Curated Information
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Curated Information Page
PubMed Id: 11231573 
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.
Zhou BP, et al. (2001) Cytoplasmic localization of p21Cip1/WAF1 by Akt-induced phosphorylation in HER-2/neu-overexpressing cells. Nat Cell Biol 3, 245-52 11231573
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T145-p - p21Cip1 (human)
Orthologous residues
p21Cip1 (human): T145‑p, p21Cip1 (mouse): T140‑p, p21Cip1 (dog): T113‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phospho-antibody
 Relevant cell lines - cell types - tissues:  293T (epithelial), 3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], MDA-MB453 (breast cell), MEF (fibroblast) [IGF1R (mouse)]
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) genetic transfer of dominant-negative enzyme, pharmacological inhibitor of upstream enzyme, pharmacological activator of upstream enzyme, co-immunoprecipitation, genetic transfer of constitutively active upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
insulin increase
LY294002 decrease
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  Phosphorylation at T145 of p21Cip1 results in cytoplasmic localization of this protein and regulates its growth-inhibiting activity


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