DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. 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 Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251153X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. 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 Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251156X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. 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 Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251154X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251144X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251150X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. Only protein-protein interactions in vitro In vitro comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251151X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251146X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251145X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. Only protein-protein interactions in vitro In vitro ion exchange chrom ion exchange chromatography IEC IEC ion exchange chrom predetermined predetermined participant predetermined Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251148X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. 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 Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251155X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. 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 Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251149X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. 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 Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251158X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251152X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. 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 Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251159X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251147X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nature structural & molecular biology 2012 imex curation Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. 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 Dou H., Buetow L., Sibbet GJ., Cameron K., Huang DT. DIP original experiment: DIP-251157X Nature structural & molecular biology 2012 IMEx BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. mdm2_human E3 ubiquitin-protein ligase Mdm2 MDM2 p53-binding protein Mdm2 Oncoprotein Mdm2 Double minute 2 protein RING-type E3 ubiquitin transferase Mdm2 protein protein human Homo sapiens Human MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP DIP protein Q00987 original sequence version: 93 DIP protein Q00987-1 original sequence version: 192 DIP protein Q00987 original sequence version: 88 DIP protein Q00987 original sequence version: 180 DIP protein Q00987 original sequence version: 188 DIP protein Q00987 original sequence version: 189 DIP protein Q00987 original sequence version: 115 DIP protein Q00987-1 original sequence version: null DIP protein Q00987 original sequence version: 149 DIP protein Q00987 original sequence version: 146 DIP protein Q00987 original sequence version: 140 DIP protein Q00987 original sequence version: 183 DIP protein Q00987 original sequence version: 145 DIP protein Q00987 original sequence version: 182 DIP protein Q00987 original sequence version: 151 DIP protein Q00987 original sequence version: 156 DIP protein Q00987-1 original sequence version: 160 DIP protein Q00987 original sequence version: 160 DIP protein Q00987 original sequence version: 168 DIP protein Q00987 original sequence version: 186 DIP protein Q00987 original sequence version: 206 F37CE163876BC983 bmi1_human Polycomb complex protein BMI-1 BMI1 PCGF4 RNF51 Polycomb group RING finger protein 4 RING finger protein 51 protein protein human Homo sapiens Human MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEDKRIITDDEIISLSIEFFDQNRLDRKVNKDKEKSKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKISHQRDGLTNAGELESDSGSDKANSPAGGIPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSGNHQSSFANRPRKSSVNGSSATSSG DIP protein P35226 original sequence version: 105 DIP protein P35226 original sequence version: 136 DIP protein P35226 original sequence version: 110 DIP protein P35226 original sequence version: 129 030A7D396BADA543 birc3_human Baculoviral IAP repeat-containing protein 3 Inhibitor of apoptosis protein 1 TNFR2-TRAF-signaling complex protein 1 IAP homolog C Apoptosis inhibitor 2 RING finger protein 49 BIRC3 API2 MIHC RNF49 RING-type E3 ubiquitin transferase BIRC3 Cellular inhibitor of apoptosis 2 protein protein human Homo sapiens Human MNIVENSIFLSNLMKSANTFELKYDLSCELYRMSTYSTFPAGVPVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKRGDSPTEKHKKLYPSCRFVQSLNSVNNLEATSQPTFPSSVTNSTHSLLPGTENSGYFRGSYSNSPSNPVNSRANQDFSALMRSSYHCAMNNENARLLTFQTWPLTFLSPTDLAKAGFYYIGPGDRVACFACGGKLSNWEPKDNAMSEHLRHFPKCPFIENQLQDTSRYTVSNLSMQTHAARFKTFFNWPSSVLVNPEQLASAGFYYVGNSDDVKCFCCDGGLRCWESGDDPWVQHAKWFPRCEYLIRIKGQEFIRQVQASYPHLLEQLLSTSDSPGDENAESSIIHFEPGEDHSEDAIMMNTPVINAAVEMGFSRSLVKQTVQRKILATGENYRLVNDLVLDLLNAEDEIREEERERATEEKESNDLLLIRKNRMALFQHLTCVIPILDSLLTAGIINEQEHDVIKQKTQTSLQARELIDTILVKGNIAATVFRNSLQEAEAVLYEHLFVQQDIKYIPTEDVSDLPVEEQLRRLQEERTCKVCMDKEVSIVFIPCGHLVVCKDCAPSLRKCPICRSTIKGTVRTFLS DIP protein Q13489 original sequence version: 127 8581A00BA9AAB4A7 ubiq_human UBIQ_HUMAN protein protein human Homo sapiens Human MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG ub2d2_human Ubiquitin-conjugating enzyme E2 D2 UBC5B UBCH4 UBE2D2 UBC4 UBCH5B Ubiquitin-protein ligase D2 Ubiquitin carrier protein D2 Ubiquitin-conjugating enzyme E2-17 kDa 2 Ubiquitin-conjugating enzyme E2(17)KB 2 PUBC1 p53-regulated ubiquitin-conjugating enzyme 1 (E3-independent) E2 ubiquitin-conjugating enzyme D2 E2 ubiquitin-conjugating enzyme D2 protein protein human Homo sapiens Human MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDREKYNRIAREWTQKYAM DIP protein P62837 original sequence version: 81 DIP protein P62837-1 original sequence version: 134 DIP protein P62837 original sequence version: 95 DIP protein P62837 original sequence version: 139 DIP protein P62837 original sequence version: 37 DIP protein P62837 original sequence version: 115 DIP protein P62837 original sequence version: 58 DIP protein P62837 original sequence version: 74 DIP protein P62837 original sequence version: 103 DIP protein P62837 original sequence version: 101 C942BE7853CBC355 ring2_human E3 ubiquitin-protein ligase RING2 RING finger protein 2 RING finger protein 1B RING finger protein BAP-1 Protein DinG Huntingtin-interacting protein 2-interacting protein 3 RNF2 BAP1 DING HIPI3 RING1B RING-type E3 ubiquitin transferase RING2 protein protein human Homo sapiens Human MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARINKHNNQQALSHSIEEGLKIQAMNRLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAMAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVLNGSFSLELVSEKYWKVNKPMELYYAPTKEHK DIP protein Q99496 original sequence version: 95 DIP protein Q99496 original sequence version: 94 DIP protein Q99496 original sequence version: 96 DIP protein Q99496 original sequence version: 125 DIP protein Q99496 original sequence version: 142 DIP protein Q99496 original sequence version: 159 DIP protein Q99496 original sequence version: 129 DIP protein Q99496 original sequence version: 99 DIP protein Q99496 original sequence version: 118 90EA546E1F4DB7EC q96ca5-1 Baculoviral IAP repeat-containing protein 7 BIRC7 KIAP LIVIN MLIAP RNF50 UNQ5800/PRO19607/PRO21344 Livin alpha Kidney inhibitor of apoptosis protein Livin Melanoma inhibitor of apoptosis protein RING finger protein 50 RING-type E3 ubiquitin transferase BIRC7 protein protein human Homo sapiens Human MGPKDSAKCLHRGPQPSHWAAGDGPTQERCGPRSLGSPVLGLDTCRAWDHVDGQILGQLRPLTEEEEEEGAGATLSRGPAFPGMGSEELRLASFYDWPLTAEVPPELLAAAGFFHTGHQDKVRCFFCYGGLQSWKRGDDPWTEHAKWFPSCQFLLRSKGRDFVHSVQETHSQLLGSWDPWEEPEDAAPVAPSVPASGYPELPTPRREVQSESAQEPGGVSPAEAQRAWWVLEPPGARDVEAQLRRLQEERTCKVCLDRAVSIVFVPCGHLVCAECAPGLQLCPICRAPVRSRVRTFLS DIP protein Q96CA5-1 original sequence version: 116 mdm4_human Protein Mdm4 MDM4 MDMX p53-binding protein Mdm4 Mdm2-like p53-binding protein Protein Mdmx Double minute 4 protein protein protein human Homo sapiens Human MTSFSTSAQCSTSDSACRISPGQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGELLGRQSFSVKDPSPLYDMLRKNLVTLATATTDAAQTLALAQDHSMDIPSQDQLKQSAEESSTSRKRTTEDDIPTLPTSEHKCIHSREDEDLIENLAQDETSRLDLGFEEWDVAGLPWWFLGNLRSNYTPRSNGSTDLQTNQDVGTAIVSDTTDDLWFLNESVSEQLGVGIKVEAADTEQTSEEVGKVSDKKVIEVGKNDDLEDSKSLSDDTDVEVTSEDEWQCTECKKFNSPSKRYCFRCWALRKDWYSDCSKLTHSLSTSDITAIPEKENEGNDVPDCRRTISAPVVRPKDAYIKKENSKLFDPCNSVEFLDLAHSSESQETISSMGEQLDNLSEQRTDTENMEDCQNLLKPCSLCEKRPRDGNIIHGRTGHLVTCFHCARRLKKAGASCPICKKEIQLVIKVFIA DIP protein O15151 original sequence version: 141 DIP protein O15151 original sequence version: 109 DIP protein O15151 original sequence version: 129 DIP protein O15151 original sequence version: 147 415E6FA5A0C69857 birc3-ub-1 2 20 unspecified role unspecified role prey prey ecolx Escherichia coli 21 unspecified role unspecified role prey prey P62837:p.Cys85Ser C85S mutation mutation certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C85S'. Wed May 02 17:44:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys85ser' Tue Jun 30 18:18:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys85Ser' ecolx Escherichia coli 19 unspecified role unspecified role bait bait Region 541-604 Region 541-604 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli association association mdm2-mdm4-10 4 24 unspecified role unspecified role prey prey Region 428-490 Region 428-490 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 17 unspecified role unspecified role bait bait Region 428-491 Region 428-491 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 physical association physical association birc7-ub-1 13 23 unspecified role unspecified role unspecified role unspecified role Region 239-298 Region 239-298 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 20 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 21 unspecified role unspecified role unspecified role unspecified role P62837:p.