UBE2A Human

Ubiquitin Conjugating Enzyme E2A, also known as UBE2A, is a crucial component of the ubiquitination pathway, which is essential for regulating protein degradation and maintaining cellular homeostasis. UBE2A is a human recombinant enzyme that plays a pivotal role in the second step of the ubiquitination process, where it acts as a ubiquitin carrier, transferring ubiquitin from the E1 activating enzyme to the E3 ligase enzyme .

UBE2A is characterized by its highly conserved ubiquitin-conjugating (UBC) domain, which is responsible for its enzymatic activity. The enzyme’s structure allows it to interact with both the E1 activating enzyme and the E3 ligase, facilitating the transfer of ubiquitin to target proteins. This process is critical for tagging proteins for degradation via the proteasome, thereby regulating various cellular processes such as cell cycle progression, DNA repair, and response to stress .

The ubiquitination pathway, in which UBE2A is a central player, is vital for controlling protein turnover and quality control within cells. Dysregulation of this pathway can lead to various diseases, including cancer, neurodegenerative disorders, and immune system dysfunctions. UBE2A, in particular, has been implicated in several pathophysiological conditions due to its role in protein degradation and cellular regulation .

Recent studies have explored the potential of UBE2A in targeted protein degradation strategies. For instance, chimeric human E2 ubiquitin-conjugating enzymes have been engineered to direct specific proteins to the ubiquitination machinery, enhancing their degradation. This approach, known as Proteolysis-Targeting Chimeras (PROTACs), leverages the natural role of UBE2A in the ubiquitin-proteasome system to selectively degrade target proteins, offering promising therapeutic avenues for diseases characterized by aberrant protein accumulation .