泛素和泛素样蛋白的翻译后修饰对于调节细胞蛋白功能非常重要。在将近20年前首次被识别出来的UFM1（泛素结构修饰物1）是泛素样蛋白家族的成员之一。UFM1与靶蛋白的共价连接是通过由E1（激活）、E2（连接）和E3（连接）酶组成的酶级联完成的。在分子水平上，UFM1的修饰（UFMylation）是蛋白功能的重要介质。UFM1连接系统的失调，例如UFMylation组分的敲除，会干扰蛋白质组稳态并引发内质网应激。这些变化与发育障碍、肿瘤发生、组织损伤、炎症以及几种遗传性神经综合症有关。本文将重点介绍UFMylation在动物发育和相关先天性疾病中的作用。我们将涵盖造血系统、肝脏、中枢神经系统、肠道、心脏、肾脏、免疫和骨骼系统，以便深入了解疾病发病机制并为可能的新型治疗方法提供启示。本文受版权保护。保留所有权利。 © 2023 Wiley Periodicals，Inc.

Post-translational modifications by ubiquitin and ubiquitin-like proteins are important in regulating cellular protein functions. UFM1 (ubiquitin-fold modifier 1), first identified almost two decades ago, is a member of the ubiquitin-like protein family. UFM1 is covalently conjugated to the target proteins in an enzymatic cascade consisting of E1 (activating), E2 (conjugating), and E3 (ligating) enzymes. At the molecular level, modification by UFM1 (UFMylation) is an important mediator of protein function. Dysregulation of the UFM1 conjugation system, e.g., the knockout of UFMylation components, disturbs proteome homeostasis and triggers endoplasmic reticulum stress. Such changes are linked to developmental disorders, tumorigenesis, tissue injury, inflammation, and several hereditary neurological syndromes. This review will focus on the role of the UFMylation in animal development and associated congenital disorders. We will cover the hematopoietic system, liver, central nervous system, intestine, heart, kidney, immune and skeletal system to provide insight into disease pathogenesis and shed light on possible novel therapeutic methods. This article is protected by copyright. All rights reserved.© 2023 Wiley Periodicals, Inc.