p300-CBP coactivator family

The p300-CBP coactivator family in humans is composed of two closely related transcriptional co-activating proteins (or coactivators):

  1. p300 (also called EP300 or E1A binding protein p300)
  2. CBP (also known as CREB-binding protein or CREBBP)

Both p300 and CBP interact with numerous transcription factors and act to increase the expression of their target genes.

Protein structure

p300 and CBP have similar structures. Both contain five protein interaction domains: the nuclear receptor interaction domain (RID), the KIX domain (CREB and MYB interaction domain), the cysteine/histidine regions (TAZ1/CH1 and TAZ2/CH3) and the interferon response binding domain (IBiD). The last four domains, KIX, TAZ1, TAZ2 and IBiD of p300, each bind tightly to a sequence spanning both transactivation domains 9aaTADs of transcription factor p53. In addition p300 and CBP each contain a protein or histone acetyltransferase (PAT/HAT) domain and a bromodomain that binds acetylated lysines and a PHD finger motif with unknown function. The conserved domains are connected by long stretches of unstructured linkers.

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