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EC 2.7.11.24 Details
EC number
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)
Comment
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.
History
created 2005 (EC 2.7.1.37 part-incorporated 2005)
EC Tree
2.7.7.16 created 1961, deleted 1972, [transferred to EC 3.1.4.22, deleted 1980]
2.7.7.17 created 1965, deleted 1972, [transferred to EC 3.1.4.23, deleted 1980]
2.7.7.20 created 1965, deleted 1972
2.7.7.26 created 1961 as EC 3.1.4.8, transferred 1965 to EC 2.7.7.26, deleted 1972
2.7.7.29 created 1972, deleted 2004