PSEA: Kinase-specific prediction and analysis of human phosphorylation substrates

被引:25
作者
Suo, Sheng-Bao [1 ]
Qiu, Jian-Ding [1 ,2 ]
Shi, Shao-Ping [1 ,3 ]
Chen, Xiang [1 ]
Liang, Ru-Ping [1 ]
机构
[1] Nanchang Univ, Dept Chem, Nanchang 330031, Peoples R China
[2] Pingxiang Coll, Dept Chem Engn, Pingxiang 337055, Peoples R China
[3] Nanchang Univ, Dept Math, Nanchang 330031, Peoples R China
基金
中国国家自然科学基金;
关键词
PROTEIN-KINASES; TYROSINE PHOSPHORYLATION; COMPUTATIONAL PREDICTION; TAU PHOSPHORYLATION; SIGNAL-TRANSDUCTION; P38; MAPK; SITES; ACTIVATION; DATABASE; INHIBITORS;
D O I
10.1038/srep04524
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Protein phosphorylation catalysed by kinases plays crucial regulatory roles in intracellular signal transduction. With the increasing number of kinase-specific phosphorylation sites and disease-related phosphorylation substrates that have been identified, the desire to explore the regulatory relationship between protein kinases and disease-related phosphorylation substrates is motivated. In this work, we analysed the kinases' characteristic of all disease-related phosphorylation substrates by using our developed Phosphorylation Set Enrichment Analysis (PSEA) method. We evaluated the efficiency of our method with independent test and concluded that our approach is reliable for identifying kinases responsible for phosphorylated substrates. In addition, we found that Mitogen-activated protein kinase (MAPK) and Glycogen synthase kinase (GSK) families are more associated with abnormal phosphorylation. It can be anticipated that our method might be helpful to identify the mechanism of phosphorylation and the relationship between kinase and phosphorylation related diseases. A user-friendly web interface is now freely available at http://bioinfo.ncu.edu.cn/PKPred_Home.aspx.
引用
收藏
页数:10
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