DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006 imex curation Shen Y., Joachimiak A., Rosner MR., Tang WJ. 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 Shen Y., Joachimiak A., Rosner MR., Tang WJ. DIP original experiment: DIP-254916X Nature 2006 IMEx Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006 imex curation Shen Y., Joachimiak A., Rosner MR., Tang WJ. 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 Shen Y., Joachimiak A., Rosner MR., Tang WJ. DIP original experiment: DIP-254926X Nature 2006 IMEx Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006 imex curation Shen Y., Joachimiak A., Rosner MR., Tang WJ. 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 Shen Y., Joachimiak A., Rosner MR., Tang WJ. DIP original experiment: DIP-254917X Nature 2006 IMEx Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006 imex curation Shen Y., Joachimiak A., Rosner MR., Tang WJ. 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 Shen Y., Joachimiak A., Rosner MR., Tang WJ. DIP original experiment: DIP-254915X Nature 2006 IMEx Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006 imex curation Shen Y., Joachimiak A., Rosner MR., Tang WJ. Only protein-protein interactions in vitro In vitro protease assay protease assay predetermined predetermined participant predetermined Shen Y., Joachimiak A., Rosner MR., Tang WJ. DIP original experiment: DIP-254920X Nature 2006 IMEx Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006 imex curation Shen Y., Joachimiak A., Rosner MR., Tang WJ. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Shen Y., Joachimiak A., Rosner MR., Tang WJ. DIP original experiment: DIP-254914X Nature 2006 IMEx Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006 imex curation Shen Y., Joachimiak A., Rosner MR., Tang WJ. 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 Shen Y., Joachimiak A., Rosner MR., Tang WJ. DIP original experiment: DIP-254923X Nature 2006 IMEx Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006 imex curation Shen Y., Joachimiak A., Rosner MR., Tang WJ. 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 Shen Y., Joachimiak A., Rosner MR., Tang WJ. DIP original experiment: DIP-254925X Nature 2006 IMEx Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006 imex curation Shen Y., Joachimiak A., Rosner MR., Tang WJ. 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 Shen Y., Joachimiak A., Rosner MR., Tang WJ. DIP original experiment: DIP-254918X Nature 2006 IMEx Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006 imex curation Shen Y., Joachimiak A., Rosner MR., Tang WJ. Only protein-protein interactions in vitro In vitro protease assay protease assay predetermined predetermined participant predetermined Shen Y., Joachimiak A., Rosner MR., Tang WJ. DIP original experiment: DIP-254919X Nature 2006 IMEx Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006 imex curation Shen Y., Joachimiak A., Rosner MR., Tang WJ. Only protein-protein interactions in vitro In vitro protease assay protease assay predetermined predetermined participant predetermined Shen Y., Joachimiak A., Rosner MR., Tang WJ. DIP original experiment: DIP-254921X Nature 2006 IMEx Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006 imex curation Shen Y., Joachimiak A., Rosner MR., Tang WJ. 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 Shen Y., Joachimiak A., Rosner MR., Tang WJ. DIP original experiment: DIP-254924X Nature 2006 IMEx Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006 imex curation Shen Y., Joachimiak A., Rosner MR., Tang WJ. Only protein-protein interactions in vitro In vitro protease assay protease assay predetermined predetermined participant predetermined Shen Y., Joachimiak A., Rosner MR., Tang WJ. DIP original experiment: DIP-254922X Nature 2006 IMEx Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. iapp_human Islet amyloid polypeptide IAPP Amylin Diabetes-associated peptide Insulinoma amyloid peptide protein protein human Homo sapiens Human MGILKLQVFLIVLSVALNHLKATPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYGKRNAVEVLKREPLNYLPL DIP protein P10997 original sequence version: 138 not sure about the protein origin DIP protein P10997 original sequence version: 92 DIP protein P10997 original sequence version: 88 mint AA8B1F7FD9FCB4BD p14735-1 Insulin-degrading enzyme IDE Abeta-degrading protease Insulin protease Insulysin protein protein human Homo sapiens Human MRYRLAWLLHPALPSTFRSVLGARLPPPERLCGFQKKTYSKMNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSCPVVGEFPCQNDINLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHINFMAAKL DIP protein P14735-1 original sequence version: 138 DIP protein P14735 original sequence version: 108 DIP protein P14735-1 original sequence version: 149 DIP protein P14735 original sequence version: 134 gluc_human Pro-glucagon GCG protein protein human Homo sapiens Human MKSIYFVAGLFVMLVQGSWQRSLQDTEEKSRSFSASQADPLSDPDQMNEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIVEELGRRHADGSFSDEMNTILDNLAARDFINWLIQTKITDRK DIP protein P01275 original sequence version: 152 DIP protein P01275 original sequence version: 107 mint homomint 7A99EEC629B2862C ins_human Insulin INS protein protein human Homo sapiens Human MALWMRLLPLLALLALWGPDPAAAFVNQHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYCN DIP protein P01308 original sequence version: 184 DIP protein P01308 original sequence version: 104 DIP protein P01308 original sequence version: 177 Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver mint homomint Defects in INS are the cause of familial hyperproinsulinemia [MIM:176730] C2C3B23B85E520E5 p05067-pro_0000000093 Amyloid-beta protein 40 APP A4 AD1 ABPP Alzheimer disease amyloid protein Cerebral vascular amyloid peptide PreA4 Protease nexin-II APPI Amyloid precursor protein Amyloid-beta A4 protein Alzheimer disease amyloid A4 protein homolog Amyloid-beta (A4) precursor protein protein protein human Homo sapiens Human DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV 672 711 D563D7858C3768F1 ide-ide-1 6 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction app-ide-1 12 18 unspecified role unspecified role unspecified role unspecified role chemical synthesis Chemical synthesis (Chemical synthesis) 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction ide-ins-1 4 17 unspecified role unspecified role unspecified role unspecified role Region 25-54 Region 25-54 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 15 unspecified role unspecified role unspecified role unspecified role Region 42-1019 Region 42-1019 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 ide-ins-2 10 17 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 25-54 Region 25-54 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 15 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli protein cleavage protein cleavage iapp-ide-1 8 14 unspecified role unspecified role unspecified role unspecified role Region 34-70 Region 34-70 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction app-ide-2 5 18 enzyme target enzyme target substrate substrate unspecified role unspecified role chemical synthesis Chemical synthesis (Chemical synthesis) 15 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli protein cleavage protein cleavage app-ide-3 1 18 unspecified role unspecified role unspecified role unspecified role chemical synthesis Chemical synthesis (Chemical synthesis) 15 unspecified role unspecified role unspecified role unspecified role Region 42-1019 Region 42-1019 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 iapp-ide-2 11 14 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 34-70 Region 34-70 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 15 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli protein cleavage protein cleavage iapp-ide-3 3 14 unspecified role unspecified role unspecified role unspecified role Region 34-70 Region 34-70 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 15 unspecified role unspecified role unspecified role unspecified role Region 42-1019 Region 42-1019 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 gcg-ide-1 2 16 unspecified role unspecified role unspecified role unspecified role Region 53-81 Region 53-81 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction gcg-ide-2 13 16 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 53-81 Region 53-81 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 15 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli protein cleavage protein cleavage ide-ins-3 7 17 unspecified role unspecified role unspecified role unspecified role Region 25-54 Region 25-54 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction gcg-ide-3 9 16 unspecified role unspecified role unspecified role unspecified role Region 53-81 Region 53-81 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 15 unspecified role unspecified role unspecified role unspecified role Region 42-1019 Region 42-1019 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