MAPK7

Mitogen-activated protein kinase 7 also known as MAP kinase 7 is an enzyme that in humans is encoded by the MAPK7 gene.[5][6]

Main article: Mitogen-activated protein kinase

MAPK7
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2Q8Y, 4B99, 4IC7, 4IC8, 4ZSJ, 4ZSL, 5BYZ, 5BYY, 4ZSG
Identifiers
Aliases	MAPK7, BMK1, ERK4, ERK5, PRKM7, mitogen-activated protein kinase 7
External IDs	OMIM: 602521 MGI: 1346347 HomoloGene: 2060 GeneCards: MAPK7
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17p11.2 Start 19,377,721 bp[1] End 19,383,544 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 B2 Start 61,488,812 bp[2] End 61,494,406 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • nucleotide binding • protein kinase activity • mitogen-activated protein kinase binding • kinase activity • GO:0001948 protein binding • ATP binding • protein serine/threonine kinase activity • MAP kinase activity Cellular component • cytoplasm • cytosol • PML body • nucleoplasm • cell nucleus Biological process • cellular response to transforming growth factor beta stimulus • negative regulation of endothelial cell apoptotic process • cell differentiation • phosphorylation • negative regulation of ERK5 cascade • cellular response to laminar fluid shear stress • positive regulation of transcription from RNA polymerase II promoter in response to stress • cellular response to growth factor stimulus • negative regulation of apoptotic process • regulation of angiogenesis • negative regulation of response to cytokine stimulus • positive regulation of protein metabolic process • protein phosphorylation • negative regulation of MAP kinase activity • peptidyl-serine phosphorylation • cell cycle • negative regulation of cyclic-nucleotide phosphodiesterase activity • negative regulation of heterotypic cell-cell adhesion • negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand • negative regulation of inflammatory response • cAMP-mediated signaling • signal transduction • positive regulation of transcription from RNA polymerase II promoter • cellular response to hydrogen peroxide • MAPK cascade • axon guidance • negative regulation of calcineurin-NFAT signaling cascade • regulation of gene expression • GO:0007243 intracellular signal transduction • cellular response to organic substance Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5598	23939
Ensembl	ENSG00000166484	ENSMUSG00000001034
UniProt	Q13164	Q9WVS8
RefSeq (mRNA)	NM_002749 NM_139032 NM_139033 NM_139034	NM_001291033 NM_001291034 NM_001291035 NM_001291036 NM_001291037 NM_011841 NM_001361989
RefSeq (protein)	NP_002740 NP_620601 NP_620602 NP_620603	NP_001277962 NP_001277963 NP_001277964 NP_001277965 NP_001277966 NP_035971 NP_001348918
Location (UCSC)	Chr 17: 19.38 – 19.38 Mb	Chr 11: 61.49 – 61.49 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

MAPK7 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 specifically activated by mitogen-activated protein kinase kinase 5 (MAP2K5/MEK5). It is involved in the downstream signaling processes of various receptor molecules including receptor tyrosine kinases, and G protein-coupled receptors. In response to extracellular signals, this kinase translocates to the cell nucleus, where it regulates gene expression by phosphorylating, and activating different transcription factors. Four alternatively spliced transcript variants of this gene encoding two distinct isoforms have been reported.[7]

MAPK7 is also critical for cardiovascular development [8] and is essential for endothelial cell function.[9][10]

Interactions

MAPK7 has been shown to interact with:

• C-Raf,[11]
• Gap junction protein, alpha 1[12]
• MAP2K5,[6]
• MEF2C,[13]
• MEF2D,[13]
• PTPRR,[14]
• SGK,[15] and
• YWHAB.[16]

References

1. GRCh38: Ensembl release 89: ENSG00000166484 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000001034 - 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. Purandare SM, Lee JD, Patel PI (March 1999). "Assignment of big MAP kinase (PRKM7) to human chromosome 17 band p11.2 with somatic cell hybrids". Cytogenet. Cell Genet. 83 (3–4): 258–9. doi:10.1159/000015199. PMID 10072598.
6. Zhou G, Bao ZQ, Dixon JE (Jun 1995). "Components of a new human protein kinase signal transduction pathway". J. Biol. Chem. 270 (21): 12665–9. doi:10.1074/jbc.270.21.12665. PMID 7759517.
7. "Entrez Gene: MAPK7 mitogen-activated protein kinase 7".
8. Hayashi M, Lee JD (Oct 2004). "Role of the BMK1/ERK5 signaling pathway: lessons from knockout mice". J. Mol. Med. 82 (12): 800–8. doi:10.1007/s00109-004-0602-8. PMID 15517128.
9. Roberts OL, Holmes K, Müller J, Cross DA, Cross MJ (Dec 2009). "ERK5 and the regulation of endothelial cell function". Biochem. Soc. Trans. 37 (Pt 6): 1254–9. doi:10.1042/BST0371254. PMID 19909257.
10. Roberts OL, Holmes K, Müller J, Cross DA, Cross MJ (Sep 2010). "ERK5 is required for VEGF-mediated survival and tubular morphogenesis of primary human microvascular endothelial cells". J. Cell Sci. 123 (Pt 18): 3189–200. doi:10.1242/jcs.072801. PMID 20736307.
11. English JM, Pearson G, Hockenberry T, Shivakumar L, White MA, Cobb MH (Oct 1999). "Contribution of the ERK5/MEK5 pathway to Ras/Raf signaling and growth control". J. Biol. Chem. 274 (44): 31588–92. doi:10.1074/jbc.274.44.31588. PMID 10531364.
12. Cameron SJ, Malik S, Akaike M, Lerner-Marmarosh N, Yan C, Lee JD, Abe J, Yang J (May 2003). "Regulation of epidermal growth factor-induced connexin 43 gap junction communication by big mitogen-activated protein kinase1/ERK5 but not ERK1/2 kinase activation". J. Biol. Chem. 278 (20): 18682–8. doi:10.1074/jbc.M213283200. PMID 12637502.
13. Yang CC, Ornatsky OI, McDermott JC, Cruz TF, Prody CA (Oct 1998). "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1". Nucleic Acids Res. 26 (20): 4771–7. doi:10.1093/nar/26.20.4771. PMC 147902. PMID 9753748.
14. Buschbeck M, Eickhoff J, Sommer MN, Ullrich A (Aug 2002). "Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway". J. Biol. Chem. 277 (33): 29503–9. doi:10.1074/jbc.M202149200. PMID 12042304.
15. Hayashi M, Tapping RI, Chao TH, Lo JF, King CC, Yang Y, Lee JD (Mar 2001). "BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase". J. Biol. Chem. 276 (12): 8631–4. doi:10.1074/jbc.C000838200. PMID 11254654.
16. Zheng Q, Yin G, Yan C, Cavet M, Berk BC (Mar 2004). "14-3-3beta binds to big mitogen-activated protein kinase 1 (BMK1/ERK5) and regulates BMK1 function". J. Biol. Chem. 279 (10): 8787–91. doi:10.1074/jbc.M310212200. PMID 14679215.

