MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it The interaction of the hnRNP family member E1B-AP5 with p53. The interaction of the hnRNP family member E1B-AP5 with p53. FEBS Lett. (0014-5793) 2005 imex curation Barral PM., Rusch A., Turnell AS., Gallimore PH., Byrd PJ., Dobner T., Grand RJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer no Pull down experiments were performed using lysates from A549 cells, HCT116 cells, C33A cells and AdE1HEK293 cells (HEK293 cells transformed with Ad5 early region 1 DNA), and Ad12E1HER2 cells (human embryonic retinoblasts (HER2 transformed with the Ad12 E1 region). r.j.a.grand@bham.ac.uk DAVET Only protein-protein interactions human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Barral PM., Rusch A., Turnell AS., Gallimore PH., Byrd PJ., Dobner T., Grand RJ. Apoptosis - Interactions involving proteins with a function related to apoptosis no Pull down experiments were performed using lysates from A549 cells, HCT116 cells, C33A cells and AdE1HEK293 cells (HEK293 cells transformed with Ad5 early region 1 DNA), and Ad12E1HER2 cells (human embryonic retinoblasts (HER2 transformed with the Ad12 E1 region). r.j.a.grand@bham.ac.uk Accepted 2007-DEC-23 by DAVET. FEBS Lett. (0014-5793) 2005 DAVET Only protein-protein interactions imex curation The interaction of the hnRNP family member E1B-AP5 with p53. The interaction of the hnRNP family member E1B-AP5 with p53. FEBS Lett. (0014-5793) 2005 imex curation Barral PM., Rusch A., Turnell AS., Gallimore PH., Byrd PJ., Dobner T., Grand RJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer no Pull down experiments were performed using lysates from A549 cells, HCT116 cells, C33A cells and AdE1HEK293 cells (HEK293 cells transformed with Ad5 early region 1 DNA), and Ad12E1HER2 cells (human embryonic retinoblasts (HER2 transformed with the Ad12 E1 region). r.j.a.grand@bham.ac.uk DAVET Only protein-protein interactions in vitro In vitro pull down pull down weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Barral PM., Rusch A., Turnell AS., Gallimore PH., Byrd PJ., Dobner T., Grand RJ. Apoptosis - Interactions involving proteins with a function related to apoptosis no Pull down experiments were performed using lysates from A549 cells, HCT116 cells, C33A cells and AdE1HEK293 cells (HEK293 cells transformed with Ad5 early region 1 DNA), and Ad12E1HER2 cells (human embryonic retinoblasts (HER2 transformed with the Ad12 E1 region). r.j.a.grand@bham.ac.uk Accepted 2007-DEC-23 by DAVET. FEBS Lett. (0014-5793) 2005 DAVET Only protein-protein interactions imex curation The interaction of the hnRNP family member E1B-AP5 with p53. The interaction of the hnRNP family member E1B-AP5 with p53. FEBS Lett. (0014-5793) 2005 imex curation Barral PM., Rusch A., Turnell AS., Gallimore PH., Byrd PJ., Dobner T., Grand RJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer no Pull down experiments were performed using lysates from A549 cells, HCT116 cells, C33A cells and AdE1HEK293 cells (HEK293 cells transformed with Ad5 early region 1 DNA), and Ad12E1HER2 cells (human embryonic retinoblasts (HER2 transformed with the Ad12 E1 region). r.j.a.grand@bham.ac.uk DAVET Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Barral PM., Rusch A., Turnell AS., Gallimore PH., Byrd PJ., Dobner T., Grand RJ. Apoptosis - Interactions involving proteins with a function related to apoptosis no Pull down experiments were performed using lysates from A549 cells, HCT116 cells, C33A cells and AdE1HEK293 cells (HEK293 cells transformed with Ad5 early region 1 DNA), and Ad12E1HER2 cells (human embryonic retinoblasts (HER2 transformed