UBE2L3 Human

Ubiquitin-Conjugating Enzyme E2L3, also known as UBE2L3 or UbcH7, is a member of the ubiquitin-conjugating (E2) enzyme family. These enzymes play a crucial role in the ubiquitination process, which is essential for the regulation of protein turnover and various cellular processes.

Ubiquitination is a post-translational modification where ubiquitin, a small regulatory protein, is covalently attached to target proteins. This process involves three main types of enzymes:

1. E1 (Ubiquitin-activating enzymes): Activate ubiquitin in an ATP-dependent manner.
2. E2 (Ubiquitin-conjugating enzymes): Transfer activated ubiquitin from E1 to the target protein.
3. E3 (Ubiquitin ligases): Facilitate the transfer of ubiquitin from E2 to the target protein, providing substrate specificity .

UBE2L3 accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. It is involved in the selective degradation of short-lived and abnormal proteins, playing a critical role in maintaining cellular homeostasis . In vitro, UBE2L3 catalyzes ‘Lys-11’-linked polyubiquitination .

UBE2L3 is involved in various cellular processes, including:

• Cell Cycle Regulation: It is down-regulated during the S-phase, indicating its role in cell cycle progression .
• Protein Degradation: By targeting proteins for degradation, UBE2L3 helps regulate protein levels and remove damaged or misfolded proteins .
• Signal Transduction: UBE2L3 is involved in signaling pathways by ubiquitinating key signaling molecules .

Recombinant UBE2L3 is produced using recombinant DNA technology, allowing for the study and application of this enzyme in various research and therapeutic contexts. It is used in biochemical assays to understand its function and interactions with other proteins .