Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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.
30-AUG-2017, entry version 171.
RecName: Full=GTP-binding nuclear protein Ran;
AltName: Full=Androgen receptor-associated protein 24;
AltName: Full=GTPase Ran;
AltName: Full=Ras-like protein TC4;
AltName: Full=Ras-related nuclear protein;
Name=RAN; Synonyms=ARA24; 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], AND TISSUE SPECIFICITY.
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 CHC1, 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.
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
INTERACTION WITH NUTF2.
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
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).
[39]
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).
[40]
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).
[41]
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).
[42]
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).
[43]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
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).
[44]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH 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).
[45]
X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF COMPLEX WITH NUP358.
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).
-!- FUNCTION: GTPase involved in nucleocytoplasmic transport,
participating both to the import and the export from the nucleus
of proteins and RNAs. Switches between a cytoplasmic GDP- and a
nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis.
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
ensure the directionality of the transport.
{ECO:0000269|PubMed:8692944, ECO:0000269|PubMed:9822603}.
-!- FUNCTION: 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:18591255,
ECO:0000269|PubMed:18617507}.
-!- SUBUNIT: Monomer. Also forms a complex with CHC1 and interacts
with the AR N-terminal poly-Gln region. The interaction with AR is
inversely correlated with the poly-Gln length. Part of a complex
consisting of RANBP9, RAN, DYRK1B and COPS5. Found in a nuclear
export complex with RANBP3 and XPO1. Component of a nuclear export
receptor complex composed of KPNB1, RAN, SNUPN and XPO1. Found in
a trimeric export complex with SNUPN, RAN and XPO1. Interacts with
RANBP10. Interacts in its GTP-bound form with BIRC5/survivin at S
and M phases of the cell cycle. Interacts with TERT; the
interaction requires hydrogen peroxide-mediated phosphorylation of
TERT and transports TERT to the nucleus. Interacts with MAD2L2.
Interacts with RANBP10 (By similarity). Interacts with VRK1 and
VRK3. Interacts with isoform 1 and isoform 2 of VRK2. Interacts
with NEMP1 and KPNB1 (By similarity). Interacts (GDP-bound form)
with NUTF2; regulates RAN nuclear import (PubMed:9822603,
PubMed:10679025). Interacts with CAPG; mediates CAPG nuclear
import (PubMed:10679025). {ECO:0000250|UniProtKB:P62827,
ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:10400640,
ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:11425870,
ECO:0000269|PubMed:11571268, ECO:0000269|PubMed:12808100,
ECO:0000269|PubMed:14500717, ECO:0000269|PubMed:14684163,
ECO:0000269|PubMed:15574331, ECO:0000269|PubMed:18591255,
ECO:0000269|PubMed:18617507, ECO:0000269|PubMed:1961752,
ECO:0000269|PubMed:19753112, ECO:0000269|PubMed:9323133,
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. Found in a complex with HTLV-1 Rex, RANBP3
and XPO1. {ECO:0000269|PubMed:14612415,
ECO:0000269|PubMed:9837918}.
-!- 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;
P61970:NUTF2; NbExp=4; 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;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9822603}.
Nucleus envelope {ECO:0000269|PubMed:9822603}. Cytoplasm
{ECO:0000269|PubMed:9822603}. Melanosome
{ECO:0000250|UniProtKB:P62827}. Note=Predominantly nuclear during
interphase. Becomes dispersed throughout the cytoplasm during
mitosis. Identified by mass spectrometry in melanosome fractions
from stage I to stage IV. {ECO:0000250|UniProtKB:P62827}.
-!- TISSUE SPECIFICITY: Expressed in a variety of tissues.
{ECO:0000269|PubMed:2108320}.
-!- 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";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
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.
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; -.
ProteinModelPortal; P62826; -.
SMR; P62826; -.
BioGrid; 111837; 152.
DIP; DIP-5929N; -.
IntAct; P62826; 79.
MINT; MINT-94188; -.
STRING; 9606.ENSP00000376176; -.
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; -.
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; -.
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; -.
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; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030496; C:midbody; 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:0043234; C:protein 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; IDA:BHF-UCL.
GO; GO:0003682; F:chromatin binding; TAS:UniProtKB.
GO; GO:0019003; F:GDP binding; IDA:CAFA.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; TAS:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA.
GO; GO:0003723; F:RNA binding; IDA: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: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: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:0060964; P:regulation of gene silencing by miRNA; 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: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.
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; 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 17 24 GTP. {ECO:0000250}.
NP_BIND 65 69 GTP. {ECO:0000250}.
NP_BIND 122 125 GTP. {ECO:0000250}.
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 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 69 69 Q->L: Probably locked in the GTP-bound
form. Loss of interaction with NUTF2.
Loss of function in importin-mediated
protein nuclear import. Blocks DNA
replication; when associated with V-19.
{ECO:0000269|PubMed:18591255,
ECO:0000269|PubMed:8421051,
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,
ECO:0000269|PubMed:8421051}.
MUTAGEN 76 76 R->E: Probable loss of interaction with
NUTF2. Loss of transport to the nucleus.
{ECO:0000269|PubMed:9822603}.
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


Related products :

