The UBE2Z gene is located on chromosome 17 at band 17q21.32 and consists of 7 exons . The gene produces two isoforms through alternative splicing . The UBE2Z cDNA spans a length of 3,054 base pairs and encodes a protein of 246 amino acids . The protein contains a conserved ubiquitin-conjugating enzyme E2 domain (UBC domain) at its N-terminal, which is responsible for its catalytic function .
UBE2Z is involved in the second step of protein ubiquitination, a process that tags proteins for degradation by the proteasome . This enzyme participates in various biological processes, including the regulation of apoptosis, protein catabolism, and the modulation of protein activities, interactions, and subcellular localization .
The ubiquitination process involves a multi-step enzymatic pathway. Initially, an ATP-dependent activating enzyme (E1) forms a thiol ester bond with ubiquitin. The ubiquitin is then transferred to a ubiquitin-conjugating enzyme (E2), such as UBE2Z, which subsequently transfers the ubiquitin to a target substrate, either directly or with the help of a ligase enzyme (E3) . In some cases, a further enzyme (E4) may be required for the formation of multiubiquitin chains .
UBE2Z is regulated through various mechanisms, including gene expression, post-translational modifications, and interactions with other proteins. The enzyme’s activity is modulated by its interaction with specific E3 ligases, which determine the substrate specificity and the type of ubiquitin modification .