XPO1_HUMAN
ID XPO1_HUMAN Reviewed; 1071 AA.
AC O14980; A6NL14; A8K1K5; D6W5E2; Q63HP8; Q68CP3; Q99433;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Exportin-1;
DE Short=Exp1;
DE AltName: Full=Chromosome region maintenance 1 protein homolog;
GN Name=XPO1; Synonyms=CRM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 757-765, INTERACTION WITH
RP NUP88 AND NUP214, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=9049309; DOI=10.1093/emboj/16.4.807;
RA Fornerod M., van Deursen J.M., van Baal S., Reynolds A., Davis D.,
RA Murti K.G., Fransen J., Grosveld G.;
RT "The human homologue of yeast CRM1 is in a dynamic subcomplex with
RT CAN/Nup214 and the novel nuclear pore component Nup88.";
RL EMBO J. 16:807-816(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Chronic myeloid leukemia cell;
RX PubMed=9368044; DOI=10.1074/jbc.272.47.29742;
RA Kudo N., Kohchbin S., Nishi K., Kitano K., Yanagida M., Yoshida M.,
RA Horinouchi S.;
RT "Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a
RT protein involved in nuclear export of proteins.";
RL J. Biol. Chem. 272:29742-29751(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 45-54; 63-88; 105-112; 130-139; 159-190; 246-253;
RP 296-305; 407-415; 424-442; 459-474; 480-492; 516-531; 538-553; 675-686;
RP 701-722; 797-810; 873-883; 996-1012 AND 1017-1038, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [9]
RP FUNCTION IN PROTEIN NUCLEAR EXPORT, AND IDENTIFICATION IN A NUCLEAR EXPORT
RP COMPLEX WITH RAN.
RX PubMed=9323133; DOI=10.1016/s0092-8674(00)80371-2;
RA Fornerod M., Ohno M., Yoshida M., Mattaj I.W.;
RT "CRM1 is an export receptor for leucine-rich nuclear export signals.";
RL Cell 90:1051-1060(1997).
RN [10]
RP FUNCTION IN PROTEIN NUCLEAR EXPORT.
RX PubMed=9311922; DOI=10.1126/science.278.5335.141;
RA Ossareh-Nazari B., Bachelerie F., Dargemont C.;
RT "Evidence for a role of CRM1 in signal-mediated nuclear protein export.";
RL Science 278:141-144(1997).
RN [11]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 REV (MICROBIAL
RP INFECTION).
RX PubMed=9837918; DOI=10.1074/jbc.273.50.33414;
RA Askjaer P., Jensen T.H., Nilsson J., Englmeier L., Kjems J.;
RT "The specificity of the CRM1-Rev nuclear export signal interaction is
RT mediated by RanGTP.";
RL J. Biol. Chem. 273:33414-33422(1998).
RN [12]
RP IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX, INTERACTION WITH IPO7;
RP KPNB1 AND SNUPN, AND IDENTIFICATION IN A TRIMERIC EXPORT COMPLEX WITH RAN
RP AND SNUPN.
RX PubMed=10209022; DOI=10.1083/jcb.145.2.255;
RA Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U.,
RA Hartmann E., Luehrmann R., Goerlich D.;
RT "CRM1-mediated recycling of snurportin 1 to the cytoplasm.";
RL J. Cell Biol. 145:255-264(1999).
RN [13]
RP INTERACTION WITH EBV BMLF1 (MICROBIAL INFECTION).
RX PubMed=10400785; DOI=10.1128/jvi.73.8.6872-6881.1999;
RA Boyle S.M., Ruvolo V., Gupta A.K., Swaminathan S.;
RT "Association with the cellular export receptor CRM 1 mediates function and
RT intracellular localization of Epstein-Barr virus SM protein, a regulator of
RT gene expression.";
RL J. Virol. 73:6872-6881(1999).
RN [14]
RP INACTIVATION BY LMB.
RX PubMed=10430904; DOI=10.1073/pnas.96.16.9112;
RA Kudo N., Matsumori N., Taoka H., Fujiwara D., Schreiner E.P., Wolff B.,
RA Yoshida M., Horinouchi S.;
RT "Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a
RT cysteine residue in the central conserved region.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9112-9117(1999).
RN [15]
RP INTERACTION WITH NUP42.
RX PubMed=10358091; DOI=10.1074/jbc.274.24.17309;
RA Farjot G., Sergeant A., Mikaelian I.;
RT "A new nucleoporin-like protein interacts with both HIV-1 Rev nuclear
RT export signal and CRM-1.";
RL J. Biol. Chem. 274:17309-17317(1999).
RN [16]
RP IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RANBP3 AND RAN, AND
RP INTERACTION WITH RANBP3.
RX PubMed=11571268; DOI=10.1093/embo-reports/kve200;
RA Englmeier L., Fornerod M., Bischoff F.R., Petosa C., Mattaj I.W., Kutay U.;
RT "RanBP3 influences interactions between CRM1 and its nuclear protein export
RT substrates.";
RL EMBO Rep. 2:926-932(2001).
RN [17]
RP INTERACTION WITH INFLUENZA A NUCLEOPROTEIN (MICROBIAL INFECTION).
RX PubMed=11119609; DOI=10.1128/jvi.75.1.408-419.2001;
RA Elton D., Simpson-Holley M., Archer K., Medcalf L., Hallam R., McCauley J.,
RA Digard P.;
RT "Interaction of the influenza virus nucleoprotein with the cellular CRM1-
RT mediated nuclear export pathway.";
RL J. Virol. 75:408-419(2001).
RN [18]
RP IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RANBP3 AND RAN, AND
RP INTERACTION WITH RANBP3.
RX PubMed=11425870; DOI=10.1083/jcb.153.7.1391;
RA Lindsay M.E., Holaska J.M., Welch K., Paschal B.M., Macara I.G.;
RT "Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein
RT export.";
RL J. Cell Biol. 153:1391-1402(2001).
RN [19]
RP INTERACTION WITH RANBP3.
RX PubMed=11932251; DOI=10.1074/jbc.c100620200;
RA Nemergut M.E., Lindsay M.E., Brownawell A.M., Macara I.G.;
RT "Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange
RT factor.";
RL J. Biol. Chem. 277:17385-17388(2002).
RN [20]
RP INTERACTION WITH HIV-1 REV (MICROBIAL INFECTION).
RX PubMed=12134013; DOI=10.1128/jvi.76.16.8079-8089.2002;
RA Hakata Y., Yamada M., Mabuchi N., Shida H.;
RT "The carboxy-terminal region of the human immunodeficiency virus type 1
RT protein Rev has multiple roles in mediating CRM1-related Rev functions.";
RL J. Virol. 76:8079-8089(2002).
RN [21]
RP IDENTIFICATION IN A 60S RIBOSOMAL SUBUNIT COMPLEX WITH RAN AND NMD3, AND
RP INTERACTION WITH NMD3.
RX PubMed=12724356; DOI=10.1242/jcs.00464;
RA Thomas F., Kutay U.;
RT "Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes
RT depend on the CRM1 export pathway.";
RL J. Cell Sci. 116:2409-2419(2003).
RN [22]
RP INTERACTION WITH TERT.
RX PubMed=12808100; DOI=10.1128/mcb.23.13.4598-4610.2003;
RA Haendeler J., Hoffmann J., Brandes R.P., Zeiher A.M., Dimmeler S.;
RT "Hydrogen peroxide triggers nuclear export of telomerase reverse
RT transcriptase via Src kinase family-dependent phosphorylation of tyrosine
RT 707.";
RL Mol. Cell. Biol. 23:4598-4610(2003).
RN [23]
RP FUNCTION (MICROBIAL INFECTION), IDENTIFICATION IN A COMPLEX WITH HTLV-1
RP REX; RANBP3 AND RAN, INTERACTION WITH HTLV-1 REX (MICROBIAL INFECTION) AND
RP RANBP3, AND MUTAGENESIS OF SER-191; VAL-284; ASP-334; ILE-337; THR-346;
RP VAL-402; PRO-411; MET-412; PHE-414; ARG-474 AND HIS-481.
RX PubMed=14612415; DOI=10.1128/mcb.23.23.8751-8761.2003;
RA Hakata Y., Yamada M., Shida H.;
RT "A multifunctional domain in human CRM1 (exportin 1) mediates RanBP3
RT binding and multimerization of human T-cell leukemia virus type 1 Rex
RT protein.";
RL Mol. Cell. Biol. 23:8751-8761(2003).
RN [24]
RP INTERACTION WITH DDX3X.
RX PubMed=15507209; DOI=10.1016/j.cell.2004.09.029;
RA Yedavalli V.S., Neuveut C., Chi Y.-H., Kleiman L., Jeang K.-T.;
RT "Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export
RT function.";
RL Cell 119:381-392(2004).
RN [25]
RP FUNCTION IN U3 SNORNA TRANSPORT, SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=15574332; DOI=10.1016/j.molcel.2004.11.013;
RA Boulon S., Verheggen C., Jady B.E., Girard C., Pescia C., Paul C.,
RA Ospina J.K., Kiss T., Matera A.G., Bordonne R., Bertrand E.;
RT "PHAX and CRM1 are required sequentially to transport U3 snoRNA to
RT nucleoli.";
RL Mol. Cell 16:777-787(2004).
RN [26]
RP INTERACTION WITH HIV-1 REV (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=15632073; DOI=10.1128/mcb.25.2.728-739.2005;
RA Daelemans D., Costes S.V., Lockett S., Pavlakis G.N.;
RT "Kinetic and molecular analysis of nuclear export factor CRM1 association
RT with its cargo in vivo.";
RL Mol. Cell. Biol. 25:728-739(2005).
RN [27]
RP INTERACTION WITH NEMF.
RX PubMed=16103875; DOI=10.1038/sj.onc.1208962;
RA Bi X., Jones T., Abbasi F., Lee H., Stultz B., Hursh D.A., Mortin M.A.;
RT "Drosophila caliban, a nuclear export mediator, can function as a tumor
RT suppressor in human lung cancer cells.";
RL Oncogene 24:8229-8239(2005).
RN [28]
RP INTERACTION WITH BOK.
RX PubMed=16302269; DOI=10.1002/mc.20156;
RA Bartholomeusz G., Wu Y., Ali Seyed M., Xia W., Kwong K.Y., Hortobagyi G.,
RA Hung M.C.;
RT "Nuclear translocation of the pro-apoptotic Bcl-2 family member Bok induces
RT apoptosis.";
RL Mol. Carcinog. 45:73-83(2006).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [30]
RP INTERACTION WITH SERTAD2.
RX PubMed=18316374; DOI=10.1074/jbc.m708365200;
RA Cheong J.K., Gunaratnam L., Hsu S.I.;
RT "CRM1-mediated nuclear export is required for 26 S proteasome-dependent
RT degradation of the TRIP-Br2 proto-oncoprotein.";
RL J. Biol. Chem. 283:11661-11676(2008).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-446 AND LYS-693, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [34]
RP INTERACTION WITH BIRC5/SURVIVIN.
RX PubMed=20826784; DOI=10.1074/jbc.m110.152777;
RA Wang H., Holloway M.P., Ma L., Cooper Z.A., Riolo M., Samkari A.,
RA Elenitoba-Johnson K.S., Chin Y.E., Altura R.A.;
RT "Acetylation directs survivin nuclear localization to repress STAT3
RT oncogenic activity.";
RL J. Biol. Chem. 285:36129-36137(2010).
RN [35]
RP IDENTIFICATION IN COMPLEX WITH CRM1 AND VENEZUELAN EQUINE ENCEPHALITIS
RP VIRUS CAPSID PROTEIN (MICROBIAL INFECTION).
RX PubMed=20147401; DOI=10.1128/jvi.02554-09;
RA Atasheva S., Fish A., Fornerod M., Frolova E.I.;
RT "Venezuelan equine encephalitis virus capsid protein forms a tetrameric
RT complex with CRM1 and importin alpha/beta that obstructs nuclear pore
RT complex function.";
RL J. Virol. 84:4158-4171(2010).
RN [36]
RP INTERACTION WITH DTNBP1, AND FUNCTION.
RX PubMed=20921223; DOI=10.1074/jbc.m110.107912;
RA Fei E., Ma X., Zhu C., Xue T., Yan J., Xu Y., Zhou J., Wang G.;
RT "Nucleocytoplasmic shuttling of dysbindin-1, a schizophrenia-related
RT protein, regulates synapsin I expression.";
RL J. Biol. Chem. 285:38630-38640(2010).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [38]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [39]
RP INTERACTION WITH HSP90AB1.
RX PubMed=22022502; DOI=10.1371/journal.pone.0026044;
RA Echeverria P.C., Bernthaler A., Dupuis P., Mayer B., Picard D.;
RT "An interaction network predicted from public data as a discovery tool:
RT application to the Hsp90 molecular chaperone machine.";
RL PLoS ONE 6:E26044-E26044(2011).
RN [40]
RP INTERACTION WITH SARS-COV VIRUS PROTEIN ORF9B (MICROBIAL INFECTION).
RX PubMed=21637748; DOI=10.1371/journal.pone.0019436;
RA Sharma K., Aakerstroem S., Sharma A.K., Chow V.T., Teow S., Abrenica B.,
RA Booth S.A., Booth T.F., Mirazimi A., Lal S.K.;
RT "SARS-CoV 9b protein diffuses into nucleus, undergoes active Crm1 mediated
RT nucleocytoplasmic export and triggers apoptosis when retained in the
RT nucleus.";
RL PLoS ONE 6:e19436-e19436(2011).
RN [41]
RP INTERACTION WITH DCAF8.
RX PubMed=22500989; DOI=10.1016/j.febslet.2012.02.053;
RA Wu F., Wang S., Xing J., Li M., Zheng C.;
RT "Characterization of nuclear import and export signals determining the
RT subcellular localization of WD repeat-containing protein 42A (WDR42A).";
RL FEBS Lett. 586:1079-1085(2012).
RN [42]
RP INTERACTION WITH SLC35G1 AND STIM1.
RX PubMed=22084111; DOI=10.1073/pnas.1117231108;
RA Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.;
RT "POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to
RT multiple transporters.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011).
RN [43]
RP INTERACTION WITH ATF2.
RX PubMed=22275354; DOI=10.1074/jbc.m111.294272;
RA Hsu C.C., Hu C.D.;
RT "Critical role of N-terminal end-localized nuclear export signal in
RT regulation of activating transcription factor 2 (ATF2) subcellular
RT localization and transcriptional activity.";
RL J. Biol. Chem. 287:8621-8632(2012).
RN [44]
RP INTERACTION WITH CPEB3.
RX PubMed=22730302; DOI=10.1093/nar/gks598;
RA Chao H.W., Lai Y.T., Lu Y.L., Lin C.L., Mai W., Huang Y.S.;
RT "NMDAR signaling facilitates the IPO5-mediated nuclear import of CPEB3.";
RL Nucleic Acids Res. 40:8484-8498(2012).
RN [45]
RP INTERACTION WITH HAX1.
RX PubMed=23164465; DOI=10.1111/febs.12066;
RA Grzybowska E.A., Zayat V., Konopinski R., Trebinska A., Szwarc M.,
RA Sarnowska E., Macech E., Korczynski J., Knapp A., Siedlecki J.A.;
RT "HAX-1 is a nucleocytoplasmic shuttling protein with a possible role in
RT mRNA processing.";
RL FEBS J. 280:256-272(2013).
RN [46]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND SER-1031, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [47]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [48]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 707-1027, ELECTRON MICROSCOPY (22
RP ANGSTROMS), IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RAN, AND
RP MUTAGENESIS OF 428-GLU--ASP-447; 430-VAL--LYS-446; 430-VAL--VAL-433;
RP TYR-454; GLU-513; LEU-525; GLN-550; ARG-553; PHE-554; PHE-561; LYS-568;
RP PHE-572; MET-583 AND LYS-590.
RX PubMed=15574331; DOI=10.1016/j.molcel.2004.11.018;
RA Petosa C., Schoehn G., Askjaer P., Bauer U., Moulin M., Steuerwald U.,
RA Soler-Lopez M., Baudin F., Mattaj I.W., Mueller C.W.;
RT "Architecture of CRM1/Exportin1 suggests how cooperativity is achieved
RT during formation of a nuclear export complex.";
RL Mol. Cell 16:761-775(2004).
