DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Nature structural & molecular biology 2014 imex curation Ge P., Durer ZA., Kudryashov D., Zhou ZH., Reisler E. Only protein-protein interactions in vitro In vitro 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Ge P., Durer ZA., Kudryashov D., Zhou ZH., Reisler E. DIP original experiment: DIP-265516X Nature structural & molecular biology 2014 IMEx Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Nature structural & molecular biology 2014 imex curation Ge P., Durer ZA., Kudryashov D., Zhou ZH., Reisler E. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Ge P., Durer ZA., Kudryashov D., Zhou ZH., Reisler E. DIP original experiment: DIP-265520X Nature structural & molecular biology 2014 IMEx Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Nature structural & molecular biology 2014 imex curation Ge P., Durer ZA., Kudryashov D., Zhou ZH., Reisler E. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Ge P., Durer ZA., Kudryashov D., Zhou ZH., Reisler E. DIP original experiment: DIP-265519X Nature structural & molecular biology 2014 IMEx Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Nature structural & molecular biology 2014 imex curation Ge P., Durer ZA., Kudryashov D., Zhou ZH., Reisler E. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Ge P., Durer ZA., Kudryashov D., Zhou ZH., Reisler E. DIP original experiment: DIP-265517X Nature structural & molecular biology 2014 IMEx Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. Nature structural & molecular biology 2014 imex curation Ge P., Durer ZA., Kudryashov D., Zhou ZH., Reisler E. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati weight by comassie molecular weight estimation by coomasie staining weight by comassie Ge P., Durer ZA., Kudryashov D., Zhou ZH., Reisler E. DIP original experiment: DIP-265518X Nature structural & molecular biology 2014 IMEx Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments. act_yeast Actin ACT1 ABY1 END7 YFL039C protein protein yeast Saccharomyces cerevisiae Baker's yeast MDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQSKRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMTQIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDLAGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSYELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMSGGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQEYDESGPSIVHHKCF 87AC19B0B0BC9E71 87AC19B0B0BC9E71 acts_rabit Actin, alpha skeletal muscle ACTA1 ACTA Alpha-actin-1 protein protein rabit Oryctolagus cuniculus (Rabbit) Rabbit MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF DIP protein P68135 original sequence version: 41 DIP protein P68135 original sequence version: 27 DIP protein P68135 original sequence version: 28 DIP protein P68135 original sequence version: 96 DIP protein P68135 original sequence version: 29 DIP protein P68135 original sequence version: 89 DIP protein P68135 original sequence version: 39 DIP protein P68135 original sequence version: 42 DIP protein P68135 original sequence version: 59 DIP protein P68135 original sequence version: 55 DIP protein P68135 original sequence version: 60 DIP protein P68135 original sequence version: 65 DIP protein P68135 original sequence version: 67 DIP protein P68135 original sequence version: 63 DIP protein P68135 original sequence version: 68 DIP protein P68135 original sequence version: 79 DIP protein P68135 original sequence version: 88 DIP protein P68135 original sequence version: 84 DIP protein P68135 original sequence version: 101 DIP protein P68135 original sequence version: 94 DIP protein P68135 original sequence version: 95 DIP protein P68135 original sequence version: 97 DIP protein P68135 original sequence version: 100 DIP protein P68135 original sequence version: 102 DIP protein P68135 original sequence version: 83 DF2A3A046346A179 coro_yeast Coronin-like protein CRN1 L9576.2 YLR429W protein protein yeast Saccharomyces cerevisiae Baker's yeast MSGKFVRASKYRHVFGQAAKKELQYEKLKVTNNAWDSNLLKTNGKFIAVNWNASGGGAFAVIPIEEVGKAPDQVPLFRGHTAQVLDTDFDPFNDHRIASGSDDSKIGIWDIPENYKFHDHVDEDGEPIDIKPVKFLTGHARKVGHVLYHPVAENVLASSSGDYTVKLWNVETGKDMITLKHPDMVTSMSFSYDGNYLATVARDKKLRVWNIREEKIVSEGPAHTGAKNQRVVWLGNSDRLATTGFSKLSDRQIGIWDAFNIEKGDLGGFYTVDQSSGILMPFYDEGNKILYLVGKGDGNIRYYEFQNDELFELSEFQSTEAQRGFAVAPKRMVNVKENEVLKGFKTVVDQRIEPVSFFVPRRSEEFQEDIYPDAPSNKPALTAEEWFSGKSVEGPILVSMRSIYDGSAPSFHEAKRPQQPTTQETALEEKKEQPKVEKPISESEKEVKQEAPKSPSPLKSASSSSTINHVLKEDNSINKLLKKSSDIDQVNNAEDPSRDTSGWEEADDEPAPIKIETPVTPTETKKDRTPKVEPSKELKPEPVSIATDRKQEQSLPQEEKSSEKTKSPEQEKSATPPSSITAAKTAITASSKEEPSAARTSPKSLGLKKSVEKLSTLVLQLEDVVDKLTKANLDKDERLLKLEQKIGELSK E4A3AC8CF5112001 E4A3AC8CF5112001 acta1-crn1-1 1 7 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit 8 unspecified role unspecified role unspecified role unspecified role Region 1-600 Region 1-600 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction crn1-yactin-1 5 6 unspecified role unspecified role unspecified role unspecified role yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 8 unspecified role unspecified role unspecified role unspecified role Region 1-600 Region 1-600 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction crn1-yactin-2 3 6 unspecified role unspecified role unspecified role unspecified role yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 8 unspecified role unspecified role unspecified role unspecified role Region 1-600 Region 1-600 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction acta1-crn1-2 4 7 unspecified role unspecified role unspecified role unspecified role Acrylodan -label Acrylodan -label acrylodan label acrylodan label certain certain sequence position certain certain certain sequence position certain rabit Oryctolagus cuniculus (Rabbit) Rabbit 8 unspecified role unspecified role unspecified role unspecified role Region 1-600 Region 1-600 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction acta1-crn1-3 2 7 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit 8 unspecified role unspecified role unspecified role unspecified role Region 1-600 Region 1-600 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction