| Literature DB >> 9346952 |
W M Yang1, Y L Yao, J M Sun, J R Davie, E Seto.
Abstract
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.Entities:
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Year: 1997 PMID: 9346952 DOI: 10.1074/jbc.272.44.28001
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157