DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266509X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266523X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266507X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266518X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266513X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266529X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266514X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266524X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266531X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266515X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266528X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266508X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266527X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266511X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266519X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266532X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266522X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266512X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266530X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266517X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266526X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266510X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266516X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266520X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266521X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266505X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266525X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nature structural & molecular biology 2015 imex curation Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Huang H., Strømme CB., Saredi G., Hödl M., Strandsby A., González-Aguilera C., Chen S., Groth A., Patel DJ. DIP original experiment: DIP-266506X Nature structural & molecular biology 2015 IMEx A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. caf1b_human Chromatin assembly factor 1 subunit B Chromatin assembly factor I p60 subunit M-phase phosphoprotein 7 CHAF1B CAF1A CAF1P60 MPHOSPH7 MPP7 protein protein human Homo sapiens Human MKVITCEIAWHNKEPVYSLDFQHGTAGRIHRLASAGVDTNVRIWKVEKGPDGKAIVEFLSNLARHTKAVNVVRFSPTGEILASGGDDAVILLWKVNDNKEPEQIAFQDEDEAQLNKENWTVVKTLRGHLEDVYDICWATDGNLMASASVDNTAIIWDVSKGQKISIFNEHKSYVQGVTWDPLGQYVATLSCDRVLRVYSIQKKRVAFNVSKMLSGIGAEGEARSYRMFHDDSMKSFFRRLSFTPDGSLLLTPAGCVESGENVMNTTYVFSRKNLKRPIAHLPCPGKATLAVRCCPVYFELRPVVETGVELMSLPYRLVFAVASEDSVLLYDTQQSFPFGYVSNIHYHTLSDISWSSDGAFLAISSTDGYCSFVTFEKDELGIPLKEKPVLNMRTPDTAKKTKSQTHRGSSPGPRPVEGTPASRTQDPSSPGTTPPQARQAPAPTVIRDPPSITPAVKSPLPGPSEEKTLQPSSQNTKAHPSRRVTLNTLQAWSKTTPRRINLTPLKTDTPPSSVPTSVISTPSTEEIQSETPGDAQGSPPELKRPRLDENKGGTESLDP DIP protein Q13112 original sequence version: 115 DIP protein Q13112 original sequence version: 163 DIP protein Q13112 original sequence version: 73 AD1846CC81B8DC9F mcm6_human DNA replication licensing factor MCM6 MCM6 p105MCM protein protein human Homo sapiens Human MDLAAAAEPGAGSQHLEVRDEVAEKCQKLFLDFLEEFQSSDGEIKYLQLAEELIRPERNTLVVSFVDLEQFNQQLSTTIQEEFYRVYPYLCRALKTFVKDRKEIPLAKDFYVAFQDLPTRHKIRELTSSRIGLLTRISGQVVRTHPVHPELVSGTFLCLDCQTVIRDVEQQFKYTQPNICRNPVCANRRRFLLDTNKSRFVDFQKVRIQETQAELPRGSIPRSLEVILRAEAVESAQAGDKCDFTGTLIVVPDVSKLSTPGARAETNSRVSGVDGYETEGIRGLRALGVRDLSYRLVFLACCVAPTNPRFGGKELRDEEQTAESIKNQMTVKEWEKVFEMSQDKNLYHNLCTSLFPTIHGNDEVKRGVLLMLFGGVPKTTGEGTSLRGDINVCIVGDPSTAKSQFLKHVEEFSPRAVYTSGKASSAAGLTAAVVRDEESHEFVIEAGALMLADNGVCCIDEFDKMDVRDQVAIHEAMEQQTISITKAGVKATLNARTSILAAANPISGHYDRSKSLKQNINLSAPIMSRFDLFFILVDECNEVTDYAIARRIVDLHSRIEESIDRVYSLDDIRRYLLFARQFKPKISKESEDFIVEQYKHLRQRDGSGVTKSSWRITVRQLESMIRLSEAMARMHCCDEVQPKHVKEAFRLLNKSIIRVETPDVNLDQEEEIQMEVDEGAGGINGHADSPAPVNGINGYNEDINQESAPKASLRLGFSEYCRISNLIVLHLRKVEEEEDESALKRSELVNWYLKEIESEIDSEEELINKKRIIEKVIHRLTHYDHVLIELTQAGLKGSTEGSESYEEDPYLVVNPNYLLED DIP protein Q14566 original sequence version: 145 DIP protein Q14566 original sequence version: 98 DIP protein Q14566 original sequence version: 109 DIP protein Q14566 original