DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation De Marco V., Gillespie PJ., Li A., Karantzelis N., Christodoulou E., Klompmaker R., van Gerwen S., Fish A., Petoukhov MV., Iliou MS., Lygerou Z., Medema RH., Blow JJ., Svergun DI., Taraviras S., Perrakis A. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined De Marco V., Gillespie PJ., Li A., Karantzelis N., Christodoulou E., Klompmaker R., van Gerwen S., Fish A., Petoukhov MV., Iliou MS., Lygerou Z., Medema RH., Blow JJ., Svergun DI., Taraviras S., Perrakis A. DIP original experiment: DIP-134776X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation De Marco V., Gillespie PJ., Li A., Karantzelis N., Christodoulou E., Klompmaker R., van Gerwen S., Fish A., Petoukhov MV., Iliou MS., Lygerou Z., Medema RH., Blow JJ., Svergun DI., Taraviras S., Perrakis A. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined De Marco V., Gillespie PJ., Li A., Karantzelis N., Christodoulou E., Klompmaker R., van Gerwen S., Fish A., Petoukhov MV., Iliou MS., Lygerou Z., Medema RH., Blow JJ., Svergun DI., Taraviras S., Perrakis A. DIP original experiment: DIP-134779X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation De Marco V., Gillespie PJ., Li A., Karantzelis N., Christodoulou E., Klompmaker R., van Gerwen S., Fish A., Petoukhov MV., Iliou MS., Lygerou Z., Medema RH., Blow JJ., Svergun DI., Taraviras S., Perrakis A. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined De Marco V., Gillespie PJ., Li A., Karantzelis N., Christodoulou E., Klompmaker R., van Gerwen S., Fish A., Petoukhov MV., Iliou MS., Lygerou Z., Medema RH., Blow JJ., Svergun DI., Taraviras S., Perrakis A. DIP original experiment: DIP-134780X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation De Marco V., Gillespie PJ., Li A., Karantzelis N., Christodoulou E., Klompmaker R., van Gerwen S., Fish A., Petoukhov MV., Iliou MS., Lygerou Z., Medema RH., Blow JJ., Svergun DI., Taraviras S., Perrakis A. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined De Marco V., Gillespie PJ., Li A., Karantzelis N., Christodoulou E., Klompmaker R., van Gerwen S., Fish A., Petoukhov MV., Iliou MS., Lygerou Z., Medema RH., Blow JJ., Svergun DI., Taraviras S., Perrakis A. DIP original experiment: DIP-134775X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation De Marco V., Gillespie PJ., Li A., Karantzelis N., Christodoulou E., Klompmaker R., van Gerwen S., Fish A., Petoukhov MV., Iliou MS., Lygerou Z., Medema RH., Blow JJ., Svergun DI., Taraviras S., Perrakis A. Only protein-protein interactions ecolx Escherichia coli saxs x ray scattering saxs predetermined predetermined participant predetermined De Marco V., Gillespie PJ., Li A., Karantzelis N., Christodoulou E., Klompmaker R., van Gerwen S., Fish A., Petoukhov MV., Iliou MS., Lygerou Z., Medema RH., Blow JJ., Svergun DI., Taraviras S., Perrakis A. DIP original experiment: DIP-134778X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation De Marco V., Gillespie PJ., Li A., Karantzelis N., Christodoulou E., Klompmaker R., van Gerwen S., Fish A., Petoukhov MV., Iliou MS., Lygerou Z., Medema RH., Blow JJ., Svergun DI., Taraviras S., Perrakis A. 