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 kumagai-1998-1 14-3-3 proteins act as negative regulators of the mitotic inducer Cdc25 in Xenopus egg extracts. in vivo in vivo coip coimmunoprecipitation co-immunoprecipitation CoIp immunoprecipitation Co-IP co-immunoprecipitation CoIp immunoprecipitation Co-IP coip predetermined predetermined participant predetermined Kumagai A., Yakowec PS., Dunphy WG. Mol. Biol. Cell (1059-1524) 1998 kumagai-1998-2 14-3-3 proteins act as negative regulators of the mitotic inducer Cdc25 in Xenopus egg extracts. in vitro In vitro pull down pull down predetermined predetermined participant predetermined Kumagai A., Yakowec PS., Dunphy WG. Mol. Biol. Cell (1059-1524) 1998 o57468_xenla ywhae.S ywhae XELAEV_18014582mg protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MEEREDLVYRAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKSICNDILDVLDKHLIPAASSGESKVFYYKMKGDYHRYLAEFAQGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEDQNKEALQDVEDENQ mint mpip2_xenla M-phase inducer phosphatase 2 cdc25-2 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MYILLTLLTKSTMESSCDNFEGLEHYYYTDAEPSSKCNKFQASGGSGVVMAESHIMSSEAPPKSNPGLNIRTNCRMILNLLREKDCSVTFSPEQPLTPVTDLAVGFSNLSTFSGETPKRCLDLSNLGDETAPLPTESPDRMSSGKLESPKTQFVQFGGLFTPDLAWKAKKCPKRNMNSVLPHLLCSTPSFKKASGGQRSLSNKENEGELFKNPNCKPVALLLPQEVVDSQLSPTPENKVDISLEEDCEMNILGSPISADPPCLDGAHDDIKMQNLDGFADFFSVDEEEMENPPGAVGNLSCSMAILLSGPLLNQDVEISNVNNISLNRSRLYRSPSMPEKLDRPMLKRPVRPLDSETPVRVKRRRSTSSPLQPEEENCQPQRRGTSLKKTLSLCDVDISTVLDEDCGHRQLIGDFSKVYALPTVTGRHQDLRYITGETLAALMHGDFNSLVEKFFIIDCRYPYEYDGGHIKSAFNLHRQEEVTDYFLQQPLTPLMVQKRLIIIFHCEFSSERGPKMCRFLREEDRASNDYPSLYYPELYLLKGGYKDFFPEYKELCEPQSYCPMHHQDFREDLLKFRTKCKTSVGDRKRREQVARLMKL This protein functions as a dosage-dependent inducer in mitotic control. It is a tyrosine protein phosphatase required for progression of the cell cycle. It may directly dephosphorylate p34(cdc2) and activate the p34(cdc2) kinase activity mint cdc25_2-ywhae-1 4042 o57468_xenla 4044 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 1.0 mpip2_xenla 4045 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level phosphoserine o-phospho-serine opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 1.0 physical association physical association false false false 14-3-3 epsilon of Xenopus binds to Cdc25 phosphorylated by Chk1 or Chk2 in Serine during interphase. When bound to 14-3-3, the cdc25 is retained in the cytoplasm and, thus, cannot activate the Cdc2 mitoyic kinase. mint cdc25_2-ywhae-2 4043 o57468_xenla 4044 unspecified role unspecified role prey prey purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 1.0 mpip2_xenla 4045 unspecified role unspecified role bait bait purified purified phosphoserine o-phospho-serine opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 1.0 direct interaction direct interaction false false false 14-3-3 epsilon of Xenopus binds to Cdc25 phosphorylated by Chk1 or Chk2 in Serine during interphase. When bound to 14-3-3, the cdc25 is retained in the cytoplasm and, thus, cannot activate the Cdc2 mitoyic kinase. mint