UB2V1 Protein, Human (sf9, His, StrepⅡ)

The UBE2V1 protein, on its own, lacks ubiquitin ligase activity. However, when forming a heterodimer with UBE2N, it catalyzes the synthesis of non-canonical poly-ubiquitin chains linked through Lys-63. This type of poly-ubiquitination activates IKK and does not involve protein degradation by the proteasome. UBE2V1 plays a crucial role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6, and TRAF2, contributing to the transcriptional activation of target genes. Additionally, it participates in cell cycle progression, differentiation, and the error-free DNA repair pathway, enhancing cell survival after DNA damage. Furthermore, UBE2V1 promotes TRIM5 capsid-specific restriction activity, collaborating with UBE2N to generate 'Lys-63'-linked polyubiquitin chains that activate the MAP3K7/TAK1 complex, leading to the induction of NF-kappa-B and MAPK-responsive inflammatory genes. Together with RNF135 and UBE2N, UBE2V1 catalyzes viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI, activating the downstream signaling pathway for interferon beta production. In association with TRAF3IP2 E3 ubiquitin ligase, UBE2V1-UBE2N mediates 'Lys-63'-linked polyubiquitination of TRAF6 in the IL17A-mediated signaling pathway. It forms a heterodimer with UBE2N and interacts with various proteins, including STUB1 and TRAF6, contributing to diverse cellular processes and signaling pathways.