PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9570517-0	1998	The amino-terminal Src homology 2 domain of phospholipase C gamma 1 is essential for TCR-induced tyrosine phosphorylation of phospholipase C gamma 1.	Tyrosine	97-105	phospholipase C gamma 1	Homo sapiens	44-67	
9570517-0	1998	The amino-terminal Src homology 2 domain of phospholipase C gamma 1 is essential for TCR-induced tyrosine phosphorylation of phospholipase C gamma 1.	Tyrosine	97-105	phospholipase C gamma 1	Homo sapiens	125-148	
9570517-1	1998	TCR engagement activates phospholipase C gamma 1 (PLC gamma 1) via a tyrosine phosphorylation-dependent mechanism.	Tyrosine	69-77	phospholipase C gamma 1	Homo sapiens	25-48	
9570517-1	1998	TCR engagement activates phospholipase C gamma 1 (PLC gamma 1) via a tyrosine phosphorylation-dependent mechanism.	Tyrosine	69-77	phospholipase C gamma 1	Homo sapiens	50-61	
9570517-2	1998	PLC gamma 1 contains a pair of Src homology 2 (SH2) domains whose function is that of promoting protein interactions by binding phosphorylated tyrosine and adjacent amino acids.	Tyrosine	143-151	phospholipase C gamma 1	Homo sapiens	0-11	
9570517-4	1998	Mutation of the amino-terminal SH2 domain (SH2(N) domain) resulted in defective tyrosine phosphorylation of PLC gamma 1 in response to TCR/CD3 perturbation.	Tyrosine	80-88	phospholipase C gamma 1	Homo sapiens	108-119	
9570517-8	1998	In contrast to TCR/CD3 ligation, treatment of cells with pervanadate induced tyrosine phosphorylation of either PLC gamma 1 SH2(N) or SH2(C) domain mutants to a level comparable with that of the wild-type protein, indicating that pervanadate treatment induces an alternate mechanism of PLC gamma 1 phosphorylation.	Tyrosine	77-85	phospholipase C gamma 1	Homo sapiens	112-123