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 Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions ecolx Escherichia coli tem transmission electron microscopy tem predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260799X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260811X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. 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 Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260804X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260800X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260806X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions in vitro In vitro ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260808X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions in vitro In vitro density sedimentation cosedimentation through density gradient density sedimentation weight silver stain molecular weight estimation by silver staining weight silver stain Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260818X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260819X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260796X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions in vitro In vitro density sedimentation cosedimentation through density gradient density sedimentation weight silver stain molecular weight estimation by silver staining weight silver stain Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260817X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260802X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260814X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions ecolx Escherichia coli light scattering light scattering predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260797X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260807X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions in vitro In vitro pull down pull down weight by staining molecular weight estimation by staining weight by staining Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260801X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260812X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260820X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions in vitro In vitro pull down pull down weight by staining molecular weight estimation by staining weight by staining Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260805X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. 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 Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260803X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions ecolx Escherichia coli density sedimentation cosedimentation through density gradient density sedimentation weight silver stain molecular weight estimation by silver staining weight silver stain Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260816X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260810X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions in vitro In vitro density sedimentation cosedimentation through density gradient density sedimentation weight silver stain molecular weight estimation by silver staining weight silver stain Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260815X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260813X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions ecolx Escherichia coli ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260798X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. Nature 2014 imex curation Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. Only protein-protein interactions in vitro In vitro ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Simon AC., Zhou JC., Perera RL., van Deursen F., Evrin C., Ivanova ME., Kilkenny ML., Renault L., Kjaer S., Matak-Vinković D., Labib K., Costa A., Pellegrini L. DIP original experiment: DIP-260809X Nature 2014 IMEx A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome. csm3_yeast Chromosome segregation in meiosis protein 3 CSM3 YM9796.01 YMR048W protein protein yeast Saccharomyces cerevisiae Baker's yeast MDQDFDSLLLGFNDSDSVQKDPTVPNGLDGSVVDPTIADPTAITARKRRPQVKLTAEKLLSDKGLPYVLKNAHKRIRISSKKNSYDNLSNIIQFYQLWAHELFPKAKFKDFMKICQTVGKTDPVLREYRVSLFRDEMGMSFDVGTRETGQDLERQSPMVEEHVTSAEERPIVADSFAQDKRNVNNVDYDNDEDDDIYHLSYRNRRGRVLDERGNNETVLNNVVPPKEDLDALLKTFRVQGPVGLEENEKKLLLGWLDAHRKMEKGSMTEEDVQLIQSLEEWEMNDIEGQHTHYDLLPGGDEFGVDQDELDAMKEMGF 0B92F561F91197AE 0B92F561F91197AE psf2_yeast DNA replication complex GINS protein PSF2 PSF2 YJL072C J1086 Partner of Sld five 2 HRF213 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSLPAHLQQTFSPEEIQFIVENEPIKIFPRITTRQKIRGDDRGTGNHTRWQLITTDDKALNNMVAMRSTEVVLWIALLLKQQSKCSIVAPQWLTTKELDRKIQYEKTHPDRFSELPWNWLVLARILFNKAKDDFHDPIHELRGKIQDLREIRQIKVLKGLKYLNESHLQLDNLSLLEINELRPFITEIMDKLREIHTASLTAGTENDEEEFNI C8B52C0462A37A3A C8B52C0462A37A3A psf1_yeast DNA replication complex GINS protein PSF1 Partner of Sld five 1 YDR013W YD8119.18 PZA208 PSF1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MYGDLGNKLVLEAKRTKQLYARSNQDVNLPMYHEDIIRNILKEVSNLRKNTEYLKEQQQLGMLDDKVAKCQYFVTLLCMERNKRCLLAYQRLRTDILDSMAWNNNGLDLMSSITFSQQDTNNLSHQEQEYLKEYCDLITDLKSGDLVDIDLSGSLVPPSDVFIDVRVLKDAGEIQTEYGVFNLIKDSQFFVRQSDVERLIQQGYLQKI 4667D8152C1AB5B4 4667D8152C1AB5B4 mcm2_yeast DNA replication licensing factor MCM2 MCM2 YBL023C YBL0438 Minichromosome maintenance protein 2 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSDNRRRRREEDDSDSENELPPSSPQQHFRGGMNPVSSPIGSPDMINPEGDDNEVDDVPDIDEVEEQMNEVDLMDDNMYEDYAADHNRDRYDPDQVDDREQQELSLSERRRIDAQLNERDRLLRNVAYIDDEDEEQEGAAQLDEMGLPVQRRRRRRQYEDLENSDDDLLSDMDIDPLREELTLESLSNVKANSYSEWITQPNVSRTIARELKSFLLEYTDETGRSVYGARIRTLGEMNSESLEVNYRHLAESKAILALFLAKCPEEMLKIFDLVAMEATELHYPDYARIHSEIHVRISDFPTIYSLRELRESNLSSLVRVTGVVTRRTGVFPQLKYVKFNCLKCGSILGPFFQDSNEEIRISFCTNCKSKGPFRVNGEKTVYRNYQRVTLQEAPGTVPPGRLPRHREVILLADLVDVSKPGEEVEVTGIYKNNYDGNLNAKNGFPVFATIIEANSIKRREGNTANEGEEGLDVFSWTEEEEREFRKISRDRGIIDKIISSMAPSIYGHRDIKTAVACSLFGGVPKNVNGKHSIRGDINVLLLGDPGTAKSQILKYVEKTAHRAVFATGQGASAVGLTASVRKDPITKEWTLEGGALVLADKGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTTLQARCSIIAAANPNGGRYNSTLPLAQNVSLTEPILSRFDILCVVRDLVDEEADERLATFVVDSHVRSHPENDEDREGEELKNNGESAIEQGEDEINEQLNARQRRLQRQRKKEEEISPIPQELLMKYIHYARTKIYPKLHQMDMDKVSRVYADLRRESISTGSFPITVRHLESILRIAESFAKMRLSEFVSSYDLDRAIKVVVDSFVDAQKVSVRRQLRRSFAIYTLGH F38FF682581B0EC0 F38FF682581B0EC0 sld5_yeast DNA replication complex GINS protein SLD5 YDR489W SLD5 protein protein yeast Saccharomyces cerevisiae Baker's yeast MDINIDDILAELDKETTAVDSTKITQGSSSTTHRDANTIVGSSLDLNDKTQIYVSPQQDFSDLMKSWKNERCSPELLPYPHQLMKRLLNRISMQSQLIENISMGFLDMQNASNANPPMPNESKLPLLCMETELERLKFVIRSYIRCRLSKIDKFSLYLRQLNEDENSLISLTDLLSKDEIKYHDTHSLIWLKLVNDSILKYMPEELQAINDTEGSVNMIDEPDWNKFVFIHVNGPPDGKWNEDPLLQENEFGKPCYTVTIPDLKEEVELTIGSIYVMRYEVIRDLLRDDKVALI 7EC516ADAD9900DD 7EC516ADAD9900DD pob3_yeast FACT complex subunit POB3 YML069W Facilitates chromatin transcription complex subunit POB3 POB3 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSTDFDRIYLNQSKFSGRFRIADSGLGWKISTSGGSAANQARKPFLLPATELSTVQWSRGCRGYDLKINTKNQGVIQLDGFSQDDYNLIKNDFHRRFNIQVEQREHSLRGWNWGKTDLARNEMVFALNGKPTFEIPYARINNTNLTSKNEVGIEFNIQDEEYQPAGDELVEMRFYIPGVIQTNVDENMTKKEESSNEVVPKKEDGAEGEDVQMAVEEKSMAEAFYEELKEKADIGEVAGDAIVSFQDVFFTTPRGRYDIDIYKNSIRLRGKTYEYKLQHRQIQRIVSLPKADDIHHLLVLAIEPPLRQGQTTYPFLVLQFQKDEETEVQLNLEDEDYEENYKDKLKKQYDAKTHIVLSHVLKGLTDRRVIVPGEYKSKYDQCAVSCSFKANEGYLYPLDNAFFFLTKPTLYIPFSDVSMVNISRAGQTSTSSRTFDLEVVLRSNRGSTTFANISKEEQQLLEQFLKSKNLRVKNEDREVQERLQTALGSDSDEEDINMGSAGEDDESVDEDFQVSSDNDADEVAEEFDSDAALSDAEGGSDEERPSKKPKVE 02C04F620C7B1450 02C04F620C7B1450 mcm4_yeast DNA replication licensing factor MCM4 MCM4 HCD21 YPR019W YP9531.13 CDC54 Cell division control protein 54 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSQQSSSPTKEDNNSSSPVVPNPDSVPPQLSSPALFYSSSSSQGDIYGRNNSQNLSQGEGNIRAAIGSSPLNFPSSSQRQNSDVFQSQGRQGRIRSSASASGRSRYHSDLRSDRALPTSSSSLGRNGQNRVHMRRNDIHTSDLSSPRRIVDFDTRSGVNTLDTSSSSAPPSEASEPLRIIWGTNVSIQECTTNFRNFLMSFKYKFRKILDEREEFINNTTDEELYYIKQLNEMRELGTSNLNLDARNLLAYKQTEDLYHQLLNYPQEVISIMDQTIKDCMVSLIVDNNLDYDLDEIETKFYKVRPYNVGSCKGMRELNPNDIDKLINLKGLVLRSTPVIPDMKVAFFKCNVCDHTMAVEIDRGVIQEPARCERIDCNEPNSMSLIHNRCSFADKQVIKLQETPDFVPDGQTPHSISLCVYDELVDSCRAGDRIEVTGTFRSIPIRANSRQRVLKSLYKTYVDVVHVKKVSDKRLDVDTSTIEQELMQNKVDHNEVEEVRQITDQDLAKIREVAAREDLYSLLARSIAPSIYELEDVKKGILLQLFGGTNKTFTKGGRYRGDINILLCGDPSTSKSQILQYVHKITPRGVYTSGKGSSAVGLTAYITRDVDTKQLVLESGALVLSDGGVCCIDEFDKMSDSTRSVLHEVMEQQTISIAKAGIITTLNARSSILASANPIGSRYNPNLPVTENIDLPPPLLSRFDLVYLVLDKVDEKNDRELAKHLTNLYLEDKPEHISQDDVLPVEFLTMYISYAKEHIHPIITEAAKTELVRAYVGMRKMGDDSRSDEKRITATTRQLESMIRLAEAHAKMKLKNVVELEDVQEAVRLIRSAIKDYATDPKTGKIDMNLVQTGKSVIQRKLQEDLSREIMNVLKDQASDSMSFNELIKQINEHSQDRVESSDIQEALSRLQQEDKVIVLGEGVRRSVRLNNRV 382D542AE38975E3 382D542AE38975E3 psf3_yeast DNA replication complex GINS protein PSF3 YOL146W Partner of Sld five 3 PSF3 protein protein yeast Saccharomyces cerevisiae Baker's yeast MGYYDIDDVLADGTEFPCKFQYDIPGLGYLENNPGRPITKNTKLSLPLWLARILAIVGGDEALVDEEPVPFVELLPPDMFSTKVMNAIKTDPVALDLHSINSHFFSLAIKWIMLFSEKELANVVSELLLQRAQELNHHASSLSIDLNADSTGKNSANTNIATSTFLLKLEEMEKEIYKKSHESYKDTKRWMFKK 3E8B60DFCE16391D 3E8B60DFCE16391D mcm3_yeast DNA replication licensing factor MCM3 MCM3 YEL032W SYGP-ORF23 Minichromosome maintenance protein 3 protein protein yeast Saccharomyces cerevisiae Baker's yeast MEGSTGFDGDATTFFAPDAVFGDRVRRFQEFLDTFTSYRDSVRSIQVYNSNNAANYNDDQDDADERDLLGDDDGDDLEKEKKAASSTSLNILPHRIIISLDDLREFDRSFWSGILVEPAYFIPPAEKALTDLADSMDDVPHPNASAVSSRHPWKLSFKGSFGAHALSPRTLTAQHLNKLVSVEGIVTKTSLVRPKLIRSVHYAAKTGRFHYRDYTDATTTLTTRIPTPAIYPTEDTEGNKLTTEYGYSTFIDHQRITVQEMPEMAPAGQLPRSIDVILDDDLVDKTKPGDRVNVVGVFKSLGAGGMNQSNSNTLIGFKTLILGNTVYPLHARSTGVAARQMLTDFDIRNINKLSKKKDIFDILSQSLAPSIYGHDHIKKAILLMLMGGVEKNLENGSHLRGDINILMVGDPSTAKSQLLRFVLNTASLAIATTGRGSSGVGLTAAVTTDRETGERRLEAGAMVLADRGVVCIDEFDKMTDVDRVAIHEVMEQQTVTIAKAGIHTTLNARCSVIAAANPVFGQYDVNRDPHQNIALPDSLLSRFDLLFVVTDDINEIRDRSISEHVLRTHRYLPPGYLEGEPVRERLNLSLAVGEDADINPEEHSNSGAGVENEGEDDEDHVFEKFNPLLQAGAKLAKNKGNYNGTEIPKLVTIPFLRKYVQYAKERVIPQLTQEAINVIVKNYTDLRNDDNTKKSPITARTLETLIRLATAHAKVRLSKTVNKVDAKVAANLLRFALLGEDIGNDIDEEESEYEEALSKRSPQKSPKKRQRVRQPASNSGSPIKSTPRRSTASSVNATPSSARRILRFQDDEQNAGEDDNDIMSPLPADEEAELQRRLQLGLRVSPRRREHLHAPEEGSSGPLTEVGTPRLPNVSSAGQDDEQQQSVISFDNVEPGTISTGRLSLISGIIARLMQTEIFEEESYPVASLFERINEELPEEEKFSAQEYLAGLKIMSDRNNLMVADDKVWRV 43DD4DACAF4456DC 43DD4DACAF4456DC cdc45_yeast Cell division control protein 45 CDC45 YLR103C L8004.11 SLD4 protein protein yeast Saccharomyces cerevisiae Baker's yeast MYYGISQFSEAYNKILRNSSSHSSCQLVIFVSCLNIDALCATKMLSLLFKKQLVQSQIVPIFGYSELRRHYSQLDDNINSLLLVGFGGVIDLEAFLEIDPQEYVIDTDEKSGEQSFRRDIYVLDAHRPWNLDNIFGSQIIQCFDDGTVDDTLGEQKEAYYKLLELDEESGDDELSGDENDNNGGDDEATDADEVTDEDEEDEDETISNKRGNSSIGPNDLSKRKQRKKQIHEYEGVLEEYYSQGTTVVNSISAQIYSLLSAIGETNLSNLWLNILGTTSLDIAYAQVYNRLYPLLQDEVKRLTPSSRNSVKTPDTLTLNIQPDYYLFLLRHSSLYDSFYYSNYVNAKLSLWNENGKKRLHKMFARMGIPLSTAQETWLYMDHSIKRELGIIFDKNLDRYGLQDIIRDGFVRTLGYRGSISASEFVEALTALLEVGNSTDKDSVKINNDNNDDTDGEEEEDNSAQKLTNLRKRWVSNFWLSWDALDDRKVELLNRGIQLAQDLQRAIFNTGVAILEKKLIKHLRIYRLCVLQDGPDLDLYRNPLTLLRLGNWLIECCAESEDKQLLPMVLASIDENTDTYLVAGLTPRYPRGLDTIHTKKPILNNFSMAFQQITAETDAKVRIDNFESSIIEIRREDLSPFLEKLTLSGLL 6500DDD62EC4E8EE 6500DDD62EC4E8EE mcm6_yeast DNA replication licensing factor MCM6 YGL201C MCM6 Minichromosome maintenance protein 6 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSSPFPADTPSSNRPSNSSPPPSSIGAGFGSSSGLDSQIGSRLHFPSSSQPHVSNSQTGPFVNDSTQFSSQRLQTDGSATNDMEGNEPARSFKSRALNHVKKVDDVTGEKVREAFEQFLEDFSVQSTDTGEVEKVYRAQIEFMKIYDLNTIYIDYQHLSMRENGALAMAISEQYYRFLPFLQKGLRRVVRKYAPELLNTSDSLKRSEGDEGQADEDEQQDDDMNGSSLPRDSGSSAAPGNGTSAMATRSITTSTSPEQTERVFQISFFNLPTVHRIRDIRSEKIGSLLSISGTVTRTSEVRPELYKASFTCDMCRAIVDNVEQSFKYTEPTFCPNPSCENRAFWTLNVTRSRFLDWQKVRIQENANEIPTGSMPRTLDVILRGDSVERAKPGDRCKFTGVEIVVPDVTQLGLPGVKPSSTLDTRGISKTTEGLNSGVTGLRSLGVRDLTYKISFLACHVISIGSNIGASSPDANSNNRETELQMAANLQANNVYQDNERDQEVFLNSLSSDEINELKEMVKDEHIYDKLVRSIAPAVFGHEAVKKGILLQMLGGVHKSTVEGIKLRGDINICVVGDPSTSKSQFLKYVVGFAPRSVYTSGKASSAAGLTAAVVRDEEGGDYTIEAGALMLADNGICCIDEFDKMDISDQVAIHEAMEQQTISIAKAGIHATLNARTSILAAANPVGGRYNRKLSLRGNLNMTAPIMSRFDLFFVILDDCNEKIDTELASHIVDLHMKRDEAIEPPFSAEQLRRYIKYARTFKPILTKEARSYLVEKYKELRKDDAQGFSRSSYRITVRQLESMIRLSEAIARANCVDEITPSFIAEAYDLLRQSIIRVDVDDVEMDEEFDNIESQSHAASGNNDDNDDGTGSGVITSEPPADIEEGQSEATARPGTSEKKKTTVTYDKYVSMMNMIVRKIAEVDREGAEELTAVDIVDWYLLQKENDLGSLAEYWEERRLAFKVIKRLVKDRILMEIHGTRHNLRDLENEENENNKTVYVIHPNCEVLDQLEPQDSS 03AB793134E64A50 03AB793134E64A50 dpoa_yeast DNA polymerase alpha catalytic subunit A POL1 CDC17 DNA polymerase alpha:primase complex p180 subunit DNA polymerase I subunit A N2181 YNL102W protein protein yeast Saccharomyces cerevisiae Baker's yeast MSSKSEKLEKLRKLQAARNGTSIDDYEGDESDGDRIYDEIDEKEYRARKRQELLHDDFVVDDDGVGYVDRGVEEDWREVDNSSSDEDTGNLASKDSKRKKNIKREKDHQITDMLRTQHSKSTLLAHAKKSQKKSIPIDNFDDILGEFESGEVEKPNILLPSKLRENLNSSPTSEFKSSIKRVNGNDESSHDAGISKKVKIDPDSSTDKYLEIESSPLKLQSRKLRYANDVQDLLDDVENSPVVATKRQNVLQDTLLANPPSAQSLADEEDDEDSDEDIILKRRTMRSVTTTRRVNIDSRSNPSTSPFVTAPGTPIGIKGLTPSKSLQSNTDVATLAVNVKKEDVVDPETDTFQMFWLDYCEVNNTLILFGKVKLKDDNCVSAMVQINGLCRELFFLPREGKTPTDIHEEIIPLLMDKYGLDNIRAKPQKMKYSFELPDIPSESDYLKVLLPYQTPKSSRDTIPSDLSSDTFYHVFGGNSNIFESFVIQNRIMGPCWLDIKGADFNSIRNASHCAVEVSVDKPQNITPTTTKTMPNLRCLSLSIQTLMNPKENKQEIVSITLSAYRNISLDSPIPENIKPDDLCTLVRPPQSTSFPLGLAALAKQKLPGRVRLFNNEKAMLSCFCAMLKVEDPDVIIGHRLQNVYLDVLAHRMHDLNIPTFSSIGRRLRRTWPEKFGRGNSNMNHFFISDICSGRLICDIANEMGQSLTPKCQSWDLSEMYQVTCEKEHKPLDIDYQNPQYQNDVNSMTMALQENITNCMISAEVSYRIQLLTLTKQLTNLAGNAWAQTLGGTRAGRNEYILLHEFSRNGFIVPDKEGNRSRAQKQRQNEENADAPVNSKKAKYQGGLVFEPEKGLHKNYVLVMDFNSLYPSIIQEFNICFTTVDRNKEDIDELPSVPPSEVDQGVLPRLLANLVDRRREVKKVMKTETDPHKRVQCDIRQQALKLTANSMYGCLGYVNSRFYAKPLAMLVTNKGREILMNTRQLAESMNLLVVYGDTDSVMIDTGCDNYADAIKIGLGFKRLVNERYRLLEIDIDNVFKKLLLHAKKKYAALTVNLDKNGNGTTVLEVKGLDMKRREFCPLSRDVSIHVLNTILSDKDPEEALQEVYDYLEDIRIKVETNNIRIDKYKINMKLSKDPKAYPGGKNMPAVQVALRMRKAGRVVKAGSVITFVITKQDEIDNAADTPALSVAERAHALNEVMIKSNNLIPDPQYYLEKQIFAPVERLLERIDSFNVVRLSEALGLDSKKYFRREGGNNNGEDINNLQPLETTITDVERFKDTVTLELSCPSCDKRFPFGGIVSSNYYRVSYNGLQCKHCEQLFTPLQLTSQIEHSIRAHISLYYAGWLQCDDSTCGIVTRQVSVFGKRCLNDGCTGVMRYKYSDKQLYNQLLYFDSLFDCEKNKKQELKPIYLPDDLDYPKEQLTESSIKALTEQNRELMETGRSVVQKYLNDCGRRYVDMTSIFDFMLN 50C9032DBE95B5AE 50C9032DBE95B5AE ctf4_yeast DNA polymerase alpha-binding protein CTF4 CHL15 POB1 YPR135W P9659.7 Chromosome transmission fidelity protein 4 Protein POB1 Chromosome replication protein CHL15 protein protein yeast Saccharomyces cerevisiae Baker's yeast MVSVIDKLVFDFGGKTLVSLAPDNNTLCVANKNGLTKILKTNNPEEEPETLDSSKLVSSIKCYSNSHFLMTTMQGDALRYNIDSSQEELLARFALPLRDCCVIHSGKMAVFGGDDLELILLELDDETHKKHAIKIDEQVSQISYNSQMNILAVSMINGKVQIFSLTSTIPNKVHELNDYIVANSYDDTHRDKILSNMMDDIDKDNDNDLSETADPDENNVADPEFCAANRICTRVAWHPKGLHFALPCADDTVKIFSIKGYSLQKTLSTNLSSTKAHFIDLQFDPLRGTYIAAVDLNNKLTVWNWETSEIHYTREFKRKITNIAWKIQADSKTLDLVLGTWSGSIAIVQNLAESVVSNIPDQSVAESSTKHGLFVDSESDLENLEGNDDINKSDKLFSDITQEANAEDVFTQTHDGPSGLSEKRKYNFEDEEDFIDDDDGAGYISGKKPHNEHSYSRVHKTHSFPISLANTGKFRYMPFSPAGTPFGFTDRRYLTMNEVGYVSTVKNSEQYSITVSFFDVGRFREYHFEDLFGYDLCFLNEKGTLFGQSKTGQIQYRPHDSIHSNWTKIIPLQAGERITSVAATPVRVIVGTSLGYFRSFNQFGVPFAVEKTSPIVALTAQNYRVFSVHYSQFHGLSYSLSELGTSSKRYYKRECPLPMSLPNINSDMKKDANLDYYNFNPMGIKSLFFSSYGDPCIFGSDNTLLLLSKWRSPEESKWLPILDSNMEIWKMSGGKETTDIHVWPLALAYDTLNCILVKGKHIWPEFPLPLPSEMEIRMPVFVKSKLLEENKAILNKKNEIGADTEAEEGEEDKEIQIPVSMAAEEEYLRSKVLSELLTDTLENDGEMYGNENEVLAALNGAYDKALLRLFASACSDQNVEKALSLAHELKQDRALTAAVKISERAELPSLVKKINNIREARYEQQLK E2ABBB244B5F8B4D E2ABBB244B5F8B4D mcm5_yeast Minichromosome maintenance protein 5 MCM5 CDC46 YLR274W L9328.1 Cell division control protein 46 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSFDRPEIYSAPVLQGESPNDDDNTEIIKSFKNFILEFRLDSQFIYRDQLRNNILVKNYSLTVNMEHLIGYNEDIYKKLSDEPSDIIPLFETAITQVAKRISILSRAQSANNNDKDPENTSMDTDSLLLNSLPTFQLILNSNANQIPLRDLDSEHVSKIVRLSGIIISTSVLSSRATYLSIMCRNCRHTTSITINNFNSITGNTVSLPRSCLSTIESESSMANESNIGDESTKKNCGPDPYIIIHESSKFIDQQFLKLQEIPELVPVGEMPRNLTMTCDRYLTNKVIPGTRVTIVGIYSIYNSKNGAGSGRSGGGNGGSGVAIRTPYIKILGIQSDVETSSIWNSVTMFTEEEEEEFLQLSRNPKLYEILTNSIAPSIFGNEDIKKAIVCLLMGGSKKILPDGMRLRGDINVLLLGDPGTAKSQLLKFVEKVSPIAVYTSGKGSSAAGLTASVQRDPMTREFYLEGGAMVLADGGVVCIDEFDKMRDEDRVAIHEAMEQQTISIAKAGITTVLNSRTSVLAAANPIYGRYDDLKSPGDNIDFQTTILSRFDMIFIVKDDHNEERDISIANHVINIHTGNANAMQNQQEENGSEISIEKMKRYITYCRLKCAPRLSPQAAEKLSSNFVTIRKQLLINELESTERSSIPITIRQLEAIIRITESLAKLELSPIAQERHVDEAIRLFQASTMDAASQDPIGGLNQASGTSLSEIRRFEQELKRRLPIGWSTSYQTLRREFVDTHRFSQLALDKALYALEKHETIQLRHQGQNIYRSGV 01D9DE208A091CF2 01D9DE208A091CF2 ctf4-pol1-3 10 37 unspecified role unspecified role unspecified role unspecified role Region 1-351 Region 1-351 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 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 ctf4-pol1-4 2 37 unspecified role