PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27193083-8 2016 Here we report the identification of critical proline residues, Pro213, Pro216, and Pro219, located within the fifth and sixth Pro-X-X-Pro motifs in the proline-rich region of tau, that are important for its binding to fyn. Proline 46-53 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 219-222 29734505-4 2018 By co-immunoprecipitation and anti-phosphotyrosine blotting, we identified proline-rich binding sites for Fyn kinase in the N-terminal, IC-loopi-ii and C-terminal. Proline 75-82 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 106-109 32905906-10 2020 FasL can recruit Fyn via the proline-rich domain leading to the recruitment of ADAP. Proline 29-36 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 17-20 28380689-4 2017 In the membrane context, the xalpha2-peptide interacts with the Fyn-SH3 domain via the proline-rich region and the beta-sheets of Fyn-SH3, with the latter wrapping around the proline-rich region in a form of a clip. Proline 87-94 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 64-67 28380689-4 2017 In the membrane context, the xalpha2-peptide interacts with the Fyn-SH3 domain via the proline-rich region and the beta-sheets of Fyn-SH3, with the latter wrapping around the proline-rich region in a form of a clip. Proline 175-182 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 64-67 27193083-8 2016 Here we report the identification of critical proline residues, Pro213, Pro216, and Pro219, located within the fifth and sixth Pro-X-X-Pro motifs in the proline-rich region of tau, that are important for its binding to fyn. Proline 153-160 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 219-222 22621321-4 2012 In addition, the concepts of proximity-driven catalysis are extended to include modification of the natural Fyn SH3 domain with metallopeptides based on a known proline-rich peptide ligand. Proline 161-168 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 108-111 22868769-3 2012 The 1.5 A resolution crystal structure of a complex between the SH3 domain of the Fyn tyrosine kinase and the C-terminal proline-rich motif of the NS5A-derived peptide APPIPPPRRKR has been solved. Proline 121-128 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 82-85 22868769-7 2012 The proline-rich motif present in the NS5A protein seems to be important for RNA replication and virus assembly, and the promiscuous interaction of the Fyn SH3 domain with the NS5A C-terminal proline-rich peptide found in this crystallographic structure may be important in the virus infection cycle. Proline 4-11 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 152-155 22868769-7 2012 The proline-rich motif present in the NS5A protein seems to be important for RNA replication and virus assembly, and the promiscuous interaction of the Fyn SH3 domain with the NS5A C-terminal proline-rich peptide found in this crystallographic structure may be important in the virus infection cycle. Proline 192-199 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 152-155 22447928-12 2012 Together, these data indicate that the proline-rich Src homology 3 domain-binding motif in TRAF6 interacts directly with activated SFKs to couple LPS engagement of TLR4 to SFK activation and loss of barrier integrity in HMVEC-Ls. Proline 39-46 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 131-134 22447928-8 2012 A cell-permeable decoy peptide corresponding to the same proline-rich motif reduced SFK binding to WT GST-TRAF6 compared with the Pro Ala-substituted peptide. Proline 57-64 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 84-87 16987982-7 2006 In addition, Vpx interacts with the cellular tyrosine kinase Fyn through its C-terminal proline-rich motif. Proline 88-95 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 61-64 22403409-8 2012 Remarkably, the protein-tyrosine kinase Fyn, which binds to the proline-rich RTPPKSP motif conserved in both MAP2 and tau, inhibits the interaction of PP2A/Balpha with either tau or MAP2c. Proline 64-71 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 40-43 19267471-12 2009 The combination of NMR and ITC data sheds light on how the Fyn tyrosine kinase is activated by binding to proline-rich targets, and represents a powerful approach for characterizing transient protein/ligand interactions. Proline 106-113 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 59-62 18301737-3 2008 Previous reports have shown that the formation of this heteromolecular complex involves interactions between a proline rich region of M2 and the Vav1 and Fyn SH3 domains. Proline 111-118 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 154-157 18930841-8 2009 Both phosphorylated FAK residue Y397 and FAK proline-rich domain are involved in Fyn binding. Proline 45-52 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 81-84 17948968-6 2007 The known stabilization of the N-terminal domain of CaM in the context of the intact protein and the known binding affinity of a proline-rich peptide to the SH3 domain in the Fyn construct were successfully quantified using the new protocol. Proline 129-136 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 175-178 12426371-5 2002 NMR analysis shows that the Fyn but not the Lck tyrosine kinase SH3 domain competes with CD2BP2 GYF-domain binding to the same CD2 proline-rich sequence in vitro. Proline 131-138 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 28-31 15615649-2 2005 Mediated