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Mitogen-activated protein kinase 1 (MAP kinase 1) (MAPK 1) (EC 2.7.11.24) (ERT1) (Extracellular signal-regulated kinase 2) (ERK-2) (MAP kinase isoform p42) (p42-MAPK) (Mitogen-activated protein kinase 2) (MAP kinase 2) (MAPK 2)

 MK01_HUMAN              Reviewed;         360 AA.
P28482; A8CZ64;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 208.
RecName: Full=Mitogen-activated protein kinase 1;
Short=MAP kinase 1;
Short=MAPK 1;
EC=2.7.11.24;
AltName: Full=ERT1;
AltName: Full=Extracellular signal-regulated kinase 2;
Short=ERK-2;
AltName: Full=MAP kinase isoform p42;
Short=p42-MAPK;
AltName: Full=Mitogen-activated protein kinase 2;
Short=MAP kinase 2;
Short=MAPK 2;
Name=MAPK1; Synonyms=ERK2, PRKM1, PRKM2;
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).
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
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 [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
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]
PROTEIN SEQUENCE OF 2-15, AND ACETYLATION AT ALA-2.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[7]
FUNCTION IN PHOSPHORYLATION OF ERF.
PubMed=7588608;
Sgouras D.N., Athanasiou M.A., Beal G.J. Jr., Fisher R.J., Blair D.G.,
Mavrothalassitis G.J.;
"ERF: an ETS domain protein with strong transcriptional repressor
activity, can suppress ets-associated tumorigenesis and is regulated
by phosphorylation during cell cycle and mitogenic stimulation.";
EMBO J. 14:4781-4793(1995).
[8]
FUNCTION IN PHOSPHORYLATION OF MAPKAPK3.
PubMed=8622688; DOI=10.1128/MCB.16.3.868;
Sithanandam G., Latif F., Duh F.-M., Bernal R., Smola U., Li H.,
Kuzmin I., Wixler V., Geil L., Shrestha S., Lloyd P.A., Bader S.,
Sekido Y., Tartof K.D., Kashuba V.I., Zabarovsky E.R., Dean M.,
Klein G., Lerman M.I., Minna J.D., Rapp U.R., Allikmets R.;
"3pK, a new mitogen-activated protein kinase-activated protein kinase
located in the small cell lung cancer tumor suppressor gene region.";
Mol. Cell. Biol. 16:868-876(1996).
[9]
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).
[10]
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).
[11]
FUNCTION IN PHOSPHORYLATION OF RPS6KA5/MSK1.
PubMed=9687510; DOI=10.1093/emboj/17.15.4426;
Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.;
"Mitogen- and stress-activated protein kinase-1 (MSK1) is directly
activated by MAPK and SAPK2/p38, and may mediate activation of CREB.";
EMBO J. 17:4426-4441(1998).
[12]
FUNCTION IN PHOSPHORYLATION OF BCL6.
PubMed=9649500; DOI=10.1101/gad.12.13.1953;
Niu H., Ye B.H., Dalla-Favera R.;
"Antigen receptor signaling induces MAP kinase-mediated
phosphorylation and degradation of the BCL-6 transcription factor.";
Genes Dev. 12:1953-1961(1998).
[13]
INTERACTION WITH DUSP6, AND FUNCTION.
PubMed=9596579; DOI=10.1126/science.280.5367.1262;
Camps M., Nichols A., Gillieron C., Antonsson B., Muda M., Chabert C.,
Boschert U., Arkinstall S.;
"Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-
activated protein kinase.";
Science 280:1262-1265(1998).
[14]
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).
[15]
FUNCTION IN PHOSPHORYLATION OF ELK1.
PubMed=10637505; DOI=10.1038/sj.onc.1203362;
Cruzalegui F.H., Cano E., Treisman R.;
"ERK activation induces phosphorylation of Elk-1 at multiple S/T-P
motifs to high stoichiometry.";
Oncogene 18:7948-7957(1999).
[16]
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).
[17]
FUNCTION AS MKNK2 KINASE.
PubMed=11154262; DOI=10.1128/MCB.21.3.743-754.2001;
Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.;
"The mitogen-activated protein kinase signal-integrating kinase Mnk2
is a eukaryotic initiation factor 4E kinase with high levels of basal
activity in mammalian cells.";
Mol. Cell. Biol. 21:743-754(2001).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
FUNCTION IN PHOSPHORYLATION OF DUSP16.
PubMed=12794087; DOI=10.1074/jbc.M213254200;
Masuda K., Shima H., Katagiri C., Kikuchi K.;
"Activation of ERK induces phosphorylation of MAPK phosphatase-7, a
JNK specific phosphatase, at Ser-446.";
J. Biol. Chem. 278:32448-32456(2003).
[23]
FUNCTION IN PHOSPHORYLATION OF CASP9.
PubMed=12792650; DOI=10.1038/ncb1005;
Allan L.A., Morrice N., Brady S., Magee G., Pathak S., Clarke P.R.;
"Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK
MAPK.";
Nat. Cell Biol. 5:647-654(2003).
[24]
SUBCELLULAR LOCATION, AND INTERACTION WITH NEK2.
PubMed=15358203; DOI=10.1016/j.bbrc.2004.06.171;
Lou Y., Xie W., Zhang D.F., Yao J.H., Luo Z.F., Wang Y.Z., Shi Y.Y.,
Yao X.B.;
"Nek2A specifies the centrosomal localization of Erk2.";
Biochem. Biophys. Res. Commun. 321:495-501(2004).
[25]
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).
[26]
FUNCTION IN PHOSPHORYLATION OF SORBS3.
PubMed=15184391; DOI=10.1074/jbc.M402304200;
Mitsushima M., Suwa A., Amachi T., Ueda K., Kioka N.;
"Extracellular signal-regulated kinase activated by epidermal growth
factor and cell adhesion interacts with and phosphorylates vinexin.";
J. Biol. Chem. 279:34570-34577(2004).
[27]
FUNCTION IN PHOSPHORYLATION OF MCL1.
PubMed=15241487; DOI=10.1038/sj.onc.1207692;
Domina A.M., Vrana J.A., Gregory M.A., Hann S.R., Craig R.W.;
"MCL1 is phosphorylated in the PEST region and stabilized upon ERK
activation in viable cells, and at additional sites with cytotoxic
okadaic acid or taxol.";
Oncogene 23:5301-5315(2004).
[28]
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).
[29]
FUNCTION IN PHOSPHORYLATION OF DAPK1, SUBCELLULAR LOCATION, AND
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).
[30]
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).
[31]
FUNCTION IN PHOSPHORYLATION OF RAF1.
PubMed=15664191; DOI=10.1016/j.molcel.2004.11.055;
Dougherty M.K., Muller J., Ritt D.A., Zhou M., Zhou X.Z.,
Copeland T.D., Conrads T.P., Veenstra T.D., Lu K.P., Morrison D.K.;
"Regulation of Raf-1 by direct feedback phosphorylation.";
Mol. Cell 17:215-224(2005).
[32]
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).
[33]
INTERACTION WITH ARHGEF2.
PubMed=18211802; DOI=10.1016/j.bbrc.2008.01.066;
Fujishiro S.H., Tanimura S., Mure S., Kashimoto Y., Watanabe K.,
Kohno M.;
"ERK1/2 phosphorylate GEF-H1 to enhance its guanine nucleotide
exchange activity toward RhoA.";
Biochem. Biophys. Res. Commun. 368:162-167(2008).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
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).
[39]
PHOSPHORYLATION AT SER-246 AND SER-248, INTERACTION WITH IPO7, AND
SUBCELLULAR LOCATION.
PubMed=18760948; DOI=10.1016/j.molcel.2008.08.007;
Chuderland D., Konson A., Seger R.;
"Identification and characterization of a general nuclear
translocation signal in signaling proteins.";
Mol. Cell 31:850-861(2008).
[40]
FUNCTION IN PHOSPHORYLATION OF TPR, INTERACTION WITH TPR, AND
MUTAGENESIS OF LYS-54; 176-PRO--ASP-179; THR-185; TYR-187; LEU-234;
ASP-318 AND ASP-321.
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).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, 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).
[42]
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).
[43]
FUNCTION AS A TRANSCRIPTIONAL REPRESSOR, AND DNA-BINDING.
PubMed=19879846; DOI=10.1016/j.cell.2009.08.037;
Hu S., Xie Z., Onishi A., Yu X., Jiang L., Lin J., Rho H.-S.,
Woodard C., Wang H., Jeong J.-S., Long S., He X., Wade H.,
Blackshaw S., Qian J., Zhu H.;
"Profiling the human protein-DNA interactome reveals ERK2 as a
transcriptional repressor of interferon signaling.";
Cell 139:610-622(2009).
[44]
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).
[45]
PHOSPHORYLATION AT TYR-187, DEPHOSPHORYLATION AT TYR-187 BY PTPRJ, AND
MUTAGENESIS OF ASP-318.
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).
[46]
PHOSPHORYLATION AT SER-29 BY SGK1, AND 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).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, 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).
[48]
PHOSPHORYLATION AT THR-190, 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).
[49]
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).
[50]
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).
[51]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, 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).
[52]
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).
[53]
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).
[54]
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).
[55]
FUNCTION, AND INTERACTION WITH PML.
PubMed=22033920; DOI=10.1074/jbc.M111.289512;
Lim J.H., Liu Y., Reineke E., Kao H.Y.;
"Mitogen-activated protein kinase extracellular signal-regulated
kinase 2 phosphorylates and promotes Pin1 protein-dependent
promyelocytic leukemia protein turnover.";
J. Biol. Chem. 286:44403-44411(2011).
[56]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, 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).
[57]
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).
[58]
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).
[59]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185 AND TYR-187, 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).
[60]
INTERACTION WITH STYX.
PubMed=23847209; DOI=10.1073/pnas.1301985110;
Reiterer V., Fey D., Kolch W., Kholodenko B.N., Farhan H.;
"Pseudophosphatase STYX modulates cell-fate decisions and cell
migration by spatiotemporal regulation of ERK1/2.";
Proc. Natl. Acad. Sci. U.S.A. 110:E2934-2943(2013).
[61]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[62]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=9827991; DOI=10.1002/pro.5560071102;
Fox T., Coll J.T., Xie X., Ford P.J., Germann U.A., Porter M.D.,
Pazhanisamy S., Fleming M.A., Galullo V., Su M.S., Wilson K.P.;
"A single amino acid substitution makes ERK2 susceptible to pyridinyl
imidazole inhibitors of p38 MAP kinase.";
Protein Sci. 7:2249-2255(1998).
[63]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=16139248; DOI=10.1016/j.bbrc.2005.08.082;
Ohori M., Kinoshita T., Okubo M., Sato K., Yamazaki A., Arakawa H.,
Nishimura S., Inamura N., Nakajima H., Neya M., Miyake H., Fujii T.;
"Identification of a selective ERK inhibitor and structural
determination of the inhibitor-ERK2 complex.";
Biochem. Biophys. Res. Commun. 336:357-363(2005).
