DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ hibbert-2011-1 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. Hibbert RG., Huang A., Boelens R., Sixma TK. Only protein-protein interactions imex curation hibbert-2011-2 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. Hibbert RG., Huang A., Boelens R., Sixma TK. Only protein-protein interactions imex curation hibbert-2011-3 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. Hibbert RG., Huang A., Boelens R., Sixma TK. Only protein-protein interactions imex curation hibbert-2011-4 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. Hibbert RG., Huang A., Boelens R., Sixma TK. Only protein-protein interactions imex curation hibbert-2011-5 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. Hibbert RG., Huang A., Boelens R., Sixma TK. Only protein-protein interactions imex curation hibbert-2011-6 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. Hibbert RG., Huang A., Boelens R., Sixma TK. Only protein-protein interactions imex curation hibbert-2011-7 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. Hibbert RG., Huang A., Boelens R., Sixma TK. Only protein-protein interactions imex curation 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 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 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 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 ube2b-rad18-2 3223456 N/A 3223463 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 false in vitro In vitro N/A 3223464 unspecified role unspecified role bait bait ecolx Escherichia coli direct interaction direct interaction false false false ub-ube2b-1 3223457 N/A 3223465 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3223464 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 false ecolx Escherichia coli covalent binding covalent binding false false false rad18-ube2b-1 3223458 N/A 3223463 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 false in vitro In vitro N/A 3223464 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false pcna-ub-6 3223459 N/A 3223466 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3223465 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli covalent binding covalent binding false false false ube2b-ubr1-1 3223460 N/A 3223467 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 false in vitro In vitro N/A 3223464 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false ub-ube2b-2 3223461 N/A 3223465 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3223464 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false rad18-ube2b-2 3223462 N/A 3223463 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 false in vitro In vitro N/A 3223464 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false