Covalent attachment of ubiquitin, a small globular polypeptide, to protein substrates is a key post-translational modification that determines the fate, function, and turnover of most cellular proteins. Ubiquitin modification exists as mono- or polyubiquitin chains involving multiple ways how ubiquitin C-termini are connected to lysine, perhaps other amino acid side chains, and N-termini of proteins, often including branching of the ubiquitin chains. Understanding this enormous complexity in protein ubiquitination, the so-called ‘ubiquitin code’, in combination with the $\sim$1000 enzymes involved in controlling ubiquitin recognition, conjugation, and deconjugation, calls for novel developments in analytical techniques. Here, we review different headways in the field mainly driven by mass spectrometry and chemical biology, referred to as “ubiquitomics”, aiming to understand this system’s biological diversity.

中文翻译：

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泛素组学：概述与未来


泛素（一种小球状多肽）与蛋白质底物的共价连接是决定大多数细胞蛋白质的命运、功能和周转的关键翻译后修饰。泛素修饰以单泛素或多泛素链的形式存在，涉及泛素 C 末端与赖氨酸（可能是其他氨基酸侧链）和蛋白质 N 末端连接的多种方式，通常包括泛素链的分支。了解蛋白质泛素化的巨大复杂性，即所谓的“泛素代码”，并结合1000 种酶参与控制泛素识别、结合和解结合，需要分析技术的新发展。在这里，我们回顾了该领域主要由质谱和化学生物学（称为“泛素组学”）驱动的不同进展，旨在了解该系统的生物多样性。