MAPK11

From Wikipedia, the free encyclopedia

Mitogen-activated protein kinase 11

Identifiers

MAPK11; P38B; P38BETA2; PRKM11; SAPK2; SAPK2B; p38-2; p38Beta

External IDs

OMIM: 602898 MGI: 1338024 HomoloGene: 55684

Gene ontology
Molecular Function:	• nucleotide binding • protein serine/threonine kinase activity • MAP kinase activity • protein binding • ATP binding • MP kinase activity • transferase activity
Cellular Component:	• cellular_component
Biological Process:	• protein amino acid phosphorylation • response to stress • signal transduction • protein kinase cascade • antimicrobial humoral response

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002751 (mRNA)
NP_002742 (protein)

NM_011161 (mRNA)
NP_035291 (protein)

Location

Chr 22: 49.04 - 49.05 Mb

Chr 15: 88.97 - 88.98 Mb

Pubmed search

[1]

[2]

Mitogen-activated protein kinase 11, also known as MAPK11, is a human gene.^[1]

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.^[1]

[edit] See also

p38 mitogen-activated protein kinases

[edit] References

^ ^a ^b Entrez Gene: MAPK11 mitogen-activated protein kinase 11.

[edit] Further reading

Jiang Y, Chen C, Li Z, et al. (1996). "Characterization of the structure and function of a new mitogen-activated protein kinase (p38beta).". J. Biol. Chem. 271 (30): 17920–6. PMID 8663524.
Kumar S, McDonnell PC, Gum RJ, et al. (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.
Goedert M, Cuenda A, Craxton M, et al. (1997). "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 (12): 3563–71. doi:10.1093/emboj/16.12.3563. PMID 9218798.
Stein B, Yang MX, Young DB, et al. (1997). "p38-2, a novel mitogen-activated protein kinase with distinct properties.". J. Biol. Chem. 272 (31): 19509–17. 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. PMID 9430721.
New L, Jiang Y, Zhao M, et al. (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. 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. PMID 9687510.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22.". Nature 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
Lee SH, Park J, Che Y, et al. (2000). "Constitutive activity and differential localization of p38alpha and p38beta MAPKs in adult mouse brain.". J. Neurosci. Res. 60 (5): 623–31. PMID 10820433.
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, et al. (2001). "Nerve growth factor inhibits apoptosis in memory B lymphocytes via inactivation of p38 MAPK, prevention of Bcl-2 phosphorylation, and cytochrome c release.". J. Biol. Chem. 276 (42): 39027–36. doi:10.1074/jbc.M102970200. PMID 11495898.
Driggers PH, Segars JH, Rubino DM (2002). "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. PMID 11579095.
Ge B, Gram H, Di Padova F, et al. (2002). "MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha.". Science 295 (5558): 1291–4. doi:10.1126/science.1067289. PMID 11847341.
Reunanen N, Li SP, Ahonen M, et al. (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. PMID 12171600.
Kinet S, Bernard F, Mongellaz C, et al. (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 (2003). "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.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
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. PMID 12510156.
Stringaris AK, Geisenhainer J, Bergmann F, et al. (2003). "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. PMID 12586546.