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 DNA-damage-responsive acetylation of pRb regulates binding to E2F-1. DNA-damage-responsive acetylation of pRb regulates binding to E2F-1. EMBO Rep. (1469-221X) 2006 imex curation Markham D., Munro S., Soloway J., O'Connor DP., La Thangue NB. Virus - Publications including interactions involving viral proteins 2009-01-08 Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Markham D., Munro S., Soloway J., O'Connor DP., La Thangue NB. Virus - Publications including interactions involving viral proteins EMBO Rep. (1469-221X) 2006 2009-01-08 Only protein-protein interactions imex curation DNA-damage-responsive acetylation of pRb regulates binding to E2F-1. DNA-damage-responsive acetylation of pRb regulates binding to E2F-1. EMBO Rep. (1469-221X) 2006 imex curation Markham D., Munro S., Soloway J., O'Connor DP., La Thangue NB. Virus - Publications including interactions involving viral proteins 2009-01-08 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 tag coip anti tag coimmunoprecipitation anti tag coip predetermined predetermined participant predetermined Markham D., Munro S., Soloway J., O'Connor DP., La Thangue NB. Virus - Publications including interactions involving viral proteins EMBO Rep. (1469-221X) 2006 2009-01-08 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 rb_human Retinoblastoma-associated protein pRb pp110 p105-Rb RB1 p110-RB1 protein protein human Homo sapiens Human MPPKTPRKTAATAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPMLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPHTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHLESACPLNLPLQNNHTAADMYLSPVRSPKKKGSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEK DIP protein P06400 original sequence version: 102 DIP protein P06400 original sequence version: 195 DIP protein P06400 original sequence version: 204 DIP protein P06400 original sequence version: 126 DIP protein P06400 original sequence version: 151 DIP protein P06400 original sequence version: 153 DIP protein P06400 original sequence version: 181 DIP protein P06400 original sequence version: 184 DIP protein P06400 original sequence version: 213 DIP protein P06400 original sequence version: 208 DIP protein P06400 original sequence version: 174 DIP protein P06400 original sequence version: 212 DIP protein P06400 original sequence version: 179 DIP protein P06400 original sequence version: 146 C8E746111E19CC32 e2f1_human Transcription factor E2F1 Retinoblastoma-associated protein 1 Retinoblastoma-binding protein 3 PBR3 E2F1 RBBP3 pRB-binding protein E2F-1 protein protein human Homo sapiens Human MALAGAPAGGPCAPALEALLGAGALRLLDSSQIVIISAAQDASAPPAPTGPAAPAAGPCDPDLLLFATPQAPRPTPSAPRPALGRPPVKRRLDLETDHQYLAESSGPARGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTTVGVGGRLEGLTQDLRQLQESEQQLDHLMNICTTQLRLLSEDTDSQRLAYVTCQDLRSIADPAEQMVMVIKAPPETQLQAVDSSENFQISLKSKQGPIDVFLCPEETVGGISPGKTPSQEVTSEEENRATDSATIVSPPPSSPPSSLTTDPSQSLLSLEQEPLLSRMGSLRAPVDEDRLSPLVAADSLLEHVREDFSGLLPEEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF DIP protein Q01094 original sequence version: 173 DIP protein Q01094 original sequence version: 168 DIP protein Q01094 original sequence version: 149 DIP protein Q01094 original sequence version: 130 DIP protein Q01094 original sequence version: 125 DIP protein Q01094 original sequence version: 153 DIP protein Q01094 original sequence version: 180 003B3F654F0C60DF rb1-mdm2-1 1 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain range MINT-1776652: original sequence: 763-928 : RLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEE tagged molecule tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Stoichiometry: 1.0 3 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role prey prey cell lysate cell lysate physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 physical association physical association F3B EMBO-Reports (Fig 3B). As a control for the integrity of the pRb mutant derivatives, we measured the binding of pRb to Mdm2, because Mdm2 interacts with the C-terminal region of pRb (Xiao et al, 1995). homomint mint rb1-e2f1-13 1 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait purified purified P06400:p.Lys874Gln mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K Q Tue Jul 12 10:07:20 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 16:56:01 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys874gln' Tue Jun 30 16:14:46 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys874Gln' range MINT-1777321: original sequence: 874-874 : EGSNPPKPLKKLRFDIEGSD tagged molecule tagged molecule tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range P06400:p.Lys873Gln mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K Q Tue Jul 12 10:07:21 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 17:13:23 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys873gln' Tue Jun 30 15:59:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys873Gln' range MINT-1777319: original sequence: 873-873 : AEGSNPPKPLKKLRFDIEGS binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain range MINT-1777317: original sequence: 763-928 : RLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEE Stoichiometry: 1.0 5 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role prey prey cell lysate cell lysate physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 physical association physical association F3B EMBO-Reports In extracts prepared from 293 cells, the binding of E2F-1 to RR873/874 was marginally reduced relative to the interaction with the wild-type pRb domain; in contrast, the binding to QQ873/874 was significantly less (Fig 3B). homomint mint rb1-e2f1-14 2 5 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell ha tagged ha tagged ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range P06400:p.Lys873Gln mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K Q Tue Jul 12 10:57:37 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 19:27:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys873gln' Tue Jun 30 20:07:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys873Gln' range MINT-1777479: original sequence: 873-873 : AEGSNPPKPLKKLRFDIEGS binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain range MINT-1777475: original sequence: 763-928 : RLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEE P06400:p.Lys874Gln mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K Q Tue Jul 12 10:21:34 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 16:07:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys874gln' Tue Jun 30 16:48:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys874Gln' range MINT-1777477: original sequence: 874-874 : EGSNPPKPLKKLRFDIEGSD Stoichiometry: 1.0 physical association physical association F3C EMBO-Reports Similar to the behaviour of the proteins in the in vitro binding assay, we found that pRb763 928 bound to E2F-1 and that altering KK873/874 to RR873/874 had a marginal effect on binding efficiency (Fig 3C). In contrast, pRb QQ873/874 was significantly reduced in its interaction with E2F-1 (Fig 3C). The interaction of pRb763 928 with E2F-1 and the influence of QQ873/874 observed in vitro is therefore recapitulated in cells. homomint mint