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 |
| Plim_0744 | msrP | Plim_0744 | Plim_3769 | Putative secreted protein; KEGG: sus:Acid_2373 calcium-binding EF-hand- containing protein. | Oxidoreductase molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereois [...] | 0.673 |
| Plim_1533 | msrP | Plim_1533 | Plim_3769 | PFAM: alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen; KEGG: sus:Acid_2373 calcium-binding EF-hand- containing protein. | Oxidoreductase molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereois [...] | 0.673 |
| Plim_3768 | msrP | Plim_3768 | Plim_3769 | Copper efflux system periplasmic protein. | Oxidoreductase molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereois [...] | 0.590 |
| Plim_3989 | Plim_3992 | Plim_3989 | Plim_3992 | Cytochrome c oxidase, subunit II. | Caa(3)-type oxidase, subunit IV. | 0.996 |
| Plim_3989 | msrP | Plim_3989 | Plim_3769 | Cytochrome c oxidase, subunit II. | Oxidoreductase molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereois [...] | 0.526 |
| Plim_3989 | msrQ | Plim_3989 | Plim_3770 | Cytochrome c oxidase, subunit II. | Oxidoreductase FAD-binding domain protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of [...] | 0.506 |
| Plim_3992 | Plim_3989 | Plim_3992 | Plim_3989 | Caa(3)-type oxidase, subunit IV. | Cytochrome c oxidase, subunit II. | 0.996 |
| Plim_3992 | msrP | Plim_3992 | Plim_3769 | Caa(3)-type oxidase, subunit IV. | Oxidoreductase molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereois [...] | 0.721 |
| msrP | Plim_0744 | Plim_3769 | Plim_0744 | Oxidoreductase molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereois [...] | Putative secreted protein; KEGG: sus:Acid_2373 calcium-binding EF-hand- containing protein. | 0.673 |
| msrP | Plim_1533 | Plim_3769 | Plim_1533 | Oxidoreductase molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereois [...] | PFAM: alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen; KEGG: sus:Acid_2373 calcium-binding EF-hand- containing protein. | 0.673 |
| msrP | Plim_3768 | Plim_3769 | Plim_3768 | Oxidoreductase molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereois [...] | Copper efflux system periplasmic protein. | 0.590 |
| msrP | Plim_3989 | Plim_3769 | Plim_3989 | Oxidoreductase molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereois [...] | Cytochrome c oxidase, subunit II. | 0.526 |
| msrP | Plim_3992 | Plim_3769 | Plim_3992 | Oxidoreductase molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereois [...] | Caa(3)-type oxidase, subunit IV. | 0.721 |
| msrP | msrQ | Plim_3769 | Plim_3770 | Oxidoreductase molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereois [...] | Oxidoreductase FAD-binding domain protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of [...] | 0.973 |
| msrQ | Plim_3989 | Plim_3770 | Plim_3989 | Oxidoreductase FAD-binding domain protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of [...] | Cytochrome c oxidase, subunit II. | 0.506 |
| msrQ | msrP | Plim_3770 | Plim_3769 | Oxidoreductase FAD-binding domain protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of [...] | Oxidoreductase molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereois [...] | 0.973 |