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External IDsGeneCards: [1]
RefSeq (mRNA)



RefSeq (protein)



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Mitogen-activated protein kinase 11 is an enzyme that in humans is encoded by the MAPK11 gene.[1][2]


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.[2]


MAPK11 has been shown to interact with HDAC3[3] and Promyelocytic leukemia protein.[4]

See also


  1. Goedert M, Cuenda A, Craxton M, Jakes R, Cohen P (Aug 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. PMC 1169981. PMID 9218798.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  2. 2.0 2.1 "Entrez Gene: MAPK11 mitogen-activated protein kinase 11".<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  3. Mahlknecht U, Will J, Varin A, Hoelzer D, Herbein G (Sep 2004). "Histone deacetylase 3, a class I histone deacetylase, suppresses MAPK11-mediated activating transcription factor-2 activation and represses TNF gene expression". J. Immunol. 173 (6): 3979–90. doi:10.4049/jimmunol.173.6.3979. PMID 15356147.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  4. Shin J, Park B, Cho S, Lee S, Kim Y, Lee SO, Cho K, Lee S, Jin BS, Ahn JH, Choi EJ, Ahn K (Sep 2004). "Promyelocytic leukemia is a direct inhibitor of SAPK2/p38 mitogen-activated protein kinase". J. Biol. Chem. 279 (39): 40994–1003. doi:10.1074/jbc.M407369200. PMID 15273249.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>

External links

Further reading

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  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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. doi:10.1038/990031. PMID 10591208.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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". J. Biol. Chem. 276 (42): 39027–36. doi:10.1074/jbc.M102970200. PMID 11495898.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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. doi:10.1126/science.1067289. PMID 11847341.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>
  • 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. PMID 12586546.<templatestyles src="Module:Citation/CS1/styles.css"></templatestyles>