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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_MOUSE              Reviewed;         358 AA.
P63085; P27703; Q3V1U6;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 161.
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;
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 [MRNA].
STRAIN=SWR/J; TISSUE=Fibroblast;
PubMed=1649458; DOI=10.1093/nar/19.13.3743;
Her J.-H., Wu J.-S., Rall T.B., Sturgill T.W., Weber M.J.;
"Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by
tyrosine phosphorylation.";
Nucleic Acids Res. 19:3743-3743(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Brain, Head, Thymus, and Urinary bladder;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
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).
[4]
PROTEIN SEQUENCE OF 54-65; 76-89; 137-162; 171-189; 193-201 AND
260-268, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 152-190.
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).
[6]
PHOSPHORYLATION AT THR-183 AND TYR-185, AND PARTIAL PROTEIN SEQUENCE.
PubMed=1849075;
Payne D.M., Rossomando A.J., Martino P., Erickson A.K., Her J.-H.,
Shabanowitz J., Hunt D.F., Weber M.J., Sturgill T.W.;
"Identification of the regulatory phosphorylation sites in
pp42/mitogen-activated protein kinase (MAP kinase).";
EMBO J. 10:885-892(1991).
[7]
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).
[8]
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).
[9]
FUNCTION IN PHOSPHORYLATION OF PXN.
PubMed=10753946; DOI=10.1074/jbc.275.15.11333;
Ku H., Meier K.E.;
"Phosphorylation of paxillin via the ERK mitogen-activated protein
kinase cascade in EL4 thymoma cells.";
J. Biol. Chem. 275:11333-11340(2000).
[10]
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).
[11]
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).
[12]
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).
[13]
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).
[14]
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, 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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
ISGYLATION.
PubMed=22022510; DOI=10.1371/journal.pone.0026068;
Maragno A.L., Pironin M., Alcalde H., Cong X., Knobeloch K.P.,
Tangy F., Zhang D.E., Ghysdael J., Quang C.T.;
"ISG15 modulates development of the erythroid lineage.";
PLoS ONE 6:E26068-E26068(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, DCC, FRS2 or
GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2,
RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2,
RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases
(such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which
enable the propagation the MAPK/ERK signal to additional cytosolic
and nuclear targets, thereby extending the specificity of the
cascade. Mediates phosphorylation of TPR in respons to EGF
stimulation. May play a role in the spindle assembly checkpoint.
Phosphorylates PML and promotes its interaction with PIN1, leading
to PML degradation. Phosphorylates CDK2AP2 (By similarity).
{ECO:0000250|UniProtKB:P28482, ECO:0000250|UniProtKB:P63086,
ECO:0000269|PubMed:10753946, ECO:0000269|PubMed:11702783,
ECO:0000269|PubMed:12134156, 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,
ARRB2, DAPK1 (via death domain), HSF4, IER3, IPO7, DUSP6, NISCH,
SGK1, and isoform 1 of NEK2. Interacts (via phosphorylated form)
with TPR (via C-terminal region and phosphorylated form); the
interaction requires dimerization of MAPK1/ERK2 and increases
following EGF stimulation (By similarity). Interacts
(phosphorylated form) with CAV2 ('Tyr-19'-phosphorylated form);
the interaction, promoted by insulin, leads to nuclear location
and MAPK1 activation. Interacts with DCC (By similarity).
Interacts with MORG1 (PubMed:15118098). Interacts with PEA15
(PubMed:16162500). Interacts with MKNK2. MKNK2 isoform 1 binding
prevents from dephosphorylation and inactivation
(PubMed:11702783). The phosphorylated form interacts with PML.
Interacts with STYX. Interacts with CDK2AP2. Interacts with CAVIN4
(By similarity). {ECO:0000250|UniProtKB:P28482,
ECO:0000250|UniProtKB:P63086, ECO:0000269|PubMed:11702783,
ECO:0000269|PubMed:15118098, ECO:0000269|PubMed:16162500}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-397697, EBI-397697;
Q62108:Dlg4; NbExp=3; IntAct=EBI-397697, EBI-300895;
Q9DBB1:Dusp6; NbExp=2; IntAct=EBI-397697, EBI-7812384;
P49841:GSK3B (xeno); NbExp=2; IntAct=EBI-397697, EBI-373586;
Q03172:Hivep1; NbExp=4; IntAct=EBI-397697, EBI-646850;
Q8CDB0:Mknk2; NbExp=23; IntAct=EBI-397697, EBI-646209;
Q8R332-1:Nup58; NbExp=3; IntAct=EBI-397697, EBI-646962;
Q62132:Ptprr; NbExp=5; IntAct=EBI-397697, EBI-6954051;
Q9Z2B9:Rps6ka4; NbExp=3; IntAct=EBI-397697, EBI-412887;
O95863:SNAI1 (xeno); NbExp=3; IntAct=EBI-397697, EBI-1045459;
G3G926:US2 (xeno); NbExp=8; IntAct=EBI-397697, EBI-11692733;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
{ECO:0000250}. Nucleus. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250}. Cytoplasm. Membrane,
caveola {ECO:0000250|UniProtKB:P63086}. Note=Associated with the
spindle during prometaphase and metaphase (By similarity). PEA15-
binding and phosphorylated DAPK1 promote its cytoplasmic
retention. Phosphorylation at Ser-244 and Ser-246 as well as
autophosphorylation at Thr-188 promote nuclear localization (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed.
-!- 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. Ligand-activated ALK induces tyrosine phosphorylation
(By similarity). Dephosphorylated by PTPRJ at Tyr-185 (By
similarity). Phosphorylated upon FLT3 and KIT signaling (By
similarity). {ECO:0000250}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:22022510}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
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EMBL; X58712; CAA41548.1; -; mRNA.
