UBE2D1 Protein, Human (GST)

The UBE2D1 protein plays a pivotal role in cellular processes by accepting ubiquitin from the E1 complex and facilitating its covalent attachment to diverse proteins (source). In vitro, UBE2D1 demonstrates a catalytic preference for 'Lys-48'-linked polyubiquitination, showcasing its versatility in modifying target proteins (source). Functioning as a key mediator in the selective degradation of short-lived and aberrant proteins, UBE2D1 also participates in the E6/E6-AP-induced ubiquitination of p53/TP53. Moreover, it facilitates the ubiquitination of PEX5 and orchestrates the auto-ubiquitination of STUB1, TRAF6, and TRIM63/MURF1 (sources). UBE2D1 exhibits the capability to ubiquitinate STUB1-associated HSP90AB1 in vitro, underscoring its involvement in intricate cellular pathways (source). Notably, UBE2D1 lacks inherent specificity for any particular lysine residue of ubiquitin, highlighting its dynamic nature in ubiquitin modification processes (source). Its essential role in viral activation of IRF3 and mediation of the polyubiquitination of CYP3A4 further emphasizes UBE2D1's multifaceted contributions to cellular function (sources).