Curated Information
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Curated Information Page
PubMed Id: 19875456 
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.
Band AM, Björklund M, Laiho M (2009) The phosphatidylinositol 3-kinase/Akt pathway regulates transforming growth factor-{beta} signaling by destabilizing ski and inducing Smad7. J Biol Chem 284, 35441-9 19875456
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T458-p - SKI (human)
Orthologous residues
SKI (human): T458‑p, SKI (mouse): T455‑p
Characterization
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  bone cancer, breast cancer
 Relevant cell lines - cell types - tissues:  COS (fibroblast), MDA-MB435 (breast cell), U2OS (bone cell)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey
 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) co-immunoprecipitation, modification site within consensus motif, transfection of wild-type enzyme, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
LY294002 decrease
tricibine decrease
insulin, serum starvation increase
insulin, serum starvation LY294002 inhibit treatment-induced increase
serum starvation, IGF-1 increase
HGF, serum starvation increase
EGF, serum starvation no change compared to control
Downstream Regulation
 Effect of modification (function):  protein degradation
 Effect of modification (process):  transcription, altered
 Comments:  reduces the activation of TGF-beta signaling


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