sequence version: 150 F94968EB25A3E501 mcm3_human DNA replication licensing factor MCM3 MCM3 DNA polymerase alpha holoenzyme-associated protein P1 RLF subunit beta p102 P1-MCM3 protein protein human Homo sapiens Human MAGTVVLDDVELREAQRDYLDFLDDEEDQGIYQSKVRELISDNQYRLIVNVNDLRRKNEKRANRLLNNAFEELVAFQRALKDFVASIDATYAKQYEEFYVGLEGSFGSKHVSPRTLTSCFLSCVVCVEGIVTKCSLVRPKVVRSVHYCPATKKTIERRYSDLTTLVAFPSSSVYPTKDEENNPLETEYGLSVYKDHQTITIQEMPEKAPAGQLPRSVDVILDDDLVDKAKPGDRVQVVGTYRCLPGKKGGYTSGTFRTVLIACNVKQMSKDAQPSFSAEDIAKIKKFSKTRSKDIFDQLAKSLAPSIHGHDYVKKAILCLLLGGVERDLENGSHIRGDINILLIGDPSVAKSQLLRYVLCTAPRAIPTTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDMDRTAIHEVMEQGRVTIAKAGIHARLNARCSVLAAANPVYGRYDQYKTPMENIGLQDSLLSRFDLLFIMLDQMDPEQDREISDHVLRMHRYRAPGEQDGDAMPLGSAVDILATDDPNFSQEDQQDTQIYEKHDNLLHGTKKKKEKMVSAAFMKKYIHVAKIIKPVLTQESATYIAEEYSRLRSQDSMSSDTARTSPVTARTLETLIRLATAHAKARMSKTVDLQDAEEAVELVQYAYFKKVLEKEKKRKKRSEDESETEDEEEKSQEDQEQKRKRRKTRQPDAKDGDSYDPYDFSDTEEEMPQVHTPKTADSQETKESQKVELSESRLKAFKVALLDVFREAHAQSIGMNRLTESINRDSEEPFSSVEIQAALSKMQDDNQVMVSEGIIFLI DIP protein P25205 original sequence version: 135 DIP protein P25205 original sequence version: 179 C967C068B7090558 caf1a_human Chromatin assembly factor 1 subunit A CHAF1A CAF CAF1P150 Chromatin assembly factor I p150 subunit protein protein human Homo sapiens Human MLEELECGAPGARGAATAMDCKDRPAFPVKKLIQARLPFKRLNLVPKGKADDMSDDQGTSVQSKSPDLEASLDTLENNCHVGSDIDFRPKLVNGKGPLDNFLRNRIETSIGQSTVIIDLTEDSNEQPDSLVDHNKLNSEASPSREAINGQREDTGDQQGLLKAIQNDKLAFPGETLSDIPCKTEEEGVGCGGAGRRGDSQECSPRSCPELTSGPRMCPRKEQDSWSEAGGILFKGKVPMVVLQDILAVRPPQIKSLPATPQGKNMTPESEVLESFPEEDSVLSHSSLSSPSSTSSPEGPPAPPKQHSSTSPFPTSTPLRRITKKFVKGSTEKNKLRLQRDQERLGKQLKLRAEREEKEKLKEEAKRAKEEAKKKKEEEKELKEKERREKREKDEKEKAEKQRLKEERRKERQEALEAKLEEKRKKEEEKRLREEEKRIKAEKAEITRFFQKPKTPQAPKTLAGSCGKFAPFEIKEHMVLAPRRRTAFHPDLCSQLDQLLQQQSGEFSFLKDLKGRQPLRSGPTHVSTRNADIFNSDVVIVERGKGDGVPERRKFGRMKLLQFCENHRPAYWGTWNKKTALIRARDPWAQDTKLLDYEVDSDEEWEEEEPGESLSHSEGDDDDDMGEDEDEDDGFFVPHGYLSEDEGVTEECADPENHKVRQKLKAKEWDEFLAKGKRFRVLQPVKIGCVWAADRDCAGDDLKVLQQFAACFLETLPAQEEQTPKASKRERRDEQILAQLLPLLHGNVNGSKVIIREFQEHCRRGLLSNHTGSPRSPSTTYLHTPTPSEDAAIPSKSRLKRLISENSVYEKRPDFRMCWYVHPQVLQSFQQEHLPVPCQWSYVTSVPSAPKEDSGSVPSTGPSQGTPISLKRKSAGSMCITQFMKKRRHDGQIGAEDMDGFQADTEEEEEEEGDCMIVDVPDAAEVQAPCGAASGAGGGVGVDTGKATLTASPLGAS DIP protein Q13111 original sequence version: 98 DIP protein Q13111 original sequence version: 147 DIP protein Q13111 original sequence version: 122 90617F8FE8DB7FD0 h33_human Histone H3.3 H3-3A H3-3B H3.3A H3.3B H3F3 H3F3A H3F3B PP781 protein protein human Homo sapiens Human MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P84243 original sequence version: 72 DIP protein P84243 original sequence version: 73 DIP protein P84243 original sequence version: 97 DIP protein P84243 original sequence version: 125 DIP protein P84243 original sequence version: 110 DIP protein P84243 original sequence version: 96 5158ED279E6F9E1C asf1a_human Histone chaperone ASF1A Anti-silencing function protein 1 homolog A CCG1-interacting factor A ASF1A CGI-98 HSPC146 protein protein human Homo sapiens Human MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDNTEKLEDAESSNPNLQSLLSTDALPSASKGWSTSENSLNVMLESHMDCM DIP protein Q9Y294 original sequence version: 111 DIP protein Q9Y294 original sequence version: 131 DIP protein Q9Y294 original sequence version: 106 This sequence has been withdrawn from Uniprot. 9819D531D3A9FC68 h4_human Histone H4 H4-16 H4C1 H4C11 H4C12 H4C13 H4C14 H4C15 H4C2 H4C3 H4C4 H4C5 H4C6 H4C8 H4C9 H4/A H4/B H4/C H4/D H4/E H4/G H4/H H4/I H4/J H4/K H4/M H4/N H4/O H4F2 H4FA H4FB H4FC H4FD H4FE H4FG H4FH H4FI H4FJ H4FK H4FM H4FN H4FO HIST1H4A HIST1H4B HIST1H4C HIST1H4D HIST1H4E HIST1H4F HIST1H4H HIST1H4I HIST1H4J HIST1H4K HIST1H4L HIST2H4 HIST2H4A HIST2H4B HIST4H4 protein protein human Homo sapiens Human MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG DIP protein P62805 original sequence version: 68 DIP protein P62805 original sequence version: 111 DIP protein P62805 original sequence version: 94 DIP protein P62805 original sequence version: 97 DIP protein P62805 original sequence version: 116 DIP protein P62805 original sequence version: 105 DIP protein P62805 original sequence version: 120 DIP protein P62805 original sequence version: 144 DIP protein P62805 original sequence version: 150 DIP protein P62805 original sequence version: 154 DIP protein P62805 original sequence version: 156 DIP protein P62805 original sequence version: 112 DIP protein P62805 original sequence version: 121 DIP protein P62805 original sequence version: 123 DIP protein P62805 original sequence version: 126 DIP protein P62805 original sequence version: 132 DIP protein P62805 original sequence version: 136 DIP protein P62805 original sequence version: 119 A9E5DFD3F8B97598 mcm2_human DNA replication licensing factor MCM2 MCM2 BM28 CDCL1 KIAA0030 Minichromosome maintenance protein 2 homolog Nuclear protein BM28 CCNL1 protein protein human Homo sapiens Human MAESSESFTMASSPAQRRRGNDPLTSSPGRSSRRTDALTSSPGRDLPPFEDESEGLLGTEGPLEEEEDGEELIGDGMERDYRAIPELDAYEAEGLALDDEDVEELTASQREAAERAMRQRDREAGRGLGRMRRGLLYDSDEEDEERPARKRRQVERATEDGEEDEEMIESIENLEDLKGHSVREWVSMAGPRLEIHHRFKNFLRTHVDSHGHNVFKERISDMCKENRESLVVNYEDLAAREHVLAYFLPEAPAELLQIFDEAALEVVLAMYPKYDRITNHIHVRISHLPLVEELRSLRQLHLNQLIRTSGVVTSCTGVLPQLSMVKYNCNKCNFVLGPFCQSQNQEVKPGSCPECQSAGPFEVNMEETIYQNYQRIRIQESPGKVAAGRLPRSKDAILLADLVDSCKPGDEIELTGIYHNNYDGSLNTANGFPVFATVILANHVAKKDNKVAVGELTDEDVKMITSLSKDQQIGEKIFASIAPSIYGHEDIKRGLALALFGGEPKNPGGKHKVRGDINVLLCGDPGTAKSQFLKYIEKVSSRAIFTTGQGASAVGLTAYVQRHPVSREWTLEAGALVLADRGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTSLQARCTVIAAANPIGGRYDPSLTFSENVDLTEPIISRFDILCVVRDTVDPVQDEMLARFVVGSHVRHHPSNKEEEGLANGSAAEPAMPNTYGVEPLPQEVLKKYIIYAKERVHPKLNQMDQDKVAKMYSDLRKESMATGSIPITVRHIESMIRMAEAHARIHLRDYVIEDDVNMAIRVMLESFIDTQKFSVMRSMRKTFARYLSFRRDNNELLLFILKQLVAEQVTYQRNRFGAQQDTIEVPEKDLVDKARQINIHNLSAFYDSELFRMNKFSHDLKRKMILQQF DIP protein P49736 original sequence version: 116 DIP protein P49736 original sequence version: 127 DIP protein P49736 original sequence version: 170 52C6DC61F128B404 h31_human Histone H3.1 H3FA H3FL H3FD H3FI H3FH H3FK H3FF H3FJ H3FB Histone H3/a Histone H3/b Histone H3/c Histone H3/d Histone H3/f Histone H3/h Histone H3/i Histone H3/j Histone H3/k Histone H3/l H3C1 HIST1H3A H3C2 HIST1H3B H3C3 H3FC HIST1H3C H3C4 HIST1H3D H3C6 HIST1H3E H3C7 HIST1H3F H3C8 HIST1H3G H3C10 HIST1H3H H3C11 HIST1H3I H3C12 HIST1H3J protein protein human Homo sapiens Human MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P68431 original sequence version: 78 DIP protein P68431 original sequence version: 79 DIP protein P68431 original sequence version: 76 DIP protein P68431 original sequence version: 92 DIP protein P68431 original sequence version: 87 DIP protein P68431 original sequence version: 101 DIP protein P68431 original sequence version: 130 DIP protein P68431 original sequence version: 115 9B89008EA50A0EF6 cenpa_human Histone H3-like centromeric protein A CENPA Centromere autoantigen A Centromere protein A protein protein human Homo sapiens Human MGPRRRSRKPEAPRRRSPSPTPTPGPSRRGPSLGASSHQHSRRRQGWLKEIRKLQKSTHLLIRKLPFSRLAREICVKFTRGVDFNWQAQALLALQEAAEAFLVHLFEDAYLLTLHAGRVTLFPKDVQLARRIRGLEEGLG DIP protein P49450 original sequence version: 101 DIP protein P49450 original sequence version: 153 DIP protein P49450 original sequence version: 162 11A28FEB54486489 h32_human Histone H3.2 H3C13 H3C14 H3C15 H3-clustered histone 13 H3-clustered histone 14 H3-clustered histone 15 H3F2 H3FM HIST2H3A HIST2H3C HIST2H3D Histone H3/m Histone H3/o protein protein human Homo sapiens Human MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein Q71DI3 original sequence version: 82 DIP protein Q71DI3 original sequence version: 133 DIP protein Q71DI3 original sequence version: 140 DIP protein Q71DI3 original sequence version: 107 6FD8508EA50A0EEC hjurp_human Holliday junction recognition protein FAKTS URLC9 14-3-3-associated AKT substrate Fetal liver-expressing gene 1 protein Up-regulated in lung cancer 9 HJURP FLEG1 protein protein human Homo sapiens Human MLGTLRAMEGEDVEDDQLLQKLRASRRRFQRRMQRLIEKYNQPFEDTPVVQMATLTYETPQGLRIWGGRLIKERNEGEIQDSSMKPADRTDGSVQAAAWGPELPSHRTVLGADSKSGEVDATSDQEESVAWALAPAVPQSPLKNELRRKYLTQVDILLQGAEYFECAGNRAGRDVRVTPLPSLASPAVPAPGYCSRISRKSPGDPAKPASSPREWDPLHPSSTDMALVPRNDSLSLQETSSSSFLSSQPFEDDDICNVTISDLYAGMLHSMSRLLSTKPSSIISTKTFIMQNWNSRRRHRYKSRMNKTYCKGARRSQRSSKENFIPCSEPVKGTGALRDCKNVLDVSCRKTGLKLEKAFLEVNRPQIHKLDPSWKERKVTPSKYSSLIYFDSSATYNLDEENRFRTLKWLISPVKIVSRPTIRQGHGENRQREIEIRFDQLHREYCLSPRNQPRRMCLPDSWAMNMYRGGPASPGGLQGLETRRLSLPSSKAKAKSLSEAFENLGKRSLEAGRCLPKSDSSSSLPKTNPTHSATRPQQTSDLHVQGNSSGIFRKSVSPSKTLSVPDKEVPGHGRNRYDEIKEEFDKLHQKYCLKSPGQMTVPLCIGVSTDKASMEVRYQTEGFLGKLNPDPHFQGFQKLPSSPLGCRKSLLGSTAIEAPSSTCVARAITRDGTRDHQFPAKRPRLSEPQGSGRQGNSLGASDGVDNTVRPGDQGSSSQPNSEERGENTSYRMEEKSDFMLEKLETKSV DIP protein Q8NCD3 original sequence version: 56 DIP protein Q8NCD3 original sequence version: 104 DE7F1410F9A748D5 cdc45_human Cell division control protein 45 homolog CDC45 CDC45L2 UNQ374/PRO710 PORC-PI-1 CDC45L protein protein human Homo sapiens Human MFVSDFRKEFYEVVQSQRVLLFVASDVDALCACKILQALFQCDHVQYTLVPVSGWQELETAFLEHKEQFHYFILINCGANVDLLDILQPDEDTIFFVCDTHRPVNVVNVYNDTQIKLLIKQDDDLEVPAYEDIFRDEEEDEEHSGNDSDGSEPSEKRTRLEEEIVEQTMRRRQRREWEARRRDILFDYEQYEYHGTSSAMVMFELAWMLSKDLNDMLWWAIVGLTDQWVQDKITQMKYVTDVGVLQRHVSRHNHRNEDEENTLSVDCTRISFEYDLRLVLYQHWSLHDSLCNTSYTAARFKLWSVHGQKRLQEFLADMGLPLKQVKQKFQAMDISLKENLREMIEESANKFGMKDMRVQTFSIHFGFKHKFLASDVVFATMSLMESPEKDGSGTDHFIQALDSLSRSNLDKLYHGLELAKKQLRATQQTIASCLCTNLVISQGPFLYCSLMEGTPDVMLFSRPASLSLLSKHLLKSFVCSTKNRRCKLLPLVMAAPLSMEHGTVTVVGIPPETDSSDRKNFFGRAFEKAAESTSSRMLHNHFDLSVIELKAEDRSKFLDALISLLS DIP protein O75419 original sequence version: 88 DIP protein O75419 original sequence version: 96 DIP protein O75419 original sequence version: 135 AE1BE2C8C8E5F867 asf1b_human Histone chaperone ASF1B Anti-silencing function protein 1 homolog B CCG1-interacting factor A-II ASF1B protein protein human Homo sapiens Human MAKVSVLNVAVLENPSPFHSPFRFEISFECSEALADDLEWKIIYVGSAESEEFDQILDSVLVGPVPAGRHMFVFQADAPNPSLIPETDAVGVTVVLITCTYHGQEFIRVGYYVNNEYLNPELRENPPMKPDFSQLQRNILASNPRVTRFHINWDNNMDRLEAIETQDPSLGCGLPLNCTPIKGLGLPGCIPGLLPENSMDCI DIP protein Q9NVP2 original sequence version: 120 DIP protein Q9NVP2 original sequence version: 98 This sequence has been withdrawn from Uniprot. BD62F726610E3A70 asf1a-hist1h4a-1 14 34 unspecified role unspecified role unspecified role unspecified role Region 1-172 Region 1-172 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 35 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 39 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 36 unspecified role unspecified role unspecified role unspecified role Region 43-160 Region 43-160 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association mcm2-hist1h4a-1 26 35 unspecified role unspecified role prey prey ecolx Escherichia coli 39 unspecified role unspecified role prey prey ecolx Escherichia coli 36 unspecified role unspecified role bait bait Region 43-160 Region 43-160 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 P49736:p.Asp80Ala D80A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain D A This feature has been corrected as a result of our quality control procedures. The original label was 'D80A'. Wed May 02 17:18:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp80ala' Tue Jun 30 20:21:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp80Ala' P49736:p.Tyr81Ala Y81A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y81A'. Wed May 02 15:41:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr81ala' Tue Jun 30 19:21:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr81Ala' P49736:p.[Asp80Ala;Tyr81Ala] D80A/Y81A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A certain certain sequence position certain certain certain sequence position certain D A This feature has been corrected as a result of our quality control procedures. The original label was 'D80A/Y81A'. Wed May 02 19:37:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp80ala,tyr81ala' Tue Jun 30 16:19:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asp80Ala;Tyr81Ala]' P49736:p.Tyr90Ala Y90A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y90A'. Wed May 02 17:02:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr90ala' Tue Jun 30 15:37:55 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr90Ala' P49736:p.[Arg110Ala;Glu114Ala;Met117Ala] R110A/E114A/M117A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain M A certain certain sequence position certain certain certain sequence position certain E A certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R110A/E114A/M117A'. Wed May 02 17:22:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg110ala,glu114ala,met117ala' Tue Jun 30 17:17:55 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg110Ala;Glu114Ala;Met117Ala]' P49736:p.Met117Ala M117A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain M A This feature has been corrected as a result of our quality control procedures. The original label was 'M117A'. Wed May 02 17:09:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'met117ala' Tue Jun 30 16:20:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Met117Ala' P49736:p.Leu72Ala L72A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain L A This feature has been corrected as a result of our quality control procedures. The original label was 'L72A'. Wed May 02 18:33:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu72ala' Tue Jun 30 16:53:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu72Ala' P49736:p.Asp88Ala D88A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain D A This feature has been corrected as a result of our quality control procedures. The original label was 'D88A'. Wed May 02 17:14:18 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp88ala' Tue Jun 30 19:21:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp88Ala' P49736:p.Glu114Ala E114A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain E A This feature has been corrected as a result of our quality control procedures. The original label was 'E114A'. Wed May 02 17:09:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu114ala' Tue Jun 30 19:54:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu114Ala' P49736:p.[Arg120Ala;Asp121Ala] R120A/D121A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain D A certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R120A/D121A'. Wed May 02 15:33:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg120ala,asp121ala' Tue Jun 30 16:01:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg120Ala;Asp121Ala]' ecolx Escherichia coli association association cenpa-hist1h4a-5 19 38 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 35 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 36 unspecified role unspecified role unspecified role unspecified role Region 43-160 Region 43-160 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association hist1h3a-mcm2-1 2 31 unspecified role unspecified role prey prey human Homo sapiens Human 36 unspecified role unspecified role prey prey human Homo sapiens Human 37 unspecified role unspecified role bait bait HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range P68431:p.[Arg64Ala;Lys65Ala] R64A/K65A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain K A certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R64A/K65A'. Wed May 02 14:52:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg64ala,lys65ala' Tue Jun 30 18:07:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg64Ala;Lys65Ala]' human Homo sapiens Human association association asf1a-hist1h4a-2 4 34 unspecified role unspecified role bait bait Region 1-155 Region 1-155 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 35 unspecified role unspecified role prey prey ecolx Escherichia coli 39 unspecified role unspecified role prey prey ecolx Escherichia coli association association asf1a-hist1h4a-3 20 34 unspecified role unspecified role bait bait Region 1-155 Region 1-155 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 Q9Y294:p.Val94Arg V94R mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain V R This feature has been corrected as a result of our quality control procedures. The original label was 'V94R'. Wed May 02 19:47:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val94arg' Tue Jun 30 19:56:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val94Arg' ecolx Escherichia coli 35 unspecified role unspecified role prey prey ecolx Escherichia coli 39 unspecified role unspecified role prey prey ecolx Escherichia coli 36 unspecified role unspecified role prey prey Region 43-160 Region 43-160 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli association association cenpa-hist1h4a-6 9 38 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 35 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction hist1h3a-mcm2-2 17 36 unspecified role unspecified role prey prey human Homo sapiens Human 37 unspecified role unspecified role bait bait HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range SNAP-tag SNAP-tag fusion protein fusion protein n-term range n-terminal range n-term range n-term range n-terminal range n-term range Tag used for western blot detection. P68431:p.[Arg64Ala;Lys65Ala] R64A/K65A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain K A certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R64A/K65A'. Wed May 02 20:25:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg64ala,lys65ala' Tue Jun 30 18:18:49 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg64Ala;Lys65Ala]' human Homo sapiens Human physical association physical association mcm2-cdc45-1 27 41 unspecified role unspecified role prey prey human Homo sapiens Human 31 unspecified role unspecified role prey prey human Homo sapiens Human 36 unspecified role unspecified role bait bait HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Tag used for western blot detection. Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human association association asf1a-mcm2-1 15 34 unspecified role unspecified role bait bait Region 1-155 Region 1-155 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 36 unspecified role unspecified role prey prey Region 43-160 Region 43-160 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P49736:p.[Asp80Ala;Tyr81Ala] D80A/Y81A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A certain certain sequence position certain certain certain sequence position certain D A This feature has been corrected as a result of our quality control procedures. The original label was 'D80A/Y81A'. Wed May 02 14:29:30 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp80ala,tyr81ala' Tue Jun 30 19:49:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asp80Ala;Tyr81Ala]' P49736:p.Tyr90Ala Y90A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y90A'. Wed May 02 15:34:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr90ala' Tue Jun 30 20:21:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr90Ala' P49736:p.Met117Ala M117A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain M A This feature has been corrected as a result of our quality control procedures. The original label was 'M117A'. Wed May 02 15:59:23 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'met117ala' Tue Jun 30 18:21:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Met117Ala' ecolx Escherichia coli physical association physical association hist1h4a-hist2h3a-1 18 35 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 39 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 36 unspecified role unspecified role unspecified role unspecified role Region 43-160 Region 43-160 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association hist1h4a-hist2h3a-2 28 35 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 39 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 36 unspecified role unspecified role unspecified role unspecified role Region 43-160 Region 43-160 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association mcm2-cenpa-1 6 38 unspecified role unspecified role prey prey ecolx Escherichia coli 35 unspecified role unspecified role prey prey ecolx Escherichia coli 36 unspecified role unspecified role bait bait Region 43-160 Region 43-160 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 association association mcm2-mcm6-12 8 30 unspecified role unspecified role prey prey human Homo sapiens Human 36 unspecified role unspecified role bait bait HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Tag used for western blot detection. Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human physical association physical association asf1a-hist1h4a-4 3 34 unspecified role unspecified role unspecified role unspecified role Region 1-172 Region 1-172 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 35 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 39 unspecified role unspecified role unspecified role unspecified role Region 57-136 Region 57-136 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 36 unspecified role unspecified role unspecified role unspecified role Region 43-160 Region 43-160 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association mcm2-hist1h4a-2 5 35 unspecified role unspecified role prey prey ecolx Escherichia coli 39 unspecified role unspecified role prey prey Q71DI3:p.[Arg64Ala;Lys65Ala] R64A/K65A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain K A certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R64A/K65A'. Wed May 02 16:51:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg64ala,lys65ala' Tue Jun 30 18:24:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg64Ala;Lys65Ala]' ecolx Escherichia coli 36 unspecified role unspecified role bait bait Region 43-160 Region 43-160 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 association association mcm2-hist1h4a-3 7 35 unspecified role unspecified role prey prey P62805:p.[Arg36Ala;Arg37Ala] R36A/R37A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain R A certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R36A/R37A'. Wed May 02 15:13:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg36ala,arg37ala' Tue Jun 30 17:08:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg36Ala;Arg37Ala]' ecolx Escherichia coli 39 unspecified role unspecified role prey prey ecolx Escherichia coli 36 unspecified role unspecified role bait bait Region 43-160 Region 43-160 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 association association h3f3a-hist1h4a-2 12 33 unspecified role unspecified role unspecified role unspecified role Region 58-136 Region 58-136 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 35 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 36 unspecified role unspecified role unspecified role unspecified role Region 61-160 Region 61-160 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association mcm2-asf1a-3 21 42 unspecified role unspecified role prey prey OneStrep-tag OneStrep-tag one-strep-tag one-strep-tag twin-strep-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human 34 unspecified role unspecified role prey prey human Homo sapiens Human 36 unspecified role unspecified role bait bait P49736:p.[Tyr81Ala;Tyr90Ala] Y81A/Y90A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y81A/Y90A'. Wed May 02 15:13:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr81ala,tyr90ala' Tue Jun 30 16:14:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Tyr81Ala;Tyr90Ala]' P49736:p.[Asp80Ala;Tyr81Ala] D80A/Y81A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A certain certain sequence position certain certain certain sequence position certain D A This feature has been corrected as a result of our quality control procedures. The original label was 'D80A/Y81A'. Wed May 02 19:14:44 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp80ala,tyr81ala' Tue Jun 30 19:08:37 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asp80Ala;Tyr81Ala]' P49736:p.Tyr90Ala Y90A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y90A'. Wed May 02 16:44:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr90ala' Tue Jun 30 16:57:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr90Ala' Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Tag used for western blot detection. human Homo sapiens Human