UGT2B17 (UDP glucuronosyltransferase family 2 member B17) is a phase II metabolic enzyme that catalyzes the glucuronidation of endogenous steroid hormones and xenobiotics to facilitate their excretion 1. The enzyme demonstrates high substrate promiscuity, metabolizing 23 out of 96 tested FDA-approved drugs and steroids, particularly alcohols and carboxylic acids, with significant activity in intestinal tissue 2. UGT2B17 plays a crucial role in androgen metabolism by glucuronidating testosterone, dihydrotestosterone, androsterone, and androstane-3α-diol, converting them into inactive, excretable metabolites 3. In prostate cancer, the enzyme exhibits complex regulatory mechanisms, being negatively regulated by miR-376c at the post-transcriptional level 4 and transcriptionally down-regulated by dihydrotestosterone and epidermal growth factor 5. Paradoxically, UGT2B17 is upregulated in castration-resistant prostate cancer, where it acquires oncogenic functions beyond androgen catabolism, including modulation of protein-folding pathways and regulation of cell division-associated transcription 6. The gene exhibits high interindividual variability due to deletion polymorphisms and serves as a minor histocompatibility antigen presented by multiple HLA alleles 7. These diverse functions make UGT2B17 clinically significant for drug metabolism, hormone regulation, and cancer progression.