ubiquitinconjugated
Ubiquitin-conjugated describes a molecule, typically a substrate protein, that has covalently attached ubiquitin as part of the ubiquitination process. Ubiquitin is a small, 76-amino-acid protein attached to substrate lysines via an isopeptide bond between the ubiquitin C-terminus and the substrate’s lysine residue. The conjugation is carried out by a three-enzyme cascade: an E1 activating enzyme transfers ubiquitin to an E2 conjugating enzyme, and an E3 ligase provides substrate specificity to attach ubiquitin to the target.
A substrate may carry a single ubiquitin (monoubiquitination) or a chain of ubiquitin molecules (polyubiquitination). The
Deubiquitinating enzymes (DUBs) reverse ubiquitination by cleaving the isopeptide bonds, thereby removing ubiquitin and restoring substrates
Detection and study employ techniques such as immunoblotting with anti-ubiquitin antibodies, immunoprecipitation under denaturing conditions, ubiquitin
Dysregulation of ubiquitination is linked to diseases including cancer, neurodegenerative disorders, and immune dysfunction. The term