Phosphorylation at the carboxy terminus of the 55-kilodalton adenovirus type 5 E1B protein regulates transforming activity.

@article{Teodoro1994PhosphorylationAT,
  title={Phosphorylation at the carboxy terminus of the 55-kilodalton adenovirus type 5 E1B protein regulates transforming activity.},
  author={Jose G Teodoro and T. Halliday and Steve G Whalen and D Takayesu and Frank L. Graham and Philip E. Branton},
  journal={Journal of virology},
  year={1994},
  volume={68 2},
  pages={776-86}
}
The 55-kDa product of early region 1B (E1B) of human adenoviruses is required for viral replication and participates in cell transformation through complex formation with and inactivation of the cellular tumor suppressor p53. We have used both biochemical and genetic approaches to show that this 496-residue (496R) protein of adenovirus type 5 is phosphorylated at serine and threonine residues near the carboxy terminus within sequences characteristic of substrates of casein kinase II. Mutations… CONTINUE READING