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 Endosomal Sorting Complex ESCRT-II Mediates the Assembly and Architecture of ESCRT-III Helices. The Endosomal Sorting Complex ESCRT-II Mediates the Assembly and Architecture of ESCRT-III Helices. Cell (0092-8674) 2012 imex curation Henne W.M., Buchkovich N.J., Zhao Y., Emr S.D. sde26@cornell.edu 8-May-2012: Contacted by IntAct-Help. Only protein-protein interactions yeast Saccharomyces cerevisiae Baker's yeast anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Henne W.M., Buchkovich N.J., Zhao Y., Emr S.D. sde26@cornell.edu Accepted 2013-APR-30 by PPORRAS 8-May-2012: Contacted by IntAct-Help. Cell (0092-8674) 2012 Only protein-protein interactions imex curation The Endosomal Sorting Complex ESCRT-II Mediates the Assembly and Architecture of ESCRT-III Helices. The Endosomal Sorting Complex ESCRT-II Mediates the Assembly and Architecture of ESCRT-III Helices. Cell (0092-8674) 2012 imex curation Henne W.M., Buchkovich N.J., Zhao Y., Emr S.D. sde26@cornell.edu 8-May-2012: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Henne W.M., Buchkovich N.J., Zhao Y., Emr S.D. sde26@cornell.edu Accepted 2013-APR-30 by PPORRAS 8-May-2012: Contacted by IntAct-Help. Cell (0092-8674) 2012 Only protein-protein interactions imex curation The Endosomal Sorting Complex ESCRT-II Mediates the Assembly and Architecture of ESCRT-III Helices. The Endosomal Sorting Complex ESCRT-II Mediates the Assembly and Architecture of ESCRT-III Helices. Cell (0092-8674) 2012 imex curation Henne W.M., Buchkovich N.J., Zhao Y., Emr S.D. sde26@cornell.edu 8-May-2012: Contacted by IntAct-Help. Only protein-protein interactions ecolx Escherichia coli pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Henne W.M., Buchkovich N.J., Zhao Y., Emr S.D. sde26@cornell.edu Accepted 2013-APR-30 by PPORRAS 8-May-2012: Contacted by IntAct-Help. Cell (0092-8674) 2012 Only protein-protein interactions imex curation snf8_yeast Vacuolar-sorting protein SNF8 Vacuolar protein-sorting-associated protein 22 SNF8 ESCRT-II complex subunit VPS22 VPS22 YPL002C protein protein yeast Saccharomyces cerevisiae Baker's yeast MKQFGLAAFDELKDGKYNDVNKTILEKQSVELRDQLMVFQERLVEFAKKHNSELQASPEFRSKFMHMCSSIGIDPLSLFDRDKHLFTVNDFYYEVCLKVIEICRQTKDMNGGVISFQELEKVHFRKLNVGLDDLEKSIDMLKSLECFEIFQIRGKKFLRSVPNELTSDQTKILEICSILGYSSISLLKANLGWEAVRSKSALDEMVANGLLWIDYQGGAEALYWDPSWITRQL 212C74F086A0325E 212C74F086A0325E vps24_yeast Vacuolar protein-sorting-associated protein 24 YKL041W YKL254 VPS24 DID3 DOA4-independent degradation protein 3 ESCRT-III complex subunit VPS24 protein protein yeast Saccharomyces cerevisiae Baker's yeast MDYIKKAIWGPDPKEQQRRIRSVLRKNGRNIEKSLRELTVLQNKTQQLIKKSAKKNDVRTVRLYAKELYQINKQYDRMYTSRAQLDSVRMKIDEAIRMNTLSNQMADSAGLMREVNSLVRLPQLRNTMIELEKELMKSGIISEMVDDTMESVGDVGEEMDEAVDEEVNKIVEQYTNEKFKNVDQVPTVELAANEEEQEIPDEKVDEEADRMVNEMRERLRALQN 6073C1B680D58E98 6073C1B680D58E98 did4_yeast DOA4-independent degradation protein 4 VPL2 VPS2 VPT14 YKL002W DID4 CHM2 GRD7 REN1 Vacuolar protein-sorting-associated protein 2 Vacuolar protein-targeting protein 14 ESCRT-III complex subunit VPS2 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSLFEWVFGKNVTPQERLKKNQRALERTQRELEREKRKLELQDKKLVSEIKKSAKNGQVAAAKVQAKDLVRTRNYIQKFDNMKAQLQAISLRIQAVRSSDQMTRSMSEATGLLAGMNRTMNLPQLQRISMEFEKQSDLMGQRQEFMDEAIDNVMGDEVDEDEEADEIVNKVLDEIGVDLNSQLQSTPQNLVSNAPIAETAMGIPEPIGAGSEFHGNPDDDLQARLNTLKKQT 200D07DB4C45DCBC 200D07DB4C45DCBC snf7_yeast Vacuolar-sorting protein SNF7 SNF7 VPS32 YLR025W DID1 Vacuolar protein-sorting-associated protein 32 DOA4-independent degradation protein 1 Sucrose nonfermenting protein 7 protein protein yeast Saccharomyces cerevisiae Baker's yeast MWSSLFGWTSSNAKNKESPTKAIVRLREHINLLSKKQSHLRTQITNQENEARIFLTKGNKVMAKNALKKKKTIEQLLSKVEGTMESMEQQLFSIESANLNLETMRAMQEGAKAMKTIHSGLDIDKVDETMDEIREQVELGDEISDAISRPLITGANEVDEDELDEELDMLAQENANQETSKIVNNNVNAAPISENKVSLPSVPSNKIKQSENSVKDGEEEEDEEDEDEKALRELQAEMGL 5241A18BB181F0C1 5241A18BB181F0C1 vps20_yeast Vacuolar protein sorting-associated protein 20 ASI10 CHM6 VPT20 YM9582.02C YMR077C VPS20 Vacuolar protein-targeting protein 20 Amino acid sensor-independent protein 10 Charged multivesicular body protein 6 ESCRT-III complex subunit VPS20 protein protein yeast Saccharomyces cerevisiae Baker's yeast MGQKSSKVHITKTDRAILEVKRSKDEIHKFTRRTDNLILVEKSQLKDLIRKNPENYKSNMKVRFLLKRIHYQEHLLQQASDQLINLENMVSTLEFKMVEKQFINGLKNGNEILKKLNKEFSNVDELMDDVQDQIAYQNEINETLSRSLVGTSNYEDDLDKELDALESELNPEKMNNAKVANMPSTEGLPSLPQGEQTEQKEREEFATEERSDTKEPLALLS CDC88BC4ADA3D602 CDC88BC4ADA3D602 vps25_yeast Vacuolar protein-sorting-associated protein 25 YJR102C J1957 VPS25 VPT25 ESCRT-II complex subunit VPS25 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSALPPVYSFPPLYTRQPNSLTRRQQISTWIDIISQYCKTKKIWYMSVDGTVINDNELDSGSTDNDDSKKISKNLFNNEDIQRSVSQVFIDEIWSQMTKEGKCLPIDQSGRRSSNTTTTRYFILWKSLDSWASLILQWFEDSGKLNQVITLYELSEGDETVNWEFHRMPESLLYYCLKPLCDRNRATMLKDENDKVIAIKVV 6A4545A8BC772CA2 6A4545A8BC772CA2 vps36_yeast Vacuolar protein-sorting-associated protein 36 VPS36 GRD12 VAC3 VPL11 YLR417W ESCRT-II complex subunit VPS36 protein protein yeast Saccharomyces cerevisiae Baker's yeast MEYWHYVETTSSGQPLLREGEKDIFIDQSVGLYHGKSKILQRQRGRIFLTSQRIIYIDDAKPTQNSLGLELDDLAYVNYSSGFLTRSPRLILFFKDPSSKDELGKSAETASADVVSTWVCPICMVSNETQGEFTKDTLPTPICINCGVPADYELTKSSINCSNAIDPNANPQNQFGVNSENICPACTFANHPQIGNCEICGHRLPNASKVRSKLNRLNFHDSRVHIELEKNSLARNKSSHSALSSSSSTGSSTEFVQLSFRKSDGVLFSQATERALENILTEKNKHIFNQNVVSVNGVDMRKGASSHEYNNEVPFIETKLSRIGISSLEKSRENQLLNNDILFNNALTDLNKLMSLATSIERLYKNSNITMKTKTLNLQDESTVNEPKTRRPLLILDREKFLNKELFLDEIAREIYEFTLSEFKDLNSDTNYMIITLVDLYAMYNKSMRIGTGLISPMEMREACERFEHLGLNELKLVKVNKRILCVTSEKFDVVKEKLVDLIGDNPGSDLLRLTQILSSNNSKSNWTLGILMEVLQNCVDEGDLLIDKQLSGIYYYKNSYWPSHI 60DDD4EA3A620409 60DDD4EA3A620409 snf7-1 2 7 unspecified role unspecified role neutral component neutral component P39929:p.Arg52Glu mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain R E Wed May 02 17:53:19 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg52glu' Tue Jun 30 20:21:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg52Glu' P39929:p.[Glu160Lys;Glu162Lys;Glu165_Glu166delinsLysLys] mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain E K certain certain sequence position certain certain certain sequence position certain E K certain certain sequence position certain certain certain sequence position certain EE KK Thu Jul 07 12:16:10 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was glu160_162_165_166lys Fri Jul 22 10:54:03 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'glu160lys,glu162lys,glu165lys,glu166lys' Wed May 02 14:32:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu160lys,glu162lys,glu_glu165-166lys_lys' Tue Jun 30 16:44:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu160Lys;Glu162Lys;Glu165_Glu166delinsLysLys]' n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain P39929:p.Arg52Glu mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain R E Wed May 02 15:17:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg52glu' Tue Jun 30 18:04:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg52Glu' P39929:p.[Glu160Lys;Glu162Lys;Glu165_Glu166delinsLysLys] mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain E K certain certain sequence position certain certain certain sequence position certain EE KK certain certain sequence position certain certain certain sequence position certain E K Thu Jul 07 12:16:09 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was glu160_162_165_166lys Fri Jul 22 10:54:20 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'glu160lys,glu162lys,glu165lys,glu166lys' Wed May 02 18:31:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu160lys,glu162lys,glu_glu165-166lys_lys' Tue Jun 30 18:56:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu160Lys;Glu162Lys;Glu165_Glu166delinsLysLys]' ecoli Escherichia coli (strain K12) 16 19 direct interaction direct interaction Fig. 3, 4A-B, 4D-F, 5C-D, 6B, Supp. Fig. 3 Complex formed protofilaments snf7-snf7-1 1 7 unspecified role unspecified role prey prey region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain 7 unspecified role unspecified role bait bait region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Fig.4C-F Tagged and untagged proteins differentiated by weight. did4-snf7 2 7 unspecified role unspecified role neutral component neutral component P39929:p.Arg52Glu