Anti-HDAC3

HDAC3(HISTONE DEACETYLASE 3) is a member of the histone deacetylase/acuc/apha family of proteins that is an enzyme that in humans is encoded by the HDAC3 gene. The HDAC3 gene is mapped to 5q31.3. HDAC3 has histone deacetylase activity and represses transcription when tethered to a promoter. It may participate in the regulation of transcription through its binding with the zinc-finger transcription factor YY1. The protein can also down-regulate p53 function and thus modulate cell growth and apoptosis. And this gene is regarded as a potential tumor suppressor gene. HDAC3 has an open reading frame of 428 amino acids and shares 53% amino acid identity with HDAC1 and 52% with HDAC2. The catalytic domain of HDAC4 interacts with HDAC3 via the transcriptional corepressor NCOR2. All experimental conditions leading to the suppression of HDAC4 binding to NCOR2 and to HDAC3 resulted in loss of enzymatic activity associated with HDAC4. Protein function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys- 27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1, increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor. Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation (PubMed:21444723, PubMed:23911289). Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress (PubMed:25190803). [The UniProt Consortium]