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Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (CRK1) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)

 MK14_MOUSE              Reviewed;         360 AA.
P47811; B2KF37; B2KF38; O08666; Q3U6R5; Q3UZS3; Q8C289; Q9JLV8;
Q9QZ80;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 199.
RecName: Full=Mitogen-activated protein kinase 14;
Short=MAP kinase 14;
Short=MAPK 14;
EC=2.7.11.24 {ECO:0000269|PubMed:18669639, ECO:0000269|PubMed:22375048};
AltName: Full=CRK1;
AltName: Full=Mitogen-activated protein kinase p38 alpha;
Short=MAP kinase p38 alpha;
Name=Mapk14; Synonyms=Crk1, Csbp1, Csbp2;
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] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=7914033; DOI=10.1126/science.7914033;
Han J., Lee J.-D., Bibbs L., Ulevitch R.J.;
"A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian
cells.";
Science 265:808-811(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Brain;
Higashitsuji H., Fujita J.;
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Kidney;
Faccio L., Fusco C., Zervos S.A.;
"Piccolo, a new alternative spliced form of p38/CSBP1/Mxi2 that is
specifically expressed in kidney and liver.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
STRAIN=C57BL/6J; TISSUE=Bone marrow, Pituitary, and Thymus;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 94-318 (ISOFORM 3).
TISSUE=Testis;
Yin Z., Li J., Sha J., Zhou Z., Lin M., Wang L.;
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 154-186.
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).
[9]
MUTAGENESIS.
PubMed=7839144; DOI=10.1126/science.7839144;
Derijard B., Raingeaud J., Barrett T., Wu I.-H., Han J.,
Ulevitch R.J., Davis R.J.;
"Independent human MAP-kinase signal transduction pathways defined by
MEK and MKK isoforms.";
Science 267:682-685(1995).
[10]
INTERACTION WITH PTPRR, AND SUBCELLULAR LOCATION.
PubMed=10601328; DOI=10.1083/jcb.147.6.1129;
Blanco-Aparicio C., Torres J., Pulido R.;
"A novel regulatory mechanism of MAP kinases activation and nuclear
translocation mediated by PKA and the PTP-SL tyrosine phosphatase.";
J. Cell Biol. 147:1129-1136(1999).
[11]
FUNCTION, AND ENZYME REGULATION.
TISSUE=Embryonic stem cell;
PubMed=10704466; DOI=10.1084/jem.191.5.859;
Allen M., Svensson L., Roach M., Hambor J., McNeish J., Gabel C.A.;
"Deficiency of the stress kinase p38alpha results in embryonic
lethality: characterization of the kinase dependence of stress
responses of enzyme-deficient embryonic stem cells.";
J. Exp. Med. 191:859-870(2000).
[12]
FUNCTION, AND SUBUNIT.
STRAIN=C57BL/6J;
PubMed=10943842; DOI=10.1016/S0092-8674(00)00027-1;
Tamura K., Sudo T., Senftleben U., Dadak A.M., Johnson R., Karin M.;
"Requirement for p38alpha in erythropoietin expression: a role for
stress kinases in erythropoiesis.";
Cell 102:221-231(2000).
[13]
FUNCTION IN ACTIVATION OF RPS6KA5/MSK1 AND RPS6KA4/MSK2.
PubMed=11909979; DOI=10.1128/MCB.22.8.2871-2881.2002;
Wiggin G.R., Soloaga A., Foster J.M., Murray-Tait V., Cohen P.,
Arthur J.S.;
"MSK1 and MSK2 are required for the mitogen- and stress-induced
phosphorylation of CREB and ATF1 in fibroblasts.";
Mol. Cell. Biol. 22:2871-2881(2002).
[14]
INTERACTION WITH SPAG9.
PubMed=12391307; DOI=10.1073/pnas.232310199;
Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
"JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules
and transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
[15]
INTERACTION WITH GADD45A, PHOSPHORYLATION AT TYR-323,
AUTOPHOSPHORYLATION, ENZYME REGULATION, AND FUNCTION.
PubMed=15735649; DOI=10.1038/ni1176;
Salvador J.M., Mittelstadt P.R., Belova G.I., Fornace A.J. Jr.,
Ashwell J.D.;
"The autoimmune suppressor Gadd45alpha inhibits the T cell alternative
p38 activation pathway.";
Nat. Immunol. 6:396-402(2005).
[16]
INTERACTION WITH SUPT20H.
PubMed=16751104; DOI=10.1016/j.cell.2006.03.048;
Zohn I.E., Li Y., Skolnik E.Y., Anderson K.V., Han J., Niswander L.;
"p38 and a p38-interacting protein are critical for downregulation of
E-cadherin during mouse gastrulation.";
Cell 125:957-969(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, 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).
