:0000244|PDB:5UWP,
ECO:0000244|PDB:5UWQ,
ECO:0000244|PDB:5UWR,
ECO:0000244|PDB:5UWS,
ECO:0000244|PDB:5UWT,
ECO:0000244|PDB:5UWU,
ECO:0000244|PDB:5UWW,
ECO:0000269|PubMed:10078529,
ECO:0000269|PubMed:10353245,
ECO:0000269|PubMed:10367892,
ECO:0000269|PubMed:11832950,
ECO:0000269|PubMed:18611384,
ECO:0000269|PubMed:19389996,
ECO:0000269|PubMed:19505478,
ECO:0000269|PubMed:26272610,
ECO:0000269|PubMed:26349033,
ECO:0000269|PubMed:28282025,
ECO:0000269|PubMed:7885480}.
NP_BIND 36 42 GTP. {ECO:0000244|PDB:1IBR,
ECO:0000244|PDB:1K5D,
ECO:0000244|PDB:1QBK,
ECO:0000244|PDB:1RRP,
ECO:0000244|PDB:3GJX,
ECO:0000244|PDB:3NBY,
ECO:0000244|PDB:3NBZ,
ECO:0000244|PDB:3NC0,
ECO:0000244|PDB:3NC1,
ECO:0000244|PDB:3ZJY,
ECO:0000244|PDB:4C0Q,
ECO:0000244|PDB:4OL0,
ECO:0000244|PDB:5CLL,
ECO:0000244|PDB:5CLQ,
ECO:0000244|PDB:5DH9,
ECO:0000244|PDB:5DHA,
ECO:0000244|PDB:5DHF,
ECO:0000244|PDB:5DI9,
ECO:0000244|PDB:5DIF,
ECO:0000244|PDB:5DIS,
ECO:0000244|PDB:5DLQ,
ECO:0000244|PDB:5JLJ,
ECO:0000244|PDB:5UWH,
ECO:0000244|PDB:5UWI,
ECO:0000244|PDB:5UWJ,
ECO:0000244|PDB:5UWO,
ECO:0000244|PDB:5UWP,
ECO:0000244|PDB:5UWQ,
ECO:0000244|PDB:5UWR,
ECO:0000244|PDB:5UWS,
ECO:0000244|PDB:5UWT,
ECO:0000244|PDB:5UWU,
ECO:0000244|PDB:5UWW,
ECO:0000269|PubMed:10078529,
ECO:0000269|PubMed:10353245,
ECO:0000269|PubMed:10367892,
ECO:0000269|PubMed:11832950,
ECO:0000269|PubMed:19389996,
ECO:0000269|PubMed:26272610,
ECO:0000269|PubMed:26349033,
ECO:0000269|PubMed:28282025,
ECO:0000269|PubMed:7885480}.
NP_BIND 122 125 GTP. {ECO:0000244|PDB:1IBR,
ECO:0000244|PDB:1K5D,
ECO:0000244|PDB:1QBK,
ECO:0000244|PDB:1RRP,
ECO:0000244|PDB:3CH5,
ECO:0000244|PDB:3GJ0,
ECO:0000244|PDB:3GJ3,
ECO:0000244|PDB:3GJ4,
ECO:0000244|PDB:3GJ5,
ECO:0000244|PDB:3GJ6,
ECO:0000244|PDB:3GJ7,
ECO:0000244|PDB:3GJ8,
ECO:0000244|PDB:3GJX,
ECO:0000244|PDB:3NBY,
ECO:0000244|PDB:3NBZ,
ECO:0000244|PDB:3NC0,
ECO:0000244|PDB:3NC1,
ECO:0000244|PDB:3ZJY,
ECO:0000244|PDB:4C0Q,
ECO:0000244|PDB:4OL0,
ECO:0000244|PDB:5CIQ,
ECO:0000244|PDB:5CIT,
ECO:0000244|PDB:5CIW,
ECO:0000244|PDB:5CJ2,
ECO:0000244|PDB:5CLL,
ECO:0000244|PDB:5DH9,
