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/ Gain of function of mutant p53: the mutant p53/NF-Y protein complex reveals an aberrant transcriptional mechanism of cell cycle regulation. Gain of function of mutant p53: the mutant p53/NF-Y protein complex reveals an aberrant transcriptional mechanism of cell cycle regulation. Cancer Cell (1535-6108) 2006 imex curation Di Agostino S., Strano S., Emiliozzi V., Zerbini V., Mottolese M., Sacchi A., Blandino G., Piaggio G. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer blandino@ifo.it 01-DEC-2006: Contacted by JYOTI. Only protein-protein interactions 14 human-colon human colon colon anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Di Agostino S., Strano S., Emiliozzi V., Zerbini V., Mottolese M., Sacchi A., Blandino G., Piaggio G. Apoptosis - Interactions involving proteins with a function related to apoptosis blandino@ifo.it Accepted 2006-OCT-5 by DAVET. 01-DEC-2006: Contacted by JYOTI. Cancer Cell (1535-6108) 2006 Only protein-protein interactions 14 imex curation Gain of function of mutant p53: the mutant p53/NF-Y protein complex reveals an aberrant transcriptional mechanism of cell cycle regulation. Gain of function of mutant p53: the mutant p53/NF-Y protein complex reveals an aberrant transcriptional mechanism of cell cycle regulation. Cancer Cell (1535-6108) 2006 imex curation Di Agostino S., Strano S., Emiliozzi V., Zerbini V., Mottolese M., Sacchi A., Blandino G., Piaggio G. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer blandino@ifo.it 01-DEC-2006: Contacted by JYOTI. Only protein-protein interactions 14 human-mcf10a Human non-transformed breast epithelial cell line mcf10a non-transformed human breast epithelial cell line anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Di Agostino S., Strano S., Emiliozzi V., Zerbini V., Mottolese M., Sacchi A., Blandino G., Piaggio G. Apoptosis - Interactions involving proteins with a function related to apoptosis blandino@ifo.it Accepted 2006-OCT-5 by DAVET. 01-DEC-2006: Contacted by JYOTI. Cancer Cell (1535-6108) 2006 Only protein-protein interactions 14 imex curation Gain of function of mutant p53: the mutant p53/NF-Y protein complex reveals an aberrant transcriptional mechanism of cell cycle regulation. Gain of function of mutant p53: the mutant p53/NF-Y protein complex reveals an aberrant transcriptional mechanism of cell cycle regulation. Cancer Cell (1535-6108) 2006 imex curation Di Agostino S., Strano S., Emiliozzi V., Zerbini V., Mottolese M., Sacchi A., Blandino G., Piaggio G. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer blandino@ifo.it 01-DEC-2006: Contacted by JYOTI. Only protein-protein interactions 14 human-skbr3 Homo sapiens SKBR3 skbr3 SKBR3 Species: human; Tissue: breast; Tumor: adenocarcinoma; Derived from: metastatic site: pleural effusion imaging technique imaging technique microscopy immunostaining immunostaining Di Agostino S., Strano S., Emiliozzi V., Zerbini V., Mottolese M., Sacchi A., Blandino G., Piaggio G. Apoptosis - Interactions involving proteins with a function related to apoptosis blandino@ifo.it Accepted 2006-OCT-5 by DAVET. 01-DEC-2006: Contacted by JYOTI. Cancer Cell (1535-6108) 2006 Only protein-protein interactions 14 imex curation Gain of function of mutant p53: the mutant p53/NF-Y protein complex reveals an aberrant transcriptional mechanism of cell cycle regulation. Gain of function of mutant p53: the mutant p53/NF-Y protein complex reveals an aberrant transcriptional mechanism of cell cycle regulation. Cancer Cell (1535-6108) 2006 imex curation Di Agostino S., Strano S., Emiliozzi V., Zerbini V., Mottolese M., Sacchi A., Blandino G., Piaggio G. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer blandino@ifo.it 01-DEC-2006: Contacted by JYOTI. Only protein-protein interactions 14 human-h1299 Homo sapiens lung lymph node carcinoma h1299 Human lung lymph node carcinoma p53 null. These cells have also been reported to secrete the peptide hormone neuromedin B (NMB), but not gastrin releasing peptide (GRP). Also known as NCI H1299 or CRL-5803. http://www.lgcpromochem.com/atcc/ ATCC number: CRL-5803. ATCC number of the cell line is CRL-5803. anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Di Agostino S., Strano S., Emiliozzi V., Zerbini V., Mottolese M., Sacchi A., Blandino G., Piaggio G. Apoptosis - Interactions involving proteins with a function related to apoptosis blandino@ifo.it Accepted 2006-OCT-5 by DAVET. 01-DEC-2006: Contacted by JYOTI. Cancer Cell (1535-6108) 2006 Only protein-protein interactions 14 imex curation Gain of function of mutant p53: the mutant p53/NF-Y protein complex reveals an aberrant transcriptional mechanism of cell cycle regulation. Gain of function of mutant p53: the mutant p53/NF-Y protein complex reveals an aberrant transcriptional mechanism of cell cycle regulation. Cancer Cell (1535-6108) 2006 imex curation Di Agostino S., Strano S., Emiliozzi V., Zerbini V., Mottolese M., Sacchi A., Blandino G., Piaggio G. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer blandino@ifo.it 01-DEC-2006: Contacted by JYOTI. Only protein-protein interactions 14 human-ht_29 Homo sapiens HT-29 caucasian women with colon adenocarcinoma ht_29 HT-29 confirmed as human with IEF of AST, LDH established from the primary tumor of a 44-year-old Caucasian woman with colon adenocarcinoma in 1964; described to be heterotransplantable forming well-differentiated grade I tumors anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Di Agostino S., Strano S., Emiliozzi V., Zerbini V., Mottolese M., Sacchi A., Blandino G., Piaggio G. Apoptosis - Interactions involving proteins with a function related to apoptosis blandino@ifo.it Accepted 2006-OCT-5 by DAVET. 01-DEC-2006: Contacted by JYOTI. Cancer Cell (1535-6108) 2006 Only protein-protein interactions 14 imex curation Gain of function of mutant p53: the mutant p53/NF-Y protein complex reveals an aberrant transcriptional mechanism of cell cycle regulation. Gain of function of mutant p53: the mutant p53/NF-Y protein complex reveals an aberrant transcriptional mechanism of cell cycle regulation. Cancer Cell (1535-6108) 2006 imex curation Di Agostino S., Strano S., Emiliozzi V., Zerbini V., Mottolese M., Sacchi A., Blandino G., Piaggio G. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer blandino@ifo.it 01-DEC-2006: Contacted by JYOTI. Only protein-protein interactions 14 human-skbr3 Homo sapiens SKBR3 skbr3 SKBR3 Species: human; Tissue: breast; Tumor: adenocarcinoma; Derived from: metastatic site: pleural effusion anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Di Agostino S., Strano S., Emiliozzi V., Zerbini V., Mottolese M., Sacchi A., Blandino G., Piaggio G. Apoptosis - Interactions involving proteins with a function related to apoptosis blandino@ifo.it Accepted 2006-OCT-5 by DAVET. 01-DEC-2006: Contacted by JYOTI. Cancer Cell (1535-6108) 2006 Only protein-protein interactions 14 imex curation 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 nfyb_human Nuclear transcription factor Y subunit beta NFYB HAP3 Nuclear transcription factor Y subunit B CAAT box DNA-binding protein subunit B protein protein human Homo sapiens Human MTMDGDSSTTDASQLGISADYIGGSHYVIQPHDDTEDSMNDHEDTNGSKESFREQDIYLPIANVARIMKNAIPQTGKIAKDAKECVQECVSEFISFITSEASERCHQEKRKTINGEDILFAMSTLGFDSYVEPLKLYLQKFREAMKGEKGIGGAVTATDGLSEELTEEAFTNQLPAGLITTDGQQQNVMVYTTSYQQISGVQQIQFS 1ADFA0E45F3CF972 p53_human Cellular tumor antigen p53 TP53 P53 Tumor suppressor p53 Phosphoprotein p53 Antigen NY-CO-13 protein protein human Homo sapiens Human MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD DIP protein P04637 original sequence version: 121 DIP protein P04637 original sequence version: 115 DIP protein P04637-1 original sequence version: 224 DIP protein P04637 original sequence version: 117 DIP protein P04637-1 original sequence version: 226 DIP protein P04637 original sequence version: 226 DIP protein P04637 original sequence version: 212 DIP protein P04637 original sequence version: 220 DIP protein P04637-1 original sequence version: 220 DIP protein P04637-1 original sequence version: 145 DIP protein P04637 original sequence version: 146 DIP protein P04637 original sequence version: 145 DIP protein P04637 original sequence version: 166 DIP protein P04637-1 original sequence version: 166 DIP protein P04637 original sequence version: 169 DIP protein P04637 original sequence version: 177 DIP protein P04637 original sequence version: 175 DIP protein P04637-1 original sequence version: 175 DIP protein P04637-1 original sequence version: 172 DIP protein P04637-1 original sequence version: 169 DIP protein P04637 original sequence version: 170 DIP protein P04637 original sequence version: 172 DIP protein P04637-1 original sequence version: 194 DIP protein P04637 original sequence version: 196 DIP protein P04637 original sequence version: 185 DIP protein P04637-1 original sequence version: 191 DIP protein P04637 original sequence version: 191 DIP protein P04637 original sequence version: 180 DIP protein P04637-1 original sequence version: 197 DIP protein P04637 original sequence version: 183 DIP protein P04637-1 original sequence version: 183 DIP protein P04637-1 original sequence version: 185 DIP protein P04637 original sequence version: 199 DIP protein P04637 original sequence version: 201 DIP protein P04637 original sequence version: 189 DIP protein P04637 original sequence version: 235 DIP protein P04637 original sequence version: 230 DIP protein P04637 original sequence version: 234 DIP protein P04637-1 original sequence version: 234 DIP protein P04637-1 original sequence version: 235 DIP protein P04637 original sequence version: 239 DIP protein P04637-1 original sequence version: 212 DIP protein P04637-1 original sequence version: 213 DIP protein P04637 original sequence version: 213 DIP protein P04637 original sequence version: 206 DIP protein P04637-1 original sequence version: 188 DIP protein P04637-1 original sequence version: 228 DIP protein P04637 original sequence version: 208 DIP protein P04637 original sequence version: 240 DIP protein P04637-1 original sequence version: 240 DIP protein P04637 original sequence version: 204 DIP protein P04637-1 original sequence version: 204 DIP protein P04637-1 original sequence version: 209 DIP protein P04637-1 original sequence version: 203 DIP protein P04637 original sequence version: 221 DIP protein P04637-1 original sequence version: 152 DIP protein P04637 original sequence version: 217 DIP protein P04637-1 original sequence version: 140 DIP protein P04637 original sequence version: 215 DIP protein P04637 original sequence version: 214 DIP protein P04637-1 original sequence version: 182 DIP protein P04637 original sequence version: 182 DIP protein P04637 original sequence version: 188 DIP protein P04637 original sequence version: 192 DIP protein P04637-1 original sequence version: 192 DIP protein P04637 original sequence version: 218 DIP protein P04637-1 original sequence version: 218 AD5C149FD8106131 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 nfya_human Nuclear transcription factor Y subunit alpha NFYA Nuclear transcription factor Y subunit A CAAT box DNA-binding protein subunit A protein protein human Homo sapiens Human MEQYTANSNSSTEQIVVQAGQIQQQQQGGVTAVQLQTEAQVASASGQQVQTLQVVQGQPLMVQVSGGQLITSTGQPIMVQAVPGGQGQTIMQVPVSGTQGLQQIQLVPPGQIQIQGGQAVQVQGQQGQTQQIIIQQPQTAVTAGQTQTQQQIAVQGQQVAQTAEGQTIVYQPVNADGTILQQVTVPVSGMITIPAASLAGAQIVQTGANTNTTSSGQGTVTVTLPVAGNVVNSGGMVMMVPGAGSVPAIQRIPLPGAEMLEEEPLYVNAKQYHRILKRRQARAKLEAEGKIPKERRKYLHESRHRHAMARKRGEGGRFFSPKEKDSPHMQDPNQADEEAMTQIIRVS D00BE17041EB1A9E tp53-nfya 1 9 unspecified role unspecified role bait bait P04637:p.[Arg273His;Pro309Ser] mutation mutation certain certain sequence position certain certain certain sequence position certain P S certain certain sequence position certain certain certain sequence position certain R H Wed May 02 19:54:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg273his,pro309ser' Tue Jun 30 19:08:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg273His;Pro309Ser]' 11 unspecified role unspecified role prey prey 8 unspecified role unspecified role prey prey association association 1 A we performed coimmunoprecipitation experiments, employing cell extracts derived from tumor cells (SKBR3, HT29, and SW480) harboring endogenous mutant p53His175, p53His273, and p53His273/Ser309 proteins, respectively. As shown in Figure 1A (lanes 5 and 6), we found the presence of protein complexes between mutant p53 and NF-YA and NF-YB. SW480 cells harbour mutant p53 (arg273his-leu309ser). Adriamycin treatment does not affect formation of the complex. tp53-nfya-1 5 9 unspecified role unspecified role bait bait P04637:p.Arg273His mutation mutation certain certain sequence position certain certain certain sequence position certain R H Wed May 02 16:06:18 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg273his' Tue Jun 30 18:26:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg273His' 11 unspecified role unspecified role prey prey 8 unspecified role unspecified role prey prey association association 1 A we performed coimmunoprecipitation experiments, employing cell extracts derived from tumor cells (SKBR3, HT29, and SW480) harboring endogenous mutant p53His175, p53His273, and p53His273/Ser309 proteins, respectively. As shown in Figure 1A (lanes 5 and 6), we found the presence of protein complexes between mutant p53 and NF-YA and NF-YB. HT-29 cells harbour mutant p53 (arg273his). Adriamycin treatment does not affect formation of the complex. tp53-nfya-2 6 9 unspecified role unspecified role bait bait P04637:p.Arg175His mutation mutation certain certain sequence position certain certain certain sequence position certain R H Wed May 02 16:18:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg175his' Tue Jun 30 19:31:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg175His' 11 unspecified role unspecified role prey prey 8 unspecified role unspecified role prey prey association association 1 A we performed coimmunoprecipitation experiments, employing cell extracts derived from tumor cells (SKBR3, HT29, and SW480) harboring endogenous mutant p53His175, p53His273, and p53His273/Ser309 proteins, respectively. As shown in Figure 1A (lanes 5 and 6), we found the presence of protein complexes between mutant p53 and NF-YA and NF-YB. SKBR3 cells harbour endogenous mutant p53 (arg175his). Adriamycin treatment does not affect formation of the complex. tp53-nfya-3 6 11 unspecified role unspecified role prey prey 7 unspecified role unspecified role prey prey 10 unspecified role unspecified role prey prey 9 unspecified role unspecified role bait bait P04637:p.Arg175His mutation mutation certain certain sequence position certain certain certain sequence position certain R H Wed May 02 16:53:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg175his' Tue Jun 30 20:02:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg175His' association association 5 C To evaluate in a more physiological context the existence of mutant p53/NF-Y/p300 protein complexes, we performed coprecipitation experiments in SKBR3 cells. Interestingly, this complex was found predominantly in cells treated with ADR This complex was found predominantly in cells treated with adriamycin. SKBR3 cells harbour endogenous mutant p53 (arg175his). tp53-nfya-4 6 11 unspecified role unspecified role prey prey 10 unspecified role unspecified role prey prey 9 unspecified role unspecified role bait bait P04637:p.Arg175His mutation mutation certain certain sequence position certain certain certain sequence position certain R H Wed May 02 18:00:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg175his' Tue Jun 30 18:39:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg175His' association association 5 C To evaluate in a more physiological context the existence of mutant p53/NF-Y/p300 protein complexes, we performed coprecipitation experiments in SKBR3 cells. Interestingly, this complex was found predominantly in cells treated with ADR (Figure 5C, lanes 5 and 6). We also found that the presence of a protein complex involving mutant p53 and HDAC1, unlike that containing p300, can be detected predominantly in the absence of ADR This complex was found in the absence of adriamycin. SKBR3 cells harbour endogenous mutant p53 (arg175his). tp53-hdac1 2 10 unspecified role unspecified role prey prey 9 unspecified role unspecified role bait bait physical association physical association 5 D wtp53 interacted preferentially with HDAC1 and not p300 in ADR-treated MCF10 wild-type p53 in MCF10 cells treated with adriamycin interacted preferentially with HDAC1 and not p300. nfya-tp53 4 7 unspecified role unspecified role prey prey 9 unspecified role unspecified role prey prey P04637:p.Arg175His mutation mutation certain certain sequence position certain certain certain sequence position certain R H Wed May 02 18:17:34 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg175his' Tue Jun 30 16:40:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg175His' 11 unspecified role unspecified role bait bait association association 5 A, B we transiently overexpressed NF-YA and p300 in H1299 cells expressing ponasterone-inducible mutant p53His175. We found that reciprocal protein complexes involving NF-YA, mutp53, and p300 were present in ponasterone-treated cells (Figure 5A, upper panels). Furthermore, mutant p53 and NF-Y are necessary for the binding of p300 Mutant p53 and NF-YA are needed for binding of p300. The H-175#41 cells are H1299 containing ponasterone-inducible mutp53 (arg175his). This complex was formed when the cells were induced with ponasterone and transfected with vectors for NF-YA and p300. Transfection p53, NF-YA and p300 were overexpressed. In the presence of p300 both NF-YA and mutant p53 (arg175his) were acetylated. nfya-tp53-1 4 11 unspecified role unspecified role bait bait 9 unspecified role unspecified role prey prey physical association physical association 5 A we transiently overexpressed NF-YA and p300 in H1299 cells expressing ponasterone-inducible mutant p53His175. We found that reciprocal protein complexes involving NF-YA, mutp53, and p300 were present in ponasterone-treated cells (Figure 5A, upper panels). Furthermore, mutant p53 and NF-Y are necessary for the binding of p300 Mutant p53 and NF-YA are needed for binding of p300. H-175#41 cells are H1299 cells containing ponasterone-inducible mutant p53 (arg173his). This complex was formed when cells were not induced with ponasterone. NF-YA and p300 were overexpressed. Transfection tp53-nfya-5 4 11 unspecified role unspecified role prey prey 7 unspecified role unspecified role prey prey 9 unspecified role unspecified role bait bait P04637:p.Arg175His mutation mutation certain certain sequence position certain certain certain sequence position certain R H Wed May 02 18:28:19 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg175his' Tue Jun 30 17:53:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg175His' association association 5 A, B we transiently overexpressed NF-YA and p300 in H1299 cells expressing ponasterone-inducible mutant p53His175. We found that reciprocal protein complexes involving NF-YA, mutp53, and p300 were present in ponasterone-treated cells (Figure 5A, upper panels). Furthermore, mutant p53 and NF-Y are necessary for the binding of p300 Mutant p53 and NF-YA are needed for binding of p300. The H-175#41 cells are H1299 cells which contain ponasterone-inducible mutant p53His175. P53, NF-YA and p300 were overexpressed. Transfection. This complex was formed when the cells were induced with ponasterone and transfected with vectors for NF-YA and p300. In the presence of p300 both NF-YA and mutant p53 (arg175his) were acetylated. tp53-nfya-6 4 9 unspecified role unspecified role bait bait P04637:p.Arg175His mutation mutation certain certain sequence position certain certain certain sequence position certain R H Wed May 02 14:52:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg175his' Tue Jun 30 19:40:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg175His' 8 unspecified role unspecified role prey prey 11 unspecified role unspecified role prey prey association association S1 B Reciprocal protein complexes involving mutant p53, NF-YA, and NF-YB were found in cells whose exogenous expression of mutant p53His175 (H-175#41) or wtp53 (H-wtp53#23) was under the control of ponasterone A Thic complex was formed in H1299 cells with ponasterone induceable wild-type p53 or mutant p53 (arg175his). Transfection The cells were tranfected with NF-YA vector, which was overexpressed. P53 was also overepxressed. nfya-tp53-2 4 11 unspecified role unspecified role prey prey 9 unspecified role unspecified role prey prey P04637:p.Arg175His mutation mutation certain certain sequence position certain certain certain sequence position certain R H Wed May 02 18:01:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg175his' Tue Jun 30 16:51:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg175His' 8 unspecified role unspecified role bait bait association association S1 B Reciprocal protein complexes involving mutant p53, NF-YA, and NF-YB were found in cells whose exogenous expression of mutant p53His175 (H-175#41) or wtp53 (H-wtp53#23) was under the control of ponasterone A Thic complex was formed in H1299 cells with ponasterone induceable wild-type p53 or mutant p53 (arg175his). Transfection The cells were tranfected with NF-YA vector, which was overexpressed. P53 was also overexpressed. nfya-tp53-3 4 8 unspecified role unspecified role bait bait 11 unspecified role unspecified role prey prey physical association physical association S1 B Reciprocal protein complexes involving mutant p53, NF-YA, and NF-YB were found in cells whose exogenous expression of mutant p53His175 (H-175#41) or wtp53 (H-wtp53#23) was under the control of ponasterone A Thic complex was formed in H1299 cells which are p53-null. Transfection The cells were tranfected with NF-YA vector, which was overexpressed. tp53-nfya-7 6 9 unspecified role unspecified role bait bait P04637:p.Arg175His mutation mutation certain certain sequence position certain certain certain sequence position certain R H Wed May 02 17:01:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg175his' Tue Jun 30 18:55:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg175His' 11 unspecified role unspecified role prey prey physical association physical association S1 C Immunodepletion experiment was carried out immunoprecipitating 300μg of SKBR3 total cell extracts. Three rounds of immunoprecipitation were performed using 3μl of sheep serum α-p53 Ab7 antibody each round. The mutant p53 immunodeprivation was monitorated round by round with western blotting (lanes 4- 6). The immunocomplexes of the three rounds were collected and 1/3 of these (i.e. 100μg of total cell extracts; lane 2) was analyzed by western blotting. SKBR3 cells harbour mutant p53 (arg175his). tp53-nfya-8 3 9 unspecified role unspecified role neutral component neutral component P04637:p.Arg175His mutation mutation certain certain sequence position certain certain certain sequence position certain R H Wed May 02 19:51:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg175his' Tue Jun 30 17:38:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg175His' 11 unspecified role unspecified role neutral component neutral component colocalization colocalization S1 B SKBR3 cells harbour mutant p53 (arg175his). Immunostaining analysis revealed that mutant p53 and NF-YA localize in the nucleus of SKBR3 cells. RNAi knockdown of mutant p53His175 did not affect the localization of NF-YA RNAi knockdown of mutant p53 (arg175his) did not affect the localization of NF-YA