PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18832348-5	2008	We next show that the Xrs2-Lif1 interaction depends on Xrs2 FHA residues (R32, S47, R48, and K75) analogous to those known in other proteins to contact phosphorylated threonines.	Threonine	167-177	Lif1p	Saccharomyces cerevisiae S288C	27-31	
18832348-6	2008	Two potential target threonines in Lif1 (T417 and T387) were inferred by identifying regions similar to a site in the human Lif1 homolog, XRCC4, known to be bound by the FHA domain of polynucleotide kinase.	Threonine	21-31	Lif1p	Saccharomyces cerevisiae S288C	35-39	
18832348-6	2008	Two potential target threonines in Lif1 (T417 and T387) were inferred by identifying regions similar to a site in the human Lif1 homolog, XRCC4, known to be bound by the FHA domain of polynucleotide kinase.	Threonine	21-31	Lif1p	Saccharomyces cerevisiae S288C	124-128	
18832348-7	2008	Mutating these threonines, especially T417, abolished the Xrs2-Lif1 interaction and impaired NHEJ epistatically with Xrs2 FHA mutation.	Threonine	15-25	Lif1p	Saccharomyces cerevisiae S288C	63-67