CC -!- FUNCTION: Mediates the nuclear export of cellular proteins (cargos)
CC bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the
CC nucleus, in association with RANBP3, binds cooperatively to the NES on
CC its target protein and to the GTPase RAN in its active GTP-bound form
CC (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is
CC mediated through binding to nucleoporins. Upon transit of a nuclear
CC export complex into the cytoplasm, disassembling of the complex and
CC hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1,
CC respectively) cause release of the cargo from the export receptor. The
CC directionality of nuclear export is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran between
CC the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal
CC bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG
CC cap. {ECO:0000269|PubMed:15574332, ECO:0000269|PubMed:20921223,
CC ECO:0000269|PubMed:9311922, ECO:0000269|PubMed:9323133}.
CC -!- FUNCTION: (Microbial infection) Mediates the export of unspliced or
CC incompletely spliced RNAs out of the nucleus from different viruses
CC including HIV-1, HTLV-1 and influenza A. Interacts with, and mediates
CC the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in
CC HTLV-1 Rex multimerization. {ECO:0000269|PubMed:14612415,
CC ECO:0000269|PubMed:9837918}.
CC -!- SUBUNIT: Found in a U snRNA export complex with PHAX/RNUXA,
CC NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA (By similarity).
CC Component of a nuclear export receptor complex composed of KPNB1, RAN,
CC SNUPN and XPO1. Found in a trimeric export complex with SNUPN, RAN and
CC XPO1. Found in a nuclear export complex with RANBP3 and RAN. Found in a
CC 60S ribosomal subunit export complex with NMD3, RAN, XPO1. Interacts
CC with DDX3X, NMD3, NUP42, NUP88, NUP214, RANBP3 and TERT. Interacts with
CC NEMF (via its N-terminus). Interacts with the monomeric form of
CC BIRC5/survivin deacetylated at 'Lys-129'. Interacts with DTNBP1 and
CC SERTAD2; the interactions translocate DTNBP1 and SERTAD2 out of the
CC nucleus. Interacts with ATF2. Interacts with SLC35G1 and STIM1.
CC Interacts with DCAF8. Interacts with CPEB3 (PubMed:22730302). Interacts
CC with HAX1 (PubMed:23164465). Interacts with BOK; translocates to the
CC cytoplasm (PubMed:16302269). Interacts with HSP90AB1 (PubMed:22022502).
CC {ECO:0000250|UniProtKB:Q6P5F9, ECO:0000269|PubMed:10209022,
CC ECO:0000269|PubMed:10358091, ECO:0000269|PubMed:11425870,
CC ECO:0000269|PubMed:11571268, ECO:0000269|PubMed:11932251,
CC ECO:0000269|PubMed:12724356, ECO:0000269|PubMed:12808100,
CC ECO:0000269|PubMed:14612415, ECO:0000269|PubMed:15507209,
CC ECO:0000269|PubMed:15574331, ECO:0000269|PubMed:16103875,
CC ECO:0000269|PubMed:16302269, ECO:0000269|PubMed:18316374,
CC ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:20921223,
CC ECO:0000269|PubMed:22022502, ECO:0000269|PubMed:22084111,
CC ECO:0000269|PubMed:22275354, ECO:0000269|PubMed:22500989,
CC ECO:0000269|PubMed:22730302, ECO:0000269|PubMed:23164465,
CC ECO:0000269|PubMed:9049309, ECO:0000269|PubMed:9323133}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Rev.
CC {ECO:0000269|PubMed:12134013, ECO:0000269|PubMed:15632073,
CC ECO:0000269|PubMed:9837918}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 Rex.
CC {ECO:0000269|PubMed:14612415}.
CC -!- SUBUNIT: (Microbial infection) Interacts with influenza A
CC nucleoprotein. {ECO:0000269|PubMed:11119609}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
CC protein BMLF1. {ECO:0000269|PubMed:10400785}.
CC -!- SUBUNIT: (Microbial infection) Part of a tetrameric complex composed of
CC CRM1, importin alpha/beta dimer and the Venezuelan equine encephalitis
CC virus (VEEV) capsid; this complex blocks the receptor-mediated
CC transport through the nuclear pore. {ECO:0000269|PubMed:20147401}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS-CoV virus protein
CC ORF9b; this interaction mediates protein ORF9b export out of the
CC nucleus. {ECO:0000269|PubMed:21637748}.
CC -!- INTERACTION:
CC O14980; O15392: BIRC5; NbExp=2; IntAct=EBI-355867, EBI-518823;
CC O14980; Q08211: DHX9; NbExp=3; IntAct=EBI-355867, EBI-352022;
CC O14980; P04626: ERBB2; NbExp=2; IntAct=EBI-355867, EBI-641062;
CC O14980; P22736: NR4A1; NbExp=2; IntAct=EBI-355867, EBI-721550;
CC O14980; P35232: PHB; NbExp=2; IntAct=EBI-355867, EBI-354213;
CC O14980; P61925: PKIA; NbExp=2; IntAct=EBI-355867, EBI-2682139;
CC O14980; O95149: SNUPN; NbExp=8; IntAct=EBI-355867, EBI-714033;
CC O14980; P04637: TP53; NbExp=3; IntAct=EBI-355867, EBI-366083;
CC O14980; P63104: YWHAZ; NbExp=2; IntAct=EBI-355867, EBI-347088;
CC O14980; P04618: rev; Xeno; NbExp=2; IntAct=EBI-355867, EBI-6164309;
CC O14980; Q9WMX2; Xeno; NbExp=3; IntAct=EBI-355867, EBI-710918;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleoplasm. Nucleus, Cajal
CC body. Nucleus, nucleolus. Note=Located in the nucleoplasm, Cajal bodies
CC and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver,
CC skeletal muscle, pancreas, spleen, thymus, prostate, testis, ovary,
CC small intestine, colon and peripheral blood leukocytes. Not expressed
CC in the kidney. {ECO:0000269|PubMed:9049309,
CC ECO:0000269|PubMed:9368044}.
