Ubiquitin E3 ligases control every aspect of eukaryotic biology by promoting protein
ubiquitination and degradation. At the end of a three-enzyme cascade, ubiquitin ligases …

E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating
transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate. The activity of …

Covalent attachment (conjugation) of one or more ubiquitin molecules to protein substrates
governs numerous eukaryotic cellular processes, including apoptosis, cell division and …

Proteins of the small ubiquitin-related modifier (SUMO) family are conjugated to proteins to
regulate such cellular processes as nuclear transport, transcription, chromosome …

Ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes
responsible for the attachment of ubiquitin (Ub) to cellular proteins. Humans have∼ 40 E2s …

The modification of proteins with ubiquitin chains can change their localization, activity
and/or stability. Although ubiquitylation requires the concerted action of ubiquitin-activating …

E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of
ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. Three distinct …

Ubiquitin-like proteins (Ubl's) are conjugated to target proteins or lipids to regulate their
activity, stability, subcellular localization, or macromolecular interactions. Similar to ubiquitin …

Post-translational modifications of proteins and the domains that recognize these
modifications have central roles in creating a highly dynamic relay system that reads and …

NEDD8 (neural precursor cell expressed developmentally downregulated protein 8) is a
ubiquitin-like protein that activates the largest ubiquitin E3 ligase family, the cullin–RING …