ST6GAL2
ST6GAL2, or beta-galactoside alpha-2,6-sialyltransferase 2, is a human gene encoding a Golgi-resident glycosyltransferase that catalyzes the transfer of sialic acid to galactose residues in alpha-2,6 linkage on N- and O-glycans and glycolipids. The enzyme uses CMP-Neu5Ac as the donor substrate and contributes to the biosynthesis of sialylated glycoconjugates that shape the cell surface glycome. ST6GAL2 is categorized in the GT29 family of glycosyltransferases and is closely related to ST6GAL1, another alpha-2,6-sialyltransferase.
Protein structure and localization: ST6GAL2 is a type II membrane protein with a short cytoplasmic N-terminus,
Expression and function: ST6GAL2 transcripts have been detected in various tissues, with expression patterns that differ
Clinical and research relevance: Altered ST6GAL2 expression has been reported in certain cancers and inflammatory conditions,