mutation mutation certain certain sequence position certain certain certain sequence position certain R E Wed May 02 14:27:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg52glu' Tue Jun 30 15:55:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg52Glu' n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 6 unspecified role unspecified role neutral component neutral component n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) physical association physical association Fig. 5E-I Molecules form a polymeric structure vps36-snf8-1 3 4 unspecified role unspecified role prey prey 10 unspecified role unspecified role bait bait region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 9 unspecified role unspecified role prey prey association association Fig. 6A vps36-snf8-2 2 9 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 7 unspecified role unspecified role neutral component neutral component P39929:p.Ile53Glu mutation mutation certain certain sequence position certain certain certain sequence position certain I E Wed May 02 19:45:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile53glu' Tue Jun 30 18:05:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile53Glu' ecolx Escherichia coli 8 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 4 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 10 unspecified role unspecified role neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli physical association physical association Fig. 6C, 6E, Supp. Fig. 7A, 7D Complex formed rings composed of highly curved ∼9 nm diameter protofilaments . Ring formation required the presence of ESCRT-II, Vps20, and Snf7R52E, as removal of either ESCRT-II or Vps20 drastically reduced ring formation in favor of linear protofilaments snf7-snf8 2 10 unspecified role unspecified role neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli 4 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 9 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 7 unspecified role unspecified role neutral component neutral component P39929:p.Ile53Glu mutation mutation certain certain sequence position certain certain certain sequence position certain I E Wed May 02 19:37:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile53glu' Tue Jun 30 19:49:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile53Glu' ecolx Escherichia coli physical association physical association Supp. Fig. 7B Complex formed protofilaments snf7-snf8-1 2 8 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 7 unspecified role unspecified role neutral component neutral component P39929:p.Ile53Glu mutation mutation certain certain sequence position certain certain certain sequence position certain I E Wed May 02 18:37:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile53glu' Tue Jun 30 16:18:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile53Glu' ecolx Escherichia coli physical association physical association Supp. Fig. 7C Complex formed rings composed of highly curved ∼9 nm diameter protofilaments . Ring formation required the presence of ESCRT-II, Vps20, and Snf7R52E, as removal of either ESCRT-II or Vps20 drastically reduced ring formation in favor of linear protofilaments did4-snf7-3 2 6 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 10 unspecified role unspecified role neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli 8 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 4 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 9 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli 7 unspecified role unspecified role neutral component neutral component P39929:p.Ile53Glu mutation mutation certain certain sequence position certain certain certain sequence position certain I E Wed May 02 19:04:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile53glu' Tue Jun 30 15:56:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile53Glu' ecolx Escherichia coli 5 unspecified role unspecified role neutral component neutral component ecolx Escherichia coli physical association physical association Supp. Fig. 7E Complex formed rings composed of highly curved ∼9 nm diameter protofilaments .