ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 3 (ST6GALNAC3)

ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 3 (ST6GALNAC3) is a type II transmembrane sialyltransferase enzyme that catalyzes the transfer of sialic acid in an α2,6 linkage specifically to N-acetylgalactosamine residues on glycolipids and O-linked glycoproteins[1][3]. It is part of the glycosyltransferase family and shows high substrate specificity, with substantial expression primarily in the brain and kidney[1][2][3]. Functionally, ST6GALNAC3 plays a key role in the regulation of sialylated glycoconjugates in neural and renal tissues, mediates ganglioside biosynthesis (notably the conversion of GM1b to GD1α), and can influence neural signaling as well as tumor cell proliferation and metastasis[1][2][3]. Genetic variation or epigenetic dysregulation (e.g., promoter hypermethylation) of ST6GALNAC3 has been implicated in prostate cancer, glioblastoma, and neural function traits, highlighting both diagnostic and possible therapeutic relevance[1][2][3].

Other names

ST6GALNACIIISIAT7CPRO7177SIA7CGalNAc alpha-2,6-sialyltransferase IIIST6GalNAcIIISTYSialyltransferase 7CST6GALNAC IIIST6 (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3