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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)

 MK11_HUMAN              Reviewed;         364 AA.
Q15759; A8K730; B0LPG1; B7Z630; E7ETQ1; L7RT27; O00284; O15472;
Q2XNF2;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 2.
28-MAR-2018, entry version 188.
RecName: Full=Mitogen-activated protein kinase 11;
Short=MAP kinase 11;
Short=MAPK 11;
EC=2.7.11.24;
AltName: Full=Mitogen-activated protein kinase p38 beta;
Short=MAP kinase p38 beta;
Short=p38b;
AltName: Full=Stress-activated protein kinase 2b;
Short=SAPK2b;
AltName: Full=p38-2;
Name=MAPK11; Synonyms=PRKM11, SAPK2, SAPK2B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=8663524; DOI=10.1074/jbc.271.30.17920;
Jiang Y., Chen C., Li Z., Guo W., Gegner J.A., Lin S., Han J.;
"Characterization of the structure and function of a new mitogen-
activated protein kinase (p38beta).";
J. Biol. Chem. 271:17920-17926(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Jiang Y., Han J.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9207191; DOI=10.1006/bbrc.1997.6849;
Kumar S., McDonnell P.C., Gum R.J., Hand A.T., Lee J.C., Young P.R.;
"Novel homologues of CSBP/p38 MAP kinase: activation, substrate
specificity and sensitivity to inhibition by pyridinyl imidazoles.";
Biochem. Biophys. Res. Commun. 235:533-538(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN PHOSPHORYLATION OF
ATF2; ELK1 AND MBP, AND ENZYME REGULATION.
TISSUE=Brain;
PubMed=9430721; DOI=10.1074/jbc.273.3.1741;
Enslen H., Raingeaud J., Davis R.J.;
"Selective activation of p38 mitogen-activated protein (MAP) kinase
isoforms by the MAP kinase kinases MKK3 and MKK6.";
J. Biol. Chem. 273:1741-1748(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ENZYME REGULATION.
PubMed=9218798; DOI=10.1093/emboj/16.12.3563;
Goedert M., Cuenda A., Craxton M., Jakes R., Cohen P.;
"Activation of the novel stress-activated protein kinase SAPK4 by
cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison
of its substrate specificity with that of other SAP kinases.";
EMBO J. 16:3563-3571(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9235954; DOI=10.1074/jbc.272.31.19509;
Stein B., Yang M.X., Young D.B., Janknecht R., Hunter T., Murray B.W.,
Barbosa M.S.;
"p38-2, a novel mitogen-activated protein kinase with distinct
properties.";
J. Biol. Chem. 272:19509-19517(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-275.
NIEHS SNPs program;
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[14]
FUNCTION IN ACTIVATION OF RPS6KA5/MSK1.
PubMed=9687510; DOI=10.1093/emboj/17.15.4426;
Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.;
"Mitogen- and stress-activated protein kinase-1 (MSK1) is directly
activated by MAPK and SAPK2/p38, and may mediate activation of CREB.";
EMBO J. 17:4426-4441(1998).
[15]
FUNCTION IN PHOSPHORYLATION OF MEF2A AND MEF2C.
PubMed=10330143; DOI=10.1128/MCB.19.6.4028;
Yang S.-H., Galanis A., Sharrocks A.D.;
"Targeting of p38 mitogen-activated protein kinases to MEF2
transcription factors.";
Mol. Cell. Biol. 19:4028-4038(1999).
[16]
INTERACTION WITH DUSP16, AND ENZYME REGULATION.
PubMed=11359773; DOI=10.1074/jbc.M101981200;
Tanoue T., Yamamoto T., Maeda R., Nishida E.;
"A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and
p38 alpha and beta MAPKs.";
J. Biol. Chem. 276:26629-26639(2001).
[17]
FUNCTION AS MKNK2 KINASE.
PubMed=11154262; DOI=10.1128/MCB.21.3.743-754.2001;
Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.;
"The mitogen-activated protein kinase signal-integrating kinase Mnk2
is a eukaryotic initiation factor 4E kinase with high levels of basal
activity in mammalian cells.";
Mol. Cell. Biol. 21:743-754(2001).
[18]
INTERACTION WITH HDAC3, PHOSPHORYLATION AT THR-180 AND TYR-182, ENZYME
REGULATION, AND FUNCTION IN ATF2 ACTIVATION.
PubMed=15356147; DOI=10.4049/jimmunol.173.6.3979;
Mahlknecht U., Will J., Varin A., Hoelzer D., Herbein G.;
"Histone deacetylase 3, a class I histone deacetylase, suppresses
MAPK11-mediated activating transcription factor-2 activation and
represses TNF gene expression.";
J. Immunol. 173:3979-3990(2004).
[19]
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).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[21]
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).
[22]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
PubMed=19622861; DOI=10.1107/S090744490901600X;
Patel S.B., Cameron P.M., O'Keefe S.J., Frantz-Wattley B.,
Thompson J., O'Neill E.A., Tennis T., Liu L., Becker J.W., Scapin G.;
"The three-dimensional structure of MAP kinase p38beta: different
features of the ATP-binding site in p38beta compared with p38alpha.";
Acta Crystallogr. D 65:777-785(2009).
[23]
VARIANTS [LARGE SCALE ANALYSIS] VAL-221 AND HIS-275.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Serine/threonine kinase which acts as an essential
component of the MAP kinase signal transduction pathway. MAPK11 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.
MAPK11 functions are mostly redundant with those of MAPK14. 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. 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. 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. Additional examples of p38 MAPK substrates
are the 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.
{ECO:0000269|PubMed:10330143, ECO:0000269|PubMed:11154262,
ECO:0000269|PubMed:15356147, ECO:0000269|PubMed:9430721,
ECO:0000269|PubMed:9687510}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by phosphorylation on threonine and
tyrosine by MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6. MAP2K3/MKK3
and MAP2K6/MKK6 are both essential for the activation of MAPK11
induced by environmental stress. HDAC3 interacts directly and
selectively with MAPK11 to repress ATF2 transcriptional activity,
and regulate TNF gene expression in LPS-stimulated cells.
Inhibited by SB203580 and pyridinyl-imidazole related compounds.
{ECO:0000269|PubMed:11359773, ECO:0000269|PubMed:15356147,
ECO:0000269|PubMed:9218798, ECO:0000269|PubMed:9430721}.
-!- SUBUNIT: Interacts with HDAC3 and DUSP16.
{ECO:0000269|PubMed:11359773, ECO:0000269|PubMed:15356147,
ECO:0000269|PubMed:19622861}.
-!- INTERACTION:
P04637:TP53; NbExp=2; IntAct=EBI-298304, EBI-366083;
O43257:ZNHIT1; NbExp=2; IntAct=EBI-298304, EBI-347522;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15759-1; Sequence=Displayed;
Name=2;
IsoId=Q15759-3; Sequence=VSP_055221, VSP_055222, VSP_055223;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highest levels in the brain and heart. Also
expressed in the placenta, lung, liver, skeletal muscle, kidney
and pancreas.
-!- 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 MAP2K3/MKK3,
MAP2K4/MKK4 and MAP2K6/MKK6, which activates the enzyme.
{ECO:0000269|PubMed:15356147}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mapk11/";
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EMBL; U53442; AAB05036.1; -; mRNA.
EMBL; AF001008; AAC51250.1; -; mRNA.
EMBL; AF001174; AAC51373.1; -; mRNA.
EMBL; AF031135; AAC12714.1; -; mRNA.
EMBL; Y14440; CAA74792.1; -; mRNA.
EMBL; U92268; AAB66313.1; -; mRNA.
EMBL; CR456514; CAG30400.1; -; mRNA.
EMBL; DQ279722; ABB72677.1; -; Genomic_DNA.
EMBL; AK291845; BAF84534.1; -; mRNA.
EMBL; AK299745; BAH13116.1; -; mRNA.
EMBL; EU332851; ABY87540.1; -; Genomic_DNA.
EMBL; JX512451; AGC09598.1; -; Genomic_DNA.
EMBL; AL022328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471138; EAW73524.1; -; Genomic_DNA.
EMBL; CH471138; EAW73525.1; -; Genomic_DNA.
EMBL; CH471138; EAW73526.1; -; Genomic_DNA.
EMBL; BC027933; AAH27933.1; -; mRNA.
CCDS; CCDS14090.1; -. [Q15759-1]
PIR; G02524; G02524.
PIR; JC5529; JC5529.
RefSeq; NP_002742.3; NM_002751.6. [Q15759-1]
UniGene; Hs.57732; -.
PDB; 3GC8; X-ray; 2.40 A; A/B=1-364.
PDB; 3GC9; X-ray; 2.05 A; A/B=1-364.
PDB; 3GP0; X-ray; 1.90 A; A=5-350.
