PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9201996-3	1997	We chose the sequence PDAASAAP from human erythropoietin (hEPO) for further systematic substitutions because it accepted GalNAc and was a fairly simple sequence consisting only of four kinds of amino acids.	N-acetylgalactosaminuronic acid	121-127	erythropoietin	Homo sapiens	42-56	
8460945-4	1993	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.	N-acetylgalactosaminuronic acid	138-144	erythropoietin	Homo sapiens	48-62	
18083109-0	2008	Monosialylated biantennary N-glycoforms containing GalNAc-GlcNAc antennae predominate when human EPO is expressed in goat milk.	N-acetylgalactosaminuronic acid	51-57	erythropoietin	Homo sapiens	97-100	
8254121-7	1993	When the incubation time was extended, serine in the EPO-based peptide was found to incorporate GalNAc at a low level, in contrast to the serine-containing HVF peptide, which did not glycosylate at all.	N-acetylgalactosaminuronic acid	96-102	erythropoietin	Homo sapiens	53-56