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 schwartz-2002-1 Rad9 phosphorylation sites couple Rad53 to the Saccharomyces cerevisiae DNA damage checkpoint. in vivo in vivo coip coimmunoprecipitation co-immunoprecipitation CoIp immunoprecipitation Co-IP co-immunoprecipitation CoIp immunoprecipitation Co-IP coip predetermined predetermined participant predetermined Schwartz MF., Duong JK., Sun Z., Morrow JS., Pradhan D., Stern DF. Mol. Cell (1097-2765) 2002 schwartz-2002-2 Rad9 phosphorylation sites couple Rad53 to the Saccharomyces cerevisiae DNA damage checkpoint. in vitro In vitro experimental interac experimental interaction detection experimental interac predetermined predetermined participant predetermined Schwartz MF., Duong JK., Sun Z., Morrow JS., Pradhan D., Stern DF. Mol. Cell (1097-2765) 2002 rad9_yeast DNA repair protein RAD9 YD9934.02C YDR217C RAD9 protein protein yeast Saccharomyces cerevisiae Baker's yeast MSGQLVQWKSSPDRVTQSAIKEALHSPLADGDMNEMNVPVDPLENKVNSTNIIEGSPKANPNPVKFMNTSEIFQKSLGLLDESPRHDDELNIEVGDNDRPNANILHNERTPDLDRIANFFKSNRTPGKENLLTKYQSSDLEDTPLMLRKKMTFQTPTDPLEQKTFKKLKSDTGFCYYGEQNDGEENASLEVTEADATFVQMAERSADNYDCALEGIVTPKRYKDELSKSGGMQDERVQKTQIMISAESPNSISSYDKNKITGNGRTTRNVNKVFNNNEDNIGAIEEKNPVKKKSENYSSDDLRERNNQIIQSNESEEINELEKNLNVSGRENDVNNLDIDINSAVSGTPSRNNAEEEMYSSESVNNREPSKKWIFRYSKDKTENNSNRSTQIVNNPRTQEMPLDSISIDTQPLSKSFNTETNNELETQIIVSSLSQGISAQKGPVFHSTGQTEEIKTQIINSPEQNALNATFETPVTLSRINFEPILEVPETSSPSKNTMSKPSNSSPIPKEKDTFNIHEREVETNNVFSNDIQNSSNAATRDDIIIAGSSDFNEQKEITDRIYLQLSGKQISDSGSDETERMSPNELDTKKESTIMSEVELTQELPEVEEQQDLQTSPKKLVVEEETLMEIKKSKGNSLQLHDDNKECNSDKQDGTESLDVALIEHESKGQSSELQKNLMQLFPSESQEIIQNRRTIKRRQKDTIEIGEEEENRSTKTSPTKHLKRNSDLDAASIKREPSCSITIQTGETGSGKDSKEQSYVFPEGIRTADNSFLSKDDIIFGNAVWCQYTWNYKFYPGILLEVDTNQDGCWIYFETGRSLTKDEDIYYLDIRIGDAVTFDGNEYVVVGLECRSHDLNIIRCIRGYDTVHLKKKNASGLLGKRTLIKALSSISLDLSEWAKRAKIILEDNEKNKGDAYRYLRHPIRGRKSMTNVLSPKKHTDDEKDINTHTEVYNNEIESSSEKKEIVKKDSRDALAEHAGAPSLLFSSGEIRTGNVFDKCIFVLTSLFENREELRQTIESQGGTVIESGFSTLFNFTHPLAKSLVNKGNTDNIRELALKLAWKPHSLFADCRFACLITKRHLRSLKYLETLALGWPTLHWKFISACIEKKRIVPHLIYQYLLPSGESFRLSLDSPSKGGIIKSNNIFSFYTQFLRGSNLRDQICGVKKMLNDYIVIVWGRSELDSFVKFAFACLSAGRMLTIDLPNIDVDDTEPLLNALDSLVPRIGSELSNRKLKFLIYANENNGKSQMKLLERLRSQISLKFKKFNYIFHTESKEWLIQTIINEDTGFHDDITDNDIYNTISEVR FCDAC16694484D8D rad53_yeast Serine/threonine-protein kinase RAD53 RAD53 MEC2 SAD1 Serine-protein kinase 1 SPK1 P2588 YPL153C CHEK2 homolog protein protein yeast Saccharomyces cerevisiae Baker's yeast MENITQPTQQSTQATQRFLIEKFSQEQIGENIVCRVICTTGQIPIRDLSADISQVLKEKRSIKKVWTFGRNPACDYHLGNISRLSNKHFQILLGEDGNLLLNDISTNGTWLNGQKVEKNSNQLLSQGDEITVGVGVESDILSLVIFINDKFKQCLEQNKVDRIRSNLKNTSKIASPGLTSSTASSMVANKTGIFKDFSIIDEVVGQGAFATVKKAIERTTGKTFAVKIISKRKVIGNMDGVTRELEVLQKLNHPRIVRLKGFYEDTESYYMVMEFVSGGDLMDFVAAHGAVGEDAGREISRQILTAIKYIHSMGISHRDLKPDNILIEQDDPVLVKITDFGLAKVQGNGSFMKTFCGTLAYVAPEVIRGKDTSVSPDEYEERNEYSSLVDMWSMGCLVYVILTGHLPFSGSTQDQLYKQIGRGSYHEGPLKDFRISEEARDFIDSLLQVDPNNRSTAAKALNHPWIKMSPLGSQSYGDFSQISLSQSLSQQKLLENMDDAQYEFVKAQRKLQMEQQLQEQDQEDQDGKIQGFKIPAHAPIRYTQPKSIEAETREQKLLHSNNTENVKSSKKKGNGRFLTLKPLPDSIIQESLEIQQGVNPFFIGRSEDCNCKIEDNRLSRVHCFIFKKRHAVGKSMYESPAQGLDDIWYCHTGTNVSYLNNNRMIQGTKFLLQDGDEIKIIWDKNNKFVIGFKVEINDTTGLFNEGLGMLQEQRVVLKQTAEEKDLVKKLTQMMAAQRANQPSASSSSMSAKKPPVSDTNNNGNNSVLNDLVESPINANTGNILKRIHSVSLSQSQIDPSKKVKRAKLDQTSKGPENLQFS 84A9612229CA72D1 rad53-rad9-1 9270 rad9_yeast 9272 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed phosphothreonine o-phospho-threonine opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 1.0 rad53_yeast 9273 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed binding site binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 physical association physical association false false false mint rad53-rad9-2 9270 rad9_yeast 9272 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed phosphothreonine o-phospho-threonine opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 1.0 rad53_yeast 9273 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed binding site binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 physical association physical association false false false mint Multiple Rad9 phosphorylation sites act in an additive or cooperative manner to recruit Rad53. The Rad9 residues 542-620 contain another PIKK phosphorylation site (Threo603) that is not a major binding site but is selected through two-hybrid assay ( Sun et al., 1998) rad53-rad9-3 9271 rad9_yeast 9272 unspecified role unspecified role unspecified role unspecified role purified purified phosphothreonine o-phospho-threonine opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 1.0 rad53_yeast 9273 unspecified role unspecified role unspecified role unspecified role purified purified binding site binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 association association false false false mint Multiple Rad9 phosphorylation sites act in an additive or cooperative manner to recruit Rad53. The Rad9 residues 542-620 contain another PIKK phosphorylation site (Threo603) that is not a major binding site but is selected through two-hybrid assay ( Sun et al., 1998) 2.5 millimolar rad53-rad9-4 9271 rad53_yeast 9273 unspecified role unspecified role unspecified role unspecified role purified purified binding site binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 rad9_yeast 9272 unspecified role unspecified role unspecified role unspecified role purified purified phosphothreonine o-phospho-threonine opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 1.0 association association false false false mint 1.4 micromolar