by the proline-rich region of tau and the SH3 domain of fyn or src, this interaction has the potential to confer novel cellular activities for tau in the growth cone and in the membrane. Proline 16-23 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 65-68 12426371-6 2002 To test the in vivo significance of this competition, we used co-immunoprecipitation experiments and found that CD2BP2 is the ligand of the membrane-proximal proline-rich tandem repeat of CD2 in detergent-soluble membrane compartments, but is replaced by Fyn SH3 after CD2 is translocated into lipid rafts upon CD2 ectodomain clustering. Proline 158-165 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 255-258 11943772-0 2002 Association of Fyn and Lyn with the proline-rich domain of glycoprotein VI regulates intracellular signaling. Proline 36-43 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 15-18 11943772-2 2002 Molecular cloning of GPVI has revealed the presence of a proline-rich domain in the sequence of GPVI cytoplasmic tail which has the consensus for interaction with the Src homology 3 (SH3) domains of Fyn and Lyn. Proline 57-64 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 199-202 11943772-4 2002 Furthermore, depletion of the proline-rich domain in GPVI (Pro(-)-GPVI) prevented binding of Fyn and Lyn and markedly reduced phosphorylation of FcR gamma-chain in transiently transfected COS-7 cells, but did not affect the association of the gamma-chain with GPVI. Proline 30-37 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 93-96 11943772-7 2002 These findings demonstrate that the proline-rich domain of GPVI mediates the association with Fyn/Lyn via their SH3 domain and that this interaction initiates activation signals through GPVI. Proline 36-43 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 94-97 9763511-5 1998 Here we report that a proline rich sequence in the amino terminus of tau interacts with the SH3 domains of fyn and src non-receptor tyrosine kinases. Proline 22-29 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 107-110 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 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 322-325 10430626-5 1999 Here we demonstrate that Lck and Fyn can be activated by proline motifs in the CD28 and CD2 proteins, respectively. Proline 57-64 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 33-36 9351809-5 1997 Comparison of the bound and unbound Nef structures revealed that a proline-rich motif (Pro-x-x-Pro), which is implicated in SH3 binding, is partially disordered in the absence of the binding partner; this motif only fully adopts a left-handed polyproline type II helix conformation upon complex formation with the Fyn SH3 domain. Proline 67-74 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 314-317 9603925-3 1998 This interaction seems to be mediated by the SH3 domain of Fyn and a proline-rich sequence located in the cytoplasmic domain of CD43. Proline 69-76 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 59-62 9856337-5 1998 In addition, the proline-rich domain of Sos also bound to the SH3 domains of other src-type tyrosine kinases, src and fyn, but not to that of PLC-gamma. Proline 17-24 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 118-121 8961927-0 1996 Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase. Proline 101-108 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 88-91 8955343-4 1996 This genetic screen clearly indicates that the interaction between SH3 domain of Fyn and the proline-rich region (residues: 80-104) of PI-3 kinase is highly specific. Proline 93-100 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 81-84 8955343-5 1996 Mutational analysis revealed that amino acid residues Asp92, Tyr93, Arg96 and Thr97 of the SH3 domain of Fyn are essential for interacting with the proline-rich peptide of PI-3 kinase. Proline 148-155 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 105-108 7589480-3 1995 Here, we report that the Src homology 3 (SH3) domain of Fyn binds to the proline-rich cytoplasmic region of FasL. Proline 73-80 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 56-59 8810341-7 1996 By examining the ability of different SH3 domains to interact with deletion variants of Sam 68 and WASP, we demonstrated that the Itk-SH3 domain and the SH3 domains of Src family kinases bind to overlapping but distinct sets of proline-rich regions in Sam 68 and WASP. Proline 228-235 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 168-171 34137596-4 2021 Here we show that binding of Fyn SH3, a small intracellular proline-binding domain, to the first polyproline tract of httex1Q35 inhibits fibril formation by both NMR and a thioflavin T fluorescence assay. Proline 60-67 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 29-32 8128248-2 1994 Here it was found that the Src homology 3 (SH3) domain of Lyn and Fyn bound to a proline-rich region (residues 84 to 99) within the 85-kilodalton subunit (p85) of PI-3 kinase. Proline 81-88 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 66-69 8294442-1 1994 Src homology 3 (SH3) domains have been recently shown to bind to proline-rich sequences contained in 3BP1, 3BP2, and SOS. Proline 65-72 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 0-3 7773778-4 1994 The orientation of the bound peptide is opposite to that of proline-rich peptides bound to the SH3 domains of Abl, Fyn and p85. Proline 60-67 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 115-118