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/ Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. DNA Repair (Amst.) (1568-7864) 2009 imex curation Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. deutscwa@pbrc.edu 26-Feb-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down anti tag western anti tag western blot anti tag western Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. His-p53, His-MDM2 and GST-RPS3 were found to be expressed in E.coli and MDM2 tags were N-terminal. (From Reference 11 -Mayo et al., 1997; Ref 16 Hegde at al.,2001.) deutscwa@pbrc.edu Accepted 2015-FEB-11 by PPORRAS DNA Repair (Amst.) (1568-7864) 2009 Only protein-protein interactions imex curation Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. DNA Repair (Amst.) (1568-7864) 2009 imex curation Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. deutscwa@pbrc.edu 26-Feb-2015: Contacted by IntAct-Help. 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. fret fluorescent resonance energy transfer FRET RET FRET analysis FRET RET FRET analysis fret tag fluorescence tag visualisation by fluorescence tag fluorescence Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. deutscwa@pbrc.edu Accepted 2015-FEB-11 by PPORRAS DNA Repair (Amst.) (1568-7864) 2009 Only protein-protein interactions imex curation Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. DNA Repair (Amst.) (1568-7864) 2009 imex curation Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. deutscwa@pbrc.edu 26-Feb-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. His-p53, His-MDM2 and GST-RPS3 were found to be expressed in E.coli and MDM2 tags were N-terminal. (From Reference 11 -Mayo et al., 1997; Ref 16 Hegde at al.,2001.) Figure 5 interactions from a "8-oxodg oligonucleotide pull-down assay" have not been included as the sequence of the 8-oxodg oligonucleotide is not given. deutscwa@pbrc.edu Accepted 2015-FEB-11 by PPORRAS DNA Repair (Amst.) (1568-7864) 2009 Only protein-protein interactions imex curation Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. DNA Repair (Amst.) (1568-7864) 2009 imex curation Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. deutscwa@pbrc.edu 26-Feb-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down fingerprinting peptide massfingerprinting fingerprinting Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. deutscwa@pbrc.edu Accepted 2015-FEB-11 by PPORRAS DNA Repair (Amst.) (1568-7864) 2009 Only protein-protein interactions imex curation Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. DNA Repair (Amst.) (1568-7864) 2009 imex curation Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. deutscwa@pbrc.edu 26-Feb-2015: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro ubiquitinase assay ubiquitinase assay ubiquitinase assay western blot western blot Immuno blot Immuno blot Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. E1 and E2 enzymes were present in these assays as well, but no origins are provided, so these proteins cannot be entered as participants. deutscwa@pbrc.edu Accepted 2015-FEB-11 by PPORRAS DNA Repair (Amst.) (1568-7864) 2009 Only protein-protein interactions imex curation Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. DNA Repair (Amst.) (1568-7864) 2009 imex curation Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. deutscwa@pbrc.edu 26-Feb-2015: Contacted by IntAct-Help. Only protein-protein interactions 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 anti tag western anti tag western blot anti tag western Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. For Fig 1E I have added an interaction for Mutant and one for WT - we would not normally add the mutant as an interactor in a separate interaction, but maybe this instance justified it?? - more than a comment at any rate... deutscwa@pbrc.edu Accepted 2015-FEB-11 by PPORRAS DNA Repair (Amst.) (1568-7864) 2009 Only protein-protein interactions imex curation Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. DNA Repair (Amst.) (1568-7864) 2009 imex curation Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. deutscwa@pbrc.edu 26-Feb-2015: Contacted by IntAct-Help. 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. pla proximity ligation assay pELISA pELISA PLA antibody detection identification by antibody antibody detection Yadavilli S., Mayo L.D., Higgins M., Lain S., Hegde V., Deutsch W.A. Affinomics - Interactions curated for the Affinomics consortium. deutscwa@pbrc.edu Accepted 2015-FEB-11 by PPORRAS DNA Repair (Amst.) (1568-7864) 2009 Only protein-protein interactions imex curation mdm2_human E3 ubiquitin-protein ligase Mdm2 MDM2 p53-binding protein Mdm2 Oncoprotein Mdm2 Double minute 2 protein RING-type E3 ubiquitin transferase Mdm2 protein protein human Homo sapiens Human MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP DIP protein Q00987 original sequence version: 93 DIP protein Q00987-1 original sequence version: 192 DIP protein Q00987 original sequence version: 88 DIP protein Q00987 original sequence version: 180 DIP protein Q00987 original sequence version: 188 DIP protein Q00987 original sequence version: 189 DIP protein Q00987 original sequence version: 115 DIP protein Q00987-1 original sequence version: null DIP protein Q00987 original sequence version: 149 DIP protein Q00987 original sequence version: 146 DIP protein Q00987 original sequence version: 140 DIP protein Q00987 original sequence version: 183 DIP protein Q00987 original sequence version: 145 DIP protein Q00987 original sequence version: 182 DIP protein Q00987 original sequence version: 151 DIP protein Q00987 original sequence version: 156 DIP protein Q00987-1 original sequence version: 160 DIP protein Q00987 original sequence version: 160 DIP protein Q00987 original sequence version: 168 DIP protein Q00987 original sequence version: 186 DIP protein Q00987 original sequence version: 206 F37CE163876BC983 rs20_human 40S ribosomal protein S20 RPS20 Small ribosomal subunit protein uS10 protein protein human Homo sapiens Human MAFKDTGKTPVEPEVAIHRIRITLTSRNVKSLEKVCADLIRGAKEKNLKVKGPVRMPTKTLRITTRKTPCGEGSKTWDRFQMRIHKRLIDLHSPSEIVKQITSISIEPGVEVEVTIADA DIP protein P60866 original sequence version: 112 8802DF7894ADDF94 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 rs3_human 40S ribosomal protein S3 RPS3 Small ribosomal subunit protein uS3 OK/SW-cl.26 protein protein human Homo sapiens Human MAVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPTGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA DIP protein P23396 original sequence version: 174 6ECBB34A8EE04AAF mdm2-rps20 4 11 unspecified role unspecified role prey prey 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. 9 unspecified role unspecified role prey prey 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. 8 unspecified role unspecified role bait bait Q00987:p.Glu250_Glu252delinsAlaAlaAla mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain EVE AAA Wed May 02 14:53:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu_val_glu250-252ala_ala_ala' Tue Jun 30 20:20:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu250_Glu252delinsAlaAlaAla' n_terminus biotin tag biotin tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) association association When full length MDM2 possessing the acidic domain mutation was used as bait, binding to RPS3 was not affected, suggesting the presence of another binding site outside of the acidic domain. Figure 1C mdm2-rps3 6 8 unspecified role unspecified role bait bait 11 unspecified role unspecified role prey prey physical association physical association Figure 1Ei When full length MDM2 possessing the acidic domain mutation was used as bait, binding to RPS3 was not affected, suggesting the presence of another binding site outside of the acidic domain. mdm2-rps20-2 1 8 unspecified role unspecified role bait bait n_terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 11 unspecified role unspecified role prey prey 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 ecoli Escherichia coli (strain K12) direct interaction direct interaction Figure 2A mdm2-rps3-1 1 11 unspecified role unspecified role prey prey 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 ecoli Escherichia coli (strain K12) 10 unspecified role unspecified role bait bait region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction Figure 2B rps3-mdm2-1 3 10 unspecified role unspecified role prey prey region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 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. 11 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 k_homology_domain required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 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. association association Figure 2C mdm2-rps3-2 2 8 unspecified role unspecified role fluorescence donor fluorescence donor n_terminus 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 11 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept n_terminus yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range proximity proximity close-contact colocalization neighbourhood interaction Figure 3 oxidative stress i.e.hydrogen peroxide - but only in the nucleus. No interaction was observed in the nucleus for the phosphorylation-defective mutant YFP-T42A, as well as a lack of interaction in the cytoplasm for the phosphorylation mimic YFP-T42D. p53-rps3-3 2 11 unspecified role unspecified role fluorescence accept fluorescence acceptor fluorescence accept n_terminus yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 10 unspecified role unspecified role fluorescence donor fluorescence donor n_terminus 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 proximity proximity close-contact colocalization neighbourhood interaction Figure 3 oxidative stress i.e. hydrogen peroxide Nutlin-3 -a cis-imidazoline analog which inhibits the interaction between mdm2 and tumour suppressor p53, but as shown here, it inhibits only under conditions of oxidative stress. The RPS3 mutant -T42D no longer was able to interact with cytoplasmic CFP-p53, but did maintain the ability to interact with nuclear CFP-p53. RPS3 mutant YFP-T42A only interacted with cytoplasmic CFP-p53. rps3-tp53 7 11 unspecified role unspecified role neutral component neutral component 10 unspecified role unspecified role neutral component neutral component proximity proximity close-contact colocalization neighbourhood interaction Figure 4 conditions of oxidative stress- hydrogen peroxide rps3-tp53-1 7 11 unspecified role unspecified role neutral component neutral component 8 unspecified role unspecified role neutral component neutral component proximity proximity close-contact colocalization neighbourhood interaction Figure 4 conditions of oxidative stress- hydrogen peroxide mdm2-tp53-22 5 8 enzyme enzyme neutral component neutral component Q00987:p.Cys464Ser mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain C S Wed May 02 15:27:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys464ser' Tue Jun 30 17:51:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys464Ser' ecoli Escherichia coli (strain K12) 10 enzyme target enzyme target substrate substrate neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) ubiquitination ubiquitination reaction ubiquitination E1 and E2 enzymes were present in these assays as well, but no origins are provided, so these proteins cannot be entered as participants. Figure 6 mdm2-rps3-3 5 11 competitor competitor competitor neutral component neutral component 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 ecoli Escherichia coli (strain K12) 10 enzyme target enzyme target substrate substrate neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 8 enzyme enzyme neutral component neutral component Q00987:p.Cys464Ser mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain C S Wed May 02 17:47:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys464ser' Tue Jun 30 16:18:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys464Ser' ecoli Escherichia coli (strain K12) ubiquitination ubiquitination reaction ubiquitination E1 and E2 enzymes were present in these assays as well, but no origins are provided, so these proteins cannot be entered as participants. Figure 6i mdm2-rps20-3 3 11 unspecified role unspecified role prey prey 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. 8 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain true Q00987:p.Glu250_Glu252delinsAlaAlaAla mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain true EVE AAA Wed May 02 17:47:44 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu_val_glu250-252ala_ala_ala' Tue Jun 30 19:52:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu250_Glu252delinsAlaAlaAla' n_terminus biotin tag biotin tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range true chemical synthesis Chemical synthesis (Chemical synthesis) physical association physical association When full length MDM2 possessing the acidic domain mutation was used as bait, binding to RPS3 was not affected, suggesting the presence of another binding site outside of the acidic domain. Figure 1C -RHS