ECO:0000244|PDB:5DHA,
ECO:0000244|PDB:5DHF,
ECO:0000244|PDB:5DI9,
ECO:0000244|PDB:5DIF,
ECO:0000244|PDB:5DIS,
ECO:0000244|PDB:5DLQ,
ECO:0000244|PDB:5JLJ,
ECO:0000244|PDB:5UWH,
ECO:0000244|PDB:5UWI,
ECO:0000244|PDB:5UWJ,
ECO:0000244|PDB:5UWO,
ECO:0000244|PDB:5UWP,
ECO:0000244|PDB:5UWQ,
ECO:0000244|PDB:5UWR,
ECO:0000244|PDB:5UWS,
ECO:0000244|PDB:5UWT,
ECO:0000244|PDB:5UWU,
ECO:0000244|PDB:5UWW,
ECO:0000269|PubMed:10078529,
ECO:0000269|PubMed:10353245,
ECO:0000269|PubMed:10367892,
ECO:0000269|PubMed:11832950,
ECO:0000269|PubMed:18611384,
ECO:0000269|PubMed:19389996,
ECO:0000269|PubMed:19505478,
ECO:0000269|PubMed:26272610,
ECO:0000269|PubMed:26349033,
ECO:0000269|PubMed:28282025,
ECO:0000269|PubMed:7885480}.
NP_BIND 150 152 GTP. {ECO:0000244|PDB:1K5G,
ECO:0000244|PDB:3CH5,
ECO:0000244|PDB:3GJ0,
ECO:0000244|PDB:3GJ3,
ECO:0000244|PDB:3GJ4,
ECO:0000244|PDB:3GJ5,
ECO:0000244|PDB:3GJ6,
ECO:0000244|PDB:3GJ7,
ECO:0000244|PDB:3GJ8,
ECO:0000244|PDB:3GJX,
ECO:0000244|PDB:3NBY,
ECO:0000244|PDB:3NBZ,
ECO:0000244|PDB:3NC0,
ECO:0000244|PDB:3NC1,
ECO:0000244|PDB:3ZJY,
ECO:0000244|PDB:4C0Q,
ECO:0000244|PDB:4OL0,
ECO:0000244|PDB:5CIQ,
ECO:0000244|PDB:5CIT,
ECO:0000244|PDB:5CIW,
ECO:0000244|PDB:5CJ2,
ECO:0000244|PDB:5CLL,
ECO:0000244|PDB:5CLQ,
ECO:0000244|PDB:5DH9,
ECO:0000244|PDB:5DHA,
ECO:0000244|PDB:5DHF,
ECO:0000244|PDB:5DI9,
ECO:0000244|PDB:5DIF,
ECO:0000244|PDB:5DIS,
ECO:0000244|PDB:5DLQ,
ECO:0000244|PDB:5JLJ,
ECO:0000244|PDB:5UWH,
ECO:0000244|PDB:5UWI,
ECO:0000244|PDB:5UWJ,
ECO:0000244|PDB:5UWO,
ECO:0000244|PDB:5UWP,
ECO:0000244|PDB:5UWQ,
ECO:0000244|PDB:5UWR,
ECO:0000244|PDB:5UWS,
ECO:0000244|PDB:5UWT,
ECO:0000244|PDB:5UWU,
ECO:0000244|PDB:5UWW,
ECO:0000269|PubMed:10078529,
ECO:0000269|PubMed:10353245,
ECO:0000269|PubMed:10367892,
ECO:0000269|PubMed:11832950,
ECO:0000269|PubMed:18611384,
ECO:0000269|PubMed:19389996,
ECO:0000269|PubMed:19505478,
ECO:0000269|PubMed:26272610,
ECO:0000269|PubMed:26349033,
ECO:0000269|PubMed:28282025,
ECO:0000269|PubMed:7885480}.
REGION 211 216 Interaction with RANBP1.
{ECO:0000269|PubMed:7891706}.
BINDING 68 68 GTP; via amide nitrogen.
{ECO:0000244|PDB:1IBR,
ECO:0000244|PDB:1K5D,
ECO:0000244|PDB:1QBK,
ECO:0000244|PDB:1RRP,
ECO:0000244|PDB:3GJX,
ECO:0000244|PDB:3NBY,
ECO:0000244|PDB:3NBZ,
ECO:0000244|PDB:3NC0,
ECO:0000244|PDB:3NC1,
ECO:0000244|PDB:3ZJY,
ECO:0000244|PDB:4C0Q,
ECO:0000244|PDB:4OL0,
ECO:0000244|PDB:5DH9,
ECO:0000244|PDB:5DHA,
ECO:0000244|PDB:5DHF,
ECO:0000244|PDB:5DI9,
ECO:0000244|PDB:5DIF,
ECO:0000244|PDB:5DIS,
ECO:0000244|PDB:5DLQ,
ECO:0000244|PDB:5JLJ,
ECO:0000244|PDB:5UWH,
ECO:0000244|PDB:5UWI,
ECO:0000244|PDB:5UWJ,
ECO:0000244|PDB:5UWO,
ECO:0000244|PDB:5UWP,
ECO:0000244|PDB:5UWQ,
ECO:0000244|PDB:5UWR,
ECO:0000244|PDB:5UWS,
ECO:0000244|PDB:5UWT,
ECO:0000244|PDB:5UWU,
ECO:0000244|PDB:5UWW,
ECO:0000269|PubMed:10078529,
ECO:0000269|PubMed:10353245,
ECO:0000269|PubMed:10367892,
ECO:0000269|PubMed:11832950,
ECO:0000269|PubMed:18611384,
ECO:0000269|PubMed:19389996,
ECO:0000269|PubMed:19505478,
ECO:0000269|PubMed:26272610,
ECO:0000269|PubMed:26349033,
ECO:0000269|PubMed:28282025,
ECO:0000269|PubMed:7885480}.
SITE 69 69 Essential for GTP hydrolysis.
{ECO:0000269|PubMed:18591255,
ECO:0000269|PubMed:26272610,
ECO:0000269|PubMed:8636225}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.12}.
MOD_RES 24 24 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 60 60 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 71 71 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 99 99 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 134 134 N6-acetyllysine.
{ECO:0000269|PubMed:29040603}.
MOD_RES 159 159 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 159 159 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P62827}.
CROSSLNK 71 71 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 71 71 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
CROSSLNK 152 152 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
MUTAGEN 19 19 G->V: Blocks DNA replication; when
associated with L-69.
{ECO:0000269|PubMed:8421051}.
MUTAGEN 24 24 T->L: Has low binding affinity for GTP
and GDP. Almost completely abolishes
interaction with BIRC5.
{ECO:0000269|PubMed:18591255}.
MUTAGEN 24 24 T->N: Has low binding affinity for GTP
and GDP. Decreases nuclear import of
proteins and RNA. Stabilizes the
interaction with RCC1. No effect on
nuclear location during interphase. Loss
of activity in triggering microtubule
assembly at mitotic chromosomes.
{ECO:0000269|PubMed:10408446,
ECO:0000269|PubMed:12194828,
ECO:0000269|PubMed:7819259,
ECO:0000269|PubMed:8636225,
ECO:0000269|PubMed:9351834}.
MUTAGEN 25 25 T->A: Minor effect on the interaction
with the alpha phosphate group of bound
GTP. {ECO:0000269|PubMed:26272610}.
MUTAGEN 39 39 Y->A: Abolishes steric hindrance that
traps the essential Q-69 in an unreactive
position, and causes slow GTP hydrolysis
in wild-type. Loss of one hydrogen bond
with the gamma phosphate group of bound
GTP. {ECO:0000269|PubMed:26272610}.
MUTAGEN 69 69 Q->L: Strongly decreased GTPase activity.
Probably locked in the GTP-bound form.
