DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Nature structural & molecular biology 2012 imex curation Shu C., Yi G., Watts T., Kao CC., Li P. Only protein-protein interactions in vitro In vitro comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel weight by comassie molecular weight estimation by coomasie staining weight by comassie Shu C., Yi G., Watts T., Kao CC., Li P. DIP original experiment: DIP-251074X Nature structural & molecular biology 2012 IMEx Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Nature structural & molecular biology 2012 imex curation Shu C., Yi G., Watts T., Kao CC., Li P. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Shu C., Yi G., Watts T., Kao CC., Li P. DIP original experiment: DIP-251070X Nature structural & molecular biology 2012 IMEx Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Nature structural & molecular biology 2012 imex curation Shu C., Yi G., Watts T., Kao CC., Li P. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Shu C., Yi G., Watts T., Kao CC., Li P. DIP original experiment: DIP-251072X Nature structural & molecular biology 2012 IMEx Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Nature structural & molecular biology 2012 imex curation Shu C., Yi G., Watts T., Kao CC., Li P. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Shu C., Yi G., Watts T., Kao CC., Li P. DIP original experiment: DIP-251073X Nature structural & molecular biology 2012 IMEx Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Nature structural & molecular biology 2012 imex curation Shu C., Yi G., Watts T., Kao CC., Li P. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Shu C., Yi G., Watts T., Kao CC., Li P. DIP original experiment: DIP-251071X Nature structural & molecular biology 2012 IMEx Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. q3tbt3-1 Stimulator of interferon genes protein Sting1 Endoplasmic reticulum interferon stimulator Eris Mediator of IRF3 activation Mita Mpys Tmem173 Transmembrane protein 173 protein protein mouse Mus musculus Mouse MPYSNLHPAIPRPRGHRSKYVALIFLVASLMILWVAKDPPNHTLKYLALHLASHELGLLLKNLCCLAEELCHVQSRYQGSYWKAVRACLGCPIHCMAMILLSSYFYFLQNTADIYLSWMFGLLVLYKSLSMLLGLQSLTPAEVSAVCEEKKLNVAHGLAWSYYIGYLRLILPGLQARIRMFNQLHNNMLSGAGSRRLYILFPLDCGVPDNLSVVDPNIRFRDMLPQQNIDRAGIKNRVYSNSVYEILENGQPAGVCILEYATPLQTLFAMSQDAKAGFSREDRLEQAKLFCRTLEEILEDVPESRNNCRLIVYQEPTDGNSFSLSQEVLRHIRQEEKEEVTMNAPMTSVAPPPSVLSQEPRLLISGMDQPLPLRTDLI DIP protein Q3TBT3-1 original sequence version: 58 tbk1_mouse Serine/threonine-protein kinase TBK1 TANK-binding kinase 1 T2K Tbk1 protein protein mouse Mus musculus Mouse MQSTSNHLWLLSDILGQGATANVFRGRHKKTGDLYAVKVFNNISFLRPVDVQMREFEVLKKLNHKNIVKLFAIEEETTTRHKVLIMEFCPCGSLYTVLEEPSNAYGLPESEFLIVLRDVVGGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDFGAARELEDDEQFVSLYGTEEYLHPDMYERAVLRKDHQKKYGATVDLWSVGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITGKPSGAISGVQKAENGPIDWSGDMPLSCSLSQGLQALLTPVLANILEADQEKCWGFDQFFAETSDVLHRMVIHVFSLQHMTAHKIYIHSYNTAAVFHELVYKQTKIVSSNQELIYEGRRLVLELGRLAQHFPKTTEENPIFVTSREQLNTVGLRYEKISLPKIHPRYDLDGDASMAKAVTGVVCYACRTASTLLLYQELMRKGVRWLVELVKDDYNETVHKKTEVVITLDFCIRNIEKTVKVYEKLMKVNLEAAELGEISDIHTKLLRLSSSQGTIESSLQDISSRLSPGGLLADTWAHQEGTHPRDRNVEKLQVLLNCITEIYYQFKKDKAERRLAYNEEQIHKFDKQKLYYHATKAMSHFSEECVRKYEAFKDKSEEWMRKMLHLRKQLLSLTNQCFDIEEEVSKYQDYTNELQETLPQKMLAASGGVKHAMAPIYPSSNTLVEMTLGMKKLKEEMEGVVKELAENNHILERFGSLTMDGGLRNVDCL DIP protein Q9WUN2 original sequence version: 53 DIP protein Q9WUN2 original sequence version: 101 DIP protein Q9WUN2 original sequence version: 100 DIP protein Q9WUN2 original sequence version: 93 978ADDE3061DACD1 irf3_human Interferon regulatory factor 3 IRF3 protein protein human Homo sapiens Human MGTPKPRILPWLVSQLDLGQLEGVAWVNKSRTRFRIPWKHGLRQDAQQEDFGIFQAWAEATGAYVPGRDKPDLPTWKRNFRSALNRKEGLRLAEDRSKDPHDPHKIYEFVNSGVGDFSQPDTSPDTNGGGSTSDTQEDILDELLGNMVLAPLPDPGPPSLAVAPEPCPQPLRSPSLDNPTPFPNLGPSENPLKRLLVPGEEWEFEVTAFYRGRQVFQQTISCPEGLRLVGSEVGDRTLPGWPVTLPDPGMSLTDRGVMSYVRHVLSCLGGGLALWRAGQWLWAQRLGHCHTYWAVSEELLPNSGHGPDGEVPKDKEGGVFDLGPFIVDLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMVKVVPTCLRALVEMARVGGASSLENTVDLHISNSHPLSLTSDQYKAYLQDLVEGMDFQGPGES DIP protein Q14653 original sequence version: 96 DIP protein Q14653 original sequence version: 75 DIP protein Q14653 original sequence version: 95 DIP protein Q14653-1 original sequence version: 128 DIP protein Q14653 original sequence version: 119 F536676FA78B0110 sting_human Stimulator of interferon genes protein STING1 ERIS Endoplasmic reticulum interferon stimulator MITA Mediator of IRF3 activation TMEM173 Transmembrane protein 173 protein protein human Homo sapiens Human MPHSSLHPSIPCPRGHGAQKAALVLLSACLVTLWGLGEPPEHTLRYLVLHLASLQLGLLLNGVCSLAEELRHIHSRYRGSYWRTVRACLGCPLRRGALLLLSIYFYYSLPNAVGPPFTWMLALLGLSQALNILLGLKGLAPAEISAVCEKGNFNVAHGLAWSYYIGYLRLILPELQARIRTYNQHYNNLLRGAVSQRLYILLPLDCGVPDNLSMADPNIRFLDKLPQQTGDHAGIKDRVYSNSIYELLENGQRAGTCVLEYATPLQTLFAMSQYSQAGFSREDRLEQAKLFCRTLEDILADAPESQNNCRLIAYQEPADDSSFSLSQEVLRHLRQEEKEEVTVGSLKTSAVPSTSTMSQEPELLISGMEKPLPLRTDFS DIP protein Q86WV6 original sequence version: 83 DIP protein Q86WV6 original sequence version: 47 DIP protein Q86WV6 original sequence version: 50 DIP protein Q86WV6 original sequence version: 100 DIP protein Q86WV6 original sequence version: 68 CB54D6A4D4D8E7C0 tmem173-1 2 9 unspecified role unspecified role unspecified role unspecified role Region 155-341 Region 155-341 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction tmem173-4 5 9 unspecified role unspecified role unspecified role unspecified role Region 149-341 Region 149-341 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction irf3-8 1 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction tbk1-4 3 7 putative self putative self unspecified role unspecified role spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm phosphorylation phosphorylation reaction phosphorylation true tbk1-tmem173-2 4 6 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 154-340 Region 154-340 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 enzyme enzyme unspecified role unspecified role spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm phosphorylation phosphorylation reaction phosphorylation