DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. Structure (London, England : 1993) 2011 imex curation Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. Only protein-protein interactions human Homo sapiens Human x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. DIP original experiment: DIP-218771X Structure (London, England : 1993) 2011 IMEx The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. Structure (London, England : 1993) 2011 imex curation Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. DIP original experiment: DIP-218769X Structure (London, England : 1993) 2011 IMEx The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. Structure (London, England : 1993) 2011 imex curation Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. Only protein-protein interactions human Homo sapiens Human solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. DIP original experiment: DIP-218768X Structure (London, England : 1993) 2011 IMEx The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. Structure (London, England : 1993) 2011 imex curation Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. DIP original experiment: DIP-218770X Structure (London, England : 1993) 2011 IMEx The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. Structure (London, England : 1993) 2011 imex curation Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. Only protein-protein interactions human Homo sapiens Human x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. DIP original experiment: DIP-218773X Structure (London, England : 1993) 2011 IMEx The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. Structure (London, England : 1993) 2011 imex curation Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. Only protein-protein interactions human Homo sapiens Human tap tandem affinity purification TAP TAP tap western blot western blot Immuno blot Immuno blot Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. DIP original experiment: DIP-218774X Structure (London, England : 1993) 2011 IMEx The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. Structure (London, England : 1993) 2011 imex curation Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. Only protein-protein interactions human Homo sapiens Human solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Harrison OJ., Jin X., Hong S., Bahna F., Ahlsen G., Brasch J., Wu Y., Vendome J., Felsovalyi K., Hampton CM., Troyanovsky RB., Ben-Shaul A., Frank J., Troyanovsky SM., Shapiro L., Honig B. DIP original experiment: DIP-218772X Structure (London, England : 1993) 2011 IMEx The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. cadh1_human Cadherin-1 Epithelial cadherin Uvomorulin CAM 120/80 CDH1 CDHE UVO protein protein human Homo sapiens Human MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPAILGILGGILALLILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD DIP protein P12830 original sequence version: 191 DIP protein P12830 original sequence version: 185 DIP protein P12830 original sequence version: 108 DIP protein P12830 original sequence version: null DIP protein P12830 original sequence version: 134 DIP protein P12830 original sequence version: 147 DIP protein P12830 original sequence version: 174 DIP protein P12830 original sequence version: 189 DIP protein P12830 original sequence version: 156 DIP protein P12830 original sequence version: 201 DIP protein P12830 original sequence version: 117 E427118043A13C67 cadh1_mouse Cadherin-1 Epithelial cadherin Uvomorulin ARC-1 Cdh1 protein protein mouse Mus musculus Mouse MGARCRSFSALLLLLQVSSWLCQELEPESCSPGFSSEVYTFPVPERHLERGHVLGRVRFEGCTGRPRTAFFSEDSRFKVATDGTITVKRHLKLHKLETSFLVRARDSSHRELSTKVTLKSMGHHHHRHHHRDPASESNPELLMFPSVYPGLRRQKRDWVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGAVPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFTVNRDTGVISVLTSGLDRESYPTYTLVVQAADLQGEGLSTTAKAVITVKDINDNAPVFNPSTYQGQVPENEVNARIATLKVTDDDAPNTPAWKAVYTVVNDPDQQFVVVTDPTTNDGILKTAKGLDFEAKQQYILHVRVENEEPFEGSLVPSTATVTVDVVDVNEAPIFMPAERRVEVPEDFGVGQEITSYTAREPDTFMDQKITYRIWRDTANWLEINPETGAIFTRAEMDREDAEHVKNSTYVALIIATDDGSPIATGTGTLLLVLLDVNDNAPIPEPRNMQFCQRNPQPHIITILDPDLPPNTSPFTAELTHGASVNWTIEYNDAAQESLILQPRKDLEIGEYKIHLKLADNQNKDQVTTLDVHVCDCEGTVNNCMKAGIVAAGLQVPAILGILGGILALLILILLLLLFLRRRTVVKEPLLPPDDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDQDQDYDYLNEWGNRFKKLADMYGGGEDD DIP protein P09803 original sequence version: 92 DIP protein P09803 original sequence version: 116 DIP protein P09803 original sequence version: 124 DIP protein P09803 original sequence version: 128 DIP protein P09803 original sequence version: 141 DIP protein P09803 original sequence version: 174 7A6444148D3D5983 cadh2_mouse Cadherin-2 Cdh2 Neural cadherin protein protein mouse Mus musculus Mouse MCRIAGAPRTLLPLLAALLQASVEASGEIALCKTGFPEDVYSAVLPKDVHEGQPLLNVKFSNCNRKRKVQYESSEPADFKVDEDGTVYAVRSFPLTAEQAKFLIYAQDKETQEKWQVAVNLSREPTLTEEPMKEPHEIEEIVFPRQLAKHSGALQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDRELIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGSVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRILSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYTLIIQATDMEGNPTYGLSNTATAVITVTDVNDNPPEFTAMTFYGEVPENRVDVIVANLTVTDKDQPHTPAWNAAYRISGGDPTGRFAILTDPNSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHAGTMLTTLTAQDPDRYMQQNIRYTKLSDPANWLKIDPVNGQITTIAVLDRESPNVKNNIYNATFLASDNGIPPMSGTGTLQIYLLDINDNAPQVLPQEAETCETPEPNSINITALDYDIDPNAGPFAFDLPLSPVTIKRNWTINRLNGDFAQLNLKIKFLEAGIYEVPIIITDSGNPPKSNISILRVKVCQCDSNGDCTDVDRIVGAGLGTGAIIAILLCIIILLILVLMFVVWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTVEPDAIKPVGIRRLDERPIHAEPQYPVRSAAPHPGDIGDFINEGLKAADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGDQDYDYLNDWGPRFKKLADMYGGGDD DIP protein P15116 original sequence version: 114 DIP protein P15116 original sequence version: 105 DIP protein P15116 original sequence version: 125 DIP protein P15116 original sequence version: 113 DIP protein P15116 original sequence version: 117 DIP protein P15116 original sequence version: 147 BDAB8063A23E1F13 cdh1-11 1 9 unspecified role unspecified role unspecified role unspecified role Ectodomain 1-5 Region 157-700 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human direct interaction direct interaction cdh1-12 3 9 unspecified role unspecified role unspecified role unspecified role Ectodomain 1-5 Region 157-700 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P09803:p.[Trp158Ala;Lys170Glu] W158A/K170E mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K E certain certain sequence position certain certain certain sequence position certain W A This feature has been corrected as a result of our quality control procedures. The original label was 'W158A/K170E'. Wed May 02 20:21:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp158ala,lys170glu' Tue Jun 30 17:18:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Trp158Ala;Lys170Glu]' human Homo sapiens Human direct interaction direct interaction cdh1-cdh1-3 6 8 unspecified role unspecified role prey prey human Homo sapiens Human 8 unspecified role unspecified role bait bait Region 1-747 Region 1-747 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain TAP-tag TAP-tag tandem tag tandem tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range human Homo sapiens Human physical association physical association cdh2-5 7 10 unspecified role unspecified role unspecified role unspecified role Ectodomain 1-5 Region 160-712 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human direct interaction direct interaction cdh1-13 2 9 unspecified role unspecified role unspecified role unspecified role Ectodomain 1-2 Region 157-369 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cdh2-6 5 10 unspecified role unspecified role unspecified role unspecified role Ectodomain 1-5 Region 160-712 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human direct interaction direct interaction cdh1-14 4 9 unspecified role unspecified role unspecified role unspecified role Ectodomain 1-2 Region 157-369 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction