CBP/p300-type histone acetyltransferase domain (IPR031162)

Short name: CBP_P300_HAT

Overlapping homologous superfamilies


Domain relationships



Histone acetyltransferase (HAT) enzymes play important roles in the regulation of chromatin assembly, RNA transcription, DNA repair and other DNA-templated reactions through the lysine side-chain acetylation of histones and other transcription factors. HATs fall into at least four different families based on sequence conservation within the HAT domain. This includes Gcn5/PCAF, CBP/p300, Rtt109 and MYST families. The different HAT families contain a structurally conserved central region associated with acetyl-Coenzyme A (Ac-CoA) cofactor binding but distinct catalytic mechanisms and structurally divergent flanking regions that mediate different chromatin regulatory functions. Protein acetylation extends beyond histones to other nuclear proteins and even cytoplasmic proteins to regulate diverse biological processes including the regulation of cell cycle, vesicular trafficking, cytoskeleton reorganisation and metabolism.

CREB-binding protein (CBP)/p300 proteins are involved in various physiological events including proliferation, differentiation and apoptosis. CBP/p300 proteins contain several well-defined protein-interaction domains as well as a centrally located 380-residue HAT domain [PMID: 18273021, PMID: 23934153, PMID: 11948408, PMID: 24287137].

The overall fold of the CBP/p300-type HAT domain consists of a central beta- sheet comprising seven beta-strands surrounded by nine alpha-helices and several loops [PMID: 18273021, PMID: 23934153].

Some proteins known to contain a cBP/p300-type HAT domain are listed below:

  • Animal CBP (also known as KAT3A), a coactivator for the cAMP-responsive transcription factor CREB.
  • Animal p300 (also known as KAT3B), binds to the adenoviral oncoprotein E1A.
  • Arabidopsis thaliana HACs, involved in the ethylene signaling pathway (HAC1, HAC2, HAC4, HAC5 and HAC12). All the HAC members share the CBP/p300- type HAT domain; however, the HAT domain of HAC1 but not that of HAC2 possesses acetyltransferase activity, while the situation had not been tested in the other HAC members [PMID: 24287137].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles