PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12847091-6	2003	Enzymatic analysis of the transferase reaction products showed that D4ST-1 far more efficiently transferred sulfate to GalNAc residues in -IdoUA-Gal-NAc-IdoUA-than in -GlcUA-GalNAc-GlcUA-sequences.	N-acetylgalactosaminuronic acid	119-125	carbohydrate sulfotransferase 14	Homo sapiens	68-74	
29976758-3	2018	In vivo, concomitant with epimerization, dermatan 4-O-sulfotransferase 1 (D4ST1) sulfates the GalNAc adjacent to iduronic acid.	N-acetylgalactosaminuronic acid	94-100	carbohydrate sulfotransferase 14	Homo sapiens	41-72	
29976758-3	2018	In vivo, concomitant with epimerization, dermatan 4-O-sulfotransferase 1 (D4ST1) sulfates the GalNAc adjacent to iduronic acid.	N-acetylgalactosaminuronic acid	94-100	carbohydrate sulfotransferase 14	Homo sapiens	74-79	
20533528-4	2010	CHST14 encodes dermatan 4-O-sulfotransferase 1 (D4ST1), which transfers active sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 4 of the N-acetyl-D-galactosamine (GalNAc) residues of dermatan sulfate (DS).	N-acetylgalactosaminuronic acid	177-183	carbohydrate sulfotransferase 14	Homo sapiens	0-6	
20533528-4	2010	CHST14 encodes dermatan 4-O-sulfotransferase 1 (D4ST1), which transfers active sulfate from 3"-phosphoadenosine 5"-phosphosulfate to position 4 of the N-acetyl-D-galactosamine (GalNAc) residues of dermatan sulfate (DS).	N-acetylgalactosaminuronic acid	177-183	carbohydrate sulfotransferase 14	Homo sapiens	48-53	
12847091-1	2003	4-O-Sulfation of GalNAc is a high frequency modification of chondroitin sulfate and dermatan sulfate (DS), and three major GalNAc 4-O-sulfotransferases including dermatan 4-O-sulfotransferase-1 (D4ST-1) and chondroitin 4-O-sulfotransferases-1 and -2 (C4ST-1 and -2) have been identified.	N-acetylgalactosaminuronic acid	17-23	carbohydrate sulfotransferase 14	Homo sapiens	162-193	
12847091-1	2003	4-O-Sulfation of GalNAc is a high frequency modification of chondroitin sulfate and dermatan sulfate (DS), and three major GalNAc 4-O-sulfotransferases including dermatan 4-O-sulfotransferase-1 (D4ST-1) and chondroitin 4-O-sulfotransferases-1 and -2 (C4ST-1 and -2) have been identified.	N-acetylgalactosaminuronic acid	17-23	carbohydrate sulfotransferase 14	Homo sapiens	195-201	
12847091-1	2003	4-O-Sulfation of GalNAc is a high frequency modification of chondroitin sulfate and dermatan sulfate (DS), and three major GalNAc 4-O-sulfotransferases including dermatan 4-O-sulfotransferase-1 (D4ST-1) and chondroitin 4-O-sulfotransferases-1 and -2 (C4ST-1 and -2) have been identified.	N-acetylgalactosaminuronic acid	123-129	carbohydrate sulfotransferase 14	Homo sapiens	162-193	
12847091-6	2003	Enzymatic analysis of the transferase reaction products showed that D4ST-1 far more efficiently transferred sulfate to GalNAc residues in -IdoUA-Gal-NAc-IdoUA-than in -GlcUA-GalNAc-GlcUA-sequences.	N-acetylgalactosaminuronic acid	174-180	carbohydrate sulfotransferase 14	Homo sapiens	68-74	
12847091-8	2003	Structural analysis of the oligosaccharides, which were isolated after chondroitinase AC-I digestion of the 35S-labeled transferase reaction products, revealed for the first time that D4ST-1, as compared with C4ST-1 and C4ST-2, most efficiently utilized GalNAc residues located not only in the sequence -IdoUA-GalNAc-IdoUA- but also in -GlcUA-Gal-NAc-IdoUA- and -IdoUA-GalNAc-GlcUA-.	N-acetylgalactosaminuronic acid	254-260	carbohydrate sulfotransferase 14	Homo sapiens	184-190	
12847091-8	2003	Structural analysis of the oligosaccharides, which were isolated after chondroitinase AC-I digestion of the 35S-labeled transferase reaction products, revealed for the first time that D4ST-1, as compared with C4ST-1 and C4ST-2, most efficiently utilized GalNAc residues located not only in the sequence -IdoUA-GalNAc-IdoUA- but also in -GlcUA-Gal-NAc-IdoUA- and -IdoUA-GalNAc-GlcUA-.	N-acetylgalactosaminuronic acid	310-316	carbohydrate sulfotransferase 14	Homo sapiens	184-190	
12847091-8	2003	Structural analysis of the oligosaccharides, which were isolated after chondroitinase AC-I digestion of the 35S-labeled transferase reaction products, revealed for the first time that D4ST-1, as compared with C4ST-1 and C4ST-2, most efficiently utilized GalNAc residues located not only in the sequence -IdoUA-GalNAc-IdoUA- but also in -GlcUA-Gal-NAc-IdoUA- and -IdoUA-GalNAc-GlcUA-.	N-acetylgalactosaminuronic acid	310-316	carbohydrate sulfotransferase 14	Homo sapiens	184-190	
11470797-6	2001	The specificity of D4ST-1 when assayed in vitro suggests that the addition of sulfate to GalNAc occurs immediately after epimerization of GlcUA to IdoUA.	N-acetylgalactosaminuronic acid	89-95	carbohydrate sulfotransferase 14	Homo sapiens	19-25	
11470797-10	2001	The properties of D4ST-1 indicate that sulfation of the GalNAc moieties in dermatan is mediated by a distinct GalNAc-4-O-sulfotransferase and occurs following epimerization of GlcUA to IdoUA.	N-acetylgalactosaminuronic acid	56-62	carbohydrate sulfotransferase 14	Homo sapiens	18-24