IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Cell (0092-8674) 2010 imex curation Wang Z., Song J., Milne TA., Wang GG., Li H., Allis CD., Patel DJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Chromatin - Epigenetic interactions resulting in chromatin modulation pateld@mskcc.org 21-Dec-2010: Contacted by JYOTI. jyoti Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Wang Z., Song J., Milne TA., Wang GG., Li H., Allis CD., Patel DJ. Apoptosis - Interactions involving proteins with a function related to apoptosis pateld@mskcc.org Accepted 2010-OCT-13 by JYOTI. 21-Dec-2010: Contacted by JYOTI. Cell (0092-8674) 2010 jyoti Only protein-protein interactions imex curation Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Cell (0092-8674) 2010 imex curation Wang Z., Song J., Milne TA., Wang GG., Li H., Allis CD., Patel DJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Chromatin - Epigenetic interactions resulting in chromatin modulation pateld@mskcc.org 21-Dec-2010: Contacted by JYOTI. jyoti Only protein-protein interactions human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. ch-ip chromatin immunoprecipitation assay ch-ip primer specific pcr primer specific pcr Wang Z., Song J., Milne TA., Wang GG., Li H., Allis CD., Patel DJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Proteins-nucleic acids cross-linked using paraformaldehyde. pateld@mskcc.org Accepted 2010-OCT-13 by JYOTI. 21-Dec-2010: Contacted by JYOTI. Cell (0092-8674) 2010 jyoti Only protein-protein interactions imex curation Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Cell (0092-8674) 2010 imex curation Wang Z., Song J., Milne TA., Wang GG., Li H., Allis CD., Patel DJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Chromatin - Epigenetic interactions resulting in chromatin modulation pateld@mskcc.org 21-Dec-2010: Contacted by JYOTI. jyoti 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 Wang Z., Song J., Milne TA., Wang GG., Li H., Allis CD., Patel DJ. Apoptosis - Interactions involving proteins with a function related to apoptosis pateld@mskcc.org Accepted 2010-OCT-13 by JYOTI. 21-Dec-2010: Contacted by JYOTI. Cell (0092-8674) 2010 jyoti Only protein-protein interactions imex curation Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Cell (0092-8674) 2010 imex curation Wang Z., Song J., Milne TA., Wang GG., Li H., Allis CD., Patel DJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Chromatin - Epigenetic interactions resulting in chromatin modulation pateld@mskcc.org 21-Dec-2010: Contacted by JYOTI. jyoti Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Wang Z., Song J., Milne TA., Wang GG., Li H., Allis CD., Patel DJ. Apoptosis - Interactions involving proteins with a function related to apoptosis pateld@mskcc.org Accepted 2010-OCT-13 by JYOTI. 21-Dec-2010: Contacted by JYOTI. Cell (0092-8674) 2010 jyoti Only protein-protein interactions imex curation Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Cell (0092-8674) 2010 imex curation Wang Z., Song J., Milne TA., Wang GG., Li H., Allis CD., Patel DJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Chromatin - Epigenetic interactions resulting in chromatin modulation pateld@mskcc.org 21-Dec-2010: Contacted by JYOTI. jyoti 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 Wang Z., Song J., Milne TA., Wang GG., Li H., Allis CD., Patel DJ. Apoptosis - Interactions involving proteins with a function related to apoptosis pateld@mskcc.org Accepted 2010-OCT-13 by JYOTI. 21-Dec-2010: Contacted by JYOTI. Cell (0092-8674) 2010 jyoti Only protein-protein interactions imex curation Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Cell (0092-8674) 2010 imex curation Wang Z., Song J., Milne TA., Wang GG., Li H., Allis CD., Patel DJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Chromatin - Epigenetic interactions resulting in chromatin modulation pateld@mskcc.org 21-Dec-2010: Contacted by JYOTI. jyoti Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Wang Z., Song J., Milne TA., Wang GG., Li H., Allis CD., Patel DJ. Apoptosis - Interactions involving proteins with a function related to apoptosis pateld@mskcc.org Accepted 2010-OCT-13 by JYOTI. 21-Dec-2010: Contacted by JYOTI. Cell (0092-8674) 2010 jyoti Only protein-protein interactions imex curation ppie_human Peptidyl-prolyl cis-trans isomerase E Cyclophilin E Cyclophilin-33 PPIE CYP33 Rotamase E protein protein human Homo sapiens Human MATTKRVLYVGGLAEEVDDKVLHAAFIPFGDITDIQIPLDYETEKHRGFAFVEFELAEDAAAAIDNMNESELFGRTIRVNLAKPMRIKEGSSRPVWSDDDWLKKFSGKTLEENKEEEGSEPPKAETQEGEPIAKKARSNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKGFGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEVTEGLDVLRQIEAQGSKDGKPKQKVIIADCGEYV DIP protein Q9UNP9 original sequence version: 150 F3226149A790BA42 kmt2a_human Histone-lysine N-methyltransferase 2A KMT2A ALL-1 ALL1 CXXC-type zinc finger protein 7 CXXC7 HRX HTRX MLL MLL1 Myeloid/lymphoid or mixed-lineage leukemia Myeloid/lymphoid or mixed-lineage leukemia protein 1 TRX1 Trithorax-like protein Zinc finger protein HRX Cysteine methyltransferase KMT2A protein protein human Homo sapiens Human MAHSCRWRFPARPGTTGGGGGGGRRGLGGAPRQRVPALLLPPGPPVGGGGPGAPPSPPAVAAAAAAAGSSGAGVPGGAAAASAASSSSASSSSSSSSSASSGPALLRVGPGFDAALQVSAAIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRSPTRSPSVKTSPRKPRGRPRSGSDRNSAILSDPSVFSPLNKSETKSGDKIKKKDSKSIEKKRGRPPTFPGVKIKITHGKDISELPKGNKEDSLKKIKRTPSATFQQATKIKKLRAGKLSPLKSKFKTGKLQIGRKGVQIVRRRGRPPSTERIKTPSGLLINSELEKPQKVRKDKEGTPPLTKEDKTVVRQSPRRIKPVRIIPSSKRTDATIAKQLLQRAKKGAQKKIEKEAAQLQGRKVKTQVKNIRQFIMPVVSAISSRIIKTPRRFIEDEDYDPPIKIARLESTPNSRFSAPSCGSSEKSSAASQHSSQMSSDSSRSSSPSVDTSTDSQASEEIQVLPEERSDTPEVHPPLPISQSPENESNDRRSRRYSVSERSFGSRTTKKLSTLQSAPQQQTSSSPPPPLLTPPPPLQPASSISDHTPWLMPPTIPLASPFLPASTAPMQGKRKSILREPTFRWTSLKHSRSEPQYFSSAKYAKEGLIRKPIFDNFRPPPLTPEDVGFASGFSASGTAASARLFSPLHSGTRFDMHKRSPLLRAPRFTPSEAHSRIFESVTLPSNRTSAGTSSSGVSNRKRKRKVFSPIRSEPRSPSHSMRTRSGRLSSSELSPLTPPSSVSSSLSISVSPLATSALNPTFTFPSHSLTQSGESAEKNQRPRKQTSAPAEPFSSSSPTPLFPWFTPGSQTERGRNKDKAPEELSKDRDADKSVEKDKSRERDREREKENKRESRKEKRKKGSEIQSSSALYPVGRVSKEKVVGEDVATSSSAKKATGRKKSSSHDSGTDITSVTLGDTTAVKTKILIKKGRGNLEKTNLDLGPTAPSLEKEKTLCLSTPSSSTVKHSTSSIGSMLAQADKLPMTDKRVASLLKKAKAQLCKIEKSKSLKQTDQPKAQGQESDSSETSVRGPRIKHVCRRAAVALGRKRAVFPDDMPTLSALPWEEREKILSSMGNDDKSSIAGSEDAEPLAPPIKPIKPVTRNKAPQEPPVKKGRRSRRCGQCPGCQVPEDCGVCTNCLDKPKFGGRNIKKQCCKMRKCQNLQWMPSKAYLQKQAKAVKKKEKKSKTSEKKDSKESSVVKNVVDSSQKPTPSAREDPAPKKSSSEPPPRKPVEEKSEEGNVSAPGPESKQATTPASRKSSKQVSQPALVIPPQPPTTGPPRKEVPKTTPSEPKKKQPPPPESGPEQSKQKKVAPRPSIPVKQKPKEKEKPPPVNKQENAGTLNILSTLSNGNSSKQKIPADGVHRIRVDFKEDCEAENVWEMGGLGILTSVPITPRVVCFLCASSGHVEFVYCQVCCEPFHKFCLEENERPLEDQLENWCCRRCKFCHVCGRQHQATKQLLECNKCRNSYHPECLGPNYPTKPTKKKKVWICTKCVRCKSCGSTTPGKGWDAQWSHDFSLCHDCAKLFAKGNFCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCVNCTERHPAEWRLALEKELQISLKQVLTALLNSRTTSHLLRYRQAAKPPDLNPETEESIPSRSSPEGPDPPVLTEVSKQDDQQPLDLEGVKRKMDQGNYTSVLEFSDDIVKIIQAAINSDGGQPEIKKANSMVKSFFIRQMERVFPWFSVKKSRFWEPNKVSSNSGMLPNAVLPPSLDHNYAQWQEREENSHTEQPPLMKKIIPAPKPKGPGEPDSPTPLHPPTPPILSTDRSREDSPELNPPPGIEDNRQCALCLTYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFLDDKKVYCQRHRDLIKGEVVPENGFEVFRRVFVDFEGISLRRKFLNGLEPENIHMMIGSMTIDCLGILNDLSDCEDKLFPIGYQCSRVYWSTTDARKRCVYTCKIVECRPPVVEPDINSTVEHDENRTIAHSPTSFTESSSKESQNTAEIISPPSPDRPPHSQTSGSCYYHVISKVPRIRTPSYSPTQRSPGCRPLPSAGSPTPTTHEIVTVGDPLLSSGLRSIGSRRHSTSSLSPQRSKLRIMSPMRTGNTYSRNNVSSVSTTGTATDLESSAKVVDHVLGPLNSSTSLGQNTSTSSNLQRTVVTVGNKNSHLDGSSSSEMKQSSASDLVSKSSSLKGEKTKVLSSKSSEGSAHNVAYPGIPKLAPQVHNTTSRELNVSKIGSFAEPSSVSFSSKEALSFPHLHLRGQRNDRDQHTDSTQSANSSPDEDTEVKTLKLSGMSNRSSIINEHMGSSSRDRRQKGKKSCKETFKEKHSSKSFLEPGQVTTGEEGNLKPEFMDEVLTPEYMGQRPCNNVSSDKIGDKGLSMPGVPKAPPMQVEGSAKELQAPRKRTVKVTLTPLKMENESQSKNALKESSPASPLQIESTSPTEPISASENPGDGPVAQPSPNNTSCQDSQSNNYQNLPVQDRNLMLPDGPKPQEDGSFKRRYPRRSARARSNMFFGLTPLYGVRSYGEEDIPFYSSSTGKKRGKRSAEGQVDGADDLSTSDEDDLYYYNFTRTVISSGGEERLASHNLFREEEQCDLPKISQLDGVDDGTESDTSVTATTRKSSQIPKRNGKENGTENLKIDRPEDAGEKEHVTKSSVGHKNEPKMDNCHSVSRVKTQGQDSLEAQLSSLESSRRVHTSTPSDKNLLDTYNTELLKSDSDNNNSDDCGNILPSDIMDFVLKNTPSMQALGESPESSSSELLNLGEGLGLDSNREKDMGLFEVFSQQLPTTEPVDSSVSSSISAEEQFELPLELPSDLSVLTTRSPTVPSQNPSRLAVISDSGEKRVTITEKSVASSESDPALLSPGVDPTPEGHMTPDHFIQGHMDADHISSPPCGSVEQGHGNNQDLTRNSSTPGLQVPVSPTVPIQNQKYVPNSTDSPGPSQISNAAVQTTPPHLKPATEKLIVVNQNMQPLYVLQTLPNGVTQKIQLTSSVSSTPSVMETNTSVLGPMGGGLTLTTGLNPSLPTSQSLFPSASKGLLPMSHHQHLHSFPAATQSSFPPNISNPPSGLLIGVQPPPDPQLLVSESSQRTDLSTTVATPSSGLKKRPISRLQTRKNKKLAPSSTPSNIAPSDVVSNMTLINFTPSQLPNHPSLLDLGSLNTSSHRTVPNIIKRSKSSIMYFEPAPLLPQSVGGTAATAAGTSTISQDTSHLTSGSVSGLASSSSVLNVVSMQTTTTPTSSASVPGHVTLTNPRLLGTPDIGSISNLLIKASQQSLGIQDQPVALPPSSGMFPQLGTSQTPSTAAITAASSICVLPSTQTTGITAASPSGEADEHYQLQHVNQLLASKTGIHSSQRDLDSASGPQVSNFTQTVDAPNSMGLEQNKALSSAVQASPTSPGGSPSSPSSGQRSASPSVPGPTKPKPKTKRFQLPLDKGNGKKHKVSHLRTSSSEAHIPDQETTSLTSGTGTPGAEAEQQDTASVEQSSQKECGQPAGQVAVLPEVQVTQNPANEQESAEPKTVEEEESNFSSPLMLWLQQEQKRKESITEKKPKKGLVFEISSDDGFQICAESIEDAWKSLTDKVQEARSNARLKQLSFAGVNGLRMLGILHDAVVFLIEQLSGAKHCRNYKFRFHKPEEANEPPLNPHGSARAEVHLRKSAFDMFNFLASKHRQPPEYNPNDEEEEEVQLKSARRATSMDLPMPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGNVIRSIQTDKREKYYDSKGIGCYMFRIDDSEVVDATMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN DIP protein Q03164 original sequence version: 85 DIP protein Q03164-1 original sequence version: 137 DIP protein Q03164 original sequence version: 140 DIP protein Q03164-1 original sequence version: 141 DIP protein Q03164 original sequence version: 172 DIP protein Q03164-1 original sequence version: 190 DIP protein Q03164-1 original sequence version: 200 DIP protein Q03164 original sequence version: 153 DIP protein Q03164-1 original sequence version: 154 DIP protein Q03164-1 original sequence version: 196 DIP protein Q03164 original sequence version: 159 1150F37EAB1430D3 q03164-pro_0000390949 MLL cleavage product N320 KMT2A ALL-1 ALL1 CXXC-type zinc finger protein 7 CXXC7 HRX HTRX MLL MLL1 Myeloid/lymphoid or mixed-lineage leukemia Myeloid/lymphoid or mixed-lineage leukemia protein 1 TRX1 Trithorax-like protein Zinc finger protein HRX Cysteine methyltransferase KMT2A protein protein human Homo sapiens Human MAHSCRWRFPARPGTTGGGGGGGRRGLGGAPRQRVPALLLPPGPPVGGGGPGAPPSPPAVAAAAAAAGSSGAGVPGGAAAASAASSSSASSSSSSSSSASSGPALLRVGPGFDAALQVSAAIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRSPTRSPSVKTSPRKPRGRPRSGSDRNSAILSDPSVFSPLNKSETKSGDKIKKKDSKSIEKKRGRPPTFPGVKIKITHGKDISELPKGNKEDSLKKIKRTPSATFQQATKIKKLRAGKLSPLKSKFKTGKLQIGRKGVQIVRRRGRPPSTERIKTPSGLLINSELEKPQKVRKDKEGTPPLTKEDKTVVRQSPRRIKPVRIIPSSKRTDATIAKQLLQRAKKGAQKKIEKEAAQLQGRKVKTQVKNIRQFIMPVVSAISSRIIKTPRRFIEDEDYDPPIKIARLESTPNSRFSAPSCGSSEKSSAASQHSSQMSSDSSRSSSPSVDTSTDSQASEEIQVLPEERSDTPEVHPPLPISQSPENESNDRRSRRYSVSERSFGSRTTKKLSTLQSAPQQQTSSSPPPPLLTPPPPLQPASSISDHTPWLMPPTIPLASPFLPASTAPMQGKRKSILREPTFRWTSLKHSRSEPQYFSSAKYAKEGLIRKPIFDNFRPPPLTPEDVGFASGFSASGTAASARLFSPLHSGTRFDMHKRSPLLRAPRFTPSEAHSRIFESVTLPSNRTSAGTSSSGVSNRKRKRKVFSPIRSEPRSPSHSMRTRSGRLSSSELSPLTPPSSVSSSLSISVSPLATSALNPTFTFPSHSLTQSGESAEKNQRPRKQTSAPAEPFSSSSPTPLFPWFTPGSQTERGRNKDKAPEELSKDRDADKSVEKDKSRERDREREKENKRESRKEKRKKGSEIQSSSALYPVGRVSKEKVVGEDVATSSSAKKATGRKKSSSHDSGTDITSVTLGDTTAVKTKILIKKGRGNLEKTNLDLGPTAPSLEKEKTLCLSTPSSSTVKHSTSSIGSMLAQADKLPMTDKRVASLLKKAKAQLCKIEKSKSLKQTDQPKAQGQESDSSETSVRGPRIKHVCRRAAVALGRKRAVFPDDMPTLSALPWEEREKILSSMGNDDKSSIAGSEDAEPLAPPIKPIKPVTRNKAPQEPPVKKGRRSRRCGQCPGCQVPEDCGVCTNCLDKPKFGGRNIKKQCCKMRKCQNLQWMPSKAYLQKQAKAVKKKEKKSKTSEKKDSKESSVVKNVVDSSQKPTPSAREDPAPKKSSSEPPPRKPVEEKSEEGNVSAPGPESKQATTPASRKSSKQVSQPALVIPPQPPTTGPPRKEVPKTTPSEPKKKQPPPPESGPEQSKQKKVAPRPSIPVKQKPKEKEKPPPVNKQENAGTLNILSTLSNGNSSKQKIPADGVHRIRVDFKEDCEAENVWEMGGLGILTSVPITPRVVCFLCASSGHVEFVYCQVCCEPFHKFCLEENERPLEDQLENWCCRRCKFCHVCGRQHQATKQLLECNKCRNSYHPECLGPNYPTKPTKKKKVWICTKCVRCKSCGSTTPGKGWDAQWSHDFSLCHDCAKLFAKGNFCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCVNCTERHPAEWRLALEKELQISLKQVLTALLNSRTTSHLLRYRQAAKPPDLNPETEESIPSRSSPEGPDPPVLTEVSKQDDQQPLDLEGVKRKMDQGNYTSVLEFSDDIVKIIQAAINSDGGQPEIKKANSMVKSFFIRQMERVFPWFSVKKSRFWEPNKVSSNSGMLPNAVLPPSLDHNYAQWQEREENSHTEQPPLMKKIIPAPKPKGPGEPDSPTPLHPPTPPILSTDRSREDSPELNPPPGIEDNRQCALCLTYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFLDDKKVYCQRHRDLIKGEVVPENGFEVFRRVFVDFEGISLRRKFLNGLEPENIHMMIGSMTIDCLGILNDLSDCEDKLFPIGYQCSRVYWSTTDARKRCVYTCKIVECRPPVVEPDINSTVEHDENRTIAHSPTSFTESSSKESQNTAEIISPPSPDRPPHSQTSGSCYYHVISKVPRIRTPSYSPTQRSPGCRPLPSAGSPTPTTHEIVTVGDPLLSSGLRSIGSRRHSTSSLSPQRSKLRIMSPMRTGNTYSRNNVSSVSTTGTATDLESSAKVVDHVLGPLNSSTSLGQNTSTSSNLQRTVVTVGNKNSHLDGSSSSEMKQSSASDLVSKSSSLKGEKTKVLSSKSSEGSAHNVAYPGIPKLAPQVHNTTSRELNVSKIGSFAEPSSVSFSSKEALSFPHLHLRGQRNDRDQHTDSTQSANSSPDEDTEVKTLKLSGMSNRSSIINEHMGSSSRDRRQKGKKSCKETFKEKHSSKSFLEPGQVTTGEEGNLKPEFMDEVLTPEYMGQRPCNNVSSDKIGDKGLSMPGVPKAPPMQVEGSAKELQAPRKRTVKVTLTPLKMENESQSKNALKESSPASPLQIESTSPTEPISASENPGDGPVAQPSPNNTSCQDSQSNNYQNLPVQDRNLMLPDGPKPQEDGSFKRRYPRRSARARSNMFFGLTPLYGVRSYGEEDIPFYSSSTGKKRGKRSAEGQVDGADDLSTSDEDDLYYYNFTRTVISSGGEERLASHNLFREEEQCDLPKISQLD Amino acids 1 � 2718. An N-terminal cleavage product of 320 kDa, identifier Q03164- PRO_0000390949. Short name is p320. 