DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261972X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. 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 Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261948X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro mst microscale thermophoresis mst predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261969X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro mst microscale thermophoresis mst predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261965X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions ecolx Escherichia coli sls static light scattering sls predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261949X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro mst microscale thermophoresis mst predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261952X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions ecolx Escherichia coli sls static light scattering sls predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261958X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro sls static light scattering sls predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261963X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. 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 Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261955X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro mst microscale thermophoresis mst predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261968X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions ecolx Escherichia coli saxs x ray scattering saxs predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261959X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro pull down pull down anti tag western anti tag western blot anti tag western Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261971X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. 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 Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261957X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. 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 Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261962X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro mst microscale thermophoresis mst predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261966X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261953X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261951X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261954X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261961X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro mst microscale thermophoresis mst predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261964X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions ecolx Escherichia coli saxs x ray scattering saxs predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261950X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro mst microscale thermophoresis mst predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261967X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro sls static light scattering sls predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261956X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261960X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. Structure (London, England : 1993) 2014 imex curation Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions in vitro In vitro pull down pull down anti tag western anti tag western blot anti tag western Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. DIP original experiment: DIP-261970X Structure (London, England : 1993) 2014 IMEx Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. e9q4y4_mouse Cep192 protein protein mouse Mus musculus Mouse MEDFRGIAEESFPSFLANSLLGNSEVLGNVTLSSNFGLPIAVSTLARSRPSTDNRCPDVQESYLIEERFSVPSASSPSCQSDNPEPRERLRLSFQGDDSALRKKNYIESPDLSHALMKPRAEEKQANAASVQGQSLLGGVSPLQQVPDSALDFHLKSWTNHEEHNIAMPDPKKHFEAVNPNRDFSHTSLLDNEKLLTLTNLDSSSDDDINDEEFYDDHLEAYFEQLAIPGMMYEAGGQESPADDFKFPANEDSILNCEFQSENNSPRLPHDACTSGNSPTAHTESEGGHGCPPGTSGCVGTVDNKMQVDNVMSLYSHAWRNEKEAAHNLKDIVPNQSRGCGGEEIVVKRLCAVDETLRSTYRHSTETEDGFDPADYIKQDSESPHQNKHFASDLETVPNVDRCLNTETPTVFIQKDGDIAASSKTNGDNGINSPDTLWSPTSERRACGLYESDSKTSDKGELSQNVVYKSEDGRWVTDLAYYTSFIDQQDLQMSPNNEMNEDFRSGSDALDLIAKDEEEFNKEHPFIQDEKIDVQNTPVALGDNSWVATVNYHLLRKSLGTSDFDKDNGSYLRLSLGEFFAERSEALGCLGGGKDVKRPSFGYFIRSPEEREPVALIKSDLSRSDLEKEATQPYRGFSSGDLNEQSQVQLSEGSVMLKAEELQRNSQVDEDDITLTASRNQTEDTLCSNNKLQEYKNTLSGGEDSVLRISTIASAFADVSVSTDPAQLVTMMKALRNKGRSKPFQDDGTQEDCPNISHVLLNDLEKSNRSNAFDMEKYLTKTEFSSCEGAREPLSRAGTSDMWDLCSPERQTVQDRSMVNVCATNSREAEETTAAIFCAENIESDTQESLRTIASSDSVLTSTRENRNSAMGRMPPSVDTLLDVRNSEKAASVSIAASRSDSLLRNPRVPSFSIVEQCEEIQDNRDHGRKKECVSETSSSDKHVTFEDGLVVLPKSVDLKTASPESGRSGFQDEESFRLSPLSHSSPSEISGNFAGCVLESLDSAYHQRPHLESELSQLACSHADMSRLTYVSEQENTFPVTAADESSEDHKSDLTSELSTTIVRASPTPPREQAVEKPRDKIPGQNAEKVSMPWVIQSKSGLANMRETPSLRTGFEDGEPNFTSSQDISSESREPLEAGKMMDSTSGSSEQDLIGQALLDKPALNHRSGPAVPNLPELIQKTVDQGQRLSSTRLSAASSEASSQVPNPGASGTQHNPAPHISAHASVAKVMNQPAVCPALWTGHSLYIAPGAPSGNATLSQCHAGMQVCGISGYSPYPAAAPELVASGLYLGPSLASGLMAPSSLYNLCSTAAPQNLLSTAKPFPMVTNCETEPRDSGMMPAFGNARVPEELRFPHACCVGIASQTLLSVLNPTDHWLQVSIRVLSIWVNGEKVDLSTQTCLVFKNKVVIRPQATEEIKILFIPTSSGIFRCTFSVASWLFSADADTVGQAEALGSRVTLTAIAETPVIEVETEKKGVLDFGDLTYAGWKALPLKLINRTHATVPIRLIINANAVAWRCFTFSKEPIHVSLKAAPHADITAQLAAPSVVSHVMPASYDGKDPEFLVVWVIFHSPKKLLTSEILGSAEEFLARVDIEVDSPNPIPVLRSVALRARAGVARIHAPRDLQTVYLLADVNSSTKHPLPLKNAGNIEVHLDIKVAEQGSQFSVDPESLFLRPGEEHEVTISFTPKDSKACEERILIIFVQPLGPQYEVVLRGEVISSGSKPLPPGPHCSDIPLILSNKQFLTWGGIPLGRTQLQKLALRNSSTTTAQNLRLFIKGQDQDCFQIQNTFGSEERLTSNCEIRICPGEDFVISVLFAPTRLSCMLAKLEIKQLGSRSQPGIKFMIPLSGYGGTSNLILEDVKKLSDSYLITMNDLIPGKESKVVFSIRNTGSRAAFVRAVCFKESQRKVLLDPKVLRIFPDKFVLKERTQEHITLVYTPSSRKNGEKPATELLTVYMFGGDEISRQQYRRAQMHTPGILKQILPEHSVLQHIDFTEAFQDEPLIDEVCDLPQRPNDIELFYGSMRKITLSVIGEFRGTICSREFLQPSSSAESKSNFSSDSKTSGKQSGNVLLDVLPVKGPQGPPFLSQSAHPAQDTAASEEGWAVHPEHLILVAPSSCDLAKTGCFQIINNSVILLKFELYWPAHCLTVTPQHGCIMPESKIQILVSPNFSVSTKESVCPWTGLIYIHCDNGQKKIVKVQIREDLTQEPLPHLPSSGTSGILAPAPEPSISRLTKLITKPPSTKVEIRSKTVIFPPTEPGRTSENYLELENCGPTDVKWHLSSFAPPYVKGVDETEDVFRATYTTFRCSPISGTLEGHGIQKVSIIFLPRDKGNYAQFWDVECHPAKEPHMKHTLRFQLSGQSIRAENDPEDSCSSRDALIKVDTAVTSRRRAVSETAAHTPGQLNSSHHGVYAPKDVYTFLPTKLGESRTLKINLRNNSFSTHALKFLSPREPFHIRHSKYTLRARHYIHIPVHFRPEAVGRFEALLVIQTDEGKSIAIRLIGESLGKS DIP protein E9Q4Y4 original sequence version: 28 ce152_mouse Centrosomal protein of 152 kDa Cep152 Kiaa0912 protein protein mouse Mus musculus Mouse MSLEFGSVALQTQNEDEEFDKEDFEREKELQQLLTDLPHDMLDDELSSPERHDSDCSMDGRAAEPHPSEHLERKWIERDILPKPHSMNCGNGWEENRSKTEDQHLGYHPGEGGDEGGSGYSPPGKREQADLYRLPEDFRPYTGGSKQAASVITFSDPQRDNFQQFGLSRGPSCGALEPYKAVYKPYRNSSVQKNSSPAQEVAASDMFEGLQQQFLGANETDSAENIHIIQLQVLNKAKERQLDSLVEKLKDSERQVRYLSHQLLIVQDEKDGLALSLRESQQLFQNGKEREMQLEAQIAALEAQVEAFRVSEEKLTKKLRTTEITLESLKQQLVELHHSESLQRAREHHESIVASLTQKHEEQVSSLQKNLDATITALQEQESICTRLKDHVQQLERNQEAVRLEKTELINRLTRSLEDSQKQCAHLLQSGSVQEVAQLQLQLQQAQKAHVLSESMNKALQEELTELKDEISLYESAAELGVLPGDSEGDLSIELTESCVDLGIKKVNWKQSKANRVTQQESPDEDPSKDELILKLKTQVQRLLTSNSVKRHLVSQLQSDLRECRETMEAFQQSKDGDSGMETKTDTSEKTTKQLWLESSEAINREDILQLKNEVQVLQKQNQELKEAEEKLRSTNQDLCNQMRQMVQEFDHDKQEAVARCERTYQQHHEAMKAQIRESLLAKHAVEKQHLLEVYEGTQSQLRSDLDKMNKEMAAVQECYLEVCREKDGLESTLRKTMEKAQEQKRQLLEAREEYVRKLKLELEEKYQETLKTERQSWLQEQAAGATQQAEKESRQKLIQQLEKEWQSKLDDSLAAWRKTTSDRGSQTEQVACPAAVSKAEAAAVLAEEQARQVQQEKELATKEALRKPEVELELKYCEIIAQKVETAVQNARSRWIQELPMLAEYKALLRAQQQEWAKQQELAVAHRLSLALSEAKEKWKSELENMKPNVMSVKELEEKVHSLQKELELKDEEVPVIVRAEVAKARTEWNKEKQEEIHKIQEQNEEDYRQFLEDHRNKINEVLAAAKEDFVKQKAELLLQKETEFQACLDQSRKEWTLQEAQQTQVEIRQYEEDTLTVLAYLLKDTQLEYGGDSQDKQLLEAMSACSSKWISVQYFEKVKACIQKALHDMLSLLTDSVASEQEKRKVVKSSADTVSWTSSEGDSAVPVPLPDSTSVRCAQSSAWLKAEAETDKKICEIKGLRCGHCFQELEKEKQECQDLRRKLEKCRRHLQHLERTHRAAVEKLGEENSRVVEELIEENHDMKNKLEALRALCRTPPRSLSAGAAESAGPSCSRQALEELRGQYIKAVRKIKRDMLRYIQESKERAAEMVKAEVLRERQETARKMRNYYLSCLQQILQDNGKEEGAEKKIMSAASKLATMAELLGTIAESDCRVRCAQAGRSVALPLASEMLTGTERSERSGVNHNIPHYVESKPNSGKTLPRSVCEQLPGRKAAPRSQRRLEESKHREMRPMASTALPSDCRCGDASCRHSGVLAKDVAPEFVPCQGEGGFDLHEKRDALGAGSEPLLYSAAHSFLGGAEKNSSPRCISESRHTTLRSPSEMPRLKALMCGSPTETDSIASEKSQGVGSQDSPVKDGVGPSSSPAWPSDSTLPCGSPAVLFLGDGSQRTQEMLGDSVQWKQFSATSCHPDAQKSNMVCRSSHTLDLPKETLHSQQGKMGATLGHPSPQSTDMLKTDFKRLSGTGPSSLCQKPLIKLTAPMPSQQDSGFDSPLE DIP protein A2AUM9 original sequence version: 65 DIP protein A2AUM9 original sequence version: 55 16D6433AFFDEBA14 spd2_caeel Spindle-defective protein 2 F32H2.3 spd-2 protein protein caeel Caenorhabditis elegans MEDDAPMNLCNEQFEEIEDSPIDDNDNESFYNADGDVELEEEEVHETPKNFKNGGRFKTNMTNPKVNDLTTIEEKNEDLRSAASSRSASRPASVMSDKSFSSQFEFQSGGENAIEEYTNQVFADENKADLLFPETSKFMNGASPPKDKHHSWEPSIHHYDKQPPPDIQTNSPVFGNLNHRKNKLIPQARAKPGANDNEIVERDNDENVPTTSDKSAFITSPMNSTNHDEKTSTPKRPTNRKIGQYQGPNFDLSSIYVGSPQHQNTSISTGQQMPTSSYSHAHSETMMTNQTINESMVRRVLNGNNKNQDLFAALEEARKRRAAQPSKPDFRINTTRTRVPIKPTSARHSGNVVSSTSNDNTTAASSKDLTTSRKAMETFRQNASMADATNSNTASMTSILSTISTARTDISRSSRNHGGGFSNTSVSTVIPANNGNVSLSHGRDGRDSVSSVRTMSRASSTSTVYAGSTFSGVSKPLRIHAKRVAFGCVAVGETLRVEVEVENISDRQCLVRASTDSTTPVYQILDNKLTMVDPKKSIKFQVSFSPSSVGRYQVIMSIEVPAQNFIHKIPMWGNGGIAKFVPTSPDLQQTINQSEYAMCTSCAKRISFKISNSAGTRDGFAMIKVFDSAMRQLPDGCVAFFPAPGFIVKKKSDKRVDIRIDSSYIDLHDENNFRTSSSLSTASTTSSFQRRILPGAKFFVHVVWGEETMRTRLRLLEVRTGQHQLIDGHDFTSFQFSDEEVLRAVPVGFPAIKPEDRDLFAASYRSFFINFFTSTTEFRAATSRKKKEICSNDDSTLLETTAFRNQTFVNDVTIVPNTRFSNRK DIP protein P91870 original sequence version: 90 DIP protein P91870 original sequence version: 93 6D8AA983F162A1E5 plk4_drome Serine/threonine-protein kinase PLK4 SAK CG7186 Polo-like kinase 4 Serine/threonine-protein kinase SAK protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MLSNRAFGETIEDYEVQHLLGKGGFATVYKARCLHTHQDVAIKMIDKKLIQGTGLTNRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIARPFTETEAASILKQVVAGLLYLHSHNIMHRDISLSNLLLSREMHVKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRTSHGLPADVWSVGCMLYTLLVGRPPFETDAVQSTLNKVVMSEYIMPAHLSYEAQDLINKLLKKLPHERITLEAVLCHPFMLKCSNGGHSAPGALNVFSQSMESGDSGIITFASSDSRNSQQIRSVENSGPQQVLPQIREEFKQVHHKLPYEQTGLFGQASTGLAEPNWPGAAKSSAFCMEAGNVPNSKQASLKEDRISVPPLNTKRLLPTRYKTKNAIMSILRNGEVVLEFLKFRPTYNEDRINDICRISDDGQRIIIYQPDPGRGLPVREQPPDLQIPSGDCVYNYDNLPSKHWKKYIYGARFVGLVKSKTPKVTYFSTLGKCQLMETMTDFEIRFYSGAKLLKTPSEGLKVYDRNGMLLSDYSCSESRSLIEHGNECFTHCVNISNALEVAQTKDNSCFPVTIGRRPITDVQPAQRLDGLRDTTNIAFSTPKSNQGSINFSLSTISSTRNTSDFGTNCSRSNMLAAHQNIPIKRINVPEIGIATELSHGVVQVQFYDGSVVSVIPSMQGGGITYTQPNGTSTHFGKGDDLPFPVRDRVGQIPNIQLKLKTAPLLGSGRKTDYNNAMTPKTTTPYYNRMLL DIP protein O97143 original sequence version: 100 DIP protein O97143 original sequence version: 130 DIP protein O97143 original sequence version: 114 F050BF60A5D94AA4 zyg1_caeel Probable serine/threonine-protein kinase zyg-1 zyg-1 F59E12.2 Zygote defective protein 1 protein protein caeel Caenorhabditis elegans MSGGKSGSRLSAYSHLKEIGKGGFGVVYAAQRENGEKVAIKRIDKKVPKNRVWTEIQTMKELKKSKYVVEFYEDFVEDGYTYIVMELCEGGSLQAYVREHGALDDATAVHVLRQLISAVSFMHRVNVIHRDLSAGNVFIKDSKKKKMTVKLGDFGLATTLGRGETTCTIVGTPGFIAPQVYDQEYTQSADVYSLGAVLYTMLTARNPPPKGLPPTCGMSPNAARLVEQMMDTDAKKRIPLTQIVLSEFMYENTNENAVIFSREHSRDGRRQRSREPVRSSRDDRSRDGRALIRSSSQPAHSGRAPLSNRPIHDRMPSTSSRGFDSERGRERDRDSGRGTVPPSREDRNRSQLWPIRMDRLEGQRVCTAGGRYIVELDTRCRFEVAAQGNFVKRILIVEVDEMVQTVYVHRIPDRTVRGRNGEEELITLTNNPFVYTSYSQMPKEVQNDYMRLQKMVAVTISGRVAKVTFRRPSQFPDAQAQLMENGDLRIKLPRSVIVRKMDNGEIFNCIDGIATQKQAVSGITLTKVNEVYKYLIRFEQCLNGMDRGMVCFPIVFSAGTNMVGSSPSSLMPSGSSQTSRFPFSNLSNNQPSLVPHSAPFLTKPTSSQRASSANVQRRVSTDENSSPSVAPSKYKIKIDPTTQKVRSIQATDGRVLRCSTSKADQFIFTDPAIRPDDQRFMRTDRVPDRASEMLHTLCERMRKLHQ DIP protein Q9GT24 original sequence version: 104 2ED1EC53CF975FE0 q64702-1 Serine/threonine-protein kinase PLK4 Plk4 Sak Stk18 Sak-a Serine/threonine-protein kinase 18 Serine/threonine-protein kinase Sak Polo-like kinase 4 protein protein mouse Mus musculus Mouse MAACIGERIEDFKVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSVLELYNYFEDNNYVYLVLEMCHNGEMNRYLKNRMKPFSEREARHFMHQIITGMLYLHSHGILHRDLTLSNILLTRNMNIKIADFGLATQLNMPHEKHYTLCGTPNYISPEIATRSAHGLESDIWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRRNPADRLSLSSVLDHPFMSRNPSPKSKDVGTVEDSMDSGHATLSTTITASSGTSLSGSLLDRRLLVGQPLPNKITVFQKNKNSSDFSSGDGSNFCTQWGNPEQEANSRGRGRVIEDAEERPHSRYLRRAHSSDRASPSNQSRAKTYSVERCHSVEMLSKPRRSLDENQHSSNHHCLGKTPFPFADQTPQMEMVQQWFGNLQMNAHLGETNEHHTVSPNRDFQDYPDLQDTLRNAWTDTRASKNADTSANVHAVKQLSAMKYMSAHHHKPEVMPQEPGLHPHSEQSKNRSMESTLGYQKPTLRSITSPLIAHRLKPIRQKTKKAVVSILDSEEVCVELLRECASEGYVKEVLQISSDGTMITVYYPNDGRGFPLADRPPLPTDNISRYSFDNLPEKYWRKYQYASRFIQLVRSKTPKITYFTRYAKCILMENSPGADFEVWFYDGAKIHKTENLIHIIEKTGISYNLKNENEVTSLKEEVKVYMDHANEGHRICLSLESVISEEEKRSRGSSFFPIIVGRKPGNTSSPKALSAPPVDPSCCKGEQASASRLSVNSAAFPTQSPGLSPSTVTVEGLGHTATATGTGVSSSLPKSAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPDGQTTRYGENEKLPEYIKQKLQCLSSILLMFSNPTPNFQ DIP protein Q64702-1 original sequence version: 123 q9vne4_drome DmAsl asl CG2919 ASL Asl Dmel\CG2919 mecD sdu Dmel_CG2919 Cep152 MecD protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MNTPGISLFQGADALNINSTLDRQEEEEALQDQKRREEELGRIMVNAFDDLLDEENTIDSTTNYQSELEQPPVLPNYPSHPHHKPLQDDAQRANEIEMHRLQILLESKNNELQNVNQVANAAHKKLDDLQKHLSIMQAELDRAIREKQNTHELLVETKETCSNKDSDLDKLRSEKKQLEEDNTRLVGQLEAAKTLLTDVQSKYDMVQASKQKWEERNADLRLKQMEEAHRAQSDLLQQQLCQMKDQLDRKQNELDQINSRYNALQSGHETMLVDKAAKINELSQALDEAQMRCNQLSARPDLQAENRRQQQCIVDLKARIAYLEQTVASLHERLNETTTELDLIDSVIQQHQADESPTSRLSQMGGSRLVGSTPLNPLDRVGHIKQELYRALGNLKNKREEVRRLEKLLEERNQELRVLRDQENQSLVQLETLNEGKMRLENKVKAMQQELEEQKHRSQQESDVHSQLNSIVAERDALREKRQQIEEDLEQLKQQNESLQRNYDQLSQENRQLRTRETADNLRLELERHKILLRDSQSEVERLKKLYSDIATDKESLGYELRKLRESDTLKELQDQRQNLATVQRNLQLAEMKSEELKKLLETEKLSHERDLQALRQRSEREKREEAVAVAKESSENCSKCIESIAEITKAEIQLLKLQNVNSMQAKELKELEHALEQSKNLQAEMQEKIELSNKQDELISDLKERAKQFEAYIRQQEEHKQQNKCTPSPKSNSVSPSDPSPKELTQNRIRLIEQRVRDEMAKLFAAELKRFTNRLQKSEERSQCLQREYQTVCAELQQRQTEVDLLKQTILAERENIDEILAGREEKQKEMLQKCRQELQAKNQRIAELLREVEEQHASIDSERQSMKAVMAQWEKQRQSVDQVEHHWRQQLESLRSTHEEAMRSAQQRYQSAKRTAHNYKLYAEDKEAHMKREYERIKHEYELSLAKIEATMNQHLERRSREKHRDKENVPSNSSSDPITNSNRKPKGNGHS DIP protein Q9VNE4 original sequence version: 59 DIP protein Q9VNE4 original sequence version: 88 DIP protein Q9VNE4 original sequence version: 90 DIP protein Q9VNE4 original sequence version: 107 DIP protein Q9VNE4 original sequence version: 73 75A90C8496BA9EC5 asl-sak-3 15 32 unspecified role unspecified role unspecified role unspecified role Region 21-60 Region 21-60 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 29 unspecified role unspecified role unspecified role unspecified role Region 383-601 Region 383-601 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 zyg_1-1 2 30 unspecified role unspecified role unspecified role unspecified role Region 338-564 Region 338-564 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 zyg_1-2 5 30 unspecified role unspecified role unspecified role unspecified role Region 338-564 Region 338-564 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 spd_2-zyg_1-1 23 28 unspecified role unspecified role unspecified role unspecified role Region 1-147 Region 1-147 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 30 unspecified role unspecified role unspecified role unspecified role Region 338-564 Region 338-564 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 cep192-zyg_1-1 4 26 unspecified role unspecified role unspecified role unspecified role Region 168-256 Region 168-256 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 30 unspecified role unspecified role unspecified role unspecified role Region 338-564 Region 338-564 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 cep192-plk4-1 1 26 unspecified role unspecified role bait bait Region 168-256 Region 168-256 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 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 31 unspecified role unspecified role prey prey MBP-tag MBP-tag mbp tag maltose binding protein tag maltose binding protein tag maltose binding protein tag mbp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Region 557-770 Region 557-770 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q64702-1:p.