泛素是一种包含76个氨基酸的小分子蛋白。泛素共价结合到底物的过程称为泛素化修饰。泛素化修饰过程是一个由级联的泛素激活酶、泛素结合酶和泛素连接酶所介导的复杂过程，泛素化修饰具有高效、ATP依赖、高度特异的特点。泛素化修饰与细胞周期调控、细胞凋亡、转录调控、DNA损伤修复等一系列生物学过程密切相关。在泛素化修饰过程中，泛素连接酶对底物的识别，是决定泛素化修饰特异性的关键环节。泛素连接酶底物识别的相关机制研究不断被报道，鉴定泛素连接酶底物的高通量方法也在不断的改进和发展。随着实验研究的不断深入，实验数据的不断产出，利用生物信息学进行泛素连接酶底物的研究也开始受到关注。对泛素连接酶识别底物的相关机制、高通量泛素连接酶底物的鉴定方法、泛素连接酶底物的生物信息学研究和生物信息学在泛素连接酶底物研究中的发展方向进行讨论。%Ubiquitin is a small-molecule protein composed of 76 amino acids. The covalent-bonding process between ubiquitin and substrates is defined as Ubiquitination. Ubiquitination modification, an efficient, ATP-dependent, and highly specific process, is mediated by a cascade regulation of ubiquitin activating enzymes, ubiquitin conjugating enzymes, ubiquitin ligase and deubiquitinating enzymes. Ubiquitination is highly relevant with biological processes like cell cycle regulation, cell apoptosis, transcription regulation, DNA damage response and so on. In the process of ubiquitination, the recognition between ubiquitin ligases and substrates is critical for the specificity. The mechanisms of such recognition are being reported moreover the high throughput methods identifying E3’s substrate are being improved and developed. With the accumulation of ubiquitination data from the deep-going research, the bioinformatics approach studying the selective relationship between E3s and substrates is becoming a hot spot. This article will discuss the recognition mechanism between E3s and substrates, the high throughput methods used for the identification of E3’s substrates, review the bioinformatics study about E3s’ substrates and highlight the future research direction.
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