UbcH7 Protein, active, 10 µg

Ubiquitin-conjugating (E2) enzymes are characterized by the presence of a highly conserved ubiquitin-conjugating domain, which accommodates ATP-activated ubiquitin (Ub) via a covalently linked thioester on its active-site residue. E2 enzymes act through selective protein-protein interactions with the ubiquitin-activating E1 enzyme and ubiquitin ligase E3 enzymes and are able to differentiate effects on downstream substrates, either with a single Ub molecule or a Ub chain. While E3s are involved in substrate selection, E2s are the main determinants for selection of the lysine to construct Ub chains, which thereby directly control the cellular fate of the substrate.

UbcH7 shows broad specificity for HECT-type E3s but does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine. Despite lacking this lysine reactivity, UbcH7 exhibits activity with the RBR family E3 enzymes, such as Parkin and ARIH1.

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