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 De Marco V., Gillespie PJ., Li A., Karantzelis N., Christodoulou E., Klompmaker R., van Gerwen S., Fish A., Petoukhov MV., Iliou MS., Lygerou Z., Medema RH., Blow JJ., Svergun DI., Taraviras S., Perrakis A. DIP original experiment: DIP-134777X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. cdt1_human DNA replication factor Cdt1 Double parked homolog CDT1 protein protein human Homo sapiens Human MEQRRVTDFFARRRPGPPRIAPPKLACRTPSPARPALRAPASATSGSRKRARPPAAPGRDQARPPARRRLRLSVDEVSSPSTPEAPDIPACPSPGQKIKKSTPAAGQPPHLTSAQDQDTISELASCLQRARELGARVRALKASAQDAGESCTPEAEGRPEEPCGEKAPAYQRFHALAQPGLPGLVLPYKYQVLAEMFRSMDTIVGMLHNRSETPTFAKVQRGVQDMMRRRFEECNVGQIKTVYPASYRFRQERSVPTFKDGTRRSDYQLTIEPLLEQEADGAAPQLTASRLLQRRQIFSQKLVEHVKEHHKAFLASLSPAMVVPEDQLTRWHPRFNVDEVPDIEPAALPQPPATEKLTTAQEVLARARNLISPRMEKALSQLALRSAAPSSPGSPRPALPATPPATPPAASPSALKGVSQDLLERIRAKEAQKQLAQMTRCPEQEQRLQRLERLPELARVLRSVFVSERKPALSMEVACARMVGSCCTIMSPGEMEKHLLLLSELLPDWLSLHRIRTDTYVKLDKAADLAHITARLAHQTRAEEGL DIP protein Q9H211 original sequence version: 69 DIP protein Q9H211 original sequence version: 124 8179D0330C135FB7 cdt1_xenla DNA replication factor Cdt1 cdt1 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MSQMRVTDFFSQSKRGTAAQNSKGRKVEAVLETRRAVTRSRAASVKAEEFLKAPCTPERASPTVSQCIGPSSKKRTRQDSDSEPLRTQQRQGKSARKKLKLPEGEHGGSVQQQLFSPCNKVALEHVTPSSLGKKIKDMVNVSLSPKFNELARNPTTPETKSPAKENLLELKSRLQRIQELAQKVNLPAASSEGKVTITDLKARLKRAQELDTKIRAKAEKTETQAIDLTEQPAQESEKAPAYQRFHNLAQDAAPGLTLPYKYKVLAEMFRSMDTIVGMLFNRSETITFSKVKQGVQDMMRKQFEQRNVGQIKTVYPNAYKYRQEKNIPTFKDGVKKTDYQLTIEPLVAEGDMLSGRPHLSASRLLERKQLFHRSLTSIVKQHHRVFLTSLNPPMLVPDDKLTRWHPRFNVDEVLDVTPAELPLPPQVERLTTAQEVLSKARGLITPKMEKALANLALKTAENAGETKNVSTEETKSTATTSTSTALKGVSQSLLERIRAKEAQKLQAIMTRRPQQEERLLMMSRLPELARILRNVFVAEKKPALTLEVTCSRVIASCRSSMSPGEMEKHLALLSEILPDWLSIHPVRKDTYYKLNQSMDLNLILERLAKKTKEEESL DIP protein Q9I9A7 original sequence version: 26 F42840DDDFE30E5E gemi_human Geminin GMNN protein protein human Homo sapiens Human MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI DIP protein O75496 original sequence version: 78 DIP protein O75496 original sequence version: 117 DIP protein O75496 original sequence version: 136 0BABE60F6F5AC252 cdt1-gmnn-15 6 9 unspecified role unspecified role unspecified role unspecified role Coiled-coil domain Region 82-145 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 158-356 Region 158-356 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cdt1-gmnn-16 4 9 unspecified role unspecified role unspecified role unspecified role Coiled-coil domain Region 82-160 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 158-356 Region 158-356 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cdt1-gmnn-17 2 9 unspecified role unspecified role prey prey Coiled-coil domain Region 82-145 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role bait bait Region 158-396 Region 158-396 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cdt1-gmnn-18 5 9 unspecified role unspecified role unspecified role unspecified role Coiled-coil domain Region 82-145 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role Region 158-356 Region 158-356 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction cdt1-gmnn-19 1 8 unspecified role unspecified role bait bait 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 9 unspecified role unspecified role prey prey Region 28-145 Region 28-145 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association cdt1-gmnn-20 3 9 unspecified role unspecified role prey prey Coiled-coil domain Region 82-145 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 7 unspecified role unspecified role bait bait Region 158-356 Region 158-356 binding region binding-associated region binding region 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 physical association physical association