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Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (Microtubule-associated protein 2 kinase) (p44-ERK1)

 MK03_HUMAN              Reviewed;         379 AA.
P27361; A8CZ58; B0LPG3; Q8NHX1;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
27-SEP-2017, entry version 203.
RecName: Full=Mitogen-activated protein kinase 3;
Short=MAP kinase 3;
Short=MAPK 3;
EC=2.7.11.24;
AltName: Full=ERT2;
AltName: Full=Extracellular signal-regulated kinase 1;
Short=ERK-1;
AltName: Full=Insulin-stimulated MAP2 kinase;
AltName: Full=MAP kinase isoform p44;
Short=p44-MAPK;
AltName: Full=Microtubule-associated protein 2 kinase;
AltName: Full=p44-ERK1;
Name=MAPK3; Synonyms=ERK1, PRKM3;
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=Hepatoma;
PubMed=7687743; DOI=10.1128/MCB.13.8.4679;
Charest D.L., Jirik F., Harder K., Pelech S.L., Mordret G.;
"Molecular cloning, expression, and characterization of the human
mitogen-activated protein kinase p44erk1.";
Mol. Cell. Biol. 13:4679-4690(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Aebersold D.M., Yung Y., Seger R.;
"Properties of human ERK1b.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Cheng H., Ren S., Qiu R., Wang M., Feng Y.H.;
"Identification of dominant negative Erk1/2 variants in cancer
cells.";
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
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 2-15; 33-41; 88-94; 117-131; 212-220; 279-287;
303-318 AND 360-370, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Dhillon A.S., Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-379 (ISOFORM 1).
PubMed=1540184; DOI=10.1016/0006-291X(92)91891-S;
Owaki H., Makar R., Boulton T.G., Cobb M.H., Geppert T.D.;
"Extracellular signal-regulated kinases in T cells: characterization
of human ERK1 and ERK2 cDNAs.";
Biochem. Biophys. Res. Commun. 182:1416-1422(1992).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-379 (ISOFORM 1).
PubMed=1319925; DOI=10.1016/0014-5793(92)80612-K;
Gonzalez F.A., Raden D.L., Rigby M.R., Davis R.J.;
"Heterogeneous expression of four MAP kinase isoforms in human
tissues.";
FEBS Lett. 304:170-178(1992).
[11]
FUNCTION IN PHOSPHORYLATION OF STMN1.
PubMed=8325880;
Marklund U., Brattsand G., Shingler V., Gullberg M.;
"Serine 25 of oncoprotein 18 is a major cytosolic target for the
mitogen-activated protein kinase.";
J. Biol. Chem. 268:15039-15047(1993).
[12]
INTERACTION WITH HIV-1 NEF.
PubMed=8794306;
Greenway A.L., Azad A., Mills J., McPhee D.A.;
"Human immunodeficiency virus type 1 Nef binds directly to LCK and
mitogen-activated protein kinase, inhibiting kinase activity.";
J. Virol. 70:6701-6708(1996).
[13]
FUNCTION IN PHOSPHORYLATION OF MKNK1/MNK1.
PubMed=9155018; DOI=10.1093/emboj/16.8.1921;
Fukunaga R., Hunter T.;
"MNK1, a new MAP kinase-activated protein kinase, isolated by a novel
expression screening method for identifying protein kinase
substrates.";
EMBO J. 16:1921-1933(1997).
[14]
FUNCTION IN PHOSPHORYLATION OF MAPKAPK5.
PubMed=9480836; DOI=10.1006/bbrc.1998.8135;
Ni H., Wang X.S., Diener K., Yao Z.;
"MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated
protein kinase, is a substrate of the extracellular-regulated kinase
(ERK) and p38 kinase.";
Biochem. Biophys. Res. Commun. 243:492-496(1998).
[15]
FUNCTION IN PHOSPHORYLATION OF CANX, AND INTERACTION WITH CANX.
PubMed=10393181; DOI=10.1093/emboj/18.13.3655;
Chevet E., Wong H.N., Gerber D., Cochet C., Fazel A., Cameron P.H.,
Gushue J.N., Thomas D.Y., Bergeron J.J.;
"Phosphorylation by CK2 and MAPK enhances calnexin association with
ribosomes.";
EMBO J. 18:3655-3666(1999).
[16]
DEPHOSPHORYLATION BY DUSP3.
PubMed=10224087; DOI=10.1074/jbc.274.19.13271;
Todd J.L., Tanner K.G., Denu J.M.;
"Extracellular regulated kinases (ERK) 1 and ERK2 are authentic
substrates for the dual-specificity protein-tyrosine phosphatase VHR.
A novel role in down-regulating the ERK pathway.";
J. Biol. Chem. 274:13271-13280(1999).
[17]
SUBCELLULAR LOCATION, INTERACTION WITH MAP2K1/MEK1, AND DOMAIN.
PubMed=10521408; DOI=10.1074/jbc.274.43.30349;
Rubinfeld H., Hanoch T., Seger R.;
"Identification of a cytoplasmic-retention sequence in ERK2.";
J. Biol. Chem. 274:30349-30352(1999).
[18]
FUNCTION IN PHOSPHORYLATION OF DUSP1.
PubMed=10617468; DOI=10.1126/science.286.5449.2514;
Brondello J.M., Pouyssegur J., McKenzie F.R.;
"Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-
dependent phosphorylation.";
Science 286:2514-2517(1999).
[19]
INTERACTION WITH HSF1.
PubMed=10747973; DOI=10.1074/jbc.M000958200;
Dai R., Frejtag W., He B., Zhang Y., Mivechi N.F.;
"c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock
factor-1 suppress its transcriptional activity.";
J. Biol. Chem. 275:18210-18218(2000).
[20]
FUNCTION IN PHOSPHORYLATION OF IER3, INTERACTION WITH IER3, AND ENZYME
REGULATION.
PubMed=12356731; DOI=10.1093/emboj/cdf488;
Garcia J., Ye Y., Arranz V., Letourneux C., Pezeron G., Porteu F.;
"IEX-1: a new ERK substrate involved in both ERK survival activity and
ERK activation.";
EMBO J. 21:5151-5163(2002).
[21]
INTERACTION WITH NISCH.
PubMed=11912194; DOI=10.1074/jbc.M111838200;
Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.;
"Insulin receptor substrate 4 associates with the protein IRAS.";
J. Biol. Chem. 277:19439-19447(2002).
[22]
REVIEW ON ROLE IN KIT SIGNALING.
PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
Ronnstrand L.;
"Signal transduction via the stem cell factor receptor/c-Kit.";
Cell. Mol. Life Sci. 61:2535-2548(2004).
[23]
FUNCTION IN PHOSPHORYLATION OF GRB10.
PubMed=15952796; DOI=10.1021/bi050413i;
Langlais P., Wang C., Dong L.Q., Carroll C.A., Weintraub S.T., Liu F.;
"Phosphorylation of Grb10 by mitogen-activated protein kinase:
identification of Ser150 and Ser476 of human Grb10zeta as major
phosphorylation sites.";
Biochemistry 44:8890-8897(2005).
[24]
INTERACTION WITH DAPK1.
PubMed=15616583; DOI=10.1038/sj.emboj.7600510;
Chen C.H., Wang W.J., Kuo J.C., Tsai H.C., Lin J.R., Chang Z.F.,
Chen R.H.;
"Bidirectional signals transduced by DAPK-ERK interaction promote the
apoptotic effect of DAPK.";
EMBO J. 24:294-304(2005).
[25]
FUNCTION IN PHOSPHORYLATION OF ATF2.
PubMed=12110590; DOI=10.1093/emboj/cdf361;
Ouwens D.M., de Ruiter N.D., van der Zon G.C., Carter A.P.,
Schouten J., van der Burgt C., Kooistra K., Bos J.L., Maassen J.A.,
van Dam H.;
"Growth factors can activate ATF2 via a two-step mechanism:
phosphorylation of Thr71 through the Ras-MEK-ERK pathway and of Thr69
through RalGDS-Src-p38.";
EMBO J. 21:3782-3793(2002).
[26]
FUNCTION IN PHOSPHORYLATION OF FRS2.
PubMed=12974390; DOI=10.1515/BC.2003.134;
Wu Y., Chen Z., Ullrich A.;
"EGFR and FGFR signaling through FRS2 is subject to negative feedback
control by ERK1/2.";
Biol. Chem. 384:1215-1226(2003).
[27]
FUNCTION IN PHOSPHORYLATION OF BTG2.
PubMed=15788397; DOI=10.1074/jbc.M500318200;
Hong J.W., Ryu M.S., Lim I.K.;
"Phosphorylation of serine 147 of tis21/BTG2/pc3 by p-Erk1/2 induces
Pin-1 binding in cytoplasm and cell death.";
J. Biol. Chem. 280:21256-21263(2005).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[29]
FUNCTION, AND INTERACTION WITH HSF4.
PubMed=16581800; DOI=10.1128/MCB.26.8.3282-3294.2006;
Hu Y., Mivechi N.F.;
"Association and regulation of heat shock transcription factor 4b with
both extracellular signal-regulated kinase mitogen-activated protein
kinase and dual-specificity tyrosine phosphatase DUSP26.";
Mol. Cell. Biol. 26:3282-3294(2006).
[30]
PHOSPHORYLATION.
PubMed=17274988; DOI=10.1016/j.febslet.2007.01.039;
Degoutin J., Vigny M., Gouzi J.Y.;
"ALK activation induces Shc and FRS2 recruitment: Signaling and
phenotypic outcomes in PC12 cells differentiation.";
FEBS Lett. 581:727-734(2007).
[31]
INTERACTION WITH ARRB2.
PubMed=18435604; DOI=10.1042/BJ20080685;
Xu T.-R., Baillie G.S., Bhari N., Houslay T.M., Pitt A.M., Adams D.R.,
Kolch W., Houslay M.D., Milligan G.;
"Mutations of beta-arrestin 2 that limit self-association also
interfere with interactions with the beta2-adrenoceptor and the ERK1/2
MAPKs: implications for beta2-adrenoceptor signalling via the ERK1/2
MAPKs.";
Biochem. J. 413:51-60(2008).
[32]
INTERACTION WITH ADAM15.
PubMed=18296648; DOI=10.1158/1541-7786.MCR-07-2028;
Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M.,
Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C.,
Edwards D.R.;
"Distinct functions of natural ADAM-15 cytoplasmic domain variants in
human mammary carcinoma.";
Mol. Cancer Res. 6:383-394(2008).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[34]
INTERACTION WITH TPR.
PubMed=18794356; DOI=10.1128/MCB.00925-08;
Vomastek T., Iwanicki M.P., Burack W.R., Tiwari D., Kumar D.,
Parsons J.T., Weber M.J., Nandicoori V.K.;
"Extracellular signal-regulated kinase 2 (ERK2) phosphorylation sites
and docking domain on the nuclear pore complex protein Tpr
cooperatively regulate ERK2-Tpr interaction.";
Mol. Cell. Biol. 28:6954-6966(2008).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND TYR-204, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], 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).
[37]
FUNCTION IN KIT SIGNALING PATHWAY, AND PHOSPHORYLATION.
PubMed=19265199; DOI=10.1074/jbc.M808058200;
Sun J., Pedersen M., Ronnstrand L.;
"The D816V mutation of c-Kit circumvents a requirement for Src family
kinases in c-Kit signal transduction.";
J. Biol. Chem. 284:11039-11047(2009).
[38]
PHOSPHORYLATION AT TYR-204, AND DEPHOSPHORYLATION AT TYR-204 BY PTPRJ.
PubMed=19494114; DOI=10.1074/jbc.M109.002758;
Sacco F., Tinti M., Palma A., Ferrari E., Nardozza A.P.,
Hooft van Huijsduijnen R., Takahashi T., Castagnoli L., Cesareni G.;
"Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the
RAS pathway by direct dephosphorylation of ERK1/2 kinases.";
J. Biol. Chem. 284:22048-22058(2009).
[39]
INTERACTION WITH SGK1.
PubMed=19447520; DOI=10.1016/j.jhep.2009.02.027;
Won M., Park K.A., Byun H.S., Kim Y.R., Choi B.L., Hong J.H., Park J.,
Seok J.H., Lee Y.H., Cho C.H., Song I.S., Kim Y.K., Shen H.M.,
Hur G.M.;
"Protein kinase SGK1 enhances MEK/ERK complex formation through the
phosphorylation of ERK2: implication for the positive regulatory role
of SGK1 on the ERK function during liver regeneration.";
J. Hepatol. 51:67-76(2009).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[41]
PHOSPHORYLATION AT THR-207, ENZYME REGULATION, SUBUNIT, AND
SUBCELLULAR LOCATION.
