DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264847X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. Only protein-protein interactions in vitro In vitro pull down pull down weight by staining molecular weight estimation by staining weight by staining Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264834X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264839X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264848X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264845X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264842X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264837X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. 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 Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264843X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264841X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. Only protein-protein interactions rat Rattus norvegicus (Rat) Rat fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret predetermined predetermined participant predetermined Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264835X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. 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 Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264846X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264840X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264836X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. 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 Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264844X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. Structure (London, England : 1993) 2015 imex curation Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Song JG., Kostan J., Drepper F., Knapp B., de Almeida Ribeiro E., Konarev PV., Grishkovskaya I., Wiche G., Gregor M., Svergun DI., Warscheid B., Djinović-Carugo K. DIP original experiment: DIP-264838X Structure (London, England : 1993) 2015 IMEx Structural insights into Ca2+-calmodulin regulation of Plectin 1a-integrin β4 interaction in hemidesmosomes. calm_human Calmodulin CALM1 CALM CAM CAM1 CALM2 CAMB CALM3 CAM3 CAMC CAMIII CAM2 CALML2 protein protein human Homo sapiens Human MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK DIP protein P62158 original sequence version: 97 DIP protein P62158 original sequence version: 144 DIP protein P62158 original sequence version: 146 DIP protein P62158 original sequence version: 73 DIP protein P62158 original sequence version: 102 DIP protein P62158 original sequence version: 98 DIP protein P62158 original sequence version: 96 DIP protein P62158 original sequence version: 111 DIP protein P62158 original sequence version: 131 DIP protein P62158 original sequence version: 136 DIP protein P62158 original sequence version: 145 DIP protein P62158 original sequence version: 154 DIP protein P62158 original sequence version: 148 DIP protein P62158 original sequence version: 116 DIP protein P62158 original sequence version: 120 DIP protein P62158 original sequence version: 130 6B4BC3FCDE10727B q9qxs1-3 Plectin Plec Plec1 Plectin-1 Plectin-6 protein protein mouse Mus musculus Mouse MSQHRLRVPEPEGLGSKRTSSEDNLYLAVLRASEGKKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLYDAMPRVPGAQDGVRANELQLRWQEYRELVLLLLQWIRHHTAAFEERKFPSSFEEIEILWCQFLKFKETELPAKEADKNRSKVIYQSLEGAVQAGQLKIPPGYHPLDVEKEWGKLHVAILEREKQLRSEFERLECLQRIVSKLQMEAGLCEEQLNQADALLQSDIRLLASGKVAQRAGEVERDLDKADGMIRLLFNDVQTLKDGRHPQGEQMYRRVYRLHERLVAIRTEYNLRLKAGVGAPVTQVTLQSTQRRPELEDSTLRYLQDLLAWVEENQRRIDSAEWGVDLPSVEAQLGSHRGMHQSIEEFRAKIERARNDESQLSPATRGAYRDCLGRLDLQYAKLLNSSKARLRSLESLHGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEIQNTGDRLLREDHPARPTVESFQAALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLQKLQETLRRKYSCDRTITVTRLEDLLQDAQDEKEQLNEYKGHLSGLAKRAKAIVQLKPRNPAHPVRGHVPLIAVCDYKQVEVTVHKGDQCQLVGPAQPSHWKVLSGSSSEAAVPSVCFLVPPPNQEAQEAVARLEAQHQALVTLWHQLHVDMKSLLAWQSLSRDIQLIRSWSLVTFRTLKPEEQRQALRNLELHYQAFLRDSQDAGGFGPEDRLVAEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKDPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKALPNGRDAPDGPSVEAEPEYTFEGLRQKVPAQQLQEAGILSQEELQRLAQGHTTVAELTQREDVYRYLKGRSSIAGLLLKPTNEKLSVYTALQRQLLSPGTALILLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVRDHGVRLLEAQIATGGIIDPVHSHRVPVDVAYKRGYFDEEMNRILSDPSDDTKGFFDPNTHENLTYLQLLERCVEDPETGLRLLPLTDKAAKGGELVYTDTEARDVFEKATVSAPFGKFQGRTVTIWEIINSEYFTAEQRRDLLQQFRTGHITVEKIIKIVITVVEEHERKGQLCFEGLRALVPAAELLDSGVISHELYQQLQRGERSVREVAEADSVRQALRGTNVIAGVWLEEAGQKLSIYEALKKDLLQPEVAVALLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPELHEKLLSAEKAVTGYRDPYSGQSVSLFQALKKGLIPREQGLRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKETNRALTSPRDDARVYHDPSTQEPVTYSQLQQRCRSDQLTGLSLLPLSEKAVRARQEEVYSELQARETLEQAKVEVPVGSFKGRAMTVWELISSEYFTEEQRQELLRQFRTGKVTVEKVIKIVITIVEEVETRRQERLSFSGLRAPVPASELLDAKILSRAQFDQLKDGKTSVKELSEVGSVRTLLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKLLSAEKAVTGYKDPYSGNTISLFQAMKKGLVLRDHAIRLLEAQVATGGIIDPVHSHRLPVDVAYQRGYFDEEMNRVLADPSDDTKGFFDPNTHENLTYLQLLERCVEDPETGLRLLPLKGAEKTEVVETTQVYTEEETRRAFEETQIDIPGGGSHGGSSMSLWEVMQSNMIPEDQRARLMADFQAGRVTKERMIIIIIEIIEKTEIIRQQNLASYDYVRRRLTAEDLYEARIISLETYNLFREGTKNLREVLEMESAWRYLYGTGAVAGVYLPGSRQTLTIYQALKKGLLSAEVARLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRLLSAERAVTGYRDPYTEQTISLFQAMKKELIPAEEALRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQLSEPSEVRSYVDPSTDERLSYTQLLKRCRRDDPSGQMLLLLSDARKLTFRGLRKQITVEELVRSQVMDEATALQLQEGLTSIEEVTKNLQKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFELLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKLLSAERAVTGYKDPYSGKLISLFQAMKKGLILKDHGIRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEILTDPSDDTKGFFDPNTEENLTYLQLMERCITDPQTGLCLLPLKEKKRERKTSSKSSVRKRRVVIVDPETGKEMSVYEAYRKGLIDHQTYLELSEQECEWEEITISSSDGVVKSMIIDRRSGRQYDIDDAITKNLIDRSALDQYRAGTLSITEFADMLSGNAGGFRSRSSSVGSSSSYPISSAGPRTQLASWSDPTEETGPVAGILDTETLEKVSITEAMHRNLVDNITGQRLLEAQACTGGIIDPSTGERFPVTEAVNKGLVDKIMVDRINLAQKAFCGFEDPRTKTKMSAAQALKKGWLYYEAGQRFLEVQYLTGGLIEPDTPGRVSLDEALQRGTVDARTAQKLRDVSAYSKYLTCPKTKLKISYKDALDRSMVEEGTGLRLLEAAAQSSKGYYSPYSVSGSGSTAGSRTGSRTGSRAGSRRGSFDATGSGFSMTFSSSSYSSSGYGRRYASGPSASLGGPESAVA DIP protein Q9QXS1-3 original sequence version: 144 Contains a phosphoserine at position 21. Contains a phosphotyrosine at position 26. itb4_human Integrin beta-4 GP150 ITGB4 protein protein human Homo sapiens Human MAGPRPSPWARLLLAALISVSLSGTLANRCKKAPVKSCTECVRVDKDCAYCTDEMFRDRRCNTQAELLAAGCQRESIVVMESSFQITEETQIDTTLRRSQMSPQGLRVRLRPGEERHFELEVFEPLESPVDLYILMDFSNSMSDDLDNLKKMGQNLARVLSQLTSDYTIGFGKFVDKVSVPQTDMRPEKLKEPWPNSDPPFSFKNVISLTEDVDEFRNKLQGERISGNLDAPEGGFDAILQTAVCTRDIGWRPDSTHLLVFSTESAFHYEADGANVLAGIMSRNDERCHLDTTGTYTQYRTQDYPSVPTLVRLLAKHNIIPIFAVTNYSYSYYEKLHTYFPVSSLGVLQEDSSNIVELLEEAFNRIRSNLDIRALDSPRGLRTEVTSKMFQKTRTGSFHIRRGEVGIYQVQLRALEHVDGTHVCQLPEDQKGNIHLKPSFSDGLKMDAGIICDVCTCELQKEVRSARCSFNGDFVCGQCVCSEGWSGQTCNCSTGSLSDIQPCLREGEDKPCSGRGECQCGHCVCYGEGRYEGQFCEYDNFQCPRTSGFLCNDRGRCSMGQCVCEPGWTGPSCDCPLSNATCIDSNGGICNGRGHCECGRCHCHQQSLYTDTICEINYSAIHPGLCEDLRSCVQCQAWGTGEKKGRTCEECNFKVKMVDELKRAEEVVVRCSFRDEDDDCTYSYTMEGDGAPGPNSTVLVHKKKDCPPGSFWWLIPLLLLLLPLLALLLLLCWKYCACCKACLALLPCCNRGHMVGFKEDHYMLRENLMASDHLDTPMLRSGNLKGRDVVRWKVTNNMQRPGFATHAASINPTELVPYGLSLRLARLCTENLLKPDTRECAQLRQEVEENLNEVYRQISGVHKLQQTKFRQQPNAGKKQDHTIVDTVLMAPRSAKPALLKLTEKQVEQRAFHDLKVAPGYYTLTADQDARGMVEFQEGVELVDVRVPLFIRPEDDDEKQLLVEAIDVPAGTATLGRRLVNITIIKEQARDVVSFEQPEFSVSRGDQVARIPVIRRVLDGGKSQVSYRTQDGTAQGNRDYIPVEGELLFQPGEAWKELQVKLLELQEVDSLLRGRQVRRFHVQLSNPKFGAHLGQPHSTTIIIRDPDELDRSFTSQMLSSQPPPHGDLGAPQNPNAKAAGSRKIHFNWLPPSGKPMGYRVKYWIQGDSESEAHLLDSKVPSVELTNLYPYCDYEMKVCAYGAQGEGPYSSLVSCRTHQEVPSEPGRLAFNVVSSTVTQLSWAEPAETNGEITAYEVCYGLVNDDNRPIGPMKKVLVDNPKNRMLLIENLRESQPYRYTVKARNGAGWGPEREAIINLATQPKRPMSIPIIPDIPIVDAQSGEDYDSFLMYSDDVLRSPSGSQRPSVSDDTGCGWKFEPLLGEELDLRRVTWRLPPELIPRLSASSGRSSDAEAPHGPPDDGGAGGKGGSLPRSATPGPPGEHLVNGRMDFAFPGSTNSLHRMTTTSAAAYGTHLSPHVPHRVLSTSSTLTRDYNSLTRSEHSHSTTLPRDYSTLTSVSSHDSRLTAGVPDTPTRLVFSALGPTSLRVSWQEPRCERPLQGYSVEYQLLNGGELHRLNIPNPAQTSVVVEDLLPNHSYVFRVRAQSQEGWGREREGVITIESQVHPQSPLCPLPGSAFTLSTPSAPGPLVFTALSPDSLQLSWERPRRPNGDIVGYLVTCEMAQGGGPATAFRVDGDSPESRLTVPGLSENVPYKFKVQARTTEGFGPEREGIITIESQDGGPFPQLGSRAGLFQHPLQSEYSSITTTHTSATEPFLVDGLTLGAQHLEAGGSLTRHVTQEFVSRTLTTSGTLSTHMDQQFFQT DIP protein P16144 original sequence version: 196 09710FFBBD719469 calm1-plec-1 2 17 unspecified role unspecified role prey prey Region 23-263 Region 23-263 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Region 1-32 Region 1-32 required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role bait bait Region 2-149 Region 2-149 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 itgb4-plec-7 9 18 unspecified role unspecified role unspecified role unspecified role Cl-E Cl-E xlnk-res-res crosslinked residues XLNK-Res-Res modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain Region 1126-1355 Region 1126-1355 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 1-263 Region 1-263 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain CL-K CL-K xlnk-res-res crosslinked residues XLNK-Res-Res modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-plec-2 14 17 unspecified role unspecified role unspecified role unspecified role Region 1-263 Region 1-263 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9QXS1-3:p.[Leu25Asp;Val29Asp] L25D/V29D 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 V D certain certain sequence position certain certain certain sequence position certain L D This feature has been corrected as a result of our quality control procedures. The original label was 'L25D/V29D'. Wed May 02 20:29:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu25asp,val29asp' Tue Jun 30 20:24:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu25Asp;Val29Asp]' ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction plec-calm1-1 10 17 unspecified role unspecified role fluorescence donor fluorescence donor Region 1-263 Region 1-263 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain CFP-tag CFP-tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q9QXS1-3:p.[Leu25Asp;Val29Asp] L25D/V29D 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 V D certain certain sequence position certain certain certain sequence position certain L D This feature has been corrected as a result of our quality control procedures. The original label was 'L25D/V29D'. Wed May 02 17:03:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu25asp,val29asp' Tue Jun 30 16:42:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu25Asp;Val29Asp]' rat Rattus norvegicus (Rat) Rat 16 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept Region 2-149 Region 2-149 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain YFP-tag YFP-tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal Out of date range Feature range: Line: 1272, Character: 10: It is not consistent to have a 'c-terminal' range position with a value different from the sequence length because 'c-terminal' means the last amino acid of the participant.However, we can accept a position null or 0 if the participant sequence is not known. Actual position : (0-0), sequence length: 149, It is not consistent to have a 'c-terminal' range position with a value different from the sequence length because 'c-terminal' means the last amino acid of the participant.However, we can accept a position null or 0 if the participant sequence is not known. Actual position : (0-0), sequence length: 149 rat Rattus norvegicus (Rat) Rat proximity proximity close-contact colocalization neighbourhood interaction itgb4-plec-8 4 18 unspecified role unspecified role unspecified role unspecified role Region 1126-1355 Region 1126-1355 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 23-263 Region 23-263 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 calm1-plec-3 15 17 unspecified role unspecified role unspecified role unspecified role Region 1-263 Region 1-263 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain CL-K CL-K xlnk-res-res crosslinked residues XLNK-Res-Res modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role Region 2-149 Region 2-149 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Cl-E Cl-E xlnk-res-res crosslinked residues XLNK-Res-Res modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-plec-4 5 17 unspecified role unspecified role unspecified role unspecified role Region 1-263 Region 1-263 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 calm1-plec-5 3 17 unspecified role unspecified role unspecified role unspecified role Region 1-263 Region 1-263 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain CL-K CL-K xlnk-res-res crosslinked residues XLNK-Res-Res modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role Region 2-149 Region 2-149 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Cl-E Cl-E xlnk-res-res crosslinked residues XLNK-Res-Res modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-plec-6 13 17 unspecified role unspecified role unspecified role unspecified role Region 1-263 Region 1-263 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain CL-K CL-K xlnk-res-res crosslinked residues XLNK-Res-Res modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role Region 2-149 Region 2-149 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Cl-E Cl-E xlnk-res-res crosslinked residues XLNK-Res-Res modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-plec-7 6 17 unspecified role unspecified role unspecified role unspecified role Region 1-263 Region 1-263 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9QXS1-3:p.[Leu25Asp;Val29Asp] L25D/V29D 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 V D certain certain sequence position certain certain certain sequence position certain L D This feature has been corrected as a result of our quality control procedures. The original label was 'L25D/V29D'. Wed May 02 19:20:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu25asp,val29asp' Tue Jun 30 19:19:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu25Asp;Val29Asp]' ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role Region 7-74 Region 7-74 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Region 84-149 Region 84-149 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 itgb4-plec-9 11 18 unspecified role unspecified role unspecified role unspecified role Region 1126-1355 Region 1126-1355 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 23-263 Region 23-263 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 itgb4-plec-10 1 18 unspecified role unspecified role unspecified role unspecified role Region 1126-1355 Region 1126-1355 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 17 unspecified role unspecified role unspecified role unspecified role Region 23-263 Region 23-263 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 calm1-plec-8 8 17 unspecified role unspecified role unspecified role unspecified role Region 23-263 Region 23-263 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 7-74 Region 7-74 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 calm1-plec-9 12 17 unspecified role unspecified role unspecified role unspecified role Region 1-263 Region 1-263 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain CL-K CL-K xlnk-res-res crosslinked residues XLNK-Res-Res modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role Region 2-149 Region 2-149 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Cl-E Cl-E xlnk-res-res crosslinked residues XLNK-Res-Res modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction calm1-plec-10 7 17 unspecified role unspecified role unspecified role unspecified role Region 1-263 Region 1-263 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain CL-K CL-K xlnk-res-res crosslinked residues XLNK-Res-Res modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role Region 2-149 Region 2-149 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Cl-E Cl-E xlnk-res-res crosslinked residues XLNK-Res-Res modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction