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 retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev. (0890-9369) 1993 Durfee T., Becherer K., Chen PL., Yeh SH., Yang Y., Kilburn AE., Lee WH., Elledge SJ. Virus - Publications including interactions involving viral proteins no manually identified in vitro In vitro pull down pull down predetermined predetermined participant predetermined Durfee T., Becherer K., Chen PL., Yeh SH., Yang Y., Kilburn AE., Lee WH., Elledge SJ. Virus - Publications including interactions involving viral proteins no manually identified Genes Dev. (0890-9369) 1993 The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev. (0890-9369) 1993 Durfee T., Becherer K., Chen PL., Yeh SH., Yang Y., Kilburn AE., Lee WH., Elledge SJ. Virus - Publications including interactions involving viral proteins no manually identified in vivo in vivo coip coimmunoprecipitation co-immunoprecipitation CoIp immunoprecipitation Co-IP co-immunoprecipitation CoIp immunoprecipitation Co-IP coip predetermined predetermined participant predetermined Durfee T., Becherer K., Chen PL., Yeh SH., Yang Y., Kilburn AE., Lee WH., Elledge SJ. Virus - Publications including interactions involving viral proteins no manually identified Genes Dev. (0890-9369) 1993 The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev. (0890-9369) 1993 Durfee T., Becherer K., Chen PL., Yeh SH., Yang Y., Kilburn AE., Lee WH., Elledge SJ. Virus - Publications including interactions involving viral proteins no manually identified in vivo in vivo 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Durfee T., Becherer K., Chen PL., Yeh SH., Yang Y., Kilburn AE., Lee WH., Elledge SJ. Virus - Publications including interactions involving viral proteins no manually identified Genes Dev. (0890-9369) 1993 pp1a_human Serine/threonine-protein phosphatase PP1-alpha catalytic subunit PPP1CA PPP1A protein protein human Homo sapiens Human MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADKNKGKYGQFSGLNPGGRPITPPRNSAKAKK DIP protein P62136 original sequence version: 72 DIP protein P62136 original sequence version: 76 DIP protein P62136 original sequence version: 123 DIP protein P62136 original sequence version: 126 DIP protein P62136-1 original sequence version: 98 60C37E1AD9831DAC 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 rb1-ppp1ca-5 1 5 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-1512654: original sequence: 768-881 : ILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIE Stoichiometry: 1.0 4 unspecified role unspecified role prey prey purified purified Stoichiometry: 1.0 direct interaction direct interaction PP1-alpha2 binds to hypophorylated forms of p110RB in a cell cycle dpendent manner (from mitosis to early G1) homomint mint rb1-ppp1ca-6 3 4 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 5 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 tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 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-1512667: original sequence: 768-881 : ILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIE Stoichiometry: 1.0 physical association physical association PP1-alpha2 binds to hypophorylated forms of p110RB in a cell cycle dpendent manner (from mitosis to early G1) homomint mint rb1-ppp1ca-7 2 4 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level Stoichiometry: 1.0 5 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level 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-1512686: original sequence: 768-881 : ILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIE Stoichiometry: 1.0 physical association physical association PP1-alpha2 binds to hypophorylated forms of p110RB in a cell cycle dpendent manner (from mitosis to early G1) homomint mint