PCAF

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K(lysine) acetyltransferase 2B
Protein PCAF PDB 1cm0.png
PDB rendering based on 1cm0.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols KAT2B ; CAF; P/CAF; PCAF
External IDs OMIM602303 MGI1343094 HomoloGene20834 ChEMBL: 5500 GeneCards: KAT2B Gene
EC number 2.3.1.48
RNA expression pattern
PBB GE PCAF 203845 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 8850 18519
Ensembl ENSG00000114166 ENSMUSG00000000708
UniProt Q92831 Q9JHD1
RefSeq (mRNA) NM_003884 NM_001190846
RefSeq (protein) NP_003875 NP_001177775
Location (UCSC) Chr 3:
20.04 – 20.15 Mb
Chr 17:
53.57 – 53.67 Mb
PubMed search [1] [2]

P300/CBP-associated factor (PCAF), also known as K(lysine) acetyltransferase 2B (KAT2B), is a human gene and transcriptional coactivator associated with p53.

Structure

Several domains of PCAF can act independently or in unison to enable its functions. PCAF has separate acetyltransferase and E3 ubiquitin ligase domains as well as a bromodomain for interaction with other proteins. PCAF also possesses sites for its own acetylation and ubiquitination.[1]

Function

CBP and p300 are large nuclear proteins that bind to many sequence-specific factors involved in cell growth and/or differentiation, including c-jun and the adenoviral oncoprotein E1A. The protein encoded by the PCAF gene associates with p300/CBP. It has in vitro and in vivo binding activity with CBP and p300, and competes with E1A for binding sites in p300/CBP. It has histone acetyl transferase activity with core histones and nucleosome core particles, indicating that this protein plays a direct role in transcriptional regulation.[2]

Regulation

The acetyltransferase activity and cellular location of PCAF are regulated through acetylation of PCAF itself. PCAF may be autoacetylated (acetylated by itself) or by p300. Acetylation leads to migration to the nucleus and enhances its acetyltransferase activity.[3] PCAF interacts with and is deacetylated by HDAC3, leading to a reduction in PCAF acetyltransferase activity and cytoplasmic localisation.[4]

Protein interactions

PCAF forms complexes with numerous proteins that guide its activity. For example PCAF is recruited by ATF[5] to acetylate histones and promote transcription of ATF4 target genes.

Targets

There are various protein targets of PCAF's acetyltransferase activity including transcription factors such as Fli1,[6] p53[7] and numerous histone residues. Hdm2, itself a ubiquitin ligase that targets p53, has also been demonstrated to be a target of the ubiquitin-ligase activity of PCAF.[1]

Interactions

PCAF has been shown to interact with:

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See also

References

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External links

Further reading

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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