Curated Information
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Curated Information Page
PubMed Id: 1656468 
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.
Hsieh JC, et al. (1991) Human vitamin D receptor is selectively phosphorylated by protein kinase C on serine 51, a residue crucial to its trans-activation function. Proc Natl Acad Sci U S A 88, 9315-9 1656468
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S51-p - VDR (human)
Orthologous residues
VDR (human): S51‑p, VDR (mouse): S51‑p, VDR (rat): S51‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing
 Relevant cell lines - cell types - tissues:  CV1 (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKCB (rat)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCA (human) pharmacological activator of upstream enzyme human rather than monkey sequence entered.
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester increase
Downstream Regulation
 Effect of modification (process):  transcription, induced
 Comments:  Mutation of S51 inhibited transcriptional activation by the vitamin D hormone, suggesting that phosphorylation of S51 could play a role in vitamin D dependent transcriptional activation.


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