1 2718 08B1A59A345C4CFD cdkn1b_human_gene Cyclin-dependent kinase inhibitor 1B (p27Kip1) gene gene human Homo sapiens Human msx2_human_gene Homeobox protein MSX-2 (Homeobox protein Hox-8) gene gene human Homo sapiens Human h31_human Histone H3.1 H3FA H3FL H3FD H3FI H3FH H3FK H3FF H3FJ H3FB Histone H3/a Histone H3/b Histone H3/c Histone H3/d Histone H3/f Histone H3/h Histone H3/i Histone H3/j Histone H3/k Histone H3/l H3C1 HIST1H3A H3C2 HIST1H3B H3C3 H3FC HIST1H3C H3C4 HIST1H3D H3C6 HIST1H3E H3C7 HIST1H3F H3C8 HIST1H3G H3C10 HIST1H3H H3C11 HIST1H3I H3C12 HIST1H3J protein protein human Homo sapiens Human MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P68431 original sequence version: 78 DIP protein P68431 original sequence version: 79 DIP protein P68431 original sequence version: 76 DIP protein P68431 original sequence version: 92 DIP protein P68431 original sequence version: 87 DIP protein P68431 original sequence version: 101 DIP protein P68431 original sequence version: 130 DIP protein P68431 original sequence version: 115 9B89008EA50A0EF6 hoxa9_human_gene Human HOXA9 gene gene gene human Homo sapiens Human mll-h31-1 5 12 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain lys-5 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 16 19 direct interaction direct interaction Supp. Table 1 1.9 A R-working:23.9% R-free:27.4% Crystal Structure of MLL1 PHD3-Bromo Cassette Bound to H3K4me3/2-Containing Peptides, mll-h31-2 6 8 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 12 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain lys-5 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp. Figure 1B Peptide pull-down assays showed that the binding for MLL1 PHD3-Bromo cassette was detected for H3K4me3/2 mll-h31-3 4 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q03164:p.Gln1587Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Q A Wed May 02 15:25:19 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln1587ala' Tue Jun 30 19:50:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln1587Ala' Q03164:p.Tyr1581Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y A Wed May 02 15:05:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr1581ala' Tue Jun 30 18:57:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr1581Ala' Q03164:p.Trp1594Glu mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain W E Wed May 02 18:00:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp1594glu' Tue Jun 30 20:25:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp1594Glu' ecoli Escherichia coli (strain K12) 12 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain lys-5 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction Figure 2D ITC profiles for the binding of H3(1-15)K4me3 peptide to wild-type (WT) MLL1 PHD3-Bromo and its W1594E, Y1581A, and Q1587A mutants mll-h31-4 4 12 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain lys-5 n6me1lys N6-methyl-L-lysine (2S)-2-amino-6-methylaminohexanoic acid