Curated Information
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Curated Information Page
PubMed Id: 11684694 
This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Sharma P, et al. (2002) Phosphorylation of MEK1 by cdk5/p35 down-regulates the mitogen-activated protein kinase pathway. J Biol Chem 277, 528-34 11684694
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T286-p - MEK1 (mouse)
Orthologous residues
MEK1 (human): T286‑p, MEK1 (mouse): T286‑p, MEK1 (rat): T286‑p, MEK1 (rabbit): T286‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CDK5 (mouse)
 Comments:  Inactive MEK1 was not phosphorylated by CDK5/p25, but Raf-phosphorylated MEK1 was good substrate of CDK5/p25.
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CDK5 (mouse) genetic transfer of dominant-negative enzyme, pharmacological activator of upstream enzyme, genetic knockout/knockin of upstream enzyme, genetic transfer of wild-type enzyme
Downstream Regulation
 Effect of modification (function):  enzymatic activity, inhibited


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