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MAPK12

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

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)^[1]

Band	22q13.33	Start	50,245,450bp^[1]
Band	22q13.33	End	50,261,716bp^[1]

Gene location (Mouse)

Chr.	Chromosome 15 (mouse)^[2]

Band	15\|15 E3	Start	89,014,787bp^[2]
Band	15\|15 E3	End	89,024,906bp^[2]

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

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Mitogen-activated protein kinase 12 (MAP kinase 12), also known asextracellular signal-regulated kinase 6 (ERK6) orstress-activated protein kinase 3 (SAPK3), is anenzyme that in humans is encoded by theMAPK12gene.^[5]

Function

[edit]

Activation of members of themitogen-activated protein kinase family is a major mechanism fortransduction 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 ofmyoblasts tomyotubes.^[5]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000188130 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000022610 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^^a ^b"Entrez Gene: mitogen-activated protein kinase 12".

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.Bibcode:2006JAChS.128.5913S.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.

v t e PDB gallery
1cm8: PHOSPHORYLATED MAP KINASE P38-GAMMA

Kinases:Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated mTOR EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1
Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3 PDK4
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4
Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase Aurora C kinase
Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-
IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP
cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY
cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1
Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3
Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase
Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2
G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6
Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK1A CAMK1B CAMK1D CAMK1G CAMK2 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1
Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4
Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2
Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19
Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4
Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1
Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14
MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14
Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3
(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)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

This article incorporates text from theUnited States National Library of Medicine, which is in thepublic domain.

This article on agene on humanchromosome 22 is astub. You can help Wikipedia byadding missing information.

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