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J Biol Chem. 1999 Oct 1;274(40):28528-36.

Identification of a human histone acetyltransferase related to monocytic leukemia zinc finger protein.

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  • 1Molecular Oncology Group, Department of Medicine, McGill University Health Center, Montréal, Québec H3A 1A1, Canada.


We describe here the identification and functional characterization of a novel human histone acetyltransferase, termed MORF (monocytic leukemia zinc finger protein-related factor). MORF is a 1781-residue protein displaying significant sequence similarity to MOZ (monocytic leukemia zinc finger protein). MORF is ubiquitously expressed in adult human tissues, and its gene is located at human chromosome band 10q22. MORF has intrinsic histone acetyltransferase activity. In addition to its histone acetyltransferase domain, MORF possesses a strong transcriptional repression domain at its N terminus and a highly potent activation domain at its C terminus. Therefore, MORF is a novel histone acetyltransferase that contains multiple functional domains and may be involved in both positive and negative regulation of transcription.

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