association association asf1b-h3f3a-1 24 42 unspecified role unspecified role unspecified role unspecified role Region 1-158 Region 1-158 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 33 unspecified role unspecified role unspecified role unspecified role Region 58-136 Region 58-136 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 35 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 36 unspecified role unspecified role unspecified role unspecified role Region 61-160 Region 61-160 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association mcm2-hjurp-1 16 40 unspecified role unspecified role prey prey human Homo sapiens Human 36 unspecified role unspecified role bait bait Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human physical association physical association mcm2-cenpa-2 11 38 unspecified role unspecified role prey prey GFP-tag GFP-tag gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human 36 unspecified role unspecified role bait bait HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Tag used for western blot detection. Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range P49736:p.[Tyr81Ala;Tyr90Ala] Y81A/Y90A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y81A/Y90A'. Wed May 02 15:41:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr81ala,tyr90ala' Tue Jun 30 17:54:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Tyr81Ala;Tyr90Ala]' human Homo sapiens Human physical association physical association hist1h4a-hist2h3a-3 1 35 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 39 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction hist1h3a-mcm2-3 10 36 unspecified role unspecified role prey prey V5-tag V5-tag v5 tag v5 tag GKPIPNPLLGLDST epitope tag GKPIPNPLLGLDST epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human 37 unspecified role unspecified role bait bait HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human physical association physical association h3f3a-hist1h4a-3 22 33 unspecified role unspecified role unspecified role unspecified role Region 58-136 Region 58-136 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 35 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 36 unspecified role unspecified role unspecified role unspecified role Region 61-160 Region 61-160 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 mcm2-hist1h4a-4 13 35 unspecified role unspecified role prey prey human Homo sapiens Human 36 unspecified role unspecified role bait bait HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Tag used for western blot detection. Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range P49736:p.[Tyr81Ala;Tyr90Ala] Y81A/Y90A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y81A/Y90A'. Wed May 02 17:21:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr81ala,tyr90ala' Tue Jun 30 15:50:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Tyr81Ala;Tyr90Ala]' human Homo sapiens Human physical association physical association hist1h3a-asf1a-3 25 29 unspecified role unspecified role prey prey human Homo sapiens Human 32 unspecified role unspecified role prey prey human Homo sapiens Human 42 unspecified role unspecified role prey prey human Homo sapiens Human 34 unspecified role unspecified role prey prey human Homo sapiens Human 36 unspecified role unspecified role prey prey human Homo sapiens Human 37 unspecified role unspecified role bait bait HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range SNAP-tag SNAP-tag fusion protein fusion protein n-term range n-terminal range n-term range n-term range n-terminal range n-term range Tag used for western blot detection. human Homo sapiens Human association association mcm2-hist1h3a-1 23 36 unspecified role unspecified role bait bait V5-tag V5-tag v5 tag v5 tag GKPIPNPLLGLDST epitope tag GKPIPNPLLGLDST epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human 37 unspecified role unspecified role prey prey HA-tag HA-tag ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human physical association physical association