DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Hibbert RG., Huang A., Boelens R., Sixma TK. Only protein-protein interactions in vitro In vitro comigration in sds comigration in sds page comigration in sds western blot western blot Immuno blot Immuno blot Hibbert RG., Huang A., Boelens R., Sixma TK. DIP original experiment: DIP-253466X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Hibbert RG., Huang A., Boelens R., Sixma TK. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Hibbert RG., Huang A., Boelens R., Sixma TK. DIP original experiment: DIP-253467X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Hibbert RG., Huang A., Boelens R., Sixma TK. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Hibbert RG., Huang A., Boelens R., Sixma TK. DIP original experiment: DIP-253469X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Hibbert RG., Huang A., Boelens R., Sixma TK. 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 Hibbert RG., Huang A., Boelens R., Sixma TK. DIP original experiment: DIP-253470X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Hibbert RG., Huang A., Boelens R., Sixma TK. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Hibbert RG., Huang A., Boelens R., Sixma TK. DIP original experiment: DIP-253471X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Hibbert RG., Huang A., Boelens R., Sixma TK. Only protein-protein interactions in vitro In vitro comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Hibbert RG., Huang A., Boelens R., Sixma TK. DIP original experiment: DIP-253465X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. Proceedings of the National Academy of Sciences of the United States of America 2011 imex curation Hibbert RG., Huang A., Boelens R., Sixma TK. 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 Hibbert RG., Huang A., Boelens R., Sixma TK. DIP original experiment: DIP-253468X Proceedings of the National Academy of Sciences of the United States of America 2011 IMEx E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6. ubr1_human E3 ubiquitin-protein ligase UBR1 N-recognin-1 Ubiquitin-protein ligase E3-alpha-1 Ubiquitin-protein ligase E3-alpha-I UBR1 RING-type E3 ubiquitin transferase UBR1 protein protein human Homo sapiens Human MADEEAGGTERMEISAELPQTPQRLASWWDQQVDFYTAFLHHLAQLVPEIYFAEMDPDLEKQEESVQMSIFTPLEWYLFGEDPDICLEKLKHSGAFQLCGRVFKSGETTYSCRDCAIDPTCVLCMDCFQDSVHKNHRYKMHTSTGGGFCDCGDTEAWKTGPFCVNHEPGRAGTIKENSRCPLNEEVIVQARKIFPSVIKYVVEMTIWEEEKELPPELQIREKNERYYCVLFNDEHHSYDHVIYSLQRALDCELAEAQLHTTAIDKEGRRAVKAGAYAACQEAKEDIKSHSENVSQHPLHVEVLHSEIMAHQKFALRLGSWMNKIMSYSSDFRQIFCQACLREEPDSENPCLISRLMLWDAKLYKGARKILHELIFSSFFMEMEYKKLFAMEFVKYYKQLQKEYISDDHDRSISITALSVQMFTVPTLARHLIEEQNVISVITETLLEVLPEYLDRNNKFNFQGYSQDKLGRVYAVICDLKYILISKPTIWTERLRMQFLEGFRSFLKILTCMQGMEEIRRQVGQHIEVDPDWEAAIAIQMQLKNILLMFQEWCACDEELLLVAYKECHKAVMRCSTSFISSSKTVVQSCGHSLETKSYRVSEDLVSIHLPLSRTLAGLHVRLSRLGAVSRLHEFVSFEDFQVEVLVEYPLRCLVLVAQVVAEMWRRNGLSLISQVFYYQDVKCREEMYDKDIIMLQIGASLMDPNKFLLLVLQRYELAEAFNKTISTKDQDLIKQYNTLIEEMLQVLIYIVGERYVPGVGNVTKEEVTMREIIHLLCIEPMPHSAIAKNLPENENNETGLENVINKVATFKKPGVSGHGVYELKDESLKDFNMYFYHYSKTQHSKAEHMQKKRRKQENKDEALPPPPPPEFCPAFSKVINLLNCDIMMYILRTVFERAIDTDSNLWTEGMLQMAFHILALGLLEEKQQLQKAPEEEVTFDFYHKASRLGSSAMNIQMLLEKLKGIPQLEGQKDMITWILQMFDTVKRLREKSCLIVATTSGSESIKNDEITHDKEKAERKRKAEAARLHRQKIMAQMSALQKNFIETHKLMYDNTSEMPGKEDSIMEEESTPAVSDYSRIALGPKRGPSVTEKEVLTCILCQEEQEVKIENNAMVLSACVQKSTALTQHRGKPIELSGEALDPLFMDPDLAYGTYTGSCGHVMHAVCWQKYFEAVQLSSQQRIHVDLFDLESGEYLCPLCKSLCNTVIPIIPLQPQKINSENADALAQLLTLARWIQTVLARISGYNIRHAKGENPIPIFFNQGMGDSTLEFHSILSFGVESSIKYSNSIKEMVILFATTIYRIGLKVPPDERDPRVPMLTWSTCAFTIQAIENLLGDEGKPLFGALQNRQHNGLKALMQFAVAQRITCPQVLIQKHLVRLLSVVLPNIKSEDTPCLLSIDLFHVLVGAVLAFPSLYWDDPVDLQPSSVSSSYNHLYLFHLITMAHMLQILLTVDTGLPLAQVQEDSEEAHSASSFFAEISQYTSGSIGCDIPGWYLWVSLKNGITPYLRCAALFFHYLLGVTPPEELHTNSAEGEYSALCSYLSLPTNLFLLFQEYWDTVRPLLQRWCADPALLNCLKQKNTVVRYPRKRNSLIELPDDYSCLLNQASHFRCPRSADDERKHPVLCLFCGAILCSQNICCQEIVNGEEVGACIFHALHCGAGVCIFLKIRECRVVLVEGKARGCAYPAPYLDEYGETDPGLKRGNPLHLSRERYRKLHLVWQQHCIIEEIARSQETNQMLFGFNWQLL