Interaction of papillomavirus E6 oncoproteins with a putative calcium-binding protein

Jason J. Chen, Carl E. Reid, Vimla Band, Elliot J. Androphy

Research output: Contribution to journalArticlepeer-review

254 Scopus citations


Human papillomaviruses (HPVs) are associated with the majority of cervical cancers and encode a transforming protein, E6, that interacts with the tumor suppressor protein p53. Because E6 has p53-independent transforming activity, the yeast two-hybrid system was used to search for other E6-binding proteins. One such protein, E6BP, interacted with cancer-associated HPV E6 and with bovine papillomavirus type 1 (BPV-1) E6. The transforming activity of BPV-1 E6 mutants correlated with their E6BP-binding ability. E6BP is identical to a putative calcium-binding protein, ERC-55, that appears to be localized in the endoplasmic reticulum.

Original languageEnglish (US)
Pages (from-to)529-531
Number of pages3
Issue number5223
StatePublished - 1995
Externally publishedYes

ASJC Scopus subject areas

  • General


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