DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Direct roles of the signaling kinase RSK2 in Cdc25C activation during Xenopus oocyte maturation. Direct roles of the signaling kinase RSK2 in Cdc25C activation during Xenopus oocyte maturation. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Wang R., Jung SY., Wu CF., Qin J., Kobayashi R., Gallick GE., Kuang J. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Wang R., Jung SY., Wu CF., Qin J., Kobayashi R., Gallick GE., Kuang J. DIP original experiment: DIP-220566X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Direct roles of the signaling kinase RSK2 in Cdc25C activation during Xenopus oocyte maturation. Direct roles of the signaling kinase RSK2 in Cdc25C activation during Xenopus oocyte maturation. Direct roles of the signaling kinase RSK2 in Cdc25C activation during Xenopus oocyte maturation. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Wang R., Jung SY., Wu CF., Qin J., Kobayashi R., Gallick GE., Kuang J. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Wang R., Jung SY., Wu CF., Qin J., Kobayashi R., Gallick GE., Kuang J. DIP original experiment: DIP-220564X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Direct roles of the signaling kinase RSK2 in Cdc25C activation during Xenopus oocyte maturation. Direct roles of the signaling kinase RSK2 in Cdc25C activation during Xenopus oocyte maturation. Direct roles of the signaling kinase RSK2 in Cdc25C activation during Xenopus oocyte maturation. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Wang R., Jung SY., Wu CF., Qin J., Kobayashi R., Gallick GE., Kuang J. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Wang R., Jung SY., Wu CF., Qin J., Kobayashi R., Gallick GE., Kuang J. DIP original experiment: DIP-220565X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Direct roles of the signaling kinase RSK2 in Cdc25C activation during Xenopus oocyte maturation. ks6a3_mouse Ribosomal protein S6 kinase alpha-3 Rps6ka3 Rps6ka-rs1 Rsk2 90 kDa ribosomal protein S6 kinase 3 Mapkapk1b Ribosomal S6 kinase 2 pp90RSK2 MAP kinase-activated protein kinase 1b protein protein mouse Mus musculus Mouse MPLAQLADPWQKMAVESPSDSAENGQQIMDEPMGEEEINPQTEEGSIKEIAITHHVKEGHEKADPSQFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQLFRGFSFVAITSDDESQAMQTVGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQRRGIKKITSTAL DIP protein P18654 original sequence version: 150 DIP protein P18654 original sequence version: 126 0CD54E5918567007 mpi1b_xenla M-phase inducer phosphatase 1-B cdc25-1-b cdc25b protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MAESHIMSSEAPPKTNTGLNFRTNCRMVLNLLREKDCSVTFSPEQPLTPVTDLAVGFSNLSTFSGETPKRCLDLSNLGDETAPLPTESPDRISSGKVESPKAQFVQFDGLFTPDLGWKAKKCPRGNMNSVLPRLLCSTPSFKKTSGGQRSVSNKENEGELFKSPNCKPVALLLPQEVVDSQFSPTPENKVDISLDEDCEMNILGSPISADPPCLDGAHDDIKMQNLDGFADFFSVDEEEMENPPGAVGNLSSSMAILLSGPLLNQDIEVSNVNNISLNRSRLYRSPSMPEKLDRPMLKRPVRPLDSETPVRVKRRRSTSSSLQPQEENFQPQRRGTSLKKTLSLCDVDISTVLDEDCGHRQLIGDFTKVYALPTVTGRHQDLRYITGETLAALIHGDFSSLVEKIFIIDCRYPYEYDGGHIKGALNLHRQEEVTDYFLKQPLTPTMAQKRLIIIFHCEFSSERGPKMCRFLREEDRARNEYPSLYYPELYLLKGGYKDFFPEYKELCEPQSYCPMHHQDFREELLKFRTKCKTSVGDRKRREQIARIMKL DIP protein P30309 original sequence version: 67 cdc25_1_b-rps6ka3-1 2 4 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli 5 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 300-349 Region 300-349 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain pS317 pS317 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 modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain pT318 pT318 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 modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain P30309:p.Ser319Ala S319A mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain S A This feature has been corrected as a result of our quality control procedures. The original label was 'S319A'. Wed May 02 15:06:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser319ala' Tue Jun 30 20:25:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser319Ala' P30309:p.[Ser317Ala;Thr318Ala;Ser319Ala] S317A/T318A/S319A mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain S A certain certain sequence position certain certain certain sequence position certain T A certain certain sequence position certain certain certain sequence position certain S A This feature has been corrected as a result of our quality control procedures. The original label was 'S317A/T318A/S319A'. Wed May 02 14:28:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser317ala,thr318ala,ser319ala' Tue Jun 30 15:48:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ser317Ala;Thr318Ala;Ser319Ala]' Region 317-321 Region 317-321 required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation cdc25_1_b-rps6ka3-2 1 4 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli 5 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 251-353 Region 251-353 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain P30309:p.[Ser317Ala;Thr318Ala;Ser319Ala] S317A/T318A/S319A mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain S A certain certain sequence position certain certain certain sequence position certain T A certain certain sequence position certain certain certain sequence position certain S A This feature has been corrected as a result of our quality control procedures. The original label was 'S317A/T318A/S319A'. Wed May 02 18:26:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser317ala,thr318ala,ser319ala' Tue Jun 30 17:44:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ser317Ala;Thr318Ala;Ser319Ala]' pRes pRes phosphorus containing modified residue phosphorus containing modified residue western blot western blot Immuno blot Immuno blot undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined pS319 pS319 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 substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain pT318 pT318 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 substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation Deletion of region 317-321 decreased the interaction rate/strength. cdc25_1_b-rps6ka3-3 3 4 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli 5 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 278-308 Region 278-308 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain P30309:p.Ser287Ala S287A mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain S A This feature has been corrected as a result of our quality control procedures. The original label was 'S287A'. Wed May 02 15:42:13 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser287ala' Tue Jun 30 17:54:47 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser287Ala' ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation