UBE2D2 Human

Ubiquitin Conjugating Enzyme E2D2, also known as UBE2D2, is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme plays a crucial role in the ubiquitination process, which is essential for the regulation of protein turnover and various cellular processes in eukaryotic cells .

Ubiquitination is a post-translational modification where ubiquitin, a small regulatory protein, is attached to a substrate protein. This process involves three main steps:

1. Activation: Ubiquitin is activated by an E1 ubiquitin-activating enzyme.
2. Conjugation: The activated ubiquitin is transferred to an E2 ubiquitin-conjugating enzyme, such as UBE2D2.
3. Ligation: The E3 ubiquitin ligase facilitates the transfer of ubiquitin from the E2 enzyme to the target protein .

UBE2D2 is responsible for the conjugation step in the ubiquitination process. It acts as an intermediary that transfers ubiquitin from the E1 enzyme to the E3 ligase, which then attaches ubiquitin to the substrate protein. This enzyme is involved in the ubiquitination of several key proteins, including the tumor-suppressor protein p53 and IkB-alpha .

The ubiquitination process, mediated by UBE2D2, is critical for maintaining cellular homeostasis. It regulates protein degradation, cell cycle progression, DNA repair, and signal transduction. Dysregulation of ubiquitination can lead to various diseases, including cancer, neurodegenerative disorders, and immune system dysfunctions .

UBE2D2 has been extensively studied for its role in targeted protein degradation. Researchers have developed chimeric E2 enzymes to enhance the degradation of specific proteins, providing a potential therapeutic approach for diseases caused by protein dysregulation . Additionally, UBE2D2 is used in various in vitro assays to study the ubiquitination process and its implications in different biological pathways .