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.

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; OMA:MAPK12 - orthologs
Gene location (Human) Chr. Chromosome 22 (human) Band 22q13.33 Start 50,245,450 bp End 50,261,716 bp
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15|15 E3 Start 89,014,787 bp End 89,024,906 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastrocnemius muscle muscle of thigh triceps brachii muscle vastus lateralis muscle Skeletal muscle tissue of rectus abdominis thoracic diaphragm right hemisphere of cerebellum anterior pituitary glutes biceps brachii Top expressed in muscle of thigh triceps brachii muscle temporal muscle ankle tibialis anterior muscle vastus lateralis muscle digastric muscle sternocleidomastoid muscle gastrocnemius muscle medial head of gastrocnemius muscle More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity protein kinase activity nucleotide binding metal ion binding kinase activity protein binding ATP binding magnesium ion binding protein serine/threonine kinase activity MAP kinase activity Cellular component cytosol mitochondrion nucleoplasm 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 DNA damage induced protein phosphorylation cell cycle myoblast differentiation signal transduction MAPK cascade regulation of gene expression 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 NP_001389948 NP_001389949 NP_001389950 NP_001389951 Location (UCSC) Chr 22: 50.25 – 50.26 Mb Chr 15: 89.01 – 89.02 Mb PubMed search
Wikidata
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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.

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. S2CID 23541383.
• 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. S2CID 22471158.
• 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. S2CID 4909652.
• 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.