DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural basis for ESCRT-III protein autoinhibition. Structural basis for ESCRT-III protein autoinhibition. Nature structural & molecular biology 2009 imex curation Bajorek M., Schubert HL., McCullough J., Langelier C., Eckert DM., Stubblefield WM., Uter NT., Myszka DG., Hill CP., Sundquist WI. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Bajorek M., Schubert HL., McCullough J., Langelier C., Eckert DM., Stubblefield WM., Uter NT., Myszka DG., Hill CP., Sundquist WI. DIP original experiment: DIP-133084X Nature structural & molecular biology 2009 IMEx Structural basis for ESCRT-III protein autoinhibition. Structural basis for ESCRT-III protein autoinhibition. Structural basis for ESCRT-III protein autoinhibition. Nature structural & molecular biology 2009 imex curation Bajorek M., Schubert HL., McCullough J., Langelier C., Eckert DM., Stubblefield WM., Uter NT., Myszka DG., Hill CP., Sundquist WI. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Bajorek M., Schubert HL., McCullough J., Langelier C., Eckert DM., Stubblefield WM., Uter NT., Myszka DG., Hill CP., Sundquist WI. DIP original experiment: DIP-133087X Nature structural & molecular biology 2009 IMEx Structural basis for ESCRT-III protein autoinhibition. Structural basis for ESCRT-III protein autoinhibition. Structural basis for ESCRT-III protein autoinhibition. Nature structural & molecular biology 2009 imex curation Bajorek M., Schubert HL., McCullough J., Langelier C., Eckert DM., Stubblefield WM., Uter NT., Myszka DG., Hill CP., Sundquist WI. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Bajorek M., Schubert HL., McCullough J., Langelier C., Eckert DM., Stubblefield WM., Uter NT., Myszka DG., Hill CP., Sundquist WI. DIP original experiment: DIP-133086X Nature structural & molecular biology 2009 IMEx Structural basis for ESCRT-III protein autoinhibition. Structural basis for ESCRT-III protein autoinhibition. Structural basis for ESCRT-III protein autoinhibition. Nature structural & molecular biology 2009 imex curation Bajorek M., Schubert HL., McCullough J., Langelier C., Eckert DM., Stubblefield WM., Uter NT., Myszka DG., Hill CP., Sundquist WI. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Bajorek M., Schubert HL., McCullough J., Langelier C., Eckert DM., Stubblefield WM., Uter NT., Myszka DG., Hill CP., Sundquist WI. DIP original experiment: DIP-133083X Nature structural & molecular biology 2009 IMEx Structural basis for ESCRT-III protein autoinhibition. Structural basis for ESCRT-III protein autoinhibition. Structural basis for ESCRT-III protein autoinhibition. Nature structural & molecular biology 2009 imex curation Bajorek M., Schubert HL., McCullough J., Langelier C., Eckert DM., Stubblefield WM., Uter NT., Myszka DG., Hill CP., Sundquist WI. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Bajorek M., Schubert HL., McCullough J., Langelier C., Eckert DM., Stubblefield WM., Uter NT., Myszka DG., Hill CP., Sundquist WI. DIP original experiment: DIP-133082X Nature structural & molecular biology 2009 IMEx Structural basis for ESCRT-III protein autoinhibition. Structural basis for ESCRT-III protein autoinhibition. Structural basis for ESCRT-III protein autoinhibition. Nature structural & molecular biology 2009 imex curation Bajorek M., Schubert HL., McCullough J., Langelier C., Eckert DM., Stubblefield WM., Uter NT., Myszka DG., Hill CP., Sundquist WI. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Bajorek M., Schubert HL., McCullough J., Langelier C., Eckert DM., Stubblefield WM., Uter NT., Myszka DG., Hill CP., Sundquist WI. DIP original experiment: DIP-133085X Nature structural & molecular biology 2009 IMEx Structural basis for ESCRT-III protein autoinhibition. p53990-4 IST1 homolog IST1 KIAA0174 Putative MAPK-activating protein PM28 protein protein human Homo sapiens Human MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPDSVVMAEAPPGVETDLIDVGFTDDVKKGGPGRGGSGGFTAPVGGPDGTVPMPMPMPMPMPSANTPFSYPLPKGPSDFNGLPMGTYQAFPNIHPPQIPATPPSYESVDDINADKNISSAQIVGPGPKPEASAKLPSRPADNYDNFVLPELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT DIP protein P53990-4 original sequence version: 79 DIP protein P53990-4 original sequence version: 131 q9y3e7-1 Charged multivesicular body protein 3 CHMP3 CGI149 NEDF VPS24 Chromatin-modifying protein 3 Neuroendocrine differentiation factor Vacuolar protein sorting-associated protein 24 CGI-149 Vps24alpha protein protein human Homo sapiens Human MGLFGKTQEKPPKELVNEWSLKIRKEMRVVDRQIRDIQREEEKVKRSVKDAAKKGQKDVCIVLAKEMIRSRKAVSKLYASKAHMNSVLMGMKNQLAVLRVAGSLQKSTEVMKAMQSLVKIPEIQATMRELSKEMMKAGIIEEMLEDTFESMDDQEEMEEEAEMEIDRILFEITAGALGKAPSKVTDALPEPEPPGAMAASEDEEEEEEALEAMQSRLATLRS DIP protein Q9Y3E7-1 original sequence version: 120 DIP protein Q9Y3E7 original sequence version: 72 DIP protein Q9Y3E7-1 original sequence version: 83 chm1b_human Charged multivesicular body protein 1b CHMP1B C18orf2 Chromatin-modifying protein 1b CHMP1.5 Vacuolar protein sorting-associated protein 46-2 protein protein human Homo sapiens Human MSNMEKHLFNLKFAAKELSRSAKKCDKEEKAEKAKIKKAIQKGNMEVARIHAENAIRQKNQAVNFLRMSARVDAVAARVQTAVTMGKVTKSMAGVVKSMDATLKTMNLEKISALMDKFEHQFETLDVQTQQMEDTMSSTTTLTTPQNQVDMLLQEMADEAGLDLNMELPQGQTGSVGTSVASAEQDELSQRLARLRDQV DIP protein Q7LBR1 original sequence version: 73 DIP protein Q7LBR1 original sequence version: 53 DIP protein Q7LBR1 original sequence version: 59 DIP protein Q7LBR1 original sequence version: 98 8071E94D20D85AB5 chm2a_human Charged multivesicular body protein 2a BC2 CHMP2 Chromatin-modifying protein 2a Putative breast adenocarcinoma marker BC-2 Vacuolar protein sorting-associated protein 2-1 CHMP2A protein protein human Homo sapiens Human MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEESDAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEAAASALADADADLEERLKNLRRD DIP protein O43633 original sequence version: 81 F2B86C623829E32E ist1-chmp1b-1 5 9 unspecified role unspecified role prey prey ecolx Escherichia coli 7 unspecified role unspecified role bait bait Region 1-189 Region 1-189 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P53990-4:p.Tyr64Asp Y64D mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y D This feature has been corrected as a result of our quality control procedures. The original label was 'Y64D'. Wed May 02 16:36:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr64asp' Tue Jun 30 18:33:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr64Asp' P53990-4:p.Tyr165Ala Y165A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y165A'. Wed May 02 14:37:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr165ala' Tue Jun 30 17:00:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr165Ala' P53990-4:p.Glu168Arg E168R mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E R This feature has been corrected as a result of our quality control procedures. The original label was 'E168R'. Wed May 02 17:36:20 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu168arg' Tue Jun 30 15:58:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu168Arg' P53990-4:p.Asp63Ala D63A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D A This feature has been corrected as a result of our quality control procedures. The original label was 'D63A'. Wed May 02 18:18:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp63ala' Tue Jun 30 16:51:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp63Ala' P53990-4:p.Glu67Ala E67A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E A This feature has been corrected as a result of our quality control procedures. The original label was 'E67A'. Wed May 02 16:48:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu67ala' Tue Jun 30 18:15:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu67Ala' P53990-4:p.Arg164Asp R164D mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R D This feature has been corrected as a result of our quality control procedures. The original label was 'R164D'. Wed May 02 19:43:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg164asp' Tue Jun 30 17:46:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg164Asp' ecolx Escherichia coli direct interaction direct interaction ist1-1 6 7 unspecified role unspecified role unspecified role unspecified role Region 1-189 Region 1-189 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P53990-4:p.Tyr43Asp Y43D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y D This feature has been corrected as a result of our quality control procedures. The original label was 'Y43D'. Wed May 02 17:42:01 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr43asp' Tue Jun 30 18:04:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr43Asp' P53990-4:p.Arg51Asp R51D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R D This feature has been corrected as a result of our quality control procedures. The original label was 'R51D'. Wed May 02 16:02:44 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg51asp' Tue Jun 30 19:30:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg51Asp' P53990-4:p.Ile54Asp I54D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain I D This feature has been corrected as a result of our quality control procedures. The original label was 'I54D'. Wed May 02 19:24:26 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile54asp' Tue Jun 30 17:38:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile54Asp' ecolx Escherichia coli direct interaction direct interaction ist1-2 1 7 unspecified role unspecified role unspecified role unspecified role Region 1-189 Region 1-189 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P53990-4:p.Tyr43Asp Y43D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y D This feature has been corrected as a result of our quality control procedures. The original label was 'Y43D'. Wed May 02 16:13:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr43asp' Tue Jun 30 16:19:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr43Asp' P53990-4:p.Arg51Asp R51D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R D This feature has been corrected as a result of our quality control procedures. The original label was 'R51D'. Wed May 02 15:37:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg51asp' Tue Jun 30 18:13:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg51Asp' P53990-4:p.Arg51Asp R51D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R D This feature has been corrected as a result of our quality control procedures. The original label was 'R51D'. Wed May 02 16:41:23 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg51asp' Tue Jun 30 16:36:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg51Asp' ecolx Escherichia coli direct interaction direct interaction chmp1b-1 3 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction chmp3-chmp2a-1 4 10 unspecified role unspecified role prey prey ecolx Escherichia coli 8 unspecified role unspecified role bait bait Region 1-150 Region 1-150 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q9Y3E7-1:p.[Val59Asp;Val62Asp] V59D/V62D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain V D certain certain sequence position certain certain certain sequence position certain V D This feature has been corrected as a result of our quality control procedures. The original label was 'V59D/V62D'. Wed May 02 20:13:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val59asp,val62asp' Tue Jun 30 20:21:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Val59Asp;Val62Asp]' Q9Y3E7-1:p.[Val59Asp;Val62Asp;Ile168Asp;Leu169Asp] V59D/V62D/I168D/L169D mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain V D certain certain sequence position certain certain certain sequence position certain V D certain certain sequence position certain certain certain sequence position certain L D certain certain sequence position certain certain certain sequence position certain I D This feature has been corrected as a result of our quality control procedures. The original label was 'V59D/V62D/I168D/L169D'. Wed May 02 14:59:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val59asp,val62asp,ile168asp,leu169asp' Tue Jun 30 17:35:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Val59Asp;Val62Asp;Ile168Asp;Leu169Asp]' GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction chmp2a-chmp3-3 2 10 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role Region 1-150 Region 1-150 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction