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Ankyrin repeat and SOCS box protein 3 (ASB3) is an intracellular protein composed of an N-terminal ankyrin repeat region (typically 11–12 repeats) and a C-terminal SOCS box domain. ASB3 acts as the substrate recognition component in ECS-type cullin-RING E3 ubiquitin ligase complexes, facilitating the ubiquitination and proteasomal degradation of target proteins, most notably tumor necrosis factor receptor 2 (TNF-R2). By promoting the breakdown of TNF-R2, ASB3 negatively regulates the JNK signaling pathway and apoptosis in response to TNF-α, as well as influencing other cell signaling and immune processes. ASB3 is implicated as a negative regulator of inflammatory signaling, a modulator in cancer biology, and possibly involved in other disease processes. There are no clinically approved drugs or validated biomarkers directly targeting ASB3 currently reported.
Inhibition of TNF-R2-mediated cell signaling via substrate-targeted ubiquitination and degradation; Regulation of antiviral and inflammatory pathways by mediating degradation of MAVS and TRAF6
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