Curated Information
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Curated Information Page
PubMed Id: 19158275 
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.
Nyman U, et al. (2009) Protein kinase C-dependent phosphorylation regulates the cell cycle-inhibitory function of the p73 carboxy terminus transactivation domain. Mol Cell Biol 29, 1814-25 19158275
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S388-p - p73 (human)
Orthologous residues
p73 (human): S388‑p, p73 iso2 (human): S388‑p, p73 (mouse): S380‑p
Characterization
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, western blotting
 Disease tissue studied:  lung cancer, small-cell lung cancer
 Relevant cell lines - cell types - tissues:  H82
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCB iso2 (human) transfection of wild-type enzyme, transfection of dominant-negative enzyme, pharmacological inhibitor of upstream enzyme, siRNA inhibition of enzyme
KINASE PKCA (human) transfection of wild-type enzyme, transfection of dominant-negative enzyme, pharmacological inhibitor of upstream enzyme, siRNA inhibition of enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
siRNA decrease
PKC412 decrease
Downstream Regulation
 Effect of modification (function):  activity, induced
 Effect of modification (process):  cell cycle regulation, transcription, altered
 Comments:  regulates genes involved in cell cycle progression


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