Ubiquitination (also known as ubiquitylation) is a form of post-translation modification (PTM) in which ubiquitin is attached to a target protein. Ubiquitin is a 76 amino acid protein that exists in the free form or can be conjugated to a protein as a single ubiquitin (i.e., monoubiquitination) or as a multiple ubiquitin (i.e., polyubiquitination). Ubiquitination plays versatile roles in protein functions ranging from protein degradation to subcellular localization and kinase activation. Three enzymes are involved in the ubiquitination pathway: Ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin-protein ligase (E3). Ubiquitination is highly relevant to the pathobiology of many human diseases. This review will explore the fundamentals of ubiquitination, its function, pathophysiology, and clinical significance of ubiquitination.
Copyright © 2024, StatPearls Publishing LLC.