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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_RAT                Reviewed;         358 AA.
P63086; P27703;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 159.
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, Mapk, Prkm1;
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].
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=2032290; DOI=10.1016/0092-8674(91)90098-J;
Boulton T.G., Nye S.H., Robbins D.J., Ip N.Y., Radziejewska E.,
Morgenbesser S.D., DePinho R.A., Panayotatos N., Cobb M.H.,
Yancopoulos G.D.;
"ERKs: a family of protein-serine/threonine kinases that are activated
and tyrosine phosphorylated in response to insulin and NGF.";
Cell 65:663-675(1991).
[2]
PROTEIN SEQUENCE OF 2-13; 69-75; 137-170; 193-201 AND 341-351,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Pheochromocytoma;
Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
Submitted (AUG-2006) to UniProtKB.
[3]
PROTEIN SEQUENCE OF 163-170, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[4]
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).
[5]
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).
[6]
INTERACTION WITH ARRB2.
PubMed=11226259; DOI=10.1073/pnas.041604898;
Luttrell L.M., Roudabush F.L., Choy E.W., Miller W.E., Field M.E.,
Pierce K.L., Lefkowitz R.J.;
"Activation and targeting of extracellular signal-regulated kinases by
beta-arrestin scaffolds.";
Proc. Natl. Acad. Sci. U.S.A. 98:2449-2454(2001).
[7]
FUNCTION, AND INTERACTION WITH CDK2AP2.
PubMed=12944431; DOI=10.1242/dev.00731;
Terret M.E., Lefebvre C., Djiane A., Rassinier P., Moreau J., Maro B.,
Verlhac M.H.;
"DOC1R: a MAP kinase substrate that control microtubule organization
of metaphase II mouse oocytes.";
Development 130:5169-5177(2003).
[8]
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).
[9]
INTERACTION WITH CAV2.
PubMed=19778377; DOI=10.1111/j.1582-4934.2009.00391.x;
Kwon H., Jeong K., Pak Y.;
"Identification of pY19-caveolin-2 as a positive regulator of insulin-
stimulated actin cytoskeleton-dependent mitogenesis.";
J. Cell. Mol. Med. 13:1549-1564(2009).
[10]
INTERACTION WITH CAV2.
PubMed=19427337; DOI=10.1016/j.bbamcr.2009.04.015;
Kwon H., Jeong K., Hwang E.M., Park J.-Y., Hong S.-G., Choi W.-S.,
Pak Y.;
"Caveolin-2 regulation of STAT3 transcriptional activation in response
to insulin.";
Biochim. Biophys. Acta 1793:1325-1333(2009).
[11]
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).
[12]
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).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, 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).
[15]
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).
[16]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=8107865; DOI=10.1038/367704a0;
Zhang F., Strand A., Robbins D., Cobb M.H., Goldsmith E.J.;
"Atomic structure of the MAP kinase ERK2 at 2.3-A resolution.";
Nature 367:704-710(1994).
[17]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP.
PubMed=8639522; DOI=10.1021/bi952723e;
Robinson M.J., Harkins P.C., Zhang J., Baer R., Haycock J.W.,
Cobb M.H., Goldsmith E.J.;
"Mutation of position 52 in ERK2 creates a nonproductive binding mode
for adenosine 5'-triphosphate.";
Biochemistry 35:5641-5646(1996).
[18]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=9298898; DOI=10.1016/S0092-8674(00)80351-7;
Canagarajah B.J., Khokhlatchev A., Cobb M.H., Goldsmith E.J.;
"Activation mechanism of the MAP kinase ERK2 by dual
phosphorylation.";
Cell 90:859-869(1997).
[19]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=9753691; DOI=10.1016/S0969-2126(98)00113-0;
Wang Z., Canagarajah B.J., Boehm J.C., Kassisa S., Cobb M.H.,
Young P.R., Abdel-Meguid S., Adams J.L., Goldsmith E.J.;
"Structural basis of inhibitor selectivity in MAP kinases.";
Structure 6:1117-1128(1998).
[20]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-357, AND INTERACTION WITH
DUSP6.
PubMed=16567630; DOI=10.1073/pnas.0510506103;
Liu S., Sun J.P., Zhou B., Zhang Z.Y.;
"Structural basis of docking interactions between ERK2 and MAP kinase
phosphatase 3.";
Proc. Natl. Acad. Sci. U.S.A. 103:5326-5331(2006).
[21]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-357.
PubMed=16765894; DOI=10.1016/j.str.2006.04.006;
Zhou T., Sun L., Humphreys J., Goldsmith E.J.;
"Docking interactions induce exposure of activation loop in the MAP
kinase ERK2.";
Structure 14:1011-1019(2006).
[22]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-358 IN COMPLEX WITH
INHIBITOR.
PubMed=18571434; DOI=10.1016/j.jsb.2008.05.002;
Rastelli G., Rosenfeld R., Reid R., Santi D.V.;
"Molecular modeling and crystal structure of ERK2-hypothemycin
complexes.";
J. Struct. Biol. 164:18-23(2008).
[23]
X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=18767165; DOI=10.1002/prot.22207;
Katayama N., Orita M., Yamaguchi T., Hisamichi H., Kuromitsu S.,
Kurihara H., Sakashita H., Matsumoto Y., Fujita S., Niimi T.;
"Identification of a key element for hydrogen-bonding patterns between
protein kinases and their inhibitors.";
Proteins 73:795-801(2008).
[24]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH DCC, FUNCTION
IN PHOSPHORYLATION OF DCC, INTERACTION WITH DCC, AND MUTAGENESIS OF
GLN-117; HIS-123 AND LEU-155.
PubMed=21070949; DOI=10.1016/j.str.2010.08.011;
Ma W., Shang Y., Wei Z., Wen W., Wang W., Zhang M.;
"Phosphorylation of DCC by ERK2 is facilitated by direct docking of
the receptor P1 domain to the kinase.";
Structure 18:1502-1511(2010).
-!- 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 (By similarity). Phosphorylates CDK2AP2
(PubMed:12944431). {ECO:0000250|UniProtKB:P28482,
ECO:0000269|PubMed:12944431, ECO:0000269|PubMed:21070949,
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:0000250|UniProtKB:P28482}.
-!- 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-183 and Tyr-185 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-27 by SGK1 results in its
activation by enhancing its interaction with MAP2K1/MEK1 and
MAP2K2/MEK2. Dephosphorylated and inactivated by DUSP3, DUSP6 and
DUSP9. Inactivated by pyrimidylpyrrole inhibitors.
-!- SUBUNIT: Binds both upstream activators and downstream substrates
in multimolecular complexes. Interacts with ADAM15, ARHGEF2, DAPK1
(via death domain), HSF4, IER3, IPO7, MKNK2, MORG1, NISCH, PEA15,
SGK1, and isoform 1 of NEK2 (By similarity). Interacts with DUSP6
(PubMed:16567630). Interacts with ARRB2 (PubMed:11226259).
Interacts (phosphorylated form) with CAV2 ('Tyr-19'-phosphorylated
form); the interaction, promoted by insulin, leads to nuclear
location and MAPK1 activation (PubMed:19778377, PubMed:19427337).
MKNK2 isoform 1 binding prevents from dephosphorylation and
inactivation (By similarity). Interacts with DCC
(PubMed:21070949). The phosphorylated form interacts with PML (By
similarity). Interacts with STYX (By similarity). Interacts with
CDK2AP2 (PubMed:12944431). Interacts with CAVIN4
(PubMed:24567387). {ECO:0000250|UniProtKB:P28482,
ECO:0000250|UniProtKB:P63085, ECO:0000269|PubMed:11226259,
ECO:0000269|PubMed:12944431, ECO:0000269|PubMed:16567630,
ECO:0000269|PubMed:19427337, ECO:0000269|PubMed:19778377,
ECO:0000269|PubMed:21070949, ECO:0000269|PubMed:24567387}.
-!- INTERACTION:
Q63155:Dcc; NbExp=10; IntAct=EBI-397710, EBI-1798965;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
{ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm
{ECO:0000269|PubMed:24567387}. Membrane, caveola
{ECO:0000269|PubMed:24567387}. Note=Associated with the spindle
during prometaphase and metaphase. PEA15-binding and
phosphorylated DAPK1 promote its cytoplasmic retention.
Phosphorylation at Ser- 244 and Ser-246 as well as
autophosphorylation at Thr-188 promote nuclear localization.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Highest levels within the nervous system,
expressed in different tissues, mostly in muscle, thymus and
heart.
-!- DEVELOPMENTAL STAGE: Increased expression during development.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-183 and Tyr-185, which activates
the enzyme. Phosphorylated upon FLT3 and KIT signaling. Ligand-
activated ALK induces tyrosine phosphorylation (By similarity).
Dephosphorylated by PTPRJ at Tyr-185 (By similarity).
Autophosphorylated on threonine and tyrosine residues in vitro,
which correlates with a slow and low level of activation.
Phosphorylation on Ser-27 by SGK1 results in its activation by
enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2 (By
similarity). {ECO:0000250}.
