MAPK12

Protein-coding gene in the species Homo sapiens
MAPK12
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1CM8, 4QUM

Identifiers
AliasesMAPK12, ERK3, ERK6, P38GAMMA, PRKM12, SAPK-3, SAPK3, ERK-6, MAPK 12, mitogen-activated protein kinase 12
External IDsOMIM: 602399 MGI: 1353438 HomoloGene: 55705 GeneCards: MAPK12
Gene location (Human)
Chromosome 22 (human)
Chr.Chromosome 22 (human)[1]
Chromosome 22 (human)
Genomic location for MAPK12
Genomic location for MAPK12
Band22q13.33Start50,245,450 bp[1]
End50,261,716 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for MAPK12
Genomic location for MAPK12
Band15|15 E3Start89,014,787 bp[2]
End89,024,906 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gastrocnemius muscle

  • triceps brachii muscle

  • vastus lateralis muscle

  • thoracic diaphragm

  • anterior pituitary

  • biceps brachii

  • stromal cell of endometrium

  • left uterine tube

  • deltoid muscle

  • cingulate gyrus
Top expressed in
  • triceps brachii muscle

  • temporal muscle

  • ankle

  • tibialis anterior muscle

  • vastus lateralis muscle

  • digastric muscle

  • sternocleidomastoid muscle

  • gastrocnemius muscle

  • soleus muscle

  • skeletal muscle tissue
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
SpeciesHumanMouse
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 MbChr 15: 89.01 – 89.02 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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]

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000188130 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "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. 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.
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  • 1cm8: PHOSPHORYLATED MAP KINASE P38-GAMMA
    1cm8: PHOSPHORYLATED MAP KINASE P38-GAMMA
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Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
  • -
Tropomyosin kinase (EC 2.7.11.28)
  • -
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
  • -
Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
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