DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli lambda two hybrid lambda repressor two hybrid BacterioMatch BacterioMatch lambda two hybrid predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252231X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli lambda two hybrid lambda repressor two hybrid BacterioMatch BacterioMatch lambda two hybrid predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252236X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli ion exchange chrom ion exchange chromatography IEC IEC ion exchange chrom predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252222X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli lambda two hybrid lambda repressor two hybrid BacterioMatch BacterioMatch lambda two hybrid predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252233X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252229X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. 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 Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252227X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. 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 Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252223X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli lambda two hybrid lambda repressor two hybrid BacterioMatch BacterioMatch lambda two hybrid predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252238X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252230X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252228X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli lambda two hybrid lambda repressor two hybrid BacterioMatch BacterioMatch lambda two hybrid predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252234X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli lambda two hybrid lambda repressor two hybrid BacterioMatch BacterioMatch lambda two hybrid predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252237X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252225X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli lambda two hybrid lambda repressor two hybrid BacterioMatch BacterioMatch lambda two hybrid predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252235X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252224X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli ion exchange chrom ion exchange chromatography IEC IEC ion exchange chrom predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252226X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli lambda two hybrid lambda repressor two hybrid BacterioMatch BacterioMatch lambda two hybrid predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252232X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. Structure (London, England : 1993) 2013 imex curation Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Junco SE., Wang R., Gaipa JC., Taylor AB., Schirf V., Gearhart MD., Bardwell VJ., Demeler B., Hart PJ., Kim CA. DIP original experiment: DIP-252221X Structure (London, England : 1993) 2013 IMEx Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs. q6w2j9-1 BCL-6 corepressor BCOR KIAA1575 Long protein protein human Homo sapiens Human MLSATPLYGNVHSWMNSERVRMCGASEDRKILVNDGDASKARLELREENPLNHNVVDASTAHRIDGLAALSMDRTGLIREGLRVPGNIVYSSLCGLGSEKGREAATSTLGGLGFSSERNPEMQFKPNTPETVEASAVSGKPPNGFSAIYKTPPGIQKSAVATAEALGLDRPASDKQSPLNINGASYLRLPWVNPYMEGATPAIYPFLDSPNKYSLNMYKALLPQQSYSLAQPLYSPVCTNGERFLYLPPPHYVGPHIPSSLASPMRLSTPSASPAIPPLVHCADKSLPWKMGVSPGNPVDSHAYPHIQNSKQPRVPSAKAVTSGLPGDTALLLPPSPRPSPRVHLPTQPAADTYSEFHKHYARISTSPSVALSKPYMTVSSEFPAARLSNGKYPKAPEGGEGAQPVPGHARKTAVQDRKDGSSPPLLEKQTVTKDVTDKPLDLSSKVVDVDASKADHMKKMAPTVLVHSRAGSGLVLSGSEIPKETLSPPGNGCAIYRSEIISTAPSSWVVPGPSPNEENNGKSMSLKNKALDWAIPQQRSSSCPRMGGTDAVITNVSGSVSSAGRPASASPAPNANADGTKTSRSSVETTPSVIQHVGQPPATPAKHSSSTSSKGAKASNPEPSFKANENGLPPSSIFLSPNEAFRSPPIPYPRSYLPYPAPEGIAVSPLSLHGKGPVYPHPVLLPNGSLFPGHLAPKPGLPYGLPTGRPEFVTYQDALGLGMVHPMLIPHTPIEITKEEKPERRSRSHERARYEDPTLRNRFSEILETSSTKLHPDVPTDKNLKPNPNWNQGKTVVKSDKLVYVDLLREEPDAKTDTNVSKPSFAAESVGQSAEPPKPSVEPALQQHRDFIALREELGRISDFHETYTFKQPVFTVSKDSVLAGTNKENLGLPVSTPFLEPPLGSDGPAVTFGKTQEDPKPFCVGSAPPSVDVTPTYTKDGADEAESNDGKVLKPKPSKLAKRIANSAGYVGDRFKCVTTELYADSSQLSREQRALQMEGLQEDSILCLPAAYCERAMMRFSELEMKEREGGHPATKDSEMCKFSPADWERLKGNQDKKPKSVTLEEAIAEQNESERCEYSVGNKHRDPFEAPEDKDLPVEKYFVERQPVSEPPADQVASDMPHSPTLRVDRKRKVSGDSSHTETTAEEVPEDPLLKAKRRRVSKDDWPEREMTNSSSNHLEDPHYSELTNLKVCIELTGLHPKKQRHLLHLRERWEQQVSAADGKPGRQSRKEVTQATQPEAIPQGTNITEEKPGRKRAEAKGNRSWSEESLKPSDNEQGLPVFSGSPPMKSLSSTSAGGKKQAQPSCAPASRPPAKQQKIKENQKTDVLCADEEEDCQAASLLQKYTDNSEKPSGKRLCKTKHLIPQESRRGLPLTGEYYVENADGKVTVRRFRKRPEPSSDYDLSPAKQEPKPFDRLQQLLPASQSTQLPCSSSPQETTQSRPMPPEARRLIVNKNAGETLLQRAARLGYEEVVLYCLENKICDVNHRDNAGYCALHEACARGWLNIVRHLLEYGADVNCSAQDGTRPLHDAVENDHLEIVRLLLSYGADPTLATYSGRTIMKMTHSELMEKFLTDYLNDLQGRNDDDASGTWDFYGSSVCEPDDESGYDVLANPPGPEDQDDDDDAYSDVFEFEFSETPLLPCYNIQVSVAQGPRNWLLLSDVLKKLKMSSRIFRCNFPNVEIVTIAEAEFYRQVSASLLFSCSKDLEAFNPESKELLDLVEFTNEIQTLLGSSVEWLHPSDLASDNYW DIP protein Q6W2J9-1 original sequence version: 97 DIP protein Q6W2J9-1 original sequence version: 95 pcgf2_human Polycomb group RING finger protein 2 PCGF2 MEL18 RNF110 ZNF144 DNA-binding protein Mel-18 RING finger protein 110 Zinc finger protein 144 protein protein human Homo sapiens Human MHRTTRIKITELNPHLMCALCGGYFIDATTIVECLHSFCKTCIVRYLETNKYCPMCDVQVHKTRPLLSIRSDKTLQDIVYKLVPGLFKDEMKRRRDFYAAYPLTEVPNGSNEDRGEVLEQEKGALSDDEIVSLSIEFYEGARDRDEKKGPLENGDGDKEKTGVRFLRCPAAMTVMHLAKFLRNKMDVPSKYKVEVLYEDEPLKEYYTLMDIAYIYPWRRNGPLPLKYRVQPACKRLTLATVPTPSEGTNTSGASECESVSDKAPSPATLPATSSSLPSPATPSHGSPSSHGPPATHPTSPTPPSTASGATTAANGGSLNCLQTPSSTSRGRKMTVNGAPVPPLT DIP protein P35227 original sequence version: 96 DIP protein P35227 original sequence version: 124 A910BCD4C0CE9927 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 phc1_human Polyhomeotic-like protein 1 Early development regulatory protein 1 PHC1 EDR1 PH1 protein protein human Homo sapiens Human METESEQNSNSTNGSSSSGGSSRPQIAQMSLYERQAVQALQALQRQPNAAQYFHQFMLQQQLSNAQLHSLAAVQQATIAASRQASSPNTSTTQQQTTTTQASINLATTSAAQLISRSQSVSSPSATTLTQSVLLGNTTSPPLNQSQAQMYLRPQLGNLLQVNRTLGRNVPLASQLILMPNGAVAAVQQEVPSAQSPGVHADADQVQNLAVRNQQASAQGPQMQGSTQKAIPPGASPVSSLSQASSQALAVAQASSGATNQSLNLSQAGGGSGNSIPGSMGPGGGGQAHGGLGQLPSSGMGGGSCPRKGTGVVQPLPAAQTVTVSQGSQTEAESAAAKKAEADGSGQQNVGMNLTRTATPAPSQTLISSATYTQIQPHSLIQQQQQIHLQQKQVVIQQQIAIHHQQQFQHRQSQLLHTATHLQLAQQQQQQQQQQQQQQQPQATTLTAPQPPQVPPTQQVPPSQSQQQAQTLVVQPMLQSSPLSLPPDAAPKPPIPIQSKPPVAPIKPPQLGAAKMSAAQQPPPHIPVQVVGTRQPGTAQAQALGLAQLAAAVPTSRGMPGTVQSGQAHLASSPPSSQAPGALQECPPTLAPGMTLAPVQGTAHVVKGGATTSSPVVAQVPAAFYMQSVHLPGKPQTLAVKRKADSEEERDDVSTLGSMLPAKASPVAESPKVMDEKSSLGEKAESVANVNANTPSSELVALTPAPSVPPPTLAMVSRQMGDSKPPQAIVKPQILTHIIEGFVIQEGAEPFPVGCSQLLKESEKPLQTGLPTGLTENQSGGPLGVDSPSAELDKKANLLKCEYCGKYAPAEQFRGSKRFCSMTCAKRYNVSCSHQFRLKRKKMKEFQEANYARVRRRGPRRSSSDIARAKIQGKCHRGQEDSSRGSDNSSYDEALSPTSPGPLSVRAGHGERDLGNPNTAPPTPELHGINPVFLSSNPSRWSVEEVYEFIASLQGCQEIAEEFRSQEIDGQALLLLKEEHLMSAMNIKLGPALKICAKINVLKET DIP protein P78364 original sequence version: 122 D53764F80931A938 q9bsm1-1 Polycomb group RING finger protein 1 PCGF1 NSPC1 RNF68 Nervous system Polycomb-1 RING finger protein 68 protein protein human Homo sapiens Human MASPQGGQIAIAMRLRNQLQSVYKMDPLRNEEEVRVKIKDLNEHIVCCLCAGYFVDATTITECLHTFCKSCIVKYLQTSKYCPMCNIKIHETQPLLNLKLDRVMQDIVYKLVPGLQDSEEKRIREFYQSRGLDRVTQPTGEEPALSNLGLPFSSFDHSKAHYYRYDEQLNLCLERLSSGKDKNKSVLQNKYVRCSVRAEVRHLRRVLCHRLMLNPQHVQLLFDNEVLPDHMTMKQIWLSRWFGKPSPLLLQYSVKEKRR DIP protein Q9BSM1-1 original sequence version: 90 q3knv8-1 Polycomb group RING finger protein 3 PCGF3 RNF3 RNF3A RING finger protein 3A protein protein human Homo sapiens Human MLTRKIKLWDINAHITCRLCSGYLIDATTVTECLHTFCRSCLVKYLEENNTCPTCRIVIHQSHPLQYIGHDRTMQDIVYKLVPGLQEAEMRKQREFYHKLGMEVPGDIKGETCSAKQHLDSHRNGETKADDSSNKEAAEEKPEEDNDYHRSDEQVSICLECNSSKLRGLKRKWIRCSAQATVLHLKKFIAKKLNLSSFNELDILCNEEILGKDHTLKFVVVTRWRFKKAPLLLHYRPKMDLL