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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.
17-JUN-2020, entry version 184.
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 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).
[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]
INTERACTION WITH DUSP7.
PubMed=27783954; DOI=10.1016/j.celrep.2016.10.007;
Tischer T., Schuh M.;
"The phosphatase Dusp7 drives meiotic resumption and chromosome alignment
in mouse oocytes.";
Cell Rep. 17:1426-1437(2016).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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:
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-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 DUSP1, 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). Interacts with DUSP7; the interaction enhances DUSP7
phosphatase activity (PubMed:27783954). {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,
ECO:0000269|PubMed:27783954}.
-!- INTERACTION:
P63086; 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). Dephosphorylated by DUSP1 at Thr-183 and
Tyr-185. {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.
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.
PDB; 6CPW; X-ray; 1.85 A; A=1-358.
PDB; 6DCG; X-ray; 1.45 A; A=1-358.
PDB; 6FI3; X-ray; 1.52 A; A=1-358.
PDB; 6FI6; X-ray; 1.65 A; A=1-358.
PDB; 6FJ0; X-ray; 1.66 A; A=1-358.
PDB; 6FJB; X-ray; 1.85 A; A=1-358.
PDB; 6FJZ; X-ray; 1.86 A; A=1-358.
PDB; 6FLE; X-ray; 1.48 A; A=1-358.
PDB; 6FLV; X-ray; 1.91 A; A=1-358.
PDB; 6FMA; X-ray; 1.67 A; A=1-358.
PDB; 6FN5; X-ray; 1.93 A; A=1-358.
PDB; 6FQ7; X-ray; 1.60 A; A=1-358.
PDB; 6FR1; X-ray; 1.56 A; A=1-358.
PDB; 6FRP; X-ray; 1.53 A; A=1-358.
PDB; 6FXV; X-ray; 1.53 A; A=1-358.
PDB; 6OPK; X-ray; 2.54 A; A=7-358.
PDB; 6OT6; X-ray; 1.65 A; A=1-358.
PDB; 6OTS; X-ray; 2.10 A; A=1-358.
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; -.
PDBsum; 6CPW; -.
PDBsum; 6DCG; -.
PDBsum; 6FI3; -.
PDBsum; 6FI6; -.
PDBsum; 6FJ0; -.
PDBsum; 6FJB; -.
PDBsum; 6FJZ; -.
PDBsum; 6FLE; -.
PDBsum; 6FLV; -.
PDBsum; 6FMA; -.
PDBsum; 6FN5; -.
PDBsum; 6FQ7; -.
PDBsum; 6FR1; -.
PDBsum; 6FRP; -.
PDBsum; 6FXV; -.
PDBsum; 6OPK; -.
PDBsum; 6OT6; -.
PDBsum; 6OTS; -.
SMR; P63086; -.
BioGRID; 250505; 14.
DIP; DIP-29117N; -.
ELM; P63086; -.
IntAct; P63086; 14.
MINT; P63086; -.
STRING; 10116.ENSRNOP00000002533; -.
BindingDB; P63086; -.
ChEMBL; CHEMBL5233; -.
CarbonylDB; P63086; -.
iPTMnet; P63086; -.
PhosphoSitePlus; P63086; -.
World-2DPAGE; 0004:P63086; -.
jPOST; 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; ENSGT00940000156771; -.
HOGENOM; CLU_000288_181_1_1; -.
InParanoid; P63086; -.
KO; K04371; -.
OMA; DIYIVQC; -.
OrthoDB; 741207at2759; -.
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-170968; Frs2-mediated activation.
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-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-5668599; RHO GTPases Activate NADPH Oxidases.
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-74749; Signal attenuation.
Reactome; R-RNO-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
Reactome; R-RNO-8939211; ESR-mediated signaling.
Reactome; R-RNO-9634635; Estrogen-stimulated signaling through PRKCZ.
Reactome; R-RNO-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
Reactome; R-RNO-982772; Growth hormone receptor signaling.
EvolutionaryTrace; P63086; -.
PRO; PR:P63086; -.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000001849; Expressed in brain and 9 other tissues.
Genevisible; P63086; RN.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005901; C:caveola; IDA:UniProtKB.
GO; GO:0005623; C:cell; IEA:GOC.
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: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; ISO:RGD.
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:0014069; C:postsynaptic density; IDA:SynGO.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0031143; C:pseudopodium; ISO:RGD.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0016301; F:kinase activity; ISO:RGD.
GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
GO; GO:0004708; F:MAP kinase kinase activity; ISO:RGD.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:RGD.
GO; GO:0019902; F:phosphatase binding; ISO:RGD.
GO; GO:0001784; F:phosphotyrosine residue binding; ISO:RGD.
GO; GO:0004672; F:protein kinase activity; ISO:RGD.
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 CTD heptapeptide repeat kinase activity; ISO:RGD.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0007568; P:aging; IDA:RGD.
GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0050853; P:B cell receptor signaling pathway; ISO:RGD.
GO; GO:0060020; P:Bergmann glial cell differentiation; ISO:RGD.
GO; GO:0061308; P:cardiac neural crest cell development involved in heart development; ISO:RGD.
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; ISO:RGD.
GO; GO:0071276; P:cellular response to cadmium ion; ISO:RGD.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
GO; GO:1903351; P:cellular response to dopamine; ISO:RGD.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISO:RGD.
GO; GO:0071310; P:cellular response to organic substance; IDA:RGD.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:RGD.
GO; GO:0019858; P:cytosine metabolic process; ISO:RGD.
GO; GO:0046697; P:decidualization; IDA:RGD.
GO; GO:0015966; P:diadenosine tetraphosphate biosynthetic process; IMP:CAFA.
GO; GO:0038127; P:ERBB signaling pathway; ISO:RGD.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:CAFA.
GO; GO:0060324; P:face development; ISO:RGD.
GO; GO:0007507; P:heart development; ISO:RGD.
GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
GO; GO:0060716; P:labyrinthine layer blood vessel development; ISO:RGD.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:RGD.
GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
GO; GO:0060425; P:lung morphogenesis; ISO:RGD.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; ISO:RGD.
GO; GO:0000165; P:MAPK cascade; IMP:RGD.
GO; GO:0045596; P:negative regulation of cell differentiation; ISO:RGD.
GO; GO:0014032; P:neural crest cell development; ISO:RGD.
GO; GO:0042473; P:outer ear morphogenesis; ISO:RGD.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:UniProtKB.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:RGD.
GO; GO:0030335; P:positive regulation of cell migration; IEP:RGD.
GO; GO:0008284; P:positive regulation of cell population proliferation; IEP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:RGD.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB.
GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD.
GO; GO:1904355; P:positive regulation of telomere capping; ISO:RGD.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD.
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; ISO:RGD.
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: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; ISO:RGD.
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; ISO:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
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; ISO:RGD.
GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
GO; GO:0048538; P:thymus development; ISO:RGD.
GO; GO:0030878; P:thyroid gland development; ISO:RGD.
GO; GO:0060440; P:trachea formation; ISO:RGD.
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; Apoptosis; ATP-binding; Cell cycle; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Kinase; Membrane;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000269|Ref.2"
CHAIN 2..358
/note="Mitogen-activated protein kinase 1"
/id="PRO_0000186249"
DOMAIN 23..311
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 29..37
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000269|PubMed:8639522"
REGION 103..109
/note="Inhibitor-binding"
MOTIF 183..185
/note="TXY"
COMPBIAS 2..7
/note="Poly-Ala"
ACT_SITE 147
/note="Proton acceptor"
BINDING 52
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000269|PubMed:8639522"
BINDING 106
/note="Inhibitor; via amide nitrogen and carbonyl oxygen"
/evidence="ECO:0000269|PubMed:18571434,
ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:9753691"
BINDING 164
/note="Inhibitor"
/evidence="ECO:0000269|PubMed:18571434,
ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:9753691"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000269|Ref.2"
MOD_RES 27
/note="Phosphoserine; by SGK1"
/evidence="ECO:0000250|UniProtKB:P28482"
MOD_RES 183
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:22673903"
MOD_RES 185
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:22673903"
MOD_RES 188
/note="Phosphothreonine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P28482"
MOD_RES 244
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P28482"
MOD_RES 246
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P28482"
MOD_RES 282
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P28482"
MUTAGEN 117
/note="Q->A: Reduced affinity for DCC. Strongly reduced
affinity for DCC; when associated with A-123."
/evidence="ECO:0000269|PubMed:21070949"
MUTAGEN 123
/note="H->A: Reduced affinity for DCC. Strongly reduced
affinity for DCC; when associated with A-117."
