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 |
| SFR58076.1 | SFR65748.1 | SAMN05216203_1560 | SAMN05216203_2259 | Thioredoxin. | Oligopeptidase A Metallo peptidase. MEROPS family M03A. | 0.411 |
| SFR58076.1 | dnaJ | SAMN05216203_1560 | SAMN05216203_1632 | Thioredoxin. | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | 0.833 |
| SFR58076.1 | htpG | SAMN05216203_1560 | SAMN05216203_0131 | Thioredoxin. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.846 |
| SFR65741.1 | SFR65748.1 | SAMN05216203_2258 | SAMN05216203_2259 | Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily. | Oligopeptidase A Metallo peptidase. MEROPS family M03A. | 0.544 |
| SFR65741.1 | SFR65753.1 | SAMN05216203_2258 | SAMN05216203_2260 | Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily. | Hypothetical protein. | 0.535 |
| SFR65748.1 | SFR58076.1 | SAMN05216203_2259 | SAMN05216203_1560 | Oligopeptidase A Metallo peptidase. MEROPS family M03A. | Thioredoxin. | 0.411 |
| SFR65748.1 | SFR65741.1 | SAMN05216203_2259 | SAMN05216203_2258 | Oligopeptidase A Metallo peptidase. MEROPS family M03A. | Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily. | 0.544 |
| SFR65748.1 | SFR65753.1 | SAMN05216203_2259 | SAMN05216203_2260 | Oligopeptidase A Metallo peptidase. MEROPS family M03A. | Hypothetical protein. | 0.785 |
| SFR65748.1 | dnaJ | SAMN05216203_2259 | SAMN05216203_1632 | Oligopeptidase A Metallo peptidase. MEROPS family M03A. | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | 0.420 |
| SFR65748.1 | htpG | SAMN05216203_2259 | SAMN05216203_0131 | Oligopeptidase A Metallo peptidase. MEROPS family M03A. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.478 |
| SFR65748.1 | pyrC | SAMN05216203_2259 | SAMN05216203_3036 | Oligopeptidase A Metallo peptidase. MEROPS family M03A. | Dihydroorotase; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. | 0.441 |
| SFR65753.1 | SFR65741.1 | SAMN05216203_2260 | SAMN05216203_2258 | Hypothetical protein. | Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily. | 0.535 |
| SFR65753.1 | SFR65748.1 | SAMN05216203_2260 | SAMN05216203_2259 | Hypothetical protein. | Oligopeptidase A Metallo peptidase. MEROPS family M03A. | 0.785 |
| dnaJ | SFR58076.1 | SAMN05216203_1632 | SAMN05216203_1560 | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | Thioredoxin. | 0.833 |
| dnaJ | SFR65748.1 | SAMN05216203_1632 | SAMN05216203_2259 | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | Oligopeptidase A Metallo peptidase. MEROPS family M03A. | 0.420 |
| dnaJ | htpG | SAMN05216203_1632 | SAMN05216203_0131 | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.996 |
| htpG | SFR58076.1 | SAMN05216203_0131 | SAMN05216203_1560 | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | Thioredoxin. | 0.846 |
| htpG | SFR65748.1 | SAMN05216203_0131 | SAMN05216203_2259 | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | Oligopeptidase A Metallo peptidase. MEROPS family M03A. | 0.478 |
| htpG | dnaJ | SAMN05216203_0131 | SAMN05216203_1632 | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] | 0.996 |
| pyrC | SFR65748.1 | SAMN05216203_3036 | SAMN05216203_2259 | Dihydroorotase; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. | Oligopeptidase A Metallo peptidase. MEROPS family M03A. | 0.441 |