PubMed=19060905; DOI=10.1038/nm.1893;
Lorenz K., Schmitt J.P., Schmitteckert E.M., Lohse M.J.;
"A new type of ERK1/2 autophosphorylation causes cardiac
hypertrophy.";
Nat. Med. 15:75-83(2009).
[42]
REVIEW ON FUNCTION.
PubMed=16393692; DOI=10.1080/02699050500284218;
Yoon S., Seger R.;
"The extracellular signal-regulated kinase: multiple substrates
regulate diverse cellular functions.";
Growth Factors 24:21-44(2006).
[43]
REVIEW ON FUNCTION, AND REVIEW ON SUBCELLULAR LOCATION.
PubMed=19565474; DOI=10.1002/biof.52;
Yao Z., Seger R.;
"The ERK signaling cascade--views from different subcellular
compartments.";
BioFactors 35:407-416(2009).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND TYR-204, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[45]
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).
[46]
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).
[47]
REVIEW ON ENZYME REGULATION, AND REVIEW ON FUNCTION.
PubMed=21779493; DOI=10.1177/1947601911407328;
Wortzel I., Seger R.;
"The ERK cascade: distinct functions within various subcellular
organelles.";
Genes Cancer 2:195-209(2011).
[48]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND TYR-204, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[49]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], 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).
[50]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], 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).
[51]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND TYR-204, 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).
[52]
INTERACTION WITH CDKN2AIP.
PubMed=24825908; DOI=10.1074/jbc.M114.547208;
Cheung C.T., Singh R., Kalra R.S., Kaul S.C., Wadhwa R.;
"Collaborator of ARF (CARF) regulates proliferative fate of human
cells by dose-dependent regulation of DNA damage signaling.";
J. Biol. Chem. 289:18258-18269(2014).
[53]
X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS), AND PHOSPHORYLATION AT
TYR-204.
PubMed=18983981; DOI=10.1016/j.bbrc.2008.10.127;
Kinoshita T., Yoshida I., Nakae S., Okita K., Gouda M., Matsubara M.,
Yokota K., Ishiguro H., Tada T.;
"Crystal structure of human mono-phosphorylated ERK1 at Tyr204.";
Biochem. Biophys. Res. Commun. 377:1123-1127(2008).
[54]
VARIANT [LARGE SCALE ANALYSIS] LYS-323.
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: Serine/threonine kinase which acts as an essential
component of the MAP kinase signal transduction pathway.
MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important
role in the MAPK/ERK cascade. They participate also in a signaling
cascade initiated by activated KIT and KITLG/SCF. Depending on the
cellular context, the MAPK/ERK cascade mediates diverse biological
functions such as cell growth, adhesion, survival and
differentiation through the regulation of transcription,
translation, cytoskeletal rearrangements. The MAPK/ERK cascade
plays also a role in initiation and regulation of meiosis,
mitosis, and postmitotic functions in differentiated cells by
phosphorylating a number of transcription factors. About 160
substrates have already been discovered for ERKs. Many of these
substrates are localized in the nucleus, and seem to participate
in the regulation of transcription upon stimulation. However,
other substrates are found in the cytosol as well as in other
cellular organelles, and those are responsible for processes such
as translation, mitosis and apoptosis. Moreover, the MAPK/ERK
cascade is also involved in the regulation of the endosomal
dynamics, including lysosome processing and endosome cycling
through the perinuclear recycling compartment (PNRC); as well as
in the fragmentation of the Golgi apparatus during mitosis. The
substrates include transcription factors (such as ATF2, BCL6,
ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as
CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of
apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG),
regulators of translation (such as EIF4EBP1) and a variety of
other signaling-related molecules (like ARHGEF2, FRS2 or GRB10).
Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2,
RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2,
RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases
(such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which
enable the propagation the MAPK/ERK signal to additional cytosolic
and nuclear targets, thereby extending the specificity of the
cascade. {ECO:0000269|PubMed:10393181,
ECO:0000269|PubMed:10617468, ECO:0000269|PubMed:12110590,
ECO:0000269|PubMed:12356731, ECO:0000269|PubMed:12974390,
ECO:0000269|PubMed:15788397, ECO:0000269|PubMed:15952796,
ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:19265199,
ECO:0000269|PubMed:8325880, ECO:0000269|PubMed:9155018,
ECO:0000269|PubMed:9480836}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Phosphorylated by MAP2K1/MEK1 and MAP2K2/MEK2
on Thr-202 and Tyr-204 in response to external stimuli like
insulin or NGF. Both phosphorylations are required for activity.
This phosphorylation causes dramatic conformational changes, which
enable full activation and interaction of MAPK1/ERK2 with its
substrates. Dephosphorylated and inactivated by DUSP3, DUSP6 and
DUSP9. {ECO:0000269|PubMed:12356731, ECO:0000269|PubMed:19060905}.
-!- SUBUNIT: Binds both upstream activators and downstream substrates
in multimolecular complexes. Found in a complex with at least
BRAF, HRAS, MAP2K1/MEK1, MAPK3 and RGS14 (By similarity). Binds to
HIV-1 Nef through its SH3 domain. This interaction inhibits its
tyrosine-kinase activity. Interacts with ADAM15, ARRB2, CANX,
DAPK1 (via death domain), HSF4, IER3, MAP2K1/MEK1, MORG1, NISCH,
and SGK1. Interacts with PEA15 and MKNK2 (By similarity). MKNK2
isoform 1 binding prevents from dephosphorylation and inactivation
(By similarity). Interacts with TPR. Interacts with CDKN2AIP.
Interacts with HSF1 (via D domain and preferentially with
hyperphosphorylated form); this interaction occurs upon heat shock
(PubMed:10747973). Interacts with CAVIN4 (By similarity).
{ECO:0000250|UniProtKB:P21708, ECO:0000250|UniProtKB:Q63844,
ECO:0000269|PubMed:10393181, ECO:0000269|PubMed:10521408,
ECO:0000269|PubMed:10747973, ECO:0000269|PubMed:11912194,
ECO:0000269|PubMed:12356731, ECO:0000269|PubMed:15616583,
ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:18296648,
ECO:0000269|PubMed:18435604, ECO:0000269|PubMed:18794356,
ECO:0000269|PubMed:19060905, ECO:0000269|PubMed:19447520,
ECO:0000269|PubMed:24825908, ECO:0000269|PubMed:8794306}.
-!- INTERACTION:
P53355:DAPK1; NbExp=5; IntAct=EBI-73995, EBI-358616;
P49366:DHPS; NbExp=3; IntAct=EBI-73995, EBI-741925;
P28562:DUSP1; NbExp=3; IntAct=EBI-73995, EBI-975493;
P19419:ELK1; NbExp=2; IntAct=EBI-73995, EBI-726632;
Q02750:MAP2K1; NbExp=2; IntAct=EBI-73995, EBI-492564;
P28482:MAPK1; NbExp=3; IntAct=EBI-73995, EBI-959949;
Q16539:MAPK14; NbExp=5; IntAct=EBI-73995, EBI-73946;
Q9EPI6:Nsmf (xeno); NbExp=2; IntAct=EBI-73995, EBI-6899705;
P14618-1:PKM; NbExp=3; IntAct=EBI-73995, EBI-4304679;
Q8N490:PNKD; NbExp=4; IntAct=EBI-73995, EBI-746368;
P23467:PTPRB; NbExp=2; IntAct=EBI-73995, EBI-1265766;
Q12913:PTPRJ; NbExp=5; IntAct=EBI-73995, EBI-2264500;
Q62132:Ptprr (xeno); NbExp=3; IntAct=EBI-73995, EBI-6954051;
Q15349:RPS6KA2; NbExp=2; IntAct=EBI-73995, EBI-1384149;
Q14160:SCRIB; NbExp=2; IntAct=EBI-73995, EBI-357345;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane, caveola
{ECO:0000250|UniProtKB:P21708}. Note=Autophosphorylation at Thr-
207 promotes nuclear localization.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P27361-1; Sequence=Displayed;
Name=2;
IsoId=P27361-2; Sequence=VSP_041906;
Name=3; Synonyms=ERK1b;
IsoId=P27361-3; Sequence=VSP_041907;
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
{ECO:0000269|PubMed:10521408}.
-!- PTM: Phosphorylated upon KIT and FLT3 signaling (By similarity).
Dually phosphorylated on Thr-202 and Tyr-204, which activates the
enzyme. Ligand-activated ALK induces tyrosine phosphorylation.
Dephosphorylated by PTPRJ at Tyr-204. {ECO:0000250,
ECO:0000269|PubMed:17274988, ECO:0000269|PubMed:18983981,
ECO:0000269|PubMed:19060905, ECO:0000269|PubMed:19265199,
ECO:0000269|PubMed:19494114}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MAPK3ID425ch16p11.html";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X60188; CAA42744.1; -; mRNA.
EMBL; AY033607; AAK52329.1; -; mRNA.
EMBL; DQ399291; ABD60302.1; -; mRNA.
EMBL; EU332853; ABY87542.1; -; Genomic_DNA.
EMBL; AC012645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471238; EAW79912.1; -; Genomic_DNA.
EMBL; CH471238; EAW79915.1; -; Genomic_DNA.
EMBL; BC013992; AAH13992.1; -; mRNA.
EMBL; M84490; AAA36142.1; -; mRNA.
EMBL; Z11696; CAA77754.1; -; mRNA.
CCDS; CCDS10672.1; -. [P27361-1]
CCDS; CCDS42148.1; -. [P27361-2]
CCDS; CCDS42149.1; -. [P27361-3]
PIR; A48082; A48082.
RefSeq; NP_001035145.1; NM_001040056.2. [P27361-3]
RefSeq; NP_001103361.1; NM_001109891.1. [P27361-2]
RefSeq; NP_002737.2; NM_002746.2. [P27361-1]
UniGene; Hs.861; -.
PDB; 2ZOQ; X-ray; 2.39 A; A/B=1-379.
PDB; 4QTB; X-ray; 1.40 A; A/B=1-379.
PDBsum; 2ZOQ; -.
PDBsum; 4QTB; -.
ProteinModelPortal; P27361; -.
SMR; P27361; -.
BioGrid; 111581; 198.
CORUM; P27361; -.
DIP; DIP-30985N; -.
ELM; P27361; -.
IntAct; P27361; 95.
MINT; MINT-99599; -.
STRING; 9606.ENSP00000263025; -.
BindingDB; P27361; -.
ChEMBL; CHEMBL3385; -.
DrugBank; DB04604; 5-iodotubercidin.
DrugBank; DB01169; Arsenic trioxide.
DrugBank; DB02733; Purvalanol.
DrugBank; DB00605; Sulindac.
GuidetoPHARMACOLOGY; 1494; -.
iPTMnet; P27361; -.
PhosphoSitePlus; P27361; -.
BioMuta; MAPK3; -.
DMDM; 232066; -.
EPD; P27361; -.
MaxQB; P27361; -.
PaxDb; P27361; -.
PeptideAtlas; P27361; -.
PRIDE; P27361; -.
DNASU; 5595; -.
Ensembl; ENST00000263025; ENSP00000263025; ENSG00000102882. [P27361-1]
Ensembl; ENST00000322266; ENSP00000327293; ENSG00000102882. [P27361-2]
Ensembl; ENST00000395199; ENSP00000378625; ENSG00000102882. [P27361-3]
Ensembl; ENST00000395202; ENSP00000378628; ENSG00000102882. [P27361-2]
GeneID; 5595; -.
KEGG; hsa:5595; -.
UCSC; uc002dws.4; human. [P27361-1]
CTD; 5595; -.
DisGeNET; 5595; -.
EuPathDB; HostDB:ENSG00000102882.11; -.
GeneCards; MAPK3; -.
HGNC; HGNC:6877; MAPK3.
HPA; CAB002683; -.
HPA; HPA003995; -.
HPA; HPA005700; -.
HPA; HPA030069; -.
MIM; 601795; gene.
neXtProt; NX_P27361; -.
OpenTargets; ENSG00000102882; -.
PharmGKB; PA30622; -.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00550000074298; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P27361; -.
KO; K04371; -.
OMA; AYGMVSS; -.
OrthoDB; EOG091G08QL; -.
PhylomeDB; P27361; -.
TreeFam; TF105097; -.
BRENDA; 2.7.11.24; 2681.
Reactome; R-HSA-110056; MAPK3 (ERK1) activation.
Reactome; R-HSA-112409; RAF-independent MAPK1/3 activation.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
Reactome; R-HSA-198753; ERK/MAPK targets.
Reactome; R-HSA-202670; ERKs are inactivated.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
Reactome; R-HSA-445144; Signal transduction by L1.
Reactome; R-HSA-450341; Activation of the AP-1 family of transcription factors.
Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-5674499; Negative feedback regulation of MAPK pathway.
Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
Reactome; R-HSA-74749; Signal attenuation.
Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-HSA-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
SignaLink; P27361; -.
SIGNOR; P27361; -.
EvolutionaryTrace; P27361; -.
GeneWiki; MAPK3; -.
GenomeRNAi; 5595; -.
PRO; PR:P27361; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000102882; -.
CleanEx; HS_MAPK3; -.
ExpressionAtlas; P27361; baseline and differential.
Genevisible; P27361; HS.
GO; GO:0005901; C:caveola; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:UniProtKB.
GO; GO:0005769; C:early endosome; TAS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; TAS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB.
GO; GO:0005770; C:late endosome; TAS:UniProtKB.
GO; GO:0005739; C:mitochondrion; TAS:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; TAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0031143; C:pseudopodium; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
GO; GO:0004708; F:MAP kinase kinase activity; IEA:Ensembl.
GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0019369; P:arachidonic acid metabolic process; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
GO; GO:0030509; P:BMP signaling pathway; IMP:BHF-UCL.
GO; GO:0061308; P:cardiac neural crest cell development involved in heart development; IEA:Ensembl.
GO; GO:0051216; P:cartilage development; IEA:Ensembl.
GO; GO:0072584; P:caveolin-mediated endocytosis; TAS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0034198; P:cellular response to amino acid starvation; IDA:CAFA.
GO; GO:0071276; P:cellular response to cadmium ion; IMP:CAFA.
GO; GO:1903351; P:cellular response to dopamine; IMP:CAFA.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:CAFA.
GO; GO:0006975; P:DNA damage induced protein phosphorylation; IDA:UniProtKB.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0060324; P:face development; IEA:Ensembl.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; TAS:Reactome.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
GO; GO:0060425; P:lung morphogenesis; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0000189; P:MAPK import into nucleus; IEA:Ensembl.
GO; GO:2000657; P:negative regulation of apolipoprotein binding; IEA:Ensembl.
GO; GO:0042473; P:outer ear morphogenesis; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:UniProtKB.
GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0031281; P:positive regulation of cyclase activity; IMP:CACAO.
GO; GO:0002741; P:positive regulation of cytokine secretion involved in immune response; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:CAFA.
GO; GO:0035066; P:positive regulation of histone acetylation; IMP:BHF-UCL.
GO; GO:0033129; P:positive regulation of histone phosphorylation; IMP:BHF-UCL.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IEA:Ensembl.
GO; GO:1905050; P:positive regulation of metallopeptidase activity; IEA:Ensembl.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL.
GO; GO:1904355; P:positive regulation of telomere capping; IMP:BHF-UCL.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
GO; GO:1904417; P:positive regulation of xenophagy; IEA:Ensembl.
GO; GO:0006461; P:protein complex assembly; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0030641; P:regulation of cellular pH; IEA:Ensembl.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0051493; P:regulation of cytoskeleton organization; TAS:UniProtKB.
GO; GO:2000641; P:regulation of early endosome to late endosome transport; TAS:UniProtKB.
GO; GO:0090170; P:regulation of Golgi inheritance; TAS:UniProtKB.
GO; GO:0030278; P:regulation of ossification; IEA:Ensembl.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; TAS:Reactome.
GO; GO:0032872; P:regulation of stress-activated MAPK cascade; TAS:UniProtKB.
GO; GO:0070849; P:response to epidermal growth factor; IDA:UniProtKB.
GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0051403; P:stress-activated MAPK cascade; IDA:CAFA.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
GO; GO:0030878; P:thyroid gland development; IEA:Ensembl.
GO; GO:0060440; P:trachea formation; IEA:Ensembl.
GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008349; MAPK_ERK1/2.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01770; ERK1ERK2MAPK.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
ATP-binding; Cell cycle; Complete proteome; Cytoplasm;
Direct protein sequencing; Host-virus interaction; Kinase; Membrane;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
CHAIN 2 379 Mitogen-activated protein kinase 3.
/FTId=PRO_0000186251.
DOMAIN 42 330 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 48 56 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 202 204 TXY.
ACT_SITE 166 166 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 71 71 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
MOD_RES 198 198 Phosphothreonine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 202 202 Phosphothreonine; by MAP2K1 and MAP2K2.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 204 204 Phosphotyrosine; by MAP2K1 and MAP2K2.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:18983981,
ECO:0000269|PubMed:19494114}.
MOD_RES 207 207 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:19060905}.
MOD_RES 263 263 Phosphoserine.
{ECO:0000250|UniProtKB:P28482}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000250|UniProtKB:P28482}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000250|UniProtKB:P28482}.
VAR_SEQ 259 302 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_041906.
VAR_SEQ 340 379 PVAEEPFTFAMELDDLPKERLKELIFQETARFQPGVLEAP
-> VGQSPAAVGLGAGEQGGT (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_041907.
VARIANT 323 323 E -> K (in dbSNP:rs55859133).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042253.
CONFLICT 174 174 I -> S (in Ref. 1; CAA42744 and 2;
AAK52329). {ECO:0000305}.
STRAND 29 31 {ECO:0000244|PDB:4QTB}.
STRAND 34 36 {ECO:0000244|PDB:4QTB}.
TURN 39 41 {ECO:0000244|PDB:4QTB}.
STRAND 42 51 {ECO:0000244|PDB:4QTB}.
STRAND 54 61 {ECO:0000244|PDB:4QTB}.
TURN 62 65 {ECO:0000244|PDB:4QTB}.
STRAND 66 73 {ECO:0000244|PDB:4QTB}.
HELIX 79 94 {ECO:0000244|PDB:4QTB}.
STRAND 105 107 {ECO:0000244|PDB:4QTB}.
TURN 112 114 {ECO:0000244|PDB:4QTB}.
STRAND 118 122 {ECO:0000244|PDB:4QTB}.
STRAND 126 128 {ECO:0000244|PDB:4QTB}.
HELIX 129 135 {ECO:0000244|PDB:4QTB}.
HELIX 140 159 {ECO:0000244|PDB:4QTB}.
HELIX 169 171 {ECO:0000244|PDB:4QTB}.
STRAND 172 174 {ECO:0000244|PDB:4QTB}.
STRAND 180 182 {ECO:0000244|PDB:4QTB}.
HELIX 193 195 {ECO:0000244|PDB:4QTB}.
HELIX 208 210 {ECO:0000244|PDB:4QTB}.
HELIX 213 215 {ECO:0000244|PDB:4QTB}.
TURN 216 218 {ECO:0000244|PDB:4QTB}.
HELIX 225 240 {ECO:0000244|PDB:4QTB}.
HELIX 250 261 {ECO:0000244|PDB:4QTB}.
HELIX 266 269 {ECO:0000244|PDB:4QTB}.
HELIX 275 282 {ECO:0000244|PDB:4QTB}.
HELIX 292 295 {ECO:0000244|PDB:4QTB}.
HELIX 301 310 {ECO:0000244|PDB:4QTB}.
HELIX 315 317 {ECO:0000244|PDB:4QTB}.
HELIX 321 325 {ECO:0000244|PDB:4QTB}.
HELIX 328 330 {ECO:0000244|PDB:4QTB}.
TURN 331 333 {ECO:0000244|PDB:4QTB}.
HELIX 336 338 {ECO:0000244|PDB:4QTB}.
HELIX 350 354 {ECO:0000244|PDB:4QTB}.
HELIX 357 368 {ECO:0000244|PDB:4QTB}.
HELIX 369 371 {ECO:0000244|PDB:4QTB}.
SEQUENCE 379 AA; 43136 MW; E6020CE413EC41F7 CRC64;
MAAAAAQGGG GGEPRRTEGV GPGVPGEVEM VKGQPFDVGP RYTQLQYIGE GAYGMVSSAY
DHVRKTRVAI KKISPFEHQT YCQRTLREIQ ILLRFRHENV IGIRDILRAS TLEAMRDVYI
VQDLMETDLY KLLKSQQLSN DHICYFLYQI LRGLKYIHSA NVLHRDLKPS NLLINTTCDL
KICDFGLARI ADPEHDHTGF LTEYVATRWY RAPEIMLNSK GYTKSIDIWS VGCILAEMLS
NRPIFPGKHY LDQLNHILGI LGSPSQEDLN CIINMKARNY LQSLPSKTKV AWAKLFPKSD
SKALDLLDRM LTFNPNKRIT VEEALAHPYL EQYYDPTDEP VAEEPFTFAM ELDDLPKERL
KELIFQETAR FQPGVLEAP


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