qPhos: a database of protein phosphorylation dynamics in humans

被引:44
|
作者
Yu, Kai [1 ]
Zhang, Qingfeng [1 ]
Liu, Zekun [1 ,2 ]
Zhao, Qi [1 ]
Zhang, Xiaolong [1 ]
Wang, Yan [1 ]
Wang, Zi-Xian [1 ]
Jin, Ying [1 ]
Li, Xiaoxing [1 ]
Liu, Ze-Xian [1 ]
Xu, Rui-Hua [1 ]
机构
[1] Sun Yat Sen Univ, State Key Lab Oncol South China, Collaborat Innovat Ctr Canc Med, Canc Ctr, Guangzhou 510060, Guangdong, Peoples R China
[2] Huazhong Univ Sci & Technol, Dept Hepatobiliary Surg, Union Hosp, Tongji Med Coll, Wuhan 430022, Hubei, Peoples R China
基金
中国国家自然科学基金; 国家重点研发计划;
关键词
POSTTRANSLATIONAL MODIFICATIONS; RESOURCE; KINASES; ACTIVATION; REVEALS; SITES; DISEASE;
D O I
10.1093/nar/gky1052
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Temporal and spatial protein phosphorylation dynamically orchestrates a broad spectrum of biological processes and plays various physiological and pathological roles in diseases and cancers. Recent advancements in high-throughput proteomics techniques greatly promoted the profiling and quantification of phosphoproteome. However, although several comprehensive databases have reserved the phosphorylated proteins and sites, a resource for phosphorylation quantification still remains to be constructed. In this study, we developed the qPhos (http://qphos.cancerbio.info) database to integrate and host the data on phosphorylation dynamics. A total of 3 537 533 quantification events for 199 071 non-redundant phosphorylation sites on 18 402 proteins under 484 conditions were collected through exhaustive curation of published literature. The experimental details, including sample materials, conditions and methods, were recorded. Various annotations, such as protein sequence and structure properties, potential upstream kinases and their inhibitors, were systematically integrated and carefully organized to present details about the quantified phosphorylation sites. Various browse and search functions were implemented for the user-defined filtering of samples, conditions and proteins. Furthermore, the qKinAct service was developed to dissect the kinase activity profile from user-submitted quantitative phosphoproteome data through annotating the kinase activity-related phosphorylation sites. Taken together, the qPhos database provides a comprehensive resource for protein phosphorylation dynamics to facilitate related investigations.
引用
收藏
页码:D451 / D458
页数:8
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