Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination.

@article{Kumar1999IdentificationOH,
  title={Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination.},
  author={Shailendra Kumar and Anna Talis and Peter M Howley},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 26},
  pages={18785-92}
}
The human papilloma virus E6-associated protein (E6AP) functions as a ubiquitin protein ligase (E3) in the E6-mediated ubiquitination of p53. E6AP is also an E3 in the absence of E6, but its normal cellular substrates have not yet been identified. Here we report the identification of HHR23A, one of the human homologues of the yeast DNA repair protein Rad23, as an E6-independent target of E6AP. HHR23A binds E6AP and is ubiquitinated in vitro in an E6AP-dependent manner. Ubiquitinated forms of… CONTINUE READING

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