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/ The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. Cancer Cell (1535-6108) 2010 imex curation Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Species of constructs supplied by authors. jayhess@umich.edu 13-Sept-2010: Contacted by JYOTI. orchard Only protein-protein interactions human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Sandra - EBI-2899046 is the one to look at. Species of constructs supplied by authors. jayhess@umich.edu Accepted 2010-AUG-26 by ORCHARD. 13-Sept-2010: Contacted by JYOTI. Cancer Cell (1535-6108) 2010 orchard Only protein-protein interactions imex curation The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. Cancer Cell (1535-6108) 2010 imex curation Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Species of constructs supplied by authors. jayhess@umich.edu 13-Sept-2010: Contacted by JYOTI. orchard Only protein-protein interactions in vitro In vitro anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Species of constructs supplied by authors. jayhess@umich.edu Accepted 2010-AUG-26 by ORCHARD. 13-Sept-2010: Contacted by JYOTI. Cancer Cell (1535-6108) 2010 orchard Only protein-protein interactions imex curation The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. Cancer Cell (1535-6108) 2010 imex curation Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Species of constructs supplied by authors. jayhess@umich.edu 13-Sept-2010: Contacted by JYOTI. orchard Only protein-protein interactions in vitro In vitro anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Species of constructs supplied by authors. jayhess@umich.edu Accepted 2010-AUG-26 by ORCHARD. 13-Sept-2010: Contacted by JYOTI. Cancer Cell (1535-6108) 2010 orchard Only protein-protein interactions imex curation The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. Cancer Cell (1535-6108) 2010 imex curation Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Species of constructs supplied by authors. jayhess@umich.edu 13-Sept-2010: Contacted by JYOTI. orchard Only protein-protein interactions human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. anti tag coip anti tag coimmunoprecipitation anti tag coip sequence tag sequence tag identification sequence tag Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Species of constructs supplied by authors. jayhess@umich.edu Accepted 2010-AUG-26 by ORCHARD. Cancer Cell (1535-6108) 2010 orchard Only protein-protein interactions imex curation The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. Cancer Cell (1535-6108) 2010 imex curation Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Species of constructs supplied by authors. jayhess@umich.edu 13-Sept-2010: Contacted by JYOTI. orchard Only protein-protein interactions mouse-bone-marrow Mouse bone marrow bone_marrow bone marrow ch-ip chromatin immunoprecipitation assay ch-ip primer specific pcr primer specific pcr Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Cell lines were generated by transducing mouse bone marrow cells with either (human) MLL-ENL or E2A-HLF. Species of constructs supplied by authors. Species of constructs supplied by authors. jayhess@umich.edu Accepted 2010-AUG-26 by ORCHARD. 13-Sept-2010: Contacted by JYOTI. Further interactions involving histone H3 species cannot be entered due to the lack of specificity of the antibodies used. Cancer Cell (1535-6108) 2010 orchard Only protein-protein interactions imex curation The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. Cancer Cell (1535-6108) 2010 imex curation Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Species of constructs supplied by authors. jayhess@umich.edu 13-Sept-2010: Contacted by JYOTI. orchard Only protein-protein interactions human-kopn_8 Human KOPN8 B cell precursor leukemia line (MLL-ENL fusion gene. kopn_8 Human B cell precursor leukemia cell line (MLL-ENL fusion) Established from the peripheral blood of a 3-month-old girl with B cell precursor acute lymphoblastic leukemia (BCP-ALL) of type B-III in 1977; cells were described to carry the t(11;19)(q23;p13) leading to the MLL-ENL fusion gene. anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Species of constructs supplied by authors. Species of constructs supplied by authors. jayhess@umich.edu Accepted 2010-AUG-26 by ORCHARD. 13-Sept-2010: Contacted by JYOTI. Cancer Cell (1535-6108) 2010 orchard Only protein-protein interactions imex curation The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. Cancer Cell (1535-6108) 2010 imex curation Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Species of constructs supplied by authors. jayhess@umich.edu 13-Sept-2010: Contacted by JYOTI. orchard Only protein-protein interactions human-293t Homo sapiens 293 cells transformed with SV40 large T antigen 293t 293 cells expressing SV40 large T antigen. The original designation of this cell line was 293tsA1609neo. It is not in Cabri,ATCC or HyperCLDB. ch-ip chromatin immunoprecipitation assay ch-ip primer specific pcr primer specific pcr Muntean AG., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly JA., Basrur V., Elenitoba-Johnson KS., Hess JL. Apoptosis - Interactions involving proteins with a function related to apoptosis Species of constructs supplied by authors. jayhess@umich.edu Accepted 2010-AUG-26 by ORCHARD. 13-Sept-2010: Contacted by JYOTI. Further interactions involving histone H3 species cannot be entered due to the lack of specificity of the antibodies used. Cancer Cell (1535-6108) 2010 orchard Only protein-protein interactions imex curation ctr9_human RNA polymerase-associated protein CTR9 homolog CTR9 KIAA0155 SH2BP1 SH2 domain-binding protein 1 protein protein human Homo sapiens Human MSRGSIEIPLRDTDEVIELDFDQLPEGDEVISILKQEHTQLHIWIALALEYYKQGKTEEFVKLLEAARIDGNLDYRDHEKDQMTCLDTLAAYYVQQARKEKNKDNKKDLITQATLLYTMADKIIMYDQNHLLGRACFCLLEGDKMDQADAQFHFVLNQSPNNIPALLGKACISFNKKDYRGALAYYKKALRTNPGCPAEVRLGMGHCFVKLNKLEKARLAFSRALELNSKCVGALVGLAVLELNNKEADSIKNGVQLLSRAYTIDPSNPMVLNHLANHFFFKKDYSKVQHLALHAFHNTEVEAMQAESCYQLARSFHVQEDYDQAFQYYYQATQFASSSFVLPFFGLGQMYIYRGDKENASQCFEKVLKAYPNNYETMKILGSLYAASEDQEKRDIAKGHLKKVTEQYPDDVEAWIELAQILEQTDIQGALSAYGTATRILQEKVQADVPPEILNNVGALHFRLGNLGEAKKYFLASLDRAKAEAEHDEHYYNAISVTTSYNLARLYEAMCEFHEAEKLYKNILREHPNYVDCYLRLGAMARDKGNFYEASDWFKEALQINQDHPDAWSLIGNLHLAKQEWGPGQKKFERILKQPSTQSDTYSMLALGNVWLQTLHQPTRDREKEKRHQDRALAIYKQVLRNDAKNLYAANGIGAVLAHKGYFREARDVFAQVREATADISDVWLNLAHIYVEQKQYISAVQMYENCLRKFYKHQNTEVVLYLARALFKCGKLQECKQTLLKARHVAPSDTVLMFNVALVLQRLATSVLKDEKSNLKEVLNAVKELELAHRYFSYLSKVGDKMRFDLALAATEARQCSDLLSQAQYHVARARKQDEEERELRAKQEQEKELLRQKLLKEQEEKRLREKEEQKKLLEQRAQYVEKTKNILMFTGETEATKEKKRGGGGGRRSKKGGEFDEFVNDDTDDDLPISKKKKRRKGSGSEQEGEDEEGGERKKKKRRRHPKGEEGSDDDETENGPKPKKRRPPKAEKKKAPKPERLPPSMKGKIKSKAIISSSDDSSDEDKLKIADEGHPRNSNSNSDSDEDEQRKKCASSESDSDENQNKSGSEAGSPRRPRRQRSDQDSDSDQPSRKRRPSGSEQSDNESVQSGRSHSGVSENDSRPASPSAESDHESERGSDNEGSGQGSGNESEPEGSNNEASDRGSEHGSDDSD DIP protein Q6PD62 original sequence version: 68 DIP protein Q6PD62 original sequence version: 122 4B5AC22A5C5573C6 wdr61_human WD repeat-containing protein 61 WDR61 Meiotic recombination REC14 protein homolog SKI8 homolog protein protein human Homo sapiens Human MTNQYGILFKQEQAHDDAIWSVAWGTNKKENSETVVTGSLDDLVKVWKWRDERLDLQWSLEGHQLGVVSVDISHTLPIAASSSLDAHIRLWDLENGKQIKSIDAGPVDAWTLAFSPDSQYLATGTHVGKVNIFGVESGKKEYSLDTRGKFILSIAYSPDGKYLASGAIDGIINIFDIATGKLLHTLEGHAMPIRSLTFSPDSQLLVTASDDGYIKIYDVQHANLAGTLSGHASWVLNVAFCPDDTHFVSSSSDKSVKVWDVGTRTCVHTFFDHQDQVWGVKYNGNGSKIVSVGDDQEIHIYDCPI DIP protein Q9GZS3 original sequence version: 72 A26C4BBD4F8ADB80 hoxa9_human_gene Human HOXA9 gene gene gene human Homo sapiens Human ctr9_mouse RNA polymerase-associated protein CTR9 homolog SH2 domain-binding protein 1 Tetratricopeptide repeat-containing, SH2-binding phosphoprotein of 150 kDa Ctr9 Kiaa0155 Sh2bp1 protein protein mouse Mus musculus Mouse MSRGSIEIPLRDTDEVIELDFDQLPEGDEVISILKQEHTQLHIWIALALEYYKQGKTEEFVKLLEAARIDGNLDYRDHEKDQMTCLDTLAAYYVQQARKEKNKDNKKDLITQATLLYTMADKIIMYDQNHLLGRACFCLLEGDKMDQADAQFHFVLNQSPNNIPALLGKACISFNKKDYRGALAYYKKALRTNPGCPAEVRLGMGHCFVKLNKLEKARLAFSRALELNSKCVGALVGLAVLELNNKEADSIKNGVQLLSRAYTIDPSNPMVLNHLANHFFFKKDYSKVQHLALHAFHNTEVEAMQAESCYQLARSFHVQEDYDQAFQYYYQATQFASSSFVLPFFGLGQMYIYRGDKENASQCFEKVLKAYPNNYETMKILGSLYAASEDQEKRDIAKGHLKKVTEQYPDDVEAWIELAQILEQTDIQGALSAYGTATRILQEKVQADVPPEILNNVGALHFRLGNLGEAKKYFLASLDRAKAEAEHDEHYYNAISVTTSYNLARLYEAMCEFHEAEKLYKNILREHPNYVDCYLRLGAMARDKGNFYEASDWFKEALQINQDHPDAWSLIGNLHLAKQEWGPGQKKFERILKQPATQSDTYSMLALGNVWLQTLHQPTRDREKEKRHQDRALAIYKQVLRNDAKNLYAANGIGAVLAHKGYFREARDVFAQVREATADISDVWLNLAHIYVEQKQYISAVQMYENCLRKFYKHQNTEVVLYLARALFKCGKLQECKQTLLKARHVAPSDTVLMFNVALVLQRLATSVLKDEKSNLKEVLNAVKELELAHRYFSYLSKVGDKMRFDLALAASEARQCSDLLSQAQYHVARARKQDEEERELRAKQEQEKELLRQKLLKEQEEKRLREKEEQKKLLEQRAQYVEKTKNILMFTGETEATKEKKRGGGGGRRSKKGGEFDEFVNDDTDDDLPVSKKKKRRKGSGSEQEGEEEEGGERKKKRRRRPPKGEEGSEEEETENGPKPKKRRPPRAEKKKAPKPERLPPSMKGKIKSKAIISSSDDSSDEDKLKIADEGHPRNSNSDSDDDERPNRRASSESDSDDNQNKSGSEAGSPRRSGRQESDEDSDSDQPSRKRRRSGSEQSDNESVQSGRSPSGASENENDSRPASPSAESDHESEQGSDNEGSGQGSGNESEPEGSNNEASDRGSEHGSDDSD 2FB84564F1BEFD79 cdc73_human Parafibromin CDC73 C1orf28 HRPT2 Cell division cycle protein 73 homolog Hyperparathyroidism 2 protein protein protein human Homo sapiens Human MADVLSVLRQYNIQKKEIVVKGDEVIFGEFSWPKNVKTNYVVWGTGKEGQPREYYTLDSILFLLNNVHLSHPVYVRRAATENIPVVRRPDRKDLLGYLNGEASTSASIDRSAPLEIGLQRSTQVKRAADEVLAEAKKPRIEDEECVRLDKERLAARLEGHKEGIVQTEQIRSLSEAMSVEKIAAIKAKIMAKKRSTIKTDLDDDITALKQRSFVDAEVDVTRDIVSRERVWRTRTTILQSTGKNFSKNIFAILQSVKAREEGRAPEQRPAPNAAPVDPTLRTKQPIPAAYNRYDQERFKGKEETEGFKIDTMGTYHGMTLKSVTEGASARKTQTPAAQPVPRPVSQARPPPNQKKGSRTPIIIIPAATTSLITMLNAKDLLQDLKFVPSDEKKKQGCQRENETLIQRRKDQMQPGGTAISVTVPYRVVDQPLKLMPQDWDRVVAVFVQGPAWQFKGWPWLLPDGSPVDIFAKIKAFHLKYDEVRLDPNVQKWDVTVLELSYHKRHLDRPVFLRFWETLDRYMVKHKSHLRF DIP protein Q6P1J9 original sequence version: 75 DIP protein Q6P1J9 original sequence version: 133 894A7448DBC0E793 q6xzl8_mouse Histone-lysine N-methyltransferase, H3 lysine-79 specific Dot1l protein protein mouse Mus musculus Mouse MGEKLELRLKSPVGAEPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLAMENYVLIDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSNGLLRHILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTEDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTIDRTILENYFSSLKNPKLREEQEAARRRQQRENKSNATTPTKVPESKAAATEAPADSGAEEEKSGVATVKKPSPSKARKKKLNKKGRKMAGRKRGRPKKMSAASAERKSKKSQSTLDLLHSPPPAPPSASPQDAYRAPHSPFYQLPPSTQLHSPNPLLVAPTPPALQKLLESFRIQYLQFLAYTKTPQYKANLQQLLDQEKEKNTQLLGTAQQLFGHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEKDNSELRSQSLRLLRARCEELRLDWSTLSLENLRKEKQALRSQISEKQRHCLELQISIVELEKTQRQQELLQLKSCVPPDDALSLHLRGKGALGRELEADAGRLRLELDCAKISLPHLSSMSPELSMNGHAASYELCNAASRPSSKQNTPQYLASPLDQEVVPCTPSHSGRPRLEKLSGLALPDYTRLSPAKIVLRRHLSQDHTGASKAATSEPHPRPEHPKESSLPYQSPGLSNSMKLSPQDPPLASPATSPLTSEKGSEKGVKERAYSSHGETITSLPVSIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVPQPRDSSATLEKQTGASAHGAGGAGAGSRSLAVAPTGFYAGSVAISGALASSPAPLASGMESAVFDESSGPSSLFATMGSRSTPPQHPPLLSQSRNSGPASPAHQLTASPRLSVTTQGSLPDTSKGELPSDPAFSDPESEAKRRIVFSISVGASSKQSPSTRHSPLTSGTRGDCVQSHGQDSRKRSRRKRASAGTPSLSTGVSPKRRALPTVAGLFTQSSGSPLNLNSMVSNINQPLEITAISSPESSLKSSPTPYQDHDQPPVLRKERPLGLTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLVGRKSAPSSEPINSSKWKSTFSPISDLGLAKAVDSPLQAGSALSHSPLFSFRPSLEEPAAEAKLPTHPRKSFAGSLGAAEGPSPGTNPPNGLAFSGGLAADLGLHSFNDGASLSHKGPDVTGLSASLSFPSQRGKDSTTEANPFLSRRQPEGLGGLKGEGNANKESGESLPLCGPSDKASLPHGSRASKGRDRELDFKGGHNLFISAAAVPPGGLLGGPGLVTVASSAGSATPTAQAPRPFLSTFAPGPQFTLGPMSLQANLGSVAGSSVLQSLFSTVPAAAGLVHVSSTATRLTNSHTMGSFSSGVAGGTVGGN DIP protein Q6XZL8 original sequence version: 51 FD6CA93249FF9161 q2q440_human protein protein human Homo sapiens Human FLCASSGHVEDANKESSKTS C2131CFE37A4CEAD paf1_mouse RNA polymerase II-associated factor 1 homolog Paf1 protein protein mouse Mus musculus Mouse MAPTIQTQAQREDGHRPNSHRTLPERSGVVCRVKYCNSLPDIPFDPKFITYPFDQNRFVQYKATSLEKQHKHDLLTEPDLGVTIDLINPDTYRIDPNVLLDPADEKLLEEEIQAPTSSKRSQQHAKVVPWMRKTEYISTEFNRYGISNEKPEVKIGVSVKQQFTEEEIYKDRDSQITAIEKTFEDAQKSISQHYSKPRVTPVEVMPVFPDFKMWINPCAQVIFDSDPAPKDTSGAAALEMMSQAMIRGMMDEEGNQFVAYFLPVEETLKKRKRDQEEEMDYAPDDVYDYKIAREYNWNVKNKASKGYEENYFFIFREGDGVYYNELETRVRLSKRRAKAGVQSGTNALLVVKHRDMNEKELEAQEARKAQLENHEPEEEEEEEMEAEEKEAGGSDEEQEKGSSSEKEGSEDEHSGSESDREEGDRDEASDKSGSGEDESSEDEARAARDKEEIFGSDADSEDDADSDDEDRGQAHRGSDNDSDSGSDGGGQRSRSQSRSRSRSASPFPSGSEHSAQEDGSEAAASDSSEADSDSD 7A5EAB1284988070 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 cdc73_mouse Parafibromin Cdc73 Cell division cycle protein 73 homolog Hyperparathyroidism 2 protein homolog protein protein mouse Mus musculus Mouse MADVLSVLRQYNIQKKEIVVKGDEVIFGEFSWPKNVKTNYVVWGTGKEGQPREYYTLDSILFLLNNVHLSHPVYVRRAATENIPVVRRPDRKDLLGYLNGEASTSASIDRSAPLEIGLQRSTQVKRAADEVLAEAKKPRIEDEECVRLDKERLAARLEGHKEGIVQTEQIRSLSEAMSVEKIAAIKAKIMAKKRSTIKTDLDDDITALKQRSFVDAEVDVTRDIVSRERVWRTRTTILQSTGKNFSKNIFAILQSVKAREEGRAPEQRPAPNAAPVDPTLRTKQPIPAAYNRYDQERFKGKEETEGFKIDTMGTYHGMTLKSVTEGASARKTQTPAAQPVPRPVSQARPPPNQKKGSRTPIIIIPAATTSLITMLNAKDLLQDLKFVPSDEKKKQGCQRENETLIQRRKDQMQPGGTAISVTVPYRVVDQPLKLMPQDWDRVVAVFVQGPAWQFKGWPWLLPDGSPVDIFAKIKAFHLKYDEVRLDPNVQKWDVTVLELSYHKRHLDRPVFLRFWETLDRYMVKHKSHLRF 894A7448DBC0E793 enl_human Protein ENL MLLT1 ENL LTG19 YEATS1 YEATS domain-containing protein 1 protein protein human Homo sapiens Human MDNQCTVQVRLELGHRAQLRKKPTTEGFTHDWMVFVRGPEQCDIQHFVEKVVFWLHDSFPKPRRVCKEPPYKVEESGYAGFIMPIEVHFKNKEEPRKVCFTYDLFLNLEGNPPVNHLRCEKLTFNNPTTEFRYKLLRAGGVMVMPEGADTVSRPSPDYPMLPTIPLSAFSDPKKTKPSHGSKDANKESSKTSKPHKVTKEHRERPRKDSESKSSSKELEREQAKSSKDTSRKLGEGRLPKEEKAPPPKAAFKEPKMALKETKLESTSPKGGPPPPPPPPPRASSKRPATADSPKPSAKKQKKSSSKGSRSAPGTSPRTSSSSSFSDKKPAKDKSSTRGEKVKAESEPREAKKALEVEESNSEDEASFKSESAQSSPSNSSSSSDSSSDSDFEPSQNHSQGPLRSMVEDLQSEESDEDDSSSGEEAAGKTNPGRDSRLSFSDSESDNSADSSLPSREPPPPQKPPPPNSKVSGRRSPESCSKPEKILKKGTYDKAYTDELVELHRRLMALRERNVLQQIVNLIEETGHFNVTNTTFDFDLFSLDETTVRKLQSCLEAVAT A8480BA0F8742173 hoxa9_mouse_gene Mouse HOXA9 gene gene gene mouse Mus musculus Mouse mll_enl_human_protein Fusion of human MLL (N-terminal region) with human ENL C-terminal residues 373-559 protein protein human Homo sapiens Human An amino acid sequence which is not represented in UniProt ccnt1_human Cyclin-T1 CCNT1 protein protein human Homo sapiens Human MEGERKNNNKRWYFTREQLENSPSRRFGVDPDKELSYRQQAANLLQDMGQRLNVSQLTINTAIVYMHRFYMIQSFTQFPGNSVAPAALFLAAKVEEQPKKLEHVIKVAHTCLHPQESLPDTRSEAYLQQVQDLVILESIILQTLGFELTIDHPHTHVVKCTQLVRASKDLAQTSYFMATNSLHLTTFSLQYTPPVVACVCIHLACKWSNWEIPVSTDGKHWWEYVDATVTLELLDELTHEFLQILEKTPNRLKRIWNWRACEAAKKTKADDRGTDEKTSEQTILNMISQSSSDTTIAGLMSMSTSTTSAVPSLPVSEESSSNLTSVEMLPGKRWLSSQPSFKLEPTQGHRTSENLALTGVDHSLPQDGSNAFISQKQNSKSVPSAKVSLKEYRAKHAEELAAQKRQLENMEANVKSQYAYAAQNLLSHHDSHSSVILKMPIEGSENPERPFLEKADKTALKMRIPVAGGDKAASSKPEEIKMRIKVHAAADKHNSVEDSVTKSREHKEKHKTHPSNHHHHHNHHSHKHSHSQLPVGTGNKRPGDPKHSSQTSNLAHKTYSLSSSFSSSSSTRKRGPSEETGGAVFDHPAKIAKSTKSSSLNFSFPSLPTMGQMPGHSSDTSGLSFSQPSCKTRVPHSKLDKGPTGANGHNTTQTIDYQDTVNMLHSLLSAQGVQPTQPTAFEFVRPYSDYLNPRSGGISSRSGNTDKPRPPPLPSEPPPPLPPLPK DIP protein O60563 original sequence version: 85 DIP protein O60563 original sequence version: 79 DIP protein O60563 original sequence version: 98 DIP protein O60563 original sequence version: 102 DIP protein O60563 original sequence version: 164 DIP protein O60563 original sequence version: 125 DIP protein O60563 original sequence version: 103 4637EFB2DDEDFE13 leo1_mouse RNA polymerase-associated protein LEO1 Leo1 Gm185 protein protein mouse Mus musculus Mouse MADMEDLFGSEAESEAERKDSESESDSDSDQDNGASGSNASGSESDQDDRGDSGQPSNKELFGDDSEEEGASHHSGSDNHSERSDNRSEASERSDHEDNEPSDEDQHSGSEAHNDDDDEGHRSDEGSRHSEAEGSEKAQSDDEKWDGEDKSDQSDDEKLQNSDDEDREQGSDEDKLQNSDDDEEKMQNTDDEDRAQISDDDRQQLSEEEKGNSDDEHPVASDNDEEKQNSDDEDQPQVSDEEKMQNSDDERPQVSDEDGRRSDGEEEQDQKSESARGSDSEDEVLRLKRKNAIPSDSEADSDTEVPKDNNGTMDLFGGADDISSGSDGEDKPPTPGQPVDENGLPQDQQEEEPIPETRIEVEIPKVNTDLGNDLYFVKLPNFLSVEPRPFDPQYYEDEFEDEEMLDEEGRTRLKLKVENTIRWRIRRDEEGNEIKESNARIVKWSDGSMSLHLGNEVFDVYKAPLQGDHNHLFIRQGTGLQGQAVFKTKLTFRPHSTDSATHRKMTLSLADRCSKTQKIRILPMAGRDPECQRTEMIKKEEERLRASIRRESQQRRMREKQHQRGLSASYLEPDRYDEEEEGEESVSLAAIKNRYKGGIREERARIYSSDSDEGSEEDKAQRLLKAKKLNSDEEGESSGKRKAEDDDKANKKHKKYVISDEEEEEDD 73A9E04DB6ACFFDB q8cj76_mouse Mllt1 protein protein mouse Mus musculus Mouse MDNQCTVQVKLELGHRAQLRKKPTTEGFTHDWMVFVRGPEQCDIQHFVEKVIFRLHDSFPKPKRVCKEPPYKVEESGYAGFIMLIEVYFKNKEEPRKVCFTYDLFLNLEGNPPVNHLRCEKLTFNNPTTEFRCKLLMAGGVMVMPEGADTVSRPSPDYPMLPTIPLSAFSDPKKNKPSHGSKDANKESGKASKPHKVAREHRERPRKDSESRSCSKEPEREPKSAKDAARKLPKEEKAPVPKAAFKEPKMALKETKLESLSPKGVPQPPTLPKASSKRPAATDSPKLSAKKPKKSGSKGTRRAPGTSPRASSFPDKKVARDKNSKGDKGKAESEPREAKRTLQTEDSNSEDEASFRSESAQSSPANASSSSDSSSDSDFEPSQNHSQGPLRSMVEDLQSEGSDEDDSSSGEENTRKANPGRESRLSFSDSESDNSADSCLPGREPLPPQKPPPPSSKVSGRRSPEPCSKPEKMLKKATYDKAYTDELVELHRRLMALRERNVLQQIVNLIEETGHFNVTNTTFDFDLFFLDESTVRKLQSCLEAVAT 2F0DFF7269903381 mll_af9_human_protein MLL-AF9 fusion protein protein protein human Homo sapiens Human MAHSCRWRFPARPGTTGGGGGGGRRGLGGAPRQRVPALLLPPGPPVGGGGPGAPPSPPAVAAAAAAAGSSGAGVPGGAAAASAASSSSASSSSSSSSSASSGPALLRVGPGFDAALQVSAAIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRSPTRSPSVKTSPRKPRGRPRSGSDRNSAILSDPSVFSPLNKSETKSGDKIKKKDSKSIEKKRGRPPTFPGVKIKITHGKDISELPKGNKEDSLKKIKRTPSATFQQATKIKKLRAGKLSPLKSKFKTGKLQIGRKGVQIVRRRGRPPSTERIKTPSGLLINSELEKPQKVRKDKEGTPPLTKEDKTVVRQSPRRIKPVRIIPSSKRTDATIAKQLLQRAKKGAQKKIEKEAAQLQGRKVKTQVKNIRQFIMPVVSAISSRIIKTPRRFIEDEDYDPPIKIARLESTPNSRFSAPSCGSSEKSSAASQHSSQMSSDSSRSSSPSVDTSTDSQASEEIQVLPEERSDTPEVHPPLPISQSPENESNDRRSRRYSVSERSFGSRTTKKLSTLQSAPQQQTSSSPPPPLLTPPPPLQPASSISDHTPWLMPPTIPLASPFLPASTAPMQGKRKSILREPTFRWTSLKHSRSEPQYFSSAKYAKEGLIRKPIFDNFRPPPLTPEDVGFASGFSASGTAASARLFSPLHSGTRFDMHKRSPLLRAPRFTPSEAHSRIFESVTLPSNRTSAGTSSSGVSNRKRKRKVFSPIRSEPRSPSHSMRTRSGRLSSSELSPLTPPSSVSSSLSISVSPLATSALNPTFTFPSHSLTQSGESAEKNQRPRKQTSAPAEPFSSSSPTPLFPWFTPGSQTERGRNKDKAPEELSKDRDADKSVEKDKSRERDREREKENKRESRKEKRKKGSEIQSSSALYPVGRVSKEKVVGEDVATSSSAKKATGRKKSSSHDSGTDITSVTLGDTTAVKTKILIKKGRGNLEKTNLDLGPTAPSLEKEKTLCLSTPSSSTVKHSTSSIGSMLAQADKLPMTDKRVASLLKKAKAQLCKIEKSKSLKQTDQPKAQGQESDSSETSVRGPRIKHVCRRAAVALGRKRAVFPDDMPTLSALPWEEREKILSSMGNDDKSSIAGSEDAEPLAPPIKPIKPVTRNKAPQEPPVKKGRRSRRCGQCPGCQVPEDCGVCTNCLDKPKFGGRNIKKQCCKMRKCQNLQWMPSKAYLQKQAKAVKKKEKKSKTSEKKDSKESSVVKNVVDSSQKPTPSAREDPAPKKSSSEPPPRKPVEEKSEEGNVSAPGPESKQATTPASRKSSKQVSQPALVIPPQPPTTGPPRKEVPKTTPSEPKKKQPPPPESGPEQSKQKKVAPRPSIPVKQKPKEKEKPPPVNKQENAGTLNILSTLSNGNSSKQKIPADKSPIKQSKSDKQIKNGECDKAYLDELVELHRRLMTLRERHILQQIVNLIEETGHFHITNTTFDFDLCSLDKTTVRKLQSYLETSGTS An amino acid sequence which is not represented in UniProt MLL derived protein of the protein corresponds to the CxxC-RD2 portion of the parent protein, only. paf1_human RNA polymerase II-associated factor 1 homolog PAF1 PD2 Pancreatic differentiation protein 2 protein protein human Homo sapiens Human MAPTIQTQAQREDGHRPNSHRTLPERSGVVCRVKYCNSLPDIPFDPKFITYPFDQNRFVQYKATSLEKQHKHDLLTEPDLGVTIDLINPDTYRIDPNVLLDPADEKLLEEEIQAPTSSKRSQQHAKVVPWMRKTEYISTEFNRYGISNEKPEVKIGVSVKQQFTEEEIYKDRDSQITAIEKTFEDAQKSISQHYSKPRVTPVEVMPVFPDFKMWINPCAQVIFDSDPAPKDTSGAAALEMMSQAMIRGMMDEEGNQFVAYFLPVEETLKKRKRDQEEEMDYAPDDVYDYKIAREYNWNVKNKASKGYEENYFFIFREGDGVYYNELETRVRLSKRRAKAGVQSGTNALLVVKHRDMNEKELEAQEARKAQLENHEPEEEEEEEMETEEKEAGGSDEEQEKGSSSEKEGSEDEHSGSESEREEGDRDEASDKSGSGEDESSEDEARAARDKEEIFGSDADSEDDADSDDEDRGQAQGGSDNDSDSGSNGGGQRSRSHSRSASPFPSGSEHSAQEDGSEAAASDSSEADSDSD DIP protein Q8N7H5 original sequence version: 43 DIP protein Q8N7H5 original sequence version: 100 756F800AA64255D6 leo1_human RNA polymerase-associated protein LEO1 LEO1 RDL Replicative senescence down-regulated leo1-like protein protein protein human Homo sapiens Human MADMEDLFGSDADSEAERKDSDSGSDSDSDQENAASGSNASGSESDQDERGDSGQPSNKELFGDDSEDEGASHHSGSDNHSERSDNRSEASERSDHEDNDPSDVDQHSGSEAPNDDEDEGHRSDGGSHHSEAEGSEKAHSDDEKWGREDKSDQSDDEKIQNSDDEERAQGSDEDKLQNSDDDEKMQNTDDEERPQLSDDERQQLSEEEKANSDDERPVASDNDDEKQNSDDEEQPQLSDEEKMQNSDDERPQASDEEHRHSDDEEEQDHKSESARGSDSEDEVLRMKRKNAIASDSEADSDTEVPKDNSGTMDLFGGADDISSGSDGEDKPPTPGQPVDENGLPQDQQEEEPIPETRIEVEIPKVNTDLGNDLYFVKLPNFLSVEPRPFDPQYYEDEFEDEEMLDEEGRTRLKLKVENTIRWRIRRDEEGNEIKESNARIVKWSDGSMSLHLGNEVFDVYKAPLQGDHNHLFIRQGTGLQGQAVFKTKLTFRPHSTDSATHRKMTLSLADRCSKTQKIRILPMAGRDPECQRTEMIKKEEERLRASIRRESQQRRMREKQHQRGLSASYLEPDRYDEEEEGEESISLAAIKNRYKGGIREERARIYSSDSDEGSEEDKAQRLLKAKKLTSDEEGEPSGKRKAEDDDKANKKHKKYVISDEEEEDDD DIP protein Q8WVC0 original sequence version: 66 EB405BE0EDA7E0B0 cxxc-rd2 4 12 unspecified role unspecified role prey prey 25 unspecified role unspecified role prey prey 26 unspecified role unspecified role prey prey 8 unspecified role unspecified role prey prey 16 unspecified role unspecified role bait bait cxxc_rd2_ domain CxxC-RD2 region including a nuclear localization signal (NLS). sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n terminus 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 9 unspecified role unspecified role prey prey association association Fig 1B. Multiple peptides corresponding to subunits of PAFc were identified. Figure legend for 1B states "Flag/HA-tagged CxxC-RD2 was expressed in 293 cells" - but I can find no reference to an HA-tag anywhere in the paper (nor in Supplement). cxxc-rd2-1 1 16 unspecified role unspecified role bait bait cxxc_rd2_ domain CxxC-RD2 region including a nuclear localization signal (NLS). sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 25 unspecified role unspecified role prey prey 9 unspecified role unspecified role prey prey 12 unspecified role unspecified role prey prey 26 unspecified role unspecified role prey prey 8 unspecified role unspecified role prey prey association association Fig 1C, S1B. Each of the five PAFc subunits identified by mass spectrometry (PAF1, CDC73, CTR9, LEO1, and WDR61) was confirmed to coimmunoprecipitate with Myc-tagged CxxC-RD2 by western blotting in 293 cells. Immunoprecipitation was preserved in the presence of Benzonase indicating the interaction is not DNA dependent. Immunoprecipitation was preserved in the presence of Benzonase indicating the interaction is not DNA dependent. mll_af9-wdr61 1 24 unspecified role unspecified role bait bait region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 8 unspecified role unspecified role prey prey 26 unspecified role unspecified role prey prey 12 unspecified role unspecified role prey prey 25 unspecified role unspecified role prey prey 9 unspecified role unspecified role prey prey association association Fig 1D. The lysate was treated with benzonase to digest DNA, indicating the PAFc interaction with CxxC-RD2 is DNA independent. Myc-tagged MLL CxxC-RD2-AF9 (MLL amino acids 1116-1397; AF9 - C terminal amino acids 276-568) interacts with PAFc subunits, showing that PAFc binding to CxxC-RD2 is maintained in the presence of the AF9 translocation partner. mll_af9-ctr9-1 1 24 unspecified role unspecified role bait bait n terminus 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 12 unspecified role unspecified role prey prey 25 unspecified role unspecified role prey prey 8 unspecified role unspecified role prey prey 9 unspecified role unspecified role prey prey association association Fig 1E. These experiments show the MLL-PAFc interaction is maintained both in the context of full-length (MLLN) as well as in the context of a leukemogenic MLL fusion protein. (MLL amino acids 1-1396;AF9 C terminal amino acids 276-568). mll-ctr9-3 1 9 unspecified role unspecified role prey prey 8 unspecified role unspecified role prey prey 16 unspecified role unspecified role bait bait 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 25 unspecified role unspecified role prey prey association association Fig 1F. These experiments show the MLL-PAFc interaction is maintained both in the context of full-length (MLLN) as well as in the context of a leukemogenic MLL fusion protein. (MLL amino acids 1-1396;AF9 C terminal amino acids 276-568). I found the amino acid nos for MLL in Muntean-2008, on Figure one. (AF9 as before from Muntean 2008 Supplement). Can find no definite info to confirm the flag tag is N terminal in the 2010 or 2008 paper. mll-paf 2 16 unspecified role unspecified role bait bait cxxc_rd2_ domain CxxC-RD2 region including a nuclear localization signal (NLS). sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain his-mocr tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 25 unspecified role unspecified role prey prey region His-MOCR tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) physical association physical association Fig 2C. PAFc co-immunoprecipitated with a small fragment of MLL N-terminal to the CxxC domain (amino acids 1115-1154). MLL CxxC-RD2 and RD2 regions specifically associated with CTR9-C, and with a weak interaction detected between RD2 and CDC73. mll-cdc73 2 12 unspecified role unspecified role prey prey region mbp tag maltose binding protein tag maltose binding protein tag maltose binding protein tag mbp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region 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 ecoli Escherichia coli (strain K12) 16 unspecified role unspecified role bait bait rd2_ domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region His-MOCR tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) physical association physical association Fig 2C. PAFc co-immunoprecipitated with a small fragment of MLL N-terminal to the CxxC domain (amino acids 1115-1154). MLL CxxC-RD2 and RD2 regions specifically associated with CTR9-C, and with a weak interaction detected between RD2 and CDC73. mll-ctr9-2 2 8 unspecified role unspecified role prey prey c terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region 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 region mbp tag maltose binding protein tag maltose binding protein tag maltose binding protein tag mbp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 16 unspecified role unspecified role bait bait region His-MOCR tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined rd2_ domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 81 86 physical association physical association Fig 2C. PAFc co-immunoprecipitated with a small fragment of MLL N-terminal to the CxxC domain (amino acids 1115-1154). MLL CxxC-RD2 and RD2 regions specifically associated with CTR9-C, and with a weak interaction detected between RD2 and CDC73. mll_af9-ctr9 1 25 unspecified role unspecified role prey prey 12 unspecified role unspecified role prey prey 8 unspecified role unspecified role prey prey 24 unspecified role unspecified role bait bait n terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined association association Fig 3B, S4A. Using (N-terminal) Myc-tagged MLL CxxC-RD2-(C terminal)AF9 (C terminal amino acids 276-568) deletion mutants there was a sharp decrease in the MLL-PAFc interaction when C-terminal deletions were made past amino acid 1299. Residual low level binding of PAFc with proteins deleted at aa 1209 or aa 1258 was detected. Association of DOT1L and the pTEFb