DIP protein Q8IWV7 original sequence version: 70 DIP protein Q8IWV7-1 original sequence version: 92 3AE0E1A749884971 ubiq_human UBIQ_HUMAN protein protein human Homo sapiens Human MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG pcna_human Proliferating cell nuclear antigen PCNA Cyclin protein protein human Homo sapiens Human MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEGS DIP protein P12004 original sequence version: 200 DIP protein P12004 original sequence version: 128 DIP protein P12004 original sequence version: 139 DIP protein P12004 original sequence version: 185 DIP protein P12004 original sequence version: 102 DIP protein P12004 original sequence version: 105 DIP protein P12004 original sequence version: 158 E6F08E7EDBC48B00 ube2b_human Ubiquitin-conjugating enzyme E2 B Ubiquitin-protein ligase B Ubiquitin carrier protein B RAD6 homolog B Ubiquitin-conjugating enzyme E2-17 kDa UBE2B RAD6B E2 ubiquitin-conjugating enzyme B protein protein human Homo sapiens Human MSTPARRRLMRDFKRLQEDPPVGVSGAPSENNIMQWNAVIFGPEGTPFEDGTFKLVIEFSEEYPNKPPTVRFLSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNSPANSQAAQLYQENKREYEKRVSAIVEQSWNDS DIP protein P63146 original sequence version: 115 DIP protein P63146 original sequence version: 51 DIP protein P63146 original sequence version: 79 DIP protein P63146 original sequence version: 101 CFDEEEE7E06840BE rad18_human E3 ubiquitin-protein ligase RAD18 RAD18 RNF73 Postreplication repair protein RAD18 RING finger protein 73 RING-type E3 ubiquitin transferase RAD18 protein protein human Homo sapiens Human MDSLAESRWPPGLAVMKTIDDLLRCGICFEYFNIAMIIPQCSHNYCSLCIRKFLSYKTQCPTCCVTVTEPDLKNNRILDELVKSLNFARNHLLQFALESPAKSPASSSSKNLAVKVYTPVASRQSLKQGSRLMDNFLIREMSGSTSELLIKENKSKFSPQKEASPAAKTKETRSVEEIAPDPSEAKRPEPPSTSTLKQVTKVDCPVCGVNIPESHINKHLDSCLSREEKKESLRSSVHKRKPLPKTVYNLLSDRDLKKKLKEHGLSIQGNKQQLIKRHQEFVHMYNAQCDALHPKSAAEIVREIENIEKTRMRLEASKLNESVMVFTKDQTEKEIDEIHSKYRKKHKSEFQLLVDQARKGYKKIAGMSQKTVTITKEDESTEKLSSVCMGQEDNMTSVTNHFSQSKLDSPEELEPDREEDSSSCIDIQEVLSSSESDSCNSSSSDIIRDLLEEEEAWEASHKNDLQDTEISPRQNRRTRAAESAEIEPRNKRNRN DIP protein Q9NS91 original sequence version: 129 DIP protein Q9NS91 original sequence version: 62 DIP protein Q9NS91 original sequence version: 64 DIP protein Q9NS91 original sequence version: 114 744A053A50C65DD7 ube2b-rad18-2 4 12 unspecified role unspecified role prey prey Region 339-366 Region 339-366 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 11 unspecified role unspecified role bait bait ecolx Escherichia coli direct interaction direct interaction ub-ube2b-1 6 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role 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 covalent binding covalent binding rad18-ube2b-1 7 12 unspecified role unspecified role unspecified role unspecified role Region 339-366 Region 339-366 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pcna-ub-6 1 10 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli covalent binding covalent binding ube2b-ubr1-1 5 8 unspecified role unspecified role unspecified role unspecified role Region 1013-1038 Region 1013-1038 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction ub-ube2b-2 3 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction rad18-ube2b-2 2 12 unspecified role unspecified role unspecified role unspecified role Region 339-366 Region 339-366 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction