泛素特异性蛋白酶14(ubiquitin-specific protease 14,USP14)是真核生物体内普遍存在的一种去泛素化酶,在编辑泛素链长度以及维持游离泛素库的稳定中发挥重要作用。它既可通过去泛素化调控靶蛋白的降解,又可通过多种信号通路参与肿瘤以及神经系统疾病的发生发展,因此USP14有望成为相关疾病治疗的极具潜力的新靶点。文章将从结构、功能、底物蛋白、信号通路、相关疾病以及抑制剂等方面对USP14的研究进展做一综述。 Ubiquitin-specific protease 14 (USP14) is a ubiquitinating enzyme that is ubiquitous in eukaryotes and plays an important role in editing the ubiquitin chain length and maintaining the stability of the free ubiquitin library. It not only can regulate the degradation of target protein by de-ubiquitination, but also participate in the development of tumor and nervous system diseases through a variety of signaling pathways. Therefore, USP14 is expected to become a new potential target for the treatment of related diseases. This article reviews the progress of USP14 in terms of structure, function, substrate proteins, signaling pathways, related diseases and inhibitors.