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 |
| CAZ98374.1 | CAZ98375.1 | ZOBELLIA_4239 | ZOBELLIA_4240 | Putative 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. | 0.533 |
| CAZ98375.1 | CAZ98374.1 | ZOBELLIA_4240 | ZOBELLIA_4239 | 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 protein. | 0.533 |
| CAZ98375.1 | pgkA | ZOBELLIA_4240 | ZOBELLIA_1724 | 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. | Phosphoglycerate kinase transfers a phosphate group from 1,3-biphosphoglycerate to ADP, forming ATP and 3-Phosphoglycerate in the seventh step of the glycolysis Embden-Meyerhof pathway). PgkA exists as a monomer containing two nearly equal-sized domains that correspond to the N- and C-termini of the protein. 3-phosphoglycerate binds to the N-terminal, while the nucleotide substrates, MgATP or MgADP, bind to the C-terminal domain of the enzyme; Localized in the cytoplasm; High confidence in function and specificity. | 0.443 |
| pgkA | CAZ98375.1 | ZOBELLIA_1724 | ZOBELLIA_4240 | Phosphoglycerate kinase transfers a phosphate group from 1,3-biphosphoglycerate to ADP, forming ATP and 3-Phosphoglycerate in the seventh step of the glycolysis Embden-Meyerhof pathway). PgkA exists as a monomer containing two nearly equal-sized domains that correspond to the N- and C-termini of the protein. 3-phosphoglycerate binds to the N-terminal, while the nucleotide substrates, MgATP or MgADP, bind to the C-terminal domain of the enzyme; 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. | 0.443 |