Overview of protein ubiquitylation

The post-translational attachment of ubiquitin (Ub) to proteins, termed ubiquitylation, controls many intracellular processes, including protein turnover,  autophagy, cell signalling and the DNA damage response.

Ubiquitin is most often conjugated to lysine residues of target proteins by an enzymatic cascade involving E1 activating, E2 conjugating and E3 ligase enzymes.

Ubiquitylation can be reversed by deubiquitylating enzymes (DUBs), which cleave ubiquitin from substrate proteins or between ubiquitins in polyubiquitin chains.

The deregulation of components of the ubiquitin system underlies  many human diseases, including cancer, neurodegeneration, and inflammatory and metabolic disorders. Our aim is to help researchers gain access to these reagents to facilitate research worldwide.