Supplementary Figure 4: Multiple sequence alignment of p300 and CBP orthologs.
From: Structure of the p300 catalytic core and implications for chromatin targeting and HAT regulation
Human (hp300), mouse (mp300), bovine (bp300) and dog (cp300). Also included are the CBP homologs human (hCBP), mouse (mCBP), rat (rCBP), Drosophila melanogaster (dCBP) and Caenorhabditis elegans (cCBP). Identical residues are shown with a red background and similar residues with red letters. Secondary structure elements of p300 are shown above the amino acid sequences. The Bromodomain (BROMO) is highlighted in yellow, the RING domain in green, the PHD domain in red and the HAT domain in blue. Intramolecular contacts between domains: Residues in the BROMO–PHD interface (•). Residues in the RING–HAT interface (Δ). Residues in the PHD–HAT interface (*). The sequence alignment was performed using ClustalW1 and the figure generated using ESPript2.
