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 proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| 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 |
| CAZ95381.1 | CAZ96982.1 | ZOBELLIA_1325 | ZOBELLIA_2835 | 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 |
| 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 | CAZ96982.1 | ZOBELLIA_1461 | ZOBELLIA_2835 | 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 | CAZ97118.1 | ZOBELLIA_1461 | ZOBELLIA_2971 | 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. | Thiol-disulfide oxidoreductase catalyzes the formation of disulfide bond in various substrates. Its exact specificity is not known; Belongs to the thioredoxin family; Localized in the cytoplasm; Specificity unclear. | 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 |
| CAZ96982.1 | CAZ95381.1 | ZOBELLIA_2835 | 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 |
| CAZ96982.1 | CAZ95517.1 | ZOBELLIA_2835 | 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 |
| CAZ96982.1 | CAZ97118.1 | ZOBELLIA_2835 | ZOBELLIA_2971 | 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. | Thiol-disulfide oxidoreductase catalyzes the formation of disulfide bond in various substrates. Its exact specificity is not known; Belongs to the thioredoxin family; Localized in the cytoplasm; Specificity unclear. | 0.466 |
| CAZ96982.1 | ZOBELLIA_1062 | ZOBELLIA_2835 | 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 |
| CAZ96982.1 | ftnA | ZOBELLIA_2835 | 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 |
| CAZ96982.1 | grpE | ZOBELLIA_2835 | 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 |
| CAZ96982.1 | hfiX | ZOBELLIA_2835 | ZOBELLIA_1848 | 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. | GTP-binding protein HflX; GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. HflX GTPase family. | 0.523 |
| CAZ96982.1 | katA1 | ZOBELLIA_2835 | 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 |
| CAZ96982.1 | katA2 | ZOBELLIA_2835 | 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 |
| CAZ96982.1 | yfiT | ZOBELLIA_2835 | ZOBELLIA_2836 | 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. | Putative metal-dependent hydrolase YfiT; YfiT exists as a dimer and binds Ni(2+) in a 1:1 stoichiometry. The protein has an unusual four-helix bundle topology and coordinates Ni(2+) in an octahedral geometry with three conserved histidines and three waters. Although there is no similarity in their overall structures, the coordination geometry of the metal and the residues that constitute the putative active site in YfiT are; Function unclear. | 0.595 |
| CAZ97118.1 | CAZ95517.1 | ZOBELLIA_2971 | ZOBELLIA_1461 | Thiol-disulfide oxidoreductase catalyzes the formation of disulfide bond in various substrates. Its exact specificity is not known; Belongs to the thioredoxin family; 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. | 0.406 |
| CAZ97118.1 | CAZ96982.1 | ZOBELLIA_2971 | ZOBELLIA_2835 | Thiol-disulfide oxidoreductase catalyzes the formation of disulfide bond in various substrates. Its exact specificity is not known; Belongs to the thioredoxin family; Localized in the cytoplasm; Specificity unclear. | 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 |
| ZOBELLIA_1062 | CAZ95517.1 | ZOBELLIA_1062 | ZOBELLIA_1461 | Pseudogene; C-terminal fragment of conserved protein found in the PhnB family protein; Possibly localized in the cytoplasm; Conserved hypothetical protein. | 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 |
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