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Like other E3 ligases, HOIP utilizes a conserved catalytic triad in which a conserved histidine proximal to the active-site cysteine acts as a general base to deprotonate the incoming acceptor ubiquitin nucleophile and mutation of this histidine, while permitting thioester formation, blocks aminolysis and renders the enzyme unable to form ubiquitin chains (Stieglitz et al., 2013