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 synaptic acetylcholinesterase tetramer assembles around a polyproline II helix. The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix. EMBO J. (0261-4189) 2004 Dvir H., Harel M., Bon S., Liu WQ., Vidal M., Garbay C., Sussman JL., Massoulie J., Silman I. Synthetic PRAD was immobilized on CNBr-activated Sepharose beads Joel.Sussman@weizmann.ac.il, Israel.Silman@weizmann.ac.il 2008-02-13: JS Garavelli, EMBL-EBI, The Wellcome Trust Genome Campus, Hinxton, UK. davet in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Dvir H., Harel M., Bon S., Liu WQ., Vidal M., Garbay C., Sussman JL., Massoulie J., Silman I. Synthetic PRAD was immobilized on CNBr-activated Sepharose beads Joel.Sussman@weizmann.ac.il, Israel.Silman@weizmann.ac.il Accepted 2008-MAR-20 by DAVET. 2008-02-13: JS Garavelli, EMBL-EBI, The Wellcome Trust Genome Campus, Hinxton, UK. EMBO J. (0261-4189) 2004 davet The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix. The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix. EMBO J. (0261-4189) 2004 Dvir H., Harel M., Bon S., Liu WQ., Vidal M., Garbay C., Sussman JL., Massoulie J., Silman I. Synthetic PRAD was immobilized on CNBr-activated Sepharose beads Joel.Sussman@weizmann.ac.il, Israel.Silman@weizmann.ac.il 2008-02-13: JS Garavelli, EMBL-EBI, The Wellcome Trust Genome Campus, Hinxton, UK. davet in vitro In vitro anti bait coip anti bait coimmunoprecipitation anti bait coip weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Dvir H., Harel M., Bon S., Liu WQ., Vidal M., Garbay C., Sussman JL., Massoulie J., Silman I. Synthetic PRAD was immobilized on CNBr-activated Sepharose beads Joel.Sussman@weizmann.ac.il, Israel.Silman@weizmann.ac.il Accepted 2008-MAR-20 by DAVET. 2008-02-13: JS Garavelli, EMBL-EBI, The Wellcome Trust Genome Campus, Hinxton, UK. EMBO J. (0261-4189) 2004 davet The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix. The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix. EMBO J. (0261-4189) 2004 Dvir H., Harel M., Bon S., Liu WQ., Vidal M., Garbay C., Sussman JL., Massoulie J., Silman I. Synthetic PRAD was immobilized on CNBr-activated Sepharose beads Joel.Sussman@weizmann.ac.il, Israel.Silman@weizmann.ac.il 2008-02-13: JS Garavelli, EMBL-EBI, The Wellcome Trust Genome Campus, Hinxton, UK. davet in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Dvir H., Harel M., Bon S., Liu WQ., Vidal M., Garbay C., Sussman JL., Massoulie J., Silman I. Synthetic PRAD was immobilized on CNBr-activated Sepharose beads Joel.Sussman@weizmann.ac.il, Israel.Silman@weizmann.ac.il Accepted 2008-MAR-20 by DAVET. 2008-02-13: JS Garavelli, EMBL-EBI, The Wellcome Trust Genome Campus, Hinxton, UK. EMBO J. (0261-4189) 2004 davet aces_rat Acetylcholinesterase Ache protein protein rat Rattus norvegicus (Rat) Rat MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 2EDAE7D46282E7C0 colq_human Acetylcholinesterase collagenic tail peptide COLQ AChE Q subunit Acetylcholinesterase-associated collagen protein protein human Homo sapiens Human MVVLNPMTLGIYLQLFFLSIVSQPTFINSVLPISAALPSLDQKKRGGHKACCLLTPPPPPLFPPPFFRGGRSPLLSPDMKNLMLELETSQSPCMQGSLGSPGPPGPQGPPGLPGKTGPKGEKGELGRPGRKGRPGPPGVPGMPGPIGWPGPEGPRGEKGDLGMMGLPGSRGPMGSKGYPGSRGEKGSRGEKGDLGPKGEKGFPGFPGMLGQKGEMGPKGEPGIAGHRGPTGRPGKRGKQGQKGDSGVMGPPGKPGPSGQPGRPGPPGPPPAGQLIMGPKGERGFPGPPGRCLCGPTMNVNNPSYGESVYGPSSPRVPVIFVVNNQEELERLNTQNAIAFRRDQRSLYFKDSLGWLPIQLTPFYPVDYTADQHGTCGDGLLQPGEECDDGNSDVGDDCIRCHRAYCGDGHRHEGVEDCDGSDFGYLTCETYLPGSYGDLQCTQYCYIDSTPCRYFT A95D3E5D5ECDBE55 aces_human Acetylcholinesterase ACHE protein protein human Homo sapiens Human MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL B9AA84C77831C302 ache-colq-1 1 5 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 6 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P22303:p.Cys611Ser mutation mutation certain certain sequence position certain certain certain sequence position certain C S Wed May 02 18:22:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys611ser' Tue Jun 30 18:10:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys611Ser' undefined mutation mutation mutation certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:54:31 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'met595semet' chemical synthesis Chemical synthesis (Chemical synthesis) 9 11 direct interaction direct interaction Fig. 3 Binding of WAT to PRAD-Sepharose. Sequence of COLQ has been updated since original publication of paper. ache-colq-2 3 6 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P22303:p.Cys611Ser mutation mutation certain certain sequence position certain certain certain sequence position certain C S Wed May 02 14:48:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys611ser' Tue Jun 30 16:11:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys611Ser' undefined mutation mutation mutation certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:54:14 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'met595semet' chemical synthesis Chemical synthesis (Chemical synthesis) 5 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction working 24.7%, free 25.9% 2.35A The crystal structure of the WAT/PRAD complex Fig. 4 ache-aces-1 2 4 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 4 unspecified role unspecified role bait bait region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association P37136 transfection Fig. 11 I have only shown the Ache data from this figure. I have not added the ClQ interaction as they have not shown the protein to actually be present in the complex and, as the complex is isolated from whole cells, ColQ may have triggered binding to something else.