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 |
| CAZ94591.1 | CAZ94593.1 | ZOBELLIA_520 | ZOBELLIA_522 | Putative protein. | Conserved protein belonging to the DUF1572 family; Localized in the cytoplasm. | 0.451 |
| CAZ94591.1 | msrB1 | ZOBELLIA_520 | ZOBELLIA_521 | Putative protein. | Peptide methionine sulphoxide reductase reverses the inactivation of many proteins due to the oxidation of critical methionine residues by reducing methionine sulphoxide to methionine. MsrB is specific for methionine-R-sulfoxides. It activates the cysteine or selenocysteine nucleophile through a unique Cys-Arg-Asp/Glu catalytic triad. Regeneration of the active site occurs through a series of thiol-disulfide exchange steps involving another active site Cys residue and thioredoxin. Localized in the cytoplasm; High confidence in function and specificity. | 0.568 |
| CAZ94593.1 | CAZ94591.1 | ZOBELLIA_522 | ZOBELLIA_520 | Conserved protein belonging to the DUF1572 family; Localized in the cytoplasm. | Putative protein. | 0.451 |
| CAZ94593.1 | bfmBC | ZOBELLIA_522 | ZOBELLIA_523 | Conserved protein belonging to the DUF1572 family; Localized in the cytoplasm. | The Dihydrolipoyl dehydrogenase is the E3 component of the branched-chain alpha-keto dehydrogenase complex. This complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It is involved in valine, leucine and isoleucine biodegradation. It contains multiple copies of three enzymatic components: branched- chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). The E3 component converts the Protein 6-N-(dihydrolipoyl)lysine to protein 6-N-(lipoyl)lysine. Dihydrolipoyl dehydrogenase is a homodimer, which binds 1 NAD [...] | 0.472 |
| CAZ94593.1 | msrB1 | ZOBELLIA_522 | ZOBELLIA_521 | Conserved protein belonging to the DUF1572 family; Localized in the cytoplasm. | Peptide methionine sulphoxide reductase reverses the inactivation of many proteins due to the oxidation of critical methionine residues by reducing methionine sulphoxide to methionine. MsrB is specific for methionine-R-sulfoxides. It activates the cysteine or selenocysteine nucleophile through a unique Cys-Arg-Asp/Glu catalytic triad. Regeneration of the active site occurs through a series of thiol-disulfide exchange steps involving another active site Cys residue and thioredoxin. Localized in the cytoplasm; High confidence in function and specificity. | 0.607 |
| bfmBC | CAZ94593.1 | ZOBELLIA_523 | ZOBELLIA_522 | The Dihydrolipoyl dehydrogenase is the E3 component of the branched-chain alpha-keto dehydrogenase complex. This complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It is involved in valine, leucine and isoleucine biodegradation. It contains multiple copies of three enzymatic components: branched- chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). The E3 component converts the Protein 6-N-(dihydrolipoyl)lysine to protein 6-N-(lipoyl)lysine. Dihydrolipoyl dehydrogenase is a homodimer, which binds 1 NAD [...] | Conserved protein belonging to the DUF1572 family; Localized in the cytoplasm. | 0.472 |
| bfmBC | msrB1 | ZOBELLIA_523 | ZOBELLIA_521 | The Dihydrolipoyl dehydrogenase is the E3 component of the branched-chain alpha-keto dehydrogenase complex. This complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It is involved in valine, leucine and isoleucine biodegradation. It contains multiple copies of three enzymatic components: branched- chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). The E3 component converts the Protein 6-N-(dihydrolipoyl)lysine to protein 6-N-(lipoyl)lysine. Dihydrolipoyl dehydrogenase is a homodimer, which binds 1 NAD [...] | Peptide methionine sulphoxide reductase reverses the inactivation of many proteins due to the oxidation of critical methionine residues by reducing methionine sulphoxide to methionine. MsrB is specific for methionine-R-sulfoxides. It activates the cysteine or selenocysteine nucleophile through a unique Cys-Arg-Asp/Glu catalytic triad. Regeneration of the active site occurs through a series of thiol-disulfide exchange steps involving another active site Cys residue and thioredoxin. Localized in the cytoplasm; High confidence in function and specificity. | 0.489 |
| msrB1 | CAZ94591.1 | ZOBELLIA_521 | ZOBELLIA_520 | Peptide methionine sulphoxide reductase reverses the inactivation of many proteins due to the oxidation of critical methionine residues by reducing methionine sulphoxide to methionine. MsrB is specific for methionine-R-sulfoxides. It activates the cysteine or selenocysteine nucleophile through a unique Cys-Arg-Asp/Glu catalytic triad. Regeneration of the active site occurs through a series of thiol-disulfide exchange steps involving another active site Cys residue and thioredoxin. Localized in the cytoplasm; High confidence in function and specificity. | Putative protein. | 0.568 |
| msrB1 | CAZ94593.1 | ZOBELLIA_521 | ZOBELLIA_522 | Peptide methionine sulphoxide reductase reverses the inactivation of many proteins due to the oxidation of critical methionine residues by reducing methionine sulphoxide to methionine. MsrB is specific for methionine-R-sulfoxides. It activates the cysteine or selenocysteine nucleophile through a unique Cys-Arg-Asp/Glu catalytic triad. Regeneration of the active site occurs through a series of thiol-disulfide exchange steps involving another active site Cys residue and thioredoxin. Localized in the cytoplasm; High confidence in function and specificity. | Conserved protein belonging to the DUF1572 family; Localized in the cytoplasm. | 0.607 |
| msrB1 | bfmBC | ZOBELLIA_521 | ZOBELLIA_523 | Peptide methionine sulphoxide reductase reverses the inactivation of many proteins due to the oxidation of critical methionine residues by reducing methionine sulphoxide to methionine. MsrB is specific for methionine-R-sulfoxides. It activates the cysteine or selenocysteine nucleophile through a unique Cys-Arg-Asp/Glu catalytic triad. Regeneration of the active site occurs through a series of thiol-disulfide exchange steps involving another active site Cys residue and thioredoxin. Localized in the cytoplasm; High confidence in function and specificity. | The Dihydrolipoyl dehydrogenase is the E3 component of the branched-chain alpha-keto dehydrogenase complex. This complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It is involved in valine, leucine and isoleucine biodegradation. It contains multiple copies of three enzymatic components: branched- chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). The E3 component converts the Protein 6-N-(dihydrolipoyl)lysine to protein 6-N-(lipoyl)lysine. Dihydrolipoyl dehydrogenase is a homodimer, which binds 1 NAD [...] | 0.489 |