A systematic exploration of the associations between amino acid variants and post-translational modifications

被引:0
|
作者
Qin, Gui-Min [1 ,2 ]
Hou, Yi-Bo [3 ]
Zhao, Xing-Ming [1 ]
机构
[1] Tongji Univ, Sch Elect & Informat Engn, Dept Comp Sci, Shanghai 201804, Peoples R China
[2] Xidian Univ, Sch Software, Xian 710126, Peoples R China
[3] Xidian Univ, Sch Comp Sci & Technol, Xian 710126, Peoples R China
基金
中国博士后科学基金;
关键词
Amino acid variants; Cross-talks; Diseases; Post-translational modifications; GENETIC POLYMORPHISMS; CROSS-TALK; PROTEIN; PHOSPHORYLATION; CANCER; DISEASE; ACETYLATION; APOPTOSIS; MUTATIONS; RESOURCE;
D O I
10.1016/j.neucom.2015.11.106
中图分类号
TP18 [人工智能理论];
学科分类号
081104 ; 0812 ; 0835 ; 1405 ;
摘要
The post-translational modifications (PTMs) are important to protein activities and play key roles in various kinds of biological processes. It has been well recognized that the alteration of PTMs may lead to diseases. However, it is still not clear how the PTMs are related to diseases. In this work, we systematically investigated the associations between PTM residues and disease related mutations. In particular, the common PTMs, including phosphorylation, ubiquitylation and acetylation, were considered here. By analyzing the PTM sites and the amino acid mutations, we found that the amino acid mutations co-occurring with PTM sites and PTM cross-talks tend to be deleterious mutations in diseases. Specifically, the deleterious single amino acid variants (SAVs) associated with cancer and muscular diseases tend to co-occur with phosphorylation residues. The PTM sites of proteins from nuclear envelope, protein complex and lysosome were found to be more likely adjacent to the deleterious amino acid variations. These findings provide insights into the associations between PTM5 and diseases, and can help identify novel disease genes in the future. (C) 2016 Elsevier B.V. All rights reserved.
引用
收藏
页码:13 / 18
页数:6
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