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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.
17-JUN-2020, entry version 221.
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 ACTIVITY 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,
ACTIVITY 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, ACTIVITY 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 ACTIVITY 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:
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;
Evidence={ECO:0000269|PubMed:18669639, ECO:0000269|PubMed:22375048};
-!- 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; Evidence={ECO:0000269|PubMed:18669639,
ECO:0000269|PubMed:22375048};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ACTIVITY 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:
P47811; Q61233: Lcp1; NbExp=5; IntAct=EBI-298727, EBI-309345;
P47811; Q9WUI1: Mapk11; NbExp=10; IntAct=EBI-298727, EBI-645081;
P47811; P49138: Mapkapk2; NbExp=2; IntAct=EBI-298727, EBI-298776;
P47811; P55012: Slc12a2; NbExp=2; IntAct=EBI-298727, EBI-621078;
P47811; Q9Z1W9: Stk39; NbExp=2; IntAct=EBI-298727, EBI-444764;
P47811; Q99956: DUSP9; Xeno; NbExp=2; IntAct=EBI-298727, EBI-3906678;
P47811; P49137-1: MAPKAPK2; Xeno; NbExp=2; IntAct=EBI-298727, EBI-15629963;
P47811; P35236: PTPN7; Xeno; NbExp=2; IntAct=EBI-298727, EBI-2265723;
-!- 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;
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; -; NOT_ANNOTATED_CDS; 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]
PDB; 1LEW; X-ray; 2.30 A; A=1-360.
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; 5NZZ; X-ray; 2.60 A; E/F/G/H=1-360.
PDB; 5O90; X-ray; 2.49 A; A=1-360.
PDB; 5UOJ; X-ray; 2.10 A; A=1-360.
PDB; 6SO1; X-ray; 1.66 A; A=1-360.
PDB; 6SO2; X-ray; 1.60 A; A=1-360.
PDB; 6SO4; X-ray; 1.51 A; A=1-360.
PDB; 6SOD; X-ray; 1.87 A; A=1-360.
PDB; 6SOI; X-ray; 1.55 A; A=1-359.
PDB; 6SOT; X-ray; 1.54 A; A=1-360.
PDB; 6SOU; X-ray; 1.50 A; A=1-360.
PDB; 6SOV; X-ray; 1.31 A; A=1-360.
PDB; 6SP9; X-ray; 1.22 A; A=1-360.
PDB; 6SPL; X-ray; 1.38 A; A=1-360.
PDB; 6Y4T; X-ray; 1.98 A; A=1-360.
PDB; 6Y4U; X-ray; 1.86 A; A=1-360.
PDB; 6Y4V; X-ray; 1.75 A; A=1-360.
PDB; 6Y4W; X-ray; 1.86 A; A=1-360.
PDB; 6Y4X; X-ray; 1.60 A; A=1-360.
PDB; 6Y6V; X-ray; 2.10 A; A=1-360.
PDB; 6Y6W; X-ray; 1.90 A; A=1-360.
PDB; 6Y70; X-ray; 1.90 A; A=1-360.
PDB; 6Y7W; X-ray; 1.39 A; A=1-360.
PDB; 6Y7X; X-ray; 1.45 A; A=1-360.
PDB; 6Y7Y; X-ray; 1.51 A; A=1-360.
PDB; 6Y7Z; X-ray; 1.35 A; A=1-360.
PDB; 6Y80; X-ray; 1.24 A; A=1-360.
PDB; 6Y81; X-ray; 1.54 A; A=1-360.
PDB; 6Y82; X-ray; 1.44 A; A=1-360.
PDB; 6Y85; X-ray; 1.58 A; A=1-360.
PDB; 6Y8H; X-ray; 1.37 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; 5NZZ; -.
PDBsum; 5O90; -.
PDBsum; 5UOJ; -.
PDBsum; 6SO1; -.
PDBsum; 6SO2; -.
PDBsum; 6SO4; -.
PDBsum; 6SOD; -.
PDBsum; 6SOI; -.
PDBsum; 6SOT; -.
PDBsum; 6SOU; -.
PDBsum; 6SOV; -.
PDBsum; 6SP9; -.
PDBsum; 6SPL; -.
PDBsum; 6Y4T; -.
PDBsum; 6Y4U; -.
PDBsum; 6Y4V; -.
PDBsum; 6Y4W; -.
PDBsum; 6Y4X; -.
PDBsum; 6Y6V; -.
PDBsum; 6Y6W; -.
PDBsum; 6Y70; -.
PDBsum; 6Y7W; -.
PDBsum; 6Y7X; -.
PDBsum; 6Y7Y; -.
PDBsum; 6Y7Z; -.
PDBsum; 6Y80; -.
PDBsum; 6Y81; -.
PDBsum; 6Y82; -.
PDBsum; 6Y85; -.
PDBsum; 6Y8H; -.
SMR; P47811; -.
BioGRID; 204969; 26.
DIP; DIP-31073N; -.
ELM; P47811; -.
IntAct; P47811; 27.
MINT; P47811; -.
STRING; 10090.ENSMUSP00000004990; -.
BindingDB; P47811; -.
ChEMBL; CHEMBL2336; -.
iPTMnet; P47811; -.
PhosphoSitePlus; P47811; -.
CPTAC; non-CPTAC-3479; -.
EPD; P47811; -.
jPOST; P47811; -.
MaxQB; P47811; -.
PaxDb; P47811; -.
PeptideAtlas; P47811; -.
PRIDE; P47811; -.
Antibodypedia; 4142; 2114 antibodies.
Ensembl; ENSMUST00000004990; ENSMUSP00000004990; ENSMUSG00000053436. [P47811-3]
Ensembl; ENSMUST00000062694; ENSMUSP00000061958; ENSMUSG00000053436. [P47811-1]
Ensembl; ENSMUST00000114752; ENSMUSP00000110400; ENSMUSG00000053436. [P47811-4]
Ensembl; ENSMUST00000114754; ENSMUSP00000110402; ENSMUSG00000053436. [P47811-4]
Ensembl; ENSMUST00000114758; ENSMUSP00000110406; ENSMUSG00000053436. [P47811-2]
GeneID; 26416; -.
KEGG; mmu:26416; -.
UCSC; uc008brl.2; mouse. [P47811-1]
CTD; 1432; -.
MGI; MGI:1346865; Mapk14.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00940000155325; -.
InParanoid; P47811; -.
KO; K04441; -.
OMA; EITNRYT; -.
OrthoDB; 683132at2759; -.
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-2559580; Oxidative Stress Induced Senescence.
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-525793; Myogenesis.
Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
SABIO-RK; P47811; -.
BioGRID-ORCS; 26416; 1 hit in 14 CRISPR screens.
ChiTaRS; Mapk14; mouse.
EvolutionaryTrace; P47811; -.
PRO; PR:P47811; -.
Proteomes; UP000000589; Chromosome 17.
RNAct; P47811; protein.
Bgee; ENSMUSG00000053436; Expressed in blood and 296 other tissues.
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:0098978; C:glutamatergic synapse; IDA:SynGO.
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; ISO:MGI.
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:0008022; F:protein C-terminus binding; ISO:MGI.
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:0071356; P:cellular response to tumor necrosis factor; IDA: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: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: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 by RNA polymerase II; IMP:MGI.
GO; GO:0046777; P:protein autophosphorylation; ISO: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:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0030278; P:regulation of ossification; IDA:MGI.
GO; GO:0099179; P:regulation of synaptic membrane adhesion; IDA:SynGO.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; 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:0051403; P:stress-activated MAPK cascade; ISO:MGI.
GO; GO:0090400; P:stress-induced premature senescence; ISO:MGI.
GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
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.
CDD; cd07877; STKc_p38alpha; 1.
IDEAL; IID50045; -.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR008352; MAPK_p38-like.
InterPro; IPR038784; p38alpha.
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;
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
/note="Removed"
/evidence="ECO:0000250|UniProtKB:Q16539"
CHAIN 2..360
/note="Mitogen-activated protein kinase 14"
/id="PRO_0000186292"
DOMAIN 24..308
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 30..38
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
REGION 106..111
/note="Inhibitor-binding"
MOTIF 180..182
/note="TXY"
ACT_SITE 168
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 32
/note="Inhibitor"
/evidence="ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333"
BINDING 35
/note="Inhibitor"
/evidence="ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333"
BINDING 53
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 53
/note="Inhibitor"
/evidence="ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333"
BINDING 71
/note="Inhibitor"
/evidence="ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333"
BINDING 109
/note="Inhibitor; via amide nitrogen and carbonyl oxygen"
/evidence="ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333"
BINDING 111
/note="Inhibitor; via amide nitrogen"
/evidence="ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333"
BINDING 168
/note="Inhibitor"
/evidence="ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333"
BINDING 169
/note="Inhibitor; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:15837310,
ECO:0000269|PubMed:15837333"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0000250|UniProtKB:Q16539"
MOD_RES 2
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q16539"
MOD_RES 16
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q16539"
MOD_RES 53
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q16539"
MOD_RES 152
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q16539"
MOD_RES 180
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:17947660, ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:21183079, ECO:0000269|PubMed:18669639"
MOD_RES 180
/note="Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and
autocatalysis"
/evidence="ECO:0000250"
MOD_RES 182
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:17947660, ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:21183079, ECO:0000269|PubMed:18669639"
MOD_RES 182
/note="Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and
autocatalysis"
/evidence="ECO:0000250"
MOD_RES 323
/note="Phosphotyrosine; by ZAP70"
/evidence="ECO:0000250|UniProtKB:Q16539"
VAR_SEQ 1..77
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:16141072"
/id="VSP_022359"
VAR_SEQ 230..254
/note="DQLKLILRLVGTPGAELLKKISSES -> NQLQQIMRLTGTPPAYLINRMPS
HE (in isoform 3)"
/evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2,
ECO:0000303|Ref.7"
/id="VSP_007544"
VAR_SEQ 255..278
/note="ARNYIQSLAQMPKMNFANVFIGAN -> DAKP (in isoform 2)"
/evidence="ECO:0000303|Ref.3"
/id="VSP_004846"
VAR_SEQ 279..360
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|Ref.3"
/id="VSP_007545"
MUTAGEN 180
/note="T->A: Phosphorylation blocked."
/evidence="ECO:0000269|PubMed:7839144"
MUTAGEN 182
/note="Y->F: Phosphorylation blocked."
/evidence="ECO:0000269|PubMed:7839144"
CONFLICT 98
/note="E -> G (in Ref. 7; AAF06348)"
/evidence="ECO:0000305"
CONFLICT 107..108
/note="HL -> LS (in Ref. 7; AAF06348)"
/evidence="ECO:0000305"
CONFLICT 115
/note="N -> R (in Ref. 7; AAF06348)"
/evidence="ECO:0000305"
CONFLICT 124
/note="D -> G (in Ref. 7; AAF06348)"
/evidence="ECO:0000305"
CONFLICT 159..162
/note="NEDC -> TQVI (in Ref. 7; AAF06348)"
/evidence="ECO:0000305"
CONFLICT 166
/note="I -> L (in Ref. 7; AAF06348)"
/evidence="ECO:0000305"
CONFLICT 202
/note="Q -> R (in Ref. 7; AAF06348)"
/evidence="ECO:0000305"
CONFLICT 211..212
/note="CI -> GF (in Ref. 7; AAF06348)"
/evidence="ECO:0000305"
CONFLICT 224
/note="P -> L (in Ref. 7; AAF06348)"
/evidence="ECO:0000305"
CONFLICT 271
/note="A -> P (in Ref. 7; AAF06348)"
/evidence="ECO:0000305"
CONFLICT 299
/note="A -> V (in Ref. 7; AAF06348)"
/evidence="ECO:0000305"
CONFLICT 315
/note="D -> Y (in Ref. 7; AAF06348)"
/evidence="ECO:0000305"
STRAND 8..13
/evidence="ECO:0000244|PDB:6SP9"
STRAND 16..21
/evidence="ECO:0000244|PDB:6SP9"
STRAND 24..33
/evidence="ECO:0000244|PDB:6SP9"
STRAND 36..43
/evidence="ECO:0000244|PDB:6SP9"
TURN 44..47
/evidence="ECO:0000244|PDB:6SP9"
STRAND 48..57
/evidence="ECO:0000244|PDB:6SP9"
HELIX 62..77
/evidence="ECO:0000244|PDB:6SP9"
STRAND 87..90
/evidence="ECO:0000244|PDB:6SP9"
HELIX 96..98
/evidence="ECO:0000244|PDB:6SP9"
STRAND 103..107
/evidence="ECO:0000244|PDB:6SP9"
STRAND 110..112
/evidence="ECO:0000244|PDB:5LAR"
HELIX 113..117
/evidence="ECO:0000244|PDB:6SP9"
HELIX 124..143
/evidence="ECO:0000244|PDB:6SP9"
HELIX 153..155
/evidence="ECO:0000244|PDB:6SP9"
STRAND 156..158
/evidence="ECO:0000244|PDB:6SP9"
STRAND 164..166
/evidence="ECO:0000244|PDB:6SP9"
STRAND 172..175
/evidence="ECO:0000244|PDB:2GTM"
HELIX 176..180
/evidence="ECO:0000244|PDB:5LAR"
HELIX 184..187
/evidence="ECO:0000244|PDB:6SOU"
HELIX 191..194
/evidence="ECO:0000244|PDB:6SP9"
STRAND 197..199
/evidence="ECO:0000244|PDB:2GTN"
HELIX 204..218
/evidence="ECO:0000244|PDB:6SP9"
HELIX 228..239
/evidence="ECO:0000244|PDB:6SP9"
HELIX 244..247
/evidence="ECO:0000244|PDB:6SP9"
HELIX 253..261
/evidence="ECO:0000244|PDB:6SP9"
HELIX 270..272
/evidence="ECO:0000244|PDB:6SP9"
TURN 274..276
/evidence="ECO:0000244|PDB:2GTN"
HELIX 279..288
/evidence="ECO:0000244|PDB:6SP9"
TURN 293..295
/evidence="ECO:0000244|PDB:6SOV"
HELIX 299..303
/evidence="ECO:0000244|PDB:6SP9"
HELIX 306..308
/evidence="ECO:0000244|PDB:6SP9"
TURN 309..311
/evidence="ECO:0000244|PDB:6SP9"
HELIX 314..316
/evidence="ECO:0000244|PDB:6SP9"
HELIX 326..329
/evidence="ECO:0000244|PDB:6SP9"
HELIX 334..347
/evidence="ECO:0000244|PDB:6SP9"
CONFLICT P47811-3:238
/note="L -> M (in Ref. 2; BAA19741)"
/evidence="ECO:0000305"
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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Related Genes :
[Mapk14 Crk1 Csbp1 Csbp2] 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)
[Mapk14 Csbp1 Csbp2] 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)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[MAPK14 CSBP1 CSBP2] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha)