DIP protein Q3KNV8-1 original sequence version: 69 DIP protein Q3KNV8 original sequence version: 84 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 cbx7_human Chromobox protein homolog 7 CBX7 protein protein human Homo sapiens Human MELSAIGEQVFAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHILDPRLVMAYEEKEERDRASGYRKRGPKPKRLLLQRLYSMDLRSSHKAKGKEKLCFSLTCPLGSGSPEGVVKAGAPELVDKGPLVPTLPFPLRKPRKAHKYLRLSRKKFPPRGPNLESHSHRRELFLQEPPAPDVLQAAGEWEPAAQPPEEEADADLAEGPPPWTPALPSSEVTVTDITANSITVTFREAQAAEGFFRDRSGKF DIP protein O95931 original sequence version: 81 DIP protein O95931 original sequence version: 82 DIP protein O95931 original sequence version: 108 A90019C1D08812B8 q5h9f3-1 BCL-6 corepressor-like protein 1 BCORL1 protein protein human Homo sapiens Human MISTAPLYSGVHNWTSSDRIRMCGINEERRAPLSDEESTTGDCQHFGSQEFCVSSSFSKVELTAVGSGSNARGADPDGSATEKLGHKSEDKPDDPQPKMDYAGNVAEAEGFLVPLSSPGDGLKLPASDSAEASNSRADCSWTPLNTQMSKQVDCSPAGVKALDSRQGVGEKNTFILATLGTGVPVEGTLPLVTTNFSPLPAPICPPAPGSASVPHSVPDAFQVPLSVPAPVPHSGLVPVQVATSVPAPSPPLAPVPALAPAPPSVPTLISDSNPLSVSASVLVPVPASAPPSGPVPLSAPAPAPLSVPVSAPPLALIQAPVPPSAPTLVLAPVPTPVLAPMPASTPPAAPAPPSVPMPTPTPSSGPPSTPTLIPAFAPTPVPAPTPAPIFTPAPTPMPAATPAAIPTSAPIPASFSLSRVCFPAAQAPAMQKVPLSFQPGTVLTPSQPLVYIPPPSCGQPLSVATLPTTLGVSSTLTLPVLPSYLQDRCLPGVLASPELRSYPYAFSVARPLTSDSKLVSLEVNRLPCTSPSGSTTTQPAPDGVPGPLADTSLVTASAKVLPTPQPLLPAPSGSSAPPHPAKMPSGTEQQTEGTSVTFSPLKSPPQLEREMASPPECSEMPLDLSSKSNRQKLPLPNQRKTPPMPVLTPVHTSSKALLSTVLSRSQRTTQAAGGNVTSCLGSTSSPFVIFPEIVRNGDPSTWVKNSTALISTIPGTYVGVANPVPASLLLNKDPNLGLNRDPRHLPKQEPISIIDQGEPKGTGATCGKKGSQAGAEGQPSTVKRYTPARIAPGLPGCQTKELSLWKPTGPANIYPRCSVNGKPTSTQVLPVGWSPYHQASLLSIGISSAGQLTPSQGAPIRPTSVVSEFSGVPSLSSSEAVHGLPEGQPRPGGSFVPEQDPVTKNKTCRIAAKPYEEQVNPVLLTLSPQTGTLALSVQPSGGDIRMNQGPEESESHLCSDSTPKMEGPQGACGLKLAGDTKPKNQVLATYMSHELVLATPQNLPKMPELPLLPHDSHPKELILDVVPSSRRGSSTERPQLGSQVDLGRVKMEKVDGDVVFNLATCFRADGLPVAPQRGQAEVRAKAGQARVKQESVGVFACKNKWQPDDVTESLPPKKMKCGKEKDSEEQQLQPQAKAVVRSSHRPKCRKLPSDPQESTKKSPRGASDSGKEHNGVRGKHKHRKPTKPESQSPGKRADSHEEGSLEKKAKSSFRDFIPVVLSTRTRSQSGSICSSFAGMADSDMGSQEVFPTEEEEEVTPTPAKRRKVRKTQRDTQYRSHHAQDKSLLSQGRRHLWRAREMPWRTEAARQMWDTNEEEEEEEEEGLLKRKKRRRQKSRKYQTGEYLTEQEDEQRRKGRADLKARKQKTSSSQSLEHRLRNRNLLLPNKVQGISDSPNGFLPNNLEEPACLENSEKPSGKRKCKTKHMATVSEEAKDVVLYCLQKDSEDVNHRDNAGYTALHEACSRGWTDILNILLEHGANVNCSAQDGTRPVHDAVVNDNLETIWLLLSYGADPTLATYSGQTAMKLASSDTMKRFLSDHLSDLQGRAEGDPGVSWDFYSSSVLEEKDGFACDLLHNPPGSSDQEGDDPMEEDDFMFELSDKPLLPCYNLQVSVSRGPCNWFLFSDVLKRLKLSSRIFQARFPHFEITTMPKAEFYRQVASSQLLTPAERPGGLDDRSPPGSSETVELVRYEPDLLRLLGSEVEFQSCNS DIP protein Q5H9F3-1 original sequence version: 79 bcorl1-pcgf3-1 4 24 unspecified role unspecified role prey prey Region 152-242 Region 152-242 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 27 unspecified role unspecified role bait bait Region 1594-1711 Region 1594-1711 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association pcgf1-bcorl1-1 13 27 unspecified role unspecified role prey prey Region 1594-1711 Region 1594-1711 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role bait bait Region 167-255 Region 167-255 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 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli physical association physical association pcgf1-bcor-7 18 19 unspecified role unspecified role prey prey Region 1634-1748 Region 1634-1748 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role bait bait Region 167-255 Region 167-255 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 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli physical association physical association bcor-pcgf1-5 12 19 unspecified role unspecified role bait bait Region 1634-1748 Region 1634-1748 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role prey prey Region 167-255 Region 167-255 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9BSM1-1:p.Tyr191Ala Y191A mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y191A'. Wed