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 fujita-2002-1 Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization. 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 J. Biol. Chem. (0021-9258) 2002 partial coverage rapid curation fujita-2002-2 Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization. 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 J. Biol. Chem. (0021-9258) 2002 partial coverage rapid curation fujita-2002-3 Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization. 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 J. Biol. Chem. (0021-9258) 2002 partial coverage rapid curation cdn1b_human Cyclin-dependent kinase inhibitor 1B Cyclin-dependent kinase inhibitor p27 p27Kip1 CDKN1B KIP1 protein protein human Homo sapiens Human MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT 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 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 ywhaq-cdkn1b 11430 cdn1b_human 11433 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 1433t_human 11434 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed Stoichiometry: 1.0 physical association physical association false false false 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 11430 cdn1b_human 11433 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 akt1_human 11435 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed Stoichiometry: 1.0 phosphorylation phosphorylation reaction phosphorylation false false false - 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 11431 cdn1b_human 11433 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 1433t_human 11434 unspecified role unspecified role unspecified role unspecified role purified purified Stoichiometry: 1.0 association association false false false 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 11431 akt1_human 11435 unspecified role unspecified role unspecified role unspecified role purified purified Stoichiometry: 1.0 cdn1b_human 11433 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 phosphorylation phosphorylation reaction phosphorylation false false false - 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 11432 1433t_human 1433T_HUMAN 11434 unspecified role unspecified role unspecified role unspecified role cdn1b_human CDN1B_HUMAN 11433 unspecified role unspecified role unspecified role unspecified role association association false false false homomint domino mint