UbcH7, also known as UBE2L3, is a member of the ubiquitin E2 conjugating enzyme family, essential components of the ubiquitin cascade.
The selectivity of the ubiquitin cascade for a particular substrate protein relies on the interaction between the E2 conjugating enzyme (of which a cell contains relatively few) and an ubiquitin E3 ligase, of which over 600 have been identified to date. The specific E2-E3 pair required for ubiquitination of a particular substrate protein in vivo may also control the type of ubiquitin modification (mono-, multi-, poly-ubiquitin), the exact substrate lysine residue(s) to be modified and, in the case of polyubiquitination, the chain length and lysine linkage type.
UbcH7 interacts with both HECT domain and RING domain E3 ligases and is involved in the E6AP mediated ubiquitination of p53.
Recombinant human UbcH7 protein expressed with a N-terminal His-tag. Protein has utility in ubiquitination reactions, polyubiquitin chain synthesis, identification of substrate specific E2-E3 pairs and determination of E2 polyubiquitin linkage specificity.