PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10372132-4	1999	Mutation of each of the 8 tyrosine residues in the cytoplasmic domain of the human GMR beta to phenylalanine (GMR beta-F8) reduced tyrosine phosphorylation of GMR beta, SHP2 and SHC, but not JAK2 or STAT5.	Phenylalanine	95-108	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	169-173	
16702225-4	2006	These studies reveal that binding of a pY peptide to the N-SH2 domain of SHP-2 is greatly enhanced by a large hydrophobic residue (Trp, Tyr, Met, or Phe) at the pY+4 and/or pY+5 positions, whereas binding to SHP-1 N-SH2 domain is enhanced by either hydrophobic or positively charged residues (Arg, Lys, or His) at these positions.	Phenylalanine	149-152	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	73-78	
15170389-4	2004	Expression of the Gab2 Tyr-614-->Phe (Y614F) mutant, defective in SHP-2 association, prevents ERK (extracellular-signal-regulated kinase) activation and expression of a luciferase reporter plasmid driven by the c-fos SRE (serum response element), indicating that interaction of SHP-2 with Gab2 is required for ERK activation in response to IL-2.	Phenylalanine	36-39	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	69-74	
15170389-4	2004	Expression of the Gab2 Tyr-614-->Phe (Y614F) mutant, defective in SHP-2 association, prevents ERK (extracellular-signal-regulated kinase) activation and expression of a luciferase reporter plasmid driven by the c-fos SRE (serum response element), indicating that interaction of SHP-2 with Gab2 is required for ERK activation in response to IL-2.	Phenylalanine	36-39	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	281-286	
30129165-8	2018	The results indicated that the primary variances between SHP2-WT and SHP2-E76K were the different interactions between Glu/Lys 76 and Arg 265, Tyr 80 and Leu 77, Leu 77 and Tyr 81, Thr 73 and Glu 258, Ala 75 and Cys 259, Phe 71 and Tyr 81, Ala 75 and Glu 258, and Tyr 73 and Glu/Lys 76.	Phenylalanine	221-224	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	57-61	
30129165-8	2018	The results indicated that the primary variances between SHP2-WT and SHP2-E76K were the different interactions between Glu/Lys 76 and Arg 265, Tyr 80 and Leu 77, Leu 77 and Tyr 81, Thr 73 and Glu 258, Ala 75 and Cys 259, Phe 71 and Tyr 81, Ala 75 and Glu 258, and Tyr 73 and Glu/Lys 76.	Phenylalanine	221-224	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	69-73	
14560030-7	2003	We have identified Tyr992 of the epidermal growth factor receptor (EGFR) to be one such site, since its mutation to Phe renders the EGFR refractory to the effect of dominant-negative SHP2.	Phenylalanine	116-119	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	183-187	
8622663-3	1996	An SHPTP2 mutant with both C-terminal tyrosyl phosphorylation sites converted to phenylalanine (PTP2YF) was also without effect; moreover, PTP2YF rescued PTP2CS-induced inhibition of EGF-induced Elk-1 transactivation.	Phenylalanine	81-94	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	3-9	
9794795-8	1998	This phosphorylation depends on Tyr-759 in the cytoplasmatic domain of gp130, since a Tyr-759-->Phe exchange abrogates SHP2 activation and in turn leads to elevated and prolonged STAT3 and STAT1 activation as well as enhanced acute-phase protein gene induction.	Phenylalanine	99-102	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	122-126	
8943348-5	1996	In addition, mutating Y720 to phenylalanine dramatically reduced PDGF-dependent tyrosine phosphorylation of SHP-2.	Phenylalanine	30-43	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	108-113