MOZ and MORF acetyltransferases: Molecular interaction, animal development and human disease.

@article{Yang2015MOZAM,
  title={MOZ and MORF acetyltransferases: Molecular interaction, animal development and human disease.},
  author={X M Yang},
  journal={Biochimica et biophysica acta},
  year={2015},
  volume={1853 8},
  pages={1818-26}
}
Lysine residues are subject to many forms of covalent modification and one such modification is acetylation of the ε-amino group. Initially identified on histone proteins in the 1960s, lysine acetylation is now considered as an important form of post-translational modification that rivals phosphorylation. However, only about a dozen of human lysine acetyltransferases have been identified. Among them are MOZ (monocytic leukemia zinc finger protein; a.k.a. MYST3 and KAT6A) and its paralog MORF (a… CONTINUE READING
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