[64]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=16242327; DOI=10.1016/j.bmcl.2005.09.055;
Kinoshita T., Warizaya M., Ohori M., Sato K., Neya M., Fujii T.;
"Crystal structure of human ERK2 complexed with a pyrazolo[3,4-
c]pyridazine derivative.";
Bioorg. Med. Chem. Lett. 16:55-58(2006).
[65]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=17194451; DOI=10.1016/j.bbrc.2006.12.083;
Ohori M., Kinoshita T., Yoshimura S., Warizaya M., Nakajima H.,
Miyake H.;
"Role of a cysteine residue in the active site of ERK and the MAPKK
family.";
Biochem. Biophys. Res. Commun. 353:633-637(2007).
[66]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-359 IN COMPLEX WITH
INHIBITOR.
PubMed=17300186; DOI=10.1021/jm061381f;
Aronov A.M., Baker C., Bemis G.W., Cao J., Chen G., Ford P.J.,
Germann U.A., Green J., Hale M.R., Jacobs M., Janetka J.W.,
Maltais F., Martinez-Botella G., Namchuk M.N., Straub J., Tang Q.,
Xie X.;
"Flipped out: structure-guided design of selective pyrazolylpyrrole
ERK inhibitors.";
J. Med. Chem. 50:1280-1287(2007).
[67]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 186-191, AND PHOSPHORYLATION
AT TYR-187.
PubMed=19053285; DOI=10.1021/bi801724n;
Critton D.A., Tortajada A., Stetson G., Peti W., Page R.;
"Structural basis of substrate recognition by hematopoietic tyrosine
phosphatase.";
Biochemistry 47:13336-13345(2008).
[68]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=19827834; DOI=10.1021/jm900630q;
Aronov A.M., Tang Q., Martinez-Botella G., Bemis G.W., Cao J.,
Chen G., Ewing N.P., Ford P.J., Germann U.A., Green J., Hale M.R.,
Jacobs M., Janetka J.W., Maltais F., Markland W., Namchuk M.N.,
Nanthakumar S., Poondru S., Straub J., ter Haar E., Xie X.;
"Structure-guided design of potent and selective pyrimidylpyrrole
inhibitors of extracellular signal-regulated kinase (ERK) using
conformational control.";
J. Med. Chem. 52:6362-6368(2009).
-!- 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, DCC, 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. Mediates phosphorylation of TPR in respons to EGF
stimulation. May play a role in the spindle assembly checkpoint.
Phosphorylates PML and promotes its interaction with PIN1, leading
to PML degradation. Phosphorylates CDK2AP2 (By similarity).
{ECO:0000250|UniProtKB:P63086, ECO:0000269|PubMed:10617468,
ECO:0000269|PubMed:10637505, ECO:0000269|PubMed:11154262,
ECO:0000269|PubMed:12110590, ECO:0000269|PubMed:12356731,
ECO:0000269|PubMed:12792650, ECO:0000269|PubMed:12794087,
ECO:0000269|PubMed:12974390, ECO:0000269|PubMed:15184391,
ECO:0000269|PubMed:15241487, ECO:0000269|PubMed:15616583,
ECO:0000269|PubMed:15664191, ECO:0000269|PubMed:15788397,
ECO:0000269|PubMed:15952796, ECO:0000269|PubMed:16581800,
ECO:0000269|PubMed:18794356, ECO:0000269|PubMed:19265199,
ECO:0000269|PubMed:19879846, ECO:0000269|PubMed:22033920,
ECO:0000269|PubMed:7588608, ECO:0000269|PubMed:8622688,
ECO:0000269|PubMed:9480836, ECO:0000269|PubMed:9596579,
ECO:0000269|PubMed:9649500, ECO:0000269|PubMed:9687510,
ECO:0000303|PubMed:15526160, ECO:0000303|PubMed:16393692,
ECO:0000303|PubMed:19565474, ECO:0000303|PubMed:21779493}.
-!- FUNCTION: Acts as a transcriptional repressor. Binds to a
[GC]AAA[GC] consensus sequence. Repress the expression of
interferon gamma-induced genes. Seems to bind to the promoter of
CCL5, DMP1, IFIH1, IFITM1, IRF7, IRF9, LAMP3, OAS1, OAS2, OAS3 and
STAT1. Transcriptional activity is independent of kinase activity.
{ECO:0000269|PubMed:19879846}.
-!- 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-185 and Tyr-187 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. Phosphorylation on Ser-29 by SGK1 results in its
activation by enhancing its interaction with MAP2K1/MEK1 and
MAP2K2/MEK2. Dephosphorylated and inactivated by DUSP3, DUSP6 and
DUSP9. Inactivated by pyrimidylpyrrole inhibitors.
{ECO:0000269|PubMed:12356731, ECO:0000269|PubMed:19060905}.
-!- SUBUNIT: Binds both upstream activators and downstream substrates
in multimolecular complexes. Binds to HIV-1 Nef through its SH3
domain. This interaction inhibits its tyrosine-kinase activity.
Interacts with ADAM15, ARHGEF2, ARRB2, DAPK1 (via death domain),
HSF4, IER3, IPO7, DUSP6, NISCH, SGK1, and isoform 1 of NEK2.
Interacts (phosphorylated form) with CAV2 ('Tyr-19'-phosphorylated
form); the interaction, promoted by insulin, leads to nuclear
location and MAPK1 activation. Interacts with MORG1, PEA15 and
MKNK2 (By similarity). MKNK2 isoform 1 binding prevents from
dephosphorylation and inactivation (By similarity). Interacts with
DCC (By similarity). The phosphorylated form interacts with PML
(isoform PML-4). Interacts with STYX. Interacts with CDK2AP2.
Interacts with CAVIN4 (By similarity).
{ECO:0000250|UniProtKB:P63085, ECO:0000250|UniProtKB:P63086,
ECO:0000269|PubMed:11912194, ECO:0000269|PubMed:12356731,
ECO:0000269|PubMed:15358203, ECO:0000269|PubMed:15616583,
ECO:0000269|PubMed:16139248, ECO:0000269|PubMed:16242327,
ECO:0000269|PubMed:16581800, ECO:0000269|PubMed:17194451,
ECO:0000269|PubMed:17300186, ECO:0000269|PubMed:18211802,
ECO:0000269|PubMed:18296648, ECO:0000269|PubMed:18435604,
ECO:0000269|PubMed:18760948, ECO:0000269|PubMed:18794356,
ECO:0000269|PubMed:19060905, ECO:0000269|PubMed:19447520,
ECO:0000269|PubMed:19827834, ECO:0000269|PubMed:22033920,
ECO:0000269|PubMed:23847209, ECO:0000269|PubMed:8794306,
ECO:0000269|PubMed:9596579, ECO:0000269|PubMed:9827991}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-959949, EBI-959949;
P32121:ARRB2; NbExp=3; IntAct=EBI-959949, EBI-714559;
P53004:BLVRA; NbExp=2; IntAct=EBI-959949, EBI-7410441;
Q9U1H0:cic (xeno); NbExp=2; IntAct=EBI-959949, EBI-98330;
Q7L5N1:COPS6; NbExp=2; IntAct=EBI-959949, EBI-486838;
P28562:DUSP1; NbExp=4; IntAct=EBI-959949, EBI-975493;
Q05922:Dusp2 (xeno); NbExp=2; IntAct=EBI-959949, EBI-7898692;
Q16690:DUSP5; NbExp=4; IntAct=EBI-959949, EBI-7487376;
P14921:ETS1; NbExp=3; IntAct=EBI-959949, EBI-913209;
Q02750:MAP2K1; NbExp=2; IntAct=EBI-959949, EBI-492564;
Q16539-3:MAPK14; NbExp=5; IntAct=EBI-959949, EBI-6932370;
P27361:MAPK3; NbExp=3; IntAct=EBI-959949, EBI-73995;
P02687:MBP (xeno); NbExp=2; IntAct=EBI-959949, EBI-908215;
Q15121:PEA15; NbExp=3; IntAct=EBI-959949, EBI-714410;
P35813:PPM1A; NbExp=19; IntAct=EBI-959949, EBI-989143;
P35236:PTPN7; NbExp=6; IntAct=EBI-959949, EBI-2265723;
Q12913:PTPRJ; NbExp=7; IntAct=EBI-959949, EBI-2264500;
Q15256:PTPRR; NbExp=3; IntAct=EBI-959949, EBI-2265659;
Q15349:RPS6KA2; NbExp=4; IntAct=EBI-959949, EBI-1384149;
P51812:RPS6KA3; NbExp=3; IntAct=EBI-959949, EBI-1046616;
P29353-2:SHC1; NbExp=4; IntAct=EBI-959949, EBI-1000553;
Q69559:U24 (xeno); NbExp=2; IntAct=EBI-959949, EBI-8015758;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
{ECO:0000250}. Nucleus. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome. Cytoplasm. Membrane, caveola
{ECO:0000250|UniProtKB:P63086}. Note=Associated with the spindle
during prometaphase and metaphase (By similarity). PEA15-binding
and phosphorylated DAPK1 promote its cytoplasmic retention.
Phosphorylation at Ser- 246 and Ser-248 as well as
autophosphorylation at Thr-190 promote nuclear localization.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P28482-1; Sequence=Displayed;
Name=2;
IsoId=P28482-2; Sequence=VSP_047815;
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Phosphorylated upon KIT and FLT3 signaling (By similarity).
Dually phosphorylated on Thr-185 and Tyr-187, which activates the
enzyme. Undergoes regulatory phosphorylation on additional
residues such as Ser-246 and Ser-248 in the kinase insert domain
(KID) These phosphorylations, which are probably mediated by more
than one kinase, are important for binding of MAPK1/ERK2 to
importin-7 (IPO7) and its nuclear translocation. In addition,
autophosphorylation of Thr-190 was shown to affect the subcellular
localization of MAPK1/ERK2 as well. Ligand-activated ALK induces
tyrosine phosphorylation. Dephosphorylated by PTPRJ at Tyr-187.
Phosphorylation on Ser-29 by SGK1 results in its activation by
enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. DUSP3
and DUSP6 dephosphorylate specifically MAPK1/ERK2 and MAPK3/ERK1
whereas DUSP9 dephosphorylates a broader range of MAPKs.
{ECO:0000250, ECO:0000269|PubMed:17274988,
ECO:0000269|PubMed:18760948, ECO:0000269|PubMed:19053285,
ECO:0000269|PubMed:19060905, ECO:0000269|PubMed:19265199,
ECO:0000269|PubMed:19447520, ECO:0000269|PubMed:19494114}.
-!- PTM: ISGylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA77753.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Extracellular signal-regulated
kinase entry;
URL="https://en.wikipedia.org/wiki/Extracellular_signal-regulated_kinase";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MAPK1ID41288ch22q11.html";
-----------------------------------------------------------------------
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EMBL; M84489; AAA58459.1; -; mRNA.
EMBL; Z11694; CAA77752.1; -; mRNA.
EMBL; Z11695; CAA77753.1; ALT_INIT; mRNA.
EMBL; DQ399292; ABD60303.1; -; mRNA.
EMBL; AP000553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017832; AAH17832.1; -; mRNA.
CCDS; CCDS13795.1; -. [P28482-1]
PIR; JQ1400; JQ1400.
RefSeq; NP_002736.3; NM_002745.4. [P28482-1]
RefSeq; NP_620407.1; NM_138957.3. [P28482-1]
UniGene; Hs.431850; -.
PDB; 1PME; X-ray; 2.00 A; A=1-360.
PDB; 1TVO; X-ray; 2.50 A; A=1-360.
PDB; 1WZY; X-ray; 2.50 A; A=1-360.
PDB; 2OJG; X-ray; 2.00 A; A=2-360.
PDB; 2OJI; X-ray; 2.60 A; A=2-360.
PDB; 2OJJ; X-ray; 2.40 A; A=2-360.
PDB; 2Y9Q; X-ray; 1.55 A; A=1-360.
PDB; 3D42; X-ray; 2.46 A; B=184-191.
PDB; 3D44; X-ray; 1.90 A; B=184-191.
PDB; 3I5Z; X-ray; 2.20 A; A=1-360.
PDB; 3I60; X-ray; 2.50 A; A=1-360.
PDB; 3SA0; X-ray; 1.59 A; A=1-360.
PDB; 3TEI; X-ray; 2.40 A; A=1-360.
PDB; 3W55; X-ray; 3.00 A; A=1-360.
PDB; 4FMQ; X-ray; 2.10 A; A=1-360.
PDB; 4FUX; X-ray; 2.20 A; A=1-360.
PDB; 4FUY; X-ray; 2.00 A; A=1-360.
PDB; 4FV0; X-ray; 2.10 A; A=1-360.
PDB; 4FV1; X-ray; 1.99 A; A=1-360.
PDB; 4FV2; X-ray; 2.00 A; A=1-360.
PDB; 4FV3; X-ray; 2.20 A; A=1-360.
PDB; 4FV4; X-ray; 2.50 A; A=1-360.
PDB; 4FV5; X-ray; 2.40 A; A=1-360.
PDB; 4FV6; X-ray; 2.50 A; A=1-360.
PDB; 4FV7; X-ray; 1.90 A; A=1-360.
PDB; 4FV8; X-ray; 2.00 A; A=1-360.
PDB; 4FV9; X-ray; 2.11 A; A=1-360.
PDB; 4G6N; X-ray; 2.00 A; A=1-360.
PDB; 4G6O; X-ray; 2.20 A; A=1-360.
PDB; 4H3P; X-ray; 2.30 A; A/D=1-360.
PDB; 4H3Q; X-ray; 2.20 A; A=1-360.
PDB; 4IZ5; X-ray; 3.19 A; A/B/C/D=8-360.
PDB; 4IZ7; X-ray; 1.80 A; A/C=8-360.
PDB; 4IZA; X-ray; 1.93 A; A/C=8-360.
PDB; 4N0S; X-ray; 1.80 A; A=1-360.
PDB; 4NIF; X-ray; 2.15 A; B/E=1-360.
PDB; 4O6E; X-ray; 1.95 A; A=13-360.
PDB; 4QP1; X-ray; 2.70 A; A/B=1-360.
PDB; 4QP2; X-ray; 2.23 A; A/B=1-360.
PDB; 4QP3; X-ray; 2.60 A; A/B=1-360.
PDB; 4QP4; X-ray; 2.20 A; A/B=1-360.
PDB; 4QP6; X-ray; 3.10 A; A/B=1-360.
PDB; 4QP7; X-ray; 2.25 A; A/B=1-360.
PDB; 4QP8; X-ray; 2.45 A; A/B=1-360.
PDB; 4QP9; X-ray; 2.00 A; A=1-360.
PDB; 4QPA; X-ray; 2.85 A; A/B=1-360.
PDB; 4QTA; X-ray; 1.45 A; A=1-360.
PDB; 4QTE; X-ray; 1.50 A; A=1-360.
PDB; 4XJ0; X-ray; 2.58 A; A/B=12-360.
PDB; 4ZXT; X-ray; 2.00 A; A=1-360.
PDB; 4ZZM; X-ray; 1.89 A; A=11-360.
PDB; 4ZZN; X-ray; 1.33 A; A=11-360.
PDB; 4ZZO; X-ray; 1.63 A; A=11-360.
PDB; 5AX3; X-ray; 2.98 A; A=1-360.
PDB; 5BUE; X-ray; 2.40 A; A=2-360.
PDB; 5BUI; X-ray; 2.12 A; A=2-360.
PDB; 5BUJ; X-ray; 1.85 A; A=2-360.
PDB; 5BVD; X-ray; 1.90 A; A=2-360.
PDB; 5BVE; X-ray; 2.00 A; A=2-360.
PDB; 5BVF; X-ray; 1.90 A; A=2-360.
PDB; 5K4I; X-ray; 1.76 A; A=9-360.
PDB; 5LCJ; X-ray; 1.78 A; A=1-360.
PDB; 5LCK; X-ray; 1.89 A; A=1-360.
PDB; 5NGU; X-ray; 2.74 A; A=1-360.
PDB; 5NHF; X-ray; 2.14 A; A=1-360.
PDB; 5NHH; X-ray; 1.94 A; A=1-360.
PDB; 5NHJ; X-ray; 2.12 A; A=1-360.
PDB; 5NHL; X-ray; 2.07 A; A=1-360.
PDB; 5NHO; X-ray; 2.24 A; A=1-360.
PDB; 5NHP; X-ray; 1.99 A; A=1-360.
PDB; 5NHV; X-ray; 2.00 A; A=1-360.
PDB; 5V60; X-ray; 2.18 A; A=8-360.
PDB; 5V61; X-ray; 2.20 A; A=8-360.
PDB; 5V62; X-ray; 1.90 A; A=10-360.
PDBsum; 1PME; -.
