PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25447263-2	2015	We have crystallized the complex between the SH3 domain of the c-Src tyrosine kinase and the C-terminal proline rich motif of the NS5A protein (A349PPIPPPRRKR359).	Proline	104-111	C-terminal Src kinase	Homo sapiens	63-84	
25447263-6	2015	Our results show the interaction of the SH3 domain of the c-Src tyrosine kinase with a proline rich motif in the NS5A protein and point to their potential interaction in vivo.	Proline	87-94	C-terminal Src kinase	Homo sapiens	58-79	
15208781-4	2004	We show that the risk allele, which is present in approximately 17% of white individuals from the general population and in approximately 28% of white individuals with RA, disrupts the P1 proline-rich motif that is important for interaction with Csk, potentially altering these proteins" normal function as negative regulators of T-cell activation.	Proline	188-195	C-terminal Src kinase	Homo sapiens	246-249	
10601992-1	1999	The proline-, glutamic acid-, serine- and threonine-enriched protein tyrosine phosphatase PEP, which is expressed primarily in hematopoietic cells, was recently discovered to be physically associated with the 50-kDa cytosolic protein tyrosine kinase (PTK) Csk, an important suppressor of Src family PTK, including Lck and Fyn in T cells.	Proline	4-11	C-terminal Src kinase	Homo sapiens	256-259	
11685249-1	2001	C-terminal Src kinase (Csk) takes part in a highly specific, high affinity interaction via its Src homology 3 (SH3) domain with the proline-enriched tyrosine phosphatase PEP in hematopoietic cells.	Proline	132-139	C-terminal Src kinase	Homo sapiens	0-21	
11685249-1	2001	C-terminal Src kinase (Csk) takes part in a highly specific, high affinity interaction via its Src homology 3 (SH3) domain with the proline-enriched tyrosine phosphatase PEP in hematopoietic cells.	Proline	132-139	C-terminal Src kinase	Homo sapiens	23-26	
11685249-2	2001	The solution structure of the Csk-SH3 domain in complex with a 25-residue peptide from the Pro/Glu/Ser/Thr-rich (PEST) domain of PEP reveals the basis for this specific peptide recognition motif involving an SH3 domain.	Proline	91-94	C-terminal Src kinase	Homo sapiens	30-33	
11685249-3	2001	Three residues, Ala 40, Thr 42 and Lys 43, in the SH3 domain of Csk specifically recognize two hydrophobic residues, Ile 625 and Val 626, in the proline-rich sequence of the PEST domain of PEP.	Proline	145-152	C-terminal Src kinase	Homo sapiens	64-67	
9582365-2	1998	This interaction was shown to involve the Src homology 3 (SH3) region of Csk and a proline-rich sequence of PEP termed P1 (SRRTDDEIPPPLPERTPESFIVVEE).	Proline	83-90	C-terminal Src kinase	Homo sapiens	73-76