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/ Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC. Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC. Biochem. Biophys. Res. Commun. (0006-291X) 2004 Hayashi F., Ito H., Fujita M., Iwase R., Uzumaki T., Ishiura M. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species replace by bn-page when available 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 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 replace by bn-page when available 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 Annotation to indicate that this entry has been checked and accepted by a senior curator. Biochem. Biophys. Res. Commun. (0006-291X) 2004 Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC. Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC. Biochem. Biophys. Res. Commun. (0006-291X) 2004 Hayashi F., Ito H., Fujita M., Iwase R., Uzumaki T., Ishiura M. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species replace by bn-page when available 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 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 replace by bn-page when available 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 Annotation to indicate that this entry has been checked and accepted by a senior curator. Biochem. Biophys. Res. Commun. (0006-291X) 2004 Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC. Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC. Biochem. Biophys. Res. Commun. (0006-291X) 2004 Hayashi F., Ito H., Fujita M., Iwase R., Uzumaki T., Ishiura M. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species replace by bn-page when available 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 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 replace by bn-page when available 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 Annotation to indicate that this entry has been checked and accepted by a senior curator. Biochem. Biophys. Res. Commun. (0006-291X) 2004 Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC. Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC. Biochem. Biophys. Res. Commun. (0006-291X) 2004 Hayashi F., Ito H., Fujita M., Iwase R., Uzumaki T., Ishiura M. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species replace by bn-page when available 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 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 replace by bn-page when available 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 Annotation to indicate that this entry has been checked and accepted by a senior curator. 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 D3B0DCBE8A580B4E kaic_theeb Circadian clock protein kinase KaiC tlr0483 kaiC protein protein theeb Thermosynechococcus elongatus (strain BP-1) MTNLPEHQSSPTEQSSAEVKKIPTMIEGFDDISHGGLPQGRTTLVSGTSGTGKTLFAVQFLYNGITIFNEPGIFVTFEESPQDIIKNALSFGWNLQSLIDQGKLFILDASPDPDGQEVAGDFDLSALIERIQYAIRKYKATRVSIDSVTAVFQQYDAASVVRREIFRLAFRLKQLGVTTIMTTERVDEYGPVARFGVEEFVSDNVVILRNVLEGERRRRTVEILKLRGTTHMKGEYPFTINNGINIFPLGAMRLTQRSSNVRVSSGVKTLDEMCGGGFFKDSIILATGATGTGKTLLVSKFLETGCQQGERALLFAYEESRAQLSRNASSWGIDFEELERRGLLRIICAYPESAGLEDHLQIIKSEIADFKPSRVAIDSLSALARGVSNNAFRQFVIGVTGFAKQEEITGFFTNTTDQFMGSNSITESHISTITDTILLLQYVEIRGEMSRAINVFKMRGSWHDKGIREYVITEKGAEIRDSFRNFEGIISGTPTRISVDEKTELARIAKGMQDLESE 34E4CDF9DE9C1824 34E4CDF9DE9C1824 kaia-kaia-1 4 5 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction kaiA proteins form a homodimer kaic-kaic-1 4 6 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 6 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction kaiC protein form a homohexamer kaia-kaic-5 4 5 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component 6 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction 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 kaic-kaic-2 2 6 enzyme target enzyme target substrate substrate unspecified role unspecified role ecoli Escherichia coli (strain K12) 6 enzyme enzyme unspecified role unspecified role ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation 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 1 5 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 6 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction 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. kaia-kaic-7 3 5 unspecified role unspecified role prey prey 6 unspecified role unspecified role bait bait ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) direct interaction direct interaction 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 3 6 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction 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.