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Polypeptide N-acetylgalactosaminyltransferase 18 (GALNT18) is a member of the GALNT family of enzymes responsible for initiating O-linked glycosylation of proteins by transferring N-acetyl-D-galactosamine (GalNAc) residues to serine or threonine residues on polypeptides[2][5][6]. This process occurs in the Golgi membrane and plays a critical role in modifying protein function and cellular signaling. GALNT18 exhibits polypeptide N-acetylgalactosaminyltransferase activity and is predicted to have carbohydrate and metal ion binding properties[3]. As of now, there are no drugs or clinical biomarkers specifically connected to GALNT18, nor are there documented safety concerns or direct disease roles. Its broader biological impact may be inferred from general roles of protein O-glycosylation in health and disease[2][5][6].
No mechanism described for drug action targeting GALNT18; general mechanism is transfer of GalNAc to polypeptides
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