GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

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.
17-JUN-2020, entry version 203.
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 ACTIVITY 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 ACTIVITY 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 ACTIVITY 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, ACTIVITY
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 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).
[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:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.24;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ACTIVITY REGULATION: 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:
Q15759; Q16644: MAPKAPK3; NbExp=3; IntAct=EBI-298304, EBI-1384657;
Q15759; P04637: TP53; NbExp=2; IntAct=EBI-298304, EBI-366083;
Q15759; 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;
-!- 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/";
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
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]
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; -.
SMR; Q15759; -.
BioGRID; 111586; 36.
IntAct; Q15759; 21.
MINT; Q15759; -.
STRING; 9606.ENSP00000333685; -.
BindingDB; Q15759; -.
ChEMBL; CHEMBL3961; -.
DrugBank; DB05157; KC706.
DrugBank; DB08896; Regorafenib.
DrugCentral; Q15759; -.
GuidetoPHARMACOLOGY; 1500; -.
iPTMnet; Q15759; -.
PhosphoSitePlus; Q15759; -.
BioMuta; MAPK11; -.
DMDM; 134047835; -.
CPTAC; CPTAC-872; -.
CPTAC; CPTAC-873; -.
EPD; Q15759; -.
jPOST; Q15759; -.
MassIVE; Q15759; -.
PaxDb; Q15759; -.
PeptideAtlas; Q15759; -.
PRIDE; Q15759; -.
ProteomicsDB; 60745; -. [Q15759-1]
ProteomicsDB; 6736; -.
Antibodypedia; 28468; 504 antibodies.
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; ENSG00000185386; Low tissue specificity.
MIM; 602898; gene.
neXtProt; NX_Q15759; -.
OpenTargets; ENSG00000185386; -.
PharmGKB; PA30618; -.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
GeneTree; ENSGT00940000160790; -.
HOGENOM; CLU_000288_181_1_1; -.
InParanoid; Q15759; -.
KO; K04441; -.
OMA; IKPRVPF; -.
OrthoDB; 683132at2759; -.
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-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-525793; Myogenesis.
Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
SignaLink; Q15759; -.
SIGNOR; Q15759; -.
BioGRID-ORCS; 5600; 3 hits in 817 CRISPR screens.
EvolutionaryTrace; Q15759; -.
GeneWiki; MAPK11; -.
GenomeRNAi; 5600; -.
Pharos; Q15759; Tchem.
PRO; PR:Q15759; -.
Proteomes; UP000005640; Chromosome 22.
RNAct; Q15759; protein.
Bgee; ENSG00000185386; Expressed in anterior cingulate cortex and 145 other tissues.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
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:0010468; P:regulation of gene expression; IBA:GO_Central.
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: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-like.
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; Cytoplasm; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Stress response;
Transcription; Transcription regulation; Transferase.
CHAIN 1..364
/note="Mitogen-activated protein kinase 11"
/id="PRO_0000186280"
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..110
/note="Inhibitor-binding"
REGION 168..169
/note="Inhibitor-binding"
MOTIF 180..182
/note="TXY"
ACT_SITE 150
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 53
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 71
/note="Nilotinib"
MOD_RES 180
/note="Phosphothreonine; by MAP2K3, MAP2K4 and MAP2K6"
/evidence="ECO:0000305|PubMed:15356147"
MOD_RES 182
/note="Phosphotyrosine; by MAP2K3, MAP2K4 and MAP2K6"
/evidence="ECO:0000305|PubMed:15356147"
MOD_RES 323
/note="Phosphotyrosine; by ZAP70"
/evidence="ECO:0000250"
VAR_SEQ 1..108
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_055221"
VAR_SEQ 204..321
/note="VDIWSVGCIMAELLQGKALFPGSDYIDQLKRIMEVVGTPSPEVLAKISSEHA
RTYIQSLPPMPQKDLSSIFRGANPLAIDLLGRMLVLDSDQRVSAAEALAHAYFSQYHDP
EDEPEAE -> GAGGRPWGDEGQGPRLALDWLCMPGLRGQARSPRMWDPHSKVALQRPL
EHDGCWPPLAVQLWTSPCLGGLGMAEEGVCPSWGLDVTVGLLEEGRGVGTLMEVPSPSH
SGYLVRGLHHG (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_055222"
VAR_SEQ 322..364
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_055223"
VARIANT 221
/note="A -> V (in a lung neuroendocrine carcinoma sample;
somatic mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042264"
VARIANT 275
/note="R -> H (in dbSNP:rs33932986)"
/evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.9"
/id="VAR_025176"
MUTAGEN 180
/note="T->A: Inactivation."
MUTAGEN 182
/note="Y->F: Inactivation."
CONFLICT 98
/note="D -> V (in Ref. 8; BAF84534)"
/evidence="ECO:0000305"
CONFLICT 122..123
/note="LS -> GAHQGARLAL (in Ref. 1; AAB05036)"
/evidence="ECO:0000305"
CONFLICT 326
/note="S -> G (in Ref. 6; AAB66313)"
/evidence="ECO:0000305"
STRAND 8..15
/evidence="ECO:0000244|PDB:3GP0"
STRAND 17..21
/evidence="ECO:0000244|PDB:3GP0"
STRAND 24..29
/evidence="ECO:0000244|PDB:3GP0"
STRAND 31..33
/evidence="ECO:0000244|PDB:3GC8"
TURN 34..37
/evidence="ECO:0000244|PDB:3GC9"
STRAND 38..43
/evidence="ECO:0000244|PDB:3GP0"
TURN 44..47
/evidence="ECO:0000244|PDB:3GP0"
STRAND 48..54
/evidence="ECO:0000244|PDB:3GP0"
HELIX 62..77
/evidence="ECO:0000244|PDB:3GP0"
STRAND 86..90
/evidence="ECO:0000244|PDB:3GP0"
HELIX 96..98
/evidence="ECO:0000244|PDB:3GP0"
STRAND 103..107
/evidence="ECO:0000244|PDB:3GP0"
STRAND 110..112
/evidence="ECO:0000244|PDB:3GP0"
HELIX 113..119
/evidence="ECO:0000244|PDB:3GP0"
HELIX 124..143
/evidence="ECO:0000244|PDB:3GP0"
HELIX 153..155
/evidence="ECO:0000244|PDB:3GP0"
STRAND 156..158
/evidence="ECO:0000244|PDB:3GP0"
STRAND 164..166
/evidence="ECO:0000244|PDB:3GP0"
HELIX 179..182
/evidence="ECO:0000244|PDB:3GC8"
HELIX 185..188
/evidence="ECO:0000244|PDB:3GP0"
HELIX 191..194
/evidence="ECO:0000244|PDB:3GP0"
HELIX 203..218
/evidence="ECO:0000244|PDB:3GP0"
HELIX 228..239
/evidence="ECO:0000244|PDB:3GP0"
HELIX 244..249
/evidence="ECO:0000244|PDB:3GP0"
TURN 253..255
/evidence="ECO:0000244|PDB:3GP0"
HELIX 256..260
/evidence="ECO:0000244|PDB:3GP0"
HELIX 270..273
/evidence="ECO:0000244|PDB:3GP0"
TURN 274..276
/evidence="ECO:0000244|PDB:3GC8"
HELIX 279..285
/evidence="ECO:0000244|PDB:3GP0"
TURN 286..288
/evidence="ECO:0000244|PDB:3GP0"
HELIX 293..295
/evidence="ECO:0000244|PDB:3GP0"
HELIX 299..302
/evidence="ECO:0000244|PDB:3GP0"
HELIX 306..308
/evidence="ECO:0000244|PDB:3GP0"
TURN 309..311
/evidence="ECO:0000244|PDB:3GP0"
HELIX 314..316
/evidence="ECO:0000244|PDB:3GP0"
HELIX 326..329
/evidence="ECO:0000244|PDB:3GP0"
HELIX 334..347
/evidence="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


Related products :

Catalog number Product name Quantity
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
EIAAB24865 MAP kinase 11,MAP kinase p38 beta,MAPK 11,Mapk11,Mitogen-activated protein kinase 11,Mitogen-activated protein kinase p38 beta,Mouse,Mus musculus,p38B,Prkm11
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
EIAAB24862 c-Jun N-terminal kinase 3,Jnk3,MAP kinase 10,MAPK 10,Mapk10,Mitogen-activated protein kinase 10,p54-beta,Prkm10,Rat,Rattus norvegicus,SAPK-beta,Stress-activated protein kinase JNK3
EIAAB24855 c-Jun N-terminal kinase 1,Homo sapiens,Human,JNK1,JNK-46,MAP kinase 8,MAPK 8,MAPK8,Mitogen-activated protein kinase 8,PRKM8,SAPK1,Stress-activated protein kinase 1,Stress-activated protein kinase JNK1
10-782-55057 Mitogen-activated protein kinase 11 - EC 2.7.11.24; Mitogen-activated protein kinase p38 beta; MAP kinase p38 beta; p38b; p38-2; Stress-activated protein kinase 2 N_A 0.005 mg
10-782-55057 Mitogen-activated protein kinase 11 - EC 2.7.11.24; Mitogen-activated protein kinase p38 beta; MAP kinase p38 beta; p38b; p38-2; Stress-activated protein kinase 2 N_A 0.001 mg
10-782-55057 Mitogen-activated protein kinase 11 - EC 2.7.11.24; Mitogen-activated protein kinase p38 beta; MAP kinase p38 beta; p38b; p38-2; Stress-activated protein kinase 2 N_A 0.02 mg
10-782-55057 Mitogen-activated protein kinase 11 - EC 2.7.11.24; Mitogen-activated protein kinase p38 beta; MAP kinase p38 beta; p38b; p38-2; Stress-activated protein kinase 2 N_A 0.01 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
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
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
EIAAB24869 MAP kinase 13,MAP kinase p38 delta,MAPK 13,Mapk13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,Rat,Rattus norvegicus,Stress-activated protein kinase 4
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
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
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
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.05 mg
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.001 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.01 mg