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/ The fly CAMTA transcription factor potentiates deactivation of rhodopsin, a G protein-coupled light receptor. The fly CAMTA transcription factor potentiates deactivation of rhodopsin, a G protein-coupled light receptor. Cell (0092-8674) 2006 imex curation Han J., Gong P., Reddig K., Mitra M., Guo P., Li HS. Calmodulin agarose was used to study binding of Proteins. The source of Calmodulin in the calmodulin agarose was determined by checking the vendors site. hong-sheng.li@umassmed.edu 08-DEC-2006: Contacted by JYOTI. orchard Only protein-protein interactions 1 in vitro In vitro emsa electrophoretic mobility shift assay Gel retardation assay band shift band shift Gel retardation assay emsa predetermined predetermined participant predetermined Han J., Gong P., Reddig K., Mitra M., Guo P., Li HS. Calmodulin agarose was used to study binding of Proteins. The source of Calmodulin in the calmodulin agarose was determined by checking the vendors site. hong-sheng.li@umassmed.edu Accepted 2006-NOV-28 by ORCHARD. 08-DEC-2006: Contacted by JYOTI. Cell (0092-8674) 2006 orchard Only protein-protein interactions 1 imex curation The fly CAMTA transcription factor potentiates deactivation of rhodopsin, a G protein-coupled light receptor. The fly CAMTA transcription factor potentiates deactivation of rhodopsin, a G protein-coupled light receptor. Cell (0092-8674) 2006 imex curation Han J., Gong P., Reddig K., Mitra M., Guo P., Li HS. Calmodulin agarose was used to study binding of Proteins. The source of Calmodulin in the calmodulin agarose was determined by checking the vendors site. hong-sheng.li@umassmed.edu 08-DEC-2006: Contacted by JYOTI. orchard Only protein-protein interactions 1 in vitro In vitro affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom predetermined predetermined participant predetermined Han J., Gong P., Reddig K., Mitra M., Guo P., Li HS. Calmodulin agarose was used to study binding of Proteins. The source of Calmodulin in the calmodulin agarose was determined by checking the vendors site. hong-sheng.li@umassmed.edu Accepted 2006-NOV-28 by ORCHARD. 08-DEC-2006: Contacted by JYOTI. Cell (0092-8674) 2006 orchard Only protein-protein interactions 1 imex curation cgcg box_dna dna deoxyribonucleic acid DNA deoxyribonucleic acid dna DNA deoxyribonucleic acid in vitro In vitro CCAACAGTCGCATGGGCAGCGTGCCCACGCGCACCATTGGCGCCAGTATGAG 68C395E129EC289F calm_bovin Calmodulin CALM CAM protein protein bovin Bos taurus (Bovine) Bovine MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK DIP protein P62157 original sequence version: 125 DIP protein P62157 original sequence version: 58 DIP protein P62157 original sequence version: null 6B4BC3FCDE10727B q95rq6_drome Camta CG8809 CG42332 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MDIRSKSGKPLARLHSNFESHDSYALGVDSPLDSLTGTNCLLSPLRKMDFALCEVSTGESSPVHDKDCDDNSTSATDVTIGNDLVLPDAVVGDSDAKVLTLAEHIIAAMPERIKNEADEMMVLGSPLTEPLTSESSALTDSFMDPLLDSLPNTHFDSDFSFDFHDHSYRYHDVSTPCSSLSPASSGPLQSPASYSILGTDPSVSSPSPPPSTKQLTEFLHASSISSYPFEADFSKLTLTDTEQRELYEAAKCIQKAYRSYKGRQKLEEQNKERSAATVIQNYYRRYKQYAYYRQMTNAALVIQHGYRSYRRNKRFKKSGLCLSSSSDHGSVSSNSQCLSSFYDHYKQDQQQLHELGSQPSTPKETSPSGPLKRTYSQSTQNQAARKIQQFMRQSRIKLQKERAEKEKLVHQRRAEYLQNLQFQGQQEMLVYHENNISAPSSGNTNASNNNNLHQIQSNQ 0E43AE02A6348512 calm-camta 2 4 unspecified role unspecified role bait bait ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role prey prey iq motif sufficient to bind sufficient binding region sufficient to bind undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-1169697]Certain and ragged-n-terminus positions must always be strictly superior to 0 and inferior or equal to the protein sequence length. Actual positions : 1741-1741, sequence length 459 [EBI-1169697]1741-1923 direct interaction direct interaction 7A, B A glutathione S-transferase (GST)-fusion protein containing a 472 aa C-terminal fragment of dCAMTA bound to calmodulin-agarose beads, The authors have carried out the assay in the presence of Calcium 2 Plus. The authors show that an Iso-Asn mutation in the IQ1 region abolishes this binding however the Iso in the IQ1 region could not be mapped. The authors have used CAMTA protein from Drosophila which is more than 1923 AA in length. The entry in UniProt is only 459AA in length. The range of protein is as specified by authors in the paper. camta-gc_box 1 5 unspecified role unspecified role neutral component neutral component cg-1 region sufficient to bind sufficient binding region sufficient to bind n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role neutral component neutral component region biotin tag biotin tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined c30g mutation mutation certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction 2B The authors have used CAMTA protein from Drosophila which is longer than 1923AA. The entry in UniProtKB is a fragment 459AA in size. Feature CG-1 binding region was determined to be at the N-terminal based on CAMTA_HUMAN CG-1 site. the CG-1 domain of dCAMTA bound specifically to a DNA fragment that contains a CGCG box