[mapk14a mapk14] Mitogen-activated protein kinase 14A (MAP kinase 14A) (MAPK 14A) (EC 2.7.11.24) (Mitogen-activated protein kinase p38a) (MAP kinase p38a) (zp38a)
[mapk14b mapk14] Mitogen-activated protein kinase 14B (MAP kinase 14B) (MAPK 14B) (EC 2.7.11.24) (Mitogen-activated protein kinase p38b) (MAP kinase p38b) (zp38b)
[MAPK11 PRKM11 SAPK2 SAPK2B] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38b) (Stress-activated protein kinase 2b) (SAPK2b) (p38-2)
[mapk14b] Mitogen-activated protein kinase 14B (MAP kinase 14B) (MAPK 14B) (EC 2.7.11.24) (Mitogen-activated protein kinase p38b) (MAP kinase p38b) (cp38b)
[mapk14a] Mitogen-activated protein kinase 14A (MAP kinase 14A) (MAPK 14A) (EC 2.7.11.24) (Mitogen-activated protein kinase p38a) (MAP kinase p38a) (cp38a)
[MAPK12 ERK6 SAPK3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[MAPK13 PRKM13 SAPK4] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Mapk13] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[Mapk13 Serk4] Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4)
[Mapk11 Prkm11] Mitogen-activated protein kinase 11 (MAP kinase 11) (MAPK 11) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 beta) (MAP kinase p38 beta) (p38B)
[MAPK14 CSBP1] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a)
[Mapk12 Sapk3] Mitogen-activated protein kinase 12 (MAP kinase 12) (MAPK 12) (EC 2.7.11.24) (Extracellular signal-regulated kinase 6) (ERK-6) (Mitogen-activated protein kinase p38 gamma) (MAP kinase p38 gamma) (Stress-activated protein kinase 3)
[p38b CG7393] Mitogen-activated protein kinase p38b (MAP kinase p38b) (MAPK p38b) (EC 2.7.11.24)
[pmk-1 B0218.3] Mitogen-activated protein kinase pmk-1 (EC 2.7.11.24) (Stress-activated protein kinase pmk-1) (p38 MAP kinase 1)
[pmk-3 F42G8.4] Mitogen-activated protein kinase pmk-3 (EC 2.7.11.24) (Stress-activated protein kinase pmk-3) (p38 MAP kinase 3)
[MAPKAPK5 PRAK] MAP kinase-activated protein kinase 5 (MAPK-activated protein kinase 5) (MAPKAP kinase 5) (MAPKAP-K5) (MAPKAPK-5) (MK-5) (MK5) (EC 2.7.11.1) (p38-regulated/activated protein kinase) (PRAK)
[MAPK1 ERK2 PRKM1 PRKM2] 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)
[MAPK3 ERK1 PRKM3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[MAP3K20 MLTK ZAK HCCS4] Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Human cervical cancer suppressor gene 4 protein) (HCCS-4) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK)
[Mapk8 Jnk1 Prkm8] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1)
[MAP3K5 ASK1 MAPKKK5 MEKK5] Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)
[Mapk8 Jnk1 Prkm8] Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (SAPK gamma) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1) (p54 gamma)
[MAP2K6 MEK6 MKK6 PRKMK6 SKK3] Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (MAPK/ERK kinase 6) (MEK 6) (Stress-activated protein kinase kinase 3) (SAPK kinase 3) (SAPKK-3) (SAPKK3)
[MAP4K2 GCK RAB8IP] Mitogen-activated protein kinase kinase kinase kinase 2 (EC 2.7.11.1) (B lymphocyte serine/threonine-protein kinase) (Germinal center kinase) (GC kinase) (MAPK/ERK kinase kinase kinase 2) (MEK kinase kinase 2) (MEKKK 2) (Rab8-interacting protein)
[Map3k5 Ask1 Mekk5] Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5)

Bibliography :