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