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 Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25. Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25. Genes Dev. (0890-9369) 1999 Kumagai A., Dunphy WG. no in vitro In vitro experimental interac experimental interaction detection experimental interac predetermined predetermined participant predetermined Kumagai A., Dunphy WG. no Genes Dev. (0890-9369) 1999 o57468_xenla ywhae.S ywhae XELAEV_18014582mg protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MEEREDLVYRAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKSICNDILDVLDKHLIPAASSGESKVFYYKMKGDYHRYLAEFAQGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEDQNKEALQDVEDENQ mint 1459137FA5090DF4 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 DB93EBD979367C4C cdc25_2-ywhae 1 2 unspecified role unspecified role unspecified role unspecified role purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-367487: original sequence: 1-255 : MEEREDLVYRAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKSICNDILDVLDKHLIPAASSGESKVFYYKMKGDYHRYLAEFAQGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEDQNKEALQDVEDEN Stoichiometry: 1.0 3 unspecified role unspecified role unspecified role unspecified role 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 range MINT-367481: original sequence: 287-287 : GFADFFSVDEEEMENPPGAV Stoichiometry: 1.0 association association 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