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 |
| SDC07694.1 | SDC57134.1 | SAMN04488588_0428 | SAMN04488588_1325 | 16S rRNA (uracil1498-N3)-methyltransferase; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | Ribosomal protein L11 methyltransferase (PrmA). | 0.674 |
| SDC07694.1 | dnaJ | SAMN04488588_0428 | SAMN04488588_1584 | 16S rRNA (uracil1498-N3)-methyltransferase; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | 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, [...] | 0.569 |
| SDC31893.1 | SDC57134.1 | SAMN04488588_0805 | SAMN04488588_1325 | PEP-utilising enzyme, mobile domain. | Ribosomal protein L11 methyltransferase (PrmA). | 0.429 |
| SDC57067.1 | SDC57105.1 | SAMN04488588_1323 | SAMN04488588_1324 | Hypothetical protein. | Hypothetical protein. | 0.773 |
| SDC57067.1 | SDC57134.1 | SAMN04488588_1323 | SAMN04488588_1325 | Hypothetical protein. | Ribosomal protein L11 methyltransferase (PrmA). | 0.547 |
| SDC57105.1 | SDC57067.1 | SAMN04488588_1324 | SAMN04488588_1323 | Hypothetical protein. | Hypothetical protein. | 0.773 |
| SDC57105.1 | SDC57134.1 | SAMN04488588_1324 | SAMN04488588_1325 | Hypothetical protein. | Ribosomal protein L11 methyltransferase (PrmA). | 0.547 |
| SDC57134.1 | SDC07694.1 | SAMN04488588_1325 | SAMN04488588_0428 | Ribosomal protein L11 methyltransferase (PrmA). | 16S rRNA (uracil1498-N3)-methyltransferase; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | 0.674 |
| SDC57134.1 | SDC31893.1 | SAMN04488588_1325 | SAMN04488588_0805 | Ribosomal protein L11 methyltransferase (PrmA). | PEP-utilising enzyme, mobile domain. | 0.429 |
| SDC57134.1 | SDC57067.1 | SAMN04488588_1325 | SAMN04488588_1323 | Ribosomal protein L11 methyltransferase (PrmA). | Hypothetical protein. | 0.547 |
| SDC57134.1 | SDC57105.1 | SAMN04488588_1325 | SAMN04488588_1324 | Ribosomal protein L11 methyltransferase (PrmA). | Hypothetical protein. | 0.547 |
| SDC57134.1 | dnaJ | SAMN04488588_1325 | SAMN04488588_1584 | Ribosomal protein L11 methyltransferase (PrmA). | 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, [...] | 0.722 |
| SDC57134.1 | rplK | SAMN04488588_1325 | SAMN04488588_0186 | Ribosomal protein L11 methyltransferase (PrmA). | LSU ribosomal protein L11P; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | 0.758 |
| dnaJ | SDC07694.1 | SAMN04488588_1584 | SAMN04488588_0428 | 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, [...] | 16S rRNA (uracil1498-N3)-methyltransferase; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | 0.569 |
| dnaJ | SDC57134.1 | SAMN04488588_1584 | SAMN04488588_1325 | 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, [...] | Ribosomal protein L11 methyltransferase (PrmA). | 0.722 |
| dnaJ | rplK | SAMN04488588_1584 | SAMN04488588_0186 | 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, [...] | LSU ribosomal protein L11P; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | 0.833 |
| rplK | SDC57134.1 | SAMN04488588_0186 | SAMN04488588_1325 | LSU ribosomal protein L11P; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Ribosomal protein L11 methyltransferase (PrmA). | 0.758 |
| rplK | dnaJ | SAMN04488588_0186 | SAMN04488588_1584 | LSU ribosomal protein L11P; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | 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 |