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M3K6_HUMAN
ID   M3K6_HUMAN              Reviewed;        1288 AA.
AC   O95382; A2ACE8; A2VDG4; A2VDG5; Q59HF4; Q5SSD4; Q75PK3; Q96B75;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 3.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase 6;
DE            EC=2.7.11.25;
DE   AltName: Full=Apoptosis signal-regulating kinase 2;
GN   Name=MAP3K6; Synonyms=ASK2, MAPKKK6, MEKK6;
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, ACTIVITY REGULATION,
RP   INTERACTION WITH MAP3K5, AND VARIANT ILE-455.
RX   PubMed=17210579; DOI=10.1074/jbc.m607177200;
RA   Takeda K., Shimozono R., Noguchi T., Umeda T., Morimoto Y., Naguro I.,
RA   Tobiume K., Saitoh M., Matsuzawa A., Ichijo H.;
RT   "Apoptosis signal-regulating kinase (ASK) 2 functions as a mitogen-
RT   activated protein kinase kinase kinase in a heteromeric complex with
RT   ASK1.";
RL   J. Biol. Chem. 282:7522-7531(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 435-1288 (ISOFORMS 1/3), AND VARIANTS ILE-455 AND
RP   ASN-969.
RC   TISSUE=Skin;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1288 (ISOFORM 3), AND VARIANT
RP   LYS-622.
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 197-1288, FUNCTION, TISSUE SPECIFICITY, AND
RP   INTERACTION WITH MAP3K5.
RX   PubMed=9875215; DOI=10.1006/bbrc.1998.9749;
RA   Wang X.S., Diener K., Tan T.-H., Yao Z.;
RT   "MAPKKK6, a novel mitogen-activated protein kinase kinase kinase, that
RT   associates with MAPKKK5.";
RL   Biochem. Biophys. Res. Commun. 253:33-37(1998).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984 AND SER-1129, AND
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984, AND IDENTIFICATION BY
RP   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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984; SER-1129 AND SER-1149,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964; SER-984 AND SER-1129,
RP   AND 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   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-869.
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).
RN   [11]
RP   VARIANTS [LARGE SCALE ANALYSIS] TRP-544; LYS-622; GLY-668; LEU-673;
RP   LEU-925; ILE-968 AND THR-1061.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Component of a protein kinase signal transduction cascade.
CC       Activates the JNK, but not ERK or p38 kinase pathways.
CC       {ECO:0000269|PubMed:17210579, ECO:0000269|PubMed:9875215}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.25;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-806.
CC       Catalytically active only when complexed with MAP3K5, with MAP3K5
CC       supporting the stability and the active configuration of MAP3K6 and
CC       MAP3K6 activating MAP3K5 by direct phosphorylation.
CC       {ECO:0000269|PubMed:17210579}.
CC   -!- SUBUNIT: Binds both upstream activators and downstream substrates in
CC       multimolecular complexes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O95382-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O95382-2; Sequence=VSP_026201, VSP_026203, VSP_026204;
CC       Name=3;
CC         IsoId=O95382-3; Sequence=VSP_026202;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD05304.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB167411; BAD12485.1; -; mRNA.
DR   EMBL; FO393419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC015914; AAH15914.1; -; mRNA.
DR   EMBL; BC129950; AAI29951.1; -; mRNA.
DR   EMBL; BC129951; AAI29952.1; -; mRNA.
DR   EMBL; AB208805; BAD92042.1; -; mRNA.
DR   EMBL; AF100318; AAD05304.1; ALT_INIT; mRNA.
DR   CCDS; CCDS299.1; -. [O95382-1]
DR   CCDS; CCDS72738.1; -. [O95382-3]
DR   RefSeq; NP_001284538.1; NM_001297609.1. [O95382-3]
DR   RefSeq; NP_004663.3; NM_004672.4. [O95382-1]
DR   AlphaFoldDB; O95382; -.
DR   SMR; O95382; -.
DR   BioGRID; 114524; 52.
DR   IntAct; O95382; 30.
DR   MINT; O95382; -.
DR   STRING; 9606.ENSP00000419591; -.
DR   BindingDB; O95382; -.
DR   ChEMBL; CHEMBL1163123; -.
DR   DrugBank; DB12010; Fostamatinib.
DR   GuidetoPHARMACOLOGY; 2081; -.
DR   GlyGen; O95382; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O95382; -.
DR   PhosphoSitePlus; O95382; -.
DR   BioMuta; MAP3K6; -.
DR   CPTAC; CPTAC-851; -.
DR   CPTAC; CPTAC-852; -.
DR   EPD; O95382; -.
DR   jPOST; O95382; -.
DR   MassIVE; O95382; -.
DR   MaxQB; O95382; -.
DR   PaxDb; O95382; -.
DR   PeptideAtlas; O95382; -.
DR   PRIDE; O95382; -.
DR   ProteomicsDB; 50834; -. [O95382-1]
DR   ProteomicsDB; 50835; -. [O95382-2]
DR   ProteomicsDB; 50836; -. [O95382-3]
DR   Antibodypedia; 30762; 222 antibodies from 29 providers.
DR   DNASU; 9064; -.
DR   Ensembl; ENST00000357582.3; ENSP00000350195.2; ENSG00000142733.17. [O95382-1]
DR   Ensembl; ENST00000374040.7; ENSP00000363152.2; ENSG00000142733.17. [O95382-3]
DR   GeneID; 9064; -.
DR   KEGG; hsa:9064; -.
DR   MANE-Select; ENST00000357582.3; ENSP00000350195.2; NM_004672.5; NP_004663.3.
DR   UCSC; uc001bny.2; human. [O95382-1]
DR   CTD; 9064; -.
DR   DisGeNET; 9064; -.
DR   GeneCards; MAP3K6; -.
DR   HGNC; HGNC:6858; MAP3K6.
DR   HPA; ENSG00000142733; Low tissue specificity.
DR   MalaCards; MAP3K6; -.
DR   MIM; 604468; gene.
DR   neXtProt; NX_O95382; -.
DR   OpenTargets; ENSG00000142733; -.
DR   Orphanet; 26106; Hereditary diffuse gastric cancer.
DR   PharmGKB; PA30602; -.
DR   VEuPathDB; HostDB:ENSG00000142733; -.
DR   eggNOG; KOG4279; Eukaryota.
DR   GeneTree; ENSGT00940000159398; -.
DR   HOGENOM; CLU_003687_3_0_1; -.
DR   InParanoid; O95382; -.
DR   OMA; HIRGGMV; -.
DR   OrthoDB; 1019877at2759; -.
DR   PhylomeDB; O95382; -.
DR   TreeFam; TF105115; -.
DR   BRENDA; 2.7.11.25; 2681.
DR   PathwayCommons; O95382; -.
DR   SignaLink; O95382; -.
DR   SIGNOR; O95382; -.
DR   BioGRID-ORCS; 9064; 11 hits in 1110 CRISPR screens.
DR   ChiTaRS; MAP3K6; human.
DR   GenomeRNAi; 9064; -.
DR   Pharos; O95382; Tchem.
DR   PRO; PR:O95382; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O95382; protein.
DR   Bgee; ENSG00000142733; Expressed in lower esophagus mucosa and 143 other tissues.
DR   ExpressionAtlas; O95382; baseline and differential.
DR   Genevisible; O95382; HS.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:UniProtKB.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR043969; MAP3K_PH.
DR   InterPro; IPR025136; MAP3K_TRAF-bd.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF19039; ASK_PH; 1.
