Curated Information
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Home > Curated Information Page > PubMed Id: 16982605
Peters GA, Li S, Sen GC (2006) Phosphorylation of specific serine residues in the PKR activation domain of PACT is essential for its ability to mediate apoptosis. J Biol Chem 281, 35129-36 16982605
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S246-p - PACT (human)
Modsite: TDyIQLLsEIAKEQG SwissProt Entrez-Gene
Orthologous residues
PACT (human): S246‑p, PACT (mouse): S246‑p, PACT (rat): S246‑p
Characterization
Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, mutation of modification site
Relevant cell lines - cell types - tissues:  HT1080 (fibroblast)
Cellular systems studied:  cell lines
Species studied:  human
Comments:  constitutive, required for S287 phosphorylation
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
actinomycin_D increase
Downstream Regulation
Effect of modification (process):  apoptosis, altered
Comments:  activates PKR

S287-p - PACT (human)
Modsite: PITVCHGsGISCGNA SwissProt Entrez-Gene
Orthologous residues
PACT (human): S287‑p, PACT (mouse): S287‑p, PACT (rat): S287‑p
Characterization
Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, mutation of modification site
Relevant cell lines - cell types - tissues:  HT1080 (fibroblast)
Cellular systems studied:  cell lines
Species studied:  human
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
actinomycin_D increase
Downstream Regulation
Effect of modification (process):  apoptosis, altered
Comments:  activates PKR