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Dual specificity mitogen-activated protein kinase kinase 3 (MAP kinase kinase 3) (MAPKK 3) (EC 2.7.12.2) (MAPK/ERK kinase 3) (MEK 3) (Stress-activated protein kinase kinase 2) (SAPK kinase 2) (SAPKK-2) (SAPKK2)

 MP2K3_HUMAN             Reviewed;         347 AA.
P46734; B3KSK7; Q99441; Q9UE71; Q9UE72;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-2002, sequence version 2.
22-NOV-2017, entry version 187.
RecName: Full=Dual specificity mitogen-activated protein kinase kinase 3;
Short=MAP kinase kinase 3;
Short=MAPKK 3;
EC=2.7.12.2 {ECO:0000269|PubMed:8622669};
AltName: Full=MAPK/ERK kinase 3;
Short=MEK 3;
AltName: Full=Stress-activated protein kinase kinase 2;
Short=SAPK kinase 2;
Short=SAPKK-2;
Short=SAPKK2;
Name=MAP2K3; Synonyms=MEK3, MKK3, PRKMK3, SKK2;
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).
TISSUE=Brain;
PubMed=7839144; DOI=10.1126/science.7839144;
Derijard B., Raingeaud J., Barrett T., Wu I.-H., Han J.,
Ulevitch R.J., Davis R.J.;
"Independent human MAP-kinase signal transduction pathways defined by
MEK and MKK isoforms.";
Science 267:682-685(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=8900184; DOI=10.1074/jbc.271.43.26981;
Moriguchi T., Toyoshima F., Gotoh Y., Iwamatsu A., Irie K., Mori E.,
Kuroyanagi N., Hagiwara M., Matsumoto K., Nishida E.;
"Purification and identification of a major activator for p38 from
osmotically shocked cells: activation of mitogen-activated protein
kinase kinase 6 by osmotic shock, tumor necrosis factor-alpha, and
H2O2.";
J. Biol. Chem. 271:26981-26988(1996).
[3]
NUCLEOTIDE SEQUENCE (ISOFORMS 2 AND 3).
Han J.;
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Trachea;
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 MRNA] (ISOFORM 3).
TISSUE=Leukocyte;
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).
[6]
PHOSPHORYLATION AT SER-218 AND THR-222, MUTAGENESIS OF SER-218 AND
THR-222, CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=8622669; DOI=10.1128/MCB.16.3.1247;
Raingeaud J., Whitmarsh A.J., Barrett T., Derijard B., Davis R.J.;
"MKK3- and MKK6-regulated gene expression is mediated by the p38
mitogen-activated protein kinase signal transduction pathway.";
Mol. Cell. Biol. 16:1247-1255(1996).
[7]
PHOSPHORYLATION BY TAOK2.
PubMed=11279118; DOI=10.1074/jbc.M100681200;
Chen Z., Cobb M.H.;
"Regulation of stress-responsive mitogen-activated protein (MAP)
kinase pathways by TAO2.";
J. Biol. Chem. 276:16070-16075(2001).
[8]
INTERACTION WITH DYRK1B.
TISSUE=Muscle;
PubMed=11980910; DOI=10.1074/jbc.M203257200;
Lim S., Jin K., Friedman E.;
"Mirk protein kinase is activated by MKK3 and functions as a
transcriptional activator of HNF1alpha.";
J. Biol. Chem. 277:25040-25046(2002).
[9]
INTERACTION WITH ARRB1.
PubMed=16709866; DOI=10.4049/jimmunol.176.11.7039;
McLaughlin N.J., Banerjee A., Kelher M.R., Gamboni-Robertson F.,
Hamiel C., Sheppard F.R., Moore E.E., Silliman C.C.;
"Platelet-activating factor-induced clathrin-mediated endocytosis
requires beta-arrestin-1 recruitment and activation of the p38 MAPK
signalosome at the plasma membrane for actin bundle formation.";
J. Immunol. 176:7039-7050(2006).
[10]
INTERACTION WITH YOPJ, AND ACETYLATION.
PubMed=16728640; DOI=10.1126/science.1126867;
Mukherjee S., Keitany G., Li Y., Wang Y., Ball H.L., Goldsmith E.J.,
Orth K.;
"Yersinia YopJ acetylates and inhibits kinase activation by blocking
phosphorylation.";
Science 312:1211-1214(2006).
[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 MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-3 AND SER-15, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
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).
[14]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH AKAP13; PKN1; MAPK14;
ZAK AND MAP2K3.
PubMed=21224381; DOI=10.1074/jbc.M110.185645;
Cariolato L., Cavin S., Diviani D.;
"A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling
complex involved in alpha1-adrenergic receptor-induced p38
activation.";
J. Biol. Chem. 286:7925-7937(2011).
[15]
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).
[16]
VARIANTS COLON CANCER TRP-175 AND VAL-215.
PubMed=11414763; DOI=10.1006/geno.2001.6551;
Teng D.-H., Chen Y., Lian L., Ha P.C., Tavtigian S.V., Wong A.K.C.;
"Mutation analyses of 268 candidate genes in human tumor cell lines.";
Genomics 74:352-364(2001).
[17]
VARIANTS [LARGE SCALE ANALYSIS] THR-26; PRO-68; THR-84; ILE-90;
LEU-94; TRP-96; HIS-293 AND MET-339.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Dual specificity kinase. Is activated by cytokines and
environmental stress in vivo. Catalyzes the concomitant
phosphorylation of a threonine and a tyrosine residue in the MAP
kinase p38. Part of a signaling cascade that begins with the
activation of the adrenergic receptor ADRA1B and leads to the
activation of MAPK14. {ECO:0000269|PubMed:21224381,
ECO:0000269|PubMed:8622669}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:8622669}.
-!- ENZYME REGULATION: Activated by dual phosphorylation on Ser-218
and Thr-222. {ECO:0000269|PubMed:8622669}.
-!- SUBUNIT: Component of a signaling complex containing at least
AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13
interacts directly with PKN1, which in turn recruits MAPK14,
MAP2K3 and ZAK (PubMed:21224381). Binds to DYRK1B/MIRK and
increases its kinase activity (PubMed:11980910). Part of a complex
with MAP3K3, RAC1 and CCM2 (By similarity). Interacts with ARRB1
(PubMed:16709866). Interacts with Yersinia yopJ (PubMed:16728640).
{ECO:0000250|UniProtKB:O09110, ECO:0000269|PubMed:11980910,
ECO:0000269|PubMed:16709866, ECO:0000269|PubMed:16728640,
ECO:0000269|PubMed:21224381}.
-!- INTERACTION:
Q9Y463:DYRK1B; NbExp=2; IntAct=EBI-602462, EBI-634187;
Q5S007:LRRK2; NbExp=5; IntAct=EBI-602462, EBI-5323863;
Q99683:MAP3K5; NbExp=4; IntAct=EBI-602462, EBI-476263;
Q16539:MAPK14; NbExp=2; IntAct=EBI-602462, EBI-73946;
Q9BSI4:TINF2; NbExp=2; IntAct=EBI-602462, EBI-717399;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=3; Synonyms=3b;
IsoId=P46734-1; Sequence=Displayed;
Name=1;
IsoId=P46734-2; Sequence=VSP_004878;
Name=2; Synonyms=3c;
IsoId=P46734-3; Sequence=VSP_004877;
-!- TISSUE SPECIFICITY: Abundant expression is seen in the skeletal
muscle. It is also widely expressed in other tissues.
-!- PTM: Autophosphorylated. Phosphorylation on Ser-218 and Thr-222 by
MAP kinase kinase kinases regulates positively the kinase activity
(PubMed:8622669). Phosphorylated by TAOK2 (PubMed:11279118).
{ECO:0000269|PubMed:11279118, ECO:0000269|PubMed:8622669}.
-!- PTM: Yersinia yopJ may acetylate Ser/Thr residues, preventing
phosphorylation and activation, thus blocking the MAPK signaling
pathway. {ECO:0000269|PubMed:16728640}.
-!- DISEASE: Note=Defects in MAP2K3 may be involved in colon cancer.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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EMBL; L36719; AAC41718.1; -; mRNA.
EMBL; D87116; BAA13248.1; -; mRNA.
EMBL; U66839; AAB40652.1; -; mRNA.
EMBL; U66840; AAB40653.1; -; Genomic_DNA.
EMBL; AK093838; BAG52769.1; -; mRNA.
EMBL; BC032478; AAH32478.1; -; mRNA.
CCDS; CCDS11217.1; -. [P46734-1]
CCDS; CCDS11218.1; -. [P46734-2]
RefSeq; NP_001303261.1; NM_001316332.1. [P46734-2]
RefSeq; NP_002747.2; NM_002756.4. [P46734-2]
RefSeq; NP_659731.1; NM_145109.2. [P46734-1]
RefSeq; XP_005256780.1; XM_005256723.2. [P46734-2]
RefSeq; XP_011522261.1; XM_011523959.1. [P46734-2]
RefSeq; XP_016880347.1; XM_017024858.1. [P46734-2]
RefSeq; XP_016880348.1; XM_017024859.1. [P46734-2]
UniGene; Hs.514012; -.
ProteinModelPortal; P46734; -.
SMR; P46734; -.
BioGrid; 111592; 35.
DIP; DIP-34242N; -.
IntAct; P46734; 20.
MINT; MINT-4300215; -.
STRING; 9606.ENSP00000345083; -.
BindingDB; P46734; -.
ChEMBL; CHEMBL2109; -.
GuidetoPHARMACOLOGY; 2064; -.
iPTMnet; P46734; -.
PhosphoSitePlus; P46734; -.
BioMuta; MAP2K3; -.
DMDM; 24638466; -.
EPD; P46734; -.
PaxDb; P46734; -.
PeptideAtlas; P46734; -.
PRIDE; P46734; -.
DNASU; 5606; -.
Ensembl; ENST00000316920; ENSP00000319139; ENSG00000034152. [P46734-2]
Ensembl; ENST00000342679; ENSP00000345083; ENSG00000034152. [P46734-1]
Ensembl; ENST00000361818; ENSP00000355081; ENSG00000034152. [P46734-2]
Ensembl; ENST00000613338; ENSP00000478619; ENSG00000034152. [P46734-2]
GeneID; 5606; -.
KEGG; hsa:5606; -.
UCSC; uc021tsq.2; human. [P46734-1]
CTD; 5606; -.
DisGeNET; 5606; -.
EuPathDB; HostDB:ENSG00000034152.18; -.
GeneCards; MAP2K3; -.
HGNC; HGNC:6843; MAP2K3.
HPA; CAB018548; -.
MIM; 602315; gene.
neXtProt; NX_P46734; -.
OpenTargets; ENSG00000034152; -.
PharmGKB; PA30588; -.
eggNOG; KOG0984; Eukaryota.
eggNOG; ENOG410XT3F; LUCA.
GeneTree; ENSGT00760000119199; -.
HOGENOM; HOG000234206; -.
HOVERGEN; HBG108518; -.
InParanoid; P46734; -.
KO; K04432; -.
OMA; ACVTIGD; -.
OrthoDB; EOG091G0A9H; -.
PhylomeDB; P46734; -.
TreeFam; TF350701; -.
BRENDA; 2.7.12.2; 2681.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
SignaLink; P46734; -.
SIGNOR; P46734; -.
ChiTaRS; MAP2K3; human.
GeneWiki; MAP2K3; -.
GenomeRNAi; 5606; -.
PMAP-CutDB; P46734; -.
PRO; PR:P46734; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000034152; -.
CleanEx; HS_MAP2K3; -.
ExpressionAtlas; P46734; baseline and differential.
Genevisible; P46734; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004708; F:MAP kinase kinase activity; TAS:ProtInc.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0035897; P:proteolysis in other organism; TAS:Reactome.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0042035; P:regulation of cytokine biosynthetic process; IEA:Ensembl.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Disease mutation; Kinase; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Transferase; Tyrosine-protein kinase.
CHAIN 1 347 Dual specificity mitogen-activated
protein kinase kinase 3.
/FTId=PRO_0000086378.
DOMAIN 64 325 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 70 78 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 190 190 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 93 93 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22814378}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000269|PubMed:8622669}.
MOD_RES 222 222 Phosphothreonine.
{ECO:0000269|PubMed:8622669}.
VAR_SEQ 1 29 Missing (in isoform 1).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:7839144}.
/FTId=VSP_004878.
VAR_SEQ 1 16 MESPASSQPASMPQSK -> MGVQGTLMSRDSQTPHLLSIL
(in isoform 2). {ECO:0000305}.
/FTId=VSP_004877.
VARIANT 26 26 R -> T. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_040817.
VARIANT 40 40 P -> T (in dbSNP:rs33911218).
/FTId=VAR_046062.
VARIANT 55 55 R -> T (in dbSNP:rs36047035).
/FTId=VAR_061742.
VARIANT 68 68 S -> P (in dbSNP:rs34105301).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_046063.
VARIANT 84 84 A -> T (in dbSNP:rs2305873).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_046064.
VARIANT 90 90 M -> I (in dbSNP:rs36076766).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_046065.
VARIANT 94 94 R -> L (in dbSNP:rs56067280).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_046066.
VARIANT 96 96 R -> W (in dbSNP:rs56216806).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_046067.
VARIANT 175 175 R -> W (in colon cancer).
{ECO:0000269|PubMed:11414763}.
/FTId=VAR_014208.
VARIANT 215 215 L -> V (in colon cancer).
{ECO:0000269|PubMed:11414763}.
/FTId=VAR_014209.
VARIANT 293 293 R -> H (in dbSNP:rs35206134).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_046068.
VARIANT 339 339 V -> M (in dbSNP:rs2363198).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_046069.
MUTAGEN 218 218 S->A: Inactivation.
{ECO:0000269|PubMed:8622669}.
MUTAGEN 218 218 S->E: Constitutive activation.
{ECO:0000269|PubMed:8622669}.
MUTAGEN 222 222 T->A: Inactivation.
{ECO:0000269|PubMed:8622669}.
MUTAGEN 222 222 T->E: Constitutive activation.
{ECO:0000269|PubMed:8622669}.
CONFLICT 341 341 E -> K (in Ref. 1 and 3). {ECO:0000305}.
SEQUENCE 347 AA; 39318 MW; A80BA4FDFF8F75A2 CRC64;
MESPASSQPA SMPQSKGKSK RKKDLRISCM SKPPAPNPTP PRNLDSRTFI TIGDRNFEVE
ADDLVTISEL GRGAYGVVEK VRHAQSGTIM AVKRIRATVN SQEQKRLLMD LDINMRTVDC
FYTVTFYGAL FREGDVWICM ELMDTSLDKF YRKVLDKNMT IPEDILGEIA VSIVRALEHL
HSKLSVIHRD VKPSNVLINK EGHVKMCDFG ISGYLVDSVA KTMDAGCKPY MAPERINPEL
NQKGYNVKSD VWSLGITMIE MAILRFPYES WGTPFQQLKQ VVEEPSPQLP ADRFSPEFVD
FTAQCLRKNP AERMSYLELM EHPFFTLHKT KKTDIAAFVK EILGEDS


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