PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22722937-3	2012	Transfer of GalNAc by beta4GalNAc-T3 and beta4GalNAc-T4 to terminal GlcNAc is divalent cation-dependent.	N-acetylgalactosaminuronic acid	12-18	beta-1,4-N-acetyl-galactosaminyltransferase 4	Homo sapiens	41-55	
22722940-3	2012	We characterized how two beta1,4-N-acetylgalactosaminyltransferases, beta4GalNAc-T3 and beta4GalNAc-T4, require the presence of both the peptide recognition motif and the N-linked oligosaccharide acceptors to transfer GalNAc in beta1,4-linkage to GlcNAc in vivo and in vitro.	N-acetylgalactosaminuronic acid	74-80	beta-1,4-N-acetyl-galactosaminyltransferase 4	Homo sapiens	88-102	
22722940-4	2012	We now show that beta4GalNAc-T3 and beta4GalNAc-T4 are able to utilize the same peptide motif to selectively add GalNAc to beta1,6-linked GlcNAc in core 2 O-linked oligosaccharide structures to form Galbeta1,3(GalNAcbeta1,4GlcNAcbeta1,6)GalNAcalphaSer/Thr.	N-acetylgalactosaminuronic acid	22-28	beta-1,4-N-acetyl-galactosaminyltransferase 4	Homo sapiens	36-50	
22722937-7	2012	beta4GalNAc-T3 and beta4GalNAc-T4 have similar but distinct specificities, resulting in a 42-fold difference in the IC(50) for transfer of GalNAc to chimeric glycoprotein substrates by agalacto human chorionic gonadotropin, comprising 29 nM for beta4GalNAc-T3 and 1.2 muM for beta4GalNAc-T4.	N-acetylgalactosaminuronic acid	5-11	beta-1,4-N-acetyl-galactosaminyltransferase 4	Homo sapiens	276-290	
35204696-2	2022	Biosynthesis of the LacdiNAc group was well studied, and two beta4-N-acetylgalactosaminyltransferases, beta4GalNAcT3 and beta4GalNAcT4, have been shown to transfer N-acetylgalactosamine (GalNAc) to N-acetylglucosamine (GlcNAc) of N- and O-glycans in a beta-1,4-linkage.	N-acetylgalactosaminuronic acid	187-193	beta-1,4-N-acetyl-galactosaminyltransferase 4	Homo sapiens	121-134