DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nature structural & molecular biology 2011 imex curation Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. DIP original experiment: DIP-218723X Nature structural & molecular biology 2011 IMEx Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nature structural & molecular biology 2011 imex curation Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. 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 Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. DIP original experiment: DIP-218721X Nature structural & molecular biology 2011 IMEx Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nature structural & molecular biology 2011 imex curation Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. Only protein-protein interactions ecolx Escherichia coli saxs x ray scattering saxs predetermined predetermined participant predetermined Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. DIP original experiment: DIP-218722X Nature structural & molecular biology 2011 IMEx Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nature structural & molecular biology 2011 imex curation Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. DIP original experiment: DIP-218716X Nature structural & molecular biology 2011 IMEx Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nature structural & molecular biology 2011 imex curation Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. DIP original experiment: DIP-218717X Nature structural & molecular biology 2011 IMEx Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nature structural & molecular biology 2011 imex curation Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. DIP original experiment: DIP-218720X Nature structural & molecular biology 2011 IMEx Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nature structural & molecular biology 2011 imex curation Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. DIP original experiment: DIP-218714X Nature structural & molecular biology 2011 IMEx Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nature structural & molecular biology 2011 imex curation Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. Only protein-protein interactions ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. DIP original experiment: DIP-218715X Nature structural & molecular biology 2011 IMEx Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nature structural & molecular biology 2011 imex curation Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. DIP original experiment: DIP-221264X Nature structural & molecular biology 2011 IMEx Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nature structural & molecular biology 2011 imex curation Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. DIP original experiment: DIP-218719X Nature structural & molecular biology 2011 IMEx Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nature structural & molecular biology 2011 imex curation Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. DIP original experiment: DIP-218724X Nature structural & molecular biology 2011 IMEx Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nature structural & molecular biology 2011 imex curation Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. Only protein-protein interactions in vitro In vitro fluorescence imaging fluorescence microscopy fluorescence imaging predetermined predetermined participant predetermined Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. DIP original experiment: DIP-218725X Nature structural & molecular biology 2011 IMEx Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. Nature structural & molecular biology 2011 imex curation Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Namgoong S., Boczkowska M., Glista MJ., Winkelman JD., Rebowski G., Kovar DR., Dominguez R. DIP original experiment: DIP-218718X Nature structural & molecular biology 2011 IMEx Mechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleation. spir_drome Protein spire spir p150-Spir CG10076 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MTEHQAEEQADTPPTKVKATPTPTPSGKFKDAKEDAFLSTSPDSANGDAQHKLPADQLAMSSSAHPQQAGQARPLILQAFHRCSSPEQCVTLHDILDSFKAPLSEDQAWALIHQFAGLYHQVAVQAHTCAADYEAALPTGFELHFHRDGSVHFSGPDQLTPKEQLQQEQIPLPPQHDVIVDQPDHSASSSGDSSVINRAFDNSNHHHHHQHHHPPLVVSHRKIISELAEIVYTALDYNLPEDEECQVSQELENLFNFMTADETDDDCIDEGIDEGDKRWDDESEEERNDTKELEHIIETCRNHIKTTLPENHYRAVCRALVTETIELRVFLQQVLNNEAGAEKLIKASESSATTQQELAKLGFNDWARFWVQVIDELRRGVRLKKSNHERTPIEYELTPYEILMGDIRAKKYQLRKVMVNGDIPPRVKKDAHAMILEFIRSRPPLKKASDRQLGPPRMCEPSPREQLMESIRKGKELKQITPPEAPTLRERVLPSANSTLSRSRQRLIKVDFSKFQDDDLFYDENSISSSHSTAATHQHHPHFAEMHRCSQPKMPPYPFGGYMVPSQARQDCRETASLMRPRRTMEPAKQVPPPEEPSFTKDEYHKFYDTALESYDLATQCESRRASLRRHTIVGCQSNLDETHSMPPTRPESRQSDDVSKETPKRSPAEQTHPSDEGSSTSSLGPWNKSFMDKQTWMERGDDRLSVTLAEIVHIRSVMTKAELEGLPMDVRVKEDVEKRRVCFLCLRTRFSFFGPWGIQCKLCQRTVCAKCYTKMRIPSEHFRNVPLVLISPSLLSSPASSSTPSPSHHAQQAHSSSTGNIMDDQFPKSLIERLLRSESDRKTRSTVGSAPSSPKHQRSNMSTPGISVGPGASSSSAAATGQAVEALHDQATMSSSYSAAMRPSGVHQQQKQHYNNAMSRSMEGPRSLPVHSPAYRPLSNNSTLERKSRFSRGFNLFSSGSHLAQTQEQKENLRGEQVTVCNDCQGLVNEITSSVKQKRSSARNRTIQNLTLDLTPVWK DIP protein Q9U1K1 original sequence version: 83 010CD024F9ABC078 q87ge5_vibpa VPA1370 protein protein vibpa vibpa MLKIKLPQQTSLAPSSETTQRLPVKISIKSICNKSICKTLHSLADKCHRFSKEIKQRSANHTPSSSHENLTTINLKSQNSAATFESTVELSIKHGSSIPPAPPLPGAIPPAPPLNLSKGAPKSSSNSLDSVNEDHSKLMEQIRQGVKLKSATKSLSADKSSADAHSKLMEELLTGGRKLKKVATSDIPAPPPLPSASTSKSPDSRNALLSEIAGFSKDRLRKTGSLETLNSSQSKDKESFEPTTHERLLSEDLFKQSPKLSEQELDELANNLADYLFQAADIDWHQVISEKTRGLTTEEMAKSEHRYVQAFCREILKYPDCYKSADVASPESPKSGGGSVIDVALKRLQTGRERLFTTTDEKGNRELKKGDAILESAINAARMAISTEEKNTILSNNVKSATFEVFCELPCMDGFAEQNGKTAFYALRAGFYSAFKNTDTAKQDITKFMKDNLQAGFSGYSYQGLTNRVAQLEAQLAALSAKLS D1A6437F04567F2F 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 q9u1k1-1 Protein spire p150-Spir CG10076 spir protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MTEHQAEEQADTPPTKVKATPTPTPSGKFKDAKEDAFLSTSPDSANGDAQHKLPADQLAMSSSAHPQQAGQARPLILQAFHRCSSPEQCVTLHDILDSFKAPLSEDQAWALIHQFAGLYHQVAVQAHTCAADYEAALPTGFELHFHRDGSVHFSGPDQLTPKEQLQQEQIPLPPQHDVIVDQPDHSASSSGDSSVINRAFDNSNHHHHHQHHHPPLVVSHRKIISELAEIVYTALDYNLPEDEECQVSQELENLFNFMTADETDDDCIDEGIDEGDKRWDDESEEERNDTKELEHIIETCRNHIKTTLPENHYRAVCRALVTETIELRVFLQQVLNNEAGAEKLIKASESSATTQQELAKLGFNDWARFWVQVIDELRRGVRLKKSNHERTPIEYELTPYEILMGDIRAKKYQLRKVMVNGDIPPRVKKDAHAMILEFIRSRPPLKKASDRQLGPPRMCEPSPREQLMESIRKGKELKQITPPEAPTLRERVLPSANSTLSRSRQRLIKVDFSKFQDDDLFYDENSISSSHSTAATHQHHPHFAEMHRCSQPKMPPYPFGGYMVPSQARQDCRETASLMRPRRTMEPAKQVPPPEEPSFTKDEYHKFYDTALESYDLATQCESRRASLRRHTIVGCQSNLDETHSMPPTRPESRQSDDVSKETPKRSPAEQTHPSDEGSSTSSLGPWNKSFMDKQTWMERGDDRLSVTLAEIVHIRSVMTKAELEGLPMDVRVKEDVEKRRVCFLCLRTRFSFFGPWGIQCKLCQRTVCAKCYTKMRIPSEHFRNVPLVLISPSLLSSPASSSTPSPSHHAQQAHSSSTGNIMDDQFPKSLIERLLRSESDRKTRSTVGSAPSSPKHQRSNMSTPGISVGPGASSSSAAATGQAVEALHDQATMSSSYSAAMRPSGVHQQQKQHYNNAMSRSMEGPRSLPVHSPAYRPLSNNSTLERKSRFSRGFNLFSSGSHLAQTQEQKENLRGEQVTVCNDCQGLVNEITSSVKQKRSSARNRTIQNLTLDLTPVWK DIP protein Q9U1K1-1 original sequence version: 83 DIP protein Q9U1K1 original sequence version: 83 DIP protein Q9U1K1 original sequence version: 99 010CD024F9ABC078 acta1-vopl-5 5 16 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit 15 unspecified role unspecified role unspecified role unspecified role Region 130-227 Region 130-227 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction acta1-vopl-6 10 16 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit 15 unspecified role unspecified role unspecified role unspecified role VCD domain Region 200-484 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction vopl-4 7 15 unspecified role unspecified role unspecified role unspecified role VCD domain Region 247-484 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction acta1-vopl-7 2 16 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit 15 unspecified role unspecified role unspecified role unspecified role VCD domain Region 247-484 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 vopl-5 3 15 unspecified role unspecified role unspecified role unspecified role VCD domain Region 247-484 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction vopl-6 8 15 unspecified role unspecified role unspecified role unspecified role VCD domain Region 247-484 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 acta1-spir-3 11 14 unspecified role unspecified role unspecified role unspecified role Region 366-482 Region 366-482 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit direct interaction direct interaction acta1-vopl-8 13 16 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit 15 unspecified role unspecified role unspecified role unspecified role Region 130-484 Region 130-484 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q87GE5:p.[Leu138Ala;Met139Ala;Leu148Ala;Lys149Ala] L138A/M139A/L148A/K149A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K A certain certain sequence position certain certain certain sequence position certain L A certain certain sequence position certain certain certain sequence position certain M A certain certain sequence position certain certain certain sequence position certain L A This feature has been corrected as a result of our quality control procedures. The original label was 'L138A/M139A/L148A/K149A'. Wed May 02 15:57:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu138ala,met139ala,leu148ala,lys149ala' Tue Jun 30 18:49:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu138Ala;Met139Ala;Leu148Ala;Lys149Ala]' Q87GE5:p.[Leu168Ala;Met169Ala;Leu179Ala;Lys180Ala] L168A/M169A/L179A/K180A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K A certain certain sequence position certain certain certain sequence position certain L A certain certain sequence position certain certain certain sequence position certain M A certain certain sequence position certain certain certain sequence position certain L A This feature has been corrected as a result of our quality control procedures. The original label was 'L168A/M169A/L179A/K180A'. Wed May 02 14:53:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu168ala,met169ala,leu179ala,lys180ala' Tue Jun 30 19:14:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu168Ala;Met169Ala;Leu179Ala;Lys180Ala]' Q87GE5:p.[Leu208Ala;Leu209Ala;Leu220Ala;Arg221Ala] L208A/L209A/L220A/R221A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R A certain certain sequence position certain certain certain sequence position certain L A certain certain sequence position certain certain certain sequence position certain L A certain certain sequence position certain certain certain sequence position certain L A This feature has been corrected as a result of our quality control procedures. The original label was 'L208A/L209A/L220A/R221A'. Wed May 02 14:46:44 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu208ala,leu209ala,leu220ala,arg221ala' Tue Jun 30 17:54:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu208Ala;Leu209Ala;Leu220Ala;Arg221Ala]' ecolx Escherichia coli direct interaction direct interaction vopl-7 4 15 unspecified role unspecified role unspecified role unspecified role VCD domain Region 247-484 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q87GE5:p.[Leu465Glu;Leu472Glu;Leu476Glu;Leu479Glu;Leu483Glu] L465E/L472E/L476E/L479E/L483E mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain L E certain certain sequence position certain certain certain sequence position certain L E certain certain sequence position certain certain certain sequence position certain L E certain certain sequence position certain certain certain sequence position certain L E certain certain sequence position certain certain certain sequence position certain L E This feature has been corrected as a result of our quality control procedures. The original label was 'L465E/L472E/L476E/L479E/L483E'. Wed May 02 15:57:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu465glu,leu472glu,leu476glu,leu479glu,leu483glu' Tue Jun 30 17:43:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu465Glu;Leu472Glu;Leu476Glu;Leu479Glu;Leu483Glu]' ecolx Escherichia coli direct interaction direct interaction acta1-vopl-9 6 16 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit 15 unspecified role unspecified role unspecified role unspecified role VCD domain Region 200-484 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction acta1-12 12 16 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit direct interaction direct interaction acta1-vopl-10 1 16 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit 15 unspecified role unspecified role unspecified role unspecified role VCD domain Region 200-484 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction acta1-spir-4 9 17 unspecified role unspecified role unspecified role unspecified role Region 366-482 Region 366-482 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role rabit Oryctolagus cuniculus (Rabbit) Rabbit direct interaction direct interaction 1 nodeMerge04 2012-07-20