Curated Information
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Curated Information Page
PubMed Id: 11923280 
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.
Ogawara Y, et al. (2002) Akt enhances Mdm2-mediated ubiquitination and degradation of p53. J Biol Chem 277, 21843-50 11923280
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S186-p - MDM2 (human)
Orthologous residues
MDM2 (human): S186‑p, MDM2 iso12 (human): , MDM2 (mouse): S183‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody
 Relevant cell lines - cell types - tissues:  293T (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) transfection of wild-type enzyme, transfection of inactive enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
serum increase
LY294002 serum inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  activity, induced


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