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 |
| PSM36_0198 | PSM36_0201 | PSM36_0198 | PSM36_0201 | Putative Alpha-L-arabinofuranosidase; Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides; High confidence in function and specificity; Belongs to the glycosyl hydrolase 43 family. | SpoU; tRNA G18 (ribose-2'-O)-methylase SpoU [Translation, ribosomal structure and biogenesis]; High confidence in function and specificity. | 0.416 |
| PSM36_0198 | trxA_3 | PSM36_0198 | PSM36_0200 | Putative Alpha-L-arabinofuranosidase; Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides; High confidence in function and specificity; Belongs to the glycosyl hydrolase 43 family. | Thioredoxin serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. In the NADPH-dependent protein disulphide reduction, thioredoxin reductase (TR) catalyses the reduction of oxidised thioredoxin (trx) by NADPH using FAD and its redox-active disulphide; reduced thioredoxin then directly reduces the disulphide i [...] | 0.503 |
| PSM36_0201 | PSM36_0198 | PSM36_0201 | PSM36_0198 | SpoU; tRNA G18 (ribose-2'-O)-methylase SpoU [Translation, ribosomal structure and biogenesis]; High confidence in function and specificity. | Putative Alpha-L-arabinofuranosidase; Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides; High confidence in function and specificity; Belongs to the glycosyl hydrolase 43 family. | 0.416 |
| PSM36_0201 | trxA_3 | PSM36_0201 | PSM36_0200 | SpoU; tRNA G18 (ribose-2'-O)-methylase SpoU [Translation, ribosomal structure and biogenesis]; High confidence in function and specificity. | Thioredoxin serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. In the NADPH-dependent protein disulphide reduction, thioredoxin reductase (TR) catalyses the reduction of oxidised thioredoxin (trx) by NADPH using FAD and its redox-active disulphide; reduced thioredoxin then directly reduces the disulphide i [...] | 0.633 |
| PSM36_1521 | PSM36_2445 | PSM36_1521 | PSM36_2445 | Glyceraldehyde-3-phosphate dehydrogenase, cytosolic; D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH; High confidence in function and specificity; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide; High confidenc [...] | 0.453 |
| PSM36_1521 | groL | PSM36_1521 | PSM36_1133 | Glyceraldehyde-3-phosphate dehydrogenase, cytosolic; D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH; High confidence in function and specificity; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | GroEL_like type I chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.523 |
| PSM36_1521 | trxA_3 | PSM36_1521 | PSM36_0200 | Glyceraldehyde-3-phosphate dehydrogenase, cytosolic; D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH; High confidence in function and specificity; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | Thioredoxin serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. In the NADPH-dependent protein disulphide reduction, thioredoxin reductase (TR) catalyses the reduction of oxidised thioredoxin (trx) by NADPH using FAD and its redox-active disulphide; reduced thioredoxin then directly reduces the disulphide i [...] | 0.520 |
| PSM36_1980 | ahpC | PSM36_1980 | PSM36_1764 | Thioredoxin reductase; High confidence in function and specificity. | Alkyl hydroperoxide reductase subunit C; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | 0.663 |
| PSM36_1980 | trxA_3 | PSM36_1980 | PSM36_0200 | Thioredoxin reductase; High confidence in function and specificity. | Thioredoxin serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. In the NADPH-dependent protein disulphide reduction, thioredoxin reductase (TR) catalyses the reduction of oxidised thioredoxin (trx) by NADPH using FAD and its redox-active disulphide; reduced thioredoxin then directly reduces the disulphide i [...] | 0.507 |
| PSM36_2445 | PSM36_1521 | PSM36_2445 | PSM36_1521 | This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide; High confidenc [...] | Glyceraldehyde-3-phosphate dehydrogenase, cytosolic; D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH; High confidence in function and specificity; Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. | 0.453 |
| PSM36_2445 | ahpC | PSM36_2445 | PSM36_1764 | This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide; High confidenc [...] | Alkyl hydroperoxide reductase subunit C; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | 0.458 |
| PSM36_2445 | gltB | PSM36_2445 | PSM36_2872 | This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide; High confidenc [...] | 2 L-glutamate + NADP(+) <=> L-glutamine + 2-oxoglutarate + NADPH; High confidence in function and specificity. | 0.929 |
| PSM36_2445 | groL | PSM36_2445 | PSM36_1133 | This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide; High confidenc [...] | GroEL_like type I chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.549 |
| PSM36_2445 | trxA_3 | PSM36_2445 | PSM36_0200 | This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide; High confidenc [...] | Thioredoxin serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. In the NADPH-dependent protein disulphide reduction, thioredoxin reductase (TR) catalyses the reduction of oxidised thioredoxin (trx) by NADPH using FAD and its redox-active disulphide; reduced thioredoxin then directly reduces the disulphide i [...] | 0.604 |
| ahpC | PSM36_1980 | PSM36_1764 | PSM36_1980 | Alkyl hydroperoxide reductase subunit C; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | Thioredoxin reductase; High confidence in function and specificity. | 0.663 |
| ahpC | PSM36_2445 | PSM36_1764 | PSM36_2445 | Alkyl hydroperoxide reductase subunit C; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide; High confidenc [...] | 0.458 |
| ahpC | gltB | PSM36_1764 | PSM36_2872 | Alkyl hydroperoxide reductase subunit C; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | 2 L-glutamate + NADP(+) <=> L-glutamine + 2-oxoglutarate + NADPH; High confidence in function and specificity. | 0.595 |
| ahpC | groL | PSM36_1764 | PSM36_1133 | Alkyl hydroperoxide reductase subunit C; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | GroEL_like type I chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.503 |
| ahpC | trxA_3 | PSM36_1764 | PSM36_0200 | Alkyl hydroperoxide reductase subunit C; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | Thioredoxin serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. In the NADPH-dependent protein disulphide reduction, thioredoxin reductase (TR) catalyses the reduction of oxidised thioredoxin (trx) by NADPH using FAD and its redox-active disulphide; reduced thioredoxin then directly reduces the disulphide i [...] | 0.526 |
| ahpC | trxB1 | PSM36_1764 | PSM36_0519 | Alkyl hydroperoxide reductase subunit C; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. | This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]; High confidence in function and specificity. | 0.663 |
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