Catalog number Product name Quantity
EIAAB33742 Androgen receptor-associated protein 24,ARA24,GTPase Ran,GTP-binding nuclear protein Ran,Homo sapiens,Human,OK_SW-cl.81,RAN,Ras-like protein TC4,Ras-related nuclear protein
18-373-88020 GTP-binding nuclear protein Ran - GTPase Ran; Ras-like protein TC4; Androgen receptor-associated protein 24 Polyclonal 0.1 ml
EIAAB33739 GTPase Ran,GTP-binding nuclear protein Ran,Mouse,Mus musculus,Ran,Rasl2-8,Ras-like protein TC4,Ras-related nuclear protein
EIAAB33741 GTPase Ran,GTP-binding nuclear protein Ran,Ran,Ras-like protein TC4,Ras-related nuclear protein,Rat,Rattus norvegicus
EIAAB33740 Bos taurus,Bovine,GTPase Ran,GTP-binding nuclear protein Ran,RAN,Ras-related nuclear protein
EIAAB33737 Chicken,Gallus gallus,GTPase Ran,GTP-binding nuclear protein Ran,RAN,Ras-like protein TC4,Ras-related nuclear protein
EIAAB33738 Canis familiaris,Canis lupus familiaris,Dog,GTPase Ran,GTP-binding nuclear protein Ran,RAN,Ras-like protein TC4,Ras-related nuclear protein
EIAAB05063 Antigen nuclear dot 52 kDa protein,Calcium-binding and coiled-coil domain-containing protein 2,CALCOCO2,Homo sapiens,Human,NDP52,Nuclear domain 10 protein 52,Nuclear domain 10 protein NDP52,Nuclear do
EIAAB26566 70 kDa androgen receptor coactivator,70 kDa AR-activator,Androgen receptor coactivator 70 kDa protein,Androgen receptor-associated protein of 70 kDa,ARA70,ELE1,Homo sapiens,Human,NCOA4,NCoA-4,Nuclear
18-003-44214 Non-POU domain-containing octamer-binding protein - NonO protein; 54 kDa nuclear RNA- and DNA-binding protein; p54(nrb); p54nrb; 55 kDa nuclear protein; NMT55; DNA-binding p52_p100 complex. 52 kDa sub 0.1 mg Protein A
18-003-43630 Non-POU domain-containing octamer-binding protein - NonO protein; 54 kDa nuclear RNA- and DNA-binding protein; p54(nrb); p54nrb; 55 kDa nuclear protein; NMT55; DNA-binding p52_p100 complex. 52 kDa sub 0.1 mg Protein A
EIAAB27848 Homo sapiens,Human,NRBP2,Nuclear receptor-binding protein 2,PP9320,Transformation-related gene 16 protein,TRG16,TRG-16
EIAAB45295 E3 ubiquitin-protein ligase UHRF1,Homo sapiens,Human,HuNp95,ICBP90,Inverted CCAAT box-binding protein of 90 kDa,NP95,Nuclear protein 95,Nuclear zinc finger protein Np95,RING finger protein 106,RNF106,
EIAAB26507 20 kDa nuclear cap-binding protein,CBP20,CBP20,Cell proliferation-inducing gene 55 protein,Homo sapiens,Human,NCBP 20 kDa subunit,NCBP2,NCBP-interacting protein 1,NIP1,Nuclear cap-binding protein subu
EIAAB27518 54 kDa nuclear RNA- and DNA-binding protein,55 kDa nuclear protein,DNA-binding p52_p100 complex, 52 kDa subunit,Homo sapiens,Human,NMT55,NONO,NonO protein,Non-POU domain-containing octamer-binding pro
EIAAB29667 Homo sapiens,Human,Nuclear poly(A)-binding protein 1,PAB2,PABII,PABP2,PABP-2,PABPN1,Poly(A)-binding protein 2,Poly(A)-binding protein II,Polyadenylate-binding nuclear protein 1,Polyadenylate-binding p
18-003-42173 SNW domain-containing protein 1 - Nuclear protein SkiP; Ski-interacting protein; Nuclear receptor coactivator NCoA-62 Polyclonal 0.05 mg Aff Pur
EIAAB27778 EAR-1R,Homo sapiens,Human,NR1D2,Nuclear receptor subfamily 1 group D member 2,Orphan nuclear hormone receptor BD73,Rev-erb-beta,V-erbA-related protein 1-related
EIAAB29665 Mouse,Mus musculus,Nuclear poly(A)-binding protein 1,Pab2,PABII,Pabp2,PABP-2,Pabpn1,Poly(A)-binding protein 2,Poly(A)-binding protein II,Polyadenylate-binding nuclear protein 1,Polyadenylate-binding p
EIAAB29666 Bos taurus,Bovine,Nuclear poly(A)-binding protein 1,PAB2,PABII,PABP2,PABP-2,PABPN1,Poly(A)-binding protein 2,Poly(A)-binding protein II,Polyadenylate-binding nuclear protein 1,Polyadenylate-binding pr
EIAAB27810 Gfrp,Hmr,Mouse,Mus musculus,N10,Nr4a1,Nuclear hormone receptor NUR_77,Nuclear protein N10,Nuclear receptor subfamily 4 group A member 1,Nur77,Orphan nuclear receptor HMR
EIAAB39941 Homo sapiens,Human,Ser_Arg-related nuclear matrix protein,Serine_arginine repetitive matrix protein 1,SRm160,SRM160,SR-related nuclear matrix protein of 160 kDa,SRRM1
EIAAB41166 p53-dependent damage-inducible nuclear protein 1,p53DINP1,Rat,Rattus norvegicus,Sip,Stress-induced protein,TEAP,Thymus-expressed acidic protein,Trp53inp1,Tumor protein p53-inducible nuclear protein 1
EIAAB41165 Mouse,Mus musculus,p53-dependent damage-inducible nuclear protein 1,p53DINP1,Sip,Stress-induced protein,TEAP,Thymus-expressed acidic protein,Trp53inp1,Tumor protein p53-inducible nuclear protein 1
EIAAB27980 CCDC55,Coiled-coil domain-containing protein 55,Homo sapiens,Human,NSRP1,NSrp70,NSRP70,Nuclear speckle splicing regulatory protein 1,Nuclear speckle-related protein 70


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur