EC 2.7.11.24 - Mitogen-activated protein kinase

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IntEnz Enzyme Nomenclature
EC 2.7.11.24

Names

Accepted name:
mitogen-activated protein kinase
Other names:
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)

Reactions

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00100 , PROSITE:PDOC01049
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004707
UniProtKB/Swiss-Prot: (203) [show] [UniProt]

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: 12721-12727 (1988). [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: 20270-20275 (1991). [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: 14373-14381 (1992). [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: 19509-19517 (1997). [PMID: 9235954]
  5. Lisnock, J., Griffin, P., Calaycay, J., Frantz, B., Parsons, J., O'Keefe, S.J. and LoGrasso, P.
    Activation of JNK3 alpha 1 requires both MKK4 and MKK7: kinetic characterization of in vitro phosphorylated JNK3α1.
    Biochemistry 39: 3141-3148 (2000). [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: 320-344 (2004). [PMID: 15187187]

[EC 2.7.11.24 created 2005 (EC 2.7.1.37 part-incorporated 2005)]