/evidence="ECO:0000269|PubMed:21070949"
MUTAGEN 155
/note="L->A: Reduced affinity for DCC."
/evidence="ECO:0000269|PubMed:21070949"
STRAND 10..17
/evidence="ECO:0000244|PDB:5HD4"
TURN 20..22
/evidence="ECO:0000244|PDB:4S32"
STRAND 23..31
/evidence="ECO:0000244|PDB:4S32"
STRAND 33..42
/evidence="ECO:0000244|PDB:4S32"
TURN 43..46
/evidence="ECO:0000244|PDB:4S32"
STRAND 47..54
/evidence="ECO:0000244|PDB:4S32"
STRAND 57..59
/evidence="ECO:0000244|PDB:6FXV"
HELIX 60..75
/evidence="ECO:0000244|PDB:4S32"
STRAND 86..88
/evidence="ECO:0000244|PDB:4S32"
TURN 93..95
/evidence="ECO:0000244|PDB:4S32"
STRAND 99..104
/evidence="ECO:0000244|PDB:4S32"
STRAND 107..109
/evidence="ECO:0000244|PDB:4S32"
HELIX 110..116
/evidence="ECO:0000244|PDB:4S32"
HELIX 121..140
/evidence="ECO:0000244|PDB:4S32"
HELIX 150..152
/evidence="ECO:0000244|PDB:4S32"
STRAND 153..155
/evidence="ECO:0000244|PDB:4S32"
STRAND 161..163
/evidence="ECO:0000244|PDB:4S32"
STRAND 170..172
/evidence="ECO:0000244|PDB:3O71"
HELIX 174..176
/evidence="ECO:0000244|PDB:4S32"
TURN 179..181
/evidence="ECO:0000244|PDB:2ERK"
HELIX 182..184
/evidence="ECO:0000244|PDB:3O71"
HELIX 189..191
/evidence="ECO:0000244|PDB:4S32"
HELIX 194..196
/evidence="ECO:0000244|PDB:4S32"
TURN 197..199
/evidence="ECO:0000244|PDB:4S32"
TURN 200..202
/evidence="ECO:0000244|PDB:6OPK"
HELIX 206..221
/evidence="ECO:0000244|PDB:4S32"
HELIX 231..242
/evidence="ECO:0000244|PDB:4S32"
HELIX 247..251
/evidence="ECO:0000244|PDB:4S32"
HELIX 256..264
/evidence="ECO:0000244|PDB:4S32"
HELIX 273..276
/evidence="ECO:0000244|PDB:4S32"
STRAND 278..280
/evidence="ECO:0000244|PDB:2ERK"
HELIX 282..291
/evidence="ECO:0000244|PDB:4S32"
TURN 296..298
/evidence="ECO:0000244|PDB:4S32"
HELIX 302..306
/evidence="ECO:0000244|PDB:4S32"
HELIX 309..311
/evidence="ECO:0000244|PDB:4S32"
TURN 312..314
/evidence="ECO:0000244|PDB:4S32"
HELIX 317..319
/evidence="ECO:0000244|PDB:4S32"
HELIX 331..333
/evidence="ECO:0000244|PDB:4N4S"
STRAND 334..336
/evidence="ECO:0000244|PDB:6OT6"
HELIX 338..348
/evidence="ECO:0000244|PDB:4S32"
HELIX 350..352
/evidence="ECO:0000244|PDB:4S32"
HELIX 354..356
/evidence="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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EIAAB24845 ERK-4,Extracellular signal-regulated kinase 4,MAP kinase 4,MAP kinase isoform p63,MAPK 4,Mapk4,Mitogen-activated protein kinase 4,MNK2,p63-MAPK,Prkm4,Rat,Rattus norvegicus
EIAAB24844 ERK4,ERK-4,Extracellular signal-regulated kinase 4,Homo sapiens,Human,MAP kinase 4,MAP kinase isoform p63,MAPK 4,MAPK4,Mitogen-activated protein kinase 4,p63-MAPK,PRKM4
EIAAB24848 ERK3,ERK-3,Extracellular signal-regulated kinase 3,Homo sapiens,Human,MAP kinase 6,MAP kinase isoform p97,MAPK 6,MAPK6,Mitogen-activated protein kinase 6,p97-MAPK,PRKM6