DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science (New York, N.Y.) 2013 imex curation Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. DIP original experiment: DIP-266843X Science (New York, N.Y.) 2013 IMEx Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science (New York, N.Y.) 2013 imex curation Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. DIP original experiment: DIP-266845X Science (New York, N.Y.) 2013 IMEx Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science (New York, N.Y.) 2013 imex curation Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. DIP original experiment: DIP-266841X Science (New York, N.Y.) 2013 IMEx Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science (New York, N.Y.) 2013 imex curation Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. DIP original experiment: DIP-266840X Science (New York, N.Y.) 2013 IMEx Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science (New York, N.Y.) 2013 imex curation Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. DIP original experiment: DIP-266844X Science (New York, N.Y.) 2013 IMEx Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science (New York, N.Y.) 2013 imex curation Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. DIP original experiment: DIP-266848X Science (New York, N.Y.) 2013 IMEx Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science (New York, N.Y.) 2013 imex curation Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. DIP original experiment: DIP-266837X Science (New York, N.Y.) 2013 IMEx Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science (New York, N.Y.) 2013 imex curation Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. DIP original experiment: DIP-266846X Science (New York, N.Y.) 2013 IMEx Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science (New York, N.Y.) 2013 imex curation Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. DIP original experiment: DIP-266838X Science (New York, N.Y.) 2013 IMEx Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science (New York, N.Y.) 2013 imex curation Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. DIP original experiment: DIP-266836X Science (New York, N.Y.) 2013 IMEx Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science (New York, N.Y.) 2013 imex curation Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. DIP original experiment: DIP-266842X Science (New York, N.Y.) 2013 IMEx Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science (New York, N.Y.) 2013 imex curation Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. DIP original experiment: DIP-266847X Science (New York, N.Y.) 2013 IMEx Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science (New York, N.Y.) 2013 imex curation Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Motz C., Schuhmann KM., Kirchhofer A., Moldt M., Witte G., Conzelmann KK., Hopfner KP. DIP original experiment: DIP-266839X Science (New York, N.Y.) 2013 IMEx Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. h0z993_taegu RNA helicase IFIH1 protein protein taegu Taeniopygia guttata Zebra finch Poephila guttata MAEGTRDERFLYMISCFRPRLKQIIQAQPVLDQLPSLSAEDKDRVRAAALQRGAAAGAEELLRAVERGPRGCGWIREFLQALERGGCSLAACYANPSLSQLPSPAEEAEHDLCVHLVQLLHGTLVDRMRAVQVAEKCLQMGIFQDEDVDRIQTVTDNRGNRDGARELLSRIVQKKDWFSSFLIALRETQHEDLADDLSGNTGESKQNGMEQTTNEETEVTSQPGNVIEENLKQEENVDDSFSSESSLLETSIEKNSVVSESDVSIGDGGVSNSNENLEQSSTTSDSDEDEVERRASPEPDLTLRDYQMEVAKPALNGENIIICLPTGSGKTRVAVYITKDHLDKKKRASEPGKVIVLVNKVPLVEQHLKTEFSPFLKRWYQVIGLSGDSQLKISFPEVVRRNDVIISTAQILENSLLNASKEDEESVHLSDFSLIIIDECHHTQKEGVYNNIMRRYLKEKMKNRKLAKENKPLIPQPQILGLTASPGVGGATSYSKAEEHILKICANLDACRIMTVEEHASQLKNQVKEPSKKTVIADDKKRDPFKEKITEIMTEIQNYCQLHPKTEFGTQTYEQWVIREEKRAAKAEKRRERVCAEHLKKYNDALQINDTIRMVDAYNLLNNFYKEEKSKKTVRSDDDDDDKPAVSKQDETDEFLIGLFHAKKKQLKELTRKPENENEKLMKLRNTLMEEFTKTEEPRGIVFTKTRLSAFALFQWIKDNPKFEEVGIKAHYLIGSGHKSEMKPMTQNEQREVIDKFRCGNVNLLIATTVAEEGLDIKECNIVIRYGLVTNEIAMVQARGRARADESTYALVVSSDSGAVERESVNIYREKMMYKAIQRVQKMPQEEYLNKIHNFQLQSIVEKQMKVMRDQRKTYKKNPSLIKFLCKNCSKSICSGEDIQVIEDMHHVSVKKDFQSLYHIRENKALQDKHADNQTNGEIICKDCGQAWGNMMVHRGLDLPCLKIRNFVVVFADKKTTNDIFKKWGDLPIRFPSFDYASHCPSSDED DIP protein H0Z993 original sequence version: 27 B2C628275E6EE038 d9n195_chick RNA helicase MDA5 protein protein chick Gallus gallus (Chicken) Chicken MSEECRDERFLYMISCFRPRLKRCIRVQPVLDWLPSLSAEEKDKVRAAALQRGEVEGAEELLCAVERGRRDPGWFTEFLLALKKGGCDLAACYVNPSQLPSPQEEDDHDLCVHLVQLLHGTLVDNMQTRQVAEKCLELGIFQEEDLVGIETVIESRGNRDGARELLSRIVQKKDWFSQFLVALRETQHESLADDLSGNTGGTEDKDYELKNNTGKKTEAASQPVYVTEDLKQQENLDDSFVRESSVLETSVGKNSVISESVAVGDASVSNSNENLGQSSTTSDSGEDEAEGRASPEPDLTLRDYQMEVAKPALNGENIIICLPTGSGKTRVAVYITKDHLDKKRKASEQGKVIVLVNKVPLVEQHLRKEFNPFLKHWYQVIGLSGDSELKISFPEVVKRYDVIICTAQILENSLLNATEEDESVRLSDFSLIIIDECHHTQKEGVYNNIMRRYLKEKIKNRKQAKENKPLIPQPQILGLTASPGVGGARSNSKAEEHILKICANLDACRIMTVKEHASQLKNQVKEPFKKTVIADDKRRDPFRERIIEIMQDIQKYCQLYPKSEFGSQPYEQWVIREERRAAKEEKRKERVCAEHLKKYNDALQINDTIRMVDAYNHLNNFYKELKRRKTAESDDDEEPLVSKQDETDEFLMRLFHAKKKQLKELARKPEYDNEKLMKLRNTLMEEFTKTEEPRGIIFTKTRQSALALYHWIMDNPKFEEVGIKAHFLIGAGHNSETKPMTQNEQREVIDKFRGGSINLLIATTVAEEGLDIKECNIVIRYGLVTNEIAMVQARGRARADESTYALVASSGSGAVEREDVNIFRENMMYKAIRRVQEMPPEEYLNKIQDFQLQSIVEKQMKAKRDQRKTYKKNPSLITFLCKNCHKLICSGEDIQVIENMHHVSVKKDFQHLYHKRENRTLQDKHADYQTNVEIICKDCGQVWGNMMVYRGLDLPCLKIRNFVVAFEDKKTTKEIFKKWGELPIIFPDFDYASHCPSSDED DIP protein D9N195 original sequence version: 33 v_piv5 Non-structural protein V P/V protein protein sv5 Simian virus 5 (strain W3) PIV5 Simian virus 5 MDPTDLSFSPDEINKLIETGLNTVEYFTSQQVTGTSSLGKNTIPPGVTGLLTNAAEAKIQESTNHQKGSVGGGAKPKKPRPKIAIVPADDKTVPGKPIPNPLLGLDSTPSTQTVLDLSGKTLPSGSYKGVKLAKFGKENLMTRFIEEPRENPIATSSPIDFKRGRDTGGFHRREYSIGWVGDEVKVTEWCNPSCSPITAAARRFECTCHQCPVTCSECERDT DIP protein P11207 original sequence version: 53 DIP protein P11207 original sequence version: 80 13D2F1627D15AFA3 v_measc Non-structural protein V P/V protein protein measc measles virus (strai MAEEQARHVKNGLECIRALKAEPIGSLAVEEAMAAWSEISDNPGQDRATCKEEEAGSSGLSKPCLSAIGSTEGGAPRIRGQGSGESDDDAETLGIPSRNLQASSTGLQCYHVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSGGDDESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLKLQSRGNNFPKLGKTLNVPPPPNPSRASTSETPIKKGHRREIGLIWNGDRVFIDRWCNPMCSKVTLGTIRARCTCGECPRVCEQCRTDTGVDTRIWYHNLPEIPE DIP protein P0C774 original sequence version: 24 FEDBD36B65E382D0 e1bjz0_bovin RNA helicase IFIH1 protein protein bovin Bos taurus (Bovine) Bovine MSSDGSSTDKNFCYLISCFRARVKRYIQVEPVLDYLTFLPPEVKEHIQRTAATTGDIQAADLLLNTLERGNWPLGWARMFVEALRQAGNPLAARYVNPELTDLPSPSSENAHDECLQLLNLLQPTLVDKLLVADVLDKCVEEKLLTIEDRNRVSAAENNGNEAGVRELLKRIVQKENWFSTFLTILRQTGNDALAREFTGTDCCEGSTESENLSQEDGLEVKEPLLLATDQPNLEVLDIENSSLESSFADSSIVSESDTSLAEGSVSCLDESLGHNSNMGSDSGTMGSDSDDENVAQRASPEPELNLRPYQLEVAQPALEGKNIIICLPTGSGKTRVAVYIAKDHLDKKKASEHGKVMVLVNKVPLVEQLFRKEFKPFLKKWYHVTRLSGDTQLKITFPEVVKSHDVIISTAQILENSLLNSEEGEDDGIELSDFSLIIIDECHHTNKEAVYNNIMRRFLKQKLKNNKLKKENKPVIPLPQIVGLTASPGVGGAKKQAKAEEHILKICANLDAVTIKTVKQNINLLKEQIKEPCKKFVIADDTKKDPFKDKLLEIMTKIQTFCQINPMSDFGTQPYEQWLIQMEKKAAKEGNRKDRVCAEHLRKYNEALQINDTIRMIDAYNHLETFYNDEKEKKFAVLLGDDSDESDDNGDDDVGDGKPPLKLHETDDFLISLFWGNKKKLKKLAQNPEHENEKLIKLRNTIMEQYSRTEGSARGIIFTKTRQSAYALSQWIIENEKFSEVGVKAHHLIGAGHSSEFKPMTQNEQKEVISKFRTGKINLLIATTVAEEGLDIKECNIVIRYGLVTNEIAMVQARGRARADESTYVLVAQSGSGVVERETVNDFREKMMYKAIDRVQNMKPEEYAHKILELQMQSIMEKKMKTKRSIAKQFKGKPSLINFLCKNCGVPACSGEDIHVIEKMHHVNMTPEFKKLYLVRGNKALQTMCVDYQTNGEIICNKCGQAWGTMMVHKGLDLPCLKIKNFVVVFQNNLPKKQYKKWVELPITFPDLNYSEYCLFSDED DIP protein E1BJZ0 original sequence version: 34 ifih1_human Interferon-induced helicase C domain-containing protein 1 Helicase with 2 CARD domains Interferon-induced with helicase C domain protein 1 Melanoma differentiation-associated protein 5 Murabutide down-regulated protein RNA helicase-DEAD box protein 116 RIG-I-like receptor 2 IFIH1 MDA5 RH116 Clinically amyopathic dermatomyositis autoantigen 140 kDa protein protein human Homo sapiens Human MSNGYSTDENFRYLISCFRARVKMYIQVEPVLDYLTFLPAEVKEQIQRTVATSGNMQAVELLLSTLEKGVWHLGWTREFVEALRRTGSPLAARYMNPELTDLPSPSFENAHDEYLQLLNLLQPTLVDKLLVRDVLDKCMEEELLTIEDRNRIAAAENNGNESGVRELLKRIVQKENWFSAFLNVLRQTGNNELVQELTGSDCSESNAEIENLSQVDGPQVEEQLLSTTVQPNLEKEVWGMENNSSESSFADSSVVSESDTSLAEGSVSCLDESLGHNSNMGSDSGTMGSDSDEENVAARASPEPELQLRPYQMEVAQPALEGKNIIICLPTGSGKTRVAVYIAKDHLDKKKKASEPGKVIVLVNKVLLVEQLFRKEFQPFLKKWYRVIGLSGDTQLKISFPEVVKSCDIIISTAQILENSLLNLENGEDAGVQLSDFSLIIIDECHHTNKEAVYNNIMRHYLMQKLKNNRLKKENKPVIPLPQILGLTASPGVGGATKQAKAEEHILKLCANLDAFTIKTVKENLDQLKNQIQEPCKKFAIADATREDPFKEKLLEIMTRIQTYCQMSPMSDFGTQPYEQWAIQMEKKAAKEGNRKERVCAEHLRKYNEALQINDTIRMIDAYTHLETFYNEEKDKKFAVIEDDSDEGGDDEYCDGDEDEDDLKKPLKLDETDRFLMTLFFENNKMLKRLAENPEYENEKLTKLRNTIMEQYTRTEESARGIIFTKTRQSAYALSQWITENEKFAEVGVKAHHLIGAGHSSEFKPMTQNEQKEVISKFRTGKINLLIATTVAEEGLDIKECNIVIRYGLVTNEIAMVQARGRARADESTYVLVAHSGSGVIEHETVNDFREKMMYKAIHCVQNMKPEEYAHKILELQMQSIMEKKMKTKRNIAKHYKNNPSLITFLCKNCSVLACSGEDIHVIEKMHHVNMTPEFKELYIVRENKALQKKCADYQINGEIICKCGQAWGTMMVHKGLDLPCLKIRNFVVVFKNNSTKKQYKKWVELPITFPNLDYSECCLFSDED DIP protein Q9BYX4 original sequence version: 130 DIP protein Q9BYX4 original sequence version: 120 DIP protein Q9BYX4 original sequence version: 123 DIP protein Q9BYX4 original sequence version: 66 DIP protein Q9BYX4 original sequence version: 82 DIP protein Q9BYX4-1 original sequence version: 136 DIP protein Q9BYX4-1 original sequence version: 107 DIP protein Q9BYX4 original sequence version: 122 789CFB4824B92DC9 q8r5f7-1 Interferon-induced helicase C domain-containing protein 1 Ifih1 Helicase with 2 CARD domains Interferon induced with helicase C domain protein 1 Melanoma differentiation-associated protein 5 RIG-I-like receptor 2 protein protein mouse Mus musculus Mouse MSIVCSAEDSFRNLILFFRPRLKMYIQVEPVLDHLIFLSAETKEQILKKINTCGNTSAAELLLSTLEQGQWPLGWTQMFVEALEHSGNPLAARYVKPTLTDLPSPSSETAHDECLHLLTLLQPTLVDKLLINDVLDTCFEKGLLTVEDRNRISAAGNSGNESGVRELLRRIVQKENWFSTFLDVLRQTGNDALFQELTGGGCPEDNTDLANSSHRDGPAANECLLPAVDESSLETEAWNVDDILPEASCTDSSVTTESDTSLAEGSVSCFDESLGHNSNMGRDSGTMGSDSDESVIQTKRVSPEPELQLRPYQMEVAQPALDGKNIIICLPTGSGKTRVAVYITKDHLDKKKQASESGKVIVLVNKVMLAEQLFRKEFNPYLKKWYRIIGLSGDTQLKISFPEVVKSYDVIISTAQILENSLLNLESGDDDGVQLSDFSLIIIDECHHTNKEAVYNNIMRRYLKQKLRNNDLKKQNKPAIPLPQILGLTASPGVGAAKKQSEAEKHILNICANLDAFTIKTVKENLGQLKHQIKEPCKKFVIADDTRENPFKEKLLEIMASIQTYCQKSPMSDFGTQHYEQWAIQMEKKAAKDGNRKDRVCAEHLRKYNEALQINDTIRMIDAYSHLETFYTDEKEKKFAVLNDSDKSDDEASSCNDQLKGDVKKSLKLDETDEFLMNLFFDNKKMLKKLAENPKYENEKLIKLRNTILEQFTRSEESSRGIIFTKTRQSTYALSQWIMENAKFAEVGVKAHHLIGAGHSSEVKPMTQTEQKEVISKFRTGEINLLIATTVAEEGLDIKECNIVIRYGLVTNEIAMVQARGRARADESTYVLVTSSGSGVTEREIVNDFREKMMYKAINRVQNMKPEEYAHKILELQVQSILEKKMKVKRSIAKQYNDNPSLITLLCKNCSMLVCSGENIHVIEKMHHVNMTPEFKGLYIVRENKALQKKFADYQTNGEIICKCGQAWGTMMVHKGLDLPCLKIRNFVVNFKNNSPKKQYKKWVELPIRFPDLDYSEYCLYSDED DIP protein Q8R5F7-1 original sequence version: 116 DIP protein Q8R5F7-1 original sequence version: 94 q6q899-1 Antiviral innate immune response receptor RIG-I Probable ATP-dependent RNA helicase DDX58 Ddx58 DEAD box protein 58 RIG-I-like receptor 1 Retinoic acid-inducible gene 1 protein Retinoic acid-inducible gene I protein protein protein mouse Mus musculus Mouse MTAEQRQNLQAFRDYIKKILDPTYILSYMSSWLEDEEVQYIQAEKNNKGPMEAASLFLQYLLKLQSEGWFQAFLDALYHAGYCGLCEAIESWDFQKIEKLEEHRLLLRRLEPEFKATVDPNDILSELSECLINQECEEIRQIRDTKGRMAGAEKMAECLIRSDKENWPKVLQLALEKDNSKFSELWIVDKGFKRAESKADEDDGAEASSIQIFIQEEPECQNLSQNPGPPSEASSNNLHSPLKPRNYQLELALPAKKGKNTIICAPTGCGKTFVSLLICEHHLKKFPCGQKGKVVFFANQIPVYEQQATVFSRYFERLGYNIASISGATSDSVSVQHIIEDNDIIILTPQILVNNLNNGAIPSLSVFTLMIFDECHNTSKNHPYNQIMFRYLDHKLGESRDPLPQVVGLTASVGVGDAKTAEEAMQHICKLCAALDASVIATVRDNVAELEQVVYKPQKISRKVASRTSNTFKCIISQLMKETEKLAKDVSEELGKLFQIQNREFGTQKYEQWIVGVHKACSVFQMADKEEESRVCKALFLYTSHLRKYNDALIISEDAQMTDALNYLKAFFHDVREAAFDETERELTRRFEEKLEELEKVSRDPSNENPKLRDLYLVLQEEYHLKPETKTILFVKTRALVDALKKWIEENPALSFLKPGILTGRGRTNRATGMTLPAQKCVLEAFRASGDNNILIATSVADEGIDIAECNLVILYEYVGNVIKMIQTRGRGRARDSKCFLLTSSADVIEKEKANMIKEKIMNESILRLQTWDEMKFGKTVHRIQVNEKLLRDSQHKPQPVPDKENKKLLCGKCKNFACYTADIRVVETSHYTVLGDAFKERFVCKPHPKPKIYDNFEKKAKIFCAKQNCSHDWGIFVRYKTFEIPVIKIESFVVEDIVSGVQNRHSKWKDFHFERIQFDPAEMSV DIP protein Q6Q899-1 original sequence version: 107 o95786-1 Antiviral innate immune response receptor RIG-I Probable ATP-dependent RNA helicase DDX58 DDX58 DEAD box protein 58 RIG-I-like receptor 1 Retinoic acid-inducible gene 1 protein Retinoic acid-inducible gene I protein protein protein human Homo sapiens Human MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAGYSGLYEAIESWDFKKIEKLEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKERNKFSELWIVEKGIKDVETEDLEDKMETSDIQIFYQEDPECQNLSENSCPPSEVSDTNLYSPFKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGSSGPLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATVKHNLEELEQVVYKPQKFFRKVESRISDKFKYIIAQLMRDTESLAKRICKDLENLSQIQNREFGTQKYEQWIVTVQKACMVFQMPDKDEESRICKALFLYTSHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESVSRDPSNENPKLEDLCFILQEEYHLNPETITILFVKTRALVDALKNWIEGNPKLSFLKPGILTGRGKTNQNTGMTLPAQKCILDAFKASGDHNILIATSVADEGIDIAQCNLVILYEYVGNVIKMIQTRGRGRARGSKCFLLTSNAGVIEKEQINMYKEKMMNDSILRLQTWDEAVFREKILHIQTHEKFIRDSQEKPKPVPDKENKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPKPKQFSSFEKRAKIFCARQNCSHDWGIHVKYKTFEIPVIKIESFVVEDIATGVQTLYSKWKDFHFEKIPFDPAEMSK DIP protein O95786-1 original sequence version: 126 DIP protein O95786-1 original sequence version: 118 DIP protein O95786 original sequence version: 63 DIP protein O95786 original sequence version: 116 DIP protein O95786-1 original sequence version: 116 DIP protein O95786 original sequence version: 105 DIP protein O95786 original sequence version: 80 DIP protein O95786-1 original sequence version: 78 DIP protein O95786 original sequence version: 102 DIP protein O95786-1 original sequence version: 131 DIP protein O95786 original sequence version: 134 DIP protein O95786 original sequence version: 135 DIP protein O95786-1 original sequence version: 120 DIP protein O95786 original sequence version: 120 a7lcx1_pig RNA helicase MDA5 protein protein pig Sus scrofa (Pig) Pig MSSDGYSADQNFCYLISCFRARVKRYIQVEPVLDYLTFLPAEVKEQIQRAVATTGNINAAELLLNTLEKGVWPPGWTRMFVQALRETGNSLAARYVNPDLTDLPSPSFESSHDECLQLLNLLQPTVVDKLLVTDVLDKCVEEQLLTGEDRNRVSAAENDGNESGVRELLKRIVQKENWFSTFLTVLRQTGNDALARELTGTDCCESNAESDDLLGENGPEVQEPLLLATDQPSLDVSDIEKSSLESSFADSSVVSESDTSLAEGSVSCLDESLGHNSNMGSDSGTMGSDSDEETVAQRASPEPELHLRPYQLEVAQPALEGKNIIICLPTGSGKTRVAVYIAKDHLDKKKEASEPGKVIVLVNKVPLVEQLFRKEFEPFLKKWYRVTRLSGDTQLKITFPEVVKSCDVIISTAQILENSLLNSEEGEDPGVQLSDFSLIIIDECHHTNKEAVYNNIMRRYLKQKLKNNKLKKEEKPVIPLPQILGLTASPGVGGAKKQAKAEEHILKICANLDAFTIKTVKKNINQLKDQIKEPCKKFVIADDTREDLFKDRLLEIMTNIQTFCQISPMSDFGTQPYEQWLIQMEKKAARDGNRKDRVCAEHLKKYNEALQINDTIRRIDAYNHLKTFYNDEKEKKFEVLEDDSDDNGDDSDNDEDENDEKKPSKLDESDIFLMTLFLRNKKILKKLAENPEYENEKLTKLRNTIMEHFTRTEESARGIIFTKTRQSAYALSQWITDNKKFAEVGVKAHHLIGAGHSSEFKPMTQNEQREVISKFRTGKINLLIATTVAEEGLDIKECNIVIRYGLVTNEIAMVQARGRARADESTYVLVAQSGSGVIERETVNDFREKMMYKAIDRVQNMKPEEYAHKILELQMQSIMEKKMKIKRSIAKQCKDNPSLISFLCKNCSVLACSGEDIHIIEKMHHVNMTPEFKNLYIVRGNKALQTKFADYQTNGEIICKKCGQAWGTMMVHKGLDLPCLKIKNYVVAFKNNLFKKQYKKWVELPITFPDLNYSEYCLSSDED DIP protein A7LCX1 original sequence version: 50 mda5-p/v-1 10 23 unspecified role unspecified role unspecified role unspecified role Region 546-808 Region 546-808 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role Region 168-219 Region 168-219 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 ifih1-p/v-1 2 17 unspecified role unspecified role prey prey human Homo sapiens Human 19 unspecified role unspecified role bait bait Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range Q9BYX4:p.Arg806Leu R806L mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain R L This feature has been corrected as a result of our quality control procedures. The original label was 'R806L'. Wed May 02 16:52:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg806leu' Tue Jun 30 16:32:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg806Leu' human Homo sapiens Human physical association physical association mda5-p/v-2 3 15 unspecified role unspecified role unspecified role unspecified role Region 297-864 Region 297-864 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction mda5-p/v-3 7 23 unspecified role unspecified role unspecified role unspecified role Region 303-887 Region 303-887 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction ifih1-p/v-2 8 20 unspecified role unspecified role unspecified role unspecified role Region 305-890 Region 305-890 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role P11207:p.Glu174Ala E174A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain E A This feature has been corrected as a result of our quality control procedures. The original label was 'E174A'. Wed May 02 16:56:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu174ala' Tue Jun 30 19:55:09 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu174Ala' ecolx Escherichia coli direct interaction direct interaction ifih1-p/v-3 11 14 unspecified role unspecified role unspecified role unspecified role Region 363-935 Region 363-935 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction ddx58-p/v-1 12 21 unspecified role unspecified role unspecified role unspecified role Q6Q899-1:p.[Leu715Arg;Glu717Gly] L715R/E717G mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain E G certain certain sequence position certain certain certain sequence position certain L R This feature has been corrected as a result of our quality control procedures. The original label was 'L715R/E717G'. Wed May 02 16:13:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu715arg,glu717gly' Tue Jun 30 17:05:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu715Arg;Glu717Gly]' ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction ifih1-p/v-4 9 19 unspecified role unspecified role unspecified role unspecified role Region 304-890 Region 304-890 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction ifih1-p/v-5 13 20 unspecified role unspecified role unspecified role unspecified role Region 305-890 Region 305-890 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q8R5F7-1:p.Arg806Leu R806L mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain R L This feature has been corrected as a result of our quality control procedures. The original label was 'R806L'. Wed May 02 19:49:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg806leu' Tue Jun 30 18:52:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg806Leu' ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction ifih1-p/v-6 1 17 unspecified role unspecified role prey prey P0C774:p.Glu235Ala E235A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain E A This feature has been corrected as a result of our quality control procedures. The original label was 'E235A'. Wed May 02 20:27:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu235ala' Tue Jun 30 15:45:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu235Ala' human Homo sapiens Human 19 unspecified role unspecified role bait bait Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human physical association physical association ifih1-p/v-7 6 20 unspecified role unspecified role unspecified role unspecified role Region 305-890 Region 305-890 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction ifih1-p/v-8 4 18 unspecified role unspecified role unspecified role unspecified role Region 303-885 Region 303-885 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction ddx58-p/v-2 5 17 unspecified role unspecified role prey prey human Homo sapiens Human 22 unspecified role unspecified role bait bait Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range O95786-1:p.Leu714Arg L714R mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain L R This feature has been corrected as a result of our quality control procedures. The original label was 'L714R'. Wed May 02 15:14:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu714arg' Tue Jun 30 15:54:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu714Arg' O95786-1:p.[Leu714Arg;Glu716Gly] L714R/E716G mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain E G certain certain sequence position certain certain certain sequence position certain L R This feature has been corrected as a result of our quality control procedures. The original label was 'L714R/E716G'. Wed May 02 14:49:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu714arg,glu716gly' Tue Jun 30 18:16:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu714Arg;Glu716Gly]' human Homo sapiens Human physical association physical association