PDBsum; 3GC8; -.
PDBsum; 3GC9; -.
PDBsum; 3GP0; -.
ProteinModelPortal; Q15759; -.
SMR; Q15759; -.
BioGrid; 111586; 34.
IntAct; Q15759; 21.
MINT; Q15759; -.
STRING; 9606.ENSP00000333685; -.
BindingDB; Q15759; -.
ChEMBL; CHEMBL3961; -.
DrugBank; DB05157; KC706.
DrugBank; DB08896; Regorafenib.
GuidetoPHARMACOLOGY; 1500; -.
iPTMnet; Q15759; -.
PhosphoSitePlus; Q15759; -.
BioMuta; MAPK11; -.
DMDM; 134047835; -.
EPD; Q15759; -.
PaxDb; Q15759; -.
PeptideAtlas; Q15759; -.
PRIDE; Q15759; -.
DNASU; 5600; -.
Ensembl; ENST00000330651; ENSP00000333685; ENSG00000185386. [Q15759-1]
Ensembl; ENST00000395764; ENSP00000379113; ENSG00000185386. [Q15759-1]
GeneID; 5600; -.
KEGG; hsa:5600; -.
UCSC; uc003bkr.4; human. [Q15759-1]
CTD; 5600; -.
DisGeNET; 5600; -.
EuPathDB; HostDB:ENSG00000185386.14; -.
GeneCards; MAPK11; -.
HGNC; HGNC:6873; MAPK11.
HPA; CAB012961; -.
HPA; HPA045069; -.
MIM; 602898; gene.
neXtProt; NX_Q15759; -.
OpenTargets; ENSG00000185386; -.
PharmGKB; PA30618; -.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00550000074271; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; Q15759; -.
KO; K04441; -.
OMA; ASDEPDC; -.
OrthoDB; EOG091G08QL; -.
PhylomeDB; Q15759; -.
TreeFam; TF105100; -.
BRENDA; 2.7.11.24; 2681.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-171007; p38MAPK events.
Reactome; R-HSA-198753; ERK/MAPK targets.
Reactome; R-HSA-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-375170; CDO in myogenesis.
Reactome; R-HSA-376172; DSCAM interactions.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-450341; Activation of the AP-1 family of transcription factors.
Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
SignaLink; Q15759; -.
SIGNOR; Q15759; -.
EvolutionaryTrace; Q15759; -.
GeneWiki; MAPK11; -.
GenomeRNAi; 5600; -.
PRO; PR:Q15759; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000185386; -.
CleanEx; HS_MAPK11; -.
ExpressionAtlas; Q15759; baseline and differential.
Genevisible; Q15759; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:2001184; P:positive regulation of interleukin-12 secretion; IMP:UniProtKB.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
GO; GO:0051090; P:regulation of DNA binding transcription factor activity; TAS:Reactome.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0051403; P:stress-activated MAPK cascade; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
InterPro; IPR011009; Kinase-like_dom_sf.
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; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Stress response; Transcription; Transcription regulation; Transferase.
CHAIN 1 364 Mitogen-activated protein kinase 11.
/FTId=PRO_0000186280.
DOMAIN 24 308 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 30 38 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 106 110 Inhibitor-binding.
REGION 168 169 Inhibitor-binding.
MOTIF 180 182 TXY.
ACT_SITE 150 150 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 53 53 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 71 71 Nilotinib.
MOD_RES 180 180 Phosphothreonine; by MAP2K3, MAP2K4 and
MAP2K6. {ECO:0000305|PubMed:15356147}.
MOD_RES 182 182 Phosphotyrosine; by MAP2K3, MAP2K4 and
MAP2K6. {ECO:0000305|PubMed:15356147}.
MOD_RES 323 323 Phosphotyrosine; by ZAP70. {ECO:0000250}.
VAR_SEQ 1 108 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055221.
VAR_SEQ 204 321 VDIWSVGCIMAELLQGKALFPGSDYIDQLKRIMEVVGTPSP
EVLAKISSEHARTYIQSLPPMPQKDLSSIFRGANPLAIDLL
GRMLVLDSDQRVSAAEALAHAYFSQYHDPEDEPEAE -> G
AGGRPWGDEGQGPRLALDWLCMPGLRGQARSPRMWDPHSKV
ALQRPLEHDGCWPPLAVQLWTSPCLGGLGMAEEGVCPSWGL
DVTVGLLEEGRGVGTLMEVPSPSHSGYLVRGLHHG (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055222.
