Carbohydrate Sulfotransferase 2 (CHST2)

N-acetylglucosamine-6-O-sulfotransferases, such as CHST2, catalyze the transfer of sulfate from 3-prime-phosphoadenosine 5-prime-phosphosulfate (PAPS) to position 6 of a nonreducing N-acetylglucosamine (GlcNAc) residue.The predicted 530-amino acid CHST2 protein contains a hydrophobic region in the N terminus that may function as a transmembrane domain for a type II protein or as a Golgi retention signal.

These authors reported that GlcNAc-6-O-sulfotransferase cDNAs could be translated to yield a deduced 484-amino acid protein as well as a longer isoform. Northern blot analysis detected expression of the major 3.6-kb GlcNAc-6-O-sulfotransferase mRNA in all tissues tested.