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Exportin-2 (Exp2) (Cellular apoptosis susceptibility protein) (Chromosome segregation 1-like protein) (Importin-alpha re-exporter)

 XPO2_HUMAN              Reviewed;         971 AA.
P55060; A3RLL6; B2R5T4; E1P5Y0; F8W904; O75432; Q32M40; Q9H5B7;
Q9NTS0; Q9UP98; Q9UP99; Q9UPA0;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
29-MAR-2005, sequence version 3.
30-AUG-2017, entry version 168.
RecName: Full=Exportin-2;
Short=Exp2;
AltName: Full=Cellular apoptosis susceptibility protein {ECO:0000303|PubMed:7479798};
AltName: Full=Chromosome segregation 1-like protein;
AltName: Full=Importin-alpha re-exporter;
Name=CSE1L; Synonyms=CAS {ECO:0000303|PubMed:7479798}, XPO2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=7479798; DOI=10.1073/pnas.92.22.10427;
Brinkmann U., Brinkmann E., Gallo M., Pastan I.;
"Cloning and characterization of a cellular apoptosis susceptibility
gene, the human homologue to the yeast chromosome segregation gene
CSE1.";
Proc. Natl. Acad. Sci. U.S.A. 92:10427-10431(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), AND
TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=10331944; DOI=10.1006/geno.1998.5700;
Brinkmann U., Brinkmann E., Bera T.K., Wellmann A., Pastan I.;
"Tissue-specific alternative splicing of the CSE1L/CAS (cellular
apoptosis susceptibility) gene.";
Genomics 58:41-49(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=11703094; DOI=10.1006/mcbr.2001.0303;
Jiang M.C., Lin T.L., Lee T.L., Huang H.T., Lin C.L., Liao C.F.;
"IRF-1-mediated CAS expression enhances interferon-gamma-induced
apoptosis of HT-29 colon adenocarcinoma cells.";
Mol. Cell Biol. Res. Commun. 4:353-358(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 1-16; 18-26; 32-67; 76-83; 94-109; 138-151;
166-217; 252-268; 282-288; 293-309; 332-371; 373-382; 396-418;
428-440; 446-481; 560-574; 698-736; 769-777; 789-816; 825-832 AND
913-934, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUN-2005) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 356-370, FUNCTION IN PROTEIN NUCLEAR EXPORT,
IDENTIFICATION IN A COMPLEX WITH RAN AND KPNA2, AND SUBCELLULAR
LOCATION.
PubMed=9323134; DOI=10.1016/S0092-8674(00)80372-4;
Kutay U., Bischoff F.R., Kostka S., Kraft R., Goerlich D.;
"Export of importin-alpha from the nucleus is mediated by a specific
nuclear transport factor.";
Cell 90:1061-1071(1997).
[10]
INTERACTION WITH KPNA2.
PubMed=9786944; DOI=10.1083/jcb.143.2.309;
Herold A., Truant R., Wiegand H., Cullen B.R.;
"Determination of the functional domain organization of the importin
alpha nuclear import factor.";
J. Cell Biol. 143:309-318(1998).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-574 AND LYS-824, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
INTERACTION WITH CFTR.
PubMed=20933420; DOI=10.1016/j.cub.2010.09.012;
Bagnat M., Navis A., Herbstreith S., Brand-Arzamendi K., Curado S.,
Gabriel S., Mostov K., Huisken J., Stainier D.Y.;
"Cse1l is a negative regulator of CFTR-dependent fluid secretion.";
Curr. Biol. 20:1840-1845(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND SER-931, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-931, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
VARIANT [LARGE SCALE ANALYSIS] PHE-842.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Export receptor for importin-alpha. Mediates importin-
alpha re-export from the nucleus to the cytoplasm after import
substrates (cargos) have been released into the nucleoplasm. In
the nucleus binds cooperatively to importin-alpha and to the
GTPase Ran in its active GTP-bound form. Docking of this trimeric
complex to the nuclear pore complex (NPC) is mediated through
binding to nucleoporins. Upon transit of a nuclear export complex
into the cytoplasm, disassembling of the complex and hydrolysis of
Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively)
cause release of the importin-alpha from the export receptor.
CSE1L/XPO2 then return to the nuclear compartment and mediate
another round of transport. The directionality of nuclear export
is thought to be conferred by an asymmetric distribution of the
GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
{ECO:0000269|PubMed:9323134}.
-!- SUBUNIT: Found in a complex with CSE1L/XPO2, Ran and KPNA2
(PubMed:9323134, PubMed:9786944). Binds with high affinity to
importin-alpha only in the presence of RanGTP. The complex is
dissociated by the combined action of RanBP1 and RanGAP1
(PubMed:9323134). Interacts with CFTR (PubMed:20933420).
{ECO:0000269|PubMed:20933420, ECO:0000269|PubMed:9323134,
ECO:0000269|PubMed:9786944}.
-!- INTERACTION:
P04637:TP53; NbExp=5; IntAct=EBI-286709, EBI-366083;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9323134}.
Nucleus {ECO:0000269|PubMed:9323134}. Note=Shuttles between the
nucleus and the cytoplasm. {ECO:0000269|PubMed:9323134}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=A;
IsoId=P55060-1; Sequence=Displayed;
Name=2;
IsoId=P55060-2; Sequence=VSP_001222, VSP_001223;
Name=3;
IsoId=P55060-3; Sequence=VSP_001224, VSP_001225;
Name=4;
IsoId=P55060-4; Sequence=VSP_047203;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in brain, placenta, ovary, testis and
trachea (at protein level) (PubMed:10331944). Widely expressed
(PubMed:10331944). Highly expressed in testis and in proliferating
cells (PubMed:7479798,PubMed:10331944).
{ECO:0000269|PubMed:10331944, ECO:0000269|PubMed:7479798}.
-!- SIMILARITY: Belongs to the XPO2/CSE1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CSE1LID40159ch20q13.html";
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EMBL; U33286; AAC50367.1; -; mRNA.
EMBL; AF053640; AAC35007.1; -; mRNA.
EMBL; AF053641; AAC35008.1; -; mRNA.
EMBL; AF053642; AAC35009.1; -; mRNA.
EMBL; AF053651; AAC35297.1; -; Genomic_DNA.
EMBL; AF053644; AAC35297.1; JOINED; Genomic_DNA.
EMBL; AF053645; AAC35297.1; JOINED; Genomic_DNA.
EMBL; AF053646; AAC35297.1; JOINED; Genomic_DNA.
EMBL; AF053647; AAC35297.1; JOINED; Genomic_DNA.
EMBL; AF053648; AAC35297.1; JOINED; Genomic_DNA.
EMBL; AF053649; AAC35297.1; JOINED; Genomic_DNA.
EMBL; AF053650; AAC35297.1; JOINED; Genomic_DNA.
EMBL; EF426455; ABO15009.1; -; mRNA.
EMBL; AK312306; BAG35231.1; -; mRNA.
EMBL; AL121903; CAI19615.1; -; Genomic_DNA.
EMBL; AL133174; CAI19615.1; JOINED; Genomic_DNA.
EMBL; AL133174; CAI42818.1; -; Genomic_DNA.
EMBL; AL121903; CAI42818.1; JOINED; Genomic_DNA.
EMBL; CH471077; EAW75676.1; -; Genomic_DNA.
EMBL; CH471077; EAW75677.1; -; Genomic_DNA.
EMBL; BC108309; AAI08310.1; -; mRNA.
EMBL; BC109313; AAI09314.1; -; mRNA.
EMBL; BC109314; AAI09315.1; -; mRNA.
CCDS; CCDS13412.1; -. [P55060-1]
CCDS; CCDS58773.1; -. [P55060-4]
PIR; I39166; I39166.
RefSeq; NP_001243064.1; NM_001256135.1. [P55060-4]
RefSeq; NP_001307.2; NM_001316.3. [P55060-1]
RefSeq; XP_011526901.1; XM_011528599.2. [P55060-3]
UniGene; Hs.90073; -.
ProteinModelPortal; P55060; -.
SMR; P55060; -.
BioGrid; 107821; 116.
DIP; DIP-32573N; -.
IntAct; P55060; 41.
