Ubiquitin-conjugating enzyme E2 A (UBE2A)

Ubiquitin-conjugating enzyme E2 A (UBE2A) is a member of the E2 ubiquitin-conjugating enzyme family involved in the transfer of ubiquitin from the E1 activating enzyme to substrate proteins, usually in concert with an E3 ubiquitin ligase[1][3]. UBE2A mediates monoubiquitination of key proteins, such as histone H2B, influencing transcriptional activation, DNA repair, and cell cycle control[1][3]. It also interacts with various E3 ligases (e.g., RNF20/40, Parkin, UBR4) and is essential for maintaining genomic and mitochondrial integrity[1][3][4]. Disruptive mutations in UBE2A cause X-linked intellectual disability characterized by cognitive deficits, seizures, and systemic anomalies, due to impaired neuronal development and deficient DNA repair or mitophagy[1][2]. UBE2A’s unique catalytic properties, with high intrinsic aminolysis activity, underlie its distinct role among E2 enzymes[2][4]. Clinically, it is not a direct therapeutic target but is important for understanding neurodevelopmental disorders and could be implicated in future research on protein quality control and genomic stability.

Other names

UBE2ARAD6AHR6AhHR6AUBC2HHR6AE2 ubiquitin-conjugating enzyme ARAD6 homolog AUbiquitin carrier protein AUbiquitin-protein ligase AMRXS30MRXSNubiquitin-conjugating enzyme E2A

In the context of therapeutic approaches (research, not clinic), hypothetical mechanisms include inhibition or modulation of E2 enzymatic activity, influencing ubiquitin transfer to target proteins, thereby altering protein degradation, DNA repair, or transcriptional outcomes[1][3].