PDBsum; 1TVO; -.
PDBsum; 1WZY; -.
PDBsum; 2OJG; -.
PDBsum; 2OJI; -.
PDBsum; 2OJJ; -.
PDBsum; 2Y9Q; -.
PDBsum; 3D42; -.
PDBsum; 3D44; -.
PDBsum; 3I5Z; -.
PDBsum; 3I60; -.
PDBsum; 3SA0; -.
PDBsum; 3TEI; -.
PDBsum; 3W55; -.
PDBsum; 4FMQ; -.
PDBsum; 4FUX; -.
PDBsum; 4FUY; -.
PDBsum; 4FV0; -.
PDBsum; 4FV1; -.
PDBsum; 4FV2; -.
PDBsum; 4FV3; -.
PDBsum; 4FV4; -.
PDBsum; 4FV5; -.
PDBsum; 4FV6; -.
PDBsum; 4FV7; -.
PDBsum; 4FV8; -.
PDBsum; 4FV9; -.
PDBsum; 4G6N; -.
PDBsum; 4G6O; -.
PDBsum; 4H3P; -.
PDBsum; 4H3Q; -.
PDBsum; 4IZ5; -.
PDBsum; 4IZ7; -.
PDBsum; 4IZA; -.
PDBsum; 4N0S; -.
PDBsum; 4NIF; -.
PDBsum; 4O6E; -.
PDBsum; 4QP1; -.
PDBsum; 4QP2; -.
PDBsum; 4QP3; -.
PDBsum; 4QP4; -.
PDBsum; 4QP6; -.
PDBsum; 4QP7; -.
PDBsum; 4QP8; -.
PDBsum; 4QP9; -.
PDBsum; 4QPA; -.
PDBsum; 4QTA; -.
PDBsum; 4QTE; -.
PDBsum; 4XJ0; -.
PDBsum; 4ZXT; -.
PDBsum; 4ZZM; -.
PDBsum; 4ZZN; -.
PDBsum; 4ZZO; -.
PDBsum; 5AX3; -.
PDBsum; 5BUE; -.
PDBsum; 5BUI; -.
PDBsum; 5BUJ; -.
PDBsum; 5BVD; -.
PDBsum; 5BVE; -.
PDBsum; 5BVF; -.
PDBsum; 5K4I; -.
PDBsum; 5LCJ; -.
PDBsum; 5LCK; -.
PDBsum; 5NGU; -.
PDBsum; 5NHF; -.
PDBsum; 5NHH; -.
PDBsum; 5NHJ; -.
PDBsum; 5NHL; -.
PDBsum; 5NHO; -.
PDBsum; 5NHP; -.
PDBsum; 5NHV; -.
PDBsum; 5V60; -.
PDBsum; 5V61; -.
PDBsum; 5V62; -.
ProteinModelPortal; P28482; -.
SMR; P28482; -.
BioGrid; 111580; 241.
CORUM; P28482; -.
DIP; DIP-519N; -.
ELM; P28482; -.
IntAct; P28482; 98.
MINT; MINT-144006; -.
STRING; 9606.ENSP00000215832; -.
BindingDB; P28482; -.
ChEMBL; CHEMBL4040; -.
DrugBank; DB07264; (S)-N-(1-(3-CHLORO-4-FLUOROPHENYL)-2-HYDROXYETHYL)-4-(4-(3-CHLOROPHENYL)-1H-PYRAZOL-3-YL)-1H-PYRROLE-2-CARBOXAMIDE.
DrugBank; DB08521; 4-[5-(4-FLUORO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-3H-IMIDAZOL-4-YL]-PYRIDINE.
DrugBank; DB08513; [4-({5-(AMINOCARBONYL)-4-[(3-METHYLPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)PHENYL]ACETIC ACID.
DrugBank; DB01169; Arsenic trioxide.
DrugBank; DB01064; Isoprenaline.
DrugBank; DB07010; N-BENZYL-4-[4-(3-CHLOROPHENYL)-1H-PYRAZOL-3-YL]-1H-PYRROLE-2-CARBOXAMIDE.
DrugBank; DB02116; Olomoucine.
DrugBank; DB02482; Phosphonothreonine.
DrugBank; DB02733; Purvalanol.
DrugBank; DB04338; SB220025.
DrugBank; DB11120; Turpentine.
GuidetoPHARMACOLOGY; 1495; -.
iPTMnet; P28482; -.
PhosphoSitePlus; P28482; -.
SwissPalm; P28482; -.
BioMuta; MAPK1; -.
DMDM; 119554; -.
OGP; P28482; -.
EPD; P28482; -.
PaxDb; P28482; -.
PeptideAtlas; P28482; -.
PRIDE; P28482; -.
DNASU; 5594; -.
Ensembl; ENST00000215832; ENSP00000215832; ENSG00000100030. [P28482-1]
Ensembl; ENST00000398822; ENSP00000381803; ENSG00000100030. [P28482-1]
Ensembl; ENST00000544786; ENSP00000440842; ENSG00000100030. [P28482-2]
GeneID; 5594; -.
KEGG; hsa:5594; -.
UCSC; uc010gtk.2; human. [P28482-1]
CTD; 5594; -.
DisGeNET; 5594; -.
EuPathDB; HostDB:ENSG00000100030.14; -.
GeneCards; MAPK1; -.
HGNC; HGNC:6871; MAPK1.
HPA; CAB004229; -.
HPA; HPA003995; -.
HPA; HPA005700; -.
HPA; HPA030069; -.
MalaCards; MAPK1; -.
MIM; 176948; gene.
neXtProt; NX_P28482; -.
OpenTargets; ENSG00000100030; -.
Orphanet; 261330; Distal 22q11.2 microdeletion syndrome.
PharmGKB; PA30616; -.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00900000140906; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P28482; -.
KO; K04371; -.
OMA; NCDLKLC; -.
OrthoDB; EOG091G08QL; -.
PhylomeDB; P28482; -.
TreeFam; TF105097; -.
BRENDA; 2.7.11.24; 2681.
Reactome; R-HSA-111995; phospho-PLA2 pathway.
Reactome; R-HSA-112409; RAF-independent MAPK1/3 activation.
Reactome; R-HSA-112411; MAPK1 (ERK2) activation.
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-437239; Recycling pathway of L1.
Reactome; R-HSA-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-HSA-444257; RSK activation.
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-6798695; Neutrophil degranulation.
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-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-8940973; RUNX2 regulates osteoblast differentiation.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
SignaLink; P28482; -.
SIGNOR; P28482; -.
ChiTaRS; MAPK1; human.
EvolutionaryTrace; P28482; -.
GeneWiki; MAPK1; -.
GenomeRNAi; 5594; -.
PRO; PR:P28482; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100030; -.
CleanEx; HS_MAPK1; -.
ExpressionAtlas; P28482; baseline and differential.
Genevisible; P28482; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005901; C:caveola; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:UniProtKB.
GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
GO; GO:0005769; C:early endosome; TAS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
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:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; TAS:UniProtKB.
GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
GO; GO:0004708; F:MAP kinase kinase activity; IEA:Ensembl.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; 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; IDA:UniProtKB.
GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
GO; GO:0061308; P:cardiac neural crest cell development involved in heart 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:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
GO; GO:1903351; P:cellular response to dopamine; IMP:CAFA.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:CAFA.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
GO; GO:0019858; P:cytosine metabolic process; IEA:Ensembl.
GO; GO:0015966; P:diadenosine tetraphosphate biosynthetic process; IEA:Ensembl.
GO; GO:0038127; P:ERBB signaling pathway; IDA:UniProtKB.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:UniProtKB.
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:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; TAS:Reactome.
GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
GO; GO:0007611; P:learning or memory; NAS:ARUK-UCL.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0060425; P:lung morphogenesis; IEA:Ensembl.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0042473; P:outer ear morphogenesis; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:UniProtKB.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:CAFA.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Ensembl.
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:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0045727; P:positive regulation of translation; 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:0031647; P:regulation of protein stability; ISS:UniProtKB.
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:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; ISS:ARUK-UCL.
GO; GO:0006950; P:response to stress; TAS:ProtInc.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0051403; P:stress-activated MAPK cascade; IDA:CAFA.
GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
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; Cytoskeleton;
Direct protein sequencing; DNA-binding; Host-virus interaction;
Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Serine/threonine-protein kinase;
Transcription; Transcription regulation; Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801}.
CHAIN 2 360 Mitogen-activated protein kinase 1.
/FTId=PRO_0000186247.
DOMAIN 25 313 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 31 39 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DNA_BIND 259 277
REGION 105 108 Inhibitor-binding.
REGION 153 154 Inhibitor-binding.
MOTIF 185 187 TXY.
MOTIF 318 322 Cytoplasmic retention motif.
MOTIF 327 333 Nuclear translocation motif.
COMPBIAS 2 9 Poly-Ala.
ACT_SITE 149 149 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 54 54 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 54 54 Inhibitor. {ECO:0000269|PubMed:16139248,
ECO:0000269|PubMed:16242327,
ECO:0000269|PubMed:17194451,
ECO:0000269|PubMed:17300186,
ECO:0000269|PubMed:19827834,
ECO:0000269|PubMed:9827991}.
BINDING 108 108 Inhibitor; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:16139248,
ECO:0000269|PubMed:16242327,
ECO:0000269|PubMed:17194451,
ECO:0000269|PubMed:17300186,
ECO:0000269|PubMed:19827834,
ECO:0000269|PubMed:9827991}.
BINDING 114 114 Inhibitor. {ECO:0000269|PubMed:16139248,
ECO:0000269|PubMed:16242327,
ECO:0000269|PubMed:17194451,
ECO:0000269|PubMed:17300186,
ECO:0000269|PubMed:19827834,
ECO:0000269|PubMed:9827991}.
BINDING 154 154 Inhibitor. {ECO:0000269|PubMed:16139248,
ECO:0000269|PubMed:16242327,
ECO:0000269|PubMed:17194451,
ECO:0000269|PubMed:17300186,
ECO:0000269|PubMed:19827834,
ECO:0000269|PubMed:9827991}.
BINDING 166 166 Inhibitor. {ECO:0000269|PubMed:16139248,
ECO:0000269|PubMed:16242327,
ECO:0000269|PubMed:17194451,
ECO:0000269|PubMed:17300186,
ECO:0000269|PubMed:19827834,
ECO:0000269|PubMed:9827991}.
BINDING 167 167 Inhibitor. {ECO:0000269|PubMed:16139248,
ECO:0000269|PubMed:16242327,
ECO:0000269|PubMed:17194451,
ECO:0000269|PubMed:17300186,
ECO:0000269|PubMed:19827834,
ECO:0000269|PubMed:9827991}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801}.
MOD_RES 29 29 Phosphoserine; by SGK1.
{ECO:0000269|PubMed:19447520}.
MOD_RES 181 181 Phosphothreonine.
{ECO:0000250|UniProtKB:P27361}.
MOD_RES 185 185 Phosphothreonine; by MAP2K1 and MAP2K2.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 187 187 Phosphotyrosine; by MAP2K1 and MAP2K2.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19053285,
ECO:0000269|PubMed:19494114}.
MOD_RES 190 190 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:19060905}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000269|PubMed:18760948}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000269|PubMed:18760948}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
VAR_SEQ 242 285 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_047815.
MUTAGEN 54 54 K->R: Does not inhibit interaction with
MAP2K1. {ECO:0000269|PubMed:18794356}.
MUTAGEN 176 179 Missing: Inhibits homodimerization and
interaction with TPR.
{ECO:0000269|PubMed:18794356}.
MUTAGEN 185 185 T->A: Inhibits interaction with TPR; when
associated with A-187.
{ECO:0000269|PubMed:18794356}.
MUTAGEN 187 187 Y->A: Inhibits interaction with TPR; when
associated with A-185.
{ECO:0000269|PubMed:18794356}.
MUTAGEN 234 234 L->A: Inhibits interaction with TPR.
{ECO:0000269|PubMed:18794356}.
MUTAGEN 318 318 D->A: Loss of dephosphorylation by PTPRJ.
{ECO:0000269|PubMed:18794356,
ECO:0000269|PubMed:19494114}.
MUTAGEN 318 318 D->N: Inhibits interaction with MAP2K1
but not with TPR; when associated with N-
321. {ECO:0000269|PubMed:18794356,
ECO:0000269|PubMed:19494114}.
MUTAGEN 321 321 D->N: Inhibits interaction with MAP2K1
but not with TPR; when associated with N-
318. {ECO:0000269|PubMed:18794356}.
CONFLICT 91 91 R -> Q (in Ref. 2; CAA77752).
{ECO:0000305}.
STRAND 12 14 {ECO:0000244|PDB:4QTA}.
STRAND 17 19 {ECO:0000244|PDB:4QTA}.
TURN 22 24 {ECO:0000244|PDB:4ZZN}.
STRAND 25 34 {ECO:0000244|PDB:4ZZN}.
STRAND 37 44 {ECO:0000244|PDB:4ZZN}.
TURN 45 48 {ECO:0000244|PDB:4ZZN}.
STRAND 49 56 {ECO:0000244|PDB:4ZZN}.
STRAND 59 61 {ECO:0000244|PDB:4G6O}.
HELIX 62 77 {ECO:0000244|PDB:4ZZN}.
STRAND 81 83 {ECO:0000244|PDB:5AX3}.
STRAND 88 90 {ECO:0000244|PDB:4ZZN}.
TURN 95 97 {ECO:0000244|PDB:4ZZN}.
STRAND 101 106 {ECO:0000244|PDB:4ZZN}.
STRAND 109 111 {ECO:0000244|PDB:4ZZN}.
HELIX 112 118 {ECO:0000244|PDB:4ZZN}.
HELIX 123 142 {ECO:0000244|PDB:4ZZN}.
HELIX 152 154 {ECO:0000244|PDB:4ZZN}.
STRAND 155 157 {ECO:0000244|PDB:4ZZN}.
TURN 159 161 {ECO:0000244|PDB:4IZ5}.
STRAND 163 165 {ECO:0000244|PDB:4ZZN}.
HELIX 168 170 {ECO:0000244|PDB:3I5Z}.
HELIX 176 178 {ECO:0000244|PDB:4ZZN}.
TURN 181 185 {ECO:0000244|PDB:2Y9Q}.
HELIX 191 193 {ECO:0000244|PDB:4ZZN}.
HELIX 196 200 {ECO:0000244|PDB:4ZZN}.
STRAND 201 203 {ECO:0000244|PDB:5K4I}.
HELIX 208 223 {ECO:0000244|PDB:4ZZN}.
HELIX 235 244 {ECO:0000244|PDB:4ZZN}.
HELIX 249 253 {ECO:0000244|PDB:4ZZN}.
HELIX 258 265 {ECO:0000244|PDB:4ZZN}.
HELIX 275 278 {ECO:0000244|PDB:4ZZN}.
STRAND 279 282 {ECO:0000244|PDB:5BUE}.
HELIX 284 293 {ECO:0000244|PDB:4ZZN}.
TURN 298 300 {ECO:0000244|PDB:4ZZN}.
HELIX 304 308 {ECO:0000244|PDB:4ZZN}.
HELIX 311 313 {ECO:0000244|PDB:4ZZN}.
TURN 314 316 {ECO:0000244|PDB:4ZZN}.
HELIX 319 321 {ECO:0000244|PDB:4ZZN}.
STRAND 331 333 {ECO:0000244|PDB:5AX3}.
HELIX 335 337 {ECO:0000244|PDB:5K4I}.
HELIX 340 351 {ECO:0000244|PDB:4ZZN}.
HELIX 352 354 {ECO:0000244|PDB:4ZZN}.
TURN 356 358 {ECO:0000244|PDB:1PME}.
SEQUENCE 360 AA; 41390 MW; E85D0B2A5D2D724E CRC64;
MAAAAAAGAG PEMVRGQVFD VGPRYTNLSY IGEGAYGMVC SAYDNVNKVR VAIKKISPFE
HQTYCQRTLR EIKILLRFRH ENIIGINDII RAPTIEQMKD VYIVQDLMET DLYKLLKTQH
LSNDHICYFL YQILRGLKYI HSANVLHRDL KPSNLLLNTT CDLKICDFGL ARVADPDHDH
TGFLTEYVAT RWYRAPEIML NSKGYTKSID IWSVGCILAE MLSNRPIFPG KHYLDQLNHI
LGILGSPSQE DLNCIINLKA RNYLLSLPHK NKVPWNRLFP NADSKALDLL DKMLTFNPHK
RIEVEQALAH PYLEQYYDPS DEPIAEAPFK FDMELDDLPK EKLKELIFEE TARFQPGYRS


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