DR   Pfam; PF13281; MAP3K_TRAF_bd; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Coiled coil; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..1288
FT                   /note="Mitogen-activated protein kinase kinase kinase 6"
FT                   /id="PRO_0000086251"
FT   DOMAIN          648..906
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          899..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1123..1157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1004..1029
FT                   /evidence="ECO:0000255"
FT   COILED          1166..1205
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        930..948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        771
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         654..662
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         677
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         806
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTR2"
FT   MOD_RES         964
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         984
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   VAR_SEQ         1..277
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026201"
FT   VAR_SEQ         161..168
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_026202"
FT   VAR_SEQ         1065..1074
FT                   /note="RLRAQGLGPA -> WMNGEDKGSF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026203"
FT   VAR_SEQ         1075..1288
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026204"
FT   VARIANT         455
FT                   /note="T -> I (in dbSNP:rs1138294)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:17210579"
FT                   /id="VAR_032832"
FT   VARIANT         499
FT                   /note="R -> C (in dbSNP:rs11247641)"
FT                   /id="VAR_046050"
FT   VARIANT         544
FT                   /note="R -> W (in dbSNP:rs55671988)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_046051"
FT   VARIANT         622
FT                   /note="N -> K (in dbSNP:rs35659744)"
FT                   /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.4"
FT                   /id="VAR_032833"
FT   VARIANT         668
FT                   /note="R -> G (in dbSNP:rs55869163)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_046052"
FT   VARIANT         673
FT                   /note="R -> L (in dbSNP:rs56359841)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_046053"
FT   VARIANT         869
FT                   /note="P -> T (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035629"
FT   VARIANT         925
FT                   /note="S -> L (in a breast pleomorphic lobular carcinoma
FT                   sample; somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_046054"
FT   VARIANT         968
FT                   /note="T -> I (in an ovarian endometrioid cancer sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_046055"
FT   VARIANT         969
FT                   /note="S -> N (in dbSNP:rs17856498)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_032834"
FT   VARIANT         1061
FT                   /note="A -> T (in dbSNP:rs55990440)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_046056"
FT   VARIANT         1233
FT                   /note="G -> A (in dbSNP:rs17162549)"
FT                   /id="VAR_046057"
FT   CONFLICT        435..440
FT                   /note="MQYYWD -> ALWVPV (in Ref. 3; AAI29952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        435..440
FT                   /note="MQYYWD -> HTWVPV (in Ref. 3; AAI29951)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1288 AA;  142596 MW;  013AF3729698080F CRC64;
     MAGPCPRSGA ERAGSCWQDP LAVALSRGRQ LAAPPGRGCA RSRPLSVVYV LTREPQPGLE
     PREGTEAEPL PLRCLREACA QVPRPRPPPQ LRSLPFGTLE LGDTAALDAF YNADVVVLEV
     SSSLVQPSLF YHLGVRESFS MTNNVLLCSQ ADLPDLQALR EDVFQKNSDC VGSYTLIPYV
     VTATGRVLCG DAGLLRGLAD GLVQAGVGTE ALLTPLVGRL ARLLEATPTD SCGYFRETIR
     RDIRQARERF SGPQLRQELA RLQRRLDSVE LLSPDIIMNL LLSYRDVQDY SAIIELVETL
     QALPTCDVAE QHNVCFHYTF ALNRRNRPGD RAKALSVLLP LVQLEGSVAP DLYCMCGRIY
     KDMFFSSGFQ DAGHREQAYH WYRKAFDVEP SLHSGINAAV LLIAAGQHFE DSKELRLIGM
     KLGCLLARKG CVEKMQYYWD VGFYLGAQIL ANDPTQVVLA AEQLYKLNAP IWYLVSVMET
     FLLYQHFRPT PEPPGGPPRR AHFWLHFLLQ SCQPFKTACA QGDQCLVLVL EMNKVLLPAK
     LEVRGTDPVS TVTLSLLEPE TQDIPSSWTF PVASICGVSA SKRDERCCFL YALPPAQDVQ
     LCFPSVGHCQ WFCGLIQAWV TNPDSTAPAE EAEGAGEMLE FDYEYTETGE RLVLGKGTYG
     VVYAGRDRHT RVRIAIKEIP ERDSRFSQPL HEEIALHRRL RHKNIVRYLG SASQGGYLKI
     FMEEVPGGSL SSLLRSVWGP LKDNESTISF YTRQILQGLG YLHDNHIVHR DIKGDNVLIN
     TFSGLLKISD FGTSKRLAGI TPCTETFTGT LQYMAPEIID QGPRGYGKAA DIWSLGCTVI
     EMATGRPPFH ELGSPQAAMF QVGMYKVHPP MPSSLSAEAQ AFLLRTFEPD PRLRASAQTL
     LGDPFLQPGK RSRSPSSPRH APRPSDAPSA SPTPSANSTT QSQTFPCPQA PSQHPPSPPK
     RCLSYGGTSQ LRVPEEPAAE EPASPEESSG LSLLHQESKR RAMLAAVLEQ ELPALAENLH
     QEQKQEQGAR LGRNHVEELL RCLGAHIHTP NRRQLAQELR ALQGRLRAQG LGPALLHRPL
     FAFPDAVKQI LRKRQIRPHW MFVLDSLLSR AVRAALGVLG PEVEKEAVSP RSEELSNEGD
     SQQSPGQQSP LPVEPEQGPA PLMVQLSLLR AETDRLREIL AGKEREYQAL VQRALQRLNE
     EARTYVLAPE PPTALSTDQG LVQWLQELNV DSGTIQMLLN HSFTLHTLLT YATRDDLIYT
     RIRGGMVCRI WRAILAQRAG STPVTSGP
 
 
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