Article
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.
The Journal of biological chemistry - 25 Mar 1993
Jurutka P W, Hsieh J C, MacDonald P N, Terpening C M, Haussler C A, Haussler M R, Whitfield G K
Abstract excerpt
The human 1,25-dihydroxyvitamin D3 receptor (hVDR), like other members of the steroid/thyroid receptor superfamily, has been observed to undergo rapid phosphorylation. We report here that the hVDR is a substrate for casein kinase II (CK-II), a regulatory enzyme of significance in the function of...
Topics
- Amino Acid Sequence
- Animals
- Calcitriol
- Casein Kinase II
- Cell Line
- Chlorocebus aethiops
- Humans
- Molecular Sequence Data
- Moths
- Mutation
- Phosphorylation
- Precipitin Tests
- Protein Serine-Threonine Kinases
- Receptors, Calcitriol