PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
31108204-9	2019	Fatty acid pattern analyses following a PUFA-free cultivation and enzymatic characterization of six selected fat-2 or fat-1 like desaturases in yeast confirmed the findings from the genetic approaches.	Fatty Acids	0-10	Pcs60p	Saccharomyces cerevisiae S288C	109-114
26019148-4	2015	However, FAT2-FAT4 deletion mutants did not show any growth defects, suggesting that FAT1 and FAA1 are involved in the activation of fatty acids produced during the metabolism of n-alkanes.	Fatty Acids	133-144	Pcs60p	Saccharomyces cerevisiae S288C	9-13
26019148-4	2015	However, FAT2-FAT4 deletion mutants did not show any growth defects, suggesting that FAT1 and FAA1 are involved in the activation of fatty acids produced during the metabolism of n-alkanes.	n-alkanes	179-188	Pcs60p	Saccharomyces cerevisiae S288C	9-13
8841414-9	1996	Expression of Pcs60p is highly inducible by oleic acid, however, the protein is dispensable for growth on oleic acid as single carbon source.	Oleic Acid	44-54	Pcs60p	Saccharomyces cerevisiae S288C	14-20
8841414-9	1996	Expression of Pcs60p is highly inducible by oleic acid, however, the protein is dispensable for growth on oleic acid as single carbon source.	Oleic Acid	106-116	Pcs60p	Saccharomyces cerevisiae S288C	14-20
8841414-9	1996	Expression of Pcs60p is highly inducible by oleic acid, however, the protein is dispensable for growth on oleic acid as single carbon source.	Carbon	127-133	Pcs60p	Saccharomyces cerevisiae S288C	14-20
8841414-10	1996	Pcs60p belongs to the family of proteins which act via an ATP-dependent covalent binding of AMP to their substrates and shows the highest degree of similarity to the Escherichia coli long chain acyl-CoA synthetase.	Adenosine Triphosphate	58-61	Pcs60p	Saccharomyces cerevisiae S288C	0-6
8841414-10	1996	Pcs60p belongs to the family of proteins which act via an ATP-dependent covalent binding of AMP to their substrates and shows the highest degree of similarity to the Escherichia coli long chain acyl-CoA synthetase.	Adenosine Monophosphate	92-95	Pcs60p	Saccharomyces cerevisiae S288C	0-6
26359497-8	2015	Interestingly, Pcs60p lacking its C-terminal tripeptide sequence was efficiently cross-linked to the same regions of Pex5p.	tripeptide K-26	45-55	Pcs60p	Saccharomyces cerevisiae S288C	15-21
26359497-11	2015	Our data indicate that Pcs60p contains a second contact site for its receptor Pex5p, beyond the C-terminal tripeptide.	tripeptide K-26	107-117	Pcs60p	Saccharomyces cerevisiae S288C	23-29