Curated Information
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Curated Information Page
PubMed Id: 18356162 
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.
Lopez-Pajares V, Kim MM, Yuan ZM (2008) Phosphorylation of MDMX mediated by Akt leads to stabilization and induces 14-3-3 binding. J Biol Chem 283, 13707-13 18356162
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S367-p - MDM4 (human)
Orthologous residues
MDM4 (human): S367‑p, MDM4 iso5 (human): S317‑p, MDM4 (mouse): S367‑p, MDM4 (rat): S368‑p
Characterization
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, 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 constitutively active enzyme, transfection of dominant-negative enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
adriamycin, MG132 increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation, protein stabilization
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
14-3-3 beta (human) Induces pull-down assay
14-3-3 zeta (human) Induces pull-down assay
 Comments:  downregulates activity of p53


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