EMBL; AK035386; BAC29053.1; -; mRNA.
EMBL; AK048127; BAC33251.1; -; mRNA.
EMBL; AK087925; BAC40044.1; -; mRNA.
EMBL; AK132241; BAE21053.1; -; mRNA.
EMBL; BC058258; AAH58258.1; -; mRNA.
EMBL; D10939; BAA01733.1; -; mRNA.
CCDS; CCDS27992.1; -.
PIR; S16444; S16444.
RefSeq; NP_001033752.1; NM_001038663.1.
RefSeq; NP_036079.1; NM_011949.3.
RefSeq; XP_006522210.1; XM_006522147.3.
UniGene; Mm.196581; -.
ProteinModelPortal; P63085; -.
SMR; P63085; -.
BioGrid; 204966; 42.
CORUM; P63085; -.
DIP; DIP-661N; -.
ELM; P63085; -.
IntAct; P63085; 34.
MINT; MINT-125264; -.
STRING; 10090.ENSMUSP00000023462; -.
BindingDB; P63085; -.
ChEMBL; CHEMBL2207; -.
iPTMnet; P63085; -.
PhosphoSitePlus; P63085; -.
SwissPalm; P63085; -.
EPD; P63085; -.
MaxQB; P63085; -.
PaxDb; P63085; -.
PeptideAtlas; P63085; -.
PRIDE; P63085; -.
Ensembl; ENSMUST00000023462; ENSMUSP00000023462; ENSMUSG00000063358.
Ensembl; ENSMUST00000069107; ENSMUSP00000065983; ENSMUSG00000063358.
Ensembl; ENSMUST00000115731; ENSMUSP00000111396; ENSMUSG00000063358.
GeneID; 26413; -.
KEGG; mmu:26413; -.
UCSC; uc007yjq.1; mouse.
CTD; 5594; -.
MGI; MGI:1346858; Mapk1.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00900000140906; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P63085; -.
KO; K04371; -.
OMA; NCDLKLC; -.
OrthoDB; EOG091G08QL; -.
PhylomeDB; P63085; -.
TreeFam; TF105097; -.
BRENDA; 2.7.11.24; 3474.
Reactome; R-MMU-111995; phospho-PLA2 pathway.
Reactome; R-MMU-112409; RAF-independent MAPK1/3 activation.
Reactome; R-MMU-112411; MAPK1 (ERK2) activation.
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-437239; Recycling pathway of L1.
Reactome; R-MMU-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-MMU-444257; RSK activation.
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-6798695; Neutrophil degranulation.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
Reactome; R-MMU-982772; Growth hormone receptor signaling.
ChiTaRS; Mapk1; mouse.
PRO; PR:P63085; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000063358; -.
CleanEx; MM_MAPK1; -.
ExpressionAtlas; P63085; baseline and differential.
Genevisible; P63085; MM.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005901; C:caveola; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
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:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:AgBase.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
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; IPI:IntAct.
GO; GO:0016301; F:kinase activity; IDA:MGI.
GO; GO:0004707; F:MAP kinase activity; IDA:MGI.
GO; GO:0004708; F:MAP kinase kinase activity; IMP:MGI.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:Ensembl.
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; IDA:UniProtKB.
GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0009887; P:animal organ morphogenesis; IDA:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI.
GO; GO:0060020; P:Bergmann glial cell differentiation; IGI:MGI.
GO; GO:0061308; P:cardiac neural crest cell development involved in heart development; IGI: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:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IDA:MGI.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
GO; GO:0019858; P:cytosine metabolic process; IDA:MGI.
GO; GO:0015966; P:diadenosine tetraphosphate biosynthetic process; IEA:Ensembl.
GO; GO:0038127; P:ERBB signaling pathway; ISO:MGI.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IGI:MGI.
GO; GO:0060324; P:face development; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:MGI.
GO; GO:0060291; P:long-term synaptic potentiation; IGI:MGI.
GO; GO:0060425; P:lung morphogenesis; IGI:MGI.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; IDA:MGI.
GO; GO:0000165; P:MAPK cascade; IDA:MGI.
GO; GO:0000189; P:MAPK import into nucleus; IEA:Ensembl.
GO; GO:0045596; P:negative regulation of cell differentiation; IGI:MGI.
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; IDA:UniProtKB.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Ensembl.
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:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA: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: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; IGI:MGI.
GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; NAS: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; IEA:Ensembl.
GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
GO; GO:0035094; P:response to nicotine; IGI:ARUK-UCL.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0051403; P:stress-activated MAPK cascade; ISO:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; IDA: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; NAS: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; 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:0000250|UniProtKB:P28482}.
CHAIN 2 358 Mitogen-activated protein kinase 1.
/FTId=PRO_0000186248.
DOMAIN 23 311 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 29 37 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 103 106 Inhibitor-binding. {ECO:0000250}.
REGION 151 152 Inhibitor-binding. {ECO:0000250}.
MOTIF 183 185 TXY.
COMPBIAS 2 7 Poly-Ala.
ACT_SITE 147 147 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 52 52 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 52 52 Inhibitor. {ECO:0000250}.
BINDING 106 106 Inhibitor; via amide nitrogen and
carbonyl oxygen. {ECO:0000250}.
BINDING 112 112 Inhibitor. {ECO:0000250}.
BINDING 152 152 Inhibitor. {ECO:0000250}.
BINDING 164 164 Inhibitor. {ECO:0000250}.
BINDING 165 165 Inhibitor. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P28482}.
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; by MAP2K1 and MAP2K2.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:1849075}.
MOD_RES 185 185 Phosphotyrosine; by MAP2K1 and MAP2K2.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:1849075}.
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}.
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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