PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
7599134-5	1995	Consensus sequences (CSs) of the ATIII N-glycosylation sites are N-X-S for 135 and N-X-T for 96, 155, and 192.	n-x-t	83-88	serpin family C member 1	Homo sapiens	33-38
7599134-6	1995	On the basis of database and in vitro glycosylation studies suggesting that N-X-S CSs are utilized less efficiently than N-X-T CSs, we hypothesized that the beta-ATIII isoform might result from inefficient core glycosylation of the N135 N-X-S CS due to the presence of a serine, rather than a threonine, in the third position.	n-x-t	121-126	serpin family C member 1	Homo sapiens	162-167
11580295-1	2001	The oligosaccharyltransferase (OST) preferentially utilizes the fully assembled dolichol-linked oligosaccharide Glc(3)Man(9)GlcNAc(2)-PP-Dol as the donor for N-linked glycosylation of asparagine residues in N-X-T/S consensus sites in newly synthesized proteins.	n-x-t	207-212	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	4-29
11580295-1	2001	The oligosaccharyltransferase (OST) preferentially utilizes the fully assembled dolichol-linked oligosaccharide Glc(3)Man(9)GlcNAc(2)-PP-Dol as the donor for N-linked glycosylation of asparagine residues in N-X-T/S consensus sites in newly synthesized proteins.	n-x-t	207-212	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	31-34