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Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22.

Elliott, G, O'Reilly, D and O'Hare, P (1999) Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22. J Virol, 73 (7). pp. 6203-6206.

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Abstract

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.

Item Type: Article
Authors :
NameEmailORCID
Elliott, Gg.elliott@surrey.ac.ukUNSPECIFIED
O'Reilly, DUNSPECIFIEDUNSPECIFIED
O'Hare, PUNSPECIFIEDUNSPECIFIED
Date : July 1999
Uncontrolled Keywords : Animals, Binding Sites, COS Cells, Casein Kinase II, Humans, Phosphorylation, Protein-Serine-Threonine Kinases, Viral Structural Proteins
Related URLs :
Depositing User : Symplectic Elements
Date Deposited : 17 May 2017 09:54
Last Modified : 17 May 2017 14:45
URI: http://epubs.surrey.ac.uk/id/eprint/825597

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