PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17693598-1	2007	Dal5p has been shown previously to act as an allantoate/ureidosuccinate permease and to play a role in the utilization of certain dipeptides as a nitrogen source in Saccharomyces cerevisiae.	Dipeptides	130-140	allantoate permease	Saccharomyces cerevisiae S288C	0-5	
17693598-2	2007	Here, we provide direct evidence that dipeptides are transported by Dal5p, although the affinity of Dal5p for allantoate and ureidosuccinate is higher than that for dipeptides.	Dipeptides	38-48	allantoate permease	Saccharomyces cerevisiae S288C	68-73	
17693598-2	2007	Here, we provide direct evidence that dipeptides are transported by Dal5p, although the affinity of Dal5p for allantoate and ureidosuccinate is higher than that for dipeptides.	Dipeptides	38-48	allantoate permease	Saccharomyces cerevisiae S288C	100-105	
17693598-2	2007	Here, we provide direct evidence that dipeptides are transported by Dal5p, although the affinity of Dal5p for allantoate and ureidosuccinate is higher than that for dipeptides.	Dipeptides	165-175	allantoate permease	Saccharomyces cerevisiae S288C	68-73	
17693598-4	2007	In contrast to the well-studied di/tripeptide transporter Ptr2p, whose substrate specificity is very broad, Dal5p preferred to transport non-N-end rule dipeptides.	Dipeptides	152-162	allantoate permease	Saccharomyces cerevisiae S288C	108-113	
17693598-9	2007	Toxic dipeptide and uptake assays indicated that either Ptr2p or Dal5p was predominantly used for dipeptide transport in the common laboratory strains S288c and W303, respectively.	Dipeptides	6-15	allantoate permease	Saccharomyces cerevisiae S288C	65-70	
17693598-9	2007	Toxic dipeptide and uptake assays indicated that either Ptr2p or Dal5p was predominantly used for dipeptide transport in the common laboratory strains S288c and W303, respectively.	Dipeptides	98-107	allantoate permease	Saccharomyces cerevisiae S288C	65-70