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 |
| ero1a | ero1b | ENSDARP00000015478 | ENSDARP00000139494 | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the folding of immunoglobulins (By similarity). Belongs to the EROs family. | Endoplasmic reticulum oxidoreductase beta. | 0.906 |
| ero1a | erp44 | ENSDARP00000015478 | ENSDARP00000017258 | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the folding of immunoglobulins (By similarity). Belongs to the EROs family. | Thioredoxin domain containing 4 (Endoplasmic reticulum). | 0.790 |
| ero1a | gpx7 | ENSDARP00000015478 | ENSDARP00000123903 | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the folding of immunoglobulins (By similarity). Belongs to the EROs family. | Glutathione peroxidase; Belongs to the glutathione peroxidase family. | 0.749 |
| ero1a | gpx8 | ENSDARP00000015478 | ENSDARP00000011955 | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the folding of immunoglobulins (By similarity). Belongs to the EROs family. | Probable glutathione peroxidase 8; Belongs to the glutathione peroxidase family. | 0.749 |
| ero1a | p4hb | ENSDARP00000015478 | ENSDARP00000138657 | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the folding of immunoglobulins (By similarity). Belongs to the EROs family. | Protein disulfide-isomerase. | 0.970 |
| ero1a | pdia4 | ENSDARP00000015478 | ENSDARP00000018458 | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the folding of immunoglobulins (By similarity). Belongs to the EROs family. | Protein disulfide-isomerase A4; Belongs to the protein disulfide isomerase family. | 0.959 |
| ero1a | pdia6 | ENSDARP00000015478 | ENSDARP00000027662 | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the folding of immunoglobulins (By similarity). Belongs to the EROs family. | Protein disulfide isomerase family A, member 6; Belongs to the protein disulfide isomerase family. | 0.948 |
| ero1a | sec63 | ENSDARP00000015478 | ENSDARP00000006629 | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the folding of immunoglobulins (By similarity). Belongs to the EROs family. | SEC63 homolog, protein translocation regulator. | 0.754 |
| ero1a | txndc16 | ENSDARP00000015478 | ENSDARP00000095835 | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the folding of immunoglobulins (By similarity). Belongs to the EROs family. | Thioredoxin domain-containing 16. | 0.885 |
| ero1a | txndc5 | ENSDARP00000015478 | ENSDARP00000116609 | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the folding of immunoglobulins (By similarity). Belongs to the EROs family. | Thioredoxin domain-containing 5; Belongs to the protein disulfide isomerase family. | 0.947 |
| ero1b | ero1a | ENSDARP00000139494 | ENSDARP00000015478 | Endoplasmic reticulum oxidoreductase beta. | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the folding of immunoglobulins (By similarity). Belongs to the EROs family. | 0.906 |
| ero1b | erp44 | ENSDARP00000139494 | ENSDARP00000017258 | Endoplasmic reticulum oxidoreductase beta. | Thioredoxin domain containing 4 (Endoplasmic reticulum). | 0.448 |
| ero1b | p4hb | ENSDARP00000139494 | ENSDARP00000138657 | Endoplasmic reticulum oxidoreductase beta. | Protein disulfide-isomerase. | 0.958 |
| ero1b | pdia4 | ENSDARP00000139494 | ENSDARP00000018458 | Endoplasmic reticulum oxidoreductase beta. | Protein disulfide-isomerase A4; Belongs to the protein disulfide isomerase family. | 0.959 |
| ero1b | pdia6 | ENSDARP00000139494 | ENSDARP00000027662 | Endoplasmic reticulum oxidoreductase beta. | Protein disulfide isomerase family A, member 6; Belongs to the protein disulfide isomerase family. | 0.949 |
| ero1b | sec63 | ENSDARP00000139494 | ENSDARP00000006629 | Endoplasmic reticulum oxidoreductase beta. | SEC63 homolog, protein translocation regulator. | 0.733 |
| ero1b | txndc16 | ENSDARP00000139494 | ENSDARP00000095835 | Endoplasmic reticulum oxidoreductase beta. | Thioredoxin domain-containing 16. | 0.428 |
| ero1b | txndc5 | ENSDARP00000139494 | ENSDARP00000116609 | Endoplasmic reticulum oxidoreductase beta. | Thioredoxin domain-containing 5; Belongs to the protein disulfide isomerase family. | 0.947 |
| erp44 | ero1a | ENSDARP00000017258 | ENSDARP00000015478 | Thioredoxin domain containing 4 (Endoplasmic reticulum). | ERO1-like protein alpha; Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the folding of immunoglobulins (By similarity). Belongs to the EROs family. | 0.790 |
| erp44 | ero1b | ENSDARP00000017258 | ENSDARP00000139494 | Thioredoxin domain containing 4 (Endoplasmic reticulum). | Endoplasmic reticulum oxidoreductase beta. | 0.448 |
page 1 of 3