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 |
| CAZ94376.1 | CAZ94379.1 | ZOBELLIA_303 | ZOBELLIA_306 | The transcriptional regulators with the Rrf2-type HTH domain control a variety of operons that encode iron-sulfur-containing proteins as well as other proteins involved in electron transport. Other rrf2-type HTH proteins are repressors of genes involved in nitrite or iron metabolism. The C-terminal part of the rrf2-type HTH domain contains 3 conserved cysteine residues that may bind an Fe-S cluster. Contains a DNA-binding, winged helix-turn-helix (wHTH) domain. Localized in the cytoplasm; Family membership. | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | 0.594 |
| CAZ94376.1 | cysI | ZOBELLIA_303 | ZOBELLIA_304 | The transcriptional regulators with the Rrf2-type HTH domain control a variety of operons that encode iron-sulfur-containing proteins as well as other proteins involved in electron transport. Other rrf2-type HTH proteins are repressors of genes involved in nitrite or iron metabolism. The C-terminal part of the rrf2-type HTH domain contains 3 conserved cysteine residues that may bind an Fe-S cluster. Contains a DNA-binding, winged helix-turn-helix (wHTH) domain. Localized in the cytoplasm; Family membership. | Sulfite reductase [NADPH] hemoprotein beta-component; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | 0.775 |
| CAZ94376.1 | cysJ | ZOBELLIA_303 | ZOBELLIA_305 | The transcriptional regulators with the Rrf2-type HTH domain control a variety of operons that encode iron-sulfur-containing proteins as well as other proteins involved in electron transport. Other rrf2-type HTH proteins are repressors of genes involved in nitrite or iron metabolism. The C-terminal part of the rrf2-type HTH domain contains 3 conserved cysteine residues that may bind an Fe-S cluster. Contains a DNA-binding, winged helix-turn-helix (wHTH) domain. Localized in the cytoplasm; Family membership. | Sulfite reductase [NADPH] flavoprotein alpha-component; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. | 0.633 |
| CAZ94379.1 | CAZ94376.1 | ZOBELLIA_306 | ZOBELLIA_303 | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | The transcriptional regulators with the Rrf2-type HTH domain control a variety of operons that encode iron-sulfur-containing proteins as well as other proteins involved in electron transport. Other rrf2-type HTH proteins are repressors of genes involved in nitrite or iron metabolism. The C-terminal part of the rrf2-type HTH domain contains 3 conserved cysteine residues that may bind an Fe-S cluster. Contains a DNA-binding, winged helix-turn-helix (wHTH) domain. Localized in the cytoplasm; Family membership. | 0.594 |
| CAZ94379.1 | CAZ95381.1 | ZOBELLIA_306 | ZOBELLIA_1325 | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.466 |
| CAZ94379.1 | CAZ95517.1 | ZOBELLIA_306 | ZOBELLIA_1461 | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | Cyclic nucleotide dependent thioredoxin reductase; This protein consists of an N-terminal cyclic nucleotide binding domain and a C-terminal thioreductase domain; This Enzyme is a pyridine nucleotide-disulphide reductases (PNDR) where the active site is a redox-active disulfide bond. Acts as an homodimer, binds one FAD molecule per subunit and is regulated by the cyclic nucleotide binding (cAMP or cGMP); Localized in the cytoplasm; High confidence in function and specificity. | 0.495 |
| CAZ94379.1 | ZOBELLIA_1062 | ZOBELLIA_306 | ZOBELLIA_1062 | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | Pseudogene; C-terminal fragment of conserved protein found in the PhnB family protein; Possibly localized in the cytoplasm; Conserved hypothetical protein. | 0.466 |
| CAZ94379.1 | cysI | ZOBELLIA_306 | ZOBELLIA_304 | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | Sulfite reductase [NADPH] hemoprotein beta-component; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | 0.623 |
| CAZ94379.1 | cysJ | ZOBELLIA_306 | ZOBELLIA_305 | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | Sulfite reductase [NADPH] flavoprotein alpha-component; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. | 0.772 |
| CAZ94379.1 | ftnA | ZOBELLIA_306 | ZOBELLIA_1316 | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | Ferritin; Iron-storage protein. | 0.490 |
| CAZ94379.1 | grpE | ZOBELLIA_306 | ZOBELLIA_2823 | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | Co-chaperone HSP-70 protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of [...] | 0.473 |
| CAZ94379.1 | katA1 | ZOBELLIA_306 | ZOBELLIA_1427 | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | Catalase; This enzyme is a mono-functional haem-containing catalase that acts as an antioxidant enzyme catalyzing the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects. Localized in the cytoplasm; High confidence in function and specificity. | 0.607 |
| CAZ94379.1 | katA2 | ZOBELLIA_306 | ZOBELLIA_3559 | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide. | 0.760 |
| CAZ95381.1 | CAZ94379.1 | ZOBELLIA_1325 | ZOBELLIA_306 | Conserved hypothetical protein; Localized in the cytoplasm. | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | 0.466 |
| CAZ95381.1 | CAZ95517.1 | ZOBELLIA_1325 | ZOBELLIA_1461 | Conserved hypothetical protein; Localized in the cytoplasm. | Cyclic nucleotide dependent thioredoxin reductase; This protein consists of an N-terminal cyclic nucleotide binding domain and a C-terminal thioreductase domain; This Enzyme is a pyridine nucleotide-disulphide reductases (PNDR) where the active site is a redox-active disulfide bond. Acts as an homodimer, binds one FAD molecule per subunit and is regulated by the cyclic nucleotide binding (cAMP or cGMP); Localized in the cytoplasm; High confidence in function and specificity. | 0.406 |
| CAZ95517.1 | CAZ94379.1 | ZOBELLIA_1461 | ZOBELLIA_306 | Cyclic nucleotide dependent thioredoxin reductase; This protein consists of an N-terminal cyclic nucleotide binding domain and a C-terminal thioreductase domain; This Enzyme is a pyridine nucleotide-disulphide reductases (PNDR) where the active site is a redox-active disulfide bond. Acts as an homodimer, binds one FAD molecule per subunit and is regulated by the cyclic nucleotide binding (cAMP or cGMP); Localized in the cytoplasm; High confidence in function and specificity. | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | 0.495 |
| CAZ95517.1 | CAZ95381.1 | ZOBELLIA_1461 | ZOBELLIA_1325 | Cyclic nucleotide dependent thioredoxin reductase; This protein consists of an N-terminal cyclic nucleotide binding domain and a C-terminal thioreductase domain; This Enzyme is a pyridine nucleotide-disulphide reductases (PNDR) where the active site is a redox-active disulfide bond. Acts as an homodimer, binds one FAD molecule per subunit and is regulated by the cyclic nucleotide binding (cAMP or cGMP); Localized in the cytoplasm; High confidence in function and specificity. | Conserved hypothetical protein; Localized in the cytoplasm. | 0.406 |
| CAZ95517.1 | ZOBELLIA_1062 | ZOBELLIA_1461 | ZOBELLIA_1062 | Cyclic nucleotide dependent thioredoxin reductase; This protein consists of an N-terminal cyclic nucleotide binding domain and a C-terminal thioreductase domain; This Enzyme is a pyridine nucleotide-disulphide reductases (PNDR) where the active site is a redox-active disulfide bond. Acts as an homodimer, binds one FAD molecule per subunit and is regulated by the cyclic nucleotide binding (cAMP or cGMP); Localized in the cytoplasm; High confidence in function and specificity. | Pseudogene; C-terminal fragment of conserved protein found in the PhnB family protein; Possibly localized in the cytoplasm; Conserved hypothetical protein. | 0.406 |
| CAZ95517.1 | katA2 | ZOBELLIA_1461 | ZOBELLIA_3559 | Cyclic nucleotide dependent thioredoxin reductase; This protein consists of an N-terminal cyclic nucleotide binding domain and a C-terminal thioreductase domain; This Enzyme is a pyridine nucleotide-disulphide reductases (PNDR) where the active site is a redox-active disulfide bond. Acts as an homodimer, binds one FAD molecule per subunit and is regulated by the cyclic nucleotide binding (cAMP or cGMP); Localized in the cytoplasm; High confidence in function and specificity. | Catalase; Serves to protect cells from the toxic effects of hydrogen peroxide. | 0.663 |
| ZOBELLIA_1062 | CAZ94379.1 | ZOBELLIA_1062 | ZOBELLIA_306 | Pseudogene; C-terminal fragment of conserved protein found in the PhnB family protein; Possibly localized in the cytoplasm; Conserved hypothetical protein. | Peroxiredoxins are thiol peroxidase. They are involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. The peroxidase reaction comprises two steps centered around a redox- active cysteine called the peroxidatic cysteine. It attacks the peroxide substrate and is oxidized to S-hydroxycysteine (a sulfenic acid). The second step is the regeneration of cysteine from S-hydroxycysteine. This regeneration is due to thiol-containing reductants such as thioredoxin. Localized in the cytoplasm; Specificity unclear. | 0.466 |
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