ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 1 (ST6GALNAC1)

ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 1 (ST6GALNAC1) is a protein-coding enzyme belonging to the sialyltransferase family. It catalyzes the transfer of sialic acid in an alpha-2,6 linkage to O-linked N-acetylgalactosamine (GalNAc) residues, primarily on mucins. This glycosylation process modifies protein function and cellular interactions. The enzyme is responsible for the biosynthesis of the sialyl-Tn antigen, a cancer-associated glycan found in many tumors and some inflammatory diseases[2][4]. Regulation of ST6GALNAC1—such as by androgen receptor in prostate cancer—can dynamically alter glycosylation patterns, thus influencing cell adhesion, phenotype, and tumor progression[4]. Manipulation of ST6GALNAC1 expression or activity impacts the formation of biomarkers like sialyl-Tn and could present a therapeutic opportunity in malignancy and inflammatory disease.

Other names

Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1ST6GALNAC1SIAT7AST6GalNAc-IST6GalNAcIhST6GalNAc-IST6GalNAc ISialyltransferase 7AGalNAc alpha-2,6-sialyltransferase ISIAT7-A

For any drugs/treatments: inhibition or modulation of sialyltransferase activity, leading to changes in glycosylation patterns on proteins, especially mucins (no specific drugs currently cited)