[Arg564Glu;Lys566Glu] R564E/K566E mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R564E/K566E'. Wed May 02 18:06:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg564glu,lys566glu' Tue Jun 30 17:15:39 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg564Glu;Lys566Glu]' Q64702-1:p.Lys660Glu K660E mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K660E'. Wed May 02 16:39:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys660glu' Tue Jun 30 17:33:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys660Glu' Q64702-1:p.Lys672Glu K672E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K672E'. Wed May 02 16:55:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys672glu' Tue Jun 30 17:05:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys672Glu' Q64702-1:p.Lys693Glu K693E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K693E'. Wed May 02 14:49:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys693glu' Tue Jun 30 19:19:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys693Glu' Q64702-1:p.[Arg766Glu;Lys767Glu] R766E/K767E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R766E/K767E'. Wed May 02 16:24:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg766glu,lys767glu' Tue Jun 30 19:52:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg766Glu;Lys767Glu]' ecolx Escherichia coli direct interaction direct interaction zyg_1-3 21 30 unspecified role unspecified role unspecified role unspecified role Region 338-564 Region 338-564 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 sak-1 13 29 unspecified role unspecified role unspecified role unspecified role Region 383-601 Region 383-601 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 cep152-sak-1 10 27 unspecified role unspecified role unspecified role unspecified role Region 1-60 Region 1-60 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 29 unspecified role unspecified role unspecified role unspecified role Region 383-601 Region 383-601 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 sak-6 11 29 unspecified role unspecified role unspecified role unspecified role Region 383-601 Region 383-601 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 zyg_1-4 17 30 unspecified role unspecified role unspecified role unspecified role Region 338-564 Region 338-564 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 spd_2-zyg_1-2 6 28 unspecified role unspecified role unspecified role unspecified role Region 11-44 Region 11-44 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 30 unspecified role unspecified role unspecified role unspecified role Region 338-564 Region 338-564 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 sak-7 7 29 unspecified role unspecified role unspecified role unspecified role Region 383-601 Region 383-601 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 sak-spd_2-1 22 28 unspecified role unspecified role unspecified role unspecified role Region 11-44 Region 11-44 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 29 unspecified role unspecified role unspecified role unspecified role Region 383-601 Region 383-601 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 zyg_1-spd_2-1 19 28 unspecified role unspecified role prey prey Region 1-424 Region 1-424 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P91870:p.[Glu12Lys;Glu15Lys;Glu16Lys;Glu18Lys;Asp19Lys] E12K/E15K/E16K/E18K/D19K 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 D K 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 E K certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E12K/E15K/E16K/E18K/D19K'. Wed May 02 18:04:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu12lys,glu15lys,glu16lys,glu18lys,asp19lys' Tue Jun 30 18:04:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu12Lys;Glu15Lys;Glu16Lys;Glu18Lys;Asp19Lys]' P91870:p.[Glu38Lys;Glu40Lys;Glu41Lys;Glu42Lys;Glu43Lys] E38K/E40K/E41K/E42K/E43K 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 E K 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 E K certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E38K/E40K/E41K/E42K/E43K'. Wed May 02 19:47:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu38lys,glu40lys,glu41lys,glu42lys,glu43lys' Tue Jun 30 19:19:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu38Lys;Glu40Lys;Glu41Lys;Glu42Lys;Glu43Lys]' yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 30 unspecified role unspecified role bait bait yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association spd_2-zyg_1-3 16 28 unspecified role unspecified role bait bait Region 1-46 Region 1-46 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain MBP-tag MBP-tag mbp tag maltose binding protein tag maltose binding protein tag maltose binding protein tag mbp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range P91870:p.[Glu12Lys;Glu15Lys;Glu16Lys;Glu18Lys;Asp19Lys] E12K/E15K/E16K/E18K/D19K 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 D K 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 E K certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E12K/E15K/E16K/E18K/D19K'. Wed May 02 17:34:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu12lys,glu15lys,glu16lys,glu18lys,asp19lys' Tue Jun 30 18:09:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu12Lys;Glu15Lys;Glu16Lys;Glu18Lys;Asp19Lys]' P91870:p.[Asp26Lys;Glu28Lys;Asp34Lys;Asp36Lys] D26K/E28K/D34K/D36K mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D K certain certain sequence position certain certain certain sequence position certain D K certain certain sequence position certain certain certain sequence position certain E K certain certain sequence position certain certain certain sequence position certain D K This feature has been corrected as a result of our quality control procedures. The original label was 'D26K/E28K/D34K/D36K'. Wed May 02 19:46:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp26lys,glu28lys,asp34lys,asp36lys' Tue Jun 30 17:40:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asp26Lys;Glu28Lys;Asp34Lys;Asp36Lys]' P91870:p.[Glu38Lys;Glu40Lys;Glu41Lys;Glu42Lys;Glu43Lys] E38K/E40K/E41K/E42K/E43K mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis 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 E K certain certain sequence position certain certain certain sequence position certain E K certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E38K/E40K/E41K/E42K/E43K'. Wed May 02 16:26:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu38lys,glu40lys,glu41lys,glu42lys,glu43lys' Tue Jun 30 16:03:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu38Lys;Glu40Lys;Glu41Lys;Glu42Lys;Glu43Lys]' ecolx Escherichia coli 30 unspecified role unspecified role prey prey Region 338-564 Region 338-564 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain His-tag His-tag 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 ecolx Escherichia coli direct interaction direct interaction sak-8 24 29 unspecified role unspecified role unspecified role unspecified role Region 383-601 Region 383-601 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 sak-asl-6 25 32 unspecified role unspecified role prey prey Region 21-60 Region 21-60 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain MBP-tag MBP-tag mbp tag maltose binding protein tag maltose binding protein tag maltose binding protein tag mbp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 29 unspecified role unspecified role bait bait Region 383-601 Region 383-601 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain His-tag His-tag 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 O97143:p.Arg490Glu R490E 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 R E This feature has been corrected as a result of our quality control procedures. The original label was 'R490E'. Wed May 02 14:35:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg490glu' Tue Jun 30 17:14:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg490Glu' O97143:p.Lys498Glu K498E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K498E'. Wed May 02 19:09:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys498glu' Tue Jun 30 18:39:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys498Glu' O97143:p.Lys510Glu K510E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K510E'. Wed May 02 19:15:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys510glu' Tue Jun 30 19:17:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys510Glu' O97143:p.Arg523Glu R523E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R523E'. Wed May 02 19:35:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg523glu' Tue Jun 30 17:25:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg523Glu' O97143:p.[Arg594Glu;Arg595Glu] R594E/R595E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain R E certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R594E/R595E'. Wed May 02 20:19:32 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg594glu,arg595glu' Tue Jun 30 19:47:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg594Glu;Arg595Glu]' ecolx Escherichia coli direct interaction direct interaction spd_2-zyg_1-4 18 28 unspecified role unspecified role bait bait MBP-tag MBP-tag mbp tag maltose binding protein tag maltose binding protein tag maltose binding protein tag mbp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 1-46 Region 1-46 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 30 unspecified role unspecified role prey prey Region 338-564 Region 338-564 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain His-tag His-tag 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 Q9GT24:p.Lys500Glu K500E 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 K E This feature has been corrected as a result of our quality control procedures. The original label was 'K500E'. Wed May 02 19:18:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys500glu' Tue Jun 30 19:40:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys500Glu' Q9GT24:p.[Arg489Glu;Lys491Glu] R489E/K491E 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 K E certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R489E/K491E'. Wed May 02 14:33:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg489glu,lys491glu' Tue Jun 30 20:17:09 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg489Glu;Lys491Glu]' Q9GT24:p.Arg470Glu R470E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R470E'. Wed May 02 15:32:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg470glu' Tue Jun 30 19:50:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg470Glu' Q9GT24:p.[Arg470Glu;Arg471Glu] R470E/R471E 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 R E certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R470E/R471E'. Wed May 02 14:32:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg470glu,arg471glu' Tue Jun 30 19:03:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg470Glu;Arg471Glu]' Q9GT24:p.Arg471Glu R471E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R471E'. Wed May 02 19:30:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg471glu' Tue Jun 30 18:50:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg471Glu' Q9GT24:p.Arg463Glu K463E 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 R E Wed May 02 19:17:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg463glu' Tue Jun 30 17:40:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg463Glu' Q9GT24:p.Lys454Glu K454E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K454E'. Wed May 02 16:58:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys454glu' Tue Jun 30 15:42:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys454Glu' ecolx Escherichia coli direct interaction direct interaction cep192-sak-1 3 26 unspecified role unspecified role unspecified role unspecified role Region 168-256 Region 168-256 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 29 unspecified role unspecified role unspecified role unspecified role Region 383-601 Region 383-601 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 asl-sak-4 14 32 unspecified role unspecified role unspecified role unspecified role Region 21-60 Region 21-60 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 29 unspecified role unspecified role unspecified role unspecified role Region 383-601 Region 383-601 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 asl-sak-5 8 32 unspecified role unspecified role unspecified role unspecified role Region 21-60 Region 21-60 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 29 unspecified role unspecified role unspecified role unspecified role Region 383-601 Region 383-601 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 spd_2-zyg_1-5 9 28 unspecified role unspecified role unspecified role unspecified role Region 1-147 Region 1-147 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 30 unspecified role unspecified role unspecified role unspecified role Region 338-564 Region 338-564 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 cep152-plk4-4 12 31 unspecified role unspecified role prey prey Region 557-770 Region 557-770 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain MBP-tag MBP-tag mbp tag maltose binding protein tag maltose binding protein tag maltose binding protein tag mbp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q64702-1:p.Arg652Glu R652E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R652E'. Wed May 02 16:42:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg652glu' Tue Jun 30 17:55:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg652Glu' Q64702-1:p.[Lys568Glu;Lys569Glu] K568E/K569E mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K568E/K569E'. Wed May 02 18:33:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys568glu,lys569glu' Tue Jun 30 17:12:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys568Glu;Lys569Glu]' Q64702-1:p.Lys660Glu K660E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K660E'. Wed May 02 15:11:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys660glu' Tue Jun 30 20:00:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys660Glu' Q64702-1:p.Lys672Glu K672E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K672E'. Wed May 02 18:52:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys672glu' Tue Jun 30 20:00:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys672Glu' Q64702-1:p.Lys693Glu K693E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K693E'. Wed May 02 18:02:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys693glu' Tue Jun 30 18:00:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys693Glu' Q64702-1:p.[Arg766Glu;Lys767Glu] R766E/K767E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R766E/K767E'. Wed May 02 14:33:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg766glu,lys767glu' Tue Jun 30 17:09:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg766Glu;Lys767Glu]' ecolx Escherichia coli 27 unspecified role unspecified role bait bait Region 1-60 Region 1-60 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 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 asl-zyg_1-1 20 32 unspecified role unspecified role unspecified role unspecified role Region 21-60 Region 21-60 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 30 unspecified role unspecified role unspecified role unspecified role Region 338-564 Region 338-564 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