Further reading

• Lee JD, Ulevitch RJ, Han J (1995). "Primary structure of BMK1: a new mammalian map kinase". Biochem. Biophys. Res. Commun. 213 (2): 715–24. doi:10.1006/bbrc.1995.2189. PMID 7646528.
• Warn-Cramer BJ, Lampe PD, Kurata WE, Kanemitsu MY, Loo LW, Eckhart W, Lau AF (1996). "Characterization of the mitogen-activated protein kinase phosphorylation sites on the connexin-43 gap junction protein". J. Biol. Chem. 271 (7): 3779–86. doi:10.1074/jbc.271.7.3779. PMID 8631994.
• Kato Y, Kravchenko VV, Tapping RI, Han J, Ulevitch RJ, Lee JD (1997). "BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C". EMBO J. 16 (23): 7054–66. doi:10.1093/emboj/16.23.7054. PMC 1170308. PMID 9384584.
• English JM, Pearson G, Baer R, Cobb MH (1998). "Identification of substrates and regulators of the mitogen-activated protein kinase ERK5 using chimeric protein kinases". J. Biol. Chem. 273 (7): 3854–60. doi:10.1074/jbc.273.7.3854. PMID 9461566.
• Grunwald ME, Yu WP, Yu HH, Yau KW (1998). "Identification of a domain on the beta-subunit of the rod cGMP-gated cation channel that mediates inhibition by calcium-calmodulin". J. Biol. Chem. 273 (15): 9148–57. doi:10.1074/jbc.273.15.9148. PMID 9535905.
• Warn-Cramer BJ, Cottrell GT, Burt JM, Lau AF (1998). "Regulation of connexin-43 gap junctional intercellular communication by mitogen-activated protein kinase". J. Biol. Chem. 273 (15): 9188–96. doi:10.1074/jbc.273.15.9188. PMID 9535909.
• Yang CC, Ornatsky OI, McDermott JC, Cruz TF, Prody CA (1998). "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1". Nucleic Acids Res. 26 (20): 4771–7. doi:10.1093/nar/26.20.4771. PMC 147902. PMID 9753748.
• Kato Y, Tapping RI, Huang S, Watson MH, Ulevitch RJ, Lee JD (1998). "Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor". Nature. 395 (6703): 713–6. doi:10.1038/27234. PMID 9790194.
• Zhao M, New L, Kravchenko VV, Kato Y, Gram H, di Padova F, Olson EN, Ulevitch RJ, Han J (1999). "Regulation of the MEF2 family of transcription factors by p38". Mol. Cell. Biol. 19 (1): 21–30. doi:10.1128/mcb.19.1.21. PMC 83862. PMID 9858528.
• Kamakura S, Moriguchi T, Nishida E (1999). "Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus". J. Biol. Chem. 274 (37): 26563–71. doi:10.1074/jbc.274.37.26563. PMID 10473620.
• English JM, Pearson G, Hockenberry T, Shivakumar L, White MA, Cobb MH (1999). "Contribution of the ERK5/MEK5 pathway to Ras/Raf signaling and growth control". J. Biol. Chem. 274 (44): 31588–92. doi:10.1074/jbc.274.44.31588. PMID 10531364.
• Fukuhara S, Marinissen MJ, Chiariello M, Gutkind JS (2000). "Signaling from G protein-coupled receptors to ERK5/Big MAPK 1 involves Galpha q and Galpha 12/13 families of heterotrimeric G proteins. Evidence for the existence of a novel Ras AND Rho-independent pathway". J. Biol. Chem. 275 (28): 21730–6. doi:10.1074/jbc.M002410200. PMID 10781600.
• Kato Y, Zhao M, Morikawa A, Sugiyama T, Chakravortty D, Koide N, Yoshida T, Tapping RI, Yang Y, Yokochi T, Lee JD (2000). "Big mitogen-activated kinase regulates multiple members of the MEF2 protein family". J. Biol. Chem. 275 (24): 18534–40. doi:10.1074/jbc.M001573200. PMID 10849446.
• Yan C, Luo H, Lee JD, Abe J, Berk BC (2001). "Molecular cloning of mouse ERK5/BMK1 splice variants and characterization of ERK5 functional domains". J. Biol. Chem. 276 (14): 10870–8. doi:10.1074/jbc.M009286200. PMID 11139578.
• Hayashi M, Tapping RI, Chao TH, Lo JF, King CC, Yang Y, Lee JD (2001). "BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase". J. Biol. Chem. 276 (12): 8631–4. doi:10.1074/jbc.C000838200. PMID 11254654.
• Dong F, Gutkind JS, Larner AC (2001). "Granulocyte colony-stimulating factor induces ERK5 activation, which is differentially regulated by protein-tyrosine kinases and protein kinase C. Regulation of cell proliferation and survival". J. Biol. Chem. 276 (14): 10811–6. doi:10.1074/jbc.M008748200. PMID 11278431.
• Watson FL, Heerssen HM, Bhattacharyya A, Klesse L, Lin MZ, Segal RA (2001). "Neurotrophins use the Erk5 pathway to mediate a retrograde survival response". Nat. Neurosci. 4 (10): 981–8. doi:10.1038/nn720. PMID 11544482.
• Esparís-Ogando A, Díaz-Rodríguez E, Montero JC, Yuste L, Crespo P, Pandiella A (2002). "Erk5 participates in neuregulin signal transduction and is constitutively active in breast cancer cells overexpressing ErbB2". Mol. Cell. Biol. 22 (1): 270–85. doi:10.1128/MCB.22.1.270-285.2002. PMC 134212. PMID 11739740.

External links

• MAP Kinase Resource .