MAPKAPK5

Mitogen-activated protein kinase-activated protein kinase 5
Identifiers
Symbols	MAPKAPK5 ; MAPKAP-K5; MK-5; MK5; PRAK
External IDs	OMIM: 606723 MGI: 1333110 HomoloGene: 69077 ChEMBL: 3094 GeneCards: MAPKAPK5 Gene
EC number	2.7.11.1
Gene ontology Molecular function • p53 binding • protein serine/threonine kinase activity • calmodulin-dependent protein kinase activity • MAP kinase kinase activity • signal transducer activity • protein binding • calmodulin binding • ATP binding • calcium-dependent protein serine/threonine kinase activity • mitogen-activated protein kinase binding Cellular component • nucleoplasm • cytoplasm Biological process • MAPK cascade • activation of MAPK activity • regulation of translation • signal transduction • cell surface receptor signaling pathway • Ras protein signal transduction • peptidyl-serine phosphorylation • negative regulation of TOR signaling • protein autophosphorylation • stress-induced premature senescence Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8550	17165
Ensembl	ENSG00000089022	ENSMUSG00000029454
UniProt	Q8IW41	O54992
RefSeq (mRNA)	NM_003668	NM_010765
RefSeq (protein)	NP_003659	NP_034895
Location (UCSC)	Chr 12: 111.84 – 111.9 Mb	Chr 5: 121.53 – 121.55 Mb
PubMed search

MAP kinase-activated protein kinase 5 is an enzyme that in humans is encoded by the MAPKAPK5 gene.^[1][2] The protein encoded by this gene is a member of the serine/threonine kinase family. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. In vitro, this kinase phosphorylates heat shock protein HSP27 at its physiologically relevant sites. Two alternately spliced transcript variants of this gene encoding distinct isoforms have been reported.^[2]

A link between Alzheimer's disease and reduced levels of MAPKAPK5 has been proposed. But clinical trials are needed to confirm if this is the case.

References

1. New L, Jiang Y, Zhao M, Liu K, Zhu W, Flood LJ, Kato Y, Parry GC, Han J (Jul 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.
2. "Entrez Gene: MAPKAPK5 mitogen-activated protein kinase-activated protein kinase 5".

Further reading

• de Carvalho MG, McCormack AL, Olson E, et al. (1996). "Identification of phosphorylation sites of human 85-kDa cytosolic phospholipase A2 expressed in insect cells and present in human monocytes.". J. Biol. Chem. 271 (12): 6987–97. doi:10.1074/jbc.271.12.6987. PMID 8636128.
• Börsch-Haubold AG, Bartoli F, Asselin J, et al. (1998). "Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells.". J. Biol. Chem. 273 (8): 4449–58. doi:10.1074/jbc.273.8.4449. PMID 9468497.
• Ni H, Wang XS, Diener K, Yao Z (1998). "MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase.". Biochem. Biophys. Res. Commun. 243 (2): 492–6. doi:10.1006/bbrc.1998.8135. PMID 9480836.
• Sudo T, Maruyama M, Osada H (2000). "p62 functions as a p38 MAP kinase regulator.". Biochem. Biophys. Res. Commun. 269 (2): 521–5. doi:10.1006/bbrc.2000.2333. PMID 10708586.
• Hefner Y, Borsch-Haubold AG, Murakami M, et al. (2001). "Serine 727 phosphorylation and activation of cytosolic phospholipase A2 by MNK1-related protein kinases.". J. Biol. Chem. 275 (48): 37542–51. doi:10.1074/jbc.M003395200. PMID 10978317.
• Zhou J, Lottenbach KR, Barenkamp SJ, et al. (2002). "Recurrent variable region gene usage and somatic mutation in the human antibody response to the capsular polysaccharide of Streptococcus pneumoniae type 23F.". Infect. Immun. 70 (8): 4083–91. doi:10.1128/IAI.70.8.4083-4091.2002. PMC 128163. PMID 12117915.
• Perfetti V, Casarini S, Palladini G, et al. (2002). "Analysis of V(lambda)-J(lambda) expression in plasma cells from primary (AL) amyloidosis and normal bone marrow identifies 3r (lambdaIII) as a new amyloid-associated germline gene segment.". Blood 100 (3): 948–53. doi:10.1182/blood-2002-01-0114. PMID 12130507.
• 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.
• 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. PMC 139241. PMID 12477932.
• New L, Jiang Y, Han J (2004). "Regulation of PRAK subcellular location by p38 MAP kinases.". Mol. Biol. Cell 14 (6): 2603–16. doi:10.1091/mbc.E02-08-0538. PMC 194907. PMID 12808055.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Sun P, Yoshizuka N, New L, et al. (2007). "PRAK is essential for ras-induced senescence and tumor suppression.". Cell 128 (2): 295–308. doi:10.1016/j.cell.2006.11.050. PMID 17254968.