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The herpes simplex virus protein VP22 is a major phosphoprotein of infected cells. In this study, we identify two serine phosphorylation sites within VP22 and show that the N-terminal site is a substrate for casein kinase II, while the extreme C-terminal site is a substrate for another, as yet unidentified, cellular kinase. Furthermore, we show that a mutant of VP22 which has both sites altered is unable to incorporate phosphate in vivo, confirming that there are no other phosphorylation sites within VP22.

Type

Journal article

Journal

J Virol

Publication Date

07/1999

Volume

73

Pages

6203 - 6206

Keywords

Animals, Binding Sites, COS Cells, Casein Kinase II, Humans, Phosphorylation, Protein-Serine-Threonine Kinases, Viral Structural Proteins