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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_RAT                Reviewed;         380 AA.
P21708; Q4PIY8; Q62686; Q9JJ13;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
30-AUG-2017, entry version 195.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=1327976; DOI=10.1016/0378-1119(92)90109-3;
Marquardt B., Stabel S.;
"Sequence of a rat cDNA encoding the ERK1-MAP kinase.";
Gene 120:297-299(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10748187; DOI=10.1074/jbc.M910060199;
Yung Y., Yao Z., Hanoch T., Seger R.;
"ERK1b, a 46-kDa ERK isoform that is differentially regulated by
MEK.";
J. Biol. Chem. 275:15799-15808(2000).
[3]
PROTEIN SEQUENCE OF 2-65; 96-132; 157-209; 213-221; 280-357 AND
361-380 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
ALA-2, PHOSPHORYLATION AT THR-203 AND TYR-205, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Pheochromocytoma;
Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
Submitted (AUG-2006) to UniProtKB.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 7-380 (ISOFORM 1).
Maisonpierre P.C., le Beau M.M., Espinosa R. III, Ip N.Y.,
Belluscio L., la Monte S.M., Squinto S., Furth M.E., Yancopoulos G.D.;
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 73-84 AND 183-190, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
Lubec G., Afjehi-Sadat L., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-380 (ISOFORM 1), AND PARTIAL PROTEIN
SEQUENCE.
PubMed=2164259; DOI=10.1126/science.2164259;
Boulton T.G., Yancopoulos G.D., Gregory J.S., Slaughter C., Moomaw C.,
Hsu J., Cobb M.H.;
"An insulin-stimulated protein kinase similar to yeast kinases
involved in cell cycle control.";
Science 249:64-67(1990).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-380 (ISOFORM 1).
TISSUE=Brain cortex;
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).
[8]
PROTEIN SEQUENCE OF 43-64 AND 167-185, AND CHARACTERIZATION.
PubMed=1846291; DOI=10.1021/bi00215a038;
Boulton T.G., Gregory J.S., Cobb M.H.;
"Purification and properties of extracellular signal-regulated kinase
1, an insulin-stimulated microtubule-associated protein 2 kinase.";
Biochemistry 30:278-286(1991).
[9]
AUTOPHOSPHORYLATION.
PubMed=1712480; DOI=10.1073/pnas.88.14.6142;
Seger R., Ahn N.G., Boulton T.G., Yancopoulos G.D., Panayotatos N.,
Radziejewska E., Ericsson L., Bratlien R.L., Cobb M.H., Krebs E.G.;
"Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo
autophosphorylation on both tyrosine and threonine residues:
implications for their mechanism of activation.";
Proc. Natl. Acad. Sci. U.S.A. 88:6142-6146(1991).
[10]
PHOSPHORYLATION OF EIF4EBP1.
PubMed=7939721; DOI=10.1126/science.7939721;
Lin T.-A., Kong X., Haystead T.A.J., Pause A., Belsham G.J.,
Sonenberg N., Lawrence J.C. Jr.;
"PHAS-I as a link between mitogen-activated protein kinase and
translation initiation.";
Science 266:653-656(1994).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[12]
IDENTIFICATION IN A COMPLEX WITH BRAF; HRAS; MAP2K1 AND RGS14.
PubMed=19319189; DOI=10.1371/journal.pone.0004884;
Willard F.S., Willard M.D., Kimple A.J., Soundararajan M.,
Oestreich E.A., Li X., Sowa N.A., Kimple R.J., Doyle D.A., Der C.J.,
Zylka M.J., Snider W.D., Siderovski D.P.;
"Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras
effector.";
PLoS ONE 4:E4884-E4884(2009).
[13]
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).
[14]
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).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[17]
SUBCELLULAR LOCATION, AND INTERACTION WITH CAVIN4.
PubMed=24567387; DOI=10.1073/pnas.1315359111;
Ogata T., Naito D., Nakanishi N., Hayashi Y.K., Taniguchi T.,
Miyagawa K., Hamaoka T., Maruyama N., Matoba S., Ikeda K., Yamada H.,
Oh H., Ueyama T.;
"MURC/Cavin-4 facilitates recruitment of ERK to caveolae and
concentric cardiac hypertrophy induced by alpha1-adrenergic
receptors.";
Proc. Natl. Acad. Sci. U.S.A. 111:3811-3816(2014).