-!- PTM: ISGylated. {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; M64300; AAA41124.1; -; mRNA.
PIR; A40033; A40033.
RefSeq; NP_446294.1; NM_053842.2.
RefSeq; XP_006248720.1; XM_006248658.3.
RefSeq; XP_006248721.1; XM_006248659.3.
RefSeq; XP_008767070.1; XM_008768848.2.
UniGene; Rn.34914; -.
PDB; 1ERK; X-ray; 2.30 A; A=1-358.
PDB; 1GOL; X-ray; 2.80 A; A=1-358.
PDB; 2ERK; X-ray; 2.40 A; A=1-358.
PDB; 2FYS; X-ray; 2.50 A; A/B=2-358.
PDB; 2GPH; X-ray; 1.90 A; A=2-358.
PDB; 2Z7L; X-ray; 2.41 A; A=1-358.
PDB; 3C9W; X-ray; 2.50 A; A/B=2-358.
PDB; 3ERK; X-ray; 2.10 A; A=1-358.
PDB; 3O71; X-ray; 1.95 A; A=1-358.
PDB; 3QYW; X-ray; 1.50 A; A=1-358.
PDB; 3QYZ; X-ray; 1.46 A; A=1-358.
PDB; 3R63; X-ray; 1.70 A; A=1-358.
PDB; 3ZU7; X-ray; 1.97 A; A=3-358.
PDB; 3ZUV; X-ray; 2.72 A; A/C=3-358.
PDB; 4ERK; X-ray; 2.20 A; A=1-358.
PDB; 4GSB; X-ray; 1.80 A; A=1-358.
PDB; 4GT3; X-ray; 1.68 A; A=1-358.
PDB; 4GVA; X-ray; 1.83 A; A=1-358.
PDB; 4I5H; X-ray; 1.90 A; A=2-358.
PDB; 4N4S; X-ray; 2.20 A; A/B=2-358.
PDB; 4QYY; X-ray; 1.65 A; A=1-358.
PDB; 4S2Z; X-ray; 1.48 A; A=1-358.
PDB; 4S30; X-ray; 2.00 A; A=1-358.
PDB; 4S31; X-ray; 1.45 A; A=1-358.
PDB; 4S32; X-ray; 1.34 A; A=1-358.
PDB; 4S33; X-ray; 1.48 A; A=1-358.
PDB; 4S34; X-ray; 2.50 A; A=1-358.
PDB; 4XNE; X-ray; 1.80 A; A=9-354.
PDB; 4XOY; X-ray; 2.10 A; A=8-358.
PDB; 4XOZ; X-ray; 1.95 A; A=8-358.
PDB; 4XP0; X-ray; 1.46 A; A=8-358.
PDB; 4XP2; X-ray; 1.75 A; A=8-358.
PDB; 4XP3; X-ray; 1.78 A; A=8-358.
PDB; 4XRJ; X-ray; 1.69 A; A=9-354.
PDB; 4XRL; X-ray; 2.55 A; A=9-353.
PDB; 5HD4; X-ray; 1.45 A; A=1-358.
PDB; 5HD7; X-ray; 1.69 A; A=1-358.
PDB; 5KE0; X-ray; 1.68 A; A=1-358.
PDB; 5U6I; X-ray; 1.69 A; A=1-358.
PDB; 5UMO; X-ray; 2.26 A; A=4-354.
PDBsum; 1ERK; -.
PDBsum; 1GOL; -.
PDBsum; 2ERK; -.
PDBsum; 2FYS; -.
PDBsum; 2GPH; -.
PDBsum; 2Z7L; -.
PDBsum; 3C9W; -.
PDBsum; 3ERK; -.
PDBsum; 3O71; -.
PDBsum; 3QYW; -.
PDBsum; 3QYZ; -.
PDBsum; 3R63; -.
PDBsum; 3ZU7; -.
PDBsum; 3ZUV; -.
PDBsum; 4ERK; -.
PDBsum; 4GSB; -.
PDBsum; 4GT3; -.
PDBsum; 4GVA; -.
PDBsum; 4I5H; -.
PDBsum; 4N4S; -.
PDBsum; 4QYY; -.
PDBsum; 4S2Z; -.
PDBsum; 4S30; -.
PDBsum; 4S31; -.
PDBsum; 4S32; -.
PDBsum; 4S33; -.
PDBsum; 4S34; -.
PDBsum; 4XNE; -.
PDBsum; 4XOY; -.
PDBsum; 4XOZ; -.
PDBsum; 4XP0; -.
PDBsum; 4XP2; -.
PDBsum; 4XP3; -.
PDBsum; 4XRJ; -.
PDBsum; 4XRL; -.
PDBsum; 5HD4; -.
PDBsum; 5HD7; -.
PDBsum; 5KE0; -.
PDBsum; 5U6I; -.
PDBsum; 5UMO; -.
ProteinModelPortal; P63086; -.
SMR; P63086; -.
BioGrid; 250505; 13.
DIP; DIP-29117N; -.
ELM; P63086; -.
IntAct; P63086; 13.
MINT; MINT-100037; -.
STRING; 10116.ENSRNOP00000002533; -.
BindingDB; P63086; -.
ChEMBL; CHEMBL5233; -.
iPTMnet; P63086; -.
PhosphoSitePlus; P63086; -.
World-2DPAGE; 0004:P63086; -.
PaxDb; P63086; -.
PRIDE; P63086; -.
Ensembl; ENSRNOT00000002533; ENSRNOP00000002533; ENSRNOG00000001849.
GeneID; 116590; -.
KEGG; rno:116590; -.
CTD; 5594; -.
RGD; 70500; Mapk1.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00900000140906; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P63086; -.
KO; K04371; -.
OMA; NCDLKLC; -.
OrthoDB; EOG091G08QL; -.
PhylomeDB; P63086; -.
BRENDA; 2.7.11.24; 5301.
Reactome; R-RNO-111995; phospho-PLA2 pathway.
Reactome; R-RNO-112409; RAF-independent MAPK1/3 activation.
Reactome; R-RNO-112411; MAPK1 (ERK2) activation.
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-437239; Recycling pathway of L1.
Reactome; R-RNO-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-RNO-444257; RSK activation.
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-6798695; Neutrophil degranulation.
Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-RNO-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
Reactome; R-RNO-982772; Growth hormone receptor signaling.
EvolutionaryTrace; P63086; -.
PRO; PR:P63086; -.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000001849; -.
Genevisible; P63086; RN.
GO; GO:0030424; C:axon; IDA:RGD.
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:0032839; C:dendrite cytoplasm; 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: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; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0043204; C:perikaryon; 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:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0016301; F:kinase activity; TAS:RGD.
GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
GO; GO:0004708; F:MAP kinase kinase activity; IEA:Ensembl.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:RGD.
GO; GO:0019902; F:phosphatase binding; IEA:Ensembl.
GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IEA:Ensembl.
GO; GO:0071310; P:cellular response to organic substance; IDA:RGD.
GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
GO; GO:0019858; P:cytosine metabolic process; IEA:Ensembl.
GO; GO:0015966; P:diadenosine tetraphosphate biosynthetic process; IMP:CAFA.
GO; GO:0038127; P:ERBB signaling pathway; IEA:Ensembl.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:CAFA.
GO; GO:0060324; P:face development; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
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; IMP:RGD.
GO; GO:0000189; P:MAPK import into nucleus; IDA:RGD.
GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
GO; GO:0042473; P:outer ear morphogenesis; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IEP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IEP:RGD.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IMP:CAFA.
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:0045893; P:positive regulation of transcription, DNA-templated; IMP:CAFA.
GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
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: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; ISS:UniProtKB.
GO; GO:0043627; P:response to estrogen; IDA:RGD.
GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; IGI:ARUK-UCL.
GO; GO:0009636; P:response to toxic substance; IDA:RGD.
GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; IDA:RGD.
GO; GO:0051403; P:stress-activated MAPK cascade; IEA:Ensembl.
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.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008349; MAPK_ERK1/2.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01770; ERK1ERK2MAPK.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Apoptosis; ATP-binding; Cell cycle;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.2}.
CHAIN 2 358 Mitogen-activated protein kinase 1.
/FTId=PRO_0000186249.
DOMAIN 23 311 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 29 37 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:8639522}.
REGION 103 109 Inhibitor-binding.
MOTIF 183 185 TXY.
COMPBIAS 2 7 Poly-Ala.
ACT_SITE 147 147 Proton acceptor.
BINDING 52 52 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:8639522}.
BINDING 106 106 Inhibitor; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:18571434,
ECO:0000269|PubMed:18767165,
ECO:0000269|PubMed:9753691}.
BINDING 164 164 Inhibitor. {ECO:0000269|PubMed:18571434,
ECO:0000269|PubMed:18767165,
ECO:0000269|PubMed:9753691}.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.2}.
MOD_RES 27 27 Phosphoserine; by SGK1.
{ECO:0000250|UniProtKB:P28482}.
MOD_RES 179 179 Phosphothreonine.
{ECO:0000250|UniProtKB:P27361}.
