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Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (MNK1) (Microtubule-associated protein 2 kinase) (p44-ERK1)

 MK03_MOUSE              Reviewed;         380 AA.
Q63844; Q61531; Q8K0X5; Q91YW5;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
25-OCT-2017, entry version 189.
RecName: Full=Mitogen-activated protein kinase 3;
Short=MAP kinase 3;
Short=MAPK 3;
EC=2.7.11.24;
AltName: Full=ERT2;
AltName: Full=Extracellular signal-regulated kinase 1;
Short=ERK-1;
AltName: Full=Insulin-stimulated MAP2 kinase;
AltName: Full=MAP kinase isoform p44;
Short=p44-MAPK;
AltName: Full=MNK1;
AltName: Full=Microtubule-associated protein 2 kinase;
AltName: Full=p44-ERK1;
Name=Mapk3; Synonyms=Erk1, Prkm3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
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).
[2]
PROTEIN SEQUENCE OF 2-65; 89-105; 110-132; 157-209; 213-221; 280-288;
304-319 AND 361-371, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryonic fibroblast;
Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.;
Submitted (FEB-2008) to UniProtKB.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-380.
PubMed=8424957; DOI=10.1016/0167-4781(93)90074-N;
Tanner B., Mueckler M.;
"Molecular cloning of a mouse extracellular signal regulated kinase
(erk-1).";
Biochim. Biophys. Acta 1171:319-320(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-19.
TISSUE=Pre-B cell;
PubMed=1717989; DOI=10.1073/pnas.88.19.8845;
Crews C.M., Alessandrini A.A., Erikson R.L.;
"Mouse Erk-1 gene product is a serine/threonine protein kinase that
has the potential to phosphorylate tyrosine.";
Proc. Natl. Acad. Sci. U.S.A. 88:8845-8849(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 77-380.
TISSUE=Fetal brain;
PubMed=1716439; DOI=10.1089/dna.1991.10.505;
de Miguel C., Kligman D., Patel J., Detera-Wadleigh S.D.;
"Molecular analysis of microtubule-associated protein-2 kinase cDNA
from mouse and rat brain.";
DNA Cell Biol. 10:505-514(1991).
[6]
PROTEIN SEQUENCE OF 136-153 AND 191-209, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 171-209.
STRAIN=CBA/J; TISSUE=Bone marrow;
PubMed=8444355; DOI=10.1016/0378-1119(93)90411-U;
Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
"Novel CDC2-related protein kinases produced in murine hematopoietic
stem cells.";
Gene 124:305-306(1993).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 171-205.
PubMed=1459009;
Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
"Identification of new protein kinase genes, similar to kinases of the
cdc2 family and expressed in murine hematopoietic stem cells.";
Dokl. Akad. Nauk SSSR 324:893-897(1992).
[9]
PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
PubMed=10080542;
Zhang S., Mantel C., Broxmeyer H.E.;
"Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and
their association with Grb2 and Shc in Baf3/Flt3 cells.";
J. Leukoc. Biol. 65:372-380(1999).
[10]
PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
PubMed=11090077;
Mizuki M., Fenski R., Halfter H., Matsumura I., Schmidt R., Muller C.,
Gruning W., Kratz-Albers K., Serve S., Steur C., Buchner T.,
Kienast J., Kanakura Y., Berdel W.E., Serve H.;
"Flt3 mutations from patients with acute myeloid leukemia induce
transformation of 32D cells mediated by the Ras and STAT5 pathways.";
Blood 96:3907-3914(2000).
[11]
INTERACTION WITH PEA15, SUBCELLULAR LOCATION, AND FUNCTION OF THE MAPK
ERK CASCADE.
PubMed=11702783; DOI=10.1016/S1534-5807(01)00035-1;
Formstecher E., Ramos J.W., Fauquet M., Calderwood D.A., Hsieh J.C.,
Canton B., Nguyen X.T., Barnier J.V., Camonis J., Ginsberg M.H.,
Chneiweiss H.;
"PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase.";
Dev. Cell 1:239-250(2001).
[12]
FUNCTION IN PHOSPHORYLATION OF FOS, AND SUBCELLULAR LOCATION.
PubMed=12134156; DOI=10.1038/ncb822;
Murphy L.O., Smith S., Chen R.H., Fingar D.C., Blenis J.;
"Molecular interpretation of ERK signal duration by immediate early
gene products.";
Nat. Cell Biol. 4:556-564(2002).
