The ubiquitin conjugating enzyme UBE2L3 regulates TNFa-induced linear ubiquitination

The inducible and reversible modification of proteins with polyubiquitin chains has emerged as one of the most common and versatile means of protein modification. Ubiquitin contains 7 lysine residues, each of which can serve as an acceptor site for formation of polyubiquitin chains. In addition, the C-terminal glycine of one ubiquitin molecule can form a conventional peptide bond with the N-terminal methionine of an acceptor ubiquitin,