Curated Information

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Curated Information Page

PubMed Id: 16982699

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.

Information from this record has been curated, but not yet edited in PhosphoSitePlus^® and may be incomplete.

Héron-Milhavet L, et al. (2006) Only Akt1 is required for proliferation, while Akt2 promotes cell cycle exit through p21 binding. Mol Cell Biol 26, 8267-80 16982699

T145-p - p21Cip1 (human)

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Orthologous residues

p21Cip1 (human): T145‑p, p21Cip1 (mouse): T140‑p, p21Cip1 (dog): T113‑p

Characterization

Enzymes shown to modify site in vitro:

Type	Enzyme
KINASE	Akt1 (human)

Downstream Regulation

Effect of modification (function): molecular association, regulation

Effect of modification (process): cell cycle regulation

Modification regulates interactions with:

Interacting molecule	Interacting domains	Effect	Consequences (function)	Consequences (process)	Detection assays
Akt2 (human)		Disrupts	molecular association, regulation		in vitro, affinity chromatography

Comments: Binding of p21Cip1 to cyclin A is not dependent on T144 phosphorylation in vitro.

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