Curated Information
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Curated Information Page
PubMed Id: 19526459 
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.
Chou CK, et al. (2009) The suppression of MAD1 by AKT-mediated phosphorylation activates MAD1 target genes transcription. Mol Carcinog 48, 1048-58 19526459
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S145-p - Mad1 (human)
Orthologous residues
Mad1 (human): S145‑p, Mad1 (mouse): S144‑p
Characterization
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 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) transfection of constitutively active enzyme, transfection of dominant-negative enzyme
KINASE p70S6K (human) pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
rapamycin decrease
PD98059 rapamycin no effect upon treatment-induced decrease
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Effect of modification (process):  cell cycle regulation, transcription, induced
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
DNA Induces pull-down assay, co-immunoprecipitation
 Comments:  inhibits MAD1-mediated transcription repression


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