CC -!- MISCELLANEOUS: Cellular target of leptomycin B (LMB), a XPO1/CRM1
CC nuclear export inhibitor.
CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/XPO1ID44168ch2p15.html";
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DR EMBL; Y08614; CAA69905.2; -; mRNA.
DR EMBL; D89729; BAA23415.1; -; mRNA.
DR EMBL; AK289920; BAF82609.1; -; mRNA.
DR EMBL; BX647758; CAH56174.1; -; mRNA.
DR EMBL; CR749840; CAH18695.1; -; mRNA.
DR EMBL; AC016727; AAY14949.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99993.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99994.1; -; Genomic_DNA.
DR EMBL; BC032847; AAH32847.1; -; mRNA.
DR CCDS; CCDS33205.1; -.
DR RefSeq; NP_003391.1; NM_003400.3.
DR RefSeq; XP_006712157.1; XM_006712094.2.
DR RefSeq; XP_011531399.1; XM_011533097.1.
DR PDB; 1W9C; X-ray; 2.30 A; A/B=707-1027.
DR PDB; 2L1L; NMR; -; B=504-630.
DR PDB; 3GB8; X-ray; 2.90 A; A=1-1071.
DR PDB; 4BSM; X-ray; 4.50 A; A=1-1032.
DR PDB; 4BSN; X-ray; 4.10 A; A=1-1032.
DR PDB; 5DIS; X-ray; 2.85 A; A=5-1048.
DR PDB; 6TVO; X-ray; 3.20 A; A=1-1036.
DR PDB; 7B51; X-ray; 2.58 A; A=1-1036.
DR PDBsum; 1W9C; -.
DR PDBsum; 2L1L; -.
DR PDBsum; 3GB8; -.
DR PDBsum; 4BSM; -.
DR PDBsum; 4BSN; -.
DR PDBsum; 5DIS; -.
DR PDBsum; 6TVO; -.
DR PDBsum; 7B51; -.
DR AlphaFoldDB; O14980; -.
DR SMR; O14980; -.
DR BioGRID; 113348; 1411.
DR CORUM; O14980; -.
DR DIP; DIP-33678N; -.
DR IntAct; O14980; 127.
DR MINT; O14980; -.
DR STRING; 9606.ENSP00000384863; -.
DR BindingDB; O14980; -.
DR ChEMBL; CHEMBL5661; -.
DR DrugBank; DB11942; Selinexor.
DR DrugCentral; O14980; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; O14980; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14980; -.
DR MetOSite; O14980; -.
DR PhosphoSitePlus; O14980; -.
DR SwissPalm; O14980; -.
DR BioMuta; XPO1; -.
DR EPD; O14980; -.
DR jPOST; O14980; -.
DR MassIVE; O14980; -.
DR MaxQB; O14980; -.
DR PaxDb; O14980; -.
DR PeptideAtlas; O14980; -.
DR PRIDE; O14980; -.
DR ProteomicsDB; 48356; -.
DR Antibodypedia; 4124; 376 antibodies from 35 providers.
DR DNASU; 7514; -.
DR Ensembl; ENST00000401558.7; ENSP00000384863.2; ENSG00000082898.19.
DR Ensembl; ENST00000404992.6; ENSP00000385942.2; ENSG00000082898.19.
DR Ensembl; ENST00000406957.5; ENSP00000385559.1; ENSG00000082898.19.
DR Ensembl; ENST00000676553.1; ENSP00000504247.1; ENSG00000082898.19.
DR Ensembl; ENST00000676667.1; ENSP00000503809.1; ENSG00000082898.19.
DR Ensembl; ENST00000677150.1; ENSP00000503167.1; ENSG00000082898.19.
DR Ensembl; ENST00000677239.1; ENSP00000504087.1; ENSG00000082898.19.
DR Ensembl; ENST00000677417.1; ENSP00000503572.1; ENSG00000082898.19.
DR Ensembl; ENST00000677813.1; ENSP00000504543.1; ENSG00000082898.19.
DR Ensembl; ENST00000677814.1; ENSP00000504848.1; ENSG00000082898.19.
DR Ensembl; ENST00000677928.1; ENSP00000504198.1; ENSG00000082898.19.
DR Ensembl; ENST00000677933.1; ENSP00000503482.1; ENSG00000082898.19.
DR Ensembl; ENST00000678182.1; ENSP00000504594.1; ENSG00000082898.19.
DR Ensembl; ENST00000678790.1; ENSP00000503419.1; ENSG00000082898.19.
DR GeneID; 7514; -.
DR KEGG; hsa:7514; -.
DR MANE-Select; ENST00000401558.7; ENSP00000384863.2; NM_003400.4; NP_003391.1.
DR UCSC; uc002sbj.4; human.
DR CTD; 7514; -.
DR DisGeNET; 7514; -.
