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
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T145-p - p21Cip1 (human)
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 affinity chromatography, in vitro
 Comments:  Binding of p21Cip1 to cyclin A is not dependent on T144 phosphorylation in vitro.


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