IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Activity of Cdc2 and its interaction with the cyclin Cdc13 depend on the molecular chaperone Cdc37 in Schizosaccharomyces pombe. Activity of Cdc2 and its interaction with the cyclin Cdc13 depend on the molecular chaperone Cdc37 in Schizosaccharomyces pombe. J. Cell. Sci. (0021-9533) 2006 imex curation Turnbull EL., Martin IV., Fantes PA. p.fantes@ed.ac.uk orchard Only protein-protein interactions schpm Schizosaccharomyces pombe (fission yeast) Fission yeast anti bait coip anti bait coimmunoprecipitation anti bait coip predetermined predetermined participant predetermined Turnbull EL., Martin IV., Fantes PA. p.fantes@ed.ac.uk Accepted 2007-APR-5 by ORCHARD. J. Cell. Sci. (0021-9533) 2006 orchard Only protein-protein interactions imex curation cg23_schpo G2/mitotic-specific cyclin cdc13 cdc13 SPBC582.03 protein protein schpo Schizosaccharomyces pombe (strain ATCC 38366 / 972) Fission yeast MTTRRLTRQHLLANTLGNNDENHPSNHIARAKSSLHSSENSLVNGKKATVSSTNVPKKRHALDDVSNFHNKEGVPLASKNTNVRHTTASVSTRRALEEKSIIPATDDEPASKKRRQPSVFNSSVPSLPQHLSTKSHSVSTHGVDAFHKDQATIPKKLKKDVDERVVSKDIPKLHRDSVESPESQDWDDLDAEDWADPLMVSEYVVDIFEYLNELEIETMPSPTYMDRQKELAWKMRGILTDWLIEVHSRFRLLPETLFLAVNIIDRFLSLRVCSLNKLQLVGIAALFIASKYEEVMCPSVQNFVYMADGGYDEEEILQAERYILRVLEFNLAYPNPMNFLRRISKADFYDIQTRTVAKYLVEIGLLDHKLLPYPPSQQCAAAMYLAREMLGRGPWNRNLVHYSGYEEYQLISVVKKMINYLQKPVQHEAFFKKYASKKFMKASLFVRDWIKKNSIPLGDDADEDYTFHKQKRIQHDMKDEEW B2C267CF57F5FD36 B2C267CF57F5FD36 cdk1_schpo Cyclin-dependent kinase 1 cdc2 swo2 SPBC11B10.09 pi002 p34 protein kinase cdk1 Cell division control protein 2 Cell division protein kinase 1 protein protein schpo Schizosaccharomyces pombe (strain ATCC 38366 / 972) Fission yeast MENYQKVEKIGEGTYGVVYKARHKLSGRIVAMKKIRLEDESEGVPSTAIREISLLKEVNDENNRSNCVRLLDILHAESKLYLVFEFLDMDLKKYMDRISETGATSLDPRLVQKFTYQLVNGVNFCHSRRIIHRDLKPQNLLIDKEGNLKLADFGLARSFGVPLRNYTHEIVTLWYRAPEVLLGSRHYSTGVDIWSVGCIFAEMIRRSPLFPGDSEIDEIFKIFQVLGTPNEEVWPGVTLLQDYKSTFPRWKRMDLHKVVPNGEEDAIELLSAMLVYDPAHRISAKRALQQNYLRDFH D04EF14BA1492875 cdc37_schpo Hsp90 co-chaperone Cdc37 cdc37 SPBC9B6.10 Hsp90 chaperone protein kinase-targeting subunit Cell division control protein 37 protein protein schpo Schizosaccharomyces pombe (strain ATCC 38366 / 972) Fission yeast MAIDYSKWDKLELSDDSDIEVHPNVDKKSFIRWRQRDIHEKRAVRKQKMEDIKGAMAMNRRLLSRISEMETVLEKESPSDPYVLLGSFLEAKKSEDMDSAIPGGMSYHHMLMSLLKVIKDAEDTTEEKSMDDSDKCLRRLKSHKERLLKLLEDAQKEYDTLEAESKNYITSEDLHLGFDSTYVQKKEPEKPKKTKTKKETIQVIESLNNPTPPTDFPGAKEQASTGNAPKNPVNENESEDEEGLSLSEDGKKFANIDFGDYSSSEEFLKEHLNILADEEESDAILLEAFNAELEGKPSLAKQYVHQALLISYCRQLGPNGLSIFFQKIKDPNHQSQRLFLEDVHNTYVRIHERSAAISKEQAESGEGVEQIQLCAVDPNTKLSITIPEAGSTDPETQKARAAFESFPPNLQKALMTNDLDKINVVLGKMAVENAEEVVEKLSSTGMLSIEEGIIDTTKGETIPQLS 647238B34CABB3C5 cdc2-cdc13 1 2 unspecified role unspecified role bait bait schpm Schizosaccharomyces pombe (fission yeast) Fission yeast 3 unspecified role unspecified role prey prey schpm Schizosaccharomyces pombe (fission yeast) Fission yeast physical association physical association Figure 6A and 