Curated Information
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Curated Information Page
PubMed Id: 11020388 
Yuan LW, Gambee JE (2000) Phosphorylation of p300 at serine 89 by protein kinase C. J Biol Chem 275, 40946-51 11020388
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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S89-p - p300 (human)
Orthologous residues
p300 (human): S89‑p, p300 (mouse): S89‑p, p300 (rat): S89‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mass spectrometry, mutation of modification site, peptide sequencing, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCA (human) pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
calphostin C decrease
Downstream Regulation
 Effect of modification (process):  transcription, inhibited


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