MOD_RES N6-methyllysine N(zeta)-methyllysine N6-methyl-L-lysine N6-methylated L-lysine epsilon-methyllysine Methyl Methylation N-methyl Lysyl N6Me1Lys certain certain sequence position certain certain certain sequence position certain region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 2A ITC binding curves of MLL1 PHD3-Bromo cassette with H3K4me-containing peptides. mll-h31-5 6 8 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 12 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain lys-5 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp. Figure 1B mll-h31-6 4 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 12 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain lys-5 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 2A ITC binding curves of MLL1 PHD3-Bromo cassette with H3K4me-containing peptides. mll-h31-7 4 12 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain lys-5 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P68431:p.Ala2[2] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain A AA Wed May 02 19:22:44 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala2ala_ala' Tue Jun 30 15:55:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala2[2]' ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Figure 2A, 2H ITC binding curves of MLL1 PHD3-Bromo cassette with H3K4me-containing peptides. mll-hoxa9 2 8 unspecified role unspecified role bait bait 13 unspecified role unspecified role prey prey association association ChIP analysis with antibodies for MLLC (B) or H3K4me3 (normalized to H3 levels) (C) at the target genes HOXA9, HOXC8, and p27KIP1. Fig. 3B, S5 CyP33 has no effect on MLL1 binding at HOXA9 and HOXC8 suggesting that its mechanism of action does not involve modulating MLL1 binding to target genes. mll-msx2-1 2 11 unspecified role unspecified role prey prey 8 unspecified role unspecified role bait bait association association ChIP analysis with antibodies for MLLC (B) or H3K4me3 (normalized to H3 levels) (C) at the target genes HOXA9, HOXC8, and p27KIP1. Fig. 3B, S5 CyP33 has no effect on MLL1 binding at HOXA9 and HOXC8 suggesting that its mechanism of action does not involve modulating MLL1 binding to target genes. mll-cdkn1b-1 2 10 unspecified role unspecified role prey prey 8 unspecified role unspecified role bait bait association association ChIP analysis with antibodies for MLLC (B) or H3K4me3 (normalized to H3 levels) (C) at the target genes HOXA9, HOXC8, and p27KIP1. Fig. 3B mlln-hoxa9-1 2 9 unspecified role unspecified role bait bait Q03164-PRO_0000390949:p.Trp1594Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain W E Wed May 02 15:21:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp1594glu' Tue Jun 30 18:21:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp1594Glu' region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 13 unspecified role unspecified role prey prey association association Fig. 3E MLL Trp1594Glu specifically disrupts the binding between MLL1 PHD3 and the H3K4me3. Protein [uniprotkb:Q03164-PRO_0000390949] has undergone a significant sequence change since this entry was originally annotated which may effect the results shown. For further information, please access the IntAct curation manual and for details of the sequence change go to [unisave] mlln-msx2-1 2 9 unspecified role unspecified role bait bait Q03164-PRO_0000390949:p.Trp1594Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain W E Wed May 02 19:46:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp1594glu' Tue Jun 30 19:12:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp1594Glu' region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 11 unspecified role unspecified role prey prey association association Fig. 3E MLL Trp1594Glu specifically disrupts the binding between MLL1 PHD3 and the H3K4me3. Protein [uniprotkb:Q03164-PRO_0000390949] has undergone a significant sequence change since this entry was originally annotated which may effect the results shown. For further information, please access the IntAct curation manual and for details of the sequence change go to [unisave] mlln-cdkn1b-1 2 10 unspecified role unspecified role prey prey 9 unspecified role unspecified role bait bait Q03164-PRO_0000390949:p.Trp1594Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain W E Wed May 02 17:00:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp1594glu' Tue Jun 30 19:27:47 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp1594Glu' region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined association association Fig. 3B MLL Trp1594Glu specifically disrupts the binding between MLL1 PHD3 and the H3K4me3. Protein [uniprotkb:Q03164-PRO_0000390949] has undergone a significant sequence change since this entry was originally annotated which may effect the results shown. For further information, please access the IntAct curation manual and for details of the sequence change go to [unisave] mll1-ppie-1 3 8 unspecified role unspecified role neutral component neutral component phd region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q03164:p.Met1606Asp mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain M D Wed May 02 19:33:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'met1606asp' Tue Jun 30 18:40:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Met1606Asp' ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component rrm region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 92 95 direct interaction direct interaction First, when full-length CyP33 was mixed with MLL1 PHD3-Bromo cassette, the gel filtration results showed that the two proteins co-migrated and formed a stable complex (Figure 4, line 4, and Figure S3C) Fig. 4, Supp. Fig. 3 mll1-ppie-2 1 7 unspecified role unspecified role neutral component neutral component rrm region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component phd region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain region 1H radiolabelled radiolabel radiolabeled radiolabelled undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region 13c label 13c label C13 13C C13 13C undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 98 100 direct interaction direct interaction The backbone trace of 20 NMR refined structures of the complex containing the MLL1 PHD3 