The major human papillomavirus protein in cervical cancers is a cytoplasmic phosphoprotein.
In a previous study, the most abundant viral transcript in a human papillomavirus type 16-associated cervical cancer and in a cancer-derived cell line was characterized, and its translation product, the E7 protein, was identified (D. Smotkin and F. O. Wettstein, Proc. Natl. Acad. Sci. USA 68:4680-4684, 1986). Here we show that the E7 protein had a half life of about 1 h and was located in the soluble cytoplasmic fraction. The protein was phosphorylated at serine residues and exhibited a high heterogeneous sedimentation rate in nondenaturing glycerol gradients, suggesting an oligomer formation or association with cellular protein.
D002460:Cell Line; D003593:Cytoplasm / Q000378:metabolism; D005260:Female; D006801:Humans; D027383:Papillomaviridae / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D010768:Phosphoserine / Q000378:metabolism; D011485:Protein Binding; D002583:Uterine Cervical Neoplasms / Q000378:metabolism* / Q000382:microbiology; D014764:Viral Proteins / Q000378:metabolism*
D010750:Phosphoproteins; D014764:Viral Proteins; D010768:Phosphoserine