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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.
12-AUG-2020, entry version 233.
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; DOI=10.1002/j.1460-2075.1995.tb00160.x;
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 (MICROBIAL INFECTION).
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 DUSP7.
PubMed=9788880;
Dowd S., Sneddon A.A., Keyse S.M.;
"Isolation of the human genes encoding the Pyst1 and Pyst2 phosphatases:
characterisation of Pyst2 as a cytosolic dual-specificity MAP kinase
phosphatase and its catalytic activation by both MAP and SAP kinases.";
J. Cell Sci. 111:3389-3399(1998).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
[18]
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).
[19]
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).
[20]
FUNCTION IN PHOSPHORYLATION OF IER3, INTERACTION WITH IER3, AND ACTIVITY
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]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
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).
[39]
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).
[40]
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).
[41]
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).
[42]
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).
[43]
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).
[44]
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).
[45]
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).
[46]
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).
[47]
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).
[48]
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).
[49]
PHOSPHORYLATION AT THR-190, ACTIVITY 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).
[50]
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).
[51]
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).
[52]
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).
[53]
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).
[54]
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).
[55]
REVIEW ON ACTIVITY 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).
[56]
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).
[57]
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).
[58]
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).
[59]
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).
[60]
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).
[61]
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).
[62]
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).
[63]
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).
[64]
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).
[65]
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).
[66]
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).
[67]
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).
[68]
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).
[69]
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:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.24;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ACTIVITY 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 DUSP1, 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. 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). Interacts with DUSP7; the interaction enhances DUSP7
phosphatase activity (PubMed:9788880). {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:9596579, ECO:0000269|PubMed:9788880,
ECO:0000269|PubMed:9827991}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Nef through its SH3
domain. {ECO:0000269|PubMed:8794306}.
-!- INTERACTION:
P28482; P32121: ARRB2; NbExp=3; IntAct=EBI-959949, EBI-714559;
P28482; P53004: BLVRA; NbExp=2; IntAct=EBI-959949, EBI-7410441;
P28482; P15882: CHN1; NbExp=3; IntAct=EBI-959949, EBI-718947;
P28482; Q7L5N1: COPS6; NbExp=2; IntAct=EBI-959949, EBI-486838;
P28482; P28562: DUSP1; NbExp=3; IntAct=EBI-959949, EBI-975493;
P28482; Q13115: DUSP4; NbExp=5; IntAct=EBI-959949, EBI-6591081;
P28482; Q16690: DUSP5; NbExp=3; IntAct=EBI-959949, EBI-7487376;
P28482; Q16828: DUSP6; NbExp=3; IntAct=EBI-959949, EBI-746870;
P28482; Q99956: DUSP9; NbExp=3; IntAct=EBI-959949, EBI-3906678;
P28482; P14921: ETS1; NbExp=3; IntAct=EBI-959949, EBI-913209;
P28482; Q9BRK4: LZTS2; NbExp=4; IntAct=EBI-959949, EBI-741037;
P28482; Q02750: MAP2K1; NbExp=2; IntAct=EBI-959949, EBI-492564;
P28482; P28482: MAPK1; NbExp=3; IntAct=EBI-959949, EBI-959949;
P28482; Q16539-3: MAPK14; NbExp=5; IntAct=EBI-959949, EBI-6932370;
P28482; P27361: MAPK3; NbExp=5; IntAct=EBI-959949, EBI-73995;
P28482; Q99750: MDFI; NbExp=3; IntAct=EBI-959949, EBI-724076;
P28482; Q9BUB5: MKNK1; NbExp=9; IntAct=EBI-959949, EBI-73837;
P28482; P35548: MSX2; NbExp=3; IntAct=EBI-959949, EBI-6447480;
P28482; Q15121: PEA15; NbExp=4; IntAct=EBI-959949, EBI-714410;
P28482; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-959949, EBI-2876622;
P28482; P62487: POLR2G; NbExp=3; IntAct=EBI-959949, EBI-347928;
P28482; P35813: PPM1A; NbExp=19; IntAct=EBI-959949, EBI-989143;
P28482; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-959949, EBI-2557469;
P28482; P25786: PSMA1; NbExp=3; IntAct=EBI-959949, EBI-359352;
P28482; A2A3K4: PTPDC1; NbExp=3; IntAct=EBI-959949, EBI-11603375;
P28482; P35236: PTPN7; NbExp=6; IntAct=EBI-959949, EBI-2265723;
P28482; Q12913: PTPRJ; NbExp=7; IntAct=EBI-959949, EBI-2264500;
P28482; Q15256: PTPRR; NbExp=3; IntAct=EBI-959949, EBI-2265659;
P28482; Q15256-5: PTPRR; NbExp=3; IntAct=EBI-959949, EBI-18347359;
P28482; O76064: RNF8; NbExp=3; IntAct=EBI-959949, EBI-373337;
P28482; Q15418: RPS6KA1; NbExp=5; IntAct=EBI-959949, EBI-963034;
P28482; Q15349: RPS6KA2; NbExp=8; IntAct=EBI-959949, EBI-1384149;
P28482; P51812: RPS6KA3; NbExp=5; IntAct=EBI-959949, EBI-1046616;
P28482; P29353-2: SHC1; NbExp=4; IntAct=EBI-959949, EBI-1000553;
P28482; P61764: STXBP1; NbExp=3; IntAct=EBI-959949, EBI-960169;
P28482; Q08117-2: TLE5; NbExp=3; IntAct=EBI-959949, EBI-11741437;
P28482; Q9Y296: TRAPPC4; NbExp=3; IntAct=EBI-959949, EBI-722888;
P28482; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-959949, EBI-12287587;
P28482; A0A384NQ31; NbExp=3; IntAct=EBI-959949, EBI-12903728;
P28482; Q9U1H0: cic; Xeno; NbExp=2; IntAct=EBI-959949, EBI-98330;
P28482; Q05922: Dusp2; Xeno; NbExp=2; IntAct=EBI-959949, EBI-7898692;
P28482; P02687: MBP; Xeno; NbExp=2; IntAct=EBI-959949, EBI-908215;
P28482; 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.
Dephosphorylated by DUSP1 at Thr-185 and Tyr-187. {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=Truncated N-terminus.; 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]
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.
PDB; 5WP1; X-ray; 1.40 A; A=4-360.
PDB; 6D5Y; X-ray; 2.86 A; A=13-360.
PDB; 6DMG; X-ray; 2.20 A; A=11-357.
PDB; 6G54; X-ray; 2.05 A; A=1-360.
PDB; 6G8X; X-ray; 1.76 A; A=1-360.
PDB; 6G91; X-ray; 1.80 A; A=1-360.
PDB; 6G92; X-ray; 1.99 A; A=1-360.
PDB; 6G93; X-ray; 1.67 A; A=1-360.
PDB; 6G97; X-ray; 1.90 A; A=1-360.
PDB; 6G9A; X-ray; 1.91 A; A=1-360.
PDB; 6G9D; X-ray; 1.80 A; A=1-360.
PDB; 6G9H; X-ray; 1.73 A; A=1-360.
PDB; 6G9J; X-ray; 1.98 A; A=1-360.
PDB; 6G9K; X-ray; 1.94 A; A=1-360.
PDB; 6G9M; X-ray; 1.86 A; A=1-360.
PDB; 6G9N; X-ray; 1.76 A; A=1-360.
PDB; 6GDM; X-ray; 1.91 A; A=1-360.
PDB; 6GDQ; X-ray; 1.86 A; A=1-360.
PDB; 6GE0; X-ray; 1.82 A; A=1-360.
PDB; 6GJB; X-ray; 1.82 A; A=1-360.
PDB; 6GJD; X-ray; 1.58 A; A=1-360.
PDB; 6NBS; X-ray; 1.90 A; A=9-360.
PDB; 6OPG; X-ray; 2.90 A; A=8-360.
PDB; 6OPH; X-ray; 2.40 A; A=8-360.
PDB; 6OPI; X-ray; 3.00 A; A=8-360.
PDB; 6Q7K; X-ray; 1.84 A; A=1-360.
PDB; 6Q7S; X-ray; 1.73 A; A=1-360.
PDB; 6Q7T; X-ray; 1.60 A; A=1-360.
PDB; 6QA1; X-ray; 1.58 A; A=1-360.
PDB; 6QA3; X-ray; 1.57 A; A=1-360.
PDB; 6QA4; X-ray; 1.60 A; A=1-360.
PDB; 6QAG; X-ray; 2.07 A; A=1-360.
PDB; 6QAH; X-ray; 1.58 A; A=1-360.
PDB; 6QAL; X-ray; 1.57 A; A=1-360.
PDB; 6QAQ; X-ray; 1.58 A; A=1-360.
PDB; 6QAW; X-ray; 1.84 A; A=1-360.
PDB; 6RQ4; X-ray; 1.96 A; A=1-360.
PDB; 6SLG; X-ray; 1.33 A; A=1-360.
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; -.
PDBsum; 5WP1; -.
PDBsum; 6D5Y; -.
PDBsum; 6DMG; -.
PDBsum; 6G54; -.
PDBsum; 6G8X; -.
PDBsum; 6G91; -.
PDBsum; 6G92; -.
PDBsum; 6G93; -.
PDBsum; 6G97; -.
PDBsum; 6G9A; -.
PDBsum; 6G9D; -.
PDBsum; 6G9H; -.
PDBsum; 6G9J; -.
PDBsum; 6G9K; -.
PDBsum; 6G9M; -.
PDBsum; 6G9N; -.
PDBsum; 6GDM; -.
PDBsum; 6GDQ; -.
PDBsum; 6GE0; -.
PDBsum; 6GJB; -.
PDBsum; 6GJD; -.
PDBsum; 6NBS; -.
PDBsum; 6OPG; -.
PDBsum; 6OPH; -.
PDBsum; 6OPI; -.
PDBsum; 6Q7K; -.
PDBsum; 6Q7S; -.
PDBsum; 6Q7T; -.
PDBsum; 6QA1; -.
PDBsum; 6QA3; -.
PDBsum; 6QA4; -.
PDBsum; 6QAG; -.
PDBsum; 6QAH; -.
PDBsum; 6QAL; -.
PDBsum; 6QAQ; -.
PDBsum; 6QAW; -.
PDBsum; 6RQ4; -.
PDBsum; 6SLG; -.
SMR; P28482; -.
BioGRID; 111580; 289.
CORUM; P28482; -.
DIP; DIP-519N; -.
ELM; P28482; -.
IntAct; P28482; 146.
MINT; P28482; -.
STRING; 9606.ENSP00000215832; -.
BindingDB; P28482; -.
ChEMBL; CHEMBL4040; -.
DrugBank; DB07905; (1aR,8S,13S,14S,15aR)-5,13,14-trihydroxy-3-methoxy-8-methyl-8,9,13,14,15,15a-hexahydro-6H-oxireno[k][2]benzoxacyclotetradecine-6,12(1aH)-dione.
DrugBank; DB07788; (3R,5Z,8S,9S,11E)-8,9,16-TRIHYDROXY-14-METHOXY-3-METHYL-3,4,9,10-TETRAHYDRO-1H-2-BENZOXACYCLOTETRADECINE-1,7(8H)-DIONE.
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-[4-(4-Fluorophenyl)-2-[4-[(R)-methylsulfinyl]phenyl]-1H-imidazol-5-yl]pyridine.
DrugBank; DB07794; 5-(2-PHENYLPYRAZOLO[1,5-A]PYRIDIN-3-YL)-1H-PYRAZOLO[3,4-C]PYRIDAZIN-3-AMINE.
DrugBank; DB08513; [4-({5-(AMINOCARBONYL)-4-[(3-METHYLPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)PHENYL]ACETIC ACID.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB01169; Arsenic trioxide.
DrugBank; DB01064; Isoprenaline.
DrugBank; DB01017; Minocycline.
DrugBank; DB06877; N,N-DIMETHYL-4-(4-PHENYL-1H-PYRAZOL-3-YL)-1H-PYRROLE-2-CARBOXAMIDE.
DrugBank; DB07010; N-BENZYL-4-[4-(3-CHLOROPHENYL)-1H-PYRAZOL-3-YL]-1H-PYRROLE-2-CARBOXAMIDE.
DrugBank; DB02116; Olomoucine.
DrugBank; DB06641; Perifosine.
DrugBank; DB02482; Phosphonothreonine.
DrugBank; DB02733; Purvalanol.
DrugBank; DB04338; SB220025.
DrugBank; DB06195; Seliciclib.
DrugBank; DB11120; Turpentine.
DrugBank; DB13930; Ulixertinib.
DrugCentral; P28482; -.
GuidetoPHARMACOLOGY; 1495; -.
MoonDB; P28482; Predicted.
MoonProt; P28482; -.
iPTMnet; P28482; -.
MetOSite; P28482; -.
PhosphoSitePlus; P28482; -.
SwissPalm; P28482; -.
BioMuta; MAPK1; -.
DMDM; 119554; -.
OGP; P28482; -.
CPTAC; CPTAC-1352; -.
CPTAC; CPTAC-1353; -.
CPTAC; CPTAC-1354; -.
CPTAC; CPTAC-1541; -.
CPTAC; CPTAC-870; -.
CPTAC; CPTAC-871; -.
EPD; P28482; -.
jPOST; P28482; -.
MassIVE; P28482; -.
PaxDb; P28482; -.
PeptideAtlas; P28482; -.
PRIDE; P28482; -.
ProteomicsDB; 1826; -.
ProteomicsDB; 54488; -. [P28482-1]
Antibodypedia; 3785; 1775 antibodies.
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; ENSG00000100030; Tissue enhanced (brain).
MalaCards; MAPK1; -.
MIM; 176948; gene.
neXtProt; NX_P28482; -.
OpenTargets; ENSG00000100030; -.
Orphanet; 261330; Distal 22q11.2 microdeletion syndrome.
PharmGKB; PA30616; -.
eggNOG; KOG0660; Eukaryota.
GeneTree; ENSGT00940000156771; -.
HOGENOM; CLU_000288_181_1_1; -.
InParanoid; P28482; -.
KO; K04371; -.
OMA; DIYIVQC; -.
PhylomeDB; P28482; -.
TreeFam; TF105097; -.
BRENDA; 2.7.11.24; 2681.
PathwayCommons; P28482; -.
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-170968; Frs2-mediated activation.
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-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-5668599; RHO GTPases Activate NADPH Oxidases.
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-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-8939211; ESR-mediated signaling.
Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
Reactome; R-HSA-9627069; Regulation of the apoptosome activity.
Reactome; R-HSA-9634635; Estrogen-stimulated signaling through PRKCZ.
Reactome; R-HSA-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
Reactome; R-HSA-9635465; Suppression of apoptosis.
Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
SignaLink; P28482; -.
SIGNOR; P28482; -.
BioGRID-ORCS; 5594; 121 hits in 912 CRISPR screens.
ChiTaRS; MAPK1; human.
EvolutionaryTrace; P28482; -.
GeneWiki; MAPK1; -.
GenomeRNAi; 5594; -.
Pharos; P28482; Tchem.
PRO; PR:P28482; -.
Proteomes; UP000005640; Chromosome 22.
RNAct; P28482; protein.
Bgee; ENSG00000100030; Expressed in putamen and 250 other tissues.
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: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:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0031143; C:pseudopodium; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
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 CTD heptapeptide repeat 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:0000186; P:activation of MAPKK activity; TAS:Reactome.
GO; GO:0007568; P:aging; IEA:Ensembl.
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:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
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:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
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:0046697; P:decidualization; 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:0035556; P:intracellular signal transduction; IBA:GO_Central.
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:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:CAFA.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IGI:ARUK-UCL.
GO; GO:0120041; P:positive regulation of macrophage proliferation; IGI:ARUK-UCL.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; 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:0051090; P:regulation of DNA-binding transcription factor activity; TAS:Reactome.
GO; GO:2000641; P:regulation of early endosome to late endosome transport; TAS:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
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: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: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: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; 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
/note="Removed"
/evidence="ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895, ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801"
CHAIN 2..360
/note="Mitogen-activated protein kinase 1"
/id="PRO_0000186247"
DOMAIN 25..313
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 31..39
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
DNA_BIND 259..277
REGION 105..108
/note="Inhibitor-binding"
REGION 153..154
/note="Inhibitor-binding"
MOTIF 185..187
/note="TXY"
/evidence="ECO:0000269|PubMed:18760948"
MOTIF 318..322
/note="Cytoplasmic retention motif"
/evidence="ECO:0000269|PubMed:18760948"
MOTIF 327..333
/note="Nuclear translocation motif"
/evidence="ECO:0000269|PubMed:18760948"
COMPBIAS 2..9
/note="Poly-Ala"
ACT_SITE 149
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 54
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 54
/note="Inhibitor"
/evidence="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
/note="Inhibitor; via amide nitrogen and carbonyl oxygen"
/evidence="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
/note="Inhibitor"
/evidence="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
/note="Inhibitor"
/evidence="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
/note="Inhibitor"
/evidence="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
/note="Inhibitor"
/evidence="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
/note="N-acetylalanine"
/evidence="ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895, ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801"
MOD_RES 29
/note="Phosphoserine; by SGK1"
/evidence="ECO:0000269|PubMed:19447520"
MOD_RES 185
/note="Phosphothreonine; by MAP2K1 and MAP2K2"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163"
MOD_RES 187
/note="Phosphotyrosine; by MAP2K1 and MAP2K2"
/evidence="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
/note="Phosphothreonine; by autocatalysis"
/evidence="ECO:0000269|PubMed:19060905"
MOD_RES 246
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:18760948"
MOD_RES 248
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:18760948"
MOD_RES 284
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19369195"
VAR_SEQ 242..285
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|Ref.3"
/id="VSP_047815"
MUTAGEN 54
/note="K->R: Does not inhibit interaction with MAP2K1."
/evidence="ECO:0000269|PubMed:18794356"
MUTAGEN 176..179
/note="Missing: Inhibits homodimerization and interaction
with TPR."
/evidence="ECO:0000269|PubMed:18794356"
MUTAGEN 185
/note="T->A: Inhibits interaction with TPR; when associated
with A-187."
/evidence="ECO:0000269|PubMed:18794356"
MUTAGEN 187
/note="Y->A: Inhibits interaction with TPR; when associated
with A-185."
/evidence="ECO:0000269|PubMed:18794356"
MUTAGEN 234
/note="L->A: Inhibits interaction with TPR."
/evidence="ECO:0000269|PubMed:18794356"
MUTAGEN 318
/note="D->A: Loss of dephosphorylation by PTPRJ."
/evidence="ECO:0000269|PubMed:18794356,
ECO:0000269|PubMed:19494114"
MUTAGEN 318
/note="D->N: Inhibits interaction with MAP2K1 but not with
TPR; when associated with N-321."
/evidence="ECO:0000269|PubMed:18794356,
ECO:0000269|PubMed:19494114"
MUTAGEN 321
/note="D->N: Inhibits interaction with MAP2K1 but not with
TPR; when associated with N-318."
/evidence="ECO:0000269|PubMed:18794356"
CONFLICT 91
/note="R -> Q (in Ref. 2; CAA77752)"
/evidence="ECO:0000305"
STRAND 12..14
/evidence="ECO:0000244|PDB:4QTA"
STRAND 17..19
/evidence="ECO:0000244|PDB:4QTA"
TURN 22..24
/evidence="ECO:0000244|PDB:4ZZN"
STRAND 25..34
/evidence="ECO:0000244|PDB:4ZZN"
STRAND 37..44
/evidence="ECO:0000244|PDB:4ZZN"
TURN 45..48
/evidence="ECO:0000244|PDB:4ZZN"
STRAND 49..56
/evidence="ECO:0000244|PDB:4ZZN"
STRAND 59..61
/evidence="ECO:0000244|PDB:6G92"
HELIX 62..77
/evidence="ECO:0000244|PDB:4ZZN"
STRAND 81..83
/evidence="ECO:0000244|PDB:5AX3"
STRAND 88..90
/evidence="ECO:0000244|PDB:4ZZN"
TURN 95..97
/evidence="ECO:0000244|PDB:4ZZN"
STRAND 101..106
/evidence="ECO:0000244|PDB:4ZZN"
STRAND 109..111
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 112..118
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 123..142
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 152..154
/evidence="ECO:0000244|PDB:4ZZN"
STRAND 155..157
/evidence="ECO:0000244|PDB:4ZZN"
TURN 159..161
/evidence="ECO:0000244|PDB:4IZ5"
STRAND 163..165
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 168..170
/evidence="ECO:0000244|PDB:3I5Z"
HELIX 176..178
/evidence="ECO:0000244|PDB:4ZZN"
TURN 181..185
/evidence="ECO:0000244|PDB:2Y9Q"
HELIX 191..193
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 196..200
/evidence="ECO:0000244|PDB:4ZZN"
STRAND 201..203
/evidence="ECO:0000244|PDB:5K4I"
HELIX 208..223
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 235..244
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 249..253
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 258..265
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 275..278
/evidence="ECO:0000244|PDB:4ZZN"
STRAND 280..282
/evidence="ECO:0000244|PDB:5NHO"
HELIX 284..293
/evidence="ECO:0000244|PDB:4ZZN"
TURN 298..300
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 304..308
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 311..313
/evidence="ECO:0000244|PDB:4ZZN"
TURN 314..316
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 319..321
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 331..334
/evidence="ECO:0000244|PDB:5V62"
HELIX 335..337
/evidence="ECO:0000244|PDB:5K4I"
HELIX 340..351
/evidence="ECO:0000244|PDB:4ZZN"
HELIX 352..354
/evidence="ECO:0000244|PDB:4ZZN"
TURN 356..358
/evidence="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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