DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ shimanovskaya-2014-1 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-2 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-3 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-4 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-5 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-6 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-7 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-8 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-9 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-10 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-11 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-12 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-13 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-14 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-15 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-16 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-17 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-18 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-19 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-20 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-21 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-22 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-23 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-24 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation shimanovskaya-2014-25 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. Shimanovskaya E., Viscardi V., Lesigang J., Lettman MM., Qiao R., Svergun DI., Round A., Oegema K., Dong G. Only protein-protein interactions imex curation 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 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 zyg1_caeel Probable serine/threonine-protein kinase zyg-1 zyg-1 F59E12.2 Zygote defective protein 1 protein protein caeel Caenorhabditis elegans MSGGKSGSRLSAYSHLKEIGKGGFGVVYAAQRENGEKVAIKRIDKKVPKNRVWTEIQTMKELKKSKYVVEFYEDFVEDGYTYIVMELCEGGSLQAYVREHGALDDATAVHVLRQLISAVSFMHRVNVIHRDLSAGNVFIKDSKKKKMTVKLGDFGLATTLGRGETTCTIVGTPGFIAPQVYDQEYTQSADVYSLGAVLYTMLTARNPPPKGLPPTCGMSPNAARLVEQMMDTDAKKRIPLTQIVLSEFMYENTNENAVIFSREHSRDGRRQRSREPVRSSRDDRSRDGRALIRSSSQPAHSGRAPLSNRPIHDRMPSTSSRGFDSERGRERDRDSGRGTVPPSREDRNRSQLWPIRMDRLEGQRVCTAGGRYIVELDTRCRFEVAAQGNFVKRILIVEVDEMVQTVYVHRIPDRTVRGRNGEEELITLTNNPFVYTSYSQMPKEVQNDYMRLQKMVAVTISGRVAKVTFRRPSQFPDAQAQLMENGDLRIKLPRSVIVRKMDNGEIFNCIDGIATQKQAVSGITLTKVNEVYKYLIRFEQCLNGMDRGMVCFPIVFSAGTNMVGSSPSSLMPSGSSQTSRFPFSNLSNNQPSLVPHSAPFLTKPTSSQRASSANVQRRVSTDENSSPSVAPSKYKIKIDPTTQKVRSIQATDGRVLRCSTSKADQFIFTDPAIRPDDQRFMRTDRVPDRASEMLHTLCERMRKLHQ spd2_caeel Spindle-defective protein 2 F32H2.3 spd-2 protein protein caeel Caenorhabditis elegans MEDDAPMNLCNEQFEEIEDSPIDDNDNESFYNADGDVELEEEEVHETPKNFKNGGRFKTNMTNPKVNDLTTIEEKNEDLRSAASSRSASRPASVMSDKSFSSQFEFQSGGENAIEEYTNQVFADENKADLLFPETSKFMNGASPPKDKHHSWEPSIHHYDKQPPPDIQTNSPVFGNLNHRKNKLIPQARAKPGANDNEIVERDNDENVPTTSDKSAFITSPMNSTNHDEKTSTPKRPTNRKIGQYQGPNFDLSSIYVGSPQHQNTSISTGQQMPTSSYSHAHSETMMTNQTINESMVRRVLNGNNKNQDLFAALEEARKRRAAQPSKPDFRINTTRTRVPIKPTSARHSGNVVSSTSNDNTTAASSKDLTTSRKAMETFRQNASMADATNSNTASMTSILSTISTARTDISRSSRNHGGGFSNTSVSTVIPANNGNVSLSHGRDGRDSVSSVRTMSRASSTSTVYAGSTFSGVSKPLRIHAKRVAFGCVAVGETLRVEVEVENISDRQCLVRASTDSTTPVYQILDNKLTMVDPKKSIKFQVSFSPSSVGRYQVIMSIEVPAQNFIHKIPMWGNGGIAKFVPTSPDLQQTINQSEYAMCTSCAKRISFKISNSAGTRDGFAMIKVFDSAMRQLPDGCVAFFPAPGFIVKKKSDKRVDIRIDSSYIDLHDENNFRTSSSLSTASTTSSFQRRILPGAKFFVHVVWGEETMRTRLRLLEVRTGQHQLIDGHDFTSFQFSDEEVLRAVPVGFPAIKPEDRDLFAASYRSFFINFFTSTTEFRAATSRKKKEICSNDDSTLLETTAFRNQTFVNDVTIVPNTRFSNRK e9q4y4_mouse Cep192 protein protein mouse Mus musculus Mouse MEDFRGIAEESFPSFLANSLLGNSEVLGNVTLSSNFGLPIAVSTLARSRPSTDNRCPDVQESYLIEERFSVPSASSPSCQSDNPEPRERLRLSFQGDDSALRKKNYIESPDLSHALMKPRAEEKQANAASVQGQSLLGGVSPLQQVPDSALDFHLKSWTNHEEHNIAMPDPKKHFEAVNPNRDFSHTSLLDNEKLLTLTNLDSSSDDDINDEEFYDDHLEAYFEQLAIPGMMYEAGGQESPADDFKFPANEDSILNCEFQSENNSPRLPHDACTSGNSPTAHTESEGGHGCPPGTSGCVGTVDNKMQVDNVMSLYSHAWRNEKEAAHNLKDIVPNQSRGCGGEEIVVKRLCAVDETLRSTYRHSTETEDGFDPADYIKQDSESPHQNKHFASDLETVPNVDRCLNTETPTVFIQKDGDIAASSKTNGDNGINSPDTLWSPTSERRACGLYESDSKTSDKGELSQNVVYKSEDGRWVTDLAYYTSFIDQQDLQMSPNNEMNEDFRSGSDALDLIAKDEEEFNKEHPFIQDEKIDVQNTPVALGDNSWVATVNYHLLRKSLGTSDFDKDNGSYLRLSLGEFFAERSEALGCLGGGKDVKRPSFGYFIRSPEEREPVALIKSDLSRSDLEKEATQPYRGFSSGDLNEQSQVQLSEGSVMLKAEELQRNSQVDEDDITLTASRNQTEDTLCSNNKLQEYKNTLSGGEDSVLRISTIASAFADVSVSTDPAQLVTMMKALRNKGRSKPFQDDGTQEDCPNISHVLLNDLEKSNRSNAFDMEKYLTKTEFSSCEGAREPLSRAGTSDMWDLCSPERQTVQDRSMVNVCATNSREAEETTAAIFCAENIESDTQESLRTIASSDSVLTSTRENRNSAMGRMPPSVDTLLDVRNSEKAASVSIAASRSDSLLRNPRVPSFSIVEQCEEIQDNRDHGRKKECVSETSSSDKHVTFEDGLVVLPKSVDLKTASPESGRSGFQDEESFRLSPLSHSSPSEISGNFAGCVLESLDSAYHQRPHLESELSQLACSHADMSRLTYVSEQENTFPVTAADESSEDHKSDLTSELSTTIVRASPTPPREQAVEKPRDKIPGQNAEKVSMPWVIQSKSGLANMRETPSLRTGFEDGEPNFTSSQDISSESREPLEAGKMMDSTSGSSEQDLIGQALLDKPALNHRSGPAVPNLPELIQKTVDQGQRLSSTRLSAASSEASSQVPNPGASGTQHNPAPHISAHASVAKVMNQPAVCPALWTGHSLYIAPGAPSGNATLSQCHAGMQVCGISGYSPYPAAAPELVASGLYLGPSLASGLMAPSSLYNLCSTAAPQNLLSTAKPFPMVTNCETEPRDSGMMPAFGNARVPEELRFPHACCVGIASQTLLSVLNPTDHWLQVSIRVLSIWVNGEKVDLSTQTCLVFKNKVVIRPQATEEIKILFIPTSSGIFRCTFSVASWLFSADADTVGQAEALGSRVTLTAIAETPVIEVETEKKGVLDFGDLTYAGWKALPLKLINRTHATVPIRLIINANAVAWRCFTFSKEPIHVSLKAAPHADITAQLAAPSVVSHVMPASYDGKDPEFLVVWVIFHSPKKLLTSEILGSAEEFLARVDIEVDSPNPIPVLRSVALRARAGVARIHAPRDLQTVYLLADVNSSTKHPLPLKNAGNIEVHLDIKVAEQGSQFSVDPESLFLRPGEEHEVTISFTPKDSKACEERILIIFVQPLGPQYEVVLRGEVISSGSKPLPPGPHCSDIPLILSNKQFLTWGGIPLGRTQLQKLALRNSSTTTAQNLRLFIKGQDQDCFQIQNTFGSEERLTSNCEIRICPGEDFVISVLFAPTRLSCMLAKLEIKQLGSRSQPGIKFMIPLSGYGGTSNLILEDVKKLSDSYLITMNDLIPGKESKVVFSIRNTGSRAAFVRAVCFKESQRKVLLDPKVLRIFPDKFVLKERTQEHITLVYTPSSRKNGEKPATELLTVYMFGGDEISRQQYRRAQMHTPGILKQILPEHSVLQHIDFTEAFQDEPLIDEVCDLPQRPNDIELFYGSMRKITLSVIGEFRGTICSREFLQPSSSAESKSNFSSDSKTSGKQSGNVLLDVLPVKGPQGPPFLSQSAHPAQDTAASEEGWAVHPEHLILVAPSSCDLAKTGCFQIINNSVILLKFELYWPAHCLTVTPQHGCIMPESKIQILVSPNFSVSTKESVCPWTGLIYIHCDNGQKKIVKVQIREDLTQEPLPHLPSSGTSGILAPAPEPSISRLTKLITKPPSTKVEIRSKTVIFPPTEPGRTSENYLELENCGPTDVKWHLSSFAPPYVKGVDETEDVFRATYTTFRCSPISGTLEGHGIQKVSIIFLPRDKGNYAQFWDVECHPAKEPHMKHTLRFQLSGQSIRAENDPEDSCSSRDALIKVDTAVTSRRRAVSETAAHTPGQLNSSHHGVYAPKDVYTFLPTKLGESRTLKINLRNNSFSTHALKFLSPREPFHIRHSKYTLRARHYIHIPVHFRPEAVGRFEALLVIQTDEGKSIAIRLIGESLGKS 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 ce152_mouse Centrosomal protein of 152 kDa Cep152 Kiaa0912 protein protein mouse Mus musculus Mouse MSLEFGSVALQTQNEDEEFDKEDFEREKELQQLLTDLPHDMLDDELSSPERHDSDCSMDGRAAEPHPSEHLERKWIERDILPKPHSMNCGNGWEENRSKTEDQHLGYHPGEGGDEGGSGYSPPGKREQADLYRLPEDFRPYTGGSKQAASVITFSDPQRDNFQQFGLSRGPSCGALEPYKAVYKPYRNSSVQKNSSPAQEVAASDMFEGLQQQFLGANETDSAENIHIIQLQVLNKAKERQLDSLVEKLKDSERQVRYLSHQLLIVQDEKDGLALSLRESQQLFQNGKEREMQLEAQIAALEAQVEAFRVSEEKLTKKLRTTEITLESLKQQLVELHHSESLQRAREHHESIVASLTQKHEEQVSSLQKNLDATITALQEQESICTRLKDHVQQLERNQEAVRLEKTELINRLTRSLEDSQKQCAHLLQSGSVQEVAQLQLQLQQAQKAHVLSESMNKALQEELTELKDEISLYESAAELGVLPGDSEGDLSIELTESCVDLGIKKVNWKQSKANRVTQQESPDEDPSKDELILKLKTQVQRLLTSNSVKRHLVSQLQSDLRECRETMEAFQQSKDGDSGMETKTDTSEKTTKQLWLESSEAINREDILQLKNEVQVLQKQNQELKEAEEKLRSTNQDLCNQMRQMVQEFDHDKQEAVARCERTYQQHHEAMKAQIRESLLAKHAVEKQHLLEVYEGTQSQLRSDLDKMNKEMAAVQECYLEVCREKDGLESTLRKTMEKAQEQKRQLLEAREEYVRKLKLELEEKYQETLKTERQSWLQEQAAGATQQAEKESRQKLIQQLEKEWQSKLDDSLAAWRKTTSDRGSQTEQVACPAAVSKAEAAAVLAEEQARQVQQEKELATKEALRKPEVELELKYCEIIAQKVETAVQNARSRWIQELPMLAEYKALLRAQQQEWAKQQELAVAHRLSLALSEAKEKWKSELENMKPNVMSVKELEEKVHSLQKELELKDEEVPVIVRAEVAKARTEWNKEKQEEIHKIQEQNEEDYRQFLEDHRNKINEVLAAAKEDFVKQKAELLLQKETEFQACLDQSRKEWTLQEAQQTQVEIRQYEEDTLTVLAYLLKDTQLEYGGDSQDKQLLEAMSACSSKWISVQYFEKVKACIQKALHDMLSLLTDSVASEQEKRKVVKSSADTVSWTSSEGDSAVPVPLPDSTSVRCAQSSAWLKAEAETDKKICEIKGLRCGHCFQELEKEKQECQDLRRKLEKCRRHLQHLERTHRAAVEKLGEENSRVVEELIEENHDMKNKLEALRALCRTPPRSLSAGAAESAGPSCSRQALEELRGQYIKAVRKIKRDMLRYIQESKERAAEMVKAEVLRERQETARKMRNYYLSCLQQILQDNGKEEGAEKKIMSAASKLATMAELLGTIAESDCRVRCAQAGRSVALPLASEMLTGTERSERSGVNHNIPHYVESKPNSGKTLPRSVCEQLPGRKAAPRSQRRLEESKHREMRPMASTALPSDCRCGDASCRHSGVLAKDVAPEFVPCQGEGGFDLHEKRDALGAGSEPLLYSAAHSFLGGAEKNSSPRCISESRHTTLRSPSEMPRLKALMCGSPTETDSIASEKSQGVGSQDSPVKDGVGPSSSPAWPSDSTLPCGSPAVLFLGDGSQRTQEMLGDSVQWKQFSATSCHPDAQKSNMVCRSSHTLDLPKETLHSQQGKMGATLGHPSPQSTDMLKTDFKRLSGTGPSSLCQKPLIKLTAPMPSQQDSGFDSPLE asl-sak-3 3267194 N/A 3267219 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 false ecolx Escherichia coli N/A 3267220 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 false ecolx Escherichia coli direct interaction direct interaction false false false zyg_1-1 3267195 N/A 3267221 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 false ecolx Escherichia coli direct interaction direct interaction false false false zyg_1-2 3267196 N/A 3267221 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 false ecolx Escherichia coli direct interaction direct interaction false false false spd_2-zyg_1-1 3267197 N/A 3267222 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 false ecolx Escherichia coli N/A 3267221 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 false ecolx Escherichia coli direct interaction direct interaction false false false cep192-zyg_1-1 3267198 N/A 3267223 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 false ecolx Escherichia coli N/A 3267221 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 false ecolx Escherichia coli direct interaction direct interaction false false false cep192-plk4-1 3267199 N/A 3267223 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 false 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 false ecolx Escherichia coli N/A 3267224 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 false 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 false 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 false certain certain sequence position certain certain certain sequence position certain false 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 false 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 false 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 false 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 false certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false zyg_1-3 3267200 N/A 3267221 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 false ecolx Escherichia coli direct interaction direct interaction false false false sak-1 3267201 N/A 3267220 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 false ecolx Escherichia coli direct interaction direct interaction false false false cep152-sak-1 3267202 N/A 3267225 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 false ecolx Escherichia coli N/A 3267220 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 false ecolx Escherichia coli direct interaction direct interaction false false false sak-6 3267203 N/A 3267220 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 false ecolx Escherichia coli direct interaction direct interaction false false false zyg_1-4 3267204 N/A 3267221 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 false ecolx Escherichia coli direct interaction direct interaction false false false spd_2-zyg_1-2 3267205 N/A 3267222 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 false ecolx Escherichia coli N/A 3267221 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 false ecolx Escherichia coli direct interaction direct interaction false false false sak-7 3267206 N/A 3267220 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 false ecolx Escherichia coli direct interaction direct interaction false false false sak-spd_2-1 3267207 N/A 3267222 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 false ecolx Escherichia coli N/A 3267220 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 false ecolx Escherichia coli direct interaction direct interaction false false false zyg_1-spd_2-1 3267208 N/A 3267222 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 false 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 false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false 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 false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast N/A 3267221 unspecified role unspecified role bait bait yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association false false false spd_2-zyg_1-3 3267209 N/A 3267222 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 false 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 false 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 false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false 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 false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false 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 false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3267221 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 false 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 false ecolx Escherichia coli direct interaction direct interaction false false false sak-8 3267210 N/A 3267220 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 false ecolx Escherichia coli direct interaction direct interaction false false false sak-asl-6 3267211 N/A 3267219 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 false 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 false ecolx Escherichia coli N/A 3267220 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 false 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 false 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 false 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 false 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 false 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 false 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 false certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false spd_2-zyg_1-4 3267212 N/A 3267222 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 false 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 false ecolx Escherichia coli N/A 3267221 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 false 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 false 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 false 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 false certain certain sequence position certain certain certain sequence position certain false 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 false 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 false certain certain sequence position certain certain certain sequence position certain false 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 false 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 false 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 false ecolx Escherichia coli direct interaction direct interaction false false false cep192-sak-1 3267213 N/A 3267223 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 false ecolx Escherichia coli N/A 3267220 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 false ecolx Escherichia coli direct interaction direct interaction false false false asl-sak-4 3267214 N/A 3267219 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 false ecolx Escherichia coli N/A 3267220 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 false ecolx Escherichia coli direct interaction direct interaction false false false asl-sak-5 3267215 N/A 3267219 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 false ecolx Escherichia coli N/A 3267220 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 false ecolx Escherichia coli direct interaction direct interaction false false false spd_2-zyg_1-5 3267216 N/A 3267222 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 false ecolx Escherichia coli N/A 3267221 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 false ecolx Escherichia coli direct interaction direct interaction false false false cep152-plk4-4 3267217 N/A 3267224 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 false 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 false 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 false 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 false certain certain sequence position certain certain certain sequence position certain false 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 false 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 false 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 false 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 false certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3267225 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 false 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 false ecolx Escherichia coli direct interaction direct interaction false false false asl-zyg_1-1 3267218 N/A 3267219 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 false ecolx Escherichia coli N/A 3267221 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 false ecolx Escherichia coli direct interaction direct interaction false false false