Curated Information
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Curated Information Page
PubMed Id: 12244303 
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.
Viglietto G, et al. (2002) Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase inhibitor p27(Kip1) by PKB/Akt-mediated phosphorylation in breast cancer. Nat Med 8, 1136-44 12244303
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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, western blotting
 Disease tissue studied:  breast cancer
 Relevant cell lines - cell types - tissues:  293 (epithelial), HMEC (endothelial), IMR-90 (fibroblast), MCF-10A (breast cell), MDA-MB468 (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  human
 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) modification site within consensus motif, transfection of constitutively active enzyme, transfection of inactive enzyme, phospho-antibody, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
LY294002 decrease
PD98059 no change compared to control
U0126 no change compared to control
Akt1 (human) increase constitutively active
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  cell cycle regulation


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