Ubiquitin-Conjugating Enzyme E2 D3

UBE2D3, historically known as UBCH5C, is the third member of the UBE2D family of general-purpose conjugating enzymes. Like its siblings it consists almost entirely of the UBC domain, is charged by the E1 UBA1, and cooperates with RING and HECT ligases across many pathways. Notably, UBE2D3 partners with the HECT enzyme E6-AP to mediate HPV E6-dependent p53 degradation, and it also supports c-Cbl-driven ubiquitination of activated receptor tyrosine kinases. The native enzyme is ubiquitously expressed at high levels, and recombinant UBE2D3 is routinely employed in ubiquitin chain assembly studies, E3 substrate screening, and characterization of ubiquitin mutants.