MAPK11

Mitogen-activated protein kinase 11 is an enzyme that in humans is encoded by the MAPK11 gene.

MAPK11
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3GC8, 3GC9, 3GP0
Identifiers
Aliases	MAPK11, P38B, P38BETA2, PRKM11, SAPK2, SAPK2B, p38-2, p38Beta, mitogen-activated protein kinase 11
External IDs	OMIM: 602898; MGI: 1338024; HomoloGene: 55684; GeneCards: MAPK11; OMA:MAPK11 - orthologs
Gene location (Human) Chr. Chromosome 22 (human) Band 22q13.33 Start 50,263,713 bp End 50,270,767 bp
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15|15 E3 Start 89,026,689 bp End 89,033,831 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right frontal lobe right hemisphere of cerebellum Brodmann area 9 middle temporal gyrus cingulate gyrus anterior cingulate cortex apex of heart caudate nucleus Brodmann area 23 putamen Top expressed in lumbar spinal ganglion ventricular zone visual cortex primary visual cortex tail of embryo superior frontal gyrus superior cervical ganglion ganglionic eminence primary motor cortex cerebellar cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity MAP kinase activity kinase activity protein serine/threonine kinase activity protein binding ATP binding Cellular component cytosol nucleoplasm nucleus cytoplasm Biological process regulation of transcription, DNA-templated regulation of cardiac muscle cell proliferation positive regulation of erythrocyte differentiation phosphorylation positive regulation of muscle cell differentiation transcription, DNA-templated protein phosphorylation positive regulation of gene expression negative regulation of cardiac muscle cell proliferation regulation of signal transduction by p53 class mediator stress-activated MAPK cascade cellular response to interleukin-1 regulation of gene expression intracellular signal transduction cellular response to organic substance Ras protein signal transduction vascular endothelial growth factor receptor signaling pathway regulation of DNA-binding transcription factor activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5600 19094 Ensembl ENSG00000185386 ENSMUSG00000053137 UniProt Q15759 Q9WUI1 RefSeq (mRNA) NM_002751 NM_011161 RefSeq (protein) NP_002742 NP_035291 Location (UCSC) Chr 22: 50.26 – 50.27 Mb Chr 15: 89.03 – 89.03 Mb PubMed search
Wikidata
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Function

The protein encoded by this gene is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation, and development. This kinase is most closely related to p38 MAP kinase, both of which can be activated by proinflammatory cytokines and environmental stress. This kinase is activated through its phosphorylation by MAP kinase kinases (MKKs), preferably by MKK6. Transcription factor ATF2/CREB2 has been shown to be a substrate of this kinase.

Interactions

MAPK11 has been shown to interact with HDAC3 and Promyelocytic leukemia protein.

See also

• p38 mitogen-activated protein kinases

External links

• MAP Kinase Resource Archived 2021-04-15 at the Wayback Machine.

Further reading

• Jiang Y, Chen C, Li Z, Guo W, Gegner JA, Lin S, Han J (1996). "Characterization of the structure and function of a new mitogen-activated protein kinase (p38beta)". J. Biol. Chem. 271 (30): 17920–6. doi:10.1074/jbc.271.30.17920. PMID 8663524.
• Kumar S, McDonnell PC, Gum RJ, Hand AT, Lee JC, Young PR (1997). "Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles". Biochem. Biophys. Res. Commun. 235 (3): 533–8. doi:10.1006/bbrc.1997.6849. PMID 9207191.
• Stein B, Yang MX, Young DB, Janknecht R, Hunter T, Murray BW, Barbosa MS (1997). "p38-2, a novel mitogen-activated protein kinase with distinct properties". J. Biol. Chem. 272 (31): 19509–17. doi:10.1074/jbc.272.31.19509. PMID 9235954.
• Enslen H, Raingeaud J, Davis RJ (1998). "Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6". J. Biol. Chem. 273 (3): 1741–8. doi:10.1074/jbc.273.3.1741. PMID 9430721.
• New L, Jiang Y, Zhao M, Liu K, Zhu W, Flood LJ, Kato Y, Parry GC, Han J (1998). "PRAK, a novel protein kinase regulated by the p38 MAP kinase". EMBO J. 17 (12): 3372–84. doi:10.1093/emboj/17.12.3372. PMC 1170675. PMID 9628874.
• Deak M, Clifton AD, Lucocq LM, Alessi DR (1998). "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 (15): 4426–41. doi:10.1093/emboj/17.15.4426. PMC 1170775. PMID 9687510.
• Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
• Lee SH, Park J, Che Y, Han PL, Lee JK (2000). "Constitutive activity and differential localization of p38alpha and p38beta MAPKs in adult mouse brain". J. Neurosci. Res. 60 (5): 623–31. doi:10.1002/(SICI)1097-4547(20000601)60:5<623::AID-JNR7>3.0.CO;2-4. PMID 10820433. S2CID 21839143.
• Tanoue T, Yamamoto T, Maeda R, Nishida E (2001). "A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs". J. Biol. Chem. 276 (28): 26629–39. doi:10.1074/jbc.M101981200. PMID 11359773.
• Torcia M, De Chiara G, Nencioni L, Ammendola S, Labardi D, Lucibello M, Rosini P, Marlier LN, Bonini P, Dello Sbarba P, Palamara AT, Zambrano N, Russo T, Garaci E, Cozzolino F (2001). "Nerve growth factor inhibits apoptosis in memory B lymphocytes via inactivation of p38 MAPK, prevention of Bcl-2 phosphorylation, and cytochrome c release" (PDF). J. Biol. Chem. 276 (42): 39027–36. doi:10.1074/jbc.M102970200. PMID 11495898.
• Driggers PH, Segars JH, Rubino DM (2001). "The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway". J. Biol. Chem. 276 (50): 46792–7. doi:10.1074/jbc.M106927200. PMC 4152864. PMID 11579095.
• Ge B, Gram H, Di Padova F, Huang B, New L, Ulevitch RJ, Luo Y, Han J (2002). "MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha". Science. 295 (5558): 1291–4. Bibcode:2002Sci...295.1291G. doi:10.1126/science.1067289. PMID 11847341. S2CID 93896233.
• Reunanen N, Li SP, Ahonen M, Foschi M, Han J, Kähäri VM (2002). "Activation of p38 alpha MAPK enhances collagenase-1 (matrix metalloproteinase (MMP)-1) and stromelysin-1 (MMP-3) expression by mRNA stabilization". J. Biol. Chem. 277 (35): 32360–8. doi:10.1074/jbc.M204296200. PMID 12060661.
• Knebel A, Haydon CE, Morrice N, Cohen P (2002). "Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways". Biochem. J. 367 (Pt 2): 525–32. doi:10.1042/BJ20020916. PMC 1222910. PMID 12171600.
• Kinet S, Bernard F, Mongellaz C, Perreau M, Goldman FD, Taylor N (2002). "gp120-mediated induction of the MAPK cascade is dependent on the activation state of CD4(+) lymphocytes". Blood. 100 (7): 2546–53. doi:10.1182/blood-2002-03-0819. PMID 12239168.
• Lim S, Zou Y, Friedman E (2002). "The transcriptional activator Mirk/Dyrk1B is sequestered by p38alpha/beta MAP kinase". J. Biol. Chem. 277 (51): 49438–45. doi:10.1074/jbc.M206840200. PMID 12384504.
• Naderi J, Hung M, Pandey S (2003). "Oxidative stress-induced apoptosis in dividing fibroblasts involves activation of p38 MAP kinase and over-expression of Bax: resistance of quiescent cells to oxidative stress". Apoptosis. 8 (1): 91–100. doi:10.1023/A:1021657220843. PMID 12510156. S2CID 19686042.
• Stringaris AK, Geisenhainer J, Bergmann F, Balshüsemann C, Lee U, Zysk G, Mitchell TJ, Keller BU, Kuhnt U, Gerber J, Spreer A, Bähr M, Michel U, Nau R (2002). "Neurotoxicity of pneumolysin, a major pneumococcal virulence factor, involves calcium influx and depends on activation of p38 mitogen-activated protein kinase". Neurobiol. Dis. 11 (3): 355–68. doi:10.1006/nbdi.2002.0561. hdl:11858/00-001M-0000-0012-F282-1. PMID 12586546. S2CID 25034287.