Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpQ | clpY | CEB3_c03280 | CEB3_c03290 | ATP-dependent protease subunit ClpQ; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | ATP-dependent protease ATPase subunit ClpY; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.999 |
| clpQ | topA_1 | CEB3_c03280 | CEB3_c03250 | ATP-dependent protease subunit ClpQ; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | DNA topoisomerase 1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.678 |
| clpQ | trmFO | CEB3_c03280 | CEB3_c03260 | ATP-dependent protease subunit ClpQ; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | methylenetetrahydrofolate--tRNA-(uracil-5-)- methyltransferase TrmFO; Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs; Belongs to the MnmG family. TrmFO subfamily. | 0.721 |
| clpQ | xerC_1 | CEB3_c03280 | CEB3_c03270 | ATP-dependent protease subunit ClpQ; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.717 |
| clpY | clpQ | CEB3_c03290 | CEB3_c03280 | ATP-dependent protease ATPase subunit ClpY; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | ATP-dependent protease subunit ClpQ; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
| clpY | topA_1 | CEB3_c03290 | CEB3_c03250 | ATP-dependent protease ATPase subunit ClpY; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | DNA topoisomerase 1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.692 |
| clpY | trmFO | CEB3_c03290 | CEB3_c03260 | ATP-dependent protease ATPase subunit ClpY; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | methylenetetrahydrofolate--tRNA-(uracil-5-)- methyltransferase TrmFO; Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs; Belongs to the MnmG family. TrmFO subfamily. | 0.728 |
| clpY | xerC_1 | CEB3_c03290 | CEB3_c03270 | ATP-dependent protease ATPase subunit ClpY; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | Tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.619 |
| nifJ_1 | nifJ_2 | CEB3_c04240 | CEB3_c27260 | Pyruvate-flavodoxin oxidoreductase. | Pyruvate-flavodoxin oxidoreductase. | 0.999 |
| nifJ_1 | nifJ_3 | CEB3_c04240 | CEB3_c44130 | Pyruvate-flavodoxin oxidoreductase. | Pyruvate-flavodoxin oxidoreductase. | 0.999 |
| nifJ_1 | nifJ_4 | CEB3_c04240 | CEB3_c47060 | Pyruvate-flavodoxin oxidoreductase. | Pyruvate-flavodoxin oxidoreductase. | 0.999 |
| nifJ_1 | topA_1 | CEB3_c04240 | CEB3_c03250 | Pyruvate-flavodoxin oxidoreductase. | DNA topoisomerase 1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.975 |
| nifJ_1 | xerC_1 | CEB3_c04240 | CEB3_c03270 | Pyruvate-flavodoxin oxidoreductase. | Tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.622 |
| nifJ_2 | nifJ_1 | CEB3_c27260 | CEB3_c04240 | Pyruvate-flavodoxin oxidoreductase. | Pyruvate-flavodoxin oxidoreductase. | 0.999 |
| nifJ_2 | nifJ_3 | CEB3_c27260 | CEB3_c44130 | Pyruvate-flavodoxin oxidoreductase. | Pyruvate-flavodoxin oxidoreductase. | 0.999 |
| nifJ_2 | nifJ_4 | CEB3_c27260 | CEB3_c47060 | Pyruvate-flavodoxin oxidoreductase. | Pyruvate-flavodoxin oxidoreductase. | 0.999 |
| nifJ_2 | topA_1 | CEB3_c27260 | CEB3_c03250 | Pyruvate-flavodoxin oxidoreductase. | DNA topoisomerase 1; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] | 0.954 |
| nifJ_2 | xerC_1 | CEB3_c27260 | CEB3_c03270 | Pyruvate-flavodoxin oxidoreductase. | Tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.628 |
| nifJ_3 | nifJ_1 | CEB3_c44130 | CEB3_c04240 | Pyruvate-flavodoxin oxidoreductase. | Pyruvate-flavodoxin oxidoreductase. | 0.999 |
| nifJ_3 | nifJ_2 | CEB3_c44130 | CEB3_c27260 | Pyruvate-flavodoxin oxidoreductase. | Pyruvate-flavodoxin oxidoreductase. | 0.999 |
page 1 of 3