Curated Information
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Curated Information Page
PubMed Id: 20605787 
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.
Lee SB, et al. (2010) Ribosomal protein S3, a new substrate of Akt, serves as a signal mediator between neuronal apoptosis and DNA repair. J Biol Chem 285, 29457-68 20605787
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T70-p - RPS3 (human)
Orthologous residues
RPS3 (human): T70‑p, RPS3 (mouse): T70‑p, RPS3 (rat): T70‑p
Characterization
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  adrenal cancer, pheochromocytoma
 Relevant cell lines - cell types - tissues:  PC-12 (chromaffin)
 Cellular systems studied:  cell lines
 Species studied:  rat
 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 (rat) co-immunoprecipitation, pharmacological activator of upstream enzyme, pharmacological inhibitor of upstream enzyme, modification site within consensus motif
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
NGF increase
LY294002 NGF inhibit treatment-induced increase
PD184352 NGF no effect upon treatment-induced increase
UV increase
etoposide increase
Downstream Regulation
 Effect of modification (function):  activity, induced, intracellular localization, molecular association, regulation
 Effect of modification (process):  apoptosis, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Akt1 (rat) Induces co-immunoprecipitation
E2F1 (rat) Disrupts co-immunoprecipitation
 Comments:  upregulates the endonuclease activity of RPS3


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