Curated Information
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Curated Information Page
PubMed Id: 14645242 
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.
Dan HC, et al. (2004) Akt phosphorylation and stabilization of X-linked inhibitor of apoptosis protein (XIAP). J Biol Chem 279, 5405-12 14645242
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S87-p - XIAP (human)
Orthologous residues
XIAP (human): S87‑p, XIAP (mouse): S87‑p, XIAP (rat): S87‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  ovarian cancer
 Relevant cell lines - cell types - tissues:  293 (epithelial), A2780 (ovarian), COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt2 (human)
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt2 (human) transfection of constitutively active enzyme, co-immunoprecipitation, phospho-motif antibody, pharmacological activator of upstream enzyme, modification site within consensus motif, pharmacological inhibitor of upstream enzyme
KINASE Akt1 (human) transfection of constitutively active enzyme, co-immunoprecipitation, phospho-motif antibody, pharmacological activator of upstream enzyme, modification site within consensus motif, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
insulin increase
LY294002 insulin inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  protein stabilization
 Effect of modification (process):  apoptosis, inhibited


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