UBE2L3 (D5G1) Rabbit mAb #8721

Protein ubiquitination requires the concerted action of the E1, E2, and E3 ubiquitin-conjugating enzymes. Ubiquitin is first activated through ATP-dependent formation of a thiol ester with ubiquitin-activating enzyme E1. The activated ubiquitin is then transferred to a thiol group of ubiquitin-carrier enzyme E2. The final step is the transfer of ubiquitin from E2 to an ε-amino group of the target protein lysine residue, which is mediated by ubiquitin-ligase enzyme E3 (1).
UBE2L3, also commonly referred to as UBCH7, is a ubiquitin-conjugating enzyme that belongs to a family of four related human genes, UBE2L1-UBE2L4. It appears as though UBE2L3 is the only member of this gene family to be transcribed and translated and that UBE2L1, UBE2L2, and UBE2L4 exist as pseudogenes (2,3). As a ubiquitin-conjugating enzyme, UBE2L3 has been linked to the ubiquitination of numerous substrates via its interaction with protein-ubiquitin E3 ligases such as NEDD4 (4), E6AP (5), Parkin (6), c-Cbl (7), and Triad1 (8,9). There is also evidence suggesting that UBE2L3 can modulate the transcriptional activity of numerous members of the nuclear hormone receptor superfamily such as the glucocorticoid receptor, progesterone receptor, androgen receptor, and retinoic acid receptors (10). Furthermore, UBE2L3 protein levels appear to be regulated by the ubiquitin-proteasome pathway allowing for it to exert control over S-phase entry and progression (11).