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/ http://www.ebi.ac.uk/ hayashi-2004-1 Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC. in vitro In vitro comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel predetermined predetermined participant predetermined Hayashi F., Ito H., Fujita M., Iwase R., Uzumaki T., Ishiura M. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Native-PAGE analysis of complex formation using purified proteins. Complex were detected by coomassie blue staining and the content was checked by western-blotting. The amount of proteins were determined by densitometry. fig 4,6 ishiura@gene.nagoya-u.ac.jp Biochem. Biophys. Res. Commun. (0006-291X) 2004 hayashi-2004-4 Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC. in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Hayashi F., Ito H., Fujita M., Iwase R., Uzumaki T., Ishiura M. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Native-PAGE analysis of complex formation using purified proteins. Complex were detected by coomassie blue staining and the content was checked by western-blotting. The amount of proteins were determined by densitometry. fig 4,6 ishiura@gene.nagoya-u.ac.jp Biochem. Biophys. Res. Commun. (0006-291X) 2004 hayashi-2004-2 Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC. in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Hayashi F., Ito H., Fujita M., Iwase R., Uzumaki T., Ishiura M. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Native-PAGE analysis of complex formation using purified proteins. Complex were detected by coomassie blue staining and the content was checked by western-blotting. The amount of proteins were determined by densitometry. fig 4,6 ishiura@gene.nagoya-u.ac.jp Biochem. Biophys. Res. Commun. (0006-291X) 2004 hayashi-2004-3 Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC. in vitro In vitro comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel predetermined predetermined participant predetermined Hayashi F., Ito H., Fujita M., Iwase R., Uzumaki T., Ishiura M. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species Native-PAGE analysis of complex formation using purified proteins. Complex were detected by coomassie blue staining and the content was checked by western-blotting. The amount of proteins were determined by densitometry. fig 4,6 ishiura@gene.nagoya-u.ac.jp Biochem. Biophys. Res. Commun. (0006-291X) 2004 kaia_theeb Circadian clock protein KaiA kaiA tlr0481 protein protein theeb Thermosynechococcus elongatus (strain BP-1) MAQSTALTICGLVYSPAIGQELVRLHTSDIDELVYFSSEREFCNYLEARRNSIACLILEWGEGTPQIITYLHHSATLLPAILIFPAAPAPPPAGPHYHIAEVILTTDQLDQLNRQIEEAITGFVKLCPGCAVPPHVLFRLPALKESSNVDPQHRLSQKLKERLGYLGVYYKRDTAFFFRRMSPADKRKLLDELRSIYRTIVLEYFNTDAKVNERIDEFVSKAFFADISVSQVLEIHVELMDTFSKQLKLEGRSEDILLDYRLTLIDVIAHLCEMYRRSIPREV D3B0DCBE8A580B4E kaic_theeb Circadian clock protein kinase KaiC tlr0483 kaiC protein protein theeb Thermosynechococcus elongatus (strain BP-1) MTNLPEHQSSPTEQSSAEVKKIPTMIEGFDDISHGGLPQGRTTLVSGTSGTGKTLFAVQFLYNGITIFNEPGIFVTFEESPQDIIKNALSFGWNLQSLIDQGKLFILDASPDPDGQEVAGDFDLSALIERIQYAIRKYKATRVSIDSVTAVFQQYDAASVVRREIFRLAFRLKQLGVTTIMTTERVDEYGPVARFGVEEFVSDNVVILRNVLEGERRRRTVEILKLRGTTHMKGEYPFTINNGINIFPLGAMRLTQRSSNVRVSSGVKTLDEMCGGGFFKDSIILATGATGTGKTLLVSKFLETGCQQGERALLFAYEESRAQLSRNASSWGIDFEELERRGLLRIICAYPESAGLEDHLQIIKSEIADFKPSRVAIDSLSALARGVSNNAFRQFVIGVTGFAKQEEITGFFTNTTDQFMGSNSITESHISTITDTILLLQYVEIRGEMSRAINVFKMRGSWHDKGIREYVITEKGAEIRDSFRNFEGIISGTPTRISVDEKTELARIAKGMQDLESE 34E4CDF9DE9C1824 kaia-kaia-1 kaiA dimer complex migration in native gel 231792 N/A 231796 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) N/A 231796 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false kaiA proteins form a homodimer kaic-kaic-1 kaiC hexamer complex migration in native gel 231792 N/A 231797 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 1.0 N/A 231797 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 5.0 direct interaction direct interaction false false false kaiC protein form a homohexamer kaia-kaic-5 kaiA-KaiC complex migration in native gel, Scatchard plot analysis 231792 N/A 231796 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 N/A 231796 unspecified role unspecified role neutral component neutral component Stoichiometry: 2.0 N/A 231797 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 6.0 direct interaction direct interaction false false false Scatchard plot anlaysis: 2 molecules of KaiA dimer bind 1 molecule of KaiC hexamer Addition of AMPPNP, a non-hydrolyzable ATP, is necessary to visualize the complex. Dissociation constant: 1.52 10-4 M kaia-kaic-7 SPR : kaiA-KaiC interactions analysis in presence of AMPPNP 231793 N/A 231796 unspecified role unspecified role prey prey Stoichiometry: 2.0 N/A 231797 unspecified role unspecified role bait bait ecoli Escherichia coli (strain K12) Stoichiometry: 6.0 N/A 231796 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 2 molecules of KaiA dimer bind 1 molecule of KaiC hexamer in presence of AMPPNP, a non-hydrolyzable ATP. In presence of AMPPNP, the apparent dissociation rate is constant (kdiss) is 1.8 10-2 s-1. In presence of AMPPNP, the apparent association rate constant (kass) of Kai dimer to immobilized KaiC hexamer is 2.0 10+4 M-1 s-1. kaia-kaic-8 SPR : kaiA-KaiC interactions analysis in presence of ATP 231793 N/A 231797 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 6.0 N/A 231796 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 1 molecule of KaiA dimer binds 1 molecule of KaiC hexamer in presence of ATP. In presence of ATP, the apparent dissociation rate is constant (kdiss) is 4.1 10-2 s-1. In presence of ATP, the apparent association rate constant (kass) of Kai dimer to immobilized KaiC hexamer is 3.0 10+4 M-1 s-1. kaic-kaic-2 kaiC autophosphorylation is enhanced by KaiA 231794 N/A 231797 enzyme target enzyme target substrate substrate unspecified role unspecified role ecoli Escherichia coli (strain K12) N/A 231797 enzyme enzyme unspecified role unspecified role ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation false false false Addition of KaiA enhance KaiC autophosphorylation. The molar ratio of KaiA dimer to KaiC hexamer that gives half saturation of the enhancement is 0.25. It suggests that 1 molecule of KaiA dimer interacts with 1 molecule of KaiC hexamer at almost saturation level of phosphorylation enhancement. kaia-kaic-6 kaiA-KaiC complex migration in 2DNS-PAGE 231795 N/A 231796 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 N/A 231796 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 N/A 231797 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 6.0 direct interaction direct interaction false false false Quantification anlaysis: 2 molecules of KaiA dimer bind 1 molecule of KaiC hexamer Addition of AMPPNP, a non-hydrolyzable ATP, is necessary to visualize the complex.