MAPKAPK5

MAPKAPK5
Identifiers
Aliases	MAPKAPK5, MAPKAP-K5, MK-5, MK5, PRAK, mitogen-activated protein kinase-activated protein kinase 5
External IDs	MGI: 1333110 HomoloGene: 69077 GeneCards: MAPKAPK5
Gene ontology Molecular function • transferase activity • nucleotide binding • protein kinase activity • calcium-dependent protein serine/threonine kinase activity • p53 binding • calmodulin binding • kinase activity • protein serine/threonine kinase activity • protein binding • calmodulin-dependent protein kinase activity • ATP binding • MAP kinase kinase activity Cellular component • cytoplasm • cytosol • nucleoplasm • nucleus Biological process • positive regulation of telomere capping • phosphorylation • stress-induced premature senescence • positive regulation of telomere maintenance via telomerase • protein phosphorylation • peptidyl-serine phosphorylation • positive regulation of telomerase activity • protein autophosphorylation • Ras protein signal transduction • regulation of translation • signal transduction • regulation of signal transduction by p53 class mediator • activation of MAPK activity • MAPK cascade • negative regulation of TOR signaling 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_139078	NM_010765
RefSeq (protein)	NP_003659.2 NP_620777.1	NP_034895.1
Location (UCSC)	Chr 12: 111.84 – 111.9 Mb	Chr 5: 121.53 – 121.55 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

MAP kinase-activated protein kinase 5 is an enzyme that in humans is encoded by the MAPKAPK5 gene.^[3][4] 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.^[4]

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. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. "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.