DR GeneCards; XPO1; -.
DR HGNC; HGNC:12825; XPO1.
DR HPA; ENSG00000082898; Low tissue specificity.
DR MalaCards; XPO1; -.
DR MIM; 602559; gene.
DR neXtProt; NX_O14980; -.
DR OpenTargets; ENSG00000082898; -.
DR Orphanet; 98838; Primary mediastinal large B-cell lymphoma.
DR PharmGKB; PA37418; -.
DR VEuPathDB; HostDB:ENSG00000082898; -.
DR eggNOG; KOG2020; Eukaryota.
DR GeneTree; ENSGT00940000153408; -.
DR HOGENOM; CLU_011906_0_0_1; -.
DR InParanoid; O14980; -.
DR OMA; HNINTLC; -.
DR OrthoDB; 132850at2759; -.
DR PhylomeDB; O14980; -.
DR TreeFam; TF105695; -.
DR PathwayCommons; O14980; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-HSA-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; O14980; -.
DR SIGNOR; O14980; -.
DR BioGRID-ORCS; 7514; 699 hits in 1090 CRISPR screens.
DR ChiTaRS; XPO1; human.
DR EvolutionaryTrace; O14980; -.
DR GeneWiki; XPO1; -.
DR GenomeRNAi; 7514; -.
DR Pharos; O14980; Tclin.
DR PRO; PR:O14980; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O14980; protein.
DR Bgee; ENSG00000082898; Expressed in tibia and 212 other tissues.
DR ExpressionAtlas; O14980; baseline and differential.
DR Genevisible; O14980; HS.
DR GO; GO:0005642; C:annulate lamellae; IDA:UniProtKB.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; TAS:ProtInc.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IMP:UniProtKB.
DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0010824; P:regulation of centrosome duplication; IEA:Ensembl.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0046825; P:regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:ParkinsonsUK-UCL.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:ParkinsonsUK-UCL.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IMP:ParkinsonsUK-UCL.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:ParkinsonsUK-UCL.
DR Gene3D; 1.25.10.10; -; 1.
DR IDEAL; IID00357; -.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR041123; CRM1_repeat.
DR InterPro; IPR041235; Exp1_repeat_2.
DR InterPro; IPR013598; Exportin-1/Importin-b-like.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR045065; XPO1/5.
DR InterPro; IPR014877; XPO1_C_dom.
DR InterPro; IPR040485; XPO1_repeat_3.
DR PANTHER; PTHR11223; PTHR11223; 1.
DR Pfam; PF08767; CRM1_C; 1.
DR Pfam; PF18777; CRM1_repeat; 1.
DR Pfam; PF18784; CRM1_repeat_2; 1.
DR Pfam; PF18787; CRM1_repeat_3; 1.
DR Pfam; PF03810; IBN_N; 1.
DR Pfam; PF08389; Xpo1; 1.
DR SMART; SM01102; CRM1_C; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; mRNA transport; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; RNA-binding; Transport.
FT CHAIN 1..1071
FT /note="Exportin-1"
FT /id="PRO_0000204705"
FT DOMAIN 46..112
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 217..240
FT /note="HEAT 1"
FT REPEAT 241..277
FT /note="HEAT 2"
FT REPEAT 354..472
FT /note="HEAT 3"
FT REPEAT 515..553
FT /note="HEAT 4"
FT REPEAT 560..597
FT /note="HEAT 5"
FT REPEAT 602..639
FT /note="HEAT 6"
FT REPEAT 775..813
FT /note="HEAT 7"
FT REPEAT 885..916
FT /note="HEAT 8"
FT REPEAT 917..954
FT /note="HEAT 9"
FT REPEAT 1002..1039
FT /note="HEAT 10"
FT REGION 1..679
FT /note="Necessary for HTLV-1 Rex-mediated mRNA export"
FT REGION 327..450
FT /note="Interaction with Ran and nuclear export complex
FT formation"
FT REGION 411..481
FT /note="Interaction with RANBP3"
FT REGION 411..414
FT /note="Necessary for HTLV-1 Rex multimerization"
FT REGION 800..820
FT /note="Interaction with HIV-1 Rev"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 446
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 448
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80U96"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80U96"
FT MOD_RES 454
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80U96"
FT MOD_RES 693
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 191
FT /note="S->A: Does not abolish Rex-mediated mRNA export."
FT /evidence="ECO:0000269|PubMed:14612415"
FT MUTAGEN 284
FT /note="V->E: Does not abolish Rex-mediated mRNA export."
FT /evidence="ECO:0000269|PubMed:14612415"
FT MUTAGEN 334
FT /note="D->G: Does not abolish Rex-mediated mRNA export."
FT /evidence="ECO:0000269|PubMed:14612415"
FT MUTAGEN 337
FT /note="I->L: Does not abolish Rex-mediated mRNA export."
FT /evidence="ECO:0000269|PubMed:14612415"
FT MUTAGEN 346
FT /note="T->A: Does not abolish Rex-mediated mRNA export."
FT /evidence="ECO:0000269|PubMed:14612415"
FT MUTAGEN 402
FT /note="V->I: Does not abolish Rex-mediated mRNA export."
FT /evidence="ECO:0000269|PubMed:14612415"
FT MUTAGEN 411
FT /note="P->T: Strongly abolishes interaction with Rex and
FT RANBP3, abolishes Rex-mediated mRNA export. Does not
FT abolish interaction with RANBP3; when associated with S-
FT 414. Abolishes Rex multimerization; when associated with S-
FT 414."
FT /evidence="ECO:0000269|PubMed:14612415"
FT MUTAGEN 412
FT /note="M->V: Does not abolish interaction with Rex and
FT RANBP3, and Rex-mediated mRNA export."
FT /evidence="ECO:0000269|PubMed:14612415"
FT MUTAGEN 414
FT /note="F->S: Strongly abolishes interaction with Rex and
FT RANBP3, abolishes Rex-mediated mRNA export. Does not
FT abolish interaction with RANBP3; when associated with T-
FT 411. Abolishes Rex multimerization; when associated with T-
FT 411."
FT /evidence="ECO:0000269|PubMed:14612415"
FT MUTAGEN 428..447
FT /note="EEVLVVENDQGEVVREFMKD->QQVLVVQNNQGQVVRQFMKN:
FT Abolishes Ran binding activity in absence of cargo and
FT abolishes partially Ran binding activity in presence of
FT cargo."
FT /evidence="ECO:0000269|PubMed:15574331"
FT MUTAGEN 430..446
FT /note="VLVVENDQGEVVREFMK->DEDEENDQGEDEEEDDD: Partially
FT restores Ran binding activity in presence of cargo."
FT /evidence="ECO:0000269|PubMed:15574331"
FT MUTAGEN 430..433
FT /note="VLVV->DEDE: Abolishes Ran binding activity both in
FT absence or presence of cargo."
FT /evidence="ECO:0000269|PubMed:15574331"
FT MUTAGEN 454
FT /note="Y->A: Does not abolish Ran binding activity and
FT nuclear export complex formation."
FT /evidence="ECO:0000269|PubMed:15574331"
FT MUTAGEN 474
FT /note="R->I: Strongly abolishes interaction with Rex and
FT RANBP3, abolishes Rex-mediated mRNA export."
FT /evidence="ECO:0000269|PubMed:14612415"
FT MUTAGEN 481
FT /note="H->Q: Strongly abolishes interaction with Rex and
FT RANBP3, abolishes Rex-mediated mRNA export."
FT /evidence="ECO:0000269|PubMed:14612415"
FT MUTAGEN 513
FT /note="E->A: Abolishes Ran binding activity and nuclear
FT export complex formation. Abolishes Ran binding activity
FT and nuclear export complex formation; when associated with
FT A-553 and A-554."
FT /evidence="ECO:0000269|PubMed:15574331"
FT MUTAGEN 525
FT /note="L->A: Enhances Ran binding activity and does not
FT abolish nuclear export complex formation. Does not abolish
FT Ran binding activity and partially abolish nuclear export
FT complex formation; when associated with A-561. Does not
FT abolish Ran binding activity and partially abolish nuclear
FT export complex formation; when associated with A-568 and A-
FT 572."
FT /evidence="ECO:0000269|PubMed:15574331"
FT MUTAGEN 550
FT /note="Q->A: Enhances Ran binding activity and does not
FT abolish nuclear export complex formation; when associated
FT with A-553 and A-590."
FT /evidence="ECO:0000269|PubMed:15574331"
FT MUTAGEN 553
FT /note="R->A: Enhances Ran binding activity and does not
FT abolish nuclear export complex formation; when associated
FT with A-550 and A-590. Abolishes Ran binding activity and
FT nuclear export complex formation; when associated with A-
FT 513 and A-554."
FT /evidence="ECO:0000269|PubMed:15574331"
FT MUTAGEN 554
FT /note="F->A: Partially abolishes Ran binding activity and
FT does not abolish nuclear export complex formation.
FT Abolishes Ran binding activity and nuclear export complex
FT formation; when associated with A-561. Abolishes Ran
FT binding activity and nuclear export complex formation; when
FT associated with A-553 and A-513."
FT /evidence="ECO:0000269|PubMed:15574331"
FT MUTAGEN 561
FT /note="F->A: Abolishes Ran binding activity and nuclear
FT export complex formation. Abolishes Ran binding activity
FT and nuclear export complex formation; when associated with
FT A-554. Does not abolish Ran binding activity and partially
FT abolish nuclear export complex formation; when associated
FT with A-525."
FT /evidence="ECO:0000269|PubMed:15574331"
FT MUTAGEN 568
FT /note="K->A: Does not abolish Ran binding activity and
FT partially abolish nuclear export complex formation; when
FT associated with A-525 and A-572."
FT /evidence="ECO:0000269|PubMed:15574331"
FT MUTAGEN 572
FT /note="F->A: Does not abolish Ran binding activity and
FT partially abolish nuclear export complex formation; when
FT associated with A-525 and A-568."
FT /evidence="ECO:0000269|PubMed:15574331"
FT MUTAGEN 583
FT /note="M->A: Enhances Ran binding activity; when associated
FT with A-590."
FT /evidence="ECO:0000269|PubMed:15574331"
FT MUTAGEN 590
FT /note="K->A: Enhances Ran binding activity and does not
FT abolish nuclear export complex formation. Enhances Ran
FT binding activity and does not abolish nuclear export
FT complex formation; when associated with A-583. Enhances Ran
FT binding activity and does not abolish nuclear export
FT complex formation; when associated with A-550 and A-553."
