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/ TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation. TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation. PLoS ONE 2012 imex curation Zurek B., Schoultz I., Neerincx A., Napolitano L.M., Birkner K., Bennek E., Sellge G., Lerm M., Meroni G., Söderholm J.D., Kufer T.A. Crohn's disease - Interactions of proteins identified as having a link to Crohn's disease IBD - Inflammatory bowel disease thomas.kufer@uk-koeln.de 12-Nov-2014: Contacted by IntAct-Help. Only protein-protein interactions human-sw480 Human SW480 adenocarcinoma cell line sw480 SW480- human primary colorectal adenocarcinoma cell line There is a G -> A mutation in codon 273 of the p53 gene resulting in an Arg -> His substitution and a C -> T mutation in codon 309 resulting in a Pro -> Ser substitution. http://www.atcc.org/ATCCAdvancedCatalogSearch/ProductDetails/tabid/452/Default.aspx?ATCCNum=CCL-228&Template=cellBiology anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Zurek B., Schoultz I., Neerincx A., Napolitano L.M., Birkner K., Bennek E., Sellge G., Lerm M., Meroni G., Söderholm J.D., Kufer T.A. Crohn's disease - Interactions of proteins identified as having a link to Crohn's disease thomas.kufer@uk-koeln.de Accepted 2014-OCT-28 by ORCHARD PLoS ONE 2012 Only protein-protein interactions imex curation TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation. TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation. PLoS ONE 2012 imex curation Zurek B., Schoultz I., Neerincx A., Napolitano L.M., Birkner K., Bennek E., Sellge G., Lerm M., Meroni G., Söderholm J.D., Kufer T.A. Crohn's disease - Interactions of proteins identified as having a link to Crohn's disease IBD - Inflammatory bowel disease thomas.kufer@uk-koeln.de 12-Nov-2014: Contacted by IntAct-Help. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Zurek B., Schoultz I., Neerincx A., Napolitano L.M., Birkner K., Bennek E., Sellge G., Lerm M., Meroni G., Söderholm J.D., Kufer T.A. Crohn's disease - Interactions of proteins identified as having a link to Crohn's disease The authors tested but could not confirm the NOD2-TRIM8 and NOD2-TRIM50 interactions by anti-Flag co-immunoprecipitation in HEK293t cells expressing Flag-tagged NOD2 and Myc-tagged TRIM8 or TRIM50. thomas.kufer@uk-koeln.de Accepted 2014-OCT-28 by ORCHARD PLoS ONE 2012 Only protein-protein interactions imex curation TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation. TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation. PLoS ONE 2012 imex curation Zurek B., Schoultz I., Neerincx A., Napolitano L.M., Birkner K., Bennek E., Sellge G., Lerm M., Meroni G., Söderholm J.D., Kufer T.A. Crohn's disease - Interactions of proteins identified as having a link to Crohn's disease IBD - Inflammatory bowel disease thomas.kufer@uk-koeln.de 12-Nov-2014: Contacted by IntAct-Help. Only protein-protein interactions human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Zurek B., Schoultz I., Neerincx A., Napolitano L.M., Birkner K., Bennek E., Sellge G., Lerm M., Meroni G., Söderholm J.D., Kufer T.A. Crohn's disease - Interactions of proteins identified as having a link to Crohn's disease thomas.kufer@uk-koeln.de Accepted 2014-OCT-28 by ORCHARD PLoS ONE 2012 Only protein-protein interactions imex curation TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation. TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation. PLoS ONE 2012 imex curation Zurek B., Schoultz I., Neerincx A., Napolitano L.M., Birkner K., Bennek E., Sellge G., Lerm M., Meroni G., Söderholm J.D., Kufer T.A. Crohn's disease - Interactions of proteins identified as having a link to Crohn's disease IBD - Inflammatory bowel disease thomas.kufer@uk-koeln.de 12-Nov-2014: Contacted by IntAct-Help. Only protein-protein interactions human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Zurek B., Schoultz I., Neerincx A., Napolitano L.M., Birkner K., Bennek E., Sellge G., Lerm M., Meroni G., Söderholm J.D., Kufer T.A. Crohn's disease - Interactions of proteins identified as having a link to Crohn's disease thomas.kufer@uk-koeln.de Accepted 2014-OCT-28 by ORCHARD PLoS ONE 2012 Only protein-protein interactions imex curation TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation. TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation. PLoS ONE 2012 imex curation Zurek B., Schoultz I., Neerincx A., Napolitano L.M., Birkner K., Bennek E., Sellge G., Lerm M., Meroni G., Söderholm J.D., Kufer T.A. Crohn's disease - Interactions of proteins identified as having a link to Crohn's disease IBD - Inflammatory bowel disease thomas.kufer@uk-koeln.de 12-Nov-2014: Contacted by IntAct-Help. Only protein-protein interactions human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 fluorescence imaging fluorescence microscopy fluorescence imaging immunocytochemistry immunocytochemistry Zurek B., Schoultz I., Neerincx A., Napolitano L.M., Birkner K., Bennek E., Sellge G., Lerm M., Meroni G., Söderholm J.D., Kufer T.A. Crohn's disease - Interactions of proteins identified as having a link to Crohn's disease thomas.kufer@uk-koeln.de Accepted 2014-OCT-28 by ORCHARD PLoS ONE 2012 Only protein-protein interactions imex curation TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation. TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation. PLoS ONE 2012 imex curation Zurek B., Schoultz I., Neerincx A., Napolitano L.M., Birkner K., Bennek E., Sellge G., Lerm M., Meroni G., Söderholm J.D., Kufer T.A. Crohn's disease - Interactions of proteins identified as having a link to Crohn's disease IBD - Inflammatory bowel disease thomas.kufer@uk-koeln.de 12-Nov-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Zurek B., Schoultz I., Neerincx A., Napolitano L.M., Birkner K., Bennek E., Sellge G., Lerm M., Meroni G., Söderholm J.D., Kufer T.A. Crohn's disease - Interactions of proteins identified as having a link to Crohn's disease thomas.kufer@uk-koeln.de Accepted 2014-OCT-28 by ORCHARD PLoS ONE 2012 Only protein-protein interactions imex curation trim5_human Tripartite motif-containing protein 5 TRIM5 RNF88 RING finger protein 88 RING-type E3 ubiquitin transferase TRIM5 protein protein human Homo sapiens Human MASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGESSCPVCRISYQPENIRPNRHVANIVEKLREVKLSPEGQKVDHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVAREYQVKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRDILDWEESNELQNLEKEEEDILKSLTNSETEMVQQTQSLRELISDLEHRLQGSVMELLQGVDGVIKRTENVTLKKPETFPKNQRRVFRAPDLKGMLEVFRELTDVRRYWVDVTVAPNNISCAVISEDKRQVSSPKPQIIYGARGTRYQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPDAMCNIEKNENYQPKYGYWVIGLEEGVKCSAFQDSSFHTPSVPFIVPLSVIICPDRVGVFLDYEACTVSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLCSPSS 8E61AAFD508AF6C0 nod2_human Nucleotide-binding oligomerization domain-containing protein 2 IBD1 NOD2 CARD15 Caspase recruitment domain-containing protein 15 Inflammatory bowel disease protein 1 protein protein human Homo sapiens Human MGEEGGSASHDEEERASVLLGHSPGCEMCSQEAFQAQRSQLVELLVSGSLEGFESVLDWLLSWEVLSWEDYEGFHLLGQPLSHLARRLLDTVWNKGTWACQKLIAAAQEAQADSQSPKLHGCWDPHSLHPARDLQSHRPAIVRRLHSHVENMLDLAWERGFVSQYECDEIRLPIFTPSQRARRLLDLATVKANGLAAFLLQHVQELPVPLALPLEAATCKKYMAKLRTTVSAQSRFLSTYDGAETLCLEDIYTENVLEVWADVGMAGPPQKSPATLGLEELFSTPGHLNDDADTVLVVGEAGSGKSTLLQRLHLLWAAGQDFQEFLFVFPFSCRQLQCMAKPLSVRTLLFEHCCWPDVGQEDIFQLLLDHPDRVLLTFDGFDEFKFRFTDRERHCSPTDPTSVQTLLFNLLQGNLLKNARKVVTSRPAAVSAFLRKYIRTEFNLKGFSEQGIELYLRKRHHEPGVADRLIRLLQETSALHGLCHLPVFSWMVSKCHQELLLQEGGSPKTTTDMYLLILQHFLLHATPPDSASQGLGPSLLRGRLPTLLHLGRLALWGLGMCCYVFSAQQLQAAQVSPDDISLGFLVRAKGVVPGSTAPLEFLHITFQCFFAAFYLALSADVPPALLRHLFNCGRPGNSPMARLLPTMCIQASEGKDSSVAALLQKAEPHNLQITAAFLAGLLSREHWGLLAECQTSEKALLRRQACARWCLARSLRKHFHSIPPAAPGEAKSVHAMPGFIWLIRSLYEMQEERLARKAARGLNVGHLKLTFCSVGPTECAALAFVLQHLRRPVALQLDYNSVGDIGVEQLLPCLGVCKALYLRDNNISDRGICKLIECALHCEQLQKLALFNNKLTDGCAHSMAKLLACRQNFLALRLGNNYITAAGAQVLAEGLRGNTSLQFLGFWGNRVGDEGAQALAEALGDHQSLRWLSLVGNNIGSVGAQALALMLAKNVMLEELCLEENHLQDEGVCSLAEGLKKNSSLKILKLSNNCITYLGAEALLQALERNDTILEVWLRGNTFSLEEVDKLGCRDTRLLL DIP protein Q9HC29 original sequence version: 141 DIP protein Q9HC29 original sequence version: 77 DIP protein Q9HC29-1 original sequence version: 100 DIP protein Q9HC29-1 original sequence version: 106 mint homomint Induces NF-kappa-B via RICK (CARDIAK, RIP2) and IKK-gamma. Confers responsiveness to intracellular bacterial lipopolysaccharides (LPS) Defects in NOD2 are the cause of Blau syndrome (BS) [MIM:186580]. BS is a rare autosomal dominant disorder characterized by early-onset granulomatous arthritis, uveitis and skin rash Defects in NOD2 are a cause of susceptibility to Crohn disease (CD) [MIM:266600]. CD is a form of remitting inflammatory bowel disease (IBD). CD may involve any part of the gastrointestinal tract, but most frequently the terminal ileum and colon. Bowel inflammation is transmural and discontinuous. Crohn disease is commonly classified as autoimmune disease Defects in NOD2 are a cause of susceptibility to ulcerative colitis [MIM:191390]. It is a chronic inflammatory bowel disease. In ulcerative colitis, the inflammation is continuous and limited to rectal and colonic mucosal layers. Ulcerative colitis is commonly classified as autoimmune disease Defects in NOD2 are the cause of early-onset sarcoidosis (EOS) [MIM:609464]. Sarcoidosis is a multiorganic inflammatory disease with unknown etiology, characterized by the histologic features of non-caseating epithelioid granulomas. In childhood, 2 distinct types of sarcoidosis have been described. Usually the disease is detected in older children by chest radiography and the clinical manifestations are characterized by a classical triad of lung, lymph node, and eye involvement, similar to those in adults. In contrast, early-onset sarcoidosis (EOS), which usually appears in those younger than 4 years of age, is quite rare and has a distinct triad of skin, joint, and eye disorders, without apparent pulmonary involvement. Compared with an asymptomatic and sometimes naturally disappearing course of the disease in older children, EOS is progressive and in many cases causes severe complications, such as blindness, joint destruction, and visceral involvement 0037592D96D7DDFF trim8_human E3 ubiquitin-protein ligase TRIM8 Tripartite motif-containing protein 8 TRIM8 GERP RNF27 RING finger protein 27 Glioblastoma-expressed RING finger protein RING-type E3 ubiquitin transferase TRIM8 protein protein human Homo sapiens Human MAENWKNCFEEELICPICLHVFVEPVQLPCKHNFCRGCIGEAWAKDSGLVRCPECNQAYNQKPGLEKNLKLTNIVEKFNALHVEKPPAALHCVFCRRGPPLPAQKVCLRCEAPCCQSHVQTHLQQPSTARGHLLVEADDVRAWSCPQHNAYRLYHCEAEQVAVCQYCCYYSGAHQGHSVCDVEIRRNEIRKMLMKQQDRLEEREQDIEDQLYKLESDKRLVEEKVNQLKEEVRLQYEKLHQLLDEDLRQTVEVLDKAQAKFCSENAAQALHLGERMQEAKKLLGSLQLLFDKTEDVSFMKNTKSVKILMDRTQTCTSSSLSPTKIGHLNSKLFLNEVAKKEKQLRKMLEGPFSTPVPFLQSVPLYPCGVSSSGAEKRKHSTAFPEASFLETSSGPVGGQYGAAGTASGEGQSGQPLGPCSSTQHLVALPGGAQPVHSSPVFPPSQYPNGSAAQQPMLPQYGGRKILVCSVDNCYCSSVANHGGHQPYPRSGHFPWTVPSQEYSHPLPPTPSVPQSLPSLAVRDWLDASQQPGHQDFYRVYGQPSTKHYVTS 1FEF89029EB9BACB tri11_human E3 ubiquitin-protein ligase TRIM11 RING finger protein 92 Protein BIA1 TRIM11 RNF92 RING-type E3 ubiquitin transferase TRIM11 Tripartite motif-containing protein 11 protein protein human Homo sapiens Human MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSPQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCPAHREPLAAFCGDELRLLCAACERSGEHWAHRVRPLQDAAEDLKAKLEKSLEHLRKQMQDALLFQAQADETCVLWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQRLEEEELEVLPRLREGAAHLGQQSAHLAELIAELEGRCQLPALGLLQDIKDALRRVQDVKLQPPEVVPMELRTVCRVPGLVETLRRFRGDVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGSYYNSSERALAPLRDPPRRVGIFLDYEAGHLSFYSATDGSLLFIFPEIPFSGTLRPLFSPLSSSPTPMTICRPKGGSGDTLAPQ 8DE4BDF79F221739 tri50_human E3 ubiquitin-protein ligase TRIM50 TRIM50 TRIM50A Tripartite motif-containing protein 50 RING-type E3 ubiquitin transferase TRIM50 protein protein human Homo sapiens Human MAWQVSLLELEDWLQCPICLEVFKEPLMLQCGHSYCKGCLVSLSCHLDAELRCPVCRQAVDGSSSLPNVSLARVIEALRLPGDPEPKVCVHHRNPLSLFCEKDQELICGLCGLLGSHQHHPVTPVSTVYSRMKEELAALISELKQEQKKVDELIAKLVNNRTRIVNESDVFSWVIRREFQELHHLVDEEKARCLEGIGGHTRGLVASLDMQLEQAQGTRERLAQAECVLEQFGNEDHHKFIRKFHSMASRAEMPQARPLEGAFSPISFKPGLHQADIKLTVWKRLFRKVLPAPEPLKLDPATAHPLLELSKGNTVVQCGLLAQRRASQPERFDYSTCVLASRGFSCGRHYWEVVVGSKSDWRLGVIKGTASRKGKLNRSPEHGVWLIGLKEGRVYEAFACPRVPLPVAGHPHRIGLYLHYEQGELTFFDADRPDDLRPLYTFQADFQGKLYPILDTCWHERGSNSLPMVLPPPSGPGPLSPEQPTKL DB06FD97C10D723C tri27_human Zinc finger protein RFP TRIM27 RNF76 RFP Ret finger protein Tripartite motif-containing protein 27 RING finger protein 76 RING-type E3 ubiquitin transferase TRIM27 protein protein human Homo sapiens Human MASGSVAECLQQETTCPVCLQYFAEPMMLDCGHNICCACLARCWGTAETNVSCPQCRETFPQRHMRPNRHLANVTQLVKQLRTERPSGPGGEMGVCEKHREPLKLYCEEDQMPICVVCDRSREHRGHSVLPLEEAVEGFKEQIQNQLDHLKRVKDLKKRRRAQGEQARAELLSLTQMEREKIVWEFEQLYHSLKEHEYRLLARLEELDLAIYNSINGAITQFSCNISHLSSLIAQLEEKQQQPTRELLQDIGDTLSRAERIRIPEPWITPPDLQEKIHIFAQKCLFLTESLKQFTEKMQSDMEKIQELREAQLYSVDVTLDPDTAYPSLILSDNLRQVRYSYLQQDLPDNPERFNLFPCVLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDSVCRKGGVTSAPQNGFWAVSLWYGKEYWALTSPMTALPLRTPLQRVGIFLDYDAGEVSFYNVTERCHTFTFSHATFCGPVRPYFSLSYSGGKSAAPLIICPMSGIDGFSGHVGNHGHSMETSP 6F963D9048D8A731 ro52_human E3 ubiquitin-protein ligase TRIM21 TRIM21 RNF81 Sjoegren