with the Ad12 E1 region). r.j.a.grand@bham.ac.uk Accepted 2007-DEC-23 by DAVET. FEBS Lett. (0014-5793) 2005 DAVET Only protein-protein interactions imex curation The interaction of the hnRNP family member E1B-AP5 with p53. The interaction of the hnRNP family member E1B-AP5 with p53. FEBS Lett. (0014-5793) 2005 imex curation Barral PM., Rusch A., Turnell AS., Gallimore PH., Byrd PJ., Dobner T., Grand RJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer no Pull down experiments were performed using lysates from A549 cells, HCT116 cells, C33A cells and AdE1HEK293 cells (HEK293 cells transformed with Ad5 early region 1 DNA), and Ad12E1HER2 cells (human embryonic retinoblasts (HER2 transformed with the Ad12 E1 region). r.j.a.grand@bham.ac.uk DAVET Only protein-protein interactions human-er2 Homo sapiens embryonic retinoblasts cells line HER2 er2 Human embryonic retinoblast cell line HER2 anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Barral PM., Rusch A., Turnell AS., Gallimore PH., Byrd PJ., Dobner T., Grand RJ. Apoptosis - Interactions involving proteins with a function related to apoptosis no Pull down experiments were performed using lysates from A549 cells, HCT116 cells, C33A cells and AdE1HEK293 cells (HEK293 cells transformed with Ad5 early region 1 DNA), and Ad12E1HER2 cells (human embryonic retinoblasts (HER2 transformed with the Ad12 E1 region). r.j.a.grand@bham.ac.uk Accepted 2007-DEC-23 by DAVET. FEBS Lett. (0014-5793) 2005 DAVET Only protein-protein interactions imex curation The interaction of the hnRNP family member E1B-AP5 with p53. The interaction of the hnRNP family member E1B-AP5 with p53. FEBS Lett. (0014-5793) 2005 imex curation Barral PM., Rusch A., Turnell AS., Gallimore PH., Byrd PJ., Dobner T., Grand RJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer no Pull down experiments were performed using lysates from A549 cells, HCT116 cells, C33A cells and AdE1HEK293 cells (HEK293 cells transformed with Ad5 early region 1 DNA), and Ad12E1HER2 cells (human embryonic retinoblasts (HER2 transformed with the Ad12 E1 region). r.j.a.grand@bham.ac.uk DAVET Only protein-protein interactions human-hct116 Human colon carcinoma HCT116 cells hct116 Human colon carcinoma line HCT116 anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Barral PM., Rusch A., Turnell AS., Gallimore PH., Byrd PJ., Dobner T., Grand RJ. Apoptosis - Interactions involving proteins with a function related to apoptosis no Pull down experiments were performed using lysates from A549 cells, HCT116 cells, C33A cells and AdE1HEK293 cells (HEK293 cells transformed with Ad5 early region 1 DNA), and Ad12E1HER2 cells (human embryonic retinoblasts (HER2 transformed with the Ad12 E1 region). r.j.a.grand@bham.ac.uk Accepted 2007-DEC-23 by DAVET. FEBS Lett. (0014-5793) 2005 DAVET Only protein-protein interactions imex curation The interaction of the hnRNP family member E1B-AP5 with p53. The interaction of the hnRNP family member E1B-AP5 with p53. FEBS Lett. (0014-5793) 2005 imex curation Barral PM., Rusch A., Turnell AS., Gallimore PH., Byrd PJ., Dobner T., Grand RJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer no Pull down experiments were performed using lysates from A549 cells, HCT116 cells, C33A cells and AdE1HEK293 cells (HEK293 cells transformed with Ad5 early region 1 DNA), and Ad12E1HER2 cells (human embryonic retinoblasts (HER2 transformed with the Ad12 E1 region). r.j.a.grand@bham.ac.uk DAVET Only protein-protein interactions human-mcf7 Homo sapiens mammary carcinoma cells mcf7 mammary carcinoma cells anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Barral PM., Rusch A., Turnell AS., Gallimore PH., Byrd PJ., Dobner T., Grand RJ. Apoptosis - Interactions involving proteins with a function related to apoptosis no Pull down experiments were performed using lysates from A549 cells, HCT116 cells, C33A cells and AdE1HEK293 cells (HEK293 cells transformed with Ad5 early region 1 DNA), and Ad12E1HER2 cells (human embryonic retinoblasts (HER2 transformed with the Ad12 E1 region). r.j.a.grand@bham.ac.uk Accepted 2007-DEC-23 by DAVET. FEBS Lett. (0014-5793) 2005 DAVET Only protein-protein interactions imex curation hnrl1_human Heterogeneous nuclear ribonucleoprotein U-like protein 1 E1BAP5 HNRNPUL1 HNRPUL1 Adenovirus early region 1B-associated protein 5 E1B-55 kDa-associated protein 5 protein protein human Homo sapiens Human MDVRRLKVNELREELQRRGLDTRGLKAELAERLQAALEAEEPDDERELDADDEPGRPGHINEEVETEGGSELEGTAQPPPPGLQPHAEPGGYSGPDGHYAMDNITRQNQFYDTQVIKQENESGYERRPLEMEQQQAYRPEMKTEMKQGAPTSFLPPEASQLKPDRQQFQSRKRPYEENRGRGYFEHREDRRGRSPQPPAEEDEDDFDDTLVAIDTYNCDLHFKVARDRSSGYPLTIEGFAYLWSGARASYGVRRGRVCFEMKINEEISVKHLPSTEPDPHVVRIGWSLDSCSTQLGEEPFSYGYGGTGKKSTNSRFENYGDKFAENDVIGCFADFECGNDVELSFTKNGKWMGIAFRIQKEALGGQALYPHVLVKNCAVEFNFGQRAEPYCSVLPGFTFIQHLPLSERIRGTVGPKSKAECEILMMVGLPAAGKTTWAIKHAASNPSKKYNILGTNAIMDKMRVMGLRRQRNYAGRWDVLIQQATQCLNRLIQIAARKKRNYILDQTNVYGSAQRRKMRPFEGFQRKAIVICPTDEDLKDRTIKRTDEEGKDVPDHAVLEMKANFTLPDVGDFLDEVLFIELQREEADKLVRQYNEEGRKAGPPPEKRFDNRGGGGFRGRGGGGGFQRYENRGPPGGNRGGFQNRGGGSGGGGNYRGGFNRSGGGGYSQNRWGNNNRDNNNSNNRGSYNRAPQQQPPPQQPPPPQPPPQQPPPPPSYSPARNPPGASTYNKNSNIPGSSANTSTPTVSSYSPPQPSYSQPPYNQGGYSQGYTAPPPPPPPPPAYNYGSYGGYNPAPYTPPPPPTAQTYPQPSYNQYQQYAQQWNQYYQNQGQWPPYYGNYDYGSYSGNTQGGTSTQ DIP protein Q9BUJ2 original sequence version: 124 6E57C0271E5F3A77 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 hnrpul1-tp53 3 8 unspecified role unspecified role prey prey human-a_549 Homo sapiens Caucasian lung carcinoma cell line a_549 Human Caucasian lung carcinoma 7 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecobb Escherichia coli (strain B / BL21) physical association physical association 2 A It can be seen that p53 is bound by GST-E1B-AP5 to a comparable extent in all of the cell lines examined. It was isolated as a binding partner for E1B-AP5 from tumour cell lines expressing wild type (A549) hnrpul1-tp53-1 3 8 unspecified role unspecified role prey prey human-hct116 Human colon carcinoma HCT116 cells hct116 Human colon carcinoma line HCT116 7 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecobb Escherichia coli (strain B / BL21) physical association physical association 2 A It can be seen that p53 is bound by GST-E1B-AP5 to a comparable extent in all of the cell lines examined. hnrpul1-tp53-2 3 7 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecobb Escherichia coli (strain B / BL21) 8 unspecified role unspecified role prey prey human-c33a Homo sapiens epihelial cervix carcinoma cells c33a C33A cells epithelial-like cells, grown as monolayer; derived from cervical carcinoma physical association physical association 2 A It can be seen that p53 is bound by GST-E1B-AP5 to a comparable extent in all of the cell lines examined. C33A cells express mutant p53. hnrpul1-tp53-3 3 8 unspecified role unspecified role prey prey human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. 7 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecobb Escherichia coli (strain B / BL21) physical association physical association 2 A It can be seen that p53 is bound by GST-E1B-AP5 to a comparable extent in all of the cell lines examined. It was isolated as a binding partner for E1B-AP5 from tumour cell lines expressing wild type (A549) and mutant protein (C33A) and from adenovirus transformed cell lines (Ad12E1HER2 cells and Ad5E1911 cells). The HEK293 cells (Ad5293) from which lysates were prepared, were transformed with the Ad5 early region 1 DNA. hnrpul1-tp53-4 3 8 unspecified role unspecified role prey prey human-er2 Homo sapiens embryonic retinoblasts cells line HER2 er2 Human embryonic retinoblast cell line HER2 7 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecobb Escherichia coli (strain B / BL21) physical association physical association 2 A The human embryonic retinoblast cell line HER2 (Ad5293) from which lysates were prepared, was transformed with the Ad12 E1 region. It can be seen that p53 is bound by GST-E1B-AP5 to a comparable extent in all of the cell lines examined. It was isolated as a binding partner for E1B-AP5 from tumour cell lines expressing wild type (A549) and mutant protein (C33A) and from adenovirus transformed cell lines (Ad12E1HER2 cells and Ad5E1911 cells). tp53-hnrpul1 6 7 unspecified role unspecified role prey prey 8 unspecified role unspecified role bait bait physical association physical association 2 B p53 was immuno-precipitated from cell lysates of MCF7 and Ad12E1HER2 cells using a rabbit polyclonal antibody. Co-precipitated E1B-AP5 was identified by Western blotting tp53-hnrpul1-1 4 8 unspecified role unspecified role bait bait 7 unspecified role unspecified role prey prey physical association physical association 2 B p53 was immuno-precipitated from cell lysates of MCF7 and Ad12E1HER2 cells using a rabbit polyclonal antibody. Co-precipitated E1B-AP5 was identified by Western blotting hrnpul1-tp53 1 7 unspecified role unspecified role bait bait 8 unspecified role unspecified role prey prey physical association physical association 2 C In reciprocal experiments E1B-AP5 was immunoprecipitated with a rabbit polyclonal antibody. Coimmunoprecipitating p53 was detected using the monoclonal antibody D01 in Western blots hrnpul1-tp53-1 5 7 unspecified role unspecified role bait bait 8 unspecified role unspecified role prey prey physical association physical association 2 C In reciprocal experiments E1B-AP5 was immunoprecipitated with a rabbit polyclonal antibody. Coimmunoprecipitating p53 was detected using the monoclonal antibody D01 in Western blots tp53-hrnpul1 2 8 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecobb Escherichia coli (strain B / BL21) 7 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined n-terminal sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain c-terminal sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction 3 E1B-AP5 was labelled with [L-a-35S]methionine in in vitro transcription-translation assays and shown to interact with GST-p53 Interaction can be seen with the C-terminal and central regions and to a somewhat lesser extent with the N-terminal region. (Densitometric scanning of the autoradiograph indicates that 8%, 2%, 9% and 5% of the input of full length, N-terminal fragment, central fragment and C-terminal fragment, respectively, bound to the GST-p53.) The C-terminal and central region polypeptides of E1B-AP5 overlap from amino acids 395-732 and it is possible that these residues encompass a major binding site for p53. tp53-hrnpul1-1 2 8 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined c-terminal sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) 7 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro direct interaction direct interaction 4 E1B-AP5 was labelled with [L-a-35S]methionine in in vitro transcription-translation assays and shown to interact with GST-p53 The results indicate that the major site of interaction p53 lies C-terminal to aa 318.