fragment (1603�1619, blue) and CyP33 RRM (2�82, magenta) Figs. 5C, 5D, Supp. Fig. 4F mll1-h31 1 8 unspecified role unspecified role neutral component neutral component phd region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain region 1H radiolabelled radiolabel radiolabeled radiolabelled undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region 13c label 13c label C13 13C C13 13C undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 12 unspecified role unspecified role neutral component neutral component lys-5 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction The backbone trace of 20 NMR refined structures of the complex containing the MLL1 PHD3 fragment (1603�1619, blue) and CyP33 RRM (2�82, magenta) Figs. 5I mll1-ppie-3 1 12 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component phd region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain region 1H radiolabelled radiolabel radiolabeled radiolabelled undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region 13c label 13c label C13 13C C13 13C undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component rrm region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) physical association physical association We observed a large downfield shift of the Trp indole cross-peak on addition of H3K4me3 to form a binary complex, followed by an upfield shift on addition of CyP33 RRM to form a ternary complex (Figure 5I). Figs. 5I, Supp. Fig. 4F mll-h31-8 4 7 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 12 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain lys-5 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Figure 5H ITC curves for binding of H3(1-15)K4me3/2 peptide to the complex of MLL1 PHD3-Bromo and full-length CyP33. mll-h31-9 4 12 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain lys-5 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction Figure 5H ITC curves for binding of H3(1-15)K4me3/2 peptide to the complex of MLL1 PHD3-Bromo and full-length CyP33. ppie-hoxa9-1 2 13 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q9UNP9:p.Phe51Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain F E Wed May 02 18:41:32 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe51glu' Tue Jun 30 16:21:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe51Glu' association association Anti-HA ChIP shows that wild-type (red bars) and F196E/M197E (purple bars) versions of CyP33 bound to HOXA9 and HOXC8, while the F51D point mutation exhibited variably reduced CyP33 binding. Fig. 6D mll-msx2-2 2 7 unspecified role unspecified role bait bait Q9UNP9:p.Phe51Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain F E Wed May 02 14:55:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe51glu' Tue Jun 30 19:53:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe51Glu' region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 11 unspecified role unspecified role prey prey association association Anti-HA ChIP shows that wild-type (red bars) and F196E/M197E (purple bars) versions of CyP33 bound to HOXA9 and HOXC8, while the F51D point mutation exhibited variably reduced CyP33 binding. Fig. 6D