[13]
INTERACTION WITH MORG1.
PubMed=15118098; DOI=10.1073/pnas.0305894101;
Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E.,
Bissonette E.A., Weber M.J.;
"Modular construction of a signaling scaffold: MORG1 interacts with
components of the ERK cascade and links ERK signaling to specific
agonists.";
Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004).
[14]
PHOSPHORYLATION OF SPZ1.
PubMed=15899793; DOI=10.1158/0008-5472.CAN-04-3658;
Hsu S.-H., Hsieh-Li H.-M., Huang H.-Y., Huang P.-H., Li H.;
"bHLH-zip transcription factor Spz1 mediates mitogen-activated protein
kinase cell proliferation, transformation, and tumorigenesis.";
Cancer Res. 65:4041-4050(2005).
[15]
INTERACTION WITH MKNK2.
PubMed=16162500; DOI=10.1074/jbc.M508356200;
Parra J.L., Buxade M., Proud C.G.;
"Features of the catalytic domains and C termini of the MAPK signal-
integrating kinases Mnk1 and Mnk2 determine their differing activities
and regulatory properties.";
J. Biol. Chem. 280:37623-37633(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[21]
PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
PubMed=21262971; DOI=10.1074/jbc.M110.205021;
Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K.,
Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D.,
Muller J.P.;
"Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase
FLT3 signaling.";
J. Biol. Chem. 286:10918-10929(2011).
[22]
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).
[23]
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).
[24]
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).
-!- FUNCTION: Serine/threonine kinase which acts as an essential
component of the MAP kinase signal transduction pathway.
MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important
role in the MAPK/ERK cascade. They participate also in a signaling
cascade initiated by activated KIT and KITLG/SCF. Depending on the
cellular context, the MAPK/ERK cascade mediates diverse biological
functions such as cell growth, adhesion, survival and
differentiation through the regulation of transcription,
translation, cytoskeletal rearrangements. The MAPK/ERK cascade
plays also a role in initiation and regulation of meiosis,
mitosis, and postmitotic functions in differentiated cells by
phosphorylating a number of transcription factors. About 160
substrates have already been discovered for ERKs. Many of these
substrates are localized in the nucleus, and seem to participate
in the regulation of transcription upon stimulation. However,
other substrates are found in the cytosol as well as in other
cellular organelles, and those are responsible for processes such
as translation, mitosis and apoptosis. Moreover, the MAPK/ERK
cascade is also involved in the regulation of the endosomal
dynamics, including lysosome processing and endosome cycling
through the perinuclear recycling compartment (PNRC); as well as
in the fragmentation of the Golgi apparatus during mitosis. The
substrates include transcription factors (such as ATF2, BCL6,
ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as
CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of
apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG),
regulators of translation (such as EIF4EBP1) and a variety of
other signaling-related molecules (like ARHGEF2, FRS2 or GRB10).
Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2,
RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2,
RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases
(such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which
enable the propagation the MAPK/ERK signal to additional cytosolic
and nuclear targets, thereby extending the specificity of the
cascade. {ECO:0000269|PubMed:11702783,
ECO:0000269|PubMed:12134156}.
-!- 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-203 and Tyr-205 in response to external stimuli like
insulin or NGF. Both phosphorylations are required for activity.
This phosphorylation causes dramatic conformational changes, which
enable full activation and interaction of MAPK1/ERK2 with its
substrates. Dephosphorylated and inactivated by DUSP3, DUSP6 and
DUSP9.
-!- SUBUNIT: Binds both upstream activators and downstream substrates
in multimolecular complexes. Found in a complex with at least
BRAF, HRAS, MAP2K1/MEK1, MAPK3 and RGS14. Interacts with TPR.
Interacts with ADAM15, ARRB2, CANX, DAPK1 (via death domain),
HSF4, IER3, MAP2K1/MEK1, NISCH, and SGK1 (By similarity).
Interacts with MORG1 (PubMed:15118098). Interacts with PEA15
(PubMed:11702783). Interacts with isoform 1 of MKNK2 and this
binding prevents from dephosphorylation and inactivation
(PubMed:16162500). Interacts with CDKN2AIP. Interacts with HSF1
(via D domain and preferentially with hyperphosphorylated form);
this interaction occurs upon heat shock. Interacts with CAVIN4 (By
similarity). {ECO:0000250|UniProtKB:P21708,
ECO:0000250|UniProtKB:P27361, ECO:0000269|PubMed:11702783,
ECO:0000269|PubMed:15118098, ECO:0000269|PubMed:16162500}.
