Article
Negative charge at the casein kinase II phosphorylation site is important for transformation but not for Rb protein binding by the E7 protein of human papillomavirus type 16.
Proceedings of the National Academy of Sciences of the United States of America - 15 Jun 1991
Firzlaff J M, Lüscher B, Eisenman R N
Abstract excerpt
The human papillomavirus E7 protein is phosphorylated at the two serines in positions 31/32, which are part of a consensus sequence for casein kinase II (CKII). In this study, we have investigated the effect of CKII phosphorylation site mutations, all of which lead to unphosphorylated E7 proteins. The replacement of the two serines by uncharged alanine residues drastically reduced the ability of E7 to cotransform...
Topics
- Adenoviridae
- Amino Acid Sequence
- Base Sequence
- Binding Sites
- Casein Kinases
- Genes, Viral
- Humans
- Molecular Sequence Data
- Mutation
- Oncogene Proteins, Viral