MINT; MINT-5001090; -.
STRING; 9606.ENSP00000262982; -.
TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
iPTMnet; P55060; -.
PhosphoSitePlus; P55060; -.
SwissPalm; P55060; -.
BioMuta; CSE1L; -.
DMDM; 62297557; -.
EPD; P55060; -.
MaxQB; P55060; -.
PaxDb; P55060; -.
PeptideAtlas; P55060; -.
PRIDE; P55060; -.
DNASU; 1434; -.
Ensembl; ENST00000262982; ENSP00000262982; ENSG00000124207. [P55060-1]
Ensembl; ENST00000396192; ENSP00000379495; ENSG00000124207. [P55060-4]
GeneID; 1434; -.
KEGG; hsa:1434; -.
UCSC; uc002xty.5; human. [P55060-1]
CTD; 1434; -.
DisGeNET; 1434; -.
GeneCards; CSE1L; -.
HGNC; HGNC:2431; CSE1L.
HPA; CAB002140; -.
HPA; HPA038059; -.
HPA; HPA038060; -.
MIM; 601342; gene.
neXtProt; NX_P55060; -.
OpenTargets; ENSG00000124207; -.
PharmGKB; PA26933; -.
eggNOG; KOG1992; Eukaryota.
eggNOG; COG5657; LUCA.
GeneTree; ENSGT00550000074884; -.
HOVERGEN; HBG080050; -.
InParanoid; P55060; -.
KO; K18423; -.
OMA; FMPYVFQ; -.
OrthoDB; EOG091G01TH; -.
PhylomeDB; P55060; -.
TreeFam; TF300473; -.
ChiTaRS; CSE1L; human.
GenomeRNAi; 1434; -.
PRO; PR:P55060; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000124207; -.
CleanEx; HS_CSE1L; -.
Genevisible; P55060; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0005049; F:nuclear export signal receptor activity; TAS:ProtInc.
GO; GO:0008536; F:Ran GTPase binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR005043; CAS_CSE1_C.
InterPro; IPR013713; Cse1.
InterPro; IPR001494; Importin-beta_N.
Pfam; PF03378; CAS_CSE1; 1.
Pfam; PF08506; Cse1; 1.
Pfam; PF03810; IBN_N; 1.
SMART; SM00913; IBN_N; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS50166; IMPORTIN_B_NT; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; Transport.
CHAIN 1 971 Exportin-2.
/FTId=PRO_0000117287.
DOMAIN 29 102 Importin N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00115}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 574 574 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 824 824 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 931 931 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 190 195 ATIELC -> VWNASW (in isoform 2).
{ECO:0000303|PubMed:10331944}.
/FTId=VSP_001222.
VAR_SEQ 196 971 Missing (in isoform 2).
{ECO:0000303|PubMed:10331944}.
/FTId=VSP_001223.
VAR_SEQ 257 312 Missing (in isoform 4).
{ECO:0000303|PubMed:11703094}.
/FTId=VSP_047203.
VAR_SEQ 943 945 VPS -> TYF (in isoform 3).
{ECO:0000303|PubMed:10331944}.
/FTId=VSP_001224.
VAR_SEQ 946 971 Missing (in isoform 3).
{ECO:0000303|PubMed:10331944}.
/FTId=VSP_001225.
VARIANT 754 754 I -> V (in dbSNP:rs2229042).
/FTId=VAR_029327.
VARIANT 842 842 C -> F (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036558.
VARIANT 968 968 V -> L (in dbSNP:rs3505).
/FTId=VAR_048836.
CONFLICT 231 233 FED -> WEG (in Ref. 1; AAC50367 and 2;
AAC35008). {ECO:0000305}.
CONFLICT 514 514 E -> G (in Ref. 1; AAC50367 and 2;
AAC35008). {ECO:0000305}.
CONFLICT 538 538 A -> T (in Ref. 3; ABO15009).
{ECO:0000305}.
CONFLICT 848 848 K -> N (in Ref. 1; AAC50367).
{ECO:0000305}.
CONFLICT 934 934 K -> M (in Ref. 1; AAC50367).
{ECO:0000305}.
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


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