DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. Nature structural & molecular biology 2014 imex curation Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. DIP original experiment: DIP-260918X Nature structural & molecular biology 2014 IMEx The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. Nature structural & molecular biology 2014 imex curation Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. DIP original experiment: DIP-260913X Nature structural & molecular biology 2014 IMEx The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. Nature structural & molecular biology 2014 imex curation Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. DIP original experiment: DIP-260921X Nature structural & molecular biology 2014 IMEx The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. Nature structural & molecular biology 2014 imex curation Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. DIP original experiment: DIP-260916X Nature structural & molecular biology 2014 IMEx The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. Nature structural & molecular biology 2014 imex curation Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. Only protein-protein interactions human Homo sapiens Human anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. DIP original experiment: DIP-260915X Nature structural & molecular biology 2014 IMEx The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. Nature structural & molecular biology 2014 imex curation Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. DIP original experiment: DIP-260912X Nature structural & molecular biology 2014 IMEx The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. Nature structural & molecular biology 2014 imex curation Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. DIP original experiment: DIP-260914X Nature structural & molecular biology 2014 IMEx The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. Nature structural & molecular biology 2014 imex curation Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. DIP original experiment: DIP-260920X Nature structural & molecular biology 2014 IMEx The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. Nature structural & molecular biology 2014 imex curation Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. DIP original experiment: DIP-260919X Nature structural & molecular biology 2014 IMEx The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. The DNA-binding domain mediates both nuclear and cytosolic functions of p53. Nature structural & molecular biology 2014 imex curation Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Follis AV., Llambi F., Ou L., Baran K., Green DR., Kriwacki RW. DIP original experiment: DIP-260917X Nature structural & molecular biology 2014 IMEx The DNA-binding domain mediates both nuclear and cytosolic functions of p53. bid_human BH3-interacting domain death agonist p22 BID BID protein protein human Homo sapiens Human MDCEVNNGSSLRDECITNLLVFGFLQSCSDNSFRRELDALGHELPVLAPQWEGYDELQTDGNRSSHSRLGRIEADSESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSRSEEDRNRDLATALEQLLQAYPRDMEKEKTMLVLALLLAKKVASHTPSLLRDVFHTTVNFINQNLRTYVRSLARNGMD DIP protein P55957 original sequence version: 105 DIP protein P55957 original sequence version: 114 DIP protein P55957-1 original sequence version: 132 DIP protein P55957 original sequence version: 144 B17A07334C1AFBEF 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 q07817-1 Bcl-2-like protein 1 BCLX Apoptosis regulator Bcl-X BCL2L1 BCL2L Bcl-xL protein protein human Homo sapiens Human MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK DIP protein Q07817 original sequence version: 82 DIP protein Q07817 original sequence version: 86 DIP protein Q07817-1 original sequence version: 100 DIP protein Q07817-1 original sequence version: 108 DIP protein Q07817 original sequence version: 131 DIP protein Q07817-1 original sequence version: 110 DIP protein Q07817-1 original sequence version: 135 DIP protein Q07817-1 original sequence version: 131 DIP protein Q07817-1 original sequence version: 172 DIP protein Q07817-1 original sequence version: 174 DIP protein Q07817 original sequence version: 174 DIP protein Q07817-1 original sequence version: 189 DIP protein Q07817-1 original sequence version: 192 DIP protein Q07817 original sequence version: 190 E09D3CDD851AE9BE bax_human Apoptosis regulator BAX BAX BCL2L4 Bcl-2-like protein 4 protein protein human Homo sapiens Human MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG DIP protein Q07812 original sequence version: 73 DIP protein Q07812 original sequence version: 156 DIP protein Q07812 original sequence version: 92 DIP protein Q07812 original sequence version: 94 DIP protein Q07812-1 original sequence version: 93 DIP protein Q07812 original sequence version: 95 DIP protein Q07812 original sequence version: 120 DIP protein Q07812 original sequence version: 126 DIP protein Q07812 original sequence version: 143 DIP protein Q07812 original sequence version: 172 DIP protein Q07812 original sequence version: 175 6C0CDB0A7DEE4994 bcl2l1-tp53-6 7 13 unspecified role unspecified role unspecified role unspecified role Region 1-211 Region 1-211 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 1-102 Region 1-102 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Region 102-312 Region 102-312 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction bcl2l1-tp53-9 6 13 unspecified role unspecified role unspecified role unspecified role Region 1-211 Region 1-211 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 1-102 Region 1-102 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction bcl2l1-tp53-10 8 13 unspecified role unspecified role unspecified role unspecified role FLuorescein-label FLuorescein-label fluorescein fluorescein label fluorescein certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction bcl2l1-bax-8 4 14 unspecified role unspecified role prey prey human Homo sapiens Human 12 unspecified role unspecified role prey prey human Homo sapiens Human 13 unspecified role unspecified role bait bait CFP-tag CFP-tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human association association bcl2l1-bax-9 1 14 unspecified role unspecified role prey prey human Homo sapiens Human 13 unspecified role unspecified role bait bait CFP-tag CFP-tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human physical association physical association bcl2l1-tp53-11 9 13 unspecified role unspecified role unspecified role unspecified role FLuorescein-label FLuorescein-label fluorescein fluorescein label fluorescein certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 1-360 Region 1-360 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P04637:p.Lys120Glu K120E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K120E'. Wed May 02 20:32:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys120glu' Tue Jun 30 17:44:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys120Glu' P04637:p.[His178Asp;Glu180Lys] H178D/E180K mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain E K certain certain sequence position certain certain certain sequence position certain H D This feature has been corrected as a result of our quality control procedures. The original label was 'H178D/E180K'. Wed May 02 15:07:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his178asp,glu180lys' Tue Jun 30 19:55:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[His178Asp;Glu180Lys]' ecolx Escherichia coli direct interaction direct interaction bcl2l1-bid-5 3 11 unspecified role unspecified role unspecified role unspecified role Region 79-103 Region 79-103 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 13 unspecified role unspecified role unspecified role unspecified role Region 1-211 Region 1-211 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction bcl2l1-tp53-12 2 13 unspecified role unspecified role unspecified role unspecified role Region 1-211 Region 1-211 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 102-312 Region 102-312 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction tp53-bcl2l1-4 5 13 unspecified role unspecified role prey prey human Homo sapiens Human 12 unspecified role unspecified role bait bait P04637:p.Lys120Glu K120E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain K E This feature has been corrected as a result of our quality control procedures. The original label was 'K120E'. Wed May 02 14:34:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys120glu' Tue Jun 30 17:24:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys120Glu' P04637:p.Glu180Lys E180K mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain E K This feature has been corrected as a result of our quality control procedures. The original label was 'E180K'. Wed May 02 16:33:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu180lys' Tue Jun 30 17:27:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu180Lys' P04637:p.Asp186Ala D168A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain D A Fri Jul 28 10:41:46 BST 2017 This feature has been corrected as a result of our quality control procedures. The original label was 'asp168ala' Wed May 02 20:09:57 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp186ala' Tue Jun 30 17:26:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp186Ala' P04637:p.[His178Asp;Glu180Lys] H178D/E180K mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain E K certain certain sequence position certain certain certain sequence position certain H D This feature has been corrected as a result of our quality control procedures. The original label was 'H178D/E180K'. Wed May 02 16:42:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his178asp,glu180lys' Tue Jun 30 17:08:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[His178Asp;Glu180Lys]' human Homo sapiens Human physical association physical association bcl2l1-tp53-13 10 12 unspecified role unspecified role prey prey human Homo sapiens Human 13 unspecified role unspecified role bait bait CFP-tag CFP-tag cfp tag cyan fluorescent protein tag CFP cyan fluorescent protein cyan fluorescent protein CFP cfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human physical association physical association