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Catalysis of the phosphorylation of tyrosine and threonine residues in a c-Jun NH2-terminal kinase (JNK), a member of a subgroup of mitogen-activated protein kinases (MAPKs), which signal in response to cytokines and exposure to environmental stress. JUN kinase kinase (JNKK) is a dual-specificity protein kinase kinase and requires activation by a serine/threonine kinase JUN kinase kinase kinase. Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. Catalysis of the reaction: ATP + a protein serine/threonine/tyrosine = ADP + protein serine/threonine/tyrosine phosphate. Catalysis of the concomitant phosphorylation of threonine (T) and tyrosine (Y) residues in a Thr-Glu-Tyr (TEY) thiolester sequence in MAP kinases. It is a dual-specificity mitogen-activated protein kinase kinase and requires activation by the serine/threonine kinase, MAP kinase kinase kinase.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: MAP kinase kinase activity
Acc: GO:0004708
Aspect: Molecular Function
Desc: Catalysis of the concomitant phosphorylation of threonine (T) and tyrosine (Y) residues in a Thr-Glu-Tyr (TEY) thiolester sequence in MAP kinases. It is a dual-specificity mitogen-activated protein kinase kinase and requires activation by the serine/threonine kinase, MAP kinase kinase kinase.
Synonyms:
  • ATP:protein phosphotransferase (MAPKKK-activated) activity
  • mitogen-activated protein kinase kinase activity
  • MKK2
  • MKK4
  • MAPKK
  • MAPKK1
  • MEK activity
  • MKK
  • MKK6
  • MAP2K
  • MKK7
  • MAPKK activity
  • MAP kinase kinase 4 activity
  • MAP kinase kinase 7 activity
  • STK27
  • MEK1
  • ERK activator kinase activity
  • MAP kinase or ERK kinase activity
  • MEK2
Proteins in PDR annotated with:
   This term: 41 [Search]
   Term or descendants: 42 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0004708 - MAP kinase kinase activity (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle