PROSITE documentation PDOC51727CBP/p300-type histone acetyltransferase (HAT) domain profile
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 (see <PDOC51186>), CBP/p300, Rtt109 (see <PDOC51728>) and MYST (see <PDOC51726>) 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 reorganization 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 [1,2,3,4].
The overall fold of the CBP/p300-type HAT domain consists of a central β-sheet comprising seven β-strands surrounded by nine α-helices and several loops (see <PDB:3BIY>) [1,2].
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 [4].
The profile we developed covers the entire CBP/p300-type HAT domain.
Last update:August 2014 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Liu X. Wang L. Zhao K. Thompson P.R. Hwang Y. Marmorstein R. Cole P.A. |
| Title | The structural basis of protein acetylation by the p300/CBP transcriptional coactivator. | |
| Source | Nature 451:846-850(2008). | |
| PubMed ID | 18273021 | |
| DOI | 10.1038/nature06546 |
| 2 | Authors | Delvecchio M. Gaucher J. Aguilar-Gurrieri C. Ortega E. Panne D. |
| Title | Structure of the p300 catalytic core and implications for chromatin targeting and HAT regulation. | |
| Source | Nat. Struct. Mol. Biol. 20:1040-1046(2013). | |
| PubMed ID | 23934153 | |
| DOI | 10.1038/nsmb.2642 |
| 3 | Authors | Yuan L.W. Giordano A. |
| Title | Acetyltransferase machinery conserved in p300/CBP-family proteins. | |
| Source | Oncogene 21:2253-2260(2002). | |
| PubMed ID | 11948408 | |
| DOI | 10.1038/sj.onc.1205283 |
| 4 | Authors | Li C. Xu J. Li J. Li Q. Yang H. |
| Title | Involvement of arabidopsis histone acetyltransferase HAC family genes in the ethylene signaling pathway. | |
| Source | Plant Cell Physiol. 55:426-435(2014). | |
| PubMed ID | 24287137 | |
| DOI | 10.1093/pcp/pct180 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)