The Enzyme Database

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EC 2.7.11.24     
Accepted name: mitogen-activated protein kinase
Reaction: ATP + a protein = ADP + a phosphoprotein
Other name(s): c-Jun N-terminal kinase; Dp38; ERK; ERK1; ERK2; extracellular signal-regulated kinase; JNK; JNK3α1; LeMPK3; MAP kinase; MAP-2 kinase; MAPK; MBP kinase I; MBP kinase II; microtubule-associated protein 2 kinase; microtubule-associated protein kinase; myelin basic protein kinase; p38δ; p38-2; p42 mitogen-activated protein kinase; p42mapk; PMK-1; PMK-2; PMK-3; pp42; pp44mapk; p44mpk; SAPK; STK26; stress-activated protein kinase
Systematic name: ATP:protein phosphotransferase (MAPKK-activated)
Comments: Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) is necessary for enzyme activation. Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline [6]. A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Ray, L.B. and Sturgill, T.W. Characterization of insulin-stimulated microtubule-associated protein kinase. Rapid isolation and stabilization of a novel serine/threonine kinase from 3T3-L1 cells. J. Biol. Chem. 263 (1988) 12721–12727. [PMID: 2842341]
2.  Rossomando, A.J., Sanghera, J.S., Marsden, L.A., Weber, M.J., Pelech, S.L. and Sturgill, T.W. Biochemical characterization of a family of serine/threonine protein kinases regulated by tyrosine and serine/threonine phosphorylations. J. Biol. Chem. 266 (1991) 20270–20275. [PMID: 1657919]
3.  Seger, R., Ahn, N.G., Posada, J., Munar, E.S., Jensen, A.M., Cooper, J.A., Cobb, M.H. and Krebs, E.G. Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor-stimulated A431 cells. J. Biol. Chem. 267 (1992) 14373–14381. [PMID: 1321146]
4.  Stein, B., Yang, M.X., Young, D.B., Janknecht, R., Hunter, T., Murray, B.W. and Barbosa, M.S. p38-2, a novel mitogen-activated protein kinase with distinct properties. J. Biol. Chem. 272 (1997) 19509–19517. [PMID: 9235954]
5.  Lisnock, J., Griffin, P., Calaycay, J., Frantz, B., Parsons, J., O'Keefe, S.J. and LoGrasso, P. Activation of JNK3α1 requires both MKK4 and MKK7: kinetic characterization of in vitro phosphorylated JNK3α1. Biochemistry 39 (2000) 3141–3148. [PMID: 10715136]
6.  Roux, P.P. and Blenis, J. ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions. Microbiol. Mol. Biol. Rev. 68 (2004) 320–344. [PMID: 15187187]
[EC 2.7.11.24 created 2005 (EC 2.7.1.37 part-incorporated 2005)]
 
 


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