May 02 15:10:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr191ala' Tue Jun 30 16:17:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr191Ala' Q9BSM1-1:p.Arg193Ala R193A mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate 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 'R193A'. Wed May 02 14:57:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg193ala' Tue Jun 30 16:38:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg193Ala' Q9BSM1-1:p.Val206Asp V206D mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain V D This feature has been corrected as a result of our quality control procedures. The original label was 'V206D'. Wed May 02 15:03:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val206asp' Tue Jun 30 18:12:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val206Asp' ecolx Escherichia coli physical association physical association bcor-pcgf1-6 5 19 unspecified role unspecified role unspecified role unspecified role Region 1634-1748 Region 1634-1748 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role Region 167-255 Region 167-255 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 phc1-pcgf2-3 2 20 unspecified role unspecified role prey prey Region 121-229 Region 121-229 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P35227:p.Phe165Ala F165A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A This feature has been corrected as a result of our quality control procedures. The original label was 'F165A'. Wed May 02 18:03:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe165ala' Tue Jun 30 17:50:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe165Ala' P35227:p.Arg164Ala R163A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain R A Wed May 02 15:56:44 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg164ala' Tue Jun 30 18:43:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg164Ala' P35227:p.Phe180Asp F180D mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain F D This feature has been corrected as a result of our quality control procedures. The original label was 'F180D'. Wed May 02 16:25:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe180asp' Tue Jun 30 18:51:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe180Asp' ecolx Escherichia coli 22 unspecified role unspecified role bait bait Region 720-760 Region 720-760 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association bcor-pcgf3-1 11 19 unspecified role unspecified role bait bait Region 1634-1748 Region 1634-1748 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 24 unspecified role unspecified role prey prey Region 152-242 Region 152-242 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association bcorl1-pcgf1-1 16 27 unspecified role unspecified role unspecified role unspecified role Region 1594-1711 Region 1594-1711 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role Region 167-255 Region 167-255 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 bcor-pcgf1-7 3 19 unspecified role unspecified role unspecified role unspecified role Region 1634-1748 Region 1634-1748 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role Region 167-255 Region 167-255 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 bcorl1-pcgf1-2 9 27 unspecified role unspecified role unspecified role unspecified role Region 1594-1711 Region 1594-1711 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role Region 167-255 Region 167-255 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 bcorl1-pcgf1-3 6 27 unspecified role unspecified role unspecified role unspecified role Region 1594-1711 Region 1594-1711 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role Region 167-255 Region 167-255 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 phc1-bmi1-1 14 21 unspecified role unspecified role prey prey Region 127-228 Region 127-228 