{PDOC51727}
{PS51727; CBP_P300_HAT}
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* CBP/p300-type histone acetyltransferase (HAT) domain profile *
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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 beta-
sheet comprising  seven  beta-strands  surrounded  by  nine  alpha-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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: August 2014 / First entry.

[ 1] Liu X., Wang L., Zhao K., Thompson P.R., Hwang Y., Marmorstein R.,
     Cole P.A.
     "The structural basis of protein acetylation by the p300/CBP
     transcriptional coactivator."
     Nature 451:846-850(2008).
     PubMed=18273021; DOI=10.1038/nature06546
[ 2] Delvecchio M., Gaucher J., Aguilar-Gurrieri C., Ortega E., Panne D.
     "Structure of the p300 catalytic core and implications for chromatin
     targeting and HAT regulation."
     Nat. Struct. Mol. Biol. 20:1040-1046(2013).
     PubMed=23934153; DOI=10.1038/nsmb.2642
[ 3] Yuan L.W., Giordano A.
     "Acetyltransferase machinery conserved in p300/CBP-family proteins."
     Oncogene 21:2253-2260(2002).
     PubMed=11948408; DOI=10.1038/sj.onc.1205283
[ 4] Li C., Xu J., Li J., Li Q., Yang H.
     "Involvement of arabidopsis histone acetyltransferase HAC family genes
     in the ethylene signaling pathway."
     Plant Cell Physiol. 55:426-435(2014).
     PubMed=24287137; DOI=10.1093/pcp/pct180

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