[19]
PHOSPHORYLATION AT THR-180 AND TYR-182, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
PubMed=18669639; DOI=10.1074/jbc.M801703200;
Zhang Y.Y., Mei Z.Q., Wu J.W., Wang Z.X.;
"Enzymatic activity and substrate specificity of mitogen-activated
protein kinase p38alpha in different phosphorylation states.";
J. Biol. Chem. 283:26591-26601(2008).
[20]
REVIEW ON FUNCTION.
PubMed=12452429; DOI=10.1515/BC.2002.173;
Shi Y., Gaestel M.;
"In the cellular garden of forking paths: how p38 MAPKs signal for
downstream assistance.";
Biol. Chem. 383:1519-1536(2002).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, 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).
[22]
REVIEW ON ENZYME REGULATION, AND REVIEW ON FUNCTION.
PubMed=20626350; DOI=10.1042/BJ20100323;
Cuadrado A., Nebreda A.R.;
"Mechanisms and functions of p38 MAPK signalling.";
Biochem. J. 429:403-417(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, 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).
[24]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=9122194; DOI=10.1073/pnas.94.6.2327;
Wang Z., Harkins P.C., Ulevitch R.J., Han J., Cobb M.H.,
Goldsmith E.J.;
"The structure of mitogen-activated protein kinase p38 at 2.1-A
resolution.";
Proc. Natl. Acad. Sci. U.S.A. 94:2327-2332(1997).
[25]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MEF2A AND
MAP2K3.
PubMed=12086621; DOI=10.1016/S1097-2765(02)00525-7;
Chang C.I., Xu B.E., Akella R., Cobb M.H., Goldsmith E.J.;
"Crystal structures of MAP kinase p38 complexed to the docking sites
on its nuclear substrate MEF2A and activator MKK3b.";
Mol. Cell 9:1241-1249(2002).
[26]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=15837310; DOI=10.1016/j.bmcl.2005.03.007;
Golebiowski A., Townes J.A., Laufersweiler M.J., Brugel T.A.,
Clark M.P., Clark C.M., Djung J.F., Laughlin S.K., Sabat M.P.,
Bookland R.G., VanRens J.C., De B., Hsieh L.C., Janusz M.J.,
Walter R.L., Webster M.E., Mekel M.J.;
"The development of monocyclic pyrazolone based cytokine synthesis
inhibitors.";
Bioorg. Med. Chem. Lett. 15:2285-2289(2005).
[27]
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=15837333; DOI=10.1016/j.bmcl.2005.02.066;
Laughlin S.K., Clark M.P., Djung J.F., Golebiowski A., Brugel T.A.,
Sabat M., Bookland R.G., Laufersweiler M.J., VanRens J.C.,
Townes J.A., De B., Hsieh L.C., Xu S.C., Walter R.L., Mekel M.J.,
Janusz M.J.;
"The development of new isoxazolone based inhibitors of tumor necrosis
factor-alpha (TNF-alpha) production.";
Bioorg. Med. Chem. Lett. 15:2399-2403(2005).
[28]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-360 IN COMPLEX WITH
MAPKAPK2.
PubMed=17395714; DOI=10.1073/pnas.0701679104;
White A., Pargellis C.A., Studts J.M., Werneburg B.G., Farmer B.T. II;
"Molecular basis of MAPK-activated protein kinase 2:p38 assembly.";
Proc. Natl. Acad. Sci. U.S.A. 104:6353-6358(2007).
[29]
X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) IN COMPLEX WITH DUSP10,
CATALYTIC ACTIVITY, DEPHOSPHORYLATION BY DUSP10, AND INTERACTION WITH
DUSP10.
PubMed=22375048; DOI=10.1126/scisignal.2002241;
Zhang Y.Y., Wu J.W., Wang Z.X.;
"A distinct interaction mode revealed by the crystal structure of the
kinase p38alpha with the MAPK binding domain of the phosphatase
MKP5.";
Sci. Signal. 4:RA88-RA88(2011).
-!- FUNCTION: Serine/threonine kinase which acts as an essential
component of the MAP kinase signal transduction pathway. MAPK14 is
one of the four p38 MAPKs which play an important role in the
cascades of cellular responses evoked by extracellular stimuli
such as proinflammatory cytokines or physical stress leading to
direct activation of transcription factors. Accordingly, p38 MAPKs
phosphorylate a broad range of proteins and it has been estimated
that they may have approximately 200 to 300 substrates each. Some
of the targets are downstream kinases which are activated through
phosphorylation and further phosphorylate additional targets.
RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and
activate transcription factors such as CREB1, ATF1, the NF-kappa-B
isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate
histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and
RPS6KA4/MSK2 play important roles in the rapid induction of
immediate-early genes in response to stress or mitogenic stimuli,
either by inducing chromatin remodeling or by recruiting the
transcription machinery. On the other hand, two other kinase
targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control
of gene expression mostly at the post-transcriptional level, by
phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by
regulating EEF2K, which is important for the elongation of mRNA
during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases
activated by p38 MAPKs, regulate protein synthesis by
phosphorylating the initiation factor EIF4E2. MAPK14 interacts
also with casein kinase II, leading to its activation through
autophosphorylation and further phosphorylation of TP53/p53. In
the cytoplasm, the p38 MAPK pathway is an important regulator of
protein turnover. For example, CFLAR is an inhibitor of TNF-
induced apoptosis whose proteasome-mediated degradation is
regulated by p38 MAPK phosphorylation. In a similar way, MAPK14
phosphorylates the ubiquitin ligase SIAH2, regulating its activity
towards EGLN3. MAPK14 may also inhibit the lysosomal degradation
pathway of autophagy by interfering with the intracellular
trafficking of the transmembrane protein ATG9. Another function of
MAPK14 is to regulate the endocytosis of membrane receptors by
different mechanisms that impinge on the small GTPase RAB5A. In
addition, clathrin-mediated EGFR internalization induced by
inflammatory cytokines and UV irradiation depends on MAPK14-
mediated phosphorylation of EGFR itself as well as of RAB5A
effectors. Ectodomain shedding of transmembrane proteins is
regulated by p38 MAPKs as well. In response to inflammatory
stimuli, p38 MAPKs phosphorylate the membrane-associated
metalloprotease ADAM17. Such phosphorylation is required for
ADAM17-mediated ectodomain shedding of TGF-alpha family ligands,
which results in the activation of EGFR signaling and cell
proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be
translocated from the extracellular space into the cytosol and
nucleus of target cells, and regulates processes such as rRNA
synthesis and cell growth. FGFR1 translocation requires p38 MAPK
activation. In the nucleus, many transcription factors are
phosphorylated and activated by p38 MAPKs in response to different
stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH,
DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as
important modulators of gene expression by regulating chromatin
modifiers and remodelers. The promoters of several genes involved
in the inflammatory response, such as IL6, IL8 and IL12B, display
a p38 MAPK-dependent enrichment of histone H3 phosphorylation on
'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This
phosphorylation enhances the accessibility of the cryptic NF-
kappa-B-binding sites marking promoters for increased NF-kappa-B
recruitment. Phosphorylates CDC25B and CDC25C which is required
for binding to 14-3-3 proteins and leads to initiation of a G2
delay after ultraviolet radiation. Phosphorylates TIAR following
DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA
degradation. The p38 MAPKs may also have kinase-independent roles,
which are thought to be due to the binding to targets in the
absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by
the OGT is regulated by MAPK14, and, although OGT does not seem to
be phosphorylated by MAPK14, their interaction increases upon
MAPK14 activation induced by glucose deprivation. This interaction
may regulate OGT activity by recruiting it to specific targets
such as neurofilament H, stimulating its O-Glc-N-acylation.
Required in mid-fetal development for the growth of embryo-derived
blood vessels in the labyrinth layer of the placenta. Also plays
an essential role in developmental and stress-induced
erythropoiesis, through regulation of EPO gene expression.
Phosphorylates S100A9 at 'Thr-113' (By similarity).
{ECO:0000250|UniProtKB:Q16539, ECO:0000269|PubMed:10704466,
ECO:0000269|PubMed:10943842, ECO:0000269|PubMed:11909979,
ECO:0000269|PubMed:15735649}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:18669639, ECO:0000269|PubMed:22375048}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Activated by cell stresses such as DNA damage,
heat shock, osmotic shock, anisomycin and sodium arsenite, as well
as pro-inflammatory stimuli such as bacterial lipopolysaccharide
(LPS) and interleukin-1. Activation occurs through dual
phosphorylation of Thr-180 and Tyr-182 by either of two dual
specificity kinases, MAP2K3/MKK3 or MAP2K6/MKK6, and potentially
also MAP2K4/MKK4, as well as by TAB1-mediated autophosphorylation.
MAPK14 phosphorylated on both Thr-180 and Tyr-182 is 10-20-fold
more active than MAPK14 phosphorylated only on Thr-180, whereas
MAPK14 phosphorylated on Tyr-182 alone is inactive. whereas Thr-
180 is necessary for catalysis, Tyr-182 may be required for auto-
activation and substrate recognition. Phosphorylated at Tyr-323 by
ZAP70 in an alternative activation pathway in response to TCR
signaling in T-cells. This alternative pathway is inhibited by
GADD45A. Inhibited by dual specificity phosphatases, such as
DUSP1, DUSP10, and DUSP16. Specifically inhibited by the binding
of pyridinyl-imidazole compounds, which are cytokine-suppressive
anti-inflammatory drugs (CSAID). SB203580 is an inhibitor of
MAPK14. {ECO:0000269|PubMed:10704466, ECO:0000269|PubMed:15735649,
ECO:0000269|PubMed:18669639}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=212 uM for ATP (when both Thr-180 and Tyr-182 are
phosphorylated) {ECO:0000269|PubMed:18669639};
KM=1669 uM for ATP (when only Thr-180 is phosphorylated)
{ECO:0000269|PubMed:18669639};
KM=656 uM for EGFR peptide as a substrate (when both Thr-180 and
Tyr-182 are phosphorylated) {ECO:0000269|PubMed:18669639};
KM=2800 uM for EGFR peptide as a substrate (when only Thr-180 is
phosphorylated) {ECO:0000269|PubMed:18669639};
KM=2.03 uM for ATF2 as a substrate (when both Thr-180 and Tyr-
182 are phosphorylated) {ECO:0000269|PubMed:18669639};
KM=20.1 uM for ATF2 as a substrate (when only Thr-180 is
phosphorylated) {ECO:0000269|PubMed:18669639};
-!- SUBUNIT: Component of a signaling complex containing at least
AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13
interacts directly with PKN1, which in turn recruits MAPK14,
MAP2K3 and ZAK (By similarity). Binds to a kinase interaction
motif within the protein tyrosine phosphatase, PTPRR (By
similarity). This interaction retains MAPK14 in the cytoplasm and
prevents nuclear accumulation (By similarity). Interacts with
SPAG9 and GADD45A (By similarity). Interacts with CDC25B, CDC25C,
DUSP1, DUSP10, DUSP16, NP60, SUPT20H and TAB1. Interacts with
casein kinase II subunits CSNK2A1 and CSNK2B. Interacts with
PPM1D. Interacts with CDK5RAP3; recruits PPM1D to MAPK14 and may
regulate its dephosphorylation (By similarity).
{ECO:0000250|UniProtKB:Q16539, ECO:0000269|PubMed:10601328,
ECO:0000269|PubMed:10943842, ECO:0000269|PubMed:12391307,
ECO:0000269|PubMed:15735649, ECO:0000269|PubMed:16751104,
ECO:0000269|PubMed:22375048}.
-!- INTERACTION:
Q99956:DUSP9 (xeno); NbExp=2; IntAct=EBI-298727, EBI-3906678;
Q61233:Lcp1; NbExp=5; IntAct=EBI-298727, EBI-309345;
Q9WUI1:Mapk11; NbExp=10; IntAct=EBI-298727, EBI-645081;
P49138:Mapkapk2; NbExp=2; IntAct=EBI-298727, EBI-298776;
P35236:PTPN7 (xeno); NbExp=2; IntAct=EBI-298727, EBI-2265723;
P55012:Slc12a2; NbExp=2; IntAct=EBI-298727, EBI-621078;
Q9Z1W9:Stk39; NbExp=2; IntAct=EBI-298727, EBI-444764;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10601328}.
Nucleus {ECO:0000269|PubMed:10601328}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P47811-1; Sequence=Displayed;
Name=2; Synonyms=Piccolo;
IsoId=P47811-2; Sequence=VSP_004846, VSP_007545;
Name=3;
IsoId=P47811-3; Sequence=VSP_007544;
Note=Ref.2 (BAA19741) sequence is in conflict in position:
238:L->M. {ECO:0000305};
Name=4;
IsoId=P47811-4; Sequence=VSP_022359;
-!- TISSUE SPECIFICITY: Macrophages, monocytes, T- and B-lymphocytes.
Isoform 2 is specifically expressed in kidney and liver.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-180 and Tyr-182 by the MAP2Ks
MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6 in response to
inflammatory cytokines, environmental stress or growth factors,
which activates the enzyme. Dual phosphorylation can also be
mediated by TAB1-mediated autophosphorylation. TCR engagement in
T-cells also leads to Tyr-323 phosphorylation by ZAP70.
Dephosphorylated and inactivated by DUPS1, DUSP10 and DUSP16.
PPM1D also mediates dephosphorylation and inactivation of MAPK14
(By similarity). {ECO:0000250|UniProtKB:Q16539,
ECO:0000269|PubMed:15735649, ECO:0000269|PubMed:18669639}.
-!- PTM: Acetylated at Lys-53 and Lys-152 by KAT2B and EP300.
Acetylation at Lys-53 increases the affinity for ATP and enhances
kinase activity. Lys-53 and Lys-152 are deacetylated by HDAC3 (By
similarity). {ECO:0000250|UniProtKB:Q16539}.
-!- PTM: Ubiquitinated. Ubiquitination leads to degradation by the
proteasome pathway (By similarity).
{ECO:0000250|UniProtKB:Q16539}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U10871; AAA20888.1; -; mRNA.
EMBL; D83073; BAA19741.1; -; mRNA.
EMBL; AF128892; AAF34818.1; -; mRNA.
EMBL; AK151348; BAE30324.1; -; mRNA.
EMBL; AK153025; BAE31659.1; -; mRNA.
EMBL; AK089059; BAC40726.1; -; mRNA.
EMBL; AK133684; BAE21782.1; -; mRNA.
EMBL; CT009661; CAQ52036.1; -; Genomic_DNA.
EMBL; CT009661; CAQ52037.1; -; Genomic_DNA.
EMBL; BC012235; AAH12235.1; -; mRNA.
EMBL; AF195850; AAF06348.1; -; mRNA.
EMBL; X65067; CAA46200.1; -; mRNA.
CCDS; CCDS28583.1; -. [P47811-1]
CCDS; CCDS50048.1; -. [P47811-3]
CCDS; CCDS50049.1; -. [P47811-4]
PIR; I49066; I49066.
RefSeq; NP_001161980.1; NM_001168508.1. [P47811-3]
RefSeq; NP_001161985.1; NM_001168513.1. [P47811-4]
RefSeq; NP_001161986.1; NM_001168514.1. [P47811-4]
RefSeq; NP_036081.1; NM_011951.3. [P47811-1]
UniGene; Mm.311337; -.
PDB; 1LEW; X-ray; 2.30 A; A=13-360.
PDB; 1LEZ; X-ray; 2.30 A; A=1-360.
PDB; 1YW2; X-ray; 2.01 A; A=1-360.
PDB; 1YWR; X-ray; 1.95 A; A=1-360.
PDB; 2EWA; X-ray; 2.10 A; A=1-360.
PDB; 2GHL; X-ray; 2.10 A; A=5-352.
PDB; 2GHM; X-ray; 2.35 A; A=5-352.
PDB; 2GTM; X-ray; 1.90 A; A=5-352.
PDB; 2GTN; X-ray; 1.80 A; A=5-352.
PDB; 2OZA; X-ray; 2.70 A; B=2-360.
PDB; 2PUU; X-ray; 2.50 A; A=5-352.
PDB; 3P4K; X-ray; 2.30 A; A=1-360.
PDB; 3P5K; X-ray; 2.09 A; A=2-360.
PDB; 3P78; X-ray; 2.30 A; A=2-360.
PDB; 3P79; X-ray; 2.10 A; A=2-360.
PDB; 3P7A; X-ray; 2.31 A; A=2-360.
PDB; 3P7B; X-ray; 1.90 A; A=2-360.
PDB; 3P7C; X-ray; 2.30 A; A=2-360.
PDB; 3PY3; X-ray; 2.10 A; A=1-360.
PDB; 3TG1; X-ray; 2.71 A; A=1-360.
PDB; 4KA3; X-ray; 2.71 A; A=1-360.
PDB; 4LOO; X-ray; 1.95 A; A=1-360.
PDB; 4LOP; X-ray; 2.05 A; A/B/C/D=1-360.
PDB; 4LOQ; X-ray; 2.32 A; A/B/C/D=1-360.
PDB; 4TYH; X-ray; 3.00 A; B=6-353.
PDB; 5LAR; X-ray; 1.50 A; A=1-360.
PDB; 5UOJ; X-ray; 2.10 A; A=1-360.
PDBsum; 1LEW; -.
PDBsum; 1LEZ; -.
PDBsum; 1YW2; -.
PDBsum; 1YWR; -.
PDBsum; 2EWA; -.
PDBsum; 2GHL; -.
PDBsum; 2GHM; -.
PDBsum; 2GTM; -.
PDBsum; 2GTN; -.
PDBsum; 2OZA; -.
PDBsum; 2PUU; -.
PDBsum; 3P4K; -.
PDBsum; 3P5K; -.
PDBsum; 3P78; -.
PDBsum; 3P79; -.
PDBsum; 3P7A; -.
PDBsum; 3P7B; -.
PDBsum; 3P7C; -.
PDBsum; 3PY3; -.
PDBsum; 3TG1; -.
PDBsum; 4KA3; -.
PDBsum; 4LOO; -.
PDBsum; 4LOP; -.
PDBsum; 4LOQ; -.
PDBsum; 4TYH; -.
PDBsum; 5LAR; -.
PDBsum; 5UOJ; -.
ProteinModelPortal; P47811; -.
SMR; P47811; -.
BioGrid; 204969; 25.
DIP; DIP-31073N; -.
ELM; P47811; -.
IntAct; P47811; 27.
MINT; MINT-1204448; -.
STRING; 10090.ENSMUSP00000004990; -.
BindingDB; P47811; -.
ChEMBL; CHEMBL2336; -.
iPTMnet; P47811; -.
PhosphoSitePlus; P47811; -.
EPD; P47811; -.
MaxQB; P47811; -.
PaxDb; P47811; -.
PeptideAtlas; P47811; -.
PRIDE; P47811; -.
Ensembl; ENSMUST00000004990; ENSMUSP00000004990; ENSMUSG00000053436. [P47811-3]
Ensembl; ENSMUST00000062694; ENSMUSP00000061958; ENSMUSG00000053436. [P47811-1]
Ensembl; ENSMUST00000114752; ENSMUSP00000110400; ENSMUSG00000053436. [P47811-4]
Ensembl; ENSMUST00000114754; ENSMUSP00000110402; ENSMUSG00000053436. [P47811-4]
GeneID; 26416; -.
KEGG; mmu:26416; -.
UCSC; uc008brl.2; mouse. [P47811-1]
CTD; 1432; -.
MGI; MGI:1346865; Mapk14.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00550000074271; -.
HOVERGEN; HBG014652; -.
InParanoid; P47811; -.
KO; K04441; -.
OMA; EQFQQVY; -.
OrthoDB; EOG091G08QL; -.
PhylomeDB; P47811; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 3474.
Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
Reactome; R-MMU-171007; p38MAPK events.
Reactome; R-MMU-198753; ERK/MAPK targets.
Reactome; R-MMU-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-375170; CDO in myogenesis.
Reactome; R-MMU-376172; DSCAM interactions.
Reactome; R-MMU-418592; ADP signalling through P2Y purinoceptor 1.
Reactome; R-MMU-432142; Platelet sensitization by LDL.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-MMU-450341; Activation of the AP-1 family of transcription factors.
Reactome; R-MMU-450604; KSRP (KHSRP) binds and destabilizes mRNA.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
SABIO-RK; P47811; -.
ChiTaRS; Mapk14; mouse.
EvolutionaryTrace; P47811; -.
PRO; PR:P47811; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000053436; -.
CleanEx; MM_MAPK14; -.
ExpressionAtlas; P47811; baseline and differential.
Genevisible; P47811; MM.
GO; GO:0005623; C:cell; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0016301; F:kinase activity; IDA:MGI.
GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; ISO:MGI.
GO; GO:0051525; F:NFAT protein binding; IPI:BHF-UCL.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0001502; P:cartilage condensation; IMP:AgBase.
GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
GO; GO:0071479; P:cellular response to ionizing radiation; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
GO; GO:0071223; P:cellular response to lipoteichoic acid; ISO:MGI.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:MGI.
GO; GO:0098586; P:cellular response to virus; ISO:MGI.
GO; GO:0002062; P:chondrocyte differentiation; IDA:MGI.
GO; GO:0000077; P:DNA damage checkpoint; IMP:MGI.
GO; GO:0019395; P:fatty acid oxidation; IMP:MGI.
GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:MGI.
GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
GO; GO:0014835; P:myoblast differentiation involved in skeletal muscle regeneration; IMP:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:AgBase.
GO; GO:0030316; P:osteoclast differentiation; IMP:BHF-UCL.
GO; GO:0038066; P:p38MAPK cascade; IDA:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0001890; P:placenta development; IMP:MGI.
GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:MGI.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IGI:MGI.
GO; GO:0031281; P:positive regulation of cyclase activity; ISO:MGI.
GO; GO:0002741; P:positive regulation of cytokine secretion involved in immune response; IMP:CAFA.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:0046326; P:positive regulation of glucose import; IMP:MGI.
GO; GO:2001184; P:positive regulation of interleukin-12 secretion; ISO:MGI.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:CAFA.
GO; GO:1905050; P:positive regulation of metallopeptidase activity; IMP:CAFA.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0045663; P:positive regulation of myoblast differentiation; IMP:UniProtKB.
GO; GO:1901741; P:positive regulation of myoblast fusion; IMP:UniProtKB.
GO; GO:0010831; P:positive regulation of myotube differentiation; IMP:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:MGI.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; ISO:MGI.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0030278; P:regulation of ossification; IDA:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
GO; GO:0032495; P:response to muramyl dipeptide; IDA:MGI.
GO; GO:0035994; P:response to muscle stretch; IMP:MGI.
GO; GO:0042770; P:signal transduction in response to DNA damage; ISO:MGI.
GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
GO; GO:0090400; P:stress-induced premature senescence; ISO:MGI.
GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; IGI:MGI.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008352; MAPK_p38.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR01773; P38MAPKINASE.
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.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Stress response;
Transcription; Transcription regulation; Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q16539}.
CHAIN 2 360 Mitogen-activated protein kinase 14.
/FTId=PRO_0000186292.
DOMAIN 24 308 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 30 38 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 106 111 Inhibitor-binding.
MOTIF 180 182 TXY.
ACT_SITE 168 168 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 32 32 Inhibitor. {ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333}.
BINDING 35 35 Inhibitor. {ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333}.
BINDING 53 53 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 53 53 Inhibitor. {ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333}.
BINDING 71 71 Inhibitor. {ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333}.
BINDING 109 109 Inhibitor; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333}.
BINDING 111 111 Inhibitor; via amide nitrogen.
{ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333}.
BINDING 168 168 Inhibitor. {ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333}.
BINDING 169 169 Inhibitor; via carbonyl oxygen.
{ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q16539}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:Q16539}.
MOD_RES 16 16 Phosphothreonine.
{ECO:0000250|UniProtKB:Q16539}.
MOD_RES 53 53 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q16539}.
MOD_RES 152 152 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q16539}.
MOD_RES 180 180 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:18669639}.
MOD_RES 180 180 Phosphothreonine; by MAP2K3, MAP2K4,
MAP2K6 and autocatalysis. {ECO:0000250}.
MOD_RES 182 182 Phosphotyrosine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:18669639}.
MOD_RES 182 182 Phosphotyrosine; by MAP2K3, MAP2K4,
MAP2K6 and autocatalysis. {ECO:0000250}.
MOD_RES 323 323 Phosphotyrosine; by ZAP70.