MOD_RES 183 183 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 185 185 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 188 188 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P28482}.
MOD_RES 244 244 Phosphoserine.
{ECO:0000250|UniProtKB:P28482}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000250|UniProtKB:P28482}.
MOD_RES 282 282 Phosphoserine.
{ECO:0000250|UniProtKB:P28482}.
MUTAGEN 117 117 Q->A: Reduced affinity for DCC. Strongly
reduced affinity for DCC; when associated
with A-123.
{ECO:0000269|PubMed:21070949}.
MUTAGEN 123 123 H->A: Reduced affinity for DCC. Strongly
reduced affinity for DCC; when associated
with A-117.
{ECO:0000269|PubMed:21070949}.
MUTAGEN 155 155 L->A: Reduced affinity for DCC.
{ECO:0000269|PubMed:21070949}.
STRAND 10 17 {ECO:0000244|PDB:5HD4}.
TURN 20 22 {ECO:0000244|PDB:4S32}.
STRAND 23 31 {ECO:0000244|PDB:4S32}.
STRAND 33 42 {ECO:0000244|PDB:4S32}.
TURN 43 46 {ECO:0000244|PDB:4S32}.
STRAND 47 54 {ECO:0000244|PDB:4S32}.
STRAND 57 59 {ECO:0000244|PDB:4S30}.
HELIX 60 75 {ECO:0000244|PDB:4S32}.
STRAND 86 88 {ECO:0000244|PDB:4S32}.
TURN 93 95 {ECO:0000244|PDB:4S32}.
STRAND 99 104 {ECO:0000244|PDB:4S32}.
STRAND 107 109 {ECO:0000244|PDB:4S32}.
HELIX 110 116 {ECO:0000244|PDB:4S32}.
HELIX 121 140 {ECO:0000244|PDB:4S32}.
HELIX 150 152 {ECO:0000244|PDB:4S32}.
STRAND 153 155 {ECO:0000244|PDB:4S32}.
STRAND 161 163 {ECO:0000244|PDB:4S32}.
STRAND 170 172 {ECO:0000244|PDB:3O71}.
HELIX 174 176 {ECO:0000244|PDB:4S32}.
TURN 179 181 {ECO:0000244|PDB:2ERK}.
HELIX 182 184 {ECO:0000244|PDB:3O71}.
HELIX 189 191 {ECO:0000244|PDB:4S32}.
HELIX 194 196 {ECO:0000244|PDB:4S32}.
TURN 197 199 {ECO:0000244|PDB:4S32}.
HELIX 206 221 {ECO:0000244|PDB:4S32}.
HELIX 231 242 {ECO:0000244|PDB:4S32}.
HELIX 247 251 {ECO:0000244|PDB:4S32}.
HELIX 256 264 {ECO:0000244|PDB:4S32}.
HELIX 273 276 {ECO:0000244|PDB:4S32}.
STRAND 278 280 {ECO:0000244|PDB:2ERK}.
HELIX 282 291 {ECO:0000244|PDB:4S32}.
TURN 296 298 {ECO:0000244|PDB:4S32}.
HELIX 302 306 {ECO:0000244|PDB:4S32}.
HELIX 309 311 {ECO:0000244|PDB:4S32}.
TURN 312 314 {ECO:0000244|PDB:4S32}.
HELIX 317 319 {ECO:0000244|PDB:4S32}.
HELIX 329 331 {ECO:0000244|PDB:2ERK}.
STRAND 333 336 {ECO:0000244|PDB:4XRJ}.
HELIX 338 348 {ECO:0000244|PDB:4S32}.
HELIX 350 352 {ECO:0000244|PDB:4S32}.
HELIX 354 356 {ECO:0000244|PDB:1GOL}.
SEQUENCE 358 AA; 41276 MW; 3BBCF22471EDBA0B CRC64;
MAAAAAAGPE MVRGQVFDVG PRYTNLSYIG EGAYGMVCSA YDNLNKVRVA IKKISPFEHQ
TYCQRTLREI KILLRFRHEN IIGINDIIRA PTIEQMKDVY IVQDLMETDL YKLLKTQHLS
NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLLNTTCD LKICDFGLAR VADPDHDHTG
FLTEYVATRW YRAPEIMLNS KGYTKSIDIW SVGCILAEML SNRPIFPGKH YLDQLNHILG
ILGSPSQEDL NCIINLKARN YLLSLPHKNK VPWNRLFPNA DSKALDLLDK MLTFNPHKRI
EVEQALAHPY LEQYYDPSDE PIAEAPFKFD MELDDLPKEK LKELIFEETA RFQPGYRS


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