Loss of interaction with NUTF2. Decreases
nuclear location and leads to cytoplasmic
location during interphase. Loss of
function in importin-mediated protein
nuclear import. High activity in
triggering microtubule assembly at
mitotic chromosomes. Blocks DNA
replication; when associated with V-19.
{ECO:0000269|PubMed:10408446,
ECO:0000269|PubMed:12194828,
ECO:0000269|PubMed:18591255,
ECO:0000269|PubMed:7819259,
ECO:0000269|PubMed:8421051,
ECO:0000269|PubMed:8636225,
ECO:0000269|PubMed:9351834,
ECO:0000269|PubMed:9822603}.
MUTAGEN 69 69 Q->N: Unable to hydrolyze GTP. Increases
binding to BIRC5 and promotes exaggerated
spindle formation.
{ECO:0000269|PubMed:18591255}.
MUTAGEN 70 70 E->A: Strongly decreases the relase of
bound GDP. {ECO:0000269|PubMed:11336674}.
MUTAGEN 76 76 R->E: Probable loss of interaction with
NUTF2. Loss of transport to the nucleus.
{ECO:0000269|PubMed:9822603}.
MUTAGEN 134 134 K->Q: Loss of normal mitotic chromosome
segregation and defective mitotic spindle
orientation.
{ECO:0000269|PubMed:29040603}.
MUTAGEN 134 134 K->R: Loss of normal mitotic chromosome
segregation and formation of sister
chromatid bridges.
{ECO:0000269|PubMed:29040603}.
MUTAGEN 211 216 Missing: No effect on GTPase activity.
Abolishes interaction with RANBP1.
{ECO:0000269|PubMed:7891706}.
CONFLICT 2 2 A -> T (in Ref. 11; AAH72000).
{ECO:0000305}.
CONFLICT 181 181 A -> C (in Ref. 5; AAC99400).
{ECO:0000305}.
TURN 2 5 {ECO:0000244|PDB:2MMG}.
STRAND 10 17 {ECO:0000244|PDB:3GJ0}.
STRAND 18 22 {ECO:0000244|PDB:1QBK}.
HELIX 23 27 {ECO:0000244|PDB:3GJ0}.
HELIX 31 35 {ECO:0000244|PDB:3GJ0}.
STRAND 38 40 {ECO:0000244|PDB:3GJ0}.
TURN 41 44 {ECO:0000244|PDB:3GJ0}.
STRAND 45 54 {ECO:0000244|PDB:3GJ0}.
STRAND 57 66 {ECO:0000244|PDB:3GJ0}.
HELIX 69 71 {ECO:0000244|PDB:3GJ0}.
HELIX 74 76 {ECO:0000244|PDB:1K5D}.
HELIX 77 80 {ECO:0000244|PDB:3GJ0}.
STRAND 85 91 {ECO:0000244|PDB:3GJ0}.
STRAND 92 94 {ECO:0000244|PDB:1RRP}.
HELIX 95 99 {ECO:0000244|PDB:3GJ0}.
HELIX 101 111 {ECO:0000244|PDB:3GJ0}.
STRAND 112 114 {ECO:0000244|PDB:5CJ2}.
STRAND 117 122 {ECO:0000244|PDB:3GJ0}.
STRAND 126 128 {ECO:0000244|PDB:3GJ0}.
HELIX 133 135 {ECO:0000244|PDB:3GJ0}.
HELIX 138 142 {ECO:0000244|PDB:3GJ0}.
STRAND 145 148 {ECO:0000244|PDB:3GJ0}.
TURN 151 154 {ECO:0000244|PDB:3GJ0}.
TURN 156 158 {ECO:0000244|PDB:3GJ0}.
HELIX 159 169 {ECO:0000244|PDB:3GJ0}.
STRAND 176 178 {ECO:0000244|PDB:3GJ0}.
TURN 185 187 {ECO:0000244|PDB:1QBK}.
HELIX 191 205 {ECO:0000244|PDB:3GJ0}.
HELIX 211 215 {ECO:0000244|PDB:2MMC}.
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


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