IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ http://www.ebi.ac.uk/ pilati-2014-2 Genomic Profiling of Hepatocellular Adenomas Reveals Recurrent FRK-Activating Mutations and the Mechanisms of Malignant Transformation. in vitro In vitro protein kinase assay protein kinase assay antibody detection identification by antibody antibody detection Pilati C., Letouzé E., Nault J.C., Imbeaud S., Boulai A., Calderaro J., Poussin K., Franconi A., Couchy G., Morcrette G., Mallet M., Taouji S., Balabaud C., Terris B., Canal F., Paradis V., Scoazec J.Y., de Muret A., Guettier C., Bioulac-Sage P., Chevet E., Calvo F., Zucman-Rossi J. Cancer - Interactions investigated in the context of cancer The Src Kinase inhibitor "SRC-Inhibitor-5" was also used in this assay system, but results have not been entered here as it has not been possible to further identify this molecule. Kinase activity detected by AlphaScreen®-based Assay (Amplified Luminescent Proximity Homogeneous Assay, -MI:0905). In this experiment Anti-phosphotyrosine antibodies were conjugated to Donor beads and Streptavidin Acceptor beads were used. jessica.zucman-rossi@inserm.fr Cancer Cell (1535-6108) 2014 Only protein-protein interactions imex curation pilati-2014-1 Genomic Profiling of Hepatocellular Adenomas Reveals Recurrent FRK-Activating Mutations and the Mechanisms of Malignant Transformation. human-hep_3b Homo sapiens hepatocellular carcinoma (HCC) cells (p53-null). hep_3b human hepatocellular carcinoma (HCC) cells (p53-null). confocal microscopy confocal microscopy immunocytochemistry immunocytochemistry Pilati C., Letouzé E., Nault J.C., Imbeaud S., Boulai A., Calderaro J., Poussin K., Franconi A., Couchy G., Morcrette G., Mallet M., Taouji S., Balabaud C., Terris B., Canal F., Paradis V., Scoazec J.Y., de Muret A., Guettier C., Bioulac-Sage P., Chevet E., Calvo F., Zucman-Rossi J. Cancer - Interactions investigated in the context of cancer jessica.zucman-rossi@inserm.fr Cancer Cell (1535-6108) 2014 Only protein-protein interactions imex curation pilati-2014-3 Genomic Profiling of Hepatocellular Adenomas Reveals Recurrent FRK-Activating Mutations and the Mechanisms of Malignant Transformation. in vitro In vitro protein kinase assay protein kinase assay tag fluorescence tag visualisation by fluorescence tag fluorescence Pilati C., Letouzé E., Nault J.C., Imbeaud S., Boulai A., Calderaro J., Poussin K., Franconi A., Couchy G., Morcrette G., Mallet M., Taouji S., Balabaud C., Terris B., Canal F., Paradis V., Scoazec J.Y., de Muret A., Guettier C., Bioulac-Sage P., Chevet E., Calvo F., Zucman-Rossi J. Cancer - Interactions investigated in the context of cancer Kinase assay using Omnia® Y Peptide 5 Kit, Life Technology. (see PMID:15782220). This assay measures the increase in fluorescence of a Sox (a synthetic amino acid) moiety, which accompanies the phosphorylation of a nearby Ser, Thr or Tyr residue. jessica.zucman-rossi@inserm.fr Cancer Cell (1535-6108) 2014 Only protein-protein interactions imex curation poly(glu:tyr) 4:1 Poly(Glu,Tyr) 4:1 random copolymer small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) frk_human Tyrosine-protein kinase FRK PTK5 RAK FYN-related kinase Nuclear tyrosine protein kinase RAK FRK Protein-tyrosine kinase 5 protein protein human Homo sapiens Human MSNICQRLWEYLEPYLPCLSTEADKSTVIENPGALCSPQSQRHGHYFVALFDYQARTAEDLSFRAGDKLQVLDTLHEGWWFARHLEKRRDGSSQQLQGYIPSNYVAEDRSLQAEPWFFGAIGRSDAEKQLLYSENKTGSFLIRESESQKGEFSLSVLDGAVVKHYRIKRLDEGGFFLTRRRIFSTLNEFVSHYTKTSDGLCVKLGKPCLKIQVPAPFDLSYKTVDQWEIDRNSIQLLKRLGSGQFGEVWEGLWNNTTPVAVKTLKPGSMDPNDFLREAQIMKNLRHPKLIQLYAVCTLEDPIYIITELMRHGSLQEYLQNDTGSKIHLTQQVDMAAQVASGMAYLESRNYIHRDLAARNVLVGEHNIYKVADFGLARVFKVDNEDIYESRHEIKLPVKWTAPEAIRSNKFSIKSDVWSFGILLYEIITYGKMPYSGMTGAQVIQMLAQNYRLPQPSNCPQQFYNIMLECWNAEPKERPTFETLRWKLEDYFETDSSYSDANNFIR src_inhibitor_1 SRC Inhibitor 1 small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) pp2 PP2 small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) dasatinib Dasatinib small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) Protein kinase inhibitor src_inhibitor_5 SRC Inhibitor 5 small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) stat3_human Signal transducer and activator of transcription 3 Acute-phase response factor STAT3 APRF protein protein human Homo sapiens Human MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMELTSECATSPM 6C00632211C8012D omnia_y_peptide_5 Omnia Y Peptide 5 peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) EAEAIYA Ac-EAEAIYAAdP(Sox)G-NH2 frk-stat3-1 1535035 n/a 1535038 enzyme target enzyme target substrate substrate neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) n/a 1535039 enzyme enzyme neutral component neutral component undefined mutation mutation increasing rate mutation increasing interaction rate mutation increasing rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain false This is a deletion of amino acids 378-380 and insertion at same site of a glutamine P42685:p.Val378_Phe379del mutation increasing rate mutation increasing interaction rate mutation increasing rate deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false n_terminus gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation false false false 2E poly(glu:tyr) 4:1 phosphotyr O-phospho-L-tyrosine FRK-WT Vmax =57 umol/mg/min, Km =8.2uM VF mutant Vmax =88 umol/mg/min, Km =3.1uM FK mutant Vmax =58 umol/mg/min, Km =4.5uM VF and FK FRK mutants exhibited an increased kinase activity compared with the wild-type FRK. frk-poly_glu_tyr__4_1-1 1535035 n/a 1535040 inhibitor inhibitor neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) n/a 1535038 enzyme target enzyme target substrate substrate neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) n/a 1535039 enzyme enzyme neutral component neutral component undefined mutation mutation increasing rate mutation increasing interaction rate mutation increasing rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain false This is a deletion of amino acids 378-380 and insertion at same site of a glutamine n_terminus gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false P42685:p.Val378_Phe379del mutation increasing rate mutation increasing interaction rate mutation increasing rate deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation false false false 2F poly(glu:tyr) 4:1 phosphotyr O-phospho-L-tyrosine frk-poly_glu_tyr__4_1-2 1535035 n/a 1535039 enzyme enzyme neutral component neutral component undefined mutation mutation increasing rate mutation increasing interaction rate mutation increasing rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain false This is a deletion of amino acids 378-380 and insertion at same site of a glutamine n_terminus gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false P42685:p.Val378_Phe379del mutation increasing rate mutation increasing interaction rate mutation increasing rate deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) n/a 1535041 inhibitor inhibitor neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) n/a 1535038 enzyme target enzyme target substrate substrate neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) phosphorylation phosphorylation reaction phosphorylation false false false 2F poly(glu:tyr) 4:1 phosphotyr O-phospho-L-tyrosine frk-poly_glu_tyr__4_1-3 1535035 n/a 1535042 inhibitor inhibitor neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) n/a 1535038 enzyme target enzyme target substrate substrate neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) n/a 1535039 enzyme enzyme neutral component neutral component n_terminus gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false P42685:p.Val378_Phe379del mutation increasing rate mutation increasing interaction rate mutation increasing rate deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false undefined mutation mutation increasing rate mutation increasing interaction rate mutation increasing rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain false This is a deletion of amino acids 378-380 and insertion at same site of a glutamine ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation false false false 2F poly(glu:tyr) 4:1 phosphotyr O-phospho-L-tyrosine frk-poly_glu_tyr__4_1-4 1535035 n/a 1535038 enzyme target enzyme target substrate substrate neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) n/a 1535039 enzyme enzyme neutral component neutral component undefined mutation mutation increasing rate mutation increasing interaction rate mutation increasing rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain false This is a deletion of amino acids 378-380 and insertion at same site of a glutamine n_terminus gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false P42685:p.Val378_Phe379del mutation increasing rate mutation increasing interaction rate mutation increasing rate deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) n/a 1535043 inhibitor inhibitor neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) phosphorylation phosphorylation reaction phosphorylation false false false 2Fi poly(glu:tyr) 4:1 phosphotyr O-phospho-L-tyrosine frk-stat3 1535036 n/a 1535044 unspecified role unspecified role neutral component neutral component required_phosphotyr_705 optyr O4'-phospho-L-tyrosine (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4-phosphotyrosine tyrosine phosphate 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine OPTyr Phospho Phospho Tyrosinyl Phosphorylation phosphorylationy certain certain sequence position certain certain certain sequence position certain false n/a 1535039 unspecified role unspecified role neutral component neutral component undefined mutation mutation mutation substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain false This is a deletion of amino acids 378-380 and insertion at same site of a glutamine P42685:p.Glu346Gly mutation mutation deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false P42685:p.Val378_Phe379del mutation mutation deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false c_terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range false c_terminus flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged c-term range C-terminal range c-term range c-term range C-terminal range c-term range false colocalization colocalization false false false 2D frk-stat3-2 1535037 n/a 1535045 enzyme target enzyme target substrate substrate neutral component neutral component n_terminus acglu N-acetyl-L-glutamic acid (2S)-2-(acetamido)pentanedioic acid 2-(acetylamino)pentanedioic acid 2-(acetylazanyl)pentanedioic acid MOD_RES N-acetylglutamate N-acetyl-L-glutamic acid N-acetylated L-glutamic acid acetylglutamic acid AcGlu n-term range n-terminal range n-term range n-term range n-terminal range n-term range false adp_sox_glycine fluorophore fluorophore c-term range C-terminal range c-term range c-term range C-terminal range c-term range false chemical synthesis Chemical synthesis (Chemical synthesis) n/a 1535039 enzyme enzyme neutral component neutral component P42685:p.Val378_Phe379del mutation increasing rate mutation increasing interaction rate mutation increasing rate deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false n_terminus gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false mouse-ba_f3 Mouse pro B cells IL-3 dependent mouse-baf3 EBI-6922762 ba_f3 Mouse pro B cells IL-3 dependent BA/F3 baf3 Mouse pro B cell line. IL-3 dependent murine pro B cell line established from peripheral blood; apparently derived from BALB/c mouse. phosphorylation phosphorylation reaction phosphorylation false false false Supp 2D omnia_y_peptide_5 phosphotyr O-phospho-L-tyrosine VF FRK mutant exhibited an increased kinase activity compared with the wild-type FRK.