Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family

J Biol Chem. 1997 Oct 31;272(44):28001-7. doi: 10.1074/jbc.272.44.28001.


Several human cDNAs encoding a histone deacetylase protein, HDAC3, have been isolated. Analysis of the predicted amino acid sequence of HDAC3 revealed an open reading frame of 428 amino acids with a predicted molecular mass of 49 kDa. The HDAC3 protein is 50% identical in DNA sequence and 53% identical in protein sequence compared with the previously cloned human HDAC1. Comparison of the HDAC3 sequence with human HDAC2 also yielded similar results, with 51% identity in DNA sequence and 52% identity in protein sequence. The expressed HDAC3 protein is functionally active because it possesses histone deacetylase activity, represses transcription when tethered to a promoter, and binds transcription factor YY1. Similar to HDAC1 and HDAC2, HDAC3 is ubiquitously expressed in many different cell types.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Cloning, Molecular
  • DNA, Complementary
  • HeLa Cells
  • Histone Deacetylases / genetics*
  • Histone Deacetylases / metabolism
  • Humans
  • Molecular Sequence Data
  • Multigene Family*
  • Peptide YY / metabolism
  • Protein Binding
  • Sequence Homology, Amino Acid


  • DNA, Complementary
  • Peptide YY
  • Histone Deacetylases
  • histone deacetylase 3

Associated data

  • GENBANK/AF005482
  • GENBANK/U75696
  • GENBANK/U75697