InterPro domain: IPR038168

The transcription factor DP (dimerization partner) forms a heterodimer with E2F and regulates genes involved in cell cycle progression. The transcriptional activity of E2F is inhibited by the retinoblastoma protein which binds to the E2F-DP heterodimer [ 1 ] and negatively regulates the G1-S transition.

Though originally the role of DP in transcriptional activation was thought to be facilitating the binding of E2F to target DNA, it was latter shown that the C-terminal acidic region of DP1 binds strongly to the PH domain of p62 of TFIIH and acts as a transactivation domain [ 2 ].

1. Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. Cell 123, 1093-106
2. The Interaction Mode of the Acidic Region of the Cell Cycle Transcription Factor DP1 with TFIIH. J. Mol. Biol. 428, 4993-5006