Curated Information
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Curated Information Page
PubMed Id: 8384219 
Jurutka PW, et al. (1993) Phosphorylation of serine 208 in the human vitamin D receptor. The predominant amino acid phosphorylated by casein kinase II, in vitro, and identification as a significant phosphorylation site in intact cells. J Biol Chem 268, 6791-9 8384219
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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S208-p - VDR (human)
Orthologous residues
VDR (human): S208‑p, VDR iso2 (human): S258‑p, VDR (mouse): N203‑p, VDR (rat): N204‑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) [VDR (human)]
 Cellular systems studied:  cell lines
 Species studied:  monkey
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (cow)


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