title: Proteome-wide analysis of amino acid variations that influence protein lysine acetylation.
abstract: Next-generation sequencing (NGS) technologies are yielding ever higher volumes of genetic variation data. Given this large amount of data, it has become both a possibility and a priority to determine what the functional implication of genetic variations is. Considering the essential roles of acetylation in protein functions, it is highly likely that acetylation related genetic variations change protein functions. In this work, we performed a proteome-wide analysis of amino acid variations that could potentially influence protein lysine acetylation characteristics in human variant proteins. Here, we defined the AcetylAAVs as acetylation related amino acid variations that affect acetylation sites or their interacting acetyltransferases, and categorized three types of AcetylAAVs. Using the developed prediction system, named KAcePred, we detected that 50.87% of amino acid variations are potential AcetylAAVs and 12.32% of disease mutations could result in AcetylAAVs. More interestingly, from the statistical analysis, we found that the amino acid variations that directly create new potential lysine acetylation sites have more chance to cause diseases. It can be anticipated that the analysis of AcetylAAVs might be useful to screen important polymorphisms and help to identify the mechanism of genetic diseases. A user-friendly web interface for analysis of AcetylAAVs is now freely available at  http://bioinfo.ncu.edu.cn/AcetylAAVs_Home.aspx .
authors.affiliation: Department of Chemistry, Nanchang Universit y, Nanchang 330031, China.
authors.forename: Sheng-Bao
authors.initials: SB
authors.lastname: Suo
authors.forename: Jian-Ding
authors.initials: JD
authors.lastname: Qiu
authors.forename: Shao-Ping
authors.initials: SP
authors.lastname: Shi
authors.forename: Xiang
authors.initials: X
authors.lastname: Chen
authors.forename: Shu-Yun
authors.initials: SY
authors.lastname: Huang
authors.forename: Ru-Ping
authors.initials: RP
authors.lastname: Liang
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000145:classification / Q000378:metabolism*; D020816:Amino Acid Motifs; D019295:Computational Biology; D030562:Databases, Protein; D014644:Genetic Variation; D006801:Humans; D020407:Internet; D008239:Lysine / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D020543:Proteome / Q000032:analysis* / Q000235:genetics / Q000378:metabolism*; D060388:Support Vector Machine; D014584:User-Computer Interface
chemical_list: D020543:Proteome; D000123:Acetyltransferases; D008239:Lysine