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 27-MAR-2024, entry version 197.
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 -!- INTERACTION:
CC O95382; P31947: SFN; NbExp=2; IntAct=EBI-1254761, EBI-476295;
CC O95382; P62258: YWHAE; NbExp=2; IntAct=EBI-1254761, EBI-356498;
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; 61.
DR IntAct; O95382; 31.
DR MINT; O95382; -.
DR STRING; 9606.ENSP00000350195; -.
DR BindingDB; O95382; -.
DR ChEMBL; CHEMBL1163123; -.
DR DrugBank; DB12010; Fostamatinib.
DR GuidetoPHARMACOLOGY; 2081; -.
DR GlyCosmos; O95382; 1 site, 1 glycan.
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; 9606-ENSP00000419591; -.
DR PeptideAtlas; O95382; -.
DR ProteomicsDB; 50834; -. [O95382-1]
DR ProteomicsDB; 50835; -. [O95382-2]
DR ProteomicsDB; 50836; -. [O95382-3]
DR Pumba; O95382; -.
DR Antibodypedia; 30762; 231 antibodies from 29 providers.
DR DNASU; 9064; -.
DR Ensembl; ENST00000357582.3; ENSP00000350195.2; ENSG00000142733.18. [O95382-1]
DR Ensembl; ENST00000374040.7; ENSP00000363152.2; ENSG00000142733.18. [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 AGR; HGNC:6858; -.
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; VEQLLHC; -.
DR OrthoDB; 5388799at2759; -.
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; 13 hits in 1188 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 145 other cell types or 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: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 CDD; cd06624; STKc_ASK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046872; DRHyd-ASK.
DR InterPro; IPR046873; HisK-N-like.
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 PANTHER; PTHR11584:SF391; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 6; 1.
DR PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF19039; ASK_PH; 1.
DR Pfam; PF20309; DRHyd-ASK; 1.
DR Pfam; PF20302; HisK-N-like; 1.
DR Pfam; PF13281; MAP3K_TRAF_bd; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 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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