Ser287
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Home > Phosphorylation Site Page: > Ser287  -  PACT (human)

Site Information
PITVCHGsGISCGNA   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 470038

In vivo Characterization
Methods used to characterize site in vivo:
2D analysis ( 4 ) , [32P] bio-synthetic labeling ( 4 ) , mutation of modification site ( 1 , 2 , 4 )
Relevant cell line - cell type - tissue:

Upstream Regulation
Treatments:
actinomycin_D ( 4 ) , oxidative_stress ( 2 )

Downstream Regulation
Effects of modification on PACT:
enzymatic activity, induced ( 2 ) , molecular association, regulation ( 1 , 2 ) , protein conformation ( 2 )
Effects of modification on biological processes:
apoptosis, altered ( 4 )
Induce interaction with:
PACT (human) ( 1 , 2 )
Inhibit interaction with:
TRBP (human) ( 1 )

References 

1

Vaughn LS, et al. (2015) Altered activation of protein kinase PKR and enhanced apoptosis in dystonia cells carrying a mutation in PKR activator protein PACT. J Biol Chem 290, 22543-57
26231208   Curated Info

2

Singh M, Patel RC (2012) Increased interaction between PACT molecules in response to stress signals is required for PKR activation. J Cell Biochem 113, 2754-64
22473766   Curated Info

3

Singh M, Castillo D, Patel CV, Patel RC (2011) Stress-Induced Phosphorylation of PACT Reduces Its Interaction with TRBP and Leads to PKR Activation. Biochemistry 50, 4550-60
21526770   Curated Info

4

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   Curated Info