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/ lamparter-2001-2 Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803. Purification, assembly, and quaternary structure. 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 Fig.6 and table 2 lamparte@zedat.fu-berlin.de Eur. J. Biochem. (0014-2956) 2001 Only protein-protein interactions imex curation lamparter-2001-1 Phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803. Purification, assembly, and quaternary structure. 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 Fig.6 and table 2 lamparte@zedat.fu-berlin.de Eur. J. Biochem. (0014-2956) 2001 Only protein-protein interactions imex curation 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 rcp1_syny3 Response regulator Rcp1 rcp1 slr0474 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MSDESNPPKVILLVEDSKADSRLVQEVLKTSTIDHELIILRDGLAAMAFLQQQGEYENSPRPNLILLDLNLPKKDGREVLAEIKQNPDLKRIPVVVLTTSHNEDDVIASYELHVNCYLTKSRNLKDLFKMVQGIESFWLETVTLPAA cph1-cph1-8 Autophosphorylation of cph1 (Synechocystis PCC6803) 366795 n/a 366797 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 false ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation false true false 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 cph1-rcp1-5 Phosphorylation of rcp1 by cph1 (Synechocystis PCC6803) 366795 N/A 366798 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 false ecoli Escherichia coli (strain K12) N/A 366797 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 false ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation false false false The red light-absorbing form (Pr form) of cph1, can phosphorylate rcp1 whereas the far-red light-absorbing form (Pfr form) cannot cph1-cph1-7 synechocystis cph1 photochrome homodimers shown by size-exclusion chromatography 366796 N/A 366797 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 false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 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. Q55168 purified