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 27-MAR-2024, entry version 219. 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 INTERACTION WITH LRPPRC. RX PubMed=28325843; DOI=10.1261/rna.060137.116; RA Volpon L., Culjkovic-Kraljacic B., Sohn H.S., Blanchet-Cohen A., RA Osborne M.J., Borden K.L.B.; RT "A biochemical framework for eIF4E-dependent mRNA export and nuclear RT recycling of the export machinery."; RL RNA 23:927-937(2017). RN [50] 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 Interacts with LRPPRC; interacts with LRPPRC alone and also when LRPPRC CC is in complex with EIF4E and with EIF4E sensitivity element (4ESE)- CC containing mRNAs to form an EIF4E-dependent mRNA export complex CC (PubMed:28325843). {ECO:0000250|UniProtKB:Q6P5F9, CC ECO:0000269|PubMed:10209022, ECO:0000269|PubMed:10358091, CC ECO:0000269|PubMed:11425870, ECO:0000269|PubMed:11571268, CC ECO:0000269|PubMed:11932251, ECO:0000269|PubMed:12724356, CC ECO:0000269|PubMed:12808100, ECO:0000269|PubMed:14612415, CC ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:15574331, CC ECO:0000269|PubMed:16103875, ECO:0000269|PubMed:16302269, CC ECO:0000269|PubMed:18316374, ECO:0000269|PubMed:20826784, CC ECO:0000269|PubMed:20921223, ECO:0000269|PubMed:22022502, CC ECO:0000269|PubMed:22084111, ECO:0000269|PubMed:22275354, CC ECO:0000269|PubMed:22500989, ECO:0000269|PubMed:22730302, CC ECO:0000269|PubMed:23164465, ECO:0000269|PubMed:28325843, 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=3; IntAct=EBI-355867, EBI-641062; CC O14980; P22736: NR4A1; NbExp=2; IntAct=EBI-355867, EBI-721550; CC O14980; P35232: PHB1; 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="https://atlasgeneticsoncology.org/gene/44168/XPO1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 EMDB; EMD-6231; -. DR SMR; O14980; -. DR BioGRID; 113348; 1514. DR CORUM; O14980; -. DR DIP; DIP-33678N; -. DR IntAct; O14980; 139. 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; 9606-ENSP00000384863; -. DR PeptideAtlas; O14980; -. DR ProteomicsDB; 48356; -. DR Pumba; O14980; -. DR Antibodypedia; 4124; 425 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 AGR; HGNC:12825; -. 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; WAFKHNN; -. DR OrthoDB; 169519at2759; -. 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 Reactome; R-HSA-9768919; NPAS4 regulates expression of target genes. DR SignaLink; O14980; -. DR SIGNOR; O14980; -. DR BioGRID-ORCS; 7514; 740 hits in 1180 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 214 other cell types or tissues. DR ExpressionAtlas; O14980; baseline and differential. 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:0006406; P:mRNA export from nucleus; ISS:UniProt. 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; Leucine-rich Repeat Variant; 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; EXPORTIN 1/5; 1. DR PANTHER; PTHR11223:SF2; EXPORTIN-1; 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; ARM repeat; 2. DR PROSITE; PS50166; IMPORTIN_B_NT; 1. DR Genevisible; O14980; HS. 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 FT S-414. Abolishes Rex multimerization; when associated with FT S-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 FT T-411. Abolishes Rex multimerization; when associated with FT T-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 FT A-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 FT A-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 //