UbcH5c/UBE2D3: Proteins and Enzymes

Ubiquitin-conjugating Enzyme H5c (UbcH5c), also known as Ubiquitin-conjugating Enzyme E2D 3 (UBE2D3), is a member of the yeast Ubc4/5 family of Ubiquitin-conjugating (E2) enzymes. Human UbcH5c/UBE2D3 has a predicted molecular weight of 17 kDa and shares 88% and 89% amino acid sequence identity with the related family members, UbcH5a and UbcH5b, respectively. In combination with Ubiquitin ligases (E3s) such as CHIP, UbcH5c/UBE2D3 mediates the ubiquitination and subsequent degradation of several regulatory proteins. For instance, UbcH5c/UBE2D3 is involved in the poly-ubiquitination and proteasome-mediated degradation of the Nuclear Factor kappaB (NF-kappaB) inhibitor, IkappaB-alpha, and is implicated in NF-kappaB-dependent inflammation. UbcH5c/UBE2D3 also mediates the ubiquitination of Histone H2A and PCNA, suggesting that it functions during transcriptional regulation, DNA replication, and DNA damage responses.