component, cyclin T1, with AF9 is maintained in all the deletion constructs used (Figure S4A). mll_af9-leo1 1 9 unspecified role unspecified role prey prey 12 unspecified role unspecified role prey prey 25 unspecified role unspecified role prey prey 26 unspecified role unspecified role prey prey 24 unspecified role unspecified role bait bait n terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined association association Fig 3D, S4A. The amino acids for the AF9 part of this fusion protein were (eventually) found in Muntean-2008 Supplement. According to the Manual I must put this is a comment rather than Full Name. Experiments using deletion constructs [(N-terminal) Myc-tagged MLL CxxC-RD2-(C terminal)AF9 (C terminal amino acids 276-568)] that begin with MLL aa 1180 (deletion of the proximal site of PAFc interaction) showed PAFc interaction with MLL is completely eliminated with deletions beyond aa 1299. Text states "Experiments using deletion constructs that begin with MLL aa 1180 " - but I cannot see that anything begins with ~1180...(1209 looks the nearest) Association of DOT1L and the pTEFb component, cyclin T1, with AF9 is maintained in all the deletion constructs used (Figure S4A). I have not entered the S4A data as a separate interaction (with HA_DOT1L and cyclin T1) - though I could have done, but does not seem relevant. hoxa9-paf1 7 25 unspecified role unspecified role bait bait 10 unspecified role unspecified role prey prey association association Fig 7D. A significant decrease in binding was observed of CDC73, PAF1, and LEO1 in both the promoter and coding region of the HOXA9 locus following knockdown of PAF complex components. hox9a-cdc73 7 12 unspecified role unspecified role bait bait 10 unspecified role unspecified role prey prey association association Fig 7D. A significant decrease in binding was observed of CDC73, PAF1, and LEO1 in both the promoter and coding region of the HOXA9 locus following knockdown of PAF complex components. hox9a-leo1 7 10 unspecified role unspecified role prey prey 26 unspecified role unspecified role bait bait association association Fig 7D. A significant decrease in binding was observed of CDC73, PAF1, and LEO1 in both the promoter and coding region of the HOXA9 locus following knockdown of PAF complex components. hox9a-mllc 7 16 unspecified role unspecified role bait bait c terminal sufficient to bind sufficient binding region sufficient to bind undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 10 unspecified role unspecified role prey prey association association Fig 7D. PAFc knockdown resulted in a marked decrease in wild-type MLL binding compared with mock treated cells. No info seems to be available about the exact aa nos of 'MLLC' - I would not like to enter it as the C180 C terminal cleavage product (PRO_0000390950)unless it is stated to be so. - unless you think otherwise? enl-cdc73 6 18 unspecified role unspecified role bait bait 12 unspecified role unspecified role prey prey 14 unspecified role unspecified role prey prey physical association physical association Fig S1C. Immunoprecipitation of endogenous MLL-ENL from KOPN8 cells and western blotting for the PAF component CDC73 shows interaction of endogenous MLL-ENL with endogenous PAFc. rd2-ctr9-1 3 16 unspecified role unspecified role prey prey his-mocr tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined rd2_ domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role bait bait c terminal sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region mbp tag maltose binding protein tag maltose binding protein tag maltose binding protein tag mbp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region 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 ecoli Escherichia coli (strain K12) 120 122 physical association physical association Fig S2 A+B. PAFc co-immunoprecipitated with a small fragment of MLL N-terminal to the CxxC domain (amino acids 1115-1154). MLL CxxC-RD2 and RD2 regions specifically associated with CTR9-C, and with a weak interaction detected between RD2 and CDC73. These interactions were confirmed by reciprocal MBP pull down of CDC73, CTR9-N and CTR9-C, which showed that the MLL CxxC-RD2 and RD2 regions specifically associated with CTR9-C, along with a weak interaction detected between RD2 and CDC73 (Figure S2). rd2-cdc73-1 3 16 unspecified role unspecified role prey prey rd2_ domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain his-mocr tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 12 unspecified role unspecified role bait bait region mbp tag maltose binding protein tag maltose binding protein tag maltose binding protein tag mbp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region 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 ecoli Escherichia coli (strain K12) physical association physical association Fig S2 These interactions were confirmed by reciprocal MBP pull down of CDC73, CTR9-N and CTR9-C, which showed that the MLL CxxC-RD2 and RD2 regions specifically associated with CTR9-C, along with a weak interaction detected between RD2 and CDC73 (Figure S2). hoxa9-paf1-1 5 20 unspecified role unspecified role ancillary ancillary 15 unspecified role unspecified role bait bait 19 unspecified role unspecified role prey prey association association Fig 6B. Co-localization of MLL-ENL and PAFc at the Meis1 and Hoxa9 loci in MLL-ENL transfected cells, with minimal binding seen in E2A-HLF cells. MLL-ENL binding is somewhat more abundant upstream and downstream of the transcriptional start site of the Hoxa9 locus. hoxa9-leo1 5 22 unspecified role unspecified role bait bait 19 unspecified role unspecified role prey prey 20 unspecified role unspecified role ancillary ancillary association association Fig 6B. Co-localization of MLL-ENL and PAFc at the Meis1 and Hoxa9 loci in MLL-ENL transfected cells, with minimal binding seen in E2A-HLF cells. MLL-ENL binding is somewhat more abundant upstream and downstream of the transcriptional start site of the Hoxa9 locus. hoxa9-cdc73 5 17 unspecified role unspecified role bait bait 19 unspecified role unspecified role prey prey 20 unspecified role unspecified role ancillary ancillary association association Fig 6B. Co-localization of MLL-ENL and PAFc at the Meis1 and Hoxa9 loci in MLL-ENL transfected cells, with minimal binding seen in E2A-HLF cells. MLL-ENL binding is somewhat more abundant upstream and downstream of the transcriptional start site of the Hoxa9 locus. I have not added an interaction involving CDC73 in E2A-HLF cells at the HoxA9 locus - though this looks to be rather more than the "minimal" stated in the text above. hoxa9-ctr9 5 11 unspecified role unspecified role bait bait 20 unspecified role unspecified role ancillary ancillary 19 unspecified role unspecified role prey prey association association Fig 6B. Co-localization of MLL-ENL and PAFc at the Meis1 and Hoxa9 loci in MLL-ENL transfected cells, with minimal binding seen in E2A-HLF cells. MLL-ENL binding is somewhat more abundant upstream and downstream of the transcriptional start site of the Hoxa9 locus. hoxa9-enl 5 19 unspecified role unspecified role prey prey 23 unspecified role unspecified role bait bait 20 unspecified role unspecified role ancillary ancillary association association Fig 6B. Co-localization of MLL-ENL and PAFc at the Meis1 and Hoxa9 loci in MLL-ENL transfected cells, with minimal binding seen in E2A-HLF cells. MLL-ENL binding is somewhat more abundant upstream and downstream of the transcriptional start site of the Hoxa9 locus. I have entered Q8CJ76 for Mouse ENL (there are 4 results searching on the mouse Ensembl MLLT1 gene ID) - this entry mentions "Leukemia in the "name" - though so does Q9EPX7 - no obvious reason to chose either entry - they both have the same reference. (antibody used to ENL was a "gift"). I have entered a Data Processing comment. mll_af9-dot1l-cyt1 1 21 unspecified role unspecified role prey prey 24 unspecified role unspecified role bait bait n terminus myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 13 unspecified role unspecified role prey prey region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined association association Fig S4A. Experiments using deletion constructs [(N-terminal) Myc-tagged MLL CxxC-RD2-(C terminal)AF9 (C terminal amino acids 276-568)] that begin with MLL aa 1180 (deletion of the proximal site of PAFc interaction) showed PAFc interaction with MLL is completely eliminated with deletions beyond aa 1299. Association of DOT1L and the pTEFb component, cyclin T1, with AF9 was maintained in all the deletion constructs used. Association of DOT1L and the pTEFb component, cyclin T1, with AF9 is maintained in all the deletion constructs used (Figure S4A). HA-dot1l not known to be human - authors contacted. 30/7/10 = Authors state this construct is MOUSE!