syndrome type A antigen Ro(SS-A) 52 kDa ribonucleoprotein autoantigen Ro/SS-A Tripartite motif-containing protein 21 RING finger protein 81 52 kDa Ro protein RO52 SSA1 RING-type E3 ubiquitin transferase TRIM21 protein protein human Homo sapiens Human MASAARLTMMWEEVTCPICLDPFVEPVSIECGHSFCQECISQVGKGGGSVCPVCRQRFLLKNLRPNRQLANMVNNLKEISQEAREGTQGERCAVHGERLHLFCEKDGKALCWVCAQSRKHRDHAMVPLEEAAQEYQEKLQVALGELRRKQELAEKLEVEIAIKRADWKKTVETQKSRIHAEFVQQKNFLVEEEQRQLQELEKDEREQLRILGEKEAKLAQQSQALQELISELDRRCHSSALELLQEVIIVLERSESWNLKDLDITSPELRSVCHVPGLKKMLRTCAVHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHFHSGKHYWEVDVTGKEAWDLGVCRDSVRRKGHFLLSSKSGFWTIWLWNKQKYEAGTYPQTPLHLQVPPCQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFFSPGFNDGGKNTAPLTLCPLNIGSQGSTDY DDFF2944AFC629FB trim1_human Probable E3 ubiquitin-protein ligase MID2 Midline defect 2 Tripartite motif-containing protein 1 RING finger protein 60 MID2 FXY2 RNF60 TRIM1 RING-type E3 ubiquitin transferase MID2 Midin-2 Midline-2 protein protein human Homo sapiens Human MGESPASVVLNASGGLFSLKMETLESELTCPICLELFEDPLLLPCAHSLCFSCAHRILVSSCSSGESIEPITAFQCPTCRYVISLNHRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSESRRERTYRPTTAMSSERIACQFCEQDPPRDAVKTCITCEVSYCDRCLRATHPNKKPFTSHRLVEPVPDTHLRGITCLDHENEKVNMYCVSDDQLICALCKLVGRHRDHQVASLNDRFEKLKQTLEMNLTNLVKRNSELENQMAKLIQICQQVEVNTAMHEAKLMEECDELVEIIQQRKQMIAVKIKETKVMKLRKLAQQVANCRQCLERSTVLINQAEHILKENDQARFLQSAKNIAERVAMATASSQVLIPDINFNDAFENFALDFSREKKLLEGLDYLTAPNPPSIREELCTASHDTITVHWISDDEFSISSYELQYTIFTGQANFISKSWCSWGLWPEIRKCKEAVSCSRLAGAPRGLYNSVDSWMIVPNIKQNHYTVHGLQSGTRYIFIVKAINQAGSRNSEPTRLKTNSQPFKLDPKMTHKKLKISNDGLQMEKDESSLKKSHTPERFSGTGCYGAAGNIFIDSGCHYWEVVMGSSTWYAIGIAYKSAPKNEWIGKNASSWVFSRCNSNFVVRHNNKEMLVDVPPHLKRLGVLLDYDNNMLSFYDPANSLHLHTFDVTFILPVCPTFTIWNKSLMILSGLPAPDFIDYPERQECNCRPQESPYVSGMKTCH 22A0EC26B050EA21 tri18_human E3 ubiquitin-protein ligase Midline-1 MID1 FXY RNF59 TRIM18 XPRF Tripartite motif-containing protein 18 Putative transcription factor XPRF Midin RING finger protein 59 RING finger protein Midline-1 RING-type E3 ubiquitin transferase Midline-1 protein protein human Homo sapiens Human METLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNESVESITAFQCPTCRHVITLSQRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSETRRERAFDANTMTSAEKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEPIPDSHIRGLMCLEHEDEKVNMYCVTDDQLICALCKLVGRHRDHQVAALSERYDKLKQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVMRLRKLAQQIANCKQCIERSASLISQAEHSLKENDHARFLQTAKNITERVSMATASSQVLIPEINLNDTFDTFALDFSREKKLLECLDYLTAPNPPTIREELCTASYDTITVHWTSDDEFSVVSYELQYTIFTGQANVVSLCNSADSWMIVPNIKQNHYTVHGLQSGTKYIFMVKAINQAGSRSSEPGKLKTNSQPFKLDPKSAHRKLKVSHDNLTVERDESSSKKSHTPERFTSQGSYGVAGNVFIDSGRHYWEVVISGSTWYAIGLAYKSAPKHEWIGKNSASWALCRCNNNWVVRHNSKEIPIEPAPHLRRVGILLDYDNGSIAFYDALNSIHLYTFDVAFAQPVCPTFTVWNKCLTIITGLPIPDHLDCTEQLP 673C5120018BA619 ripk2_human Receptor-interacting serine/threonine-protein kinase 2 RIPK2 CARDIAK RICK RIP2 UNQ277/PRO314/PRO34092 RIP-like-interacting CLARP kinase Receptor-interacting protein 2 CARD-containing interleukin-1 beta-converting enzyme-associated kinase Tyrosine-protein kinase RIPK2 protein protein human Homo sapiens Human MNGEAICSALPTIPYHKLADLRYLSRGASGTVSSARHADWRVQVAVKHLHIHTPLLDSERKDVLREAEILHKARFSYILPILGICNEPEFLGIVTEYMPNGSLNELLHRKTEYPDVAWPLRFRILHEIALGVNYLHNMTPPLLHHDLKTQNILLDNEFHVKIADFGLSKWRMMSLSQSRSSKSAPEGGTIIYMPPENYEPGQKSRASIKHDIYSYAVITWEVLSRKQPFEDVTNPLQIMYSVSQGHRPVINEESLPYDIPHRARMISLIESGWAQNPDERPSFLKCLIELEPVLRTFEEITFLEAVIQLKKTKLQSVSSAIHLCDKKKMELSLNIPVNHGPQEESCGSSQLHENSGSPETSRSLPAPQDNDFLSRKAQDCYFMKLHHCPGNHSWDSTISGSQRAAFCDHKTTPCSSAIINPLSTAGNSERLQPGIAQQWIQSKREDIVNQMTEACLNQSLDALLSRDLIMKEDYELVSTKPTRTSKVRQLLDTTDIQGEEFAKVIVQKLKDNKQMGLQPYPEILVVSRSPSLNLLQNKSM DIP protein O43353 original sequence version: 159 DIP protein O43353-1 original sequence version: 116 DIP protein O43353 original sequence version: 116 575A692239505792 tri13_human E3 ubiquitin-protein ligase TRIM13 TRIM13 LEU5 RFP2 RNF77 B-cell chronic lymphocytic leukemia tumor suppressor Leu5 Leukemia-associated protein 5 Putative tumor suppressor RFP2 RING finger protein 77 Ret finger protein 2 Tripartite motif-containing protein 13 RING-type E3 ubiquitin transferase TRIM13 protein protein human Homo sapiens Human MELLEEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGILEGSVRNSLWRPAPFKCPTCRKETSATGINSLQVNYSLKGIVEKYNKIKISPKMPVCKGHLGQPLNIFCLTDMQLICGICATRGEHTKHVFCSIEDAYAQERDAFESLFQSFETWRRGDALSRLDTLETSKRKSLQLLTKDSDKVKEFFEKLQHTLDQKKNEILSDFETMKLAVMQAYDPEINKLNTILQEQRMAFNIAEAFKDVSEPIVFLQQMQEFREKIKVIKETPLPPSNLPASPLMKNFDTSQWEDIKLVDVDKLSLPQDTGTFISKIPWSFYKLFLLILLLGLVIVFGPTMFLEWSLFDDLATWKGCLSNFSSYLTKTADFIEQSVFYWEQVTDGFFIFNERFKNFTLVVLNNVAEFVCKYKLL 94B624345124AEBF mefv_human Pyrin MEFV MEF Marenostrin TRIM20 protein protein human Homo sapiens Human MAKTPSDHLLSTLEELVPYDFEKFKFKLQNTSVQKEHSRIPRSQIQRARPVKMATLLVTYYGEEYAVQLTLQVLRAINQRLLAEELHRAAIQEYSTQENGTDDSAASSSLGENKPRSLKTPDHPEGNEGNGPRPYGGGAASLRCSQPEAGRGLSRKPLSKRREKASEGLDAQGKPRTRSPALPGGRSPGPCRALEGGQAEVRLRRNASSAGRLQGLAGGAPGQKECRPFEVYLPSGKMRPRSLEVTISTGEKAPANPEILLTLEEKTAANLDSATEPRARPTPDGGASADLKEGPGNPEHSVTGRPPDTAASPRCHAQEGDPVDGTCVRDSCSFPEAVSGHPQASGSRSPGCPRCQDSHERKSPGSLSPQPLPQCKRHLKQVQLLFCEDHDEPICLICSLSQEHQGHRVRPIEEVALEHKKKIQKQLEHLKKLRKSGEEQRSYGEEKAVSFLKQTEALKQRVQRKLEQVYYFLEQQEHFFVASLEDVGQMVGQIRKAYDTRVSQDIALLDALIGELEAKECQSEWELLQDIGDILHRAKTVPVPEKWTTPQEIKQKIQLLHQKSEFVEKSTKYFSETLRSEMEMFNVPELIGAQAHAVNVILDAETAYPNLIFSDDLKSVRLGNKWERLPDGPQRFDSCIIVLGSPSFLSGRRYWEVEVGDKTAWILGACKTSISRKGNMTLSPENGYWVVIMMKENEYQASSVPPTRLLIKEPPKRVGIFVDYRVGSISFYNVTARSHIYTFASCSFSGPLQPIFSPGTRDGGKNTAPLTICPVGGQGPD DIP protein O15553 original sequence version: 151 Defects in MEFV are the cause of familial Mediterranean fever autosomal recessive (ARFMF) [MIM:249100]. ARFMF is an inherited disorder characterized by recurrent episodic fever, serosal inflammation and pain in the abdomen, chest or joints. ARFMF is frequently complicated by amyloidosis, which leads to renal failure and can be prophylactically treated with colchicine. ARFMF primarily affects ancestral ethnic groups living around the Mediterranean basin: North African Jews, Armenians, Arabs and Turks. The disease is also distributed in other populations including Greeks, Cypriots, Italians and Spanish, although at a lower prevalence Probably controls the inflammatory response in myelomonocytic cells at the level of the cytoskeleton organization mint Defects in MEFV are the cause of familial Mediterranean fever autosomal dominant (ADFMF) [MIM:134610]. ADFMF is characterized by periodic fever, serosal inflammation and pain in the abdomen, chest or joints as seen also in the autosomal recessive form of the disease. It is associated with renal amyloidosis and characterized by colchicine unresponsiveness 3692E5E6E9FC8204 nod2-trim27 4 8 unspecified role unspecified role bait bait n-terminus 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 p-loop_ntpase sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain 12 unspecified role unspecified role prey prey n-terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association Fig. 1a, 2a, 3d, Suppl. Fig. S4a trim27-nod2 4 8 unspecified role unspecified role prey prey n-terminus 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 12 unspecified role unspecified role bait bait n-terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association Fig. 1b nod2-trim27-1 3 8 unspecified role unspecified role bait bait n-terminus 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 12 unspecified role unspecified role prey prey physical association physical association Fig. 1c nod2-trim27-2 1 8 unspecified role unspecified role bait bait 12 unspecified role unspecified role prey prey physical association physical association Fig. 1d muramyl dipeptide (MDP) (CHEBI:59414) (10 micromolar), a bacterial peptidoglycan fragment trim27-nod2-1 6 8 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 autoradiography autoradiography undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro 12 unspecified role unspecified role bait bait 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 region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain 562-rosetta ii de3 Escherichia coli rosetta ii de3 rosetta ii de3 direct interaction direct interaction Fig. 1e The TRIM27 construct (residues 133-513) lacking the Ring and B-box domains was sufficient to bind NOD2 but binding was weaker compared to the full length TRIM27 or the TRIM27 construct (residues 63-513) lacking only the Ring domain. P14373 increases degradation at protein level of Q9HC27 P14373 is required for ubiquitination of Q9HC27 nod2-trim27-3 3 8 unspecified role unspecified role bait bait n-terminus 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 12 unspecified role unspecified role prey prey n-terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association Fig. 3e muramyl dipeptide (MDP) (CHEBI:59414) (10 micromolar), a bacterial peptidoglycan fragment nod2-trim27-5 5 8 unspecified role unspecified role neutral component neutral component Q9HC29:p.Lys305Arg mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K R Wed May 02 16:28:39 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys305arg' Tue Jun 30 18:06:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys305Arg' mutant does not localize to the nucleus n-terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 12 unspecified role unspecified role neutral component neutral component colocalization colocalization Fig. 5a Sufficient cells (30%) with NOD2 localized to the nucleus were only obtained after treatment with leptomycin B (LMB) (50 nM), an inhibitor of nuclear export. In only a small fraction (less than 5%) of untreated cells NOD2 was found in the nucleus. nod2-ripk2-1 4 8 unspecified role unspecified role bait bait n-terminus 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 16 unspecified role unspecified role prey prey region vsv tag vsv tag vesicular stomatitis virus tag vesicular stomatitis virus tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Suppl. Fig. S4a nod2-ripk2-2 4 8 unspecified role unspecified role bait bait n-terminus 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 16 unspecified role unspecified role prey prey region vsv tag vsv tag vesicular stomatitis virus tag vesicular stomatitis virus tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 12 unspecified role unspecified role prey prey n-terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range association association Suppl. Fig. S4a trim8-nod2 2 8 unspecified role unspecified role prey prey 9 unspecified role unspecified role bait bait physical association physical association Suppl. Fig. S1a trim50-nod2 2 8 unspecified role unspecified role prey prey 11 unspecified role unspecified role bait bait physical association physical association Suppl. Fig. S1a trim27-nod2-2 2 8 unspecified role unspecified role prey prey 12 unspecified role unspecified role bait bait physical association physical association Suppl. Fig. S1a trim8-trim27 2 12 unspecified role unspecified role prey prey 9 unspecified role unspecified role bait bait physical association physical association Suppl. Fig. S1a mid1-trim27 2 12 unspecified role unspecified role prey prey 15 unspecified role unspecified role bait bait physical association physical association Suppl. Fig. S1a mid2-mid2 2 14 unspecified role unspecified role bait bait 14 unspecified role unspecified role prey prey physical association physical association Suppl. Fig. S1a trim5-trim5-1 2 7 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait physical association physical association Suppl. Fig. S1a trim8-trim8-1 2 9 unspecified role unspecified role prey prey 9 unspecified role unspecified role bait bait physical association physical association Suppl. Fig. S1a trim11-trim11 2 10 unspecified role unspecified role prey prey 10 unspecified role unspecified role bait bait physical association physical association Suppl. Fig. S1a trim13-trim13 2 17 unspecified role unspecified role prey prey 17 unspecified role unspecified role bait bait physical association physical association Suppl. Fig. S1a mid1-mid1-9 2 15 unspecified role unspecified role prey prey 15 unspecified role unspecified role bait bait physical association physical association Suppl. Fig. S1a mefv-mefv 2 18 unspecified role unspecified role bait bait 18 unspecified role unspecified role prey prey physical association physical association Suppl. Fig. S1a trim21-trim21-1 2 13 unspecified role unspecified role prey prey 13 unspecified role unspecified role bait bait physical association physical association Suppl. Fig. S1a trim27-trim27 2 12 unspecified role unspecified role prey prey 12 unspecified role unspecified role bait bait physical association physical association Suppl. Fig. S1a trim50-trim50 2 11 unspecified role unspecified role prey prey 11 unspecified role unspecified role bait bait physical association physical association Suppl. Fig. S1a nod2-trim27-4 4 8 unspecified role unspecified role bait bait n-terminus 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 12 unspecified role unspecified role prey prey n-terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range spry_dom sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain physical association physical association Fig. 1a, 2b, 3d, Suppl. Fig. S4a