Curated Information
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Home > Curated Information Page > PubMed Id: 11463845
Rössig L, et al. (2001) Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding and proliferation of endothelial cells. Mol Cell Biol 21, 5644-57 11463845
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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T145-p - p21Cip1 (human)
Modsite: QGRkRRQtsMTDFyH SwissProt Entrez-Gene
Orthologous residues
p21Cip1 (human): T145‑p, p21Cip1 (mouse): T140‑p, p21Cip1 (dog): T113‑p
Characterization
Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phosphopeptide mapping
Relevant cell lines - cell types - tissues:  HUVEC (endothelial)
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) pharmacological inhibitor of upstream enzyme, phosphopeptide analysis, transfection of wild-type enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
LY294002 decrease
serum increase
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
CDK2 (human) Disrupts co-immunoprecipitation
PCNA (human) Disrupts co-immunoprecipitation
CDK4 (human) Disrupts co-immunoprecipitation