Curated Information
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Curated Information Page
PubMed Id: 12244302 
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.
Liang J, et al. (2002) PKB/Akt phosphorylates p27, impairs nuclear import of p27 and opposes p27-mediated G1 arrest. Nat Med 8, 1153-60 12244302
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T157-p - p27Kip1 (human)
Orthologous residues
p27Kip1 (human): T157‑p, p27Kip1 (mouse): A157‑p, p27Kip1 (rat): A157‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  MCF-7 (breast cell), WM239 (melanocyte), WM35 (melanocyte)
 Cellular systems studied:  cell lines
 Species studied:  human
 Comments:  Phosphorylation is minimal in G0 and rises within 4 hours of exit from quiescence.
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) inhibition of upstream enzyme, phospho-antibody
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
LY294002 decrease
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  cell cycle regulation
 Comments:  Impaires G1 inhibitory function.


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