UBE2J2 Human

Ubiquitin-Conjugating Enzyme E2, J2 (UBE2J2) is a significant protein-coding gene involved in the ubiquitination process, a crucial cellular mechanism for protein regulation. This enzyme is part of the E2 ubiquitin-conjugating enzyme family and is located in the membrane of the endoplasmic reticulum .

Ubiquitination is a post-translational modification that regulates various cellular processes, including protein turnover, stress response, cell cycle, organelle synthesis, and intracellular homeostasis . The ubiquitination process involves three main classes of enzymes:

1. E1 Ubiquitin-Activating Enzymes: These enzymes activate ubiquitin using ATP.
2. E2 Ubiquitin-Conjugating Enzymes: These enzymes, including UBE2J2, transfer the activated ubiquitin to substrate proteins.
3. E3 Ubiquitin Ligases: These enzymes facilitate the transfer of ubiquitin from E2 to the substrate protein .

UBE2J2 catalyzes the covalent attachment of ubiquitin to other proteins, playing a role in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD) . It also cooperates with the GATOR2 complex to catalyze ‘Lys-6’-linked ubiquitination of NPRL2 .

UBE2J2 is associated with several diseases, including Parkinson’s Disease and Congenital Myasthenic Syndrome . Its involvement in protein ubiquitination pathways, such as Class I MHC mediated antigen processing and presentation, highlights its importance in cellular function and disease mechanisms .

Research on UBE2J2 and other ubiquitin-conjugating enzymes continues to uncover their roles in various diseases and cellular processes. Understanding the mechanisms of these enzymes can lead to potential therapeutic targets for diseases related to protein misfolding and degradation .