DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Nekooki-Machida Y., Kurosawa M., Nukina N., Ito K., Oda T., Tanaka M. Only protein-protein interactions in vitro In vitro filter trap assay filter trap assay Filter retention assay Filter retention assay western blot western blot Immuno blot Immuno blot Nekooki-Machida Y., Kurosawa M., Nukina N., Ito K., Oda T., Tanaka M. DIP original experiment: DIP-260321X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Nekooki-Machida Y., Kurosawa M., Nukina N., Ito K., Oda T., Tanaka M. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Nekooki-Machida Y., Kurosawa M., Nukina N., Ito K., Oda T., Tanaka M. DIP original experiment: DIP-260322X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Nekooki-Machida Y., Kurosawa M., Nukina N., Ito K., Oda T., Tanaka M. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Nekooki-Machida Y., Kurosawa M., Nukina N., Ito K., Oda T., Tanaka M. DIP original experiment: DIP-260323X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Nekooki-Machida Y., Kurosawa M., Nukina N., Ito K., Oda T., Tanaka M. Only protein-protein interactions in vitro In vitro x-ray fiber diffrac x-ray fiber diffraction X-ray X-ray x-ray fiber diffrac predetermined predetermined participant predetermined Nekooki-Machida Y., Kurosawa M., Nukina N., Ito K., Oda T., Tanaka M. DIP original experiment: DIP-260324X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. hd_human Huntingtin HTT IT15 HD Huntington disease protein protein protein human Homo sapiens Human MATLEKLMKAFESLKSFQQQQQQQQQQQQQQQQQQQQQPPPPPPPPPPPQLPQPPPQAQPLLPQPQPPPPPPPPPPGPAVAEEPLHRPKKELSATKKDRVNHCLTICENIVAQSVRNSPEFQKLLGIAMELFLLCSDDAESDVRMVADECLNKVIKALMDSNLPRLQLELYKEIKKNGAPRSLRAALWRFAELAHLVRPQKCRPYLVNLLPCLTRTSKRPEESVQETLAAAVPKIMASFGNFANDNEIKVLLKAFIANLKSSSPTIRRTAAGSAVSICQHSRRTQYFYSWLLNVLLGLLVPVEDEHSTLLILGVLLTLRYLVPLLQQQVKDTSLKGSFGVTRKEMEVSPSAEQLVQVYELTLHHTQHQDHNVVTGALELLQQLFRTPPPELLQTLTAVGGIGQLTAAKEESGGRSRSGSIVELIAGGGSSCSPVLSRKQKGKVLLGEEEALEDDSESRSDVSSSALTASVKDEISGELAASSGVSTPGSAGHDIITEQPRSQHTLQADSVDLASCDLTSSATDGDEEDILSHSSSQVSAVPSDPAMDLNDGTQASSPISDSSQTTTEGPDSAVTPSDSSEIVLDGTDNQYLGLQIGQPQDEDEEATGILPDEASEAFRNSSMALQQAHLLKNMSHCRQPSDSSVDKFVLRDEATEPGDQENKPCRIKGDIGQSTDDDSAPLVHCVRLLSASFLLTGGKNVLVPDRDVRVSVKALALSCVGAAVALHPESFFSKLYKVPLDTTEYPEEQYVSDILNYIDHGDPQVRGATAILCGTLICSILSRSRFHVGDWMGTIRTLTGNTFSLADCIPLLRKTLKDESSVTCKLACTAVRNCVMSLCSSSYSELGLQLIIDVLTLRNSSYWLVRTELLETLAEIDFRLVSFLEAKAENLHRGAHHYTGLLKLQERVLNNVVIHLLGDEDPRVRHVAAASLIRLVPKLFYKCDQGQADPVVAVARDQSSVYLKLLMHETQPPSHFSVSTITRIYRGYNLLPSITDVTMENNLSRVIAAVSHELITSTTRALTFGCCEALCLLSTAFPVCIWSLGWHCGVPPLSASDESRKSCTVGMATMILTLLSSAWFPLDLSAHQDALILAGNLLAASAPKSLRSSWASEEEANPAATKQEEVWPALGDRALVPMVEQLFSHLLKVINICAHVLDDVAPGPAIKAALPSLTNPPSLSPIRRKGKEKEPGEQASVPLSPKKGSEASAASRQSDTSGPVTTSKSSSLGSFYHLPSYLKLHDVLKATHANYKVTLDLQNSTEKFGGFLRSALDVLSQILELATLQDIGKCVEEILGYLKSCFSREPMMATVCVQQLLKTLFGTNLASQFDGLSSNPSKSQGRAQRLGSSSVRPGLYHYCFMAPYTHFTQALADASLRNMVQAEQENDTSGWFDVLQKVSTQLKTNLTSVTKNRADKNAIHNHIRLFEPLVIKALKQYTTTTCVQLQKQVLDLLAQLVQLRVNYCLLDSDQVFIGFVLKQFEYIEVGQFRESEAIIPNIFFFLVLLSYERYHSKQIIGIPKIIQLCDGIMASGRKAVTHAIPALQPIVHDLFVLRGTNKADAGKELETQKEVVVSMLLRLIQYHQVLEMFILVLQQCHKENEDKWKRLSRQIADIILPMLAKQQMHIDSHEALGVLNTLFEILAPSSLRPVDMLLRSMFVTPNTMASVSTVQLWISGILAILRVLISQSTEDIVLSRIQELSFSPYLISCTVINRLRDGDSTSTLEEHSEGKQIKNLPEETFSRFLLQLVGILLEDIVTKQLKVEMSEQQHTFYCQELGTLLMCLIHIFKSGMFRRITAAATRLFRSDGCGGSFYTLDSLNLRARSMITTHPALVLLWCQILLLVNHTDYRWWAEVQQTPKRHSLSSTKLLSPQMSGEEEDSDLAAKLGMCNREIVRRGALILFCDYVCQNLHDSEHLTWLIVNHIQDLISLSHEPPVQDFISAVHRNSAASGLFIQAIQSRCENLSTPTMLKKTLQCLEGIHLSQSGAVLTLYVDRLLCTPFRVLARMVDILACRRVEMLLAANLQSSMAQLPMEELNRIQEYLQSSGLAQRHQRLYSLLDRFRLSTMQDSLSPSPPVSSHPLDGDGHVSLETVSPDKDWYVHLVKSQCWTRSDSALLEGAELVNRIPAEDMNAFMMNSEFNLSLLAPCLSLGMSEISGGQKSALFEAAREVTLARVSGTVQQLPAVHHVFQPELPAEPAAYWSKLNDLFGDAALYQSLPTLARALAQYLVVVSKLPSHLHLPPEKEKDIVKFVVATLEALSWHLIHEQIPLSLDLQAGLDCCCLALQLPGLWSVVSSTEFVTHACSLIYCVHFILEAVAVQPGEQLLSPERRTNTPKAISEEEEEVDPNTQNPKYITAACEMVAEMVESLQSVLALGHKRNSGVPAFLTPLLRNIIISLARLPLVNSYTRVPPLVWKLGWSPKPGGDFGTAFPEIPVEFLQEKEVFKEFIYRINTLGWTSRTQFEETWATLLGVLVTQPLVMEQEESPPEEDTERTQINVLAVQAITSLVLSAMTVPVAGNPAVSCLEQQPRNKPLKALDTRFGRKLSIIRGIVEQEIQAMVSKRENIATHHLYQAWDPVPSLSPATTGALISHEKLLLQINPERELGSMSYKLGQVSIHSVWLGNSITPLREEEWDEEEEEEADAPAPSSPPTSPVNSRKHRAGVDIHSCSQFLLELYSRWILPSSSARRTPAILISEVVRSLLVVSDLFTERNQFELMYVTLTELRRVHPSEDEILAQYLVPATCKAAAVLGMDKAVAEPVSRLLESTLRSSHLPSRVGALHGVLYVLECDLLDDTAKQLIPVISDYLLSNLKGIAHCVNIHSQQHVLVMCATAFYLIENYPLDVGPEFSASIIQMCGVMLSGSEESTPSIIYHCALRGLERLLLSEQLSRLDAESLVKLSVDRVNVHSPHRAMAALGLMLTCMYTGKEKVSPGRTSDPNPAAPDSESVIVAMERVSVLFDRIRKGFPCEARVVARILPQFLDDFFPPQDIMNKVIGEFLSNQQPYPQFMATVVYKVFQTLHSTGQSSMVRDWVMLSLSNFTQRAPVAMATWSLSCFFVSASTSPWVAAILPHVISRMGKLEQVDVNLFCLVATDFYRHQIEEELDRRAFQSVLEVVAAPGSPYHRLLTCLRNVHKVTTC DIP protein P42858 original sequence version: 148 DIP protein P42858 original sequence version: 145 DIP protein P42858 original sequence version: 142 DIP protein P42858 original sequence version: 157 DIP protein P42858 original sequence version: 158 DIP protein P42858 original sequence version: 156 A267509E84D52F0D htt-1 1 5 unspecified role unspecified role unspecified role unspecified role Region 1-120 Region 1-120 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P42858:p.Gln18[42] PolyQ42 mutation mutation certain certain sequence position certain certain certain sequence position certain QQQQQQQQQQQQQQQQQQQQQ QQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQ Tue Jun 30 18:55:09 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln18[42]' ecolx Escherichia coli direct interaction direct interaction htt-2 4 5 unspecified role unspecified role unspecified role unspecified role Region 1-120 Region 1-120 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P42858:p.Gln18[42] q42 poly-glutamine extension mutation mutation certain certain sequence position certain certain certain sequence position certain QQQQQQQQQQQQQQQQQQQQQ QQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQ Wed Jun 13 18:34:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'p.gln18[42]' Tue Jun 30 19:09:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln18[42]' ecolx Escherichia coli direct interaction direct interaction htt-3 2 5 unspecified role unspecified role unspecified role unspecified role Region 1-120 Region 1-120 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P42858:p.Gln18[42] q42 poly-glutamine extension mutation mutation certain certain sequence position certain certain certain sequence position certain QQQQQQQQQQQQQQQQQQQQQ QQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQ Wed Jun 13 18:47:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'p.gln18[42]' Tue Jun 30 19:11:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln18[42]' ecolx Escherichia coli direct interaction direct interaction htt-4 3 5 unspecified role unspecified role unspecified role unspecified role Region 1-120 Region 1-120 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P42858:p.Gln18[42] q42 poly-glutamine extension mutation mutation certain certain sequence position certain certain certain sequence position certain QQQQQQQQQQQQQQQQQQQQQ QQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQ Wed Jun 13 18:55:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'p.gln18[42]' Tue Jun 30 17:48:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln18[42]' ecolx Escherichia coli direct interaction direct interaction