-!- INTERACTION:
Q60793:Klf4; NbExp=3; IntAct=EBI-397682, EBI-3043905;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane, caveola
{ECO:0000250|UniProtKB:P21708}. Note=Autophosphorylation at Thr-
207 promotes nuclear localization (By similarity). PEA15-binding
redirects the biological outcome of MAPK3 kinase-signaling by
sequestering MAPK3 into the cytoplasm. {ECO:0000250}.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-203 and Tyr-205, which activates
the enzyme. Ligand-activated ALK induces tyrosine phosphorylation
(By similarity). Dephosphorylated by PTPRJ at Tyr-205 (By
similarity). Autophosphorylated on threonine and tyrosine residues
in vitro. Phosphorylated upon FLT3 and KIT signaling (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
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EMBL; BC013754; AAH13754.1; -; mRNA.
EMBL; BC029712; AAH29712.1; -; mRNA.
EMBL; S58470; AAB19973.1; -; mRNA.
EMBL; X64605; CAA45889.1; -; mRNA.
CCDS; CCDS21841.1; -.
PIR; S28184; S28184.
RefSeq; NP_036082.1; NM_011952.2.
UniGene; Mm.8385; -.
ProteinModelPortal; Q63844; -.
SMR; Q63844; -.
BioGrid; 204970; 18.
CORUM; Q63844; -.
DIP; DIP-31078N; -.
ELM; Q63844; -.
IntAct; Q63844; 8.
MINT; MINT-1524109; -.
STRING; 10090.ENSMUSP00000051619; -.
BindingDB; Q63844; -.
ChEMBL; CHEMBL5510; -.
iPTMnet; Q63844; -.
PhosphoSitePlus; Q63844; -.
SwissPalm; Q63844; -.
EPD; Q63844; -.
MaxQB; Q63844; -.
PaxDb; Q63844; -.
PeptideAtlas; Q63844; -.
PRIDE; Q63844; -.
Ensembl; ENSMUST00000057669; ENSMUSP00000051619; ENSMUSG00000063065.
GeneID; 26417; -.
KEGG; mmu:26417; -.
UCSC; uc009jsm.1; mouse.
CTD; 5595; -.
MGI; MGI:1346859; Mapk3.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00900000140906; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; Q63844; -.
KO; K04371; -.
OrthoDB; EOG091G08QL; -.
PhylomeDB; Q63844; -.
TreeFam; TF105097; -.
Reactome; R-MMU-110056; MAPK3 (ERK1) activation.
Reactome; R-MMU-112409; RAF-independent MAPK1/3 activation.
Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
Reactome; R-MMU-1295596; Spry regulation of FGF signaling.
Reactome; R-MMU-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
Reactome; R-MMU-198753; ERK/MAPK targets.
Reactome; R-MMU-202670; ERKs are inactivated.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-MMU-2559585; Oncogene Induced Senescence.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
Reactome; R-MMU-445144; Signal transduction by L1.
Reactome; R-MMU-450341; Activation of the AP-1 family of transcription factors.
Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
Reactome; R-MMU-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-MMU-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-MMU-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-MMU-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-5674135; MAP2K and MAPK activation.
Reactome; R-MMU-5674499; Negative feedback regulation of MAPK pathway.
Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-74749; Signal attenuation.
Reactome; R-MMU-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
Reactome; R-MMU-982772; Growth hormone receptor signaling.
ChiTaRS; Mapk3; mouse.
PRO; PR:Q63844; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000063065; -.
CleanEx; MM_MAPK3; -.
ExpressionAtlas; Q63844; baseline and differential.
Genevisible; Q63844; MM.
GO; GO:0005901; C:caveola; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005769; C:early endosome; TAS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005925; C:focal adhesion; TAS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB.
GO; GO:0005770; C:late endosome; TAS:UniProtKB.
GO; GO:0005739; C:mitochondrion; TAS:UniProtKB.
GO; GO:0005635; C:nuclear envelope; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0031143; C:pseudopodium; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0004707; F:MAP kinase activity; IDA:MGI.
GO; GO:0004708; F:MAP kinase kinase activity; IMP:MGI.
GO; GO:0019902; F:phosphatase binding; ISO:MGI.
GO; GO:0001784; F:phosphotyrosine residue binding; IMP:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0009887; P:animal organ morphogenesis; IDA:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0019369; P:arachidonic acid metabolic process; IEA:Ensembl.
GO; GO:0060020; P:Bergmann glial cell differentiation; IGI:MGI.
GO; GO:0030509; P:BMP signaling pathway; ISO:MGI.
GO; GO:0061308; P:cardiac neural crest cell development involved in heart development; IGI:MGI.
GO; GO:0051216; P:cartilage development; IDA:MGI.
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; ISO:MGI.
GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
GO; GO:1903351; P:cellular response to dopamine; ISO:MGI.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
GO; GO:0006975; P:DNA damage induced protein phosphorylation; ISO:MGI.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:CAFA.
GO; GO:0060324; P:face development; IGI:MGI.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:MGI.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:MGI.
GO; GO:0060425; P:lung morphogenesis; IGI:MGI.
GO; GO:0000189; P:MAPK import into nucleus; IEA:Ensembl.
GO; GO:2000657; P:negative regulation of apolipoprotein binding; IMP:BHF-UCL.
GO; GO:0014032; P:neural crest cell development; IGI:MGI.
GO; GO:0042473; P:outer ear morphogenesis; IGI:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISO:MGI.
GO; GO:0016310; P:phosphorylation; ISO:MGI.
GO; GO:0031281; P:positive regulation of cyclase activity; ISO:MGI.
GO; GO:0002741; P:positive regulation of cytokine secretion involved in immune response; IMP:CAFA.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0035066; P:positive regulation of histone acetylation; ISO:MGI.
GO; GO:0033129; P:positive regulation of histone phosphorylation; ISO:MGI.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:CAFA.
GO; GO:1905050; P:positive regulation of metallopeptidase activity; IMP:CAFA.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
GO; GO:1904417; P:positive regulation of xenophagy; IGI:MGI.
GO; GO:0006461; P:protein complex assembly; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0030641; P:regulation of cellular pH; IMP:MGI.
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; IGI:MGI.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; IMP:UniProtKB.
GO; GO:0032872; P:regulation of stress-activated MAPK cascade; TAS:UniProtKB.
GO; GO:0070849; P:response to epidermal growth factor; ISS:UniProtKB.
GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:MGI.
GO; GO:0051403; P:stress-activated MAPK cascade; ISO:MGI.
GO; GO:0048538; P:thymus development; IGI:MGI.
GO; GO:0030878; P:thyroid gland development; IGI:MGI.
GO; GO:0060440; P:trachea formation; IGI:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IMP:UniProtKB.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008349; MAPK_ERK1/2.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01770; ERK1ERK2MAPK.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; ATP-binding; Cell cycle; Complete proteome;
Cytoplasm; Direct protein sequencing; Kinase; Membrane;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.2}.
CHAIN 2 380 Mitogen-activated protein kinase 3.
/FTId=PRO_0000186252.
DOMAIN 43 331 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 49 57 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 203 205 TXY.
ACT_SITE 167 167 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 72 72 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.2}.
MOD_RES 199 199 Phosphothreonine.
{ECO:0000250|UniProtKB:P27361}.
MOD_RES 203 203 Phosphothreonine; by MAP2K1 and MAP2K2.
{ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 205 205 Phosphotyrosine; by MAP2K1 and MAP2K2.
{ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 208 208 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P27361}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000250|UniProtKB:P28482}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000250|UniProtKB:P28482}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000250|UniProtKB:P28482}.
CONFLICT 178 178 T -> P (in Ref. 7; CAA45889 and 8; no
nucleotide entry). {ECO:0000305}.
SEQUENCE 380 AA; 43066 MW; 49C14A95B627237F CRC64;
MAAAAAAPGG GGGEPRGTAG VVPVVPGEVE VVKGQPFDVG PRYTQLQYIG EGAYGMVSSA
YDHVRKTRVA IKKISPFEHQ TYCQRTLREI QILLRFRHEN VIGIRDILRA PTLEAMRDVY
IVQDLMETDL YKLLKSQQLS NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLINTTCD
LKICDFGLAR IADPEHDHTG FLTEYVATRW YRAPEIMLNS KGYTKSIDIW SVGCILAEML
SNRPIFPGKH YLDQLNHILG ILGSPSQEDL NCIINMKARN YLQSLPSKTK VAWAKLFPKS
DSKALDLLDR MLTFNPNKRI TVEEALAHPY LEQYYDPTDE PVAEEPFTFD MELDDLPKER
LKELIFQETA RFQPGAPEGP


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