[Ser22Arg;Asn77Ala;Cys85Ser] C85S/S22R/N77A mutation mutation certain certain sequence position certain certain certain sequence position certain C S certain certain sequence position certain certain certain sequence position certain N A certain certain sequence position certain certain certain sequence position certain S R Wed May 02 16:05:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser22arg,asn77ala,cys85ser' Tue Jun 30 16:34:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ser22Arg;Asn77Ala;Cys85Ser]' ecolx Escherichia coli physical association physical association birc7-ub-2 14 23 unspecified role unspecified role bait bait ecolx Escherichia coli 20 unspecified role unspecified role prey prey ecolx Escherichia coli 21 unspecified role unspecified role prey prey P62837:p.Cys85Ser C85S mutation mutation certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C85S'. Wed May 02 15:44:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys85ser' Tue Jun 30 18:52:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys85Ser' P62837:p.Ile88Ala I88A 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 'I88A'. Wed May 02 19:03:23 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile88ala' Tue Jun 30 16:31:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile88Ala' P62837:p.Ser108Arg S108R 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 S R This feature has been corrected as a result of our quality control procedures. The original label was 'S108R'. Wed May 02 19:04:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser108arg' Tue Jun 30 17:56:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser108Arg' ecolx Escherichia coli association association birc7-ub-3 12 23 unspecified role unspecified role bait bait ecolx Escherichia coli 20 unspecified role unspecified role prey prey L8D L8D 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 G35E G35E 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 I36A I36A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain I44A I44A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 21 unspecified role unspecified role prey prey P62837:p.Cys85Ser C85S mutation mutation certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C85S'. Wed May 02 16:28:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys85ser' Tue Jun 30 19:54:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys85Ser' ecolx Escherichia coli association association mdm4-mdm2-3 8 24 unspecified role unspecified role bait bait Region 428-490 Region 428-490 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 17 unspecified role unspecified role prey prey Region 428-491 Region 428-491 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 physical association physical association ub-ube2d2-6 9 20 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 21 unspecified role unspecified role unspecified role unspecified role P62837:p.Cys85Ser C85S mutation mutation certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C85S'. Wed May 02 16:59:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys85ser' Tue Jun 30 17:57:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys85Ser' ecolx Escherichia coli direct interaction direct interaction birc7-ub-4 1 23 unspecified role unspecified role unspecified role unspecified role Region 239-298 Region 239-298 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 20 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 21 unspecified role unspecified role unspecified role unspecified role P62837:p.[Ser22Arg;Asn77Ala;Cys85Ser] C85S/S22R/N77A mutation mutation certain certain sequence position certain certain certain sequence position certain C S certain certain sequence position certain certain certain sequence position certain N A certain certain sequence position certain certain certain sequence position certain S R Wed May 02 15:41:18 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser22arg,asn77ala,cys85ser' Tue Jun 30 18:48:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ser22Arg;Asn77Ala;Cys85Ser]' ecolx Escherichia coli direct interaction direct interaction ub-ube2d2-7 11 20 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 21 unspecified role unspecified role unspecified role unspecified role P62837:p.Cys85Ser C85S mutation mutation certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C85S'. Wed May 02 18:15:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys85ser' Tue Jun 30 16:57:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys85Ser' ecolx Escherichia coli direct interaction direct interaction rnf2-bmi1-5 7 18 unspecified role unspecified role prey prey Region 1-109 Region 1-109 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 22 unspecified role unspecified role bait bait Region 1-114 Region 1-114 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 physical association physical association ub-ube2d2-8 5 20 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 21 unspecified role unspecified role unspecified role unspecified role P62837:p.[Ser22Arg;Asn77Arg;Cys85Ser] C85S/S22R/N77R mutation mutation certain certain sequence position certain certain certain sequence position certain C S certain certain sequence position certain certain certain sequence position certain N R certain certain sequence position certain certain certain sequence position certain S R Fri Jul 28 10:52:48 BST 2017 This feature has been corrected as a result of our quality control procedures. The original label was 'ser22arg,asn77ala,cys85ser' Wed May 02 15:18:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser22arg,asn77arg,cys85ser' Tue Jun 30 19:22:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ser22Arg;Asn77Arg;Cys85Ser]' ecolx Escherichia coli direct interaction direct interaction birc7-ub-5 16 23 unspecified role unspecified role bait bait Region 239-298 Region 239-298 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q96CA5-1:p.Val263Arg V263R 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 'V263R'. Wed May 02 17:59:44 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val263arg' Tue Jun 30 19:45:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val263Arg' Q96CA5-1:p.Phe296_Ser298del Δ296-298 mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain FLS ... Wed May 02 19:18:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe_leu_ser296-298del_del_del' Tue Jun 30 17:26:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe296_Ser298del' Q96CA5-1:p.Val254Ala V254A mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain V A This feature has been corrected as a result of our quality control procedures. The original label was 'V254A'. Wed May 02 17:12:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val254ala' Tue Jun 30 19:02:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val254Ala' Q96CA5-1:p.Ile284Ala I284A 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 'I284A'. Wed May 02 19:49:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile284ala' Tue Jun 30 16:02:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile284Ala' Q96CA5-1:p.Arg286Ala R286A 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 This feature has been corrected as a result of our quality control procedures. The original label was 'R286A'. Wed May 02 15:02:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg286ala' Tue Jun 30 17:11:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg286Ala' Q96CA5-1:p.Phe296His F296H 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 F H This feature has been corrected as a result of our quality control procedures. The original label was 'F296H'. Wed May 02 17:13:23 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe296his' Tue Jun 30 17:13:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe296His' ecolx Escherichia coli 20 unspecified role unspecified role prey prey ecolx Escherichia coli 21 unspecified role unspecified role prey prey P62837:p.Cys85Ser C85S mutation mutation certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C85S'. Wed May 02 16:26:39 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys85ser' Tue Jun 30 17:37:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys85Ser' ecolx Escherichia coli association association birc3-ube2d2-1 10 21 unspecified role unspecified role prey prey ecolx Escherichia coli 19 unspecified role unspecified role bait bait Region 541-604 Region 541-604 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 birc7-1 3 23 unspecified role unspecified role unspecified role unspecified role Q96CA5-1:p.Val263Arg V263R 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 'V263R'. Wed May 02 19:23:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val263arg' Tue Jun 30 18:28:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val263Arg' Q96CA5-1:p.Phe296_Ser298del Δ296-298 mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain FLS ... Wed Aug 02 13:51:00 BST 2017 This feature has been corrected as a result of our quality control procedures. The original label was 'phe_lys_ser296-298del_del_del' Wed May 02 17:15:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe_leu_ser296-298del_del_del' Tue Jun 30 19:40:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe296_Ser298del' ecolx Escherichia coli direct interaction direct interaction ub-ube2d2-9 6 20 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 21 unspecified role unspecified role unspecified role unspecified role P62837:p.Cys85Ser C85S mutation mutation certain certain sequence position certain certain certain sequence position certain C S This feature has been corrected as a result of our quality control procedures. The original label was 'C85S'. Wed May 02 19:12:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys85ser' Tue Jun 30 20:06:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys85Ser' ecolx Escherichia coli direct interaction direct interaction bmi1-rnf2-9 15 18 unspecified role unspecified role bait bait Region 1-109 Region 1-109 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 22 unspecified role unspecified role prey prey Region 1-114 Region 1-114 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 physical association physical association