{ECO:0000250|UniProtKB:Q16539}.
VAR_SEQ 1 77 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_022359.
VAR_SEQ 230 254 DQLKLILRLVGTPGAELLKKISSES -> NQLQQIMRLTGT
PPAYLINRMPSHE (in isoform 3).
{ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.2, ECO:0000303|Ref.7}.
/FTId=VSP_007544.
VAR_SEQ 255 278 ARNYIQSLAQMPKMNFANVFIGAN -> DAK (in
isoform 2). {ECO:0000303|Ref.3}.
/FTId=VSP_004846.
VAR_SEQ 279 360 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_007545.
MUTAGEN 180 180 T->A: Phosphorylation blocked.
{ECO:0000269|PubMed:7839144}.
MUTAGEN 182 182 Y->F: Phosphorylation blocked.
{ECO:0000269|PubMed:7839144}.
CONFLICT 98 98 E -> G (in Ref. 7; AAF06348).
{ECO:0000305}.
CONFLICT 107 108 HL -> LS (in Ref. 7; AAF06348).
{ECO:0000305}.
CONFLICT 115 115 N -> R (in Ref. 7; AAF06348).
{ECO:0000305}.
CONFLICT 124 124 D -> G (in Ref. 7; AAF06348).
{ECO:0000305}.
CONFLICT 159 162 NEDC -> TQVI (in Ref. 7; AAF06348).
{ECO:0000305}.
CONFLICT 166 166 I -> L (in Ref. 7; AAF06348).
{ECO:0000305}.
CONFLICT 202 202 Q -> R (in Ref. 7; AAF06348).
{ECO:0000305}.
CONFLICT 211 212 CI -> GF (in Ref. 7; AAF06348).
{ECO:0000305}.
CONFLICT 224 224 P -> L (in Ref. 7; AAF06348).
{ECO:0000305}.
CONFLICT 271 271 A -> P (in Ref. 7; AAF06348).
{ECO:0000305}.
CONFLICT 299 299 A -> V (in Ref. 7; AAF06348).
{ECO:0000305}.
CONFLICT 315 315 D -> Y (in Ref. 7; AAF06348).
{ECO:0000305}.
STRAND 8 13 {ECO:0000244|PDB:5LAR}.
STRAND 16 21 {ECO:0000244|PDB:5LAR}.
STRAND 24 30 {ECO:0000244|PDB:5LAR}.
HELIX 31 33 {ECO:0000244|PDB:5LAR}.
STRAND 34 43 {ECO:0000244|PDB:5LAR}.
TURN 44 46 {ECO:0000244|PDB:5LAR}.
STRAND 49 54 {ECO:0000244|PDB:5LAR}.
HELIX 62 77 {ECO:0000244|PDB:5LAR}.
STRAND 87 90 {ECO:0000244|PDB:5LAR}.
HELIX 96 98 {ECO:0000244|PDB:5LAR}.
STRAND 103 107 {ECO:0000244|PDB:5LAR}.
STRAND 110 112 {ECO:0000244|PDB:5LAR}.
HELIX 113 117 {ECO:0000244|PDB:5LAR}.
HELIX 124 143 {ECO:0000244|PDB:5LAR}.
HELIX 153 155 {ECO:0000244|PDB:5LAR}.
STRAND 156 158 {ECO:0000244|PDB:5LAR}.
STRAND 164 166 {ECO:0000244|PDB:5LAR}.
STRAND 172 175 {ECO:0000244|PDB:2GTM}.
HELIX 176 180 {ECO:0000244|PDB:5LAR}.
STRAND 182 184 {ECO:0000244|PDB:2OZA}.
HELIX 185 188 {ECO:0000244|PDB:2GTN}.
HELIX 191 194 {ECO:0000244|PDB:5LAR}.
STRAND 197 199 {ECO:0000244|PDB:2GTN}.
HELIX 203 218 {ECO:0000244|PDB:5LAR}.
HELIX 228 239 {ECO:0000244|PDB:5LAR}.
HELIX 244 247 {ECO:0000244|PDB:5LAR}.
HELIX 253 261 {ECO:0000244|PDB:5LAR}.
HELIX 270 272 {ECO:0000244|PDB:5LAR}.
TURN 274 276 {ECO:0000244|PDB:2GTN}.
HELIX 279 288 {ECO:0000244|PDB:5LAR}.
HELIX 293 295 {ECO:0000244|PDB:5LAR}.
HELIX 299 303 {ECO:0000244|PDB:5LAR}.
HELIX 306 308 {ECO:0000244|PDB:5LAR}.
TURN 309 311 {ECO:0000244|PDB:5LAR}.
HELIX 314 316 {ECO:0000244|PDB:2GTN}.
HELIX 326 329 {ECO:0000244|PDB:5LAR}.
HELIX 334 346 {ECO:0000244|PDB:5LAR}.
