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Ankyrin repeat domain-containing protein 9 (ANKRD9) is a cytosolic protein that contains multiple ankyrin repeats, a structural motif commonly involved in protein–protein interactions[2][1][4]. ANKRD9 acts as a substrate receptor in a cullin-RING ligase (CUL5-based E3 ubiquitin ligase complex), regulating ubiquitination and proteasomal degradation of target proteins, notably IMPDH2, an enzyme critical in GTP biosynthesis[2][5]. ANKRD9 is implicated in various cellular processes including copper ion homeostasis, regulation of cell proliferation, and protein catabolic processes[2][5]. Although variants in ANKRD9 are associated with neuropsychiatric conditions such as drug-induced mental disorders and substance-induced psychosis, there is currently limited direct evidence of therapeutic targeting or biomarker relevance for this protein[2]. Ankyrin repeat domains, including those in ANKRD9, are widely distributed and participate in scaffolding and signaling functions, but ANKRD9 itself has no known enzymatic activity[1][3].
Not applicable (no approved drugs targeting ANKRD9 to date). Theoretically, drugs acting as inhibitors or modulators could alter protein ubiquitination and degradation pathways.
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