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P35226:p.Tyr163Ala Y163A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y163A'. Wed May 02 17:02:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr163ala' Tue Jun 30 19:24:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr163Ala' P35226:p.Arg165Ala R165A mutation decreasing strength mutation decreasing interaction strength mutation decreasing 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 'R165A'. Wed May 02 19:58:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg165ala' Tue Jun 30 18:55:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg165Ala' P35226:p.Phe178Asp F178D mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain F D This feature has been corrected as a result of our quality control procedures. The original label was 'F178D'. Wed May 02 19:33:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe178asp' Tue Jun 30 20:05:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe178Asp' ecolx Escherichia coli 22 unspecified role unspecified role bait bait Region 720-760 Region 720-760 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association bcor-pcgf1-8 7 19 unspecified role unspecified role unspecified role unspecified role Region 1634-1748 Region 1634-1748 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role Region 167-255 Region 167-255 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 bcor-pcgf1-9 1 19 unspecified role unspecified role bait bait Region 1634-1748 Region 1634-1748 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 23 unspecified role unspecified role prey prey Region 167-255 Region 167-255 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association bcorl1-pcgf1-4 10 27 unspecified role unspecified role unspecified role unspecified role Region 1594-1711 Region 1594-1711 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role Region 167-255 Region 167-255 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 bcor-pcgf1-10 15 19 unspecified role unspecified role unspecified role unspecified role Region 1634-1748 Region 1634-1748 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role unspecified role unspecified role Region 167-255 Region 167-255 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 bcorl1-pcgf1-5 17 27 unspecified role unspecified role bait bait Region 1594-1711 Region 1594-1711 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 23 unspecified role unspecified role prey prey Region 167-255 Region 167-255 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q9BSM1-1:p.Tyr191Ala Y191A mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Y A This feature has been corrected as a result of our quality control procedures. The original label was 'Y191A'. Wed May 02 19:34:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr191ala' Tue Jun 30 17:15:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr191Ala' Q9BSM1-1:p.Arg193Ala R193A mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate 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 'R193A'. Wed May 02 18:28:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg193ala' Tue Jun 30 18:09:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg193Ala' Q9BSM1-1:p.Val206Asp V206D mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain V D This feature has been corrected as a result of our quality control procedures. The original label was 'V206D'. Wed May 02 17:08:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val206asp' Tue Jun 30 18:26:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val206Asp' ecolx Escherichia coli physical association physical association cbx7-rnf2-10 8 26 unspecified role unspecified role bait bait Region 211-251 Region 211-251 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 25 unspecified role unspecified role prey prey Region 222-336 Region 222-336 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association