Phosphorylation of p53 serine 15 increases interaction with CBP.

@article{Lambert1998PhosphorylationOP,
  title={Phosphorylation of p53 serine 15 increases interaction with CBP.},
  author={Paul F. Lambert and Fatah Kashanchi and Michael F. Radonovich and Ramin Shiekhattar and John N. Brady},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 49},
  pages={
          33048-53
        }
}
p53 exerts its cell cycle regulatory effects through its ability to function as a sequence-specific DNA binding transcription factor. CREB-binding protein (CBP)/p300, through its interaction with the N terminus of p53, acts as a coactivator for p53 and increases the sequence-specific DNA-binding activity of p53 by acetylating its C terminus. The same N-terminal domain of p53 has recently been shown to be phosphorylated at Ser15 in response to gamma-irradiation. Remarkably, we now demonstrate… CONTINUE READING
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