VAR_SEQ 322 364 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055223.
VARIANT 221 221 A -> V (in a lung neuroendocrine
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042264.
VARIANT 275 275 R -> H (in dbSNP:rs33932986).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.9}.
/FTId=VAR_025176.
MUTAGEN 180 180 T->A: Inactivation.
MUTAGEN 182 182 Y->F: Inactivation.
CONFLICT 98 98 D -> V (in Ref. 8; BAF84534).
{ECO:0000305}.
CONFLICT 122 123 LS -> GAHQGARLAL (in Ref. 1; AAB05036).
{ECO:0000305}.
CONFLICT 326 326 S -> G (in Ref. 6; AAB66313).
{ECO:0000305}.
STRAND 8 15 {ECO:0000244|PDB:3GP0}.
STRAND 17 21 {ECO:0000244|PDB:3GP0}.
STRAND 24 29 {ECO:0000244|PDB:3GP0}.
STRAND 31 33 {ECO:0000244|PDB:3GC8}.
TURN 34 37 {ECO:0000244|PDB:3GC9}.
STRAND 38 43 {ECO:0000244|PDB:3GP0}.
TURN 44 47 {ECO:0000244|PDB:3GP0}.
STRAND 48 54 {ECO:0000244|PDB:3GP0}.
HELIX 62 77 {ECO:0000244|PDB:3GP0}.
STRAND 86 90 {ECO:0000244|PDB:3GP0}.
HELIX 96 98 {ECO:0000244|PDB:3GP0}.
STRAND 103 107 {ECO:0000244|PDB:3GP0}.
STRAND 110 112 {ECO:0000244|PDB:3GP0}.
HELIX 113 119 {ECO:0000244|PDB:3GP0}.
HELIX 124 143 {ECO:0000244|PDB:3GP0}.
HELIX 153 155 {ECO:0000244|PDB:3GP0}.
STRAND 156 158 {ECO:0000244|PDB:3GP0}.
STRAND 164 166 {ECO:0000244|PDB:3GP0}.
HELIX 179 182 {ECO:0000244|PDB:3GC8}.
HELIX 185 188 {ECO:0000244|PDB:3GP0}.
HELIX 191 194 {ECO:0000244|PDB:3GP0}.
HELIX 203 218 {ECO:0000244|PDB:3GP0}.
HELIX 228 239 {ECO:0000244|PDB:3GP0}.
HELIX 244 249 {ECO:0000244|PDB:3GP0}.
TURN 253 255 {ECO:0000244|PDB:3GP0}.
HELIX 256 260 {ECO:0000244|PDB:3GP0}.
HELIX 270 273 {ECO:0000244|PDB:3GP0}.
TURN 274 276 {ECO:0000244|PDB:3GC8}.
HELIX 279 285 {ECO:0000244|PDB:3GP0}.
TURN 286 288 {ECO:0000244|PDB:3GP0}.
HELIX 293 295 {ECO:0000244|PDB:3GP0}.
HELIX 299 302 {ECO:0000244|PDB:3GP0}.
HELIX 306 308 {ECO:0000244|PDB:3GP0}.
TURN 309 311 {ECO:0000244|PDB:3GP0}.
HELIX 314 316 {ECO:0000244|PDB:3GP0}.
HELIX 326 329 {ECO:0000244|PDB:3GP0}.
HELIX 334 347 {ECO:0000244|PDB:3GP0}.
SEQUENCE 364 AA; 41357 MW; 68DA4C7B7C721475 CRC64;
MSGPRAGFYR QELNKTVWEV PQRLQGLRPV GSGAYGSVCS AYDARLRQKV AVKKLSRPFQ
SLIHARRTYR ELRLLKHLKH ENVIGLLDVF TPATSIEDFS EVYLVTTLMG ADLNNIVKCQ
ALSDEHVQFL VYQLLRGLKY IHSAGIIHRD LKPSNVAVNE DCELRILDFG LARQADEEMT
GYVATRWYRA PEIMLNWMHY NQTVDIWSVG CIMAELLQGK ALFPGSDYID QLKRIMEVVG
TPSPEVLAKI SSEHARTYIQ SLPPMPQKDL SSIFRGANPL AIDLLGRMLV LDSDQRVSAA
EALAHAYFSQ YHDPEDEPEA EPYDESVEAK ERTLEEWKEL TYQEVLSFKP PEPPKPPGSL
EIEQ


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