Polypeptide N-acetylgalactosaminyltransferase 17 (GALNT17)

Polypeptide N-acetylgalactosaminyltransferase 17 is an enzyme that catalyzes the first step of O-linked oligosaccharide biosynthesis. It transfers an N-acetyl-D-galactosamine residue from UDP-GalNAc to serine or threonine residues on target proteins, a modification important for protein function and cell signaling. The gene encoding this enzyme is located near the region commonly deleted in Williams-Beuren syndrome and may play a role in protein membrane trafficking and metabolism of proteins. No directly identified small-molecule drugs or clinical inhibitors are listed for this enzyme. Its mutation or deletion is implicated in the genomic context of Williams-Beuren syndrome, contributing likely to the syndrome's multisystem developmental features, but the precise pathophysiological roles are not fully characterized. Typically, this enzyme's activity is associated with post-translational modification rather than as a direct drug target or biomarker.

Other names

PpGalNAc-T17GalNAc-T5LGalNAc-T19GalNAc-T17GALNTL3WBSCR17UDP-GalNAc:Polypeptide N-acetylgalactosaminyltransferase-Like Protein 3Protein-UDP Acetylgalactosaminyltransferase-Like Protein 3Williams-Beuren syndrome chromosomal region 17 proteinPolypeptide N-acetylgalactosaminyltransferase-Like 3Williams-Beuren syndrome chromosome region 17Polypeptide GalNAc Transferase-Like Protein 3Polypeptide GalNAc Transferase 3Pp-GaNTase-Like Protein 3GalNAc-T-Like Protein 3EC 2.4.1.41UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 16Putative Polypeptide N-acetylgalactosaminyltransferase-Like Protein 3Polypeptide N-acetylgalactosaminyltransferase WBSCR17Pp-GalNAc-Transferase 20GALNACT17GALNT16GALNT20