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/ Proapoptotic function of the retinoblastoma tumor suppressor protein. Proapoptotic function of the retinoblastoma tumor suppressor protein. Cancer Cell (1535-6108) 2009 imex curation Ianari A., Natale T., Calo E., Ferretti E., Alesse E., Screpanti I., Haigis K., Gulino A., Lees JA. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer jalees@mit.edu 29-Mar-2010: Contacted by JYOTI. orchard Only protein-protein interactions 7 human-t98g Human caucasian glioblastoma line T98G t98g Human Caucasian glioblastoma T98G anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Ianari A., Natale T., Calo E., Ferretti E., Alesse E., Screpanti I., Haigis K., Gulino A., Lees JA. Apoptosis - Interactions involving proteins with a function related to apoptosis jalees@mit.edu Accepted 2010-MAR-23 by ORCHARD. 29-Mar-2010: Contacted by JYOTI. Cancer Cell (1535-6108) 2009 orchard Only protein-protein interactions 7 imex curation Proapoptotic function of the retinoblastoma tumor suppressor protein. Proapoptotic function of the retinoblastoma tumor suppressor protein. Cancer Cell (1535-6108) 2009 imex curation Ianari A., Natale T., Calo E., Ferretti E., Alesse E., Screpanti I., Haigis K., Gulino A., Lees JA. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer jalees@mit.edu 29-Mar-2010: Contacted by JYOTI. orchard Only protein-protein interactions 7 human-imr_90 Homo sapiens embryonic fetal lung fibroblast imr_90 human, Caucasian female 16 fetal weeks; Tissue: lung, embryonic fibroblast ch-ip chromatin immunoprecipitation assay ch-ip primer specific pcr primer specific pcr Ianari A., Natale T., Calo E., Ferretti E., Alesse E., Screpanti I., Haigis K., Gulino A., Lees JA. Apoptosis - Interactions involving proteins with a function related to apoptosis Human IMR-90 cells expressing the murine ecotropic receptor were used. PMID: 15741165 gives the source of the Adenovirus E1A protein as strain Ad5. jalees@mit.edu Accepted 2010-MAR-23 by ORCHARD. 29-Mar-2010: Contacted by JYOTI. Cancer Cell (1535-6108) 2009 orchard Only protein-protein interactions 7 imex curation Proapoptotic function of the retinoblastoma tumor suppressor protein. Proapoptotic function of the retinoblastoma tumor suppressor protein. Cancer Cell (1535-6108) 2009 imex curation Ianari A., Natale T., Calo E., Ferretti E., Alesse E., Screpanti I., Haigis K., Gulino A., Lees JA. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer jalees@mit.edu 29-Mar-2010: Contacted by JYOTI. orchard Only protein-protein interactions 7 human-t98g Human caucasian glioblastoma line T98G t98g Human Caucasian glioblastoma T98G ch-ip chromatin immunoprecipitation assay ch-ip primer specific pcr primer specific pcr Ianari A., Natale T., Calo E., Ferretti E., Alesse E., Screpanti I., Haigis K., Gulino A., Lees JA. Apoptosis - Interactions involving proteins with a function related to apoptosis reChIP using an antibody to acetyl-H4, a marker of transcriptional activation. jalees@mit.edu Accepted 2010-MAR-23 by ORCHARD. 29-Mar-2010: Contacted by JYOTI. Cancer Cell (1535-6108) 2009 orchard Only protein-protein interactions 7 imex curation Proapoptotic function of the retinoblastoma tumor suppressor protein. Proapoptotic function of the retinoblastoma tumor suppressor protein. Cancer Cell (1535-6108) 2009 imex curation Ianari A., Natale T., Calo E., Ferretti E., Alesse E., Screpanti I., Haigis K., Gulino A., Lees JA. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer jalees@mit.edu 29-Mar-2010: Contacted by JYOTI. orchard Only protein-protein interactions 7 human-u2-os Human U2-OS osteosarcoma cell line u2-os U2-OS osteocaroma cell line Not in CAPRI and no primary literature reference anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Ianari A., Natale T., Calo E., Ferretti E., Alesse E., Screpanti I., Haigis K., Gulino A., Lees JA. Apoptosis - Interactions involving proteins with a function related to apoptosis Human IMR-90 cells expressing the murine ecotropic receptor were used. jalees@mit.edu Accepted 2010-MAR-23 by ORCHARD. 