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 http://mint.bio.uniroma2.it/mint barbosa-1990-1 The region of the HPV E7 oncoprotein homologous to adenovirus E1a and Sv40 large T antigen contains separate domains for Rb binding and casein kinase II phosphorylation. unknown Unknown enzymatic study enzymatic study predetermined predetermined participant predetermined Barbosa MS., Edmonds C., Fisher C., Schiller JT., Lowy DR., Vousden KH. Virus - Publications including interactions involving viral proteins EMBO J. (0261-4189) 1990 rapid curation rapid curation barbosam-1990-1 The region of the HPV E7 oncoprotein homologous to adenovirus E1a and Sv40 large T antigen contains separate domains for Rb binding and casein kinase II phosphorylation. unknown Unknown coip coimmunoprecipitation co-immunoprecipitation CoIp immunoprecipitation Co-IP co-immunoprecipitation CoIp immunoprecipitation Co-IP coip predetermined predetermined participant predetermined Barbosa MS., Edmonds C., Fisher C., Schiller JT., Lowy DR., Vousden KH. Virus - Publications including interactions involving viral proteins EMBO J. (0261-4189) 1990 rapid curation rapid curation ve7_hpv16 Protein E7 E7 protein protein hpv16 Human papillomavirus type 16 MHGDTPTLHEYMLDLQPETTDLYCYEQLNDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPICSQKP csk21_human Casein kinase II subunit alpha CSNK2A1 CK2A1 protein protein human Homo sapiens Human MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMGSSSMPGGSTPVSSANMMSGISSVPTPSPLGPLAGSPVIAAANPLGMPVPAAAGAQQ ve7_hpv18 Protein E7 E7 protein protein hpv18 Human papillomavirus type 18 MHGPKATLQDIVLHLEPQNEIPVDLLCHEQLSDSEEENDEIDGVNHQHLPARRAEPQRHTMLCMCCKCEARIKLVVESSADDLRAFQQLFLNTLSFVCPWCASQQ ve7_hpv6b Protein E7 E7 protein protein hpv6b Human papillomavirus type 6b MHGRHVTLKDIVLDLQPPDPVGLHCYEQLVDSSEDEVDEVDGQDSQPLKQHFQIVTCCCGCDSNVRLVVQCTETDIREVQQLLLGTLNIVCPICAPKT E7 protein has both transforming and trans-activating activities. Disrupts the function of host retinoblastoma protein RB1/pRb, which is a key regulator of the cell cycle. Induces the disassembly of the E2F1 transcription factors from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. Interferes with histone deacetylation mediated by HDAC1 and HDAC2, leading to activation of transcription mint rb_human Retinoblastoma-associated protein pRb pp110 p105-Rb RB1 p110-RB1 protein protein human Homo sapiens Human MPPKTPRKTAATAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPMLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPHTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHLESACPLNLPLQNNHTAADMYLSPVRSPKKKGSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEK csnk2a1-e7 743169 ve7_hpv16 743171 unspecified role unspecified role neutral component neutral component csk21_human 743172 unspecified role unspecified role neutral component neutral component phosphorylation phosphorylation reaction phosphorylation false false false F3 F8 homomint mint csnk2a1-e7-1 743169 ve7_hpv18 743173 unspecified role unspecified role neutral component neutral component csk21_human 743172 unspecified role unspecified role neutral component neutral component phosphorylation phosphorylation reaction phosphorylation false false false F8 homomint mint csnk2a1-e7-2 743169 ve7_hpv6b 743174 unspecified role unspecified role neutral component neutral component csk21_human 743172 unspecified role unspecified role neutral component neutral component phosphorylation phosphorylation reaction phosphorylation false false false F8 homomint mint e7-rb1-27 743170 ve7_hpv16 743171 unspecified role unspecified role bait bait rb_human 743175 unspecified role unspecified role prey prey physical association physical association false false false F7 homomint mint e7-rb1-28 743170 rb_human 743175 unspecified role unspecified role prey prey ve7_hpv18 743173 unspecified role unspecified role bait bait physical association physical association false false false F7 homomint mint e7-rb1-29 743170 ve7_hpv6b 743174 unspecified role unspecified role bait bait rb_human 743175 unspecified role unspecified role prey prey physical association physical association false false false F7 homomint mint