PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17869481-4	2007	The N-SH3 domain of Grb2 is linked to a proline-rich sequence of the C2 domain of PLC-gamma1, PLC-gamma1 itself is linked, through its SH3 domain, to the C-terminal proline-rich region of Sos.	Proline	40-47	phospholipase C gamma 1	Homo sapiens	82-92	
20544725-1	2010	The constitutive interaction between the P1 domain (a 67-amino-acid functional domain within the proline-rich region) of SLP76 and the SH3 domain of phospholipase Cgamma1 (PLCgamma1) has been shown.	Proline	97-104	phospholipase C gamma 1	Homo sapiens	149-170	
17869481-4	2007	The N-SH3 domain of Grb2 is linked to a proline-rich sequence of the C2 domain of PLC-gamma1, PLC-gamma1 itself is linked, through its SH3 domain, to the C-terminal proline-rich region of Sos.	Proline	40-47	phospholipase C gamma 1	Homo sapiens	94-104	
17869481-4	2007	The N-SH3 domain of Grb2 is linked to a proline-rich sequence of the C2 domain of PLC-gamma1, PLC-gamma1 itself is linked, through its SH3 domain, to the C-terminal proline-rich region of Sos.	Proline	165-172	phospholipase C gamma 1	Homo sapiens	82-92	
17869481-4	2007	The N-SH3 domain of Grb2 is linked to a proline-rich sequence of the C2 domain of PLC-gamma1, PLC-gamma1 itself is linked, through its SH3 domain, to the C-terminal proline-rich region of Sos.	Proline	165-172	phospholipase C gamma 1	Homo sapiens	94-104	
16525023-6	2006	We demonstrated that the interaction is mediated by the binding of PLC-gamma1 Src homology (SH) 3 domain to Akt proline-rich motifs.	Proline	112-119	phospholipase C gamma 1	Homo sapiens	67-77	
16525023-7	2006	We also provide a novel model to depict how the interaction between PLC-gamma1 SH3 domain and Akt proline-rich motifs is dependent on EGF stimulation.	Proline	98-105	phospholipase C gamma 1	Homo sapiens	68-78	
16525023-8	2006	In this model, phosphorylation of PLC-gamma1 Y783 by EGF causes the conformational change of PLC-gamma1 to allow the interaction of its SH3 domain with Akt proline-rich motifs.	Proline	156-163	phospholipase C gamma 1	Homo sapiens	34-44	
16525023-8	2006	In this model, phosphorylation of PLC-gamma1 Y783 by EGF causes the conformational change of PLC-gamma1 to allow the interaction of its SH3 domain with Akt proline-rich motifs.	Proline	156-163	phospholipase C gamma 1	Homo sapiens	93-103	
15607032-9	2004	Together, our data reveal that the amino acid residues Pro(500) and His(503) are critical for binding of PLC-gamma1 to one of its substrates, PI(4,5)P(2) in the membrane.	Proline	55-58	phospholipase C gamma 1	Homo sapiens	105-115	
11390650-8	2001	The adjacent Gads-binding domain of SLP-76, also within the proline-rich region, mediates inducible recruitment of SLP-76 to a PLC-gamma1-containing complex via the recruitment of both PLC-gamma1 and Gads to another cell-type-specific adapter, LAT.	Proline	60-67	phospholipase C gamma 1	Homo sapiens	127-137	
12941616-4	2003	Additional data indicate that the SH3 domain of PLCgamma1 binds to both canonical and noncanonical SH3 domain-binding sites in the proline-rich region of c-Cbl.	Proline	131-138	phospholipase C gamma 1	Homo sapiens	48-57	
11390650-8	2001	The adjacent Gads-binding domain of SLP-76, also within the proline-rich region, mediates inducible recruitment of SLP-76 to a PLC-gamma1-containing complex via the recruitment of both PLC-gamma1 and Gads to another cell-type-specific adapter, LAT.	Proline	60-67	phospholipase C gamma 1	Homo sapiens	185-195	
9712732-6	1998	The interaction of this extended PLCgamma1 SH3 domain fusion protein with Cbl was shown to depend entirely upon the interaction of the domain with a proline-rich motif in Cbl, ruling out the possibility that amino acids adjacent to the core SH3 domain of PLCgamma1 provide independent Cbl binding.	Proline	149-156	phospholipase C gamma 1	Homo sapiens	33-42	
10940929-3	2000	We observed association between the PLCgamma1-SH3 domain and the human Ras guanine nucleotide exchange factor son-of-sevenless-2 (hSos2) through a proline-rich domain interaction.	Proline	147-154	phospholipase C gamma 1	Homo sapiens	36-45	
10913276-5	2000	The carboxyl-terminal proline-rich domain of SOS1 is involved in the interaction with the PLC-gamma1 SH3 domain.	Proline	22-29	phospholipase C gamma 1	Homo sapiens	90-100	
7876130-4	1995	We show that the residues 4 and 5 amino acids COOH-terminal to Tyr1021 (+4 Leu and +5 Pro) are required for efficient PLC-gamma 1 binding, and that their replacement with the corresponding residues from a phosphatidylinositol 3"-kinase binding site abrogates stable association with PLC-gamma 1.	Proline	86-89	phospholipase C gamma 1	Homo sapiens	118-129	
7876130-4	1995	We show that the residues 4 and 5 amino acids COOH-terminal to Tyr1021 (+4 Leu and +5 Pro) are required for efficient PLC-gamma 1 binding, and that their replacement with the corresponding residues from a phosphatidylinositol 3"-kinase binding site abrogates stable association with PLC-gamma 1.	Proline	86-89	phospholipase C gamma 1	Homo sapiens	283-294