FT /evidence="ECO:0000269|PubMed:15574331"
FT CONFLICT 406
FT /note="R -> G (in Ref. 4; CAH56174)"
FT /evidence="ECO:0000305"
FT CONFLICT 953
FT /note="V -> G (in Ref. 4; CAH18695)"
FT /evidence="ECO:0000305"
FT CONFLICT 989
FT /note="L -> I (in Ref. 4; CAH56174)"
FT /evidence="ECO:0000305"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:7B51"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 40..55
FT /evidence="ECO:0007829|PDB:7B51"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6TVO"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 73..90
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 96..115
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 124..145
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 161..179
FT /evidence="ECO:0007829|PDB:7B51"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 202..215
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 219..232
FT /evidence="ECO:0007829|PDB:7B51"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:7B51"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:7B51"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:5DIS"
FT HELIX 280..297
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 313..338
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 344..357
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 363..383
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:7B51"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 413..423
FT /evidence="ECO:0007829|PDB:7B51"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:7B51"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:7B51"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 449..467
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 469..484
FT /evidence="ECO:0007829|PDB:7B51"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:3GB8"
FT HELIX 491..503
FT /evidence="ECO:0007829|PDB:7B51"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 510..530
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 534..549
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 552..557
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 559..572
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 580..595
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 596..599
FT /evidence="ECO:0007829|PDB:7B51"
FT STRAND 605..608
FT /evidence="ECO:0007829|PDB:3GB8"
FT HELIX 610..615
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 618..621
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 627..642
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 647..657
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 659..674
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 676..680
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 682..702
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:7B51"
FT HELIX 711..713
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 714..735
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 738..741
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 743..764
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 769..775
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 777..789
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 793..795
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 799..811
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 812..818
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 819..834
FT /evidence="ECO:0007829|PDB:1W9C"
FT TURN 837..839
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 842..858
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 862..865
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 868..881
FT /evidence="ECO:0007829|PDB:1W9C"
FT STRAND 884..886
FT /evidence="ECO:0007829|PDB:3GB8"
FT HELIX 887..906
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 908..931
FT /evidence="ECO:0007829|PDB:1W9C"
FT STRAND 932..934
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 936..938
FT /evidence="ECO:0007829|PDB:6TVO"
FT HELIX 939..954
FT /evidence="ECO:0007829|PDB:1W9C"
FT STRAND 961..963
FT /evidence="ECO:0007829|PDB:5DIS"
FT STRAND 964..966
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 970..985
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 991..1003
FT /evidence="ECO:0007829|PDB:1W9C"
FT TURN 1004..1006
FT /evidence="ECO:0007829|PDB:1W9C"
FT HELIX 1008..1023
FT /evidence="ECO:0007829|PDB:1W9C"
FT TURN 1024..1026
FT /evidence="ECO:0007829|PDB:1W9C"
FT TURN 1028..1030
FT /evidence="ECO:0007829|PDB:3GB8"
FT HELIX 1035..1047
FT /evidence="ECO:0007829|PDB:5DIS"
FT HELIX 1053..1055
FT /evidence="ECO:0007829|PDB:3GB8"
SQ SEQUENCE 1071 AA; 123386 MW; FDB00C065DA2FB1D CRC64;
MPAIMTMLAD HAARQLLDFS QKLDINLLDN VVNCLYHGEG AQQRMAQEVL THLKEHPDAW
TRVDTILEFS QNMNTKYYGL QILENVIKTR WKILPRNQCE GIKKYVVGLI IKTSSDPTCV
EKEKVYIGKL NMILVQILKQ EWPKHWPTFI SDIVGASRTS ESLCQNNMVI LKLLSEEVFD
FSSGQITQVK SKHLKDSMCN EFSQIFQLCQ FVMENSQNAP LVHATLETLL RFLNWIPLGY
IFETKLISTL IYKFLNVPMF RNVSLKCLTE IAGVSVSQYE EQFVTLFTLT MMQLKQMLPL
NTNIRLAYSN GKDDEQNFIQ NLSLFLCTFL KEHDQLIEKR LNLRETLMEA LHYMLLVSEV
EETEIFKICL EYWNHLAAEL YRESPFSTSA SPLLSGSQHF DVPPRRQLYL PMLFKVRLLM
VSRMAKPEEV LVVENDQGEV VREFMKDTDS INLYKNMRET LVYLTHLDYV DTERIMTEKL
HNQVNGTEWS WKNLNTLCWA IGSISGAMHE EDEKRFLVTV IKDLLGLCEQ KRGKDNKAII
ASNIMYIVGQ YPRFLRAHWK FLKTVVNKLF EFMHETHDGV QDMACDTFIK IAQKCRRHFV
QVQVGEVMPF IDEILNNINT IICDLQPQQV HTFYEAVGYM IGAQTDQTVQ EHLIEKYMLL
PNQVWDSIIQ QATKNVDILK DPETVKQLGS ILKTNVRACK AVGHPFVIQL GRIYLDMLNV
YKCLSENISA AIQANGEMVT KQPLIRSMRT VKRETLKLIS GWVSRSNDPQ MVAENFVPPL
LDAVLIDYQR NVPAAREPEV LSTMAIIVNK LGGHITAEIP QIFDAVFECT LNMINKDFEE
YPEHRTNFFL LLQAVNSHCF PAFLAIPPTQ FKLVLDSIIW AFKHTMRNVA DTGLQILFTL
LQNVAQEEAA AQSFYQTYFC DILQHIFSVV TDTSHTAGLT MHASILAYMF NLVEEGKIST
SLNPGNPVNN QIFLQEYVAN LLKSAFPHLQ DAQVKLFVTG LFSLNQDIPA FKEHLRDFLV
QIKEFAGEDT SDLFLEEREI ALRQADEEKH KRQMSVPGIF NPHEIPEEMC D
