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/ Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants. Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants. Plant J. (0960-7412) 2004 imex curation Rohila JS., Chen M., Cerny R., Fromm ME. The authors provided details of the TAP tag design as follows "the peptide sequence of the TAP tag was used to design a synthetic gene according to the principles used for the synthetic Bacillus thuringiensis insecticidal and synthetic Green Fluorescent Protein genes, by third codon position changes to remove cryptic splice sites, polyadenylation sites, and AT- or GC-rich regions. Additionally, the duplicated 180-bp regions of the tandem protein A domains were made non-identical (76% homology) to reduce recombination and the possibility of repeat-induced gene silencing. The nucleotide sequence of the synthetic TAP tag gene has 76% identity with the original TAP tag gene sequences while encoding the identical protein domains, with the exceptions of two amino acids added between the duplicated protein A domains and differences in the amino acids flanking the CBP region (Figure 1). These synthetic N-terminal or C-terminal TAP tag genes also include the castor bean catalase intron 1 and were cloned into a binary vector containing lambda recombination sites (GATEWAY�, Invitrogen, Carlsbad, CA, USA), either N-terminal to the attR1 recombination site or C-terminal to the attR2 site (Figure 1). " . References and further details are available within the paper. mfromm@unlnotes.edu 01-Sep-2009: Contacted by JYOTI. jyoti Only protein-protein interactions nicbe Nicotiana benthamiana tap tandem affinity purification TAP TAP tap fingerprinting peptide massfingerprinting fingerprinting Rohila JS., Chen M., Cerny R., Fromm ME. The authors provided details of the TAP tag design as follows "the peptide sequence of the TAP tag was used to design a synthetic gene according to the principles used for the synthetic Bacillus thuringiensis insecticidal and synthetic Green Fluorescent Protein genes, by third codon position changes to remove cryptic splice sites, polyadenylation sites, and AT- or GC-rich regions. Additionally, the duplicated 180-bp regions of the tandem protein A domains were made non-identical (76% homology) to reduce recombination and the possibility of repeat-induced gene silencing. The nucleotide sequence of the synthetic TAP tag gene has 76% identity with the original TAP tag gene sequences while encoding the identical protein domains, with the exceptions of two amino acids added between the duplicated protein A domains and differences in the amino acids flanking the CBP region (Figure 1). These synthetic N-terminal or C-terminal TAP tag genes also include the castor bean catalase intron 1 and were cloned into a binary vector containing lambda recombination sites (GATEWAY�, Invitrogen, Carlsbad, CA, USA), either N-terminal to the attR1 recombination site or C-terminal to the attR2 site (Figure 1). " . References and further details are available within the paper. mfromm@unlnotes.edu Accepted 2009-SEP-18 by JYOTI. 01-Sep-2009: Contacted by JYOTI. Plant J. (0960-7412) 2004 jyoti Only protein-protein interactions imex curation Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants. Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants. Plant J. (0960-7412) 2004 imex curation Rohila JS., Chen M., Cerny R., Fromm ME. The authors provided details of the TAP tag design as follows "the peptide sequence of the TAP tag was used to design a synthetic gene according to the principles used for the synthetic Bacillus thuringiensis insecticidal and synthetic Green Fluorescent Protein genes, by third codon position changes to remove cryptic splice sites, polyadenylation sites, and AT- or GC-rich regions. Additionally, the duplicated 180-bp regions of the tandem protein A domains were made non-identical (76% homology) to reduce recombination and the possibility of repeat-induced gene silencing. The nucleotide sequence of the synthetic TAP tag gene has 76% identity with the original TAP tag gene sequences while encoding the identical protein domains, with the exceptions of two amino acids added between the duplicated protein A domains and differences in the amino acids flanking the CBP region (Figure 1). These synthetic N-terminal or C-terminal TAP tag genes also include the castor bean catalase intron 1 and were cloned into a binary vector containing lambda recombination sites (GATEWAY�, Invitrogen, Carlsbad, CA, USA), either N-terminal to the attR1 recombination site or C-terminal to the attR2 site (Figure 1). " . References and further details are available within the paper. mfromm@unlnotes.edu 01-Sep-2009: Contacted by JYOTI. jyoti Only protein-protein interactions nicbe Nicotiana benthamiana tap tandem affinity purification TAP TAP tap fingerprinting peptide massfingerprinting fingerprinting Rohila JS., Chen M., Cerny R., Fromm ME. The authors provided details of the TAP tag design as follows "the peptide sequence of the TAP tag was used to design a synthetic gene according to the principles used for the synthetic Bacillus thuringiensis insecticidal and synthetic Green Fluorescent Protein genes, by third codon position changes to remove cryptic splice sites, polyadenylation sites, and AT- or GC-rich regions. Additionally, the duplicated 180-bp regions of the tandem protein A domains were made non-identical (76% homology) to reduce recombination and the possibility of repeat-induced gene silencing. The nucleotide sequence of the synthetic TAP tag gene has 76% identity with the original TAP tag gene sequences while encoding the identical protein domains, with the exceptions of two amino acids added between the duplicated protein A domains and differences in the amino acids flanking the CBP region (Figure 1). These synthetic N-terminal or C-terminal TAP tag genes also include the castor bean catalase intron 1 and were cloned into a binary vector containing lambda recombination sites (GATEWAY�, Invitrogen, Carlsbad, CA, USA), either N-terminal to the attR1 recombination site or C-terminal to the attR2 site (Figure 1). " . References and further details are available within the paper. mfromm@unlnotes.edu Accepted 2009-SEP-18 by JYOTI. 01-Sep-2009: Contacted by JYOTI. Plant J. (0960-7412) 2004 jyoti Only protein-protein interactions imex curation gvg_peptide protein protein rat Rattus norvegicus (Rat) Rat An amino acid sequence which is not represented in UniProt The organism source is indicated to be rat , however the protein consists of the DNA-binding domain of the yeast transcription factor GAL4, the transactivating domain of the herpes viral protein VP16, and the receptor domain of the rat glucocorticoid receptor (GR). q67bd0_tobac HSP70-3 protein protein tobac Nicotiana tabacum (Common tobacco) Common tobacco MAGKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVGFTDSERLIGDAAKNQVAMNPINTVFDAKRLIGRRFSDASVQSDIKLWPFKVISGPGDKPMIVVNYKGEEKQFAAEEISSMVLIKMKEIAEAFLGSTVKNAVVTVPAYFNDSQRQATKDAGVISGLNVMRIINEPTAAAIAYGLDKKATSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFVQEFKRKHKKDITGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLYEGVDFYSTITRARFEELNMDLFRKCMEPVEKCLRDAKMDKSTVHDVVLVGGSTRIPKVQQLLQDFFNGKELCKSINPDEAVAYGAAVQAAILSGEGNEKVQDLLLLDVTPLSLGLETAGGVMTVLIPRNTTIPTKKEQVFSTYSDNQPGVLIQVYEGERARTRDNNLLGKFELSGIPPAPRGVPQITVCFDIDANGILNVSAEDKTTGQKNKITITNDKGRLSKEEIEKMVQEAEKYKAEDEEHKKKVEAKNALENYAYNMRNTIKDEKIGSKLSSDDKKKIEDAIDQAISWLDSNQLAEADEFEDKMKELESICNPIIAKMYQGAGGEAGAPMDDDAPPAGGSSAGPKIEEVD BE77EC38B61777CA gvg-hsp70 1 3 unspecified role unspecified role bait bait n-terminal tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range 4 unspecified role unspecified role prey prey physical association physical association Figure 5a The authors identified HSP90 protein in the TAP tagged assay , but from the amino acid sequence information provided it is not possible to differentiate between HSP90-1 and HSP90-2 isoforms of the HSP90 protein. gvg-hsp70-1 2 4 unspecified role unspecified role prey prey 3 unspecified role unspecified role bait bait n-terminal tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association Figure 5a