ID XPO2_HUMAN Reviewed; 971 AA. AC P55060; A3RLL6; B2R5T4; E1P5Y0; F8W904; O75432; Q32M40; Q9H5B7; Q9NTS0; AC Q9UP98; Q9UP99; Q9UPA0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 3. DT 27-MAR-2024, entry version 211. DE RecName: Full=Exportin-2; DE Short=Exp2; DE AltName: Full=Cellular apoptosis susceptibility protein {ECO:0000303|PubMed:7479798}; DE AltName: Full=Chromosome segregation 1-like protein; DE AltName: Full=Importin-alpha re-exporter; GN Name=CSE1L; Synonyms=CAS {ECO:0000303|PubMed:7479798}, XPO2; 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] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Placenta; RX PubMed=7479798; DOI=10.1073/pnas.92.22.10427; RA Brinkmann U., Brinkmann E., Gallo M., Pastan I.; RT "Cloning and characterization of a cellular apoptosis susceptibility gene, RT the human homologue to the yeast chromosome segregation gene CSE1."; RL Proc. Natl. Acad. Sci. U.S.A. 92:10427-10431(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=10331944; DOI=10.1006/geno.1998.5700; RA Brinkmann U., Brinkmann E., Bera T.K., Wellmann A., Pastan I.; RT "Tissue-specific alternative splicing of the CSE1L/CAS (cellular apoptosis RT susceptibility) gene."; RL Genomics 58:41-49(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). RX PubMed=11703094; DOI=10.1006/mcbr.2001.0303; RA Jiang M.C., Lin T.L., Lee T.L., Huang H.T., Lin C.L., Liao C.F.; RT "IRF-1-mediated CAS expression enhances interferon-gamma-induced apoptosis RT of HT-29 colon adenocarcinoma cells."; RL Mol. Cell Biol. Res. Commun. 4:353-358(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cerebellum; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). 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] (ISOFORM 1). 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 1-16; 18-26; 32-67; 76-83; 94-109; 138-151; 166-217; RP 252-268; 282-288; 293-309; 332-371; 373-382; 396-418; 428-440; 446-481; RP 560-574; 698-736; 769-777; 789-816; 825-832 AND 913-934, ACETYLATION AT RP MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (JUN-2005) to UniProtKB. RN [9] RP PROTEIN SEQUENCE OF 356-370, FUNCTION IN PROTEIN NUCLEAR EXPORT, RP IDENTIFICATION IN A COMPLEX WITH RAN AND KPNA2, AND SUBCELLULAR LOCATION. RX PubMed=9323134; DOI=10.1016/s0092-8674(00)80372-4; RA Kutay U., Bischoff F.R., Kostka S., Kraft R., Goerlich D.; RT "Export of importin-alpha from the nucleus is mediated by a specific RT nuclear transport factor."; RL Cell 90:1061-1071(1997). RN [10] RP INTERACTION WITH KPNA2. RX PubMed=9786944; DOI=10.1083/jcb.143.2.309; RA Herold A., Truant R., Wiegand H., Cullen B.R.; RT "Determination of the functional domain organization of the importin alpha RT nuclear import factor."; RL J. Cell Biol. 143:309-318(1998). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-574 AND LYS-824, 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 [14] RP INTERACTION WITH CFTR. RX PubMed=20933420; DOI=10.1016/j.cub.2010.09.012; RA Bagnat M., Navis A., Herbstreith S., Brand-Arzamendi K., Curado S., RA Gabriel S., Mostov K., Huisken J., Stainier D.Y.; RT "Cse1l is a negative regulator of CFTR-dependent fluid secretion."; RL Curr. Biol. 20:1840-1845(2010). RN [15] 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 [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND SER-931, 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-931, AND IDENTIFICATION BY RP 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 [20] 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 [21] RP VARIANT [LARGE SCALE ANALYSIS] PHE-842. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Export receptor for importin-alpha. Mediates importin-alpha CC re-export from the nucleus to the cytoplasm after import substrates CC (cargos) have been released into the nucleoplasm. In the nucleus binds CC cooperatively to importin-alpha and to the GTPase Ran in its active CC GTP-bound form. Docking of this trimeric complex to the nuclear pore CC complex (NPC) is mediated through binding to nucleoporins. Upon transit CC of a nuclear export complex into the cytoplasm, disassembling of the CC complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and CC RANGAP1, respectively) cause release of the importin-alpha from the CC export receptor. CSE1L/XPO2 then return to the nuclear compartment and CC mediate another round of transport. The directionality of nuclear CC export is thought to be conferred by an asymmetric distribution of the CC GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. CC {ECO:0000269|PubMed:9323134}. CC -!- SUBUNIT: Found in a complex with CSE1L/XPO2, Ran and KPNA2 CC (PubMed:9323134, PubMed:9786944). Binds with high affinity to importin- CC alpha only in the presence of RanGTP. The complex is dissociated by the CC combined action of RanBP1 and RanGAP1 (PubMed:9323134). Interacts with CC CFTR (PubMed:20933420). {ECO:0000269|PubMed:20933420, CC ECO:0000269|PubMed:9323134, ECO:0000269|PubMed:9786944}. CC -!- INTERACTION: CC P55060; Q96JQ5: MS4A4A; NbExp=2; IntAct=EBI-286709, EBI-12820341; CC P55060; Q15077: P2RY6; NbExp=2; IntAct=EBI-286709, EBI-10235794; CC P55060; Q9Y275: TNFSF13B; NbExp=2; IntAct=EBI-286709, EBI-519169; CC P55060; P04637: TP53; NbExp=5; IntAct=EBI-286709, EBI-366083; CC P55060; Q9H1C4: UNC93B1; NbExp=2; IntAct=EBI-286709, EBI-4401271; CC P55060; Q9BTM9: URM1; NbExp=2; IntAct=EBI-286709, EBI-714589; CC P55060; O95183: VAMP5; NbExp=2; IntAct=EBI-286709, EBI-10191195; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9323134}. Nucleus CC {ECO:0000269|PubMed:9323134}. Note=Shuttles between the nucleus and the CC cytoplasm. {ECO:0000269|PubMed:9323134}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=A; CC IsoId=P55060-1; Sequence=Displayed; CC Name=2; CC IsoId=P55060-2; Sequence=VSP_001222, VSP_001223; CC Name=3; CC IsoId=P55060-3; Sequence=VSP_001224, VSP_001225; CC Name=4; CC IsoId=P55060-4; Sequence=VSP_047203; CC -!- TISSUE SPECIFICITY: Detected in brain, placenta, ovary, testis and CC trachea (at protein level) (PubMed:10331944). Widely expressed CC (PubMed:10331944). Highly expressed in testis and in proliferating CC cells (PubMed:7479798, PubMed:10331944). {ECO:0000269|PubMed:10331944, CC ECO:0000269|PubMed:7479798}. CC -!- SIMILARITY: Belongs to the XPO2/CSE1 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40159/CSE1L"; 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; U33286; AAC50367.1; -; mRNA. DR EMBL; AF053640; AAC35007.1; -; mRNA. DR EMBL; AF053641; AAC35008.1; -; mRNA. DR EMBL; AF053642; AAC35009.1; -; mRNA. DR EMBL; AF053651; AAC35297.1; -; Genomic_DNA. DR EMBL; AF053644; AAC35297.1; JOINED; Genomic_DNA. DR EMBL; AF053645; AAC35297.1; JOINED; Genomic_DNA. DR EMBL; AF053646; AAC35297.1; JOINED; Genomic_DNA. DR EMBL; AF053647; AAC35297.1; JOINED; Genomic_DNA. DR EMBL; AF053648; AAC35297.1; JOINED; Genomic_DNA. DR EMBL; AF053649; AAC35297.1; JOINED; Genomic_DNA. DR EMBL; AF053650; AAC35297.1; JOINED; Genomic_DNA. DR EMBL; EF426455; ABO15009.1; -; mRNA. DR EMBL; AK312306; BAG35231.1; -; mRNA. DR EMBL; AL121903; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133174; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW75676.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75677.1; -; Genomic_DNA. DR EMBL; BC108309; AAI08310.1; -; mRNA. DR EMBL; BC109313; AAI09314.1; -; mRNA. DR EMBL; BC109314; AAI09315.1; -; mRNA. DR CCDS; CCDS13412.1; -. [P55060-1] DR CCDS; CCDS58773.1; -. [P55060-4] DR PIR; I39166; I39166. DR RefSeq; NP_001243064.1; NM_001256135.1. [P55060-4] DR RefSeq; NP_001307.2; NM_001316.3. [P55060-1] DR RefSeq; XP_011526901.1; XM_011528599.2. DR AlphaFoldDB; P55060; -. DR SMR; P55060; -. DR BioGRID; 107821; 306. DR CORUM; P55060; -. DR DIP; DIP-32573N; -. DR IntAct; P55060; 77. DR MINT; P55060; -. DR STRING; 9606.ENSP00000262982; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR GlyGen; P55060; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P55060; -. DR MetOSite; P55060; -. DR PhosphoSitePlus; P55060; -. DR SwissPalm; P55060; -. DR BioMuta; CSE1L; -. DR DMDM; 62297557; -. DR EPD; P55060; -. DR jPOST; P55060; -. DR MassIVE; P55060; -. DR MaxQB; P55060; -. DR PaxDb; 9606-ENSP00000262982; -. DR PeptideAtlas; P55060; -. DR ProteomicsDB; 30232; -. DR ProteomicsDB; 56771; -. [P55060-1] DR ProteomicsDB; 56772; -. [P55060-2] DR ProteomicsDB; 56773; -. [P55060-3] DR Pumba; P55060; -. DR Antibodypedia; 28372; 611 antibodies from 40 providers. DR DNASU; 1434; -. DR Ensembl; ENST00000262982.3; ENSP00000262982.2; ENSG00000124207.17. [P55060-1] DR Ensembl; ENST00000396192.7; ENSP00000379495.3; ENSG00000124207.17. [P55060-4] DR GeneID; 1434; -. DR KEGG; hsa:1434; -. DR MANE-Select; ENST00000262982.3; ENSP00000262982.2; NM_001316.4; NP_001307.2. DR UCSC; uc002xty.5; human. [P55060-1] DR AGR; HGNC:2431; -. DR CTD; 1434; -. DR DisGeNET; 1434; -. DR GeneCards; CSE1L; -. DR HGNC; HGNC:2431; CSE1L. DR HPA; ENSG00000124207; Low tissue specificity. DR MIM; 601342; gene. DR neXtProt; NX_P55060; -. DR OpenTargets; ENSG00000124207; -. DR PharmGKB; PA26933; -. DR VEuPathDB; HostDB:ENSG00000124207; -. DR eggNOG; KOG1992; Eukaryota. DR GeneTree; ENSGT00550000074884; -. DR HOGENOM; CLU_009614_0_0_1; -. DR InParanoid; P55060; -. DR OMA; AENEFLM; -. DR OrthoDB; 178772at2759; -. DR PhylomeDB; P55060; -. DR TreeFam; TF300473; -. DR PathwayCommons; P55060; -. DR SignaLink; P55060; -. DR SIGNOR; P55060; -. DR BioGRID-ORCS; 1434; 836 hits in 1166 CRISPR screens. DR ChiTaRS; CSE1L; human. DR GenomeRNAi; 1434; -. DR Pharos; P55060; Tbio. DR PRO; PR:P55060; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; P55060; Protein. DR Bgee; ENSG00000124207; Expressed in primordial germ cell in gonad and 219 other cell types or tissues. DR ExpressionAtlas; P55060; baseline and differential. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0005049; F:nuclear export signal receptor activity; IBA:GO_Central. DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro. DR GO; GO:0006611; P:protein export from nucleus; IBA:GO_Central. DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR001494; Importin-beta_N. DR InterPro; IPR005043; XPO2_C. DR InterPro; IPR013713; XPO2_central. DR PANTHER; PTHR10997:SF8; EXPORTIN-2; 1. DR PANTHER; PTHR10997; IMPORTIN-7, 8, 11; 1. DR Pfam; PF03378; CAS_CSE1; 1. DR Pfam; PF08506; Cse1; 1. DR Pfam; PF03810; IBN_N; 1. DR SMART; SM00913; IBN_N; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS50166; IMPORTIN_B_NT; 1. DR Genevisible; P55060; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing; KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Transport. FT CHAIN 1..971 FT /note="Exportin-2" FT /id="PRO_0000117287" FT DOMAIN 29..102 FT /note="Importin N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 112 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 574 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 824 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 931 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 190..195 FT /note="ATIELC -> VWNASW (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10331944" FT /id="VSP_001222" FT VAR_SEQ 196..971 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10331944" FT /id="VSP_001223" FT VAR_SEQ 257..312 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11703094" FT /id="VSP_047203" FT VAR_SEQ 943..945 FT /note="VPS -> TYF (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10331944" FT /id="VSP_001224" FT VAR_SEQ 946..971 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10331944" FT /id="VSP_001225" FT VARIANT 754 FT /note="I -> V (in dbSNP:rs2229042)" FT /id="VAR_029327" FT VARIANT 842 FT /note="C -> F (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036558" FT VARIANT 968 FT /note="V -> L (in dbSNP:rs3505)" FT /id="VAR_048836" FT CONFLICT 231..233 FT /note="FED -> WEG (in Ref. 1; AAC50367 and 2; AAC35008)" FT /evidence="ECO:0000305" FT CONFLICT 514 FT /note="E -> G (in Ref. 1; AAC50367 and 2; AAC35008)" FT /evidence="ECO:0000305" FT CONFLICT 538 FT /note="A -> T (in Ref. 3; ABO15009)" FT /evidence="ECO:0000305" FT CONFLICT 848 FT /note="K -> N (in Ref. 1; AAC50367)" FT /evidence="ECO:0000305" FT CONFLICT 934 FT /note="K -> M (in Ref. 1; AAC50367)" FT /evidence="ECO:0000305" SQ SEQUENCE 971 AA; 110417 MW; 08E837AB5008EBFD CRC64; MELSDANLQT LTEYLKKTLD PDPAIRRPAE KFLESVEGNQ NYPLLLLTLL EKSQDNVIKV CASVTFKNYI KRNWRIVEDE PNKICEADRV AIKANIVHLM LSSPEQIQKQ LSDAISIIGR EDFPQKWPDL LTEMVNRFQS GDFHVINGVL RTAHSLFKRY RHEFKSNELW TEIKLVLDAF ALPLTNLFKA TIELCSTHAN DASALRILFS SLILISKLFY SLNFQDLPEF FEDNMETWMN NFHTLLTLDN KLLQTDDEEE AGLLELLKSQ ICDNAALYAQ KYDEEFQRYL PRFVTAIWNL LVTTGQEVKY DLLVSNAIQF LASVCERPHY KNLFEDQNTL TSICEKVIVP NMEFRAADEE AFEDNSEEYI RRDLEGSDID TRRRAACDLV RGLCKFFEGP VTGIFSGYVN SMLQEYAKNP SVNWKHKDAA IYLVTSLASK AQTQKHGITQ ANELVNLTEF FVNHILPDLK SANVNEFPVL KADGIKYIMI FRNQVPKEHL LVSIPLLINH LQAESIVVHT YAAHALERLF TMRGPNNATL FTAAEIAPFV EILLTNLFKA LTLPGSSENE YIMKAIMRSF SLLQEAIIPY IPTLITQLTQ KLLAVSKNPS KPHFNHYMFE AICLSIRITC KANPAAVVNF EEALFLVFTE ILQNDVQEFI PYVFQVMSLL LETHKNDIPS SYMALFPHLL QPVLWERTGN IPALVRLLQA FLERGSNTIA SAAADKIPGL LGVFQKLIAS KANDHQGFYL LNSIIEHMPP ESVDQYRKQI FILLFQRLQN SKTTKFIKSF LVFINLYCIK YGALALQEIF DGIQPKMFGM VLEKIIIPEI QKVSGNVEKK ICAVGITKLL TECPPMMDTE YTKLWTPLLQ SLIGLFELPE DDTIPDEEHF IDIEDTPGYQ TAFSQLAFAG KKEHDPVGQM VNNPKIHLAQ SLHKLSTACP GRVPSMVSTS LNAEALQYLQ GYLQAASVTL L //