Characterization and Prediction of Lysine (K)-Acetyl-Transferase Specific Acetylation Sites

• DOI: 10.1074/mcp.m111.011080
• Publication Date: 2011-10-01T05:43:44Z
• Authors: Tingting Li; Yipeng Du; Likun Wang; Lei Huang; Wenlin Li; Ming Lu; Xuegong Zhang; Wei-Guo Zhu
• Keywords: Transferase; Characterization

Lysine acetylation is a well-studied post-translational modification on both histone and nonhistone proteins. More than 2000 acetylated proteins 4000 lysine sites have been identified by large scale mass spectrometry or traditional experimental methods. Although over 20 (K)-acetyl-transferases (KATs) characterized, which KAT responsible for given protein site mostly unknown. In this work, we collected KAT-specific manually analyzed sequence features surrounding the of substrates from three main families (CBP/p300, GCN5/PCAF, MYST family). We found that each acetylates lysines with different features. Based these differences, developed computer program, Acetylation Set Enrichment method to predict KAT-families are site. Finally, evaluated efficiency our method, experimentally detected four were predicted be two when one representative member family expressed. conclude approach, combined more methods, may useful identifying proteome-wide.