MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex. Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex. EMBO J. (0261-4189) 2011 imex curation Bentley ML., Corn JE., Dong KC., Phung Q., Cheung TK., Cochran AG. 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 Bentley ML., Corn JE., Dong KC., Phung Q., Cheung TK., Cochran AG. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex. Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex. EMBO J. (0261-4189) 2011 imex curation Bentley ML., Corn JE., Dong KC., Phung Q., Cheung TK., Cochran AG. 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 Bentley ML., Corn JE., Dong KC., Phung Q., Cheung TK., Cochran AG. EMBO J. (0261-4189) 2011 Only protein-protein interactions imex curation 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 ub2d3_human Ubiquitin-conjugating enzyme E2 D3 UBC5C Ubiquitin-protein ligase D3 Ubiquitin carrier protein D3 Ubiquitin-conjugating enzyme E2-17 kDa 3 Ubiquitin-conjugating enzyme E2(17)KB 3 UBE2D3 UBCH5C (E3-independent) E2 ubiquitin-conjugating enzyme D3 E2 ubiquitin-conjugating enzyme D3 protein protein human Homo sapiens Human MALKRINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDRDKYNRISREWTQKYAM ADD74A8A708EFEE3 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 bmi1-rnf2-4 1 UbcH5c 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Ring1b 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Bmi1 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association homomint mint f1 t1 f7a bmi1-rnf2-5 2 Bmi1 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 1.1 Ring1b 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Stoichiometry: 1.1 direct interaction direct interaction sf6 homomint mint All mutants were co-expressed in Escherichia coli with the wild-type (wt) partner, and, like the wt RING domains, formed stable 1:1 Bmi1/Ring1b heterodimers as assessed by gel filtration (Supplementary Figure S6).