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 Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization. Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization. J. Biol. Chem. (0021-9258) 2002 Fujita N., Sato S., Katayama K., Tsuruo T. Virus - Publications including interactions involving viral proteins no partial coverage rapid curation in vivo in vivo coip coimmunoprecipitation co-immunoprecipitation CoIp immunoprecipitation Co-IP co-immunoprecipitation CoIp immunoprecipitation Co-IP coip predetermined predetermined participant predetermined Fujita N., Sato S., Katayama K., Tsuruo T. Virus - Publications including interactions involving viral proteins no J. Biol. Chem. (0021-9258) 2002 partial coverage rapid curation Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization. Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization. J. Biol. Chem. (0021-9258) 2002 Fujita N., Sato S., Katayama K., Tsuruo T. Virus - Publications including interactions involving viral proteins no partial coverage rapid curation in vitro In vitro experimental interac experimental interaction detection experimental interac predetermined predetermined participant predetermined Fujita N., Sato S., Katayama K., Tsuruo T. Virus - Publications including interactions involving viral proteins no J. Biol. Chem. (0021-9258) 2002 partial coverage rapid curation Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization. Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization. J. Biol. Chem. (0021-9258) 2002 Fujita N., Sato S., Katayama K., Tsuruo T. Virus - Publications including interactions involving viral proteins no partial coverage rapid curation unknown Unknown coip coimmunoprecipitation co-immunoprecipitation CoIp immunoprecipitation Co-IP co-immunoprecipitation CoIp immunoprecipitation Co-IP coip predetermined predetermined participant predetermined Fujita N., Sato S., Katayama K., Tsuruo T. Virus - Publications including interactions involving viral proteins no J. Biol. Chem. (0021-9258) 2002 partial coverage rapid curation akt1_human RAC-alpha serine/threonine-protein kinase AKT1 PKB RAC RAC-PK-alpha Protein kinase B Proto-oncogene c-Akt Protein kinase B alpha protein protein human Homo sapiens Human MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA DIP protein P31749 original sequence version: 184 DIP protein P31749 original sequence version: 168 DIP protein P31749 original sequence version: 102 DIP protein P31749 original sequence version: 110 DIP protein P31749 original sequence version: 160 DIP protein P31749 original sequence version: 136 DIP protein P31749 original sequence version: 175 DIP protein P31749 original sequence version: 201 DIP protein P31749 original sequence version: 166 DIP protein P31749 original sequence version: 178 DIP protein P31749-1 original sequence version: 194 DIP protein P31749 original sequence version: 106 DIP protein P31749 original sequence version: 141 6EAFF4F8AD436714 cdn1b_human Cyclin-dependent kinase inhibitor 1B Cyclin-dependent kinase inhibitor p27 p27Kip1 CDKN1B KIP1 protein protein human Homo sapiens Human MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT DIP protein P46527 original sequence version: 120 DIP protein P46527 original sequence version: 115 DIP protein P46527 original sequence version: 154 DIP protein P46527 original sequence version: 168 DIP protein P46527 original sequence version: 164 DIP protein P46527 original sequence version: 118 1118D58901CDF3FC 1433t_human 14-3-3 protein theta YWHAQ 14-3-3 protein tau 14-3-3 protein T-cell Protein HS1 protein protein human Homo sapiens Human MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIDNSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN DIP protein P27348 original sequence version: 164 DIP protein P27348 original sequence version: 173 175534325E9E37C4 ywhaq-cdkn1b 1 5 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 range MINT-716016: original sequence: 198-198 : PKKPGLRRRQ Stoichiometry: 1.0 6 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed Stoichiometry: 1.0 physical association physical association CoIP in 293 cells, with p27-FLAG , western with HA-14-3-3: Tau -HA binds well, epsilon and eta binds poorly, beta and zeta do not coimmunoprecipitaternThe mutants 14-3-3 tau R56A, R60A- FLAG tagged does not coimmunoprecipitate p27-HA. rnP27 binding site: p27-HA ,T198 phosphorylated by Akt, is bound by 14-3-3 tau-FLAG ( coIP)rnPeptide binding with bio-PKKPGLRRRQT (+/- P)-amidern homomint domino mint akt1-cdkn1b-1 1 5 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 range MINT-716028: original sequence: 198-198 : PKKPGLRRRQ Stoichiometry: 1.0 4 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed Stoichiometry: 1.0 phosphorylation phosphorylation reaction phosphorylation - coIP with Flag-p27 and anti Akt ( both proteins over-expressed level)rn- Akt activated phosphorylates p27 : in vivo overexpression both proteins and Akt mutants ( inactive)rn- T198 is phosphorylated by Akt:- 293 transfected with Flag-p27 and Akt ( active or inactive) with different mutants of p27 . Only T198A is not phosphorylated by Akt rn homomint mint cdkn1b-ywhaq-4 2 5 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 range MINT-716042: original sequence: 198-198 : PKKPGLRRRQ Stoichiometry: 1.0 6 unspecified role unspecified role unspecified role unspecified role purified purified Stoichiometry: 1.0 association association CoIP in 293 cells, with p27-FLAG , western with HA-14-3-3: Tau -HA binds well, epsilon and eta binds poorly, beta and zeta do not coimmunoprecipitaternThe mutants 14-3-3 tau R56A, R60A- FLAG tagged does not coimmunoprecipitate p27-HA. rnP27 binding site: p27-HA ,T198 phosphorylated by Akt, is bound by 14-3-3 tau-FLAG ( coIP)rnPeptide binding with bio-PKKPGLRRRQT (+/- P)-amidern homomint domino mint akt1-cdkn1b-2 2 4 unspecified role unspecified role unspecified role unspecified role purified purified Stoichiometry: 1.0 5 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 range MINT-716056: original sequence: 198-198 : PKKPGLRRRQ Stoichiometry: 1.0 phosphorylation phosphorylation reaction phosphorylation - coIP with Flag-p27 and anti Akt ( both proteins over-expressed level)rn- Akt activated phosphorylates p27 : in vivo overexpression both proteins and Akt mutants ( inactive)rn- T198 is phosphorylated by Akt:- 293 transfected with Flag-p27 and Akt ( active or inactive) with different mutants of p27 . Only T198A is not phosphorylated by Akt rn homomint mint cdkn1b-ywhaq-5 3 1433T_HUMAN 6 unspecified role unspecified role unspecified role unspecified role CDN1B_HUMAN 5 unspecified role unspecified role unspecified role unspecified role association association homomint domino mint