PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8416996-1	1993	We have previously shown that two serine residues present in two conserved regions of the bovine cation-independent mannose 6-phosphate receptor (CI-MPR) cytoplasmic domain are phosphorylated in vivo (residues 2421 and 2492 of the full length bovine CI-MPR precursor).	Serine	34-40	insulin like growth factor 2 receptor	Bos taurus	97-144	
8416996-1	1993	We have previously shown that two serine residues present in two conserved regions of the bovine cation-independent mannose 6-phosphate receptor (CI-MPR) cytoplasmic domain are phosphorylated in vivo (residues 2421 and 2492 of the full length bovine CI-MPR precursor).	Serine	34-40	insulin like growth factor 2 receptor	Bos taurus	146-152	
8416996-1	1993	We have previously shown that two serine residues present in two conserved regions of the bovine cation-independent mannose 6-phosphate receptor (CI-MPR) cytoplasmic domain are phosphorylated in vivo (residues 2421 and 2492 of the full length bovine CI-MPR precursor).	Serine	34-40	insulin like growth factor 2 receptor	Bos taurus	250-256	
8416996-2	1993	In this study, we have used CHO cells to investigate the phosphorylation state of these two serines along the different steps of the CI-MPR exocytic and endocytic recycling pathways.	Serine	92-99	insulin like growth factor 2 receptor	Bos taurus	133-139	
8416996-3	1993	Transport and phosphorylation of the CI-MPR in the biosynthetic pathway were examined using deoxymannojirimycin (dMM), a specific inhibitor of the cis-Golgi processing enzyme alpha-mannosidase I which leads to the accumulation of N-linked high mannose oligosaccharides on glycoproteins.	1-Deoxynojirimycin	92-111	insulin like growth factor 2 receptor	Bos taurus	37-43	
8416996-3	1993	Transport and phosphorylation of the CI-MPR in the biosynthetic pathway were examined using deoxymannojirimycin (dMM), a specific inhibitor of the cis-Golgi processing enzyme alpha-mannosidase I which leads to the accumulation of N-linked high mannose oligosaccharides on glycoproteins.	dimethylmyleran	113-116	insulin like growth factor 2 receptor	Bos taurus	37-43	
8416996-3	1993	Transport and phosphorylation of the CI-MPR in the biosynthetic pathway were examined using deoxymannojirimycin (dMM), a specific inhibitor of the cis-Golgi processing enzyme alpha-mannosidase I which leads to the accumulation of N-linked high mannose oligosaccharides on glycoproteins.	n-linked high mannose oligosaccharides	230-268	insulin like growth factor 2 receptor	Bos taurus	37-43	
8416996-4	1993	Upon removal of dMM, normal processing to complex-type oligosaccharides (galactosylation and then sialylation) occurs on the newly synthesized glycoproteins, including the CI-MPR which could then be purified and analyzed on lectin affinity columns.	dimethylmyleran	16-19	insulin like growth factor 2 receptor	Bos taurus	172-178	
8416996-4	1993	Upon removal of dMM, normal processing to complex-type oligosaccharides (galactosylation and then sialylation) occurs on the newly synthesized glycoproteins, including the CI-MPR which could then be purified and analyzed on lectin affinity columns.	Oligosaccharides	55-71	insulin like growth factor 2 receptor	Bos taurus	172-178	
8416996-5	1993	Phosphorylation of the newly synthesized CI-MPR was concomitant with the sialylation of its oligosaccharides and appeared as a major albeit transient modification.	Oligosaccharides	92-108	insulin like growth factor 2 receptor	Bos taurus	41-47	
8416996-10	1993	Collectively, these results indicate that phosphorylation of the two serines in the CI-MPR cytoplasmic domain is associated with a single step of transport of its recycling pathways and occurs when this receptor is in the trans-Golgi network and/or has left this compartment via clathrin-coated vesicles.	Serine	69-76	insulin like growth factor 2 receptor	Bos taurus	84-90