PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32971290-3	2020	ST6Gal I is a sialyltransferase using activated CMP-sialic acids as donor substrates to catalyze the formation of a alpha2,6-glycosidic bond between the sialic acid residue and the acceptor disaccharide LacNAc.	Disaccharides	190-202	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	0-8	
21098517-3	2011	The sialyltransferase enzyme ST6Gal I transfers sialic acid from CMP-sialic acid to type 2 (Galbeta1,4GlcNAc) free disaccharides or the termini of N- or O-linked oligosaccharides using an alpha2,6-linkage.	Disaccharides	115-128	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	29-37	
12603328-7	2003	Enzymatic assays indicate that the best acceptor substrate of ST6Gal II was the free disaccharide Galbeta1-4GlcNAc structure whereas ST6Gal I preferred Galbeta1-4GlcNAc-R disaccharide sequence linked to a protein.	Disaccharides	85-97	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	62-70