MAPK11

MAPK11

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
3GC8, 3GC9, 3GP0

Identifiers

MAPK11, P38B, P38BETA2, PRKM11, SAPK2, SAPK2B, p38-2, p38Beta, mitogen-activated protein kinase 11

External IDs

OMIM: 602898; MGI: 1338024; HomoloGene: 55684; GeneCards: MAPK11; OMA:MAPK11 - orthologs

Gene location (Human)

Chr.	Chromosome 22 (human)^[1]

Band	22q13.33	Start	50,263,713 bp^[1]
Band	22q13.33	End	50,270,767 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 15 (mouse)^[2]

Band	15\|15 E3	Start	89,026,689 bp^[2]
Band	15\|15 E3	End	89,033,831 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

right frontal lobe

right hemisphere of cerebellum

Brodmann area 9

middle temporal gyrus

cingulate gyrus

anterior cingulate cortex

apex of heart

caudate nucleus

Brodmann area 23

putamen

Top expressed in

lumbar spinal ganglion

ventricular zone

visual cortex

primary visual cortex

tail of embryo

superior frontal gyrus

superior cervical ganglion

ganglionic eminence

primary motor cortex

cerebellar cortex

More reference expression data


More reference expression data

Gene ontology
Molecular function	transferase activity nucleotide binding protein kinase activity MAP kinase activity kinase activity protein serine/threonine kinase activity protein binding ATP binding
Cellular component	cytosol nucleoplasm nucleus cytoplasm
Biological process	regulation of transcription, DNA-templated regulation of cardiac muscle cell proliferation positive regulation of erythrocyte differentiation phosphorylation positive regulation of muscle cell differentiation transcription, DNA-templated protein phosphorylation positive regulation of gene expression negative regulation of cardiac muscle cell proliferation regulation of signal transduction by p53 class mediator stress-activated MAPK cascade cellular response to interleukin-1 regulation of gene expression intracellular signal transduction cellular response to organic substance Ras protein signal transduction vascular endothelial growth factor receptor signaling pathway regulation of DNA-binding transcription factor activity
Sources:Amigo / QuickGO

Species

Human

Mouse


5600


19094


ENSG00000185386


ENSMUSG00000053137


Q15759


Q9WUI1

RefSeq (mRNA)


NM_002751


NM_011161

RefSeq (protein)


NP_002742


NP_035291

Location (UCSC)

Chr 22: 50.26 – 50.27 Mb

Chr 15: 89.03 – 89.03 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

Mitogen-activated protein kinase 11 is an enzyme that in humans is encoded by the MAPK11 gene.^[5]^[6]

Function

The protein encoded by this gene is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation, and development. This kinase is most closely related to p38 MAP kinase, both of which can be activated by proinflammatory cytokines and environmental stress. This kinase is activated through its phosphorylation by MAP kinase kinases (MKKs), preferably by MKK6. Transcription factor ATF2/CREB2 has been shown to be a substrate of this kinase.^[6]

Interactions

MAPK11 has been shown to interact with HDAC3^[7] and Promyelocytic leukemia protein.^[8]

See also

p38 mitogen-activated protein kinases

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000185386 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000053137 – 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.
^ Goedert M, Cuenda A, Craxton M, Jakes R, Cohen P (Aug 1997). "Activation of the novel stress-activated protein kinase SAPK4 by cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison of its substrate specificity with that of other SAP kinases". EMBO J. 16 (12): 3563–71. doi:10.1093/emboj/16.12.3563. PMC 1169981. PMID 9218798.
^ ^a ^b "Entrez Gene: MAPK11 mitogen-activated protein kinase 11".
^ Mahlknecht U, Will J, Varin A, Hoelzer D, Herbein G (Sep 2004). "Histone deacetylase 3, a class I histone deacetylase, suppresses MAPK11-mediated activating transcription factor-2 activation and represses TNF gene expression". J. Immunol. 173 (6): 3979–90. doi:10.4049/jimmunol.173.6.3979. PMID 15356147.
^ Shin J, Park B, Cho S, Lee S, Kim Y, Lee SO, Cho K, Lee S, Jin BS, Ahn JH, Choi EJ, Ahn K (Sep 2004). "Promyelocytic leukemia is a direct inhibitor of SAPK2/p38 mitogen-activated protein kinase". J. Biol. Chem. 279 (39): 40994–1003. doi:10.1074/jbc.M407369200. PMID 15273249.

External links

MAP Kinase Resource Archived 2021-04-15 at the Wayback Machine.

