Article
A glutamine residue in the membrane-associating domain of the bovine papillomavirus type 1 E5 oncoprotein mediates its binding to a transmembrane component of the vacuolar H(+)-ATPase.
Journal of virology - 1 Jan 1992
Goldstein D J, Kulke R, Dimaio D, Schlegel R
Abstract excerpt
The 44-amino-acid E5 oncoprotein is the major transforming protein of bovine papillomavirus type 1. It is a highly hydrophobic polypeptide which dimerizes and localizes to the Golgi apparatus and endoplasmic reticulum membranes. Recent evidence suggests that E5 modulates the phosphorylation and internalization of the epidermal growth factor and colony-stimulating factor 1 receptors and constitutively activates...
Topics
- Amino Acid Sequence
- Base Sequence
- Cell Line
- Cell Membrane
- Cell Transformation, Viral
- Chromatography, High Pressure Liquid
- Cloning, Molecular
- DNA, Viral
- Epitopes
- Glutamine