29-Mar-2010: Contacted by JYOTI. Cancer Cell (1535-6108) 2009 orchard Only protein-protein interactions 7 imex curation Proapoptotic function of the retinoblastoma tumor suppressor protein. Proapoptotic function of the retinoblastoma tumor suppressor protein. Cancer Cell (1535-6108) 2009 imex curation Ianari A., Natale T., Calo E., Ferretti E., Alesse E., Screpanti I., Haigis K., Gulino A., Lees JA. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer jalees@mit.edu 29-Mar-2010: Contacted by JYOTI. orchard Only protein-protein interactions 7 human-imr_90 Homo sapiens embryonic fetal lung fibroblast imr_90 human, Caucasian female 16 fetal weeks; Tissue: lung, embryonic fibroblast anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Ianari A., Natale T., Calo E., Ferretti E., Alesse E., Screpanti I., Haigis K., Gulino A., Lees JA. Apoptosis - Interactions involving proteins with a function related to apoptosis Human IMR-90 cells expressing the murine ecotropic receptor were used. PMID: 15741165 gives the source of the Adenovirus E1A protein as strain Ad5. jalees@mit.edu Accepted 2010-MAR-23 by ORCHARD. 29-Mar-2010: Contacted by JYOTI. Cancer Cell (1535-6108) 2009 orchard Only protein-protein interactions 7 imex curation Proapoptotic function of the retinoblastoma tumor suppressor protein. Proapoptotic function of the retinoblastoma tumor suppressor protein. Cancer Cell (1535-6108) 2009 imex curation Ianari A., Natale T., Calo E., Ferretti E., Alesse E., Screpanti I., Haigis K., Gulino A., Lees JA. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer jalees@mit.edu 29-Mar-2010: Contacted by JYOTI. orchard Only protein-protein interactions 7 human-t98g Human caucasian glioblastoma line T98G t98g Human Caucasian glioblastoma T98G ch-ip chromatin immunoprecipitation assay ch-ip primer specific pcr primer specific pcr Ianari A., Natale T., Calo E., Ferretti E., Alesse E., Screpanti I., Haigis K., Gulino A., Lees JA. Apoptosis - Interactions involving proteins with a function related to apoptosis jalees@mit.edu Accepted 2010-MAR-23 by ORCHARD. 29-Mar-2010: Contacted by JYOTI. Cancer Cell (1535-6108) 2009 orchard Only protein-protein interactions 7 imex curation casp7_human_gene Human CASP7 gene gene gene human Homo sapiens Human rb_human Retinoblastoma-associated protein pRb pp110 p105-Rb RB1 p110-RB1 protein protein human Homo sapiens Human MPPKTPRKTAATAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPMLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPHTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHLESACPLNLPLQNNHTAADMYLSPVRSPKKKGSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEK DIP protein P06400 original sequence version: 102 DIP protein P06400 original sequence version: 195 DIP protein P06400 original sequence version: 204 DIP protein P06400 original sequence version: 126 DIP protein P06400 original sequence version: 151 DIP protein P06400 original sequence version: 153 DIP protein P06400 original sequence version: 181 DIP protein P06400 original sequence version: 184 DIP protein P06400 original sequence version: 213 DIP protein P06400 original sequence version: 208 DIP protein P06400 original sequence version: 174 DIP protein P06400 original sequence version: 212 DIP protein P06400 original sequence version: 179 DIP protein P06400 original sequence version: 146 C8E746111E19CC32 hdac1_human Histone deacetylase 1 HDAC1 RPD3L1 protein protein human Homo sapiens Human MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA DIP protein Q13547 original sequence version: 106 DIP protein Q13547 original sequence version: 173 DIP protein Q13547 original sequence version: 100 DIP protein Q13547 original sequence version: 166 DIP protein Q13547 original sequence version: 153 DIP protein Q13547 original sequence version: 164 DIP protein Q13547 original sequence version: 175 DIP protein Q13547 original sequence version: 191 DIP protein Q13547 original sequence version: 185 DIP protein Q13547 original sequence version: 165 DIP protein Q13547 original sequence version: 162 DIP protein Q13547 original sequence version: 189 DIP protein Q13547 original sequence version: 158 DIP protein Q13547 original sequence version: 134 DIP protein Q13547 original sequence version: 124 4D35B7C1ED7838D6 e1a_ade05 Early E1A protein Early E1A 32 kDa protein protein protein ade05 Human adenovirus C serotype 5 (HAdV-5) HAdV-5 Human adenovirus 5 MRHIICHGGVITEEMAASLLDQLIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDEEGEEFVLDYVEHPGHGCRSCHYHRRNTGDPDIMCSLCYMRTCGMFVYSPVSEPEPEPEPEPEPARPTRRPKMAPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRVGGRRQAVECIEDLLNEPGQPLDLSCKRPRP DIP protein P03255 original sequence version: 73 DIP protein P03255 original sequence version: 110 8C5997A3908C40D7 h4_human Histone H4 H4-16 H4C1 H4C11 H4C12 H4C13 H4C14 H4C15 H4C2 H4C3 H4C4 H4C5 H4C6 H4C8 H4C9 H4/A H4/B H4/C H4/D H4/E H4/G H4/H H4/I H4/J H4/K H4/M H4/N H4/O H4F2 H4FA H4FB H4FC H4FD H4FE H4FG H4FH H4FI H4FJ H4FK H4FM H4FN H4FO HIST1H4A HIST1H4B HIST1H4C HIST1H4D HIST1H4E HIST1H4F HIST1H4H HIST1H4I HIST1H4J HIST1H4K HIST1H4L HIST2H4 HIST2H4A HIST2H4B HIST4H4 protein protein human Homo sapiens Human MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG DIP protein P62805 original sequence version: 68 DIP protein P62805 original sequence version: 111 DIP protein P62805 original sequence version: 94 DIP protein P62805 original sequence version: 97 DIP protein P62805 original sequence version: 116 DIP protein P62805 original sequence version: 105 DIP protein P62805 original sequence version: 120 DIP protein P62805 original sequence version: 144 DIP protein P62805 original sequence version: 150 DIP protein P62805 original sequence version: 154 DIP protein P62805 original sequence version: 156 DIP protein P62805 original sequence version: 112 DIP protein P62805 original sequence version: 121 DIP protein P62805 original sequence version: 123 DIP protein P62805 original sequence version: 126 DIP protein P62805 original sequence version: 132 DIP protein P62805 original sequence version: 136 DIP protein P62805 original sequence version: 119 A9E5DFD3F8B97598 kat2b_human Histone acetyltransferase KAT2B P300/CBP-associated factor PCAF Lysine acetyltransferase 2B Histone acetyltransferase PCAF KAT2B Spermidine acetyltransferase KAT2B protein protein human Homo sapiens Human MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKERQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSGLEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHDILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK DIP protein Q92831 original sequence version: 159 DIP protein Q92831 original sequence version: 153 DIP protein Q92831 original sequence version: 84 72F516E8BC00CC0C e2f3_human Transcription factor E2F3 E2F3 KIAA0075 protein protein human Homo sapiens Human MRKGIQPALEQYLVTAGGGEGAAVVAAAAAASMDKRALLASPGFAAAAAAAAAPGAYIQILTTNTSTTSCSSSLQSGAVAAGPLLPSAPGAEQTAGSLLYTTPHGPSSRAGLLQQPPALGRGGSGGGGGPPAKRRLELGESGHQYLSDGLKTPKGKGRAALRSPDSPKTPKSPSEKTRYDTSLGLLTKKFIQLLSQSPDGVLDLNKAAEVLKVQKRRIYDITNVLEGIHLIKKKSKNNVQWMGCSLSEDGGMLAQCQGLSKEVTELSQEEKKLDELIQSCTLDLKLLTEDSENQRLAYVTYQDIRKISGLKDQTVIVVKAPPETRLEVPDSIESLQIHLASTQGPIEVYLCPEETETHSPMKTNNQDHNGNIPKPASKDLASTNSGHSDCSVSMGNLSPLASPANLLQQTEDQIPSNLEGPFVNLLPPLLQEDYLLSLGEEEGISDLFDAYDLEKLPLVEDFMCS DIP protein O00716 original sequence version: 137 4641565842CA99EC ccna2_human_gene Human CCNA2 gene gene gene human Homo sapiens Human rpb1_human DNA-directed RNA polymerase II subunit RPB1 POLR2A DNA-directed RNA polymerase II subunit A DNA-directed RNA polymerase III largest subunit POLR2 RNA-directed RNA polymerase II subunit RPB1 protein protein human Homo sapiens Human MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVDFSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYIIRDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWSTFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQDTLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHINCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEMGHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKAHNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKINISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHAMGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGESVEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMREDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKLVIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAIAHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLTVFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMPDFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIRIMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKIIITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALERELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLMEAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTGMFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPGYSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPASPKYTPTSPSYSPSSPEYTPTSPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN DIP protein P24928 original sequence version: 108 DIP protein P24928 original sequence version: 147 DIP protein P24928 original sequence version: 158 DIP protein P24928 original sequence version: 157 DIP protein P24928 original sequence version: 179 DIP protein P24928 original sequence version: 181 DIP protein P24928 original sequence version: 161 DIP protein P24928 original sequence version: 175 DIP protein P24928-1 original sequence version: 175 DIP protein P24928 original sequence version: 68 DIP protein P24928 original sequence version: 116 28D6FD25693A6472 tp73_human_gene Human TP73 gene gene gene human Homo sapiens Human e2f1_human Transcription factor E2F1 Retinoblastoma-associated protein 1 Retinoblastoma-binding protein 3 PBR3 E2F1 RBBP3 pRB-binding protein E2F-1 protein protein human Homo sapiens Human MALAGAPAGGPCAPALEALLGAGALRLLDSSQIVIISAAQDASAPPAPTGPAAPAAGPCDPDLLLFATPQAPRPTPSAPRPALGRPPVKRRLDLETDHQYLAESSGPARGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTTVGVGGRLEGLTQDLRQLQESEQQLDHLMNICTTQLRLLSEDTDSQRLAYVTCQDLRSIADPAEQMVMVIKAPPETQLQAVDSSENFQISLKSKQGPIDVFLCPEETVGGISPGKTPSQEVTSEEENRATDSATIVSPPPSSPPSSLTTDPSQSLLSLEQEPLLSRMGSLRAPVDEDRLSPLVAADSLLEHVREDFSGLLPEEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF DIP protein Q01094 original sequence version: 173 DIP protein Q01094 original sequence version: 168 DIP protein Q01094 original sequence version: 149 DIP protein Q01094 original sequence version: 130 DIP protein Q01094 original sequence version: 125 DIP protein Q01094 original sequence version: 153 DIP protein Q01094 original sequence version: 180 003B3F654F0C60DF rb1-kat2b 1 17 unspecified role unspecified role prey prey 8 unspecified role unspecified role bait bait 12 unspecified role unspecified role prey prey physical association physical association Asynchronous T98G cells untreated (−) or treated with 2 μM doxorubicin (doxo) for 24 hr (+) were screened by immunoprecipitation (IP) using an antibody against pRB followed by western blotting (WB) to assess levels of pRB and associated E2F1 and P/CAF (A) doxorubicin Fig 1A. rb1-e2f1-3 1 8 unspecified role unspecified role bait bait region (possible) phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 17 unspecified role unspecified role prey prey physical association physical association Using a phospho-specific pRB cocktail of antibodies to demonstrate that phosphorylated pRB can participate in the formation of a complex with E2F1 in arrested and proliferating cells. doxorubicin Fig 1D-F. Fig 1B shows cell cycle distribution (by FACS) of asynchronous T98G cells. casp7-rb1 6 7 unspecified role unspecified role prey prey 8 unspecified role unspecified role bait bait association association Doxorubicin treatment induced the recruitment of pRB and other proteins to both cell-cycle and proapoptotic promoters, resulting in activation of Caspase 7 and p73, and the repression of Cyclin A2. doxorubicin Fig 2B, Fig S1 for quantitative analysis of results. tp73-rb1 6 16 unspecified role unspecified role prey prey 8 unspecified role unspecified role bait bait association association Doxorubicin treatment induced the recruitment of pRB and other proteins to both cell-cycle and proapoptotic promoters, resulting in activation of Caspase 7 and p73, and the repression of Cyclin A2. doxorubicin Fig 2B, Fig S1 for quantitative analysis of results. cyca2-rb1 6 8 unspecified role unspecified role bait bait 14 unspecified role unspecified role prey prey association association Doxorubicin treatment induced recruitment of pRB to both cell-cycle and proapoptotic promoters, resulting in activation of Caspase 7 and p73, and the repression of Cyclin A2. HDAC1 was also specifically recruited to the Cyclin A2 promoter after Doxorubicin treatment. doxorubicin Fig 2B, Fig S1 for quantitative analysis of results. casp7-rb1-h4 3 11 unspecified role unspecified role bait bait acetyl-h4 naclys N-acetylated L-lysine NAcLys undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 7 unspecified role unspecified role prey prey 8 unspecified role unspecified role prey prey association association Acetyl-H4 was bound at the transcriptionally active Caspase 7 gene promoter. doxorubicin Fig 2C. rb1-e2f1-4 5 8 unspecified role unspecified role bait bait 17 unspecified role unspecified role prey prey physical association physical association In a manner similar to T98G and U2OS cells, Doxorubicin promotes formation of pRB-E2F1 complexes in IMR-90 cells in the absence of E1A. doxorubicin Fig 5A. rb1-e2f3 5 13 unspecified role unspecified role prey prey 8 unspecified role unspecified role bait bait 17 unspecified role unspecified role prey prey 10 unspecified role unspecified role prey prey physical association physical association doxorubicin Fig 5B. E1A yielded an increase in the intracellular levels of pRB, E2F1 and E2F3. The 243 amino acid "S12" form of E1A was used, which shares conserved regions "1+2" with the full length (13S) form. This S12 protein may be (SwissProt P03255-2) "Isoform early E1A 26 kDa protein" which also has 243 amino acids. rb1-e1a-1 5 8 unspecified role unspecified role prey prey 17 unspecified role unspecified role prey prey 10 unspecified role unspecified role bait bait association association The binding of E1A to pRB and E2F1 is also detected via IP of E1A. doxorubicin Fig 5C. The 243 amino acid "S12" form of E1A was used, which shares conserved regions "1+2" with the full length (13S) form. This S12 protein may be "Isoform early E1A 26 kDa protein" (SwissProt P03255-2),which also has 243 amino acids. rb1p-e2f1-6 5 8 unspecified role unspecified role bait bait region (possible) phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 17 unspecified role unspecified role prey prey physical association physical association E1A also enhanced the formation of phosphorylated RB species and their binding to E2F1. Fig 5D. rb1-tp73 2 16 unspecified role unspecified role prey prey 8 unspecified role unspecified role bait bait association association doxorubicin Fig 5E. pRB bound to the p73 and Cyclin A2 promoters in the presence and absence of E1A. e1a-ccna2 2 14 unspecified role unspecified role prey prey 10 unspecified role unspecified role bait bait association association doxorubicin Fig 5E. E1A bound to the p73 and Cyclin A2 promoters. In the E1A-infected cells, pRB, E2F1, E1A, and acetyl-H4 all associated with both the Cyclin A2 and p73 promoters. The 243 amino acid "S12" form of E1A was used, which shares conserved regions "1+2" with the full length (13S) form. This S12 protein may be "Isoform early E1A 26 kDa protein" (SwissProt P03255-2),which also has 243 amino acids. This source-text was lifted from near the "Discussion" section. ef1-tp73-1 2 16 unspecified role unspecified role prey prey 17 unspecified role unspecified role bait bait association association doxorubicin Fig 5E. E2F1 bound to the p73 and Cyclin A2 promoters. In the E1A-infected cells, pRB, E2F1, E1A, and acetyl-H4 all associated with both the Cyclin A2 and p73 promoters. source-text from the paper - near Discussion section. h4-tp73-2 2 16 unspecified role unspecified role prey prey 11 unspecified role unspecified role bait bait ach4 naclys N-acetylated L-lysine NAcLys undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined association association doxorubicin Fig 5E. Acetylated Histone H4 bound to the p73 and Cyclin A2 promoters. In the E1A-infected cells, pRB, E2F1, E1A, and acetyl-H4 all associated with both the Cyclin A2 and p73 promoters. source text from near Discussion section. e1a-tp73-1 2 16 unspecified role unspecified role prey prey 10 unspecified role unspecified role bait bait association association doxorubicin Fig 5E. E1A bound to the p73 and Cyclin A2 promoters. In the E1A-infected cells, pRB, E2F1, E1A, and acetyl-H4 all associated with both the Cyclin A2 and p73 promoters. The 243 amino acid "S12" form of E1A was used, which shares conserved regions "1+2" with the full length (13S) form. This S12 protein may be "Isoform early E1A 26 kDa protein" (SwissProt P03255-2),which also has 243 amino acids. ef1-ccn2 2 14 unspecified role unspecified role prey prey 17 unspecified role unspecified role bait bait association association doxorubicin Fig 5E. E2F1 bound to the p73 and Cyclin A2 promoters. In the E1A-infected cells, pRB, E2F1, E1A, and acetyl-H4 all associated with both the Cyclin A2 and p73 promoters. source-text near to discusssion section. rb1-ccn2 2 8 unspecified role unspecified role bait bait 14 unspecified role unspecified role prey prey association association doxorubicin Fig 5E. pRB bound to the p73 and Cyclin A2 promoters in the presence and absence of E1A. This source-text was lifted from near the "Discussion" section. h4-ccn2 2 11 unspecified role unspecified role bait bait ach4 naclys N-acetylated L-lysine NAcLys undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 14 unspecified role unspecified role prey prey association association doxorubicin Fig 5E. Acetylated Histone H4 bound to the p73 and Cyclin A2 promoters. In the E1A-infected cells, pRB, E2F1, E1A, and acetyl-H4 all associated with both the Cyclin A2 and p73 promoters. casp7-rpb1 6 7 unspecified role unspecified role prey prey 15 unspecified role unspecified role bait bait association association Doxorubicin treatment induced the recruitment of pRB and other proteins to both cell-cycle and proapoptotic promoters, resulting in activation of Caspase 7 and p73, and the repression of Cyclin A2. doxorubicin Fig 2B, Fig S1 for quantitative analysis of results. casp7-e2f1 6 7 unspecified role unspecified role prey prey 17 unspecified role unspecified role bait bait association association Doxorubicin treatment induced the recruitment of pRB and other proteins to both cell-cycle and proapoptotic promoters, resulting in activation of Caspase 7 and p73, and the repression of Cyclin A2. doxorubicin Fig 2B, Fig S1 for quantitative analysis of results. Transcription factor E2F1 bound to the Caspase 7 promoter. tp73-rpb1 6 15 unspecified role unspecified role bait bait 16 unspecified role unspecified role prey prey association association Doxorubicin treatment induced the recruitment of pRB and other proteins to both cell-cycle and proapoptotic promoters, resulting in activation of Caspase 7 and p73, and the repression of Cyclin A2. doxorubicin Fig 2B, Fig S1 for quantitative analysis of results. tp73-e2f1 6 17 unspecified role unspecified role bait bait 16 unspecified role unspecified role prey prey association association Doxorubicin treatment induced the recruitment of pRB and other proteins to both cell-cycle and proapoptotic promoters, resulting in activation of Caspase 7 and p73, and the repression of Cyclin A2. doxorubicin Fig 2B, Fig S1 for quantitative analysis of results. cyca2-hdac1 6 9 unspecified role unspecified role bait bait 14 unspecified role unspecified role prey prey association association Doxorubicin treatment induced recruitment of pRB to both cell-cycle and proapoptotic promoters, resulting in activation of Caspase 7 and p73, and the repression of Cyclin A2. HDAC1 was also specifically recruited to the Cyclin A2 promoter after Doxorubicin treatment. doxorubicin Fig 2B, Fig S1 for quantitative analysis of results. cyca2-e2f1 6 14 unspecified role unspecified role prey prey 17 unspecified role unspecified role bait bait association association Doxorubicin treatment induced recruitment of pRB to both cell-cycle and proapoptotic promoters, resulting in activation of Caspase 7 and p73, and the repression of Cyclin A2. HDAC1 was also specifically recruited to the Cyclin A2 promoter after Doxorubicin treatment. doxorubicin Fig 2B, Fig S1 for quantitative analysis of results. cyca2-rpb1 6 14 unspecified role unspecified role prey prey 15 unspecified role unspecified role bait bait association association Doxorubicin treatment induced recruitment of pRB to both cell-cycle and proapoptotic promoters, resulting in activation of Caspase 7 and p73, and the repression of Cyclin A2. HDAC1 was also specifically recruited to the Cyclin A2 promoter after Doxorubicin treatment. doxorubicin Fig 2B, Fig S1 for quantitative analysis of results. rb1-e2f1-6 4 8 unspecified role unspecified role bait bait 17 unspecified role unspecified role prey prey physical association physical association doxorubicin, etoposide, camptothecin. Supplementary Material, Fig S2A.