unspecified role unspecified role unspecified role Region 1-351 Region 1-351 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 30 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 33 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 28 unspecified role unspecified role unspecified role unspecified role Region 1-164 Region 1-164 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 ctf4-1 9 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 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 sld5-ctf4-1 18 30 unspecified role unspecified role bait bait Region 1-18 Region 1-18 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q03406:p.Ile8Ala I8A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain I A This feature has been corrected as a result of our quality control procedures. The original label was 'I8A'. Wed May 02 17:39:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile8ala' Tue Jun 30 19:08:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile8Ala' Q03406:p.Leu9Ala L9A mutation disrupting strength mutation disrupting interaction strength mutation disrupting 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 'L9A'. Wed May 02 18:00:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu9ala' Tue Jun 30 17:54:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu9Ala' 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 38 unspecified role unspecified role prey prey Region 471-927 Region 471-927 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 ctf4-2 13 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 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 ctf4-3 24 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 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 psf1-psf2-2 20 30 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 33 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 28 unspecified role unspecified role unspecified role unspecified role Region 1-164 Region 1-164 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 ctf4-4 1 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 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 ctf4-pol1-5 16 37 unspecified role unspecified role unspecified role unspecified role Region 1-351 Region 1-351 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 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 mcm4-mcm2-1 17 29 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 36 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 39 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 32 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 c-term range C-terminal range c-term range c-term range C-terminal range c-term range yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast association association ctf4-5 4 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 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 psf1-psf2-3 5 30 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 33 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 28 unspecified role unspecified role unspecified role unspecified role Region 1-164 Region 1-164 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 ctf4-psf1-2 14 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 30 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 33 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 28 unspecified role unspecified role unspecified role unspecified role Region 1-164 Region 1-164 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 ctf4-pol1-6 7 37 unspecified role unspecified role unspecified role unspecified role Region 1-351 Region 1-351 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 30 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 33 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 28 unspecified role unspecified role unspecified role unspecified role Region 1-164 Region 1-164 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 pol1-ctf4-1 15 37 unspecified role unspecified role bait bait Region 137-149 Region 137-149 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain P13382:p.Phe140Ala F140A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A This feature has been corrected as a result of our quality control procedures. The original label was 'F140A'. Wed May 02 20:26:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe140ala' Tue Jun 30 18:45:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe140Ala' P13382:p.Asp142Ala D142A 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 'D142A'. Wed May 02 16:57:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp142ala' Tue Jun 30 19:58:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp142Ala' P13382:p.Ile143Ala I143A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain I A This feature has been corrected as a result of our quality control procedures. The original label was 'I143A'. Wed May 02 16:19:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile143ala' Tue Jun 30 18:07:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile143Ala' P13382:p.Leu144Ala L144A mutation disrupting strength mutation disrupting interaction strength mutation disrupting 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 'L144A'. Wed May 02 15:20:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu144ala' Tue Jun 30 17:23:45 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu144Ala' P13382:p.Phe147Ala F147A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A This feature has been corrected as a result of our quality control procedures. The original label was 'F147A'. Wed May 02 17:50:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe147ala' Tue Jun 30 19:38:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe147Ala' 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 38 unspecified role unspecified role prey prey Region 471-927 Region 471-927 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 ctf4-sld5-1 12 30 unspecified role unspecified role unspecified role unspecified role Region 1-19 Region 1-19 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Fluorescein-label Fluorescein-label fluorescein fluorescein label fluorescein n-term range n-terminal range n-term range n-term range n-terminal range n-term range in vitro In vitro 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 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 ctf4-pol1-7 23 37 unspecified role unspecified role unspecified role unspecified role Region 137-149 Region 137-149 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Fluorescein-label Fluorescein-label fluorescein fluorescein label fluorescein n-term range n-terminal range n-term range n-term range n-terminal range n-term range in vitro In vitro 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 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 mcm4-cdc45-1 8 33 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 35 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 28 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 30 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 37 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 38 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 26 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 31 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 29 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 36 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 39 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 32 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 c-term range C-terminal range c-term range c-term range C-terminal range c-term range yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast association association pol1-cdc45-1 11 38 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 34 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 35 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 28 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 30 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 37 unspecified role unspecified role bait bait Myc-tag Myc-tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast association association ctf4-pol1-8 6 37 unspecified role unspecified role unspecified role unspecified role Region 137-149 Region 137-149 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 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 ctf4-pol1-9 19 37 unspecified role unspecified role unspecified role unspecified role Region 137-149 Region 137-149 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 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 ctf4-sld5-2 25 30 unspecified role unspecified role unspecified role unspecified role Region 1-19 Region 1-19 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 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 ctf4-sld5-3 3 30 unspecified role unspecified role unspecified role unspecified role Region 1-19 Region 1-19 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 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 ctf4-psf1-3 21 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 30 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 33 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 28 unspecified role unspecified role unspecified role unspecified role Region 1-164 Region 1-164 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 ctf4-psf1-4 22 38 unspecified role unspecified role unspecified role unspecified role Region 471-927 Region 471-927 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 30 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 33 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 27 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 28 unspecified role unspecified role unspecified role unspecified role Region 1-164 Region 1-164 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