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Ubiquitination is a dynamic protein modification that determines the fate and function of target proteins through the covalent attachment of ubiquitin molecules. This process is orchestrated by a sequential enzymatic cascade involving ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). Beyond its classical role in proteasome-mediated protein degradation, ubiquitination regulates diverse cellular processes, including protein degradation, trafficking, DNA damage repair, cell cycle progression, and immune responses. Dysregulated ubiquitination is implicated in multiple diseases, particularly cancer and neurodegenerative disorders, making it an important target for disease mechanism studies and therapeutic development.