泛素-蛋白酶体系统(Ubiquitin-proteasome system, UPS)介导了真核生物80%~85%的蛋白质降解, 该蛋白质降解途径具有依赖ATP、高效、高度选择性的特点。除参与蛋白质降解之外, 泛素化修饰还可以直接影响蛋白质的活性和定位。由于泛素化修饰底物蛋白在细胞中的广泛存在, 泛素化修饰可以调控包括细胞周期、细胞凋亡、转录调控、DNA损伤修复以及免疫应答等在内的多种细胞活动。近年来, 泛素-蛋白酶体系统相关的蛋白质组学数据不断产出, 有效地管理、组织并合理分析这些数据显得尤为必要。文章综述了当前世界范围内针对蛋白质泛素化修饰展开的生物信息学研究, 总结了前人的工作结果, 包括UPS相关蛋白质数据的收录、泛素化修饰网络的构建和分析、泛素化修饰位点的预测及泛素化修饰motif的研究等方面内容, 并对该领域未来的发展方向进行了讨论。
Ubiquitin-proteasome system (UPS) mediates 80% to 85% of the protein degradation in eukaryotic cells. The characteristics of UPS pathway are dependent on ATP, efficient and highly selective. Ubiquitination not only participates in protein degradation, but also directly affects protein activity and localization. Ubiquitination can regulate multiple cellular processes including cell cycle progression, apoptosis, transcriptional regulation, DNA damage repair and immune response. More and more datasets about UPS are published, and it is necessary to organize and analyze these data efficiently. We re-view the related bioinformatics studies in UPS datasets, such as collection of UPS related proteins, construction and analy-sis of ubiquitination networks, prediction of ubiquitination sites and motifs. Some potential perspectives are also discussed.
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