Zinc finger (ZnF) domains are present in at least 5% of human proteins. First characterized as binding to DNA, ZnFs display extraordinary binding plasticity and can bind to RNA, lipids, proteins, and protein post-translational modifications (PTMs). The diverse binding properties of ZnFs have made their functional characterization challenging. While once confined to large and poorly characterized protein families, proteomic, cellular, and molecular studies have begun to shed light on their involvement as protectors of the genome. We focus here on the emergent roles of ZnF domain-containing proteins in promoting genome integrity, including their involvement in telomere maintenance and DNA repair. These findings have highlighted the need for further characterization of ZnF proteins, which can reveal the functions of this large gene class in normal cell function and human diseases, including those involving genome instability such as aging and cancer.

锌指（ZnF）域存在于至少5％的人类蛋白质中。ZnFs首先被表征为与DNA结合，显示出非凡的结合可塑性，并且可以与RNA，脂质，蛋白质和蛋白质翻译后修饰（PTM）结合。ZnFs的各种结合特性使其功能表征具有挑战性。蛋白质组学，细胞学和分子学研究虽然曾经仅限于大型且特征不充分的蛋白质家族，但已开始阐明它们作为基因组保护者的作用。我们在这里集中于含ZnF域的蛋白质在促进基因组完整性方面的新兴作用，包括它们参与端粒维持和DNA修复的作用。这些发现凸显了进一步表征ZnF蛋白的必要性，