PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
7957044-3	1994	The a-agglutinin is bound via two S-S bridges (Cys7 and Cys50) to a cell wall component, most probably the gene product of AGA1.	CYS7	47-51	Aga1p	Saccharomyces cerevisiae S288C	123-127
2072914-6	1991	The AGA1 gene was cloned by complementation; the gene sequence indicated that it could encode a protein of 725 amino acids with high serine and threonine content, a putative N-terminal signal sequence, and a C-terminal hydrophobic sequence similar to signals for the attachment to glycosyl phosphatidylinositol anchors.	Serine	133-139	Aga1p	Saccharomyces cerevisiae S288C	4-8
2072914-6	1991	The AGA1 gene was cloned by complementation; the gene sequence indicated that it could encode a protein of 725 amino acids with high serine and threonine content, a putative N-terminal signal sequence, and a C-terminal hydrophobic sequence similar to signals for the attachment to glycosyl phosphatidylinositol anchors.	Threonine	144-153	Aga1p	Saccharomyces cerevisiae S288C	4-8
2072914-6	1991	The AGA1 gene was cloned by complementation; the gene sequence indicated that it could encode a protein of 725 amino acids with high serine and threonine content, a putative N-terminal signal sequence, and a C-terminal hydrophobic sequence similar to signals for the attachment to glycosyl phosphatidylinositol anchors.	Glycosylphosphatidylinositols	281-310	Aga1p	Saccharomyces cerevisiae S288C	4-8
10923021-6	2000	These results proved that the constructed Aga1p-Aga2p fusion protein was enoughly functional for the interaction with the Agalpha1 protein, and that this phenomenon occurred dependent on glucose concentration, but independent of the peptide pheromones secreted by the cells of the opposite mating types.	Glucose	187-194	Aga1p	Saccharomyces cerevisiae S288C	42-47
14555493-5	2003	By studying the yeast sexual adhesin subunit Aga1p, we found that deletion of its signal sequence for GPI addition eliminated its activity, while deletions of different internal domains had various effects on function.	GPI 1046	102-105	Aga1p	Saccharomyces cerevisiae S288C	45-50
14555493-6	2003	Substitution of the Aga1p GPI signal domain with those of other GPI-anchored proteins, a single transmembrane domain, or a cysteine capable of forming a disulfide all produced functional adhesins.	Disulfides	153-162	Aga1p	Saccharomyces cerevisiae S288C	20-25
15976011-2	2005	The available commercial yeast display vector pYD1 (Invitrogen) displays the protein of interest flanked on the N-terminus by Aga2, the disulfide of which binds the myristylated surface membrane protein Aga1.	Disulfides	136-145	Aga1p	Saccharomyces cerevisiae S288C	203-207
11278672-2	2001	Cell wall attachment of Aga2p is mediated through two disulfide bonds to Aga1p (Cappellaro, C., Baldermann, C., Rachel, R., and Tanner, W. (1994) EMBO J.	Disulfides	54-63	Aga1p	Saccharomyces cerevisiae S288C	73-78
11278672-5	2001	Aga2p co-expressed with a 149-residue fragment of Aga1p formed a disulfide-linked complex with specific activity 43-fold higher than Aga2p expressed alone.	Disulfides	65-74	Aga1p	Saccharomyces cerevisiae S288C	50-55
11278672-7	2001	A 30-residue Cys-rich Aga1p fragment was partially active in stabilization of Aga2p activity.	Cysteine	13-16	Aga1p	Saccharomyces cerevisiae S288C	22-27
11278672-9	2001	Thus the roles of Aga1p include both cell wall anchorage and cysteine-dependent conformational restriction of the binding subunit Aga2p.	Cysteine	61-69	Aga1p	Saccharomyces cerevisiae S288C	18-23
10923021-7	2000	Using this system, the role of two disulphide linkages between Aga1p and Aga2p on the binding activity between Aga2p and Aga1p was first evaluated.	disulphide	35-45	Aga1p	Saccharomyces cerevisiae S288C	63-68
10923021-7	2000	Using this system, the role of two disulphide linkages between Aga1p and Aga2p on the binding activity between Aga2p and Aga1p was first evaluated.	disulphide	35-45	Aga1p	Saccharomyces cerevisiae S288C	121-126
10923021-8	2000	Under the treatment by the SH-compound (dithiothreitol), in which Agalpha2p is easily released into the medium from the intact cell surface, the Aga1p and Aga2p fusion protein was a good tool to make clear the role of the disulphide linkages.	Dithiothreitol	40-54	Aga1p	Saccharomyces cerevisiae S288C	145-150
10923021-8	2000	Under the treatment by the SH-compound (dithiothreitol), in which Agalpha2p is easily released into the medium from the intact cell surface, the Aga1p and Aga2p fusion protein was a good tool to make clear the role of the disulphide linkages.	disulphide	222-232	Aga1p	Saccharomyces cerevisiae S288C	145-150