-!- 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.
-!- 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 ADAM15,
ARRB2, CANX, DAPK1 (via death domain), HSF4, IER3, MAP2K1/MEK1,
MORG1, NISCH, PEA15, SGK1 and MKNK2. MKNK2 isoform 1 binding
prevents from dephosphorylation and inactivation. Interacts with
TPR. Interacts with HSF1 (via D domain and preferentially with
hyperphosphorylated form); this interaction occurs upon heat
shock. Interacts with CDKN2AIP (By similarity). Interacts with
CAVIN4 (PubMed:24567387). {ECO:0000250|UniProtKB:P27361,
ECO:0000250|UniProtKB:Q63844, ECO:0000269|PubMed:24567387}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24567387}.
Nucleus. Membrane, caveola {ECO:0000269|PubMed:24567387}.
Note=Autophosphorylation at Thr-207 promotes nuclear localization.
PEA15-binding redirects the biological outcome of MAPK3 kinase-
signaling by sequestering MAPK3 into the cytoplasm. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=A;
IsoId=P21708-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=P21708-2; Sequence=VSP_004830;
-!- TISSUE SPECIFICITY: Highest levels within the nervous system,
expressed in different tissues, mostly in intestine, placenta and
lung.
-!- DEVELOPMENTAL STAGE: Increased expression during development.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Phosphorylated upon FLT3 and KIT signaling. Ligand-activated
ALK induces tyrosine phosphorylation (By similarity).
Dephosphorylated by PTPRJ at Tyr-205 (By similarity). Dually
phosphorylated on Thr-203 and Tyr-205, which activates the enzyme.
{ECO:0000250, ECO:0000269|PubMed:7939721, ECO:0000269|Ref.3}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
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EMBL; S46779; AAA11604.1; -; mRNA.
EMBL; X65198; CAA46318.1; -; mRNA.
EMBL; AF155236; AAF71666.1; -; mRNA.
EMBL; M61177; AAA63486.1; -; mRNA.
EMBL; M38194; AAA41123.1; -; mRNA.
EMBL; U12008; AAA20009.1; -; mRNA.
PIR; JC1451; JC1451.
RefSeq; NP_059043.1; NM_017347.2.
UniGene; Rn.2592; -.
ProteinModelPortal; P21708; -.
SMR; P21708; -.
BioGrid; 248427; 4.
DIP; DIP-487N; -.
IntAct; P21708; 270.
MINT; MINT-100073; -.
STRING; 10116.ENSRNOP00000026627; -.
ChEMBL; CHEMBL5809; -.
iPTMnet; P21708; -.
PhosphoSitePlus; P21708; -.
PaxDb; P21708; -.
PRIDE; P21708; -.
Ensembl; ENSRNOT00000087625; ENSRNOP00000070784; ENSRNOG00000053583. [P21708-1]
GeneID; 50689; -.
KEGG; rno:50689; -.
UCSC; RGD:3046; rat. [P21708-1]
CTD; 5595; -.
RGD; 3046; Mapk3.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00550000074298; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P21708; -.
KO; K04371; -.
OMA; AYGMVSS; -.
OrthoDB; EOG091G08QL; -.
PhylomeDB; P21708; -.
TreeFam; TF105097; -.
BRENDA; 2.7.11.24; 5301.
Reactome; R-RNO-110056; MAPK3 (ERK1) activation.
Reactome; R-RNO-112409; RAF-independent MAPK1/3 activation.
Reactome; R-RNO-1169408; ISG15 antiviral mechanism.
Reactome; R-RNO-1295596; Spry regulation of FGF signaling.
Reactome; R-RNO-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
Reactome; R-RNO-198753; ERK/MAPK targets.
Reactome; R-RNO-202670; ERKs are inactivated.
Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence.
Reactome; R-RNO-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-RNO-2559585; Oncogene Induced Senescence.
Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-RNO-375165; NCAM signaling for neurite out-growth.
Reactome; R-RNO-445144; Signal transduction by L1.
Reactome; R-RNO-450341; Activation of the AP-1 family of transcription factors.
Reactome; R-RNO-456926; Thrombin signalling through proteinase activated receptors (PARs).
Reactome; R-RNO-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-RNO-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-RNO-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-RNO-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
Reactome; R-RNO-5674135; MAP2K and MAPK activation.
Reactome; R-RNO-5674499; Negative feedback regulation of MAPK pathway.
Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-RNO-73728; RNA Polymerase I Promoter Opening.
Reactome; R-RNO-74749; Signal attenuation.
Reactome; R-RNO-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
Reactome; R-RNO-982772; Growth hormone receptor signaling.
PRO; PR:P21708; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000053583; -.
Genevisible; P21708; RN.
GO; GO:0005901; C:caveola; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005769; C:early endosome; TAS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0031143; C:pseudopodium; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
GO; GO:0004708; F:MAP kinase kinase activity; IEA:Ensembl.
GO; GO:0019902; F:phosphatase binding; IEA:Ensembl.
GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IC:RGD.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0019369; P:arachidonic acid metabolic process; IEP:RGD.
GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
GO; GO:0061308; P:cardiac neural crest cell development involved in heart development; IEA:Ensembl.
GO; GO:0051216; P:cartilage development; IEA:Ensembl.
GO; GO:0072584; P:caveolin-mediated endocytosis; TAS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0034198; P:cellular response to amino acid starvation; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
GO; GO:0006975; P:DNA damage induced protein phosphorylation; IEA:Ensembl.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0060324; P:face development; IEA:Ensembl.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
GO; GO:0060425; P:lung morphogenesis; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; IMP:RGD.
GO; GO:0000189; P:MAPK import into nucleus; IDA:RGD.
GO; GO:2000657; P:negative regulation of apolipoprotein binding; IEA:Ensembl.
GO; GO:0042473; P:outer ear morphogenesis; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:RGD.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IEA:Ensembl.
GO; GO:0031281; P:positive regulation of cyclase activity; IEA:Ensembl.
GO; GO:0002741; P:positive regulation of cytokine secretion involved in immune response; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0035066; P:positive regulation of histone acetylation; IEA:Ensembl.
GO; GO:0033129; P:positive regulation of histone phosphorylation; IEA:Ensembl.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IEA:Ensembl.
GO; GO:1905050; P:positive regulation of metallopeptidase activity; IEA:Ensembl.
GO; GO:0051973; P:positive regulation of telomerase activity; IEA:Ensembl.
GO; GO:1904355; P:positive regulation of telomere capping; IEA:Ensembl.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEP:RGD.
GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
GO; GO:1904417; P:positive regulation of xenophagy; IEA:Ensembl.
GO; GO:0006461; P:protein complex assembly; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0030641; P:regulation of cellular pH; IEA:Ensembl.
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:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IDA:RGD.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0051403; P:stress-activated MAPK cascade; 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:Ensembl.
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; Alternative splicing; 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.3}.
CHAIN 2 380 Mitogen-activated protein kinase 3.
/FTId=PRO_0000186253.
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.3}.
MOD_RES 199 199 Phosphothreonine.
{ECO:0000250|UniProtKB:P27361}.
MOD_RES 203 203 Phosphothreonine; by MAP2K1 and MAP2K2.
{ECO:0000244|PubMed:16641100,
ECO:0000244|PubMed:22673903,
ECO:0000269|Ref.3}.
MOD_RES 205 205 Phosphotyrosine; by MAP2K1 and MAP2K2.
{ECO:0000244|PubMed:16641100,
ECO:0000244|PubMed:22673903,
ECO:0000269|Ref.3}.
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}.
VAR_SEQ 340 340 E -> EVSRPPAAGRGISVPSVRPVPYCLCPQ (in
isoform 2).
{ECO:0000303|PubMed:10748187}.
/FTId=VSP_004830.
CONFLICT 95 95 R -> G (in Ref. 1; AAA11604/CAA46318, 4;
AAA63486 and 7; AAA20009). {ECO:0000305}.
SEQUENCE 380 AA; 43081 MW; 49C4EA95B627237F 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 RFQPGAPEAP


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