PCAF Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Interacts with SIRT1. Interacts (unsumoylated form) with NR2C1; the interaction promotes transactivation activity. Interacts with EP300, CREBBP and DDX17. Interacts with NCOA1 and NCOA3. Component of a large chromatin remodeling complex, at least composed of MYSM1, KAT2B/PCAF, RBM10 and KIF11/TRIP5. Interacts with NR2C2 (hypophosphorylated and unsumoylated form); the interaction promotes the transactivation activity of NR2C2. Binds to HTLV-1 Tax. Interacts with and acetylates HIV-1 Tat. Interacts with KLF1; the interaction does not acetylate KLF1 and there is no enhancement of its transactivational activity. Interacts with NFE4. Interacts with MECOM. Interacts with E2F1; the interaction acetylates E2F1 augmenting its DNA-binding and transcriptional activity. Ubiquitously expressed but most abundant in heart and skeletal muscle. Belongs to the GCN5 family. Note: This description may include information from UniProtKB.
Protein type: Acetyltransferase; EC 2.3.1.48; Nuclear receptor co-regulator
Chromosomal Location of Human Ortholog: 17 C|17 27.86 cM
Cellular Component:  A band; actomyosin; Ada2/Gcn5/Ada3 transcription activator complex; centrosome; cytoplasm; cytoskeleton; cytosol; histone acetyltransferase complex; I band; kinetochore; nuclear chromatin; nucleus; protein-containing complex
Molecular Function:  acetyltransferase activity; chromatin binding; cyclin-dependent protein serine/threonine kinase inhibitor activity; diamine N-acetyltransferase activity; histone acetyltransferase activity; histone acetyltransferase binding; histone deacetylase binding; lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; peptide-lysine-N-acetyltransferase activity; protein binding; protein kinase binding; RNA polymerase II regulatory region sequence-specific DNA binding; transcription coactivator activity; transcription coregulator activity; transcription factor binding; transferase activity; transferase activity, transferring acyl groups
Biological Process:  cell cycle; cellular response to insulin stimulus; chromatin remodeling; histone acetylation; histone H3 acetylation; histone H3-K9 acetylation; internal peptidyl-lysine acetylation; N-terminal peptidyl-lysine acetylation; negative regulation of cell proliferation; negative regulation of centriole replication; negative regulation of cyclin-dependent protein serine/threonine kinase activity; peptidyl-lysine acetylation; positive regulation of blood vessel diameter; positive regulation of chromatin binding; positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter; positive regulation of histone H3-K14 acetylation; positive regulation of histone H3-K9 acetylation; positive regulation of neuron projection development; positive regulation of transcription by RNA polymerase II; positive regulation of transcription, DNA-templated; protein acetylation; regulation of protein ADP-ribosylation; regulation of transcription, DNA-templated; rhythmic process
Reference #:  Q9JHD1 (UniProtKB)
Alt. Names/Synonyms: A930006P13Rik; AI461839; AW536563; Histone acetylase PCAF; Histone acetyltransferase KAT2B; Histone acetyltransferase PCAF; K(lysine) acetyltransferase 2B; Kat2b; Lysine acetyltransferase 2B; P/CAF; P300/CBP-associated factor; Pcaf
Gene Symbols: Kat2b
Molecular weight: 91,769 Da
Basal Isoelectric point: 9.25  Predict pI for various phosphorylation states
CST Pathways:  G2/M DNA Damage Checkpoint  |  NF-kB Signaling  |  Protein Acetylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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PCAF

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  NURSA