Further reading

Jiang Y, Chen C, Li Z, Guo W, Gegner JA, Lin S, Han J (1996). "Characterization of the structure and function of a new mitogen-activated protein kinase (p38beta)". J. Biol. Chem. 271 (30): 17920–6. doi:10.1074/jbc.271.30.17920. PMID 8663524.
Kumar S, McDonnell PC, Gum RJ, Hand AT, Lee JC, Young PR (1997). "Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles". Biochem. Biophys. Res. Commun. 235 (3): 533–8. doi:10.1006/bbrc.1997.6849. PMID 9207191.
Stein B, Yang MX, Young DB, Janknecht R, Hunter T, Murray BW, Barbosa MS (1997). "p38-2, a novel mitogen-activated protein kinase with distinct properties". J. Biol. Chem. 272 (31): 19509–17. doi:10.1074/jbc.272.31.19509. PMID 9235954.
Enslen H, Raingeaud J, Davis RJ (1998). "Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6". J. Biol. Chem. 273 (3): 1741–8. doi:10.1074/jbc.273.3.1741. PMID 9430721.
New L, Jiang Y, Zhao M, Liu K, Zhu W, Flood LJ, Kato Y, Parry GC, Han J (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.
Deak M, Clifton AD, Lucocq LM, Alessi DR (1998). "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB". EMBO J. 17 (15): 4426–41. doi:10.1093/emboj/17.15.4426. PMC 1170775. PMID 9687510.
Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
Lee SH, Park J, Che Y, Han PL, Lee JK (2000). "Constitutive activity and differential localization of p38alpha and p38beta MAPKs in adult mouse brain". J. Neurosci. Res. 60 (5): 623–31. doi:10.1002/(SICI)1097-4547(20000601)60:5<623::AID-JNR7>3.0.CO;2-4. PMID 10820433. S2CID 21839143.
Tanoue T, Yamamoto T, Maeda R, Nishida E (2001). "A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs". J. Biol. Chem. 276 (28): 26629–39. doi:10.1074/jbc.M101981200. PMID 11359773.
Torcia M, De Chiara G, Nencioni L, Ammendola S, Labardi D, Lucibello M, Rosini P, Marlier LN, Bonini P, Dello Sbarba P, Palamara AT, Zambrano N, Russo T, Garaci E, Cozzolino F (2001). "Nerve growth factor inhibits apoptosis in memory B lymphocytes via inactivation of p38 MAPK, prevention of Bcl-2 phosphorylation, and cytochrome c release" (PDF). J. Biol. Chem. 276 (42): 39027–36. doi:10.1074/jbc.M102970200. PMID 11495898.
Driggers PH, Segars JH, Rubino DM (2001). "The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway". J. Biol. Chem. 276 (50): 46792–7. doi:10.1074/jbc.M106927200. PMC 4152864. PMID 11579095.
Ge B, Gram H, Di Padova F, Huang B, New L, Ulevitch RJ, Luo Y, Han J (2002). "MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha". Science. 295 (5558): 1291–4. Bibcode:2002Sci...295.1291G. doi:10.1126/science.1067289. PMID 11847341. S2CID 93896233.
Reunanen N, Li SP, Ahonen M, Foschi M, Han J, Kähäri VM (2002). "Activation of p38 alpha MAPK enhances collagenase-1 (matrix metalloproteinase (MMP)-1) and stromelysin-1 (MMP-3) expression by mRNA stabilization". J. Biol. Chem. 277 (35): 32360–8. doi:10.1074/jbc.M204296200. PMID 12060661.
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.
Kinet S, Bernard F, Mongellaz C, Perreau M, Goldman FD, Taylor N (2002). "gp120-mediated induction of the MAPK cascade is dependent on the activation state of CD4(+) lymphocytes". Blood. 100 (7): 2546–53. doi:10.1182/blood-2002-03-0819. PMID 12239168.
Lim S, Zou Y, Friedman E (2002). "The transcriptional activator Mirk/Dyrk1B is sequestered by p38alpha/beta MAP kinase". J. Biol. Chem. 277 (51): 49438–45. doi:10.1074/jbc.M206840200. PMID 12384504.
Naderi J, Hung M, Pandey S (2003). "Oxidative stress-induced apoptosis in dividing fibroblasts involves activation of p38 MAP kinase and over-expression of Bax: resistance of quiescent cells to oxidative stress". Apoptosis. 8 (1): 91–100. doi:10.1023/A:1021657220843. PMID 12510156. S2CID 19686042.
Stringaris AK, Geisenhainer J, Bergmann F, Balshüsemann C, Lee U, Zysk G, Mitchell TJ, Keller BU, Kuhnt U, Gerber J, Spreer A, Bähr M, Michel U, Nau R (2002). "Neurotoxicity of pneumolysin, a major pneumococcal virulence factor, involves calcium influx and depends on activation of p38 mitogen-activated protein kinase". Neurobiol. Dis. 11 (3): 355–68. doi:10.1006/nbdi.2002.0561. hdl:11858/00-001M-0000-0012-F282-1. PMID 12586546. S2CID 25034287.

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	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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