MAPK11

Protein-coding gene in the species Homo sapiens
MAPK11
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3GC8, 3GC9, 3GP0

Identifiers
AliasesMAPK11, P38B, P38BETA2, PRKM11, SAPK2, SAPK2B, p38-2, p38Beta, mitogen-activated protein kinase 11
External IDsOMIM: 602898; MGI: 1338024; HomoloGene: 55684; GeneCards: MAPK11; OMA:MAPK11 - orthologs
Gene location (Human)
Chromosome 22 (human)
Chr.Chromosome 22 (human)[1]
Chromosome 22 (human)
Genomic location for MAPK11
Genomic location for MAPK11
Band22q13.33Start50,263,713 bp[1]
End50,270,767 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for MAPK11
Genomic location for MAPK11
Band15|15 E3Start89,026,689 bp[2]
End89,033,831 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Brodmann area 9

  • middle temporal gyrus

  • cingulate gyrus

  • caudate nucleus

  • Brodmann area 23

  • putamen

  • nucleus accumbens

  • anterior pituitary

  • amygdala

  • ganglionic eminence
Top expressed in
  • visual cortex

  • superior frontal gyrus

  • superior cervical ganglion

  • ganglionic eminence

  • primary motor cortex

  • cerebellar cortex

  • blood

  • facial motor nucleus

  • prefrontal cortex

  • conjunctival fornix
More reference expression data
BioGPS




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
Orthologs
SpeciesHumanMouse
Entrez

5600

19094

Ensembl

ENSG00000185386

ENSMUSG00000053137

UniProt

Q15759

Q9WUI1

RefSeq (mRNA)

NM_002751

NM_011161

RefSeq (protein)

NP_002742

NP_035291

Location (UCSC)Chr 22: 50.26 – 50.27 MbChr 15: 89.03 – 89.03 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000185386 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000053137 – 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. ^ 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.
  6. ^ a b "Entrez Gene: MAPK11 mitogen-activated protein kinase 11".
  7. ^ 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.
  8. ^ 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

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.
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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)
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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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