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Ankyrin repeat and SOCS box protein 9 (ASB9) is a substrate-recognition component of the Cullin-RING E3 ubiquitin ligase complex, specifically the Elongin-Cullin-SOCS box-type (ECS/CRL5) E3 ligase. It contains an N-terminal intrinsically disordered region, an ankyrin repeat domain that binds substrate proteins, and a C-terminal SOCS box that mediates complex formation with Elongin B/C and Cullin 5. ASB9 binds to creatine kinase with high affinity, targeting it for ubiquitination and subsequent proteasomal degradation, which has roles in energy metabolism, cellular homeostasis, and possibly reproductive physiology[1][2][7][8]. There is currently no evidence of approved therapeutic drugs explicitly targeting ASB9, but its function as a molecular adaptor implicates it in pathways fundamental to cell function and disease.
Ubiquitination of target proteins (e.g., creatine kinase) leading to their proteasomal degradation
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