MAPK7
From Wikipedia, the free encyclopedia
Mitogen-activated protein kinase 7
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Identifiers | |||||||||||
Symbol(s) | MAPK7; BMK1; ERK4; ERK5; PRKM7 | ||||||||||
External IDs | OMIM: 602521 MGI: 1346347 HomoloGene: 2060 | ||||||||||
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RNA expression pattern | |||||||||||
Orthologs | |||||||||||
Human | Mouse | ||||||||||
Entrez | 5598 | 23939 | |||||||||
Ensembl | ENSG00000166484 | ENSMUSG00000001034 | |||||||||
Uniprot | Q13164 | Q3U2N7 | |||||||||
Refseq | NM_002749 (mRNA) NP_002740 (protein) |
NM_011841 (mRNA) NP_035971 (protein) |
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Location | Chr 17: 19.22 - 19.23 Mb | Chr 11: 61.31 - 61.31 Mb | |||||||||
Pubmed search | [1] | [2] |
Mitogen-activated protein kinase 7, also known as MAPK7, is a human gene.
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 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 type kinases, and G protein-coupled receptors. In response to extracellular signals, this kinase translocates to 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.[1]
[edit] References
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- Zhou G, Bao ZQ, Dixon JE (1995). "Components of a new human protein kinase signal transduction pathway.". J. Biol. Chem. 270 (21): 12665–9. PMID 7759517.
- Warn-Cramer BJ, Lampe PD, Kurata WE, et al. (1996). "Characterization of the mitogen-activated protein kinase phosphorylation sites on the connexin-43 gap junction protein.". J. Biol. Chem. 271 (7): 3779–86. PMID 8631994.
- Kato Y, Kravchenko VV, Tapping RI, et al. (1998). "BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C.". EMBO J. 16 (23): 7054–66. doi: . 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. 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. 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. PMID 9535909.
- Yang CC, Ornatsky OI, McDermott JC, et al. (1998). "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1.". Nucleic Acids Res. 26 (20): 4771–7. PMID 9753748.
- Kato Y, Tapping RI, Huang S, et al. (1998). "Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor.". Nature 395 (6703): 713–6. doi: . PMID 9790194.
- Zhao M, New L, Kravchenko VV, et al. (1999). "Regulation of the MEF2 family of transcription factors by p38.". Mol. Cell. Biol. 19 (1): 21–30. PMID 9858528.
- Purandare SM, Lee JD, Patel PI (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. PMID 10072598.
- 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. PMID 10473620.
- English JM, Pearson G, Hockenberry T, et al. (1999). "Contribution of the ERK5/MEK5 pathway to Ras/Raf signaling and growth control.". J. Biol. Chem. 274 (44): 31588–92. 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: . PMID 10781600.
- Kato Y, Zhao M, Morikawa A, et al. (2000). "Big mitogen-activated kinase regulates multiple members of the MEF2 protein family.". J. Biol. Chem. 275 (24): 18534–40. doi: . PMID 10849446.
- Yan C, Luo H, Lee JD, et al. (2001). "Molecular cloning of mouse ERK5/BMK1 splice variants and characterization of ERK5 functional domains.". J. Biol. Chem. 276 (14): 10870–8. doi: . PMID 11139578.
- Hayashi M, Tapping RI, Chao TH, et al. (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: . 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: . PMID 11278431.
- Watson FL, Heerssen HM, Bhattacharyya A, et al. (2001). "Neurotrophins use the Erk5 pathway to mediate a retrograde survival response.". Nat. Neurosci. 4 (10): 981–8. doi: . PMID 11544482.
- Esparís-Ogando A, Díaz-Rodríguez E, Montero JC, et al. (2002). "Erk5 participates in neuregulin signal transduction and is constitutively active in breast cancer cells overexpressing ErbB2.". Mol. Cell. Biol. 22 (1): 270–85. PMID 11739740.