SEQUENCE 360 AA; 41287 MW; DFB03EBCE97BB51A CRC64;
MSQERPTFYR QELNKTIWEV PERYQNLSPV GSGAYGSVCA AFDTKTGHRV AVKKLSRPFQ
SIIHAKRTYR ELRLLKHMKH ENVIGLLDVF TPARSLEEFN DVYLVTHLMG ADLNNIVKCQ
KLTDDHVQFL IYQILRGLKY IHSADIIHRD LKPSNLAVNE DCELKILDFG LARHTDDEMT
GYVATRWYRA PEIMLNWMHY NQTVDIWSVG CIMAELLTGR TLFPGTDHID QLKLILRLVG
TPGAELLKKI SSESARNYIQ SLAQMPKMNF ANVFIGANPL AVDLLEKMLV LDSDKRITAA
QALAHAYFAQ YHDPDDEPVA DPYDQSFESR DLLIDEWKSL TYDEVISFVP PPLDQEEMES


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EIAAB24873 CRK1,Crk1,Csbp1,Csbp2,MAP kinase 14,MAP kinase p38 alpha,MAPK 14,Mapk14,Mitogen-activated protein kinase 14,Mitogen-activated protein kinase p38 alpha,Mouse,Mus musculus
EIAAB24874 CRK1,Csbp1,Csbp2,MAP kinase 14,MAP kinase p38 alpha,MAPK 14,Mapk14,Mitogen-activated protein kinase 14,Mitogen-activated protein kinase p38 alpha,Rat,Rattus norvegicus
E1206m ELISA kit Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protei 96T
E1206r ELISA kit Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protei 96T
U1206r CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T
U1206m CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T
E1206b ELISA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM 96T
U1206b CLIA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM1 96T
E1206r ELISA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kin 96T
E1206m ELISA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kin 96T
E1206b ELISA kit Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2 96T
EIAAB24970 Leucine zipper- and sterile alpha motif kinase ZAK,Mitogen-activated protein kinase kinase kinase MLT,Mixed lineage kinase-related kinase,MLK-like mitogen-activated protein triple kinase,MLK-related k
E1206h ELISA kit ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,Homo sapiens,Human,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-ac 96T
U1206h CLIA ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,Homo sapiens,Human,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activate 96T
E1206h ELISA ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,Homo sapiens,Human,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activat 96T
EIAAB24870 Homo sapiens,Human,MAP kinase 13,MAP kinase p38 delta,MAPK 13,MAPK13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,PRKM13,SAPK4,Stress-activated protein kinase 4
EIAAB24864 Homo sapiens,Human,MAP kinase 11,MAP kinase p38 beta,MAPK 11,MAPK11,Mitogen-activated protein kinase 11,Mitogen-activated protein kinase p38 beta,p38-2,p38b,PRKM11,SAPK2,Stress-activated protein kinas
EIAAB24875 Canis familiaris,Canis lupus familiaris,CSBP1,CSBP2,Dog,MAP kinase 14,MAP kinase p38 alpha,MAPK 14,MAPK14,Mitogen-activated protein kinase 14,Mitogen-activated protein kinase p38 alpha
EIAAB24858 c-Jun N-terminal kinase 2,Jnk2,MAP kinase 9,MAPK 9,Mapk9,Mitogen-activated protein kinase 9,p54-alpha,Prkm9,Rat,Rattus norvegicus,SAPK-alpha,Stress-activated protein kinase JNK2
EIAAB24867 ERK6,ERK-6,Extracellular signal-regulated kinase 6,Homo sapiens,Human,MAP kinase 12,MAP kinase p38 gamma,MAPK 12,MAPK12,Mitogen-activated protein kinase 12,Mitogen-activated protein kinase p38 gamma,S
EIAAB24866 ERK-6,Extracellular signal-regulated kinase 6,MAP kinase 12,MAP kinase p38 gamma,MAPK 12,Mapk12,Mitogen-activated protein kinase 12,Mitogen-activated protein kinase p38 gamma,Mouse,Mus musculus,Sapk3,
18-662-20087 Mitogen-activated protein kinase 1 - EC 2.7.11.24; Extracellular signal-regulated kinase 2; ERK-2; Mitogen-activated protein kinase 2; MAP kinase 2; MAPK 2; p42-MAPK; ERT1 Polyclonal 0.1 ml
15-288-22768 Mitogen-activated protein kinase 1 - EC 2.7.11.24; Extracellular signal-regulated kinase 2; ERK-2; Mitogen-activated protein kinase 2; MAP kinase 2; MAPK 2; p42-MAPK; ERT1 Polyclonal 0.05 mg
15-288-22768 Mitogen-activated protein kinase 1 - EC 2.7.11.24; Extracellular signal-regulated kinase 2; ERK-2; Mitogen-activated protein kinase 2; MAP kinase 2; MAPK 2; p42-MAPK; ERT1 Polyclonal 0.1 mg
EIAAB24872 MAP kinase 13,MAP kinase p38 delta,MAPK 13,Mapk13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,Mouse,Mus musculus,Serk4,Stress-activated protein kinase 4


 

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