MAPK12

Mitogen-activated protein kinase 12 (MAP kinase 12), also known as extracellular signal-regulated kinase 6 (ERK6) or stress-activated protein kinase 3 (SAPK3), is an enzyme that in humans is encoded by the MAPK12 gene.[5]

MAPK12
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1CM8, 4QUM
Identifiers
Aliases	MAPK12, ERK3, ERK6, P38GAMMA, PRKM12, SAPK-3, SAPK3, ERK-6, MAPK 12, mitogen-activated protein kinase 12
External IDs	OMIM: 602399 MGI: 1353438 HomoloGene: 55705 GeneCards: MAPK12
Gene location (Human) Chr. Chromosome 22 (human)[1] Band 22q13.33 Start 50,245,450 bp[1] End 50,261,716 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15|15 E3 Start 89,130,584 bp[2] End 89,140,703 bp[2]
Gene ontology Molecular function • transferase activity • protein kinase activity • nucleotide binding • metal ion binding • kinase activity • GO:0001948 protein binding • ATP binding • magnesium ion binding • protein serine/threonine kinase activity • MAP kinase activity Cellular component • cytosol • mitochondrion • nucleoplasm • cell nucleus • cytoplasm Biological process • regulation of transcription, DNA-templated • phosphorylation • positive regulation of muscle cell differentiation • muscle organ development • negative regulation of cell cycle • transcription, DNA-templated • positive regulation of peptidase activity • protein phosphorylation • peptidyl-serine phosphorylation • cell cycle arrest • DNA damage induced protein phosphorylation • cell cycle • myoblast differentiation • signal transduction • MAPK cascade • regulation of gene expression • GO:0007243 intracellular signal transduction • cellular response to organic substance Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6300	29857
Ensembl	ENSG00000188130	ENSMUSG00000022610
UniProt	P53778	O08911
RefSeq (mRNA)	NM_002969 NM_001303252	NM_013871
RefSeq (protein)	NP_001290181 NP_002960	NP_038899
Location (UCSC)	Chr 22: 50.25 – 50.26 Mb	Chr 15: 89.13 – 89.14 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Activation of members of the mitogen-activated protein kinase family is a major mechanism for transduction of extracellular signals. Stress-activated protein kinases are one subclass of MAP kinases. The protein encoded by this gene functions as a signal transducer during differentiation of myoblasts to myotubes.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000188130 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022610 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: mitogen-activated protein kinase 12".

Further reading

• Stiffler MA, Grantcharova VP, Sevecka M, MacBeath G (2006). "Uncovering quantitative protein interaction networks for mouse PDZ domains using protein microarrays". J. Am. Chem. Soc. 128 (17): 5913–22. doi:10.1021/ja060943h. PMC 2533859. PMID 16637659.
• Joneson T, Bar-Sagi D (1997). "Ras effectors and their role in mitogenesis and oncogenesis". J. Mol. Med. 75 (8): 587–93. doi:10.1007/s001090050143. PMID 9297626.
• Hou SW, Zhi HY, Pohl N, et al. (2010). "PTPH1 dephosphorylates and cooperates with p38gamma MAPK to increase ras oncogenesis through PDZ-mediated interaction". Cancer Res. 70 (7): 2901–10. doi:10.1158/0008-5472.CAN-09-3229. PMC 2848905. PMID 20332238.
• Gutierrez-Sanmartin D, Varela-Ledo E, Aguilera A, et al. (2008). "Implication of p38 mitogen-activated protein kinase isoforms (alpha, beta, gamma and delta) in CD4+ T-cell infection with human immunodeficiency virus type I." J. Gen. Virol. 89 (Pt 7): 1661–71. doi:10.1099/vir.0.82971-0. PMID 18559936.
• Sabio G, Cerezo-Guisado MI, Del Reino P, et al. (2010). "p38gamma regulates interaction of nuclear PSF and RNA with the tumour-suppressor hDlg in response to osmotic shock". J. Cell Sci. 123 (Pt 15): 2596–604. doi:10.1242/jcs.066514. PMC 2908048. PMID 20605917.
• Zhang J, Harrison JS, Studzinski GP (2011). "Isoforms of p38MAPK gamma and delta contribute to differentiation of human AML cells induced by 1,25-dihydroxyvitamin D₃". Exp. Cell Res. 317 (1): 117–30. doi:10.1016/j.yexcr.2010.08.010. PMC 2998239. PMID 20804750.
• Kwong J, Hong L, Liao R, et al. (2009). "p38alpha and p38gamma mediate oncogenic ras-induced senescence through differential mechanisms". J. Biol. Chem. 284 (17): 11237–46. doi:10.1074/jbc.M808327200. PMC 2670128. PMID 19251701.
• Morishima-Kawashima M, Hasegawa M, Takio K, et al. (1995). "Hyperphosphorylation of tau in PHF". Neurobiol. Aging. 16 (3): 365–71, discussion 371–80. doi:10.1016/0197-4580(95)00027-C. PMID 7566346.
• Diskin R, Askari N, Capone R, et al. (2004). "Active mutants of the human p38alpha mitogen-activated protein kinase". J. Biol. Chem. 279 (45): 47040–9. doi:10.1074/jbc.M404595200. PMID 15284239.
• Askari N, Diskin R, Avitzour M, et al. (2007). "Hyperactive variants of p38alpha induce, whereas hyperactive variants of p38gamma suppress, activating protein 1-mediated transcription". J. Biol. Chem. 282 (1): 91–9. doi:10.1074/jbc.M608012200. PMID 17088247.
• Krauss RS, Cole F, Gaio U, et al. (2005). "Close encounters: regulation of vertebrate skeletal myogenesis by cell-cell contact". J. Cell Sci. 118 (Pt 11): 2355–62. doi:10.1242/jcs.02397. PMID 15923648.
• Talmud PJ, Drenos F, Shah S, et al. (2009). "Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip". Am. J. Hum. Genet. 85 (5): 628–42. doi:10.1016/j.ajhg.2009.10.014. PMC 2775832. PMID 19913121.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• Tosti E, Waldbaum L, Warshaw G, et al. (2004). "The stress kinase MRK contributes to regulation of DNA damage checkpoints through a p38gamma-independent pathway". J. Biol. Chem. 279 (46): 47652–60. doi:10.1074/jbc.M409961200. PMID 15342622.
• 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.
• Qi X, Pohl NM, Loesch M, et al. (2007). "p38alpha antagonizes p38gamma activity through c-Jun-dependent ubiquitin-proteasome pathways in regulating Ras transformation and stress response". J. Biol. Chem. 282 (43): 31398–408. doi:10.1074/jbc.M703857200. PMID 17724032.
• Collins JE, Wright CL, Edwards CA, et al. (2004). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
• Kukkonen-Macchi A, Sicora O, Kaczynska K, et al. (2011). "Loss of p38gamma MAPK induces pleiotropic mitotic defects and massive cell death". J. Cell Sci. 124 (Pt 2): 216–27. doi:10.1242/jcs.068254. PMID 21172807.
• Sofroniew MV, Howe CL, Mobley WC (2001). "Nerve growth factor signaling, neuroprotection, and neural repair". Annu. Rev. Neurosci. 24: 1217–81. doi:10.1146/annurev.neuro.24.1.1217. PMID 11520933.
• Bailey SD, Xie C, Do R, et al. (2010). "Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study". Diabetes Care. 33 (10): 2250–3. doi:10.2337/dc10-0452. PMC 2945168. PMID 20628086.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.