MAPK7

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Mitogen-activated protein kinase 7
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols MAPK7 ; BMK1; ERK4; ERK5; PRKM7
External IDs OMIM602521 MGI1346347 HomoloGene2060 ChEMBL: 5332 GeneCards: MAPK7 Gene
EC number 2.7.11.24
RNA expression pattern
PBB GE MAPK7 35617 at tn.png
PBB GE MAPK7 207292 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5598 23939
Ensembl ENSG00000166484 ENSMUSG00000001034
UniProt Q13164 Q9WVS8
RefSeq (mRNA) NM_002749 NM_011841
RefSeq (protein) NP_002740 NP_035971
Location (UCSC) Chr 17:
19.28 – 19.29 Mb
Chr 11:
61.49 – 61.49 Mb
PubMed search [1] [2]

Mitogen-activated protein kinase 7 also known as MAP kinase 7 is an enzyme that in humans is encoded by the MAPK7 gene.[1][2]

Function[edit]

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.[3]

MAPK7 is also critical for cardiovascular development [4] and is essential for endothelial cell function.[5][6]

Interactions[edit]

MAPK7 has been shown to interact with SGK,[7] MEF2C,[8] YWHAB,[9] MEF2D,[8] C-Raf,[10] PTPRR,[11] Gap junction protein, alpha 1[12] and MAP2K5.[2]

References[edit]

  1. ^ Purandare SM, Lee JD, Patel PI (Mar 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. 
  2. ^ a b 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. 
  3. ^ "Entrez Gene: MAPK7 mitogen-activated protein kinase 7". 
  4. ^ 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. 
  5. ^ Roberts OL, Holmes K, Müller J, Cross DA, Cross MJ. (Dec 2009). "ERK5 and the regulation of endothelial cell function". Biochem Soc Trans. 37 (6): 1254–9. doi:10.1042/BST0371254. PMID 19909257. 
  6. ^ 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 (18): 3189–3200. doi:10.1242/jcs.072801. PMID 20736307. 
  7. ^ Hayashi, M; Tapping R I, Chao T H, Lo J F, King C C, Yang Y, Lee J D (Mar 2001). "BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase". J. Biol. Chem. (United States) 276 (12): 8631–4. doi:10.1074/jbc.C000838200. ISSN 0021-9258. PMID 11254654. 
  8. ^ a b Yang, C C; Ornatsky O I, McDermott J C, Cruz T F, Prody C A (Oct 1998). "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1". Nucleic Acids Res. (ENGLAND) 26 (20): 4771–7. doi:10.1093/nar/26.20.4771. ISSN 0305-1048. PMC 147902. PMID 9753748. 
  9. ^ Zheng, Qinlei; Yin Guoyong, Yan Chen, Cavet Megan, Berk Bradford C (Mar 2004). "14-3-3beta binds to big mitogen-activated protein kinase 1 (BMK1/ERK5) and regulates BMK1 function". J. Biol. Chem. (United States) 279 (10): 8787–91. doi:10.1074/jbc.M310212200. ISSN 0021-9258. PMID 14679215. 
  10. ^ English, J M; Pearson G, Hockenberry T, Shivakumar L, White M A, Cobb M H (Oct 1999). "Contribution of the ERK5/MEK5 pathway to Ras/Raf signaling and growth control". J. Biol. Chem. (UNITED STATES) 274 (44): 31588–92. doi:10.1074/jbc.274.44.31588. ISSN 0021-9258. PMID 10531364. 
  11. ^ Buschbeck, Marcus; Eickhoff Jan, Sommer Marc N, Ullrich Axel (Aug 2002). "Phosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathway". J. Biol. Chem. (United States) 277 (33): 29503–9. doi:10.1074/jbc.M202149200. ISSN 0021-9258. PMID 12042304. 
  12. ^ Cameron, Scott J; Malik Sundeep, Akaike Masashi, Lerner-Marmarosh Nicole, Yan Chen, Lee Jiing-Dwan, Abe Jun-Ichi, Yang Jay (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. (United States) 278 (20): 18682–8. doi:10.1074/jbc.M213283200. ISSN 0021-9258. PMID 12637502. 

External links[edit]

Further reading[edit]