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/ Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803. Purification, assembly, and quaternary structure. Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803. Purification, assembly, and quaternary structure. Eur. J. Biochem. (0014-2956) 2001 imex curation Lamparter T., Esteban B., Hughes J. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species revisit when small molecule editor in place. Interactions of Cph1 with phytocyanobilin, phycoeritrin and biliverdin. Fig.6 and table 2 lamparte@zedat.fu-berlin.de Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Lamparter T., Esteban B., Hughes J. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species revisit when small molecule editor in place. Interactions of Cph1 with phytocyanobilin, phycoeritrin and biliverdin. Fig.6 and table 2 lamparte@zedat.fu-berlin.de Accepted 2006-JUN-19 by DAVET. Eur. J. Biochem. (0014-2956) 2001 Only protein-protein interactions imex curation Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803. Purification, assembly, and quaternary structure. Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803. Purification, assembly, and quaternary structure. Eur. J. Biochem. (0014-2956) 2001 imex curation Lamparter T., Esteban B., Hughes J. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species revisit when small molecule editor in place. Interactions of Cph1 with phytocyanobilin, phycoeritrin and biliverdin. Fig.6 and table 2 lamparte@zedat.fu-berlin.de Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Lamparter T., Esteban B., Hughes J. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species revisit when small molecule editor in place. Interactions of Cph1 with phytocyanobilin, phycoeritrin and biliverdin. Fig.6 and table 2 lamparte@zedat.fu-berlin.de Accepted 2006-JUN-19 by DAVET. Eur. J. Biochem. (0014-2956) 2001 Only protein-protein interactions imex curation rcp1_syny3 Response regulator Rcp1 rcp1 slr0474 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MSDESNPPKVILLVEDSKADSRLVQEVLKTSTIDHELIILRDGLAAMAFLQQQGEYENSPRPNLILLDLNLPKKDGREVLAEIKQNPDLKRIPVVVLTTSHNEDDVIASYELHVNCYLTKSRNLKDLFKMVQGIESFWLETVTLPAA C854E8036C9FD58E phy1_syny3 Phytochrome-like protein Cph1 Light-regulated histidine kinase 1 cph1 slr0473 Bacteriophytochrome Cph1 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MATTVQLSDQSLRQLETLAIHTAHLIQPHGLVVVLQEPDLTISQISANCTGILGRSPEDLLGRTLGEVFDSFQIDPIQSRLTAGQISSLNPSKLWARVMGDDFVIFDGVFHRNSDGLLVCELEPAYTSDNLPFLGFYHMANAALNRLRQQANLRDFYDVIVEEVRRMTGFDRVMLYRFDENNHGDVIAEDKRDDMEPYLGLHYPESDIPQPARRLFIHNPIRVIPDVYGVAVPLTPAVNPSTNRAVDLTESILRSAYHCHLTYLKNMGVGASLTISLIKDGHLWGLIACHHQTPKVIPFELRKACEFFGRVVFSNISAQEDTETFDYRVQLAEHEAVLLDKMTTAADFVEGLTNHPDRLLGLTGSQGAAICFGEKLILVGETPDEKAVQYLLQWLENREVQDVFFTSSLSQIYPDAVNFKSVASGLLAIPIARHNFLLWFRPEVLQTVNWGGDPNHAYEATQEDGKIELHPRQSFDLWKEIVRLQSLPWQSVEIQSALALKKAIVNLILRQAEELAQLARNLERSNADLKKFAYIASHDLQEPLNQVSNYVQLLEMRYSEALDEDAKDFIDFAVTGVSLMQTLIDDILTYAKVDTQYAQLTFTDVQEVVDKALANLKQRIEESGAEIEVGSMPAVMADQIQLMQVFQNLIANGIKFAGDKSPKIKIWGDRQEDAWVFAVQDNGIGIDPQFFERIFVIFQRLHTRDEYKGTGMGLAICKKIIEGHQGQIWLESNPGEGSTFYFSIPIGN DIP protein Q55168 original sequence version: 128 A9ECA6D8D5B3C88A cph1-cph1-7 1 4 unspecified role unspecified role neutral component neutral component c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) direct interaction direct interaction Cph1 adducted with phycocyanobilin forms dimers in both photo-states Pr and Pfr (red and far red light absorbing form respectively). Preparative electrophoresis and basic column buffer (ph9) prevent the dimers formation. The molecular mass of the monomer as calculated from the amino-acid sequence is 85 kDa, thus we assume that the major PCB holoprotein peak <200 kDa of our size-exclusion experiments corresponds to the dimer form, whereas the major peak of the apoprotein probably corresponds to a potentially nonglobular monomer. Q55168 purified cph1-cph1-8 2 4 putative self putative self putative self putative self c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation true The red light-absorbing form (Pr form) of cph1, exhibited a higher rate of ATP-dependant autophosphorylation compared to the far red light-absorbing form (Pfr form). Q55168 purified Our affinitypurified Cph1 holoprotein gave the same pattern as was described by Yeh et al. [10]; autophosphorylation was stronger after far-red irradiation than after red irradiation (Fig. 8). cph1-rcp1-5 2 3 enzyme target enzyme target substrate substrate unspecified role unspecified role c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) 4 enzyme enzyme unspecified role unspecified role c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation The red light-absorbing form (Pr form) of cph1, can phosphorylate rcp1 whereas the far-red light-absorbing form (Pfr form) cannot