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XPO6_HUMAN
ID   XPO6_HUMAN              Reviewed;        1125 AA.
AC   Q96QU8; A1L3W4; D3DWF9; Q2YDX3; Q53G88; Q68G50; Q76N88; Q96CP8; Q9BT21;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Exportin-6;
DE            Short=Exp6;
DE   AltName: Full=Ran-binding protein 20;
GN   Name=XPO6; Synonyms=KIAA0370, RANBP20;
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), FUNCTION IN ACTIN AND
RP   PROFILIN-ACTIN COMPLEXES EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN; ACTB
RP   AND PFN1, AND INTERACTION WITH ACTB.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=14592989; DOI=10.1093/emboj/cdg565;
RA   Stueven T., Hartmann E., Goerlich D.;
RT   "Exportin 6: a novel nuclear export receptor that is specific for
RT   profilin.actin complexes.";
RL   EMBO J. 22:5928-5940(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA   Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VII. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 4:141-150(1997).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
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=Choriocarcinoma, Skin, and 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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 715-1125.
RC   TISSUE=Thyroid;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204 AND SER-224, AND
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   [11]
RP   IDENTIFICATION BY MASS 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201; THR-204 AND SER-224, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [13]
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   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204 AND SER-208, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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).
CC   -!- FUNCTION: Mediates the nuclear export of actin and profilin-actin
CC       complexes in somatic cells. {ECO:0000269|PubMed:14592989}.
CC   -!- SUBUNIT: Found in a complex with XPO6, Ran, ACTB and PFN1. Interacts
CC       with ACTB (PubMed:14592989). Interacts with ACTB in a RanGTP-dependent
CC       manner (PubMed:14592989). {ECO:0000269|PubMed:14592989}.
CC   -!- INTERACTION:
CC       Q96QU8; P37198: NUP62; NbExp=3; IntAct=EBI-1022896, EBI-347978;
CC       Q96QU8-2; P37198: NUP62; NbExp=3; IntAct=EBI-10293124, EBI-347978;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14592989}. Cytoplasm
CC       {ECO:0000269|PubMed:14592989}. Note=Shuttles between the nucleus and
CC       the cytoplasm. {ECO:0000269|PubMed:14592989}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96QU8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96QU8-2; Sequence=VSP_055756;
CC   -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA20825.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY026388; AAK01471.1; -; mRNA.
DR   EMBL; AB002368; BAA20825.3; ALT_INIT; mRNA.
DR   EMBL; AK123846; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC136611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471145; EAW55736.1; -; Genomic_DNA.
DR   EMBL; CH471145; EAW55738.1; -; Genomic_DNA.
DR   EMBL; CH471145; EAW55739.1; -; Genomic_DNA.
DR   EMBL; BC004403; AAH04403.1; -; mRNA.
DR   EMBL; BC014071; AAH14071.2; -; mRNA.
DR   EMBL; BC078674; AAH78674.1; -; mRNA.
DR   EMBL; BC108286; AAI08287.1; -; mRNA.
DR   EMBL; BC130304; AAI30305.1; -; mRNA.
DR   EMBL; AK223043; BAD96763.1; -; mRNA.
DR   CCDS; CCDS42135.1; -. [Q96QU8-1]
DR   CCDS; CCDS59266.1; -. [Q96QU8-2]
DR   RefSeq; NP_001257869.1; NM_001270940.1. [Q96QU8-2]
DR   RefSeq; NP_055986.1; NM_015171.3. [Q96QU8-1]
DR   AlphaFoldDB; Q96QU8; -.
DR   SMR; Q96QU8; -.
DR   BioGRID; 116821; 86.
DR   IntAct; Q96QU8; 23.
DR   MINT; Q96QU8; -.
DR   STRING; 9606.ENSP00000302790; -.
DR   CarbonylDB; Q96QU8; -.
DR   iPTMnet; Q96QU8; -.
DR   PhosphoSitePlus; Q96QU8; -.
DR   BioMuta; XPO6; -.
DR   DMDM; 74724278; -.
DR   EPD; Q96QU8; -.
DR   jPOST; Q96QU8; -.
DR   MassIVE; Q96QU8; -.
DR   MaxQB; Q96QU8; -.
DR   PaxDb; Q96QU8; -.
DR   PeptideAtlas; Q96QU8; -.
DR   PRIDE; Q96QU8; -.
DR   ProteomicsDB; 12772; -.
DR   ProteomicsDB; 77908; -. [Q96QU8-1]
DR   Antibodypedia; 26312; 65 antibodies from 19 providers.
DR   DNASU; 23214; -.
DR   Ensembl; ENST00000304658.10; ENSP00000302790.4; ENSG00000169180.12. [Q96QU8-1]
DR   Ensembl; ENST00000565698.5; ENSP00000457341.1; ENSG00000169180.12. [Q96QU8-2]
DR   GeneID; 23214; -.
DR   KEGG; hsa:23214; -.
DR   MANE-Select; ENST00000304658.10; ENSP00000302790.4; NM_015171.4; NP_055986.1.
DR   UCSC; uc002dpa.4; human. [Q96QU8-1]
DR   CTD; 23214; -.
DR   DisGeNET; 23214; -.
DR   GeneCards; XPO6; -.
DR   HGNC; HGNC:19733; XPO6.
DR   HPA; ENSG00000169180; Low tissue specificity.
DR   MIM; 608411; gene.
DR   neXtProt; NX_Q96QU8; -.
DR   OpenTargets; ENSG00000169180; -.
DR   PharmGKB; PA134989996; -.
DR   VEuPathDB; HostDB:ENSG00000169180; -.
DR   eggNOG; KOG2020; Eukaryota.
DR   GeneTree; ENSGT00390000002810; -.
DR   HOGENOM; CLU_004473_0_0_1; -.
DR   InParanoid; Q96QU8; -.
DR   OMA; DYQRRQW; -.
DR   OrthoDB; 214523at2759; -.
DR   PhylomeDB; Q96QU8; -.
DR   TreeFam; TF323443; -.
DR   PathwayCommons; Q96QU8; -.
DR   SignaLink; Q96QU8; -.
DR   BioGRID-ORCS; 23214; 27 hits in 1085 CRISPR screens.
DR   ChiTaRS; XPO6; human.
DR   GeneWiki; XPO6; -.
DR   GenomeRNAi; 23214; -.
DR   Pharos; Q96QU8; Tbio.
DR   PRO; PR:Q96QU8; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q96QU8; protein.
DR   Bgee; ENSG00000169180; Expressed in blood and 196 other tissues.
DR   ExpressionAtlas; Q96QU8; baseline and differential.
DR   Genevisible; Q96QU8; HS.
DR   GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR   GO; GO:0005049; F:nuclear export signal receptor activity; IDA:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR013598; Exportin-1/Importin-b-like.
DR   InterPro; IPR001494; Importin-beta_N.
DR   InterPro; IPR040016; XPO6.
DR   PANTHER; PTHR21452; PTHR21452; 1.
DR   Pfam; PF03810; IBN_N; 1.
DR   Pfam; PF08389; Xpo1; 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; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..1125
FT                   /note="Exportin-6"
FT                   /id="PRO_0000235301"
FT   DOMAIN          31..97
FT                   /note="Importin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q924Z6"
FT   MOD_RES         201
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         204
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332"
FT   VAR_SEQ         1..14
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055756"
FT   VARIANT         1029
FT                   /note="V -> L (in dbSNP:rs14672)"
FT                   /id="VAR_048961"
FT   CONFLICT        378..379
FT                   /note="FV -> L (in Ref. 7; AAI08287)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        811
FT                   /note="Y -> H (in Ref. 7; AAH78674)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        891
FT                   /note="K -> R (in Ref. 8; BAD96763)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1125 AA;  128883 MW;  753D5F815EC110A2 CRC64;
     MASEEASLRA LESLMTEFFH DCTTNERKRE IEELLNNFAQ QIGAWRFCLY FLSSTRNDYV
     MMYSLTVFEN LINKMWLGVP SQDKMEIRSC LPKLLLAHHK TLPYFIRNKL CKVIVDIGRQ
     DWPMFYHDFF TNILQLIQSP VTTPLGLIML KTTSEELACP REDLSVARKE ELRKLLLDQV
     QTVLGLLTGI LETVWDKHSV TAATPPPSPT SGESGDLLSN LLQSPSSAKL LNQPIPILDV
     ESEYICSLAL ECLAHLFSWI PLSASITPSL LTTIFHFARF GCDIRARKMA SVNGSSQNCV
     SGQERGRLGV LAMSCINELM SKNCVPMEFE EYLLRMFQQT FYLLQKITKD NNAHTVKSRL
     EELDESYIEK FTDFLRLFVS VHLRRIESYS QFPVVEFLTL LFKYTFHQPT HEGYFSCLDI
     WTLFLDYLTS KIKSRLGDKE AVLNRYEDAL VLLLTEVLNR IQFRYNQAQL EELDDETLDD
     DQQTEWQRYL RQSLEVVAKV MELLPTHAFS TLFPVLQDNL EVYLGLQQFI VTSGSGHRLN
     ITAENDCRRL HCSLRDLSSL LQAVGRLAEY FIGDVFAARF NDALTVVERL VKVTLYGSQI
     KLYNIETAVP SVLKPDLIDV HAQSLAALQA YSHWLAQYCS EVHRQNTQQF VTLISTTMDA
     ITPLISTKVQ DKLLLSACHL LVSLATTVRP VFLISIPAVQ KVFNRITDAS ALRLVDKAQV
     LVCRALSNIL LLPWPNLPEN EQQWPVRSIN HASLISALSR DYRNLKPSAV APQRKMPLDD
     TKLIIHQTLS VLEDIVENIS GESTKSRQIC YQSLQESVQV SLALFPAFIH QSDVTDEMLS
     FFLTLFRGLR VQMGVPFTEQ IIQTFLNMFT REQLAESILH EGSTGCRVVE KFLKILQVVV
     QEPGQVFKPF LPSIIALCME QVYPIIAERP SPDVKAELFE LLFRTLHHNW RYFFKSTVLA
     SVQRGIAEEQ MENEPQFSAI MQAFGQSFLQ PDIHLFKQNL FYLETLNTKQ KLYHKKIFRT
     AMLFQFVNVL LQVLVHKSHD LLQEEIGIAI YNMASVDFDG FFAAFLPEFL TSCDGVDANQ
     KSVLGRNFKM DRDLPSFTQN VHRLVNDLRY YRLCNDSLPP GTVKL
 
 
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