UbcH7 mediates the selective degradation of short-lived and abnormal proteins and is highly homologous to UbcH5. UbcH7 interacts with the HECT domain of E6-AP and the RING domain of c-Cbl, and can mediate the multi-ubiquitination of many different types of protein substrates. This enzyme has a mutation of the active site from cysteine to serine which abolishes the ability of UbcH7 to transfer ubiquitin to an accepting E3 protein. Ideal for use as a negative or competitive control, or to study protein-protein interactions.