Curated Information

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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

T286-p - MEK1 (mouse)

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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 wild-type enzyme, pharmacological activator of upstream enzyme, genetic transfer of dominant-negative enzyme, genetic knockout/knockin of upstream enzyme

Downstream Regulation

Effect of modification (function): enzymatic activity, inhibited

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