Curated Information
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Curated Information Page
PubMed Id: 12524439 
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.
Kovacina KS, et al. (2003) Identification of a proline-rich Akt substrate as a 14-3-3 binding partner. J Biol Chem 278, 10189-94 12524439
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T246-p - PRAS40 (human)
Orthologous residues
PRAS40 (human): T246‑p, PRAS40 iso3 (human): T266‑p, PRAS40 (mouse): T247‑p, PRAS40 (rat): T247‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 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 activator of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
4-HT increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
14-3-3 eta (human) Induces co-immunoprecipitation


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