DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. Only protein-protein interactions human Homo sapiens Human anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252352X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. Only protein-protein interactions ecolx Escherichia coli tem transmission electron microscopy tem predetermined predetermined participant predetermined Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252349X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252359X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252361X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252357X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252356X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252360X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252348X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. 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 Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252350X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. Only protein-protein interactions ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252351X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252354X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252355X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. 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 Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252353X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. Structure (London, England : 1993) 2012 imex curation Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. 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 Elliott PR., Irvine AF., Jung HS., Tozawa K., Pastok MW., Picone R., Badyal SK., Basran J., Rudland PS., Barraclough R., Lian LY., Bagshaw CR., Kriajevska M., Barsukov IL. DIP original experiment: DIP-252358X Structure (London, England : 1993) 2012 IMEx Asymmetric mode of Ca²⁺-S100A4 interaction with nonmuscle myosin IIA generates nanomolar affinity required for filament remodeling. s10a4_human Protein S100-A4 S100 calcium-binding protein A4 Metastasin Protein Mts1 Placental calcium-binding protein Calvasculin S100A4 CAPL MTS1 protein protein human Homo sapiens Human MACPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQKLMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGFPDKQPRKK DIP protein P26447 original sequence version: 119 DIP protein P26447 original sequence version: 123 286D2B7B07EDB562 myh9_human Myosin-9 MYH9 Myosin heavy chain 9 Myosin heavy chain, non-muscle IIa Non-muscle myosin heavy chain IIa Cellular myosin heavy chain, type A Non-muscle myosin heavy chain A protein protein human Homo sapiens Human MAQQAADKYLYVDKNFINNPLAQADWAAKKLVWVPSDKSGFEPASLKEEVGEEAIVELVENGKKVKVNKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEERDLKITDVIIGFQACCRGYLARKAFAKRQQQLTAMKVLQRNCAAYLKLRNWQWWRLFTKVKPLLQVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGDLPFVVPRRMARKGAGDGSDEEVDGKADGAEAKPAE DIP protein P35579 original sequence version: 126 DIP protein P35579-1 original sequence version: 142 DIP protein P35579-1 original sequence version: 133 DIP protein P35579 original sequence version: 186 DIP protein P35579-1 original sequence version: 186 DIP protein P35579-1 original sequence version: 146 DIP protein P35579 original sequence version: 146 588F84BB8C106E6F myh9-s100a4-2 8 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 16 unspecified role unspecified role unspecified role unspecified role Region 1761-1960 Region 1761-1960 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 myh9-s100a4-3 11 16 unspecified role unspecified role unspecified role unspecified role Region 1868-1938 Region 1868-1938 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 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction myh9-5 3 16 unspecified role unspecified role unspecified role unspecified role Region 1761-1960 Region 1761-1960 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 s100a4-4 2 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction myh9-s100a4-4 12 16 unspecified role unspecified role unspecified role unspecified role Region 1868-1938 Region 1868-1938 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction s100a4-5 9 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction myh9-s100a4-5 7 16 unspecified role unspecified role unspecified role unspecified role Region 1897-1935 Region 1897-1935 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction s100a4-6 10 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction myh9-s100a4-6 6 16 unspecified role unspecified role unspecified role unspecified role Region 1897-1935 Region 1897-1935 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction s100a4-myh9-1 1 16 unspecified role unspecified role prey prey human Homo sapiens Human 15 unspecified role unspecified role bait bait P26447:p.Val77Asp V77D mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis 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 'V77D'. Wed May 02 16:50:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val77asp' Tue Jun 30 19:31:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val77Asp' P26447:p.Cys81Asp C81D mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain C D This feature has been corrected as a result of our quality control procedures. The original label was 'C81D'. Wed May 02 14:39:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys81asp' Tue Jun 30 17:02:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys81Asp' human Homo sapiens Human physical association physical association myh9-s100a4-7 4 16 unspecified role unspecified role unspecified role unspecified role Region 1897-1935 Region 1897-1935 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P35579:p.Phe1928Trp F1928W mutation mutation certain certain sequence position certain certain certain sequence position certain F W This feature has been corrected as a result of our quality control procedures. The original label was 'F1928W'. Wed May 02 18:06:15 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe1928trp' Tue Jun 30 18:18:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe1928Trp' in vitro In vitro 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction myh9-s100a4-8 5 16 unspecified role unspecified role unspecified role unspecified role Region 1897-1935 Region 1897-1935 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction s100a4-myh9-2 14 16 unspecified role unspecified role prey prey Region 1897-1935 Region 1897-1935 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 15 unspecified role unspecified role bait bait ecolx Escherichia coli direct interaction direct interaction myh9-s100a4-9 13 16 unspecified role unspecified role unspecified role unspecified role Region 1868-1938 Region 1868-1938 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 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction