Curated Information
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Curated Information Page
PubMed Id: 9891036 
Chen D, Pace PE, Coombes RC, Ali S (1999) Phosphorylation of human estrogen receptor alpha by protein kinase A regulates dimerization. Mol Cell Biol 19, 1002-15 9891036
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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S236-p - ER-alpha (human)
Orthologous residues
ER‑alpha (human): S236‑p, ER‑alpha (mouse): S240‑p, ER‑alpha (rat): S241‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKACA (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) transfection of wild-type enzyme, pharmacological activator of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
cAMP analog increase
Downstream Regulation
 Effect of modification (process):  transcription, inhibited


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