6B. Another possible explanation for the reduced activity of Cdc2 in cdc37ts mutants at 36c is that the ability of Cdc2 to form a stable complex with the mitotic Cdc13 might be impaired. Formation of a complex between Cdc13 and Cdc2 is essential for Cdc2 activity and entry into mitosis (Nurse, 1997). Native protein extracts were prepared from cdc37-184, cdc37-681 and cdc37+ strains cultured at 28 and 36c. For comparison, a cdc25-22 strain was treated in the same way. Immunoprecipitations were carried out with the anti-Cdc13 antibody. Western blot analysis with the anti-PSTAIR antibody revealed that the level of Cdc2 that co-precipitated with Cdc13 was reduced in cdc37ts mutants incubated at 36c (Fig. 6A,B). Western blot analysis with the anti-PSTAIR antibody revealed that the level of Cdc2 that co-precipitated with Cdc13 was reduced in cdc37ts mutant cells (cdc37-184:-ala284asp and cdc37-681:-leu285pro) incubated at 36c which may result from a breakdown of the Cdc2-Cdc13 complex, or an inability to maintain the complex. This infers that cdc37 may be involved in the formation of the cdc13-cdc2 complex. cdc2-cdc37 1 3 unspecified role unspecified role prey prey schpm Schizosaccharomyces pombe (fission yeast) Fission yeast 4 unspecified role unspecified role bait bait O94740:p.Glu287Asp mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E D Wed May 02 15:43:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu287asp' Tue Jun 30 18:06:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu287Asp' O94740:p.Leu285Pro mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain L P Wed May 02 16:11:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu285pro' Tue Jun 30 19:32:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu285Pro' schpm Schizosaccharomyces pombe (fission yeast) Fission yeast physical association physical association Figure 6C. To investigate this possibility further, the biochemical interaction between Cdc2 and Cdc37 was investigated by immunoprecipitation experiments. Immunoprecipitates of Cdc37 from cdc37+, cdc37-681 and cdc37-184 cells grown at 28 and 36c contained Cdc2, identifying a biochemical interaction between the Cdk and the molecular chaperone protein (Fig. 6C). The level of Cdc2 bound to Cdc37 was reduced in cdc37-681 and cdc37-184 protein extracts from cells cultured at both 28 and 36c compared with immunoprecipitation experiments with the cdc37+ strain ED1022 (Fig. 6C). In the reverse immunoprecipitation experiment using a Cdc2-HA-tagged strain ED1576, we were unable to detect a biochemical interaction between Cdc2 and Cdc37. It is possible that the HA tag subtly affects stability of the complex, making it harder to detect by immunoprecipitation. There was an interaction between between cdc2 and cdc37 but the level of Cdc2 that co-precipitated with Cdc37 was reduced in cdc37ts mutants incubated at both 28 and 36c. Also in the reverse immunoprecipitatin using a HA-tagged strain ED1576, there was no detectable interaction between cdc2 and cdc37.