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/ The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein. The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein. Biochem. Biophys. Res. Commun. (0006-291X) 2006 imex curation Chen TY., Liu PH., Ruan CT., Chiu L., Kung FL. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Synapse - Interactions of proteins with an established role in the presynapse. Apoptosis - Interactions involving proteins with a function related to apoptosis Alzheimers - Interactions investigated in the context of Alzheimers disease flkung@ha.mc.ntu.edu.tw 16-Dec-2008: Contacted by JYOTI. Human brain cDNA. davet Only protein-protein interactions human-sh_sy5y Homo sapiens SH-SY5Y cell line sh_sy5y Human neuroblastoma cells anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Chen TY., Liu PH., Ruan CT., Chiu L., Kung FL. Synapse - Interactions of proteins with an established role in the presynapse. flkung@ha.mc.ntu.edu.tw Accepted 2008-Not a month!-2 by DAVET. 16-Dec-2008: Contacted by JYOTI. Human brain cDNA. Biochem. Biophys. Res. Commun. (0006-291X) 2006 davet Only protein-protein interactions imex curation The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein. The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein. Biochem. Biophys. Res. Commun. (0006-291X) 2006 imex curation Chen TY., Liu PH., Ruan CT., Chiu L., Kung FL. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Synapse - Interactions of proteins with an established role in the presynapse. Apoptosis - Interactions involving proteins with a function related to apoptosis Alzheimers - Interactions investigated in the context of Alzheimers disease flkung@ha.mc.ntu.edu.tw 16-Dec-2008: Contacted by JYOTI. Human brain cDNA. davet Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Chen TY., Liu PH., Ruan CT., Chiu L., Kung FL. Synapse - Interactions of proteins with an established role in the presynapse. flkung@ha.mc.ntu.edu.tw Accepted 2008-Not a month!-2 by DAVET. 16-Dec-2008: Contacted by JYOTI. Human brain cDNA. Biochem. Biophys. Res. Commun. (0006-291X) 2006 davet Only protein-protein interactions imex curation The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein. The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein. Biochem. Biophys. Res. Commun. (0006-291X) 2006 imex curation Chen TY., Liu PH., Ruan CT., Chiu L., Kung FL. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Synapse - Interactions of proteins with an established role in the presynapse. Apoptosis - Interactions involving proteins with a function related to apoptosis Alzheimers - Interactions investigated in the context of Alzheimers disease flkung@ha.mc.ntu.edu.tw 16-Dec-2008: Contacted by JYOTI. Human brain cDNA. davet 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 Chen TY., Liu PH., Ruan CT., Chiu L., Kung FL. Synapse - Interactions of proteins with an established role in the presynapse. flkung@ha.mc.ntu.edu.tw Accepted 2008-Not a month!-2 by DAVET. 16-Dec-2008: Contacted by JYOTI. Human brain cDNA. Biochem. Biophys. Res. Commun. (0006-291X) 2006 davet Only protein-protein interactions imex curation The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein. The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein. Biochem. Biophys. Res. Commun. (0006-291X) 2006 imex curation Chen TY., Liu PH., Ruan CT., Chiu L., Kung FL. Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Synapse - Interactions of proteins with an established role in the presynapse. Apoptosis - Interactions involving proteins with a function related to apoptosis Alzheimers - Interactions investigated in the context of Alzheimers disease flkung@ha.mc.ntu.edu.tw 16-Dec-2008: Contacted by JYOTI. Human brain cDNA. davet 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 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Chen TY., Liu PH., Ruan CT., Chiu L., Kung FL. Synapse - Interactions of proteins with an established role in the presynapse. flkung@ha.mc.ntu.edu.tw Accepted 2008-Not a month!-2 by DAVET. 16-Dec-2008: Contacted by JYOTI. Human brain cDNA. Biochem. Biophys. Res. Commun. (0006-291X) 2006 davet Only protein-protein interactions imex curation flot1_human Flotillin-1 FLOT1 protein protein human Homo sapiens Human MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVTGEVLDILTRLPESVERLTGVSISQVNHKPLRTA C69E5421E565F53A p53_mouse Cellular tumor antigen p53 Tp53 P53 Trp53 Tumor suppressor p53 protein protein mouse Mus musculus Mouse MTAMEESQSDISLELPLSQETFSGLWKLLPPEDILPSPHCMDDLLLPQDVEEFFEGPSEALRVSGAPAAQDPVTETPGPVAPAPATPWPLSSFVPSQKTYQGNYGFHLGFLQSGTAKSVMCTYSPPLNKLFCQLAKTCPVQLWVSATPPAGSRVRAMAIYKKSQHMTEVVRRCPHHERCSDGDGLAPPQHLIRVEGNLYPEYLEDRQTFRHSVVVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENFRKKEVLCPELPPGSAKRALPTCTSASPPQKKKPLDGEYFTLKIRGRKRFEMFRELNEALELKDAHATEESGDSRAHSSYLKTKKGQSTSRHKKTMVKKVGPDSD DIP protein P02340 original sequence version: 117 DIP protein P02340 original sequence version: 165 DIP protein P02340 original sequence version: 187 DIP protein P02340 original sequence version: 201 DIP protein P02340 original sequence version: 111 DIP protein P02340 original sequence version: 141 DIP protein P02340 original sequence version: 180 DIP protein P02340 original sequence version: 163 DIP protein P02340 original sequence version: 152 ED5A607378D921D7 a4_human Amyloid-beta precursor protein APP A4 AD1 Alzheimer disease amyloid protein ABPP PreA4 Cerebral vascular amyloid peptide 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 MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN DIP protein P05067 original sequence version: 160 DIP protein P05067 original sequence version: 207 DIP protein P05067 original sequence version: 185 DIP protein P05067 original sequence version: 188 A12EE761403740F5 lt_sv40 Large T antigen protein protein sv40 sv40 SV40 MDKVLNREESLQLMDLLGLERSAWGNIPLMRKAYLKKCKEFHPDKGGDEEKMKKMNTLYKKMEDGVKYAHQPDFGGFWDATEIPTYGTDEWEQWWNAFNEENLFCSEEMPSSDDEATADSQHSTPPKKKRKVEDPKDFPSELLSFLSHAVFSNRTLACFAIYTTKEKAALLYKKIMEKYSVTFISRHNSYNHNILFFLTPHRHRVSAINNYAQKLCTFSFLICKGVNKEYLMYSALTRDPFSVIEESLPGGLKEHDFNPEEAEETKQVSWKLVTEYAMETKCDDVLLLLGMYLEFQYSFEMCLKCIKKEQPSHYKYHEKHYANAAIFADSKNQKTICQQAVDTVLAKKRVDSLQLTREQMLTNRFNDLLDRMDIMFGSTGSADIEEWMAGVAWLHCLLPKMDSVVYDFLKCMVYNIPKKRYWLFKGPIDSGKTTLAAALLELCGGKALNVNLPLDRLNFELGVAIDQFLVVFEDVKGTGGESRDLPSGQGINNLDNLRDYLDGSVKVNLEKKHLNKRTQIFPPGIVTMNEYSVPKTLQARFVKQIDFRPKDYLKHCLERSEFLLEKRIIQSGIALLLMLIWYRPVAEFAQSIQSRIVEWKERLDKEFSLSVYQKMKFNVAMGIGVLDWLRNSDDDDEDSQENADKNEDGGEKNMEDSGHETGIDSQSQGSFQAPQSSQSVHDHNQPYHICRGFTCFKKPPTPPPEPET 3E37D4BAFC5D59BD app-flot1-1 4 5 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind full dna sequence full identification by DNA sequencing full dna sequence certain certain sequence position certain certain certain sequence position certain 7 unspecified role unspecified role bait bait cytoplasmic region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 13 11 physical association physical association Yeast two-hybrid analysis of the interaction of AICD with flotillin-1 tp53-sv40-1 3 8 unspecified role unspecified role prey prey 6 unspecified role unspecified role bait bait physical association physical association AH109 cotransformed with pGBKT7-53/pGADT7-T was used as a positive control since p53 is known to interact with SV40 large T-antigen, Fig. 1 Positive control app-flot1-2 2 5 unspecified role unspecified role prey prey human-sh_sy5y Homo sapiens SH-SY5Y cell line sh_sy5y Human neuroblastoma cells 7 unspecified role unspecified role bait bait cytoplasmic region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) physical association physical association Our results indicate that GST-AICD, but not GST alone, is able to bind to the full-length flotillin-1 (Fig. 3A). Fig. 2A app-flot1-3 3 7 unspecified role unspecified role bait bait cytoplasmic region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 5 unspecified role unspecified role prey prey region required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain physical association physical association Yeast two-hybrid analysis of the interaction of AICD with flotillin-1 Fig. 1 Fig 5 app-flot1-4 1 7 unspecified role unspecified role bait bait 5 unspecified role unspecified role prey prey physical association physical association Results shown in Fig. 4 reveal that flotillin-1 could be coprecipitated with APP and/or APP C-terminal fragment(s) and vice versa. Fig. 4 app-flot1-5 1 5 unspecified role unspecified role bait bait 7 unspecified role unspecified role prey prey physical association physical association Results shown in Fig. 4 reveal that flotillin-1 could be coprecipitated with APP and/or APP C-terminal fragment(s) and vice versa. Fig. 4