XPO2_HUMAN
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 03-AUG-2022, entry version 202.
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="http://atlasgeneticsoncology.org/Genes/CSE1LID40159ch20q13.html";
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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; 254.
DR CORUM; P55060; -.
DR DIP; DIP-32573N; -.
DR IntAct; P55060; 72.
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; P55060; -.
DR PeptideAtlas; P55060; -.
DR PRIDE; P55060; -.
DR ProteomicsDB; 30232; -.
DR ProteomicsDB; 56771; -. [P55060-1]
DR ProteomicsDB; 56772; -. [P55060-2]
DR ProteomicsDB; 56773; -. [P55060-3]
DR Antibodypedia; 28372; 553 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 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; YRYEFKS; -.
DR OrthoDB; 1248958at2759; -.
DR PhylomeDB; P55060; -.
DR TreeFam; TF300473; -.
DR PathwayCommons; P55060; -.
DR SignaLink; P55060; -.
DR BioGRID-ORCS; 1434; 802 hits in 1086 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 endothelial cell and 217 other tissues.
DR ExpressionAtlas; P55060